data_9AXJ
# 
_entry.id   9AXJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9AXJ         pdb_00009axj 10.2210/pdb9axj/pdb 
WWPDB D_1000281891 ?            ?                   
# 
_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       2025-01-15 
# 
_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                        9AXJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-06 
_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              arbuller@wisc.edu 
_pdbx_contact_author.name_first         Andrew 
_pdbx_contact_author.name_last          Buller 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9635-4844 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Perkins, L.J.' 1 0000-0002-5895-8540 
'Zmich, A.P.'   2 0000-0002-4362-6105 
'Bingman, C.A.' 3 0000-0002-3073-5089 
'Buller, A.R.'  4 0000-0002-9635-4844 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            14 
_citation.language                  ? 
_citation.page_first                11196 
_citation.page_last                 11204 
_citation.title                     
'Elucidation of the stereochemical mechanism of cystathionine gamma-lyase reveals how substrate specificity constrains catalysis.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c02281 
_citation.pdbx_database_id_PubMed   39391268 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zmich, A.'     1 ?                   
primary 'Perkins, L.J.' 2 ?                   
primary 'Bingman, C.'   3 ?                   
primary 'Buller, A.R.'  4 0000-0002-9635-4844 
# 
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 'Cystathionine gamma-synthase'                                                                              
41551.824 1   2.5.1.48 ? ? ? 
2 non-polymer syn '(2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid' 
330.230   1   ?        ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                                     
106.120   1   ?        ? ? ? 
4 non-polymer syn 'IODIDE ION'                                                                                                
126.904   2   ?        ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                                                                                             
24.305    3   ?        ? ? ? 
6 water       nat water                                                                                                       
18.015    377 ?        ? ? ? 
# 
_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       
;MSYEGFETLAIHAGQEADAETGAVVVPIYQTSTYRQDGVGGLRGGYEYSRTANPTRTALEECLAALEGGVRGLAFASGMA
AEDTLLRTIARPGDHLIIPNDAYGGTFRLVSKVFERWGVSWDAVDLSNPEAVRTAIRPETVAIWVETPTNPLLNIADIAA
LADIAHAADALLVVDNTFASPYLQRPLSLGADVVVHSTTKYLGGHSDVVGGALVVADAELGERLAFHQNSMGAVAGPFDA
WLTLRGIKTLGVRMDRHCANAERVVEALVGHPEVAEVLYPGLPDHPGHKVAVDQMRAFGGMVSFRMRGGEEAALRVCAKT
KVFTLAESLGGVESLIEHPGKMTHASTAGSLLEVPSDLVRLSVGIETVDDLVNDLLQALEPLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSYEGFETLAIHAGQEADAETGAVVVPIYQTSTYRQDGVGGLRGGYEYSRTANPTRTALEECLAALEGGVRGLAFASGMA
AEDTLLRTIARPGDHLIIPNDAYGGTFRLVSKVFERWGVSWDAVDLSNPEAVRTAIRPETVAIWVETPTNPLLNIADIAA
LADIAHAADALLVVDNTFASPYLQRPLSLGADVVVHSTTKYLGGHSDVVGGALVVADAELGERLAFHQNSMGAVAGPFDA
WLTLRGIKTLGVRMDRHCANAERVVEALVGHPEVAEVLYPGLPDHPGHKVAVDQMRAFGGMVSFRMRGGEEAALRVCAKT
KVFTLAESLGGVESLIEHPGKMTHASTAGSLLEVPSDLVRLSVGIETVDDLVNDLLQALEPLEHHHHHH
;
_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 
2 '(2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid' 4LM 
3 'DI(HYDROXYETHYL)ETHER'                                                                                     PEG 
4 'IODIDE ION'                                                                                                IOD 
5 'MAGNESIUM ION'                                                                                             MG  
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   TYR n 
1 4   GLU n 
1 5   GLY n 
1 6   PHE n 
1 7   GLU n 
1 8   THR n 
1 9   LEU n 
1 10  ALA n 
1 11  ILE n 
1 12  HIS n 
1 13  ALA n 
1 14  GLY n 
1 15  GLN n 
1 16  GLU n 
1 17  ALA n 
1 18  ASP n 
1 19  ALA n 
1 20  GLU n 
1 21  THR n 
1 22  GLY n 
1 23  ALA n 
1 24  VAL n 
1 25  VAL n 
1 26  VAL n 
1 27  PRO n 
1 28  ILE n 
1 29  TYR n 
1 30  GLN n 
1 31  THR n 
1 32  SER n 
1 33  THR n 
1 34  TYR n 
1 35  ARG n 
1 36  GLN n 
1 37  ASP n 
1 38  GLY n 
1 39  VAL n 
1 40  GLY n 
1 41  GLY n 
1 42  LEU n 
1 43  ARG n 
1 44  GLY n 
1 45  GLY n 
1 46  TYR n 
1 47  GLU n 
1 48  TYR n 
1 49  SER n 
1 50  ARG n 
1 51  THR n 
1 52  ALA n 
1 53  ASN n 
1 54  PRO n 
1 55  THR n 
1 56  ARG n 
1 57  THR n 
1 58  ALA n 
1 59  LEU n 
1 60  GLU n 
1 61  GLU n 
1 62  CYS n 
1 63  LEU n 
1 64  ALA n 
1 65  ALA n 
1 66  LEU n 
1 67  GLU n 
1 68  GLY n 
1 69  GLY n 
1 70  VAL n 
1 71  ARG n 
1 72  GLY n 
1 73  LEU n 
1 74  ALA n 
1 75  PHE n 
1 76  ALA n 
1 77  SER n 
1 78  GLY n 
1 79  MET n 
1 80  ALA n 
1 81  ALA n 
1 82  GLU n 
1 83  ASP n 
1 84  THR n 
1 85  LEU n 
1 86  LEU n 
1 87  ARG n 
1 88  THR n 
1 89  ILE n 
1 90  ALA n 
1 91  ARG n 
1 92  PRO n 
1 93  GLY n 
1 94  ASP n 
1 95  HIS n 
1 96  LEU n 
1 97  ILE n 
1 98  ILE n 
1 99  PRO n 
1 100 ASN n 
1 101 ASP n 
1 102 ALA n 
1 103 TYR n 
1 104 GLY n 
1 105 GLY n 
1 106 THR n 
1 107 PHE n 
1 108 ARG n 
1 109 LEU n 
1 110 VAL n 
1 111 SER n 
1 112 LYS n 
1 113 VAL n 
1 114 PHE n 
1 115 GLU n 
1 116 ARG n 
1 117 TRP n 
1 118 GLY n 
1 119 VAL n 
1 120 SER n 
1 121 TRP n 
1 122 ASP n 
1 123 ALA n 
1 124 VAL n 
1 125 ASP n 
1 126 LEU n 
1 127 SER n 
1 128 ASN n 
1 129 PRO n 
1 130 GLU n 
1 131 ALA n 
1 132 VAL n 
1 133 ARG n 
1 134 THR n 
1 135 ALA n 
1 136 ILE n 
1 137 ARG n 
1 138 PRO n 
1 139 GLU n 
1 140 THR n 
1 141 VAL n 
1 142 ALA n 
1 143 ILE n 
1 144 TRP n 
1 145 VAL n 
1 146 GLU n 
1 147 THR n 
1 148 PRO n 
1 149 THR n 
1 150 ASN n 
1 151 PRO n 
1 152 LEU n 
1 153 LEU n 
1 154 ASN n 
1 155 ILE n 
1 156 ALA n 
1 157 ASP n 
1 158 ILE n 
1 159 ALA n 
1 160 ALA n 
1 161 LEU n 
1 162 ALA n 
1 163 ASP n 
1 164 ILE n 
1 165 ALA n 
1 166 HIS n 
1 167 ALA n 
1 168 ALA n 
1 169 ASP n 
1 170 ALA n 
1 171 LEU n 
1 172 LEU n 
1 173 VAL n 
1 174 VAL n 
1 175 ASP n 
1 176 ASN n 
1 177 THR n 
1 178 PHE n 
1 179 ALA n 
1 180 SER n 
1 181 PRO n 
1 182 TYR n 
1 183 LEU n 
1 184 GLN n 
1 185 ARG n 
1 186 PRO n 
1 187 LEU n 
1 188 SER n 
1 189 LEU n 
1 190 GLY n 
1 191 ALA n 
1 192 ASP n 
1 193 VAL n 
1 194 VAL n 
1 195 VAL n 
1 196 HIS n 
1 197 SER n 
1 198 THR n 
1 199 THR n 
1 200 LYS n 
1 201 TYR n 
1 202 LEU n 
1 203 GLY n 
1 204 GLY n 
1 205 HIS n 
1 206 SER n 
1 207 ASP n 
1 208 VAL n 
1 209 VAL n 
1 210 GLY n 
1 211 GLY n 
1 212 ALA n 
1 213 LEU n 
1 214 VAL n 
1 215 VAL n 
1 216 ALA n 
1 217 ASP n 
1 218 ALA n 
1 219 GLU n 
1 220 LEU n 
1 221 GLY n 
1 222 GLU n 
1 223 ARG n 
1 224 LEU n 
1 225 ALA n 
1 226 PHE n 
1 227 HIS n 
1 228 GLN n 
1 229 ASN n 
1 230 SER n 
1 231 MET n 
1 232 GLY n 
1 233 ALA n 
1 234 VAL n 
1 235 ALA n 
1 236 GLY n 
1 237 PRO n 
1 238 PHE n 
1 239 ASP n 
1 240 ALA n 
1 241 TRP n 
1 242 LEU n 
1 243 THR n 
1 244 LEU n 
1 245 ARG n 
1 246 GLY n 
1 247 ILE n 
1 248 LYS n 
1 249 THR n 
1 250 LEU n 
1 251 GLY n 
1 252 VAL n 
1 253 ARG n 
1 254 MET n 
1 255 ASP n 
1 256 ARG n 
1 257 HIS n 
1 258 CYS n 
1 259 ALA n 
1 260 ASN n 
1 261 ALA n 
1 262 GLU n 
1 263 ARG n 
1 264 VAL n 
1 265 VAL n 
1 266 GLU n 
1 267 ALA n 
1 268 LEU n 
1 269 VAL n 
1 270 GLY n 
1 271 HIS n 
1 272 PRO n 
1 273 GLU n 
1 274 VAL n 
1 275 ALA n 
1 276 GLU n 
1 277 VAL n 
1 278 LEU n 
1 279 TYR n 
1 280 PRO n 
1 281 GLY n 
1 282 LEU n 
1 283 PRO n 
1 284 ASP n 
1 285 HIS n 
1 286 PRO n 
1 287 GLY n 
1 288 HIS n 
1 289 LYS n 
1 290 VAL n 
1 291 ALA n 
1 292 VAL n 
1 293 ASP n 
1 294 GLN n 
1 295 MET n 
1 296 ARG n 
1 297 ALA n 
1 298 PHE n 
1 299 GLY n 
1 300 GLY n 
1 301 MET n 
1 302 VAL n 
1 303 SER n 
1 304 PHE n 
1 305 ARG n 
1 306 MET n 
1 307 ARG n 
1 308 GLY n 
1 309 GLY n 
1 310 GLU n 
1 311 GLU n 
1 312 ALA n 
1 313 ALA n 
1 314 LEU n 
1 315 ARG n 
1 316 VAL n 
1 317 CYS n 
1 318 ALA n 
1 319 LYS n 
1 320 THR n 
1 321 LYS n 
1 322 VAL n 
1 323 PHE n 
1 324 THR n 
1 325 LEU n 
1 326 ALA n 
1 327 GLU n 
1 328 SER n 
1 329 LEU n 
1 330 GLY n 
1 331 GLY n 
1 332 VAL n 
1 333 GLU n 
1 334 SER n 
1 335 LEU n 
1 336 ILE n 
1 337 GLU n 
1 338 HIS n 
1 339 PRO n 
1 340 GLY n 
1 341 LYS n 
1 342 MET n 
1 343 THR n 
1 344 HIS n 
1 345 ALA n 
1 346 SER n 
1 347 THR n 
1 348 ALA n 
1 349 GLY n 
1 350 SER n 
1 351 LEU n 
1 352 LEU n 
1 353 GLU n 
1 354 VAL n 
1 355 PRO n 
1 356 SER n 
1 357 ASP n 
1 358 LEU n 
1 359 VAL n 
1 360 ARG n 
1 361 LEU n 
1 362 SER n 
1 363 VAL n 
1 364 GLY n 
1 365 ILE n 
1 366 GLU n 
1 367 THR n 
1 368 VAL n 
1 369 ASP n 
1 370 ASP n 
1 371 LEU n 
1 372 VAL n 
1 373 ASN n 
1 374 ASP n 
1 375 LEU n 
1 376 LEU n 
1 377 GLN n 
1 378 ALA n 
1 379 LEU n 
1 380 GLU n 
1 381 PRO n 
1 382 LEU n 
1 383 GLU n 
1 384 HIS n 
1 385 HIS n 
1 386 HIS n 
1 387 HIS n 
1 388 HIS n 
1 389 HIS 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                   389 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Tfu_0440 
_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      'Thermobifida fusca' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2021 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
4LM non-polymer         . 
'(2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid' ? 'C12 H15 N2 O7 P' 
330.230 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
IOD non-polymer         . 'IODIDE ION' ? 'I -1'            126.904 
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 
MG  non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'            24.305  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'       106.120 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   TYR 3   3   3   TYR TYR A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLU 16  16  16  GLU GLU A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  GLN 36  36  36  GLN GLN A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  ARG 43  43  43  ARG ARG A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  CYS 62  62  62  CYS CYS A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  MET 79  79  79  MET MET A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  HIS 95  95  95  HIS HIS A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 TRP 117 117 117 TRP TRP A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 TRP 121 121 121 TRP TRP A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 ARG 133 133 133 ARG ARG A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 TRP 144 144 144 TRP TRP A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ASN 154 154 154 ASN ASN A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 HIS 166 166 166 HIS HIS A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 GLN 184 184 184 GLN GLN A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 TYR 201 201 201 TYR TYR A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ASP 207 207 207 ASP ASP A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ASP 217 217 217 ASP ASP A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 HIS 227 227 227 HIS HIS A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 MET 231 231 231 MET MET A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 ALA 235 235 235 ALA ALA A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 PHE 238 238 238 PHE PHE A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 TRP 241 241 241 TRP TRP A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 MET 254 254 254 MET MET A . n 
A 1 255 ASP 255 255 255 ASP ASP A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 HIS 257 257 257 HIS HIS A . n 
A 1 258 CYS 258 258 258 CYS CYS A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 ALA 261 261 261 ALA ALA A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 ARG 263 263 263 ARG ARG A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 GLU 266 266 266 GLU GLU A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 HIS 271 271 271 HIS HIS A . n 
A 1 272 PRO 272 272 272 PRO PRO A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 PRO 280 280 280 PRO PRO 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 PRO 283 283 283 PRO PRO A . n 
A 1 284 ASP 284 284 284 ASP ASP A . n 
A 1 285 HIS 285 285 285 HIS HIS A . n 
A 1 286 PRO 286 286 286 PRO PRO A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 HIS 288 288 288 HIS HIS A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 VAL 292 292 292 VAL VAL A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 GLN 294 294 294 GLN GLN A . n 
A 1 295 MET 295 295 295 MET MET A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 GLY 299 299 299 GLY GLY A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 MET 301 301 301 MET MET A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 PHE 304 304 304 PHE PHE A . n 
A 1 305 ARG 305 305 305 ARG ARG A . n 
A 1 306 MET 306 306 306 MET MET A . n 
A 1 307 ARG 307 307 307 ARG ARG A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 GLU 310 310 310 GLU GLU A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 ARG 315 315 315 ARG ARG A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 CYS 317 317 317 CYS CYS A . n 
A 1 318 ALA 318 318 318 ALA ALA A . n 
A 1 319 LYS 319 319 319 LYS LYS A . n 
A 1 320 THR 320 320 320 THR THR A . n 
A 1 321 LYS 321 321 321 LYS LYS A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 PHE 323 323 323 PHE PHE A . n 
A 1 324 THR 324 324 324 THR THR A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 SER 328 328 328 SER SER A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 VAL 332 332 332 VAL VAL A . n 
A 1 333 GLU 333 333 333 GLU GLU A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 ILE 336 336 336 ILE ILE A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 PRO 339 339 339 PRO PRO A . n 
A 1 340 GLY 340 340 340 GLY GLY A . n 
A 1 341 LYS 341 341 341 LYS LYS A . n 
A 1 342 MET 342 342 342 MET MET A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 HIS 344 344 344 HIS HIS A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 THR 347 347 347 THR THR A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 GLY 349 349 349 GLY GLY A . n 
A 1 350 SER 350 350 350 SER SER A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 LEU 352 352 352 LEU LEU A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 PRO 355 355 355 PRO PRO A . n 
A 1 356 SER 356 356 356 SER SER A . n 
A 1 357 ASP 357 357 357 ASP ASP A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 VAL 359 359 359 VAL VAL A . n 
A 1 360 ARG 360 360 360 ARG ARG A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 SER 362 362 362 SER SER A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 THR 367 367 367 THR THR A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 VAL 372 372 372 VAL VAL A . n 
A 1 373 ASN 373 373 373 ASN ASN A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 GLN 377 377 377 GLN GLN A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 GLU 380 380 380 GLU GLU A . n 
A 1 381 PRO 381 381 381 PRO PRO A . n 
A 1 382 LEU 382 382 ?   ?   ?   A . n 
A 1 383 GLU 383 383 ?   ?   ?   A . n 
A 1 384 HIS 384 384 ?   ?   ?   A . n 
A 1 385 HIS 385 385 ?   ?   ?   A . n 
A 1 386 HIS 386 386 ?   ?   ?   A . n 
A 1 387 HIS 387 387 ?   ?   ?   A . n 
A 1 388 HIS 388 388 ?   ?   ?   A . n 
A 1 389 HIS 389 389 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        4LM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   4LM 
_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 
B 2 4LM 1   401 401 4LM LIG A . 
C 3 PEG 1   402 402 PEG PEG A . 
D 4 IOD 1   403 1   IOD IOD A . 
E 4 IOD 1   404 2   IOD IOD A . 
F 5 MG  1   405 1   MG  MG  A . 
G 5 MG  1   406 2   MG  MG  A . 
H 5 MG  1   407 3   MG  MG  A . 
I 6 HOH 1   501 323 HOH HOH A . 
I 6 HOH 2   502 244 HOH HOH A . 
I 6 HOH 3   503 240 HOH HOH A . 
I 6 HOH 4   504 388 HOH HOH A . 
I 6 HOH 5   505 138 HOH HOH A . 
I 6 HOH 6   506 302 HOH HOH A . 
I 6 HOH 7   507 251 HOH HOH A . 
I 6 HOH 8   508 175 HOH HOH A . 
I 6 HOH 9   509 69  HOH HOH A . 
I 6 HOH 10  510 274 HOH HOH A . 
I 6 HOH 11  511 199 HOH HOH A . 
I 6 HOH 12  512 168 HOH HOH A . 
I 6 HOH 13  513 40  HOH HOH A . 
I 6 HOH 14  514 164 HOH HOH A . 
I 6 HOH 15  515 232 HOH HOH A . 
I 6 HOH 16  516 79  HOH HOH A . 
I 6 HOH 17  517 372 HOH HOH A . 
I 6 HOH 18  518 137 HOH HOH A . 
I 6 HOH 19  519 298 HOH HOH A . 
I 6 HOH 20  520 255 HOH HOH A . 
I 6 HOH 21  521 15  HOH HOH A . 
I 6 HOH 22  522 56  HOH HOH A . 
I 6 HOH 23  523 257 HOH HOH A . 
I 6 HOH 24  524 55  HOH HOH A . 
I 6 HOH 25  525 26  HOH HOH A . 
I 6 HOH 26  526 375 HOH HOH A . 
I 6 HOH 27  527 87  HOH HOH A . 
I 6 HOH 28  528 121 HOH HOH A . 
I 6 HOH 29  529 71  HOH HOH A . 
I 6 HOH 30  530 36  HOH HOH A . 
I 6 HOH 31  531 95  HOH HOH A . 
I 6 HOH 32  532 239 HOH HOH A . 
I 6 HOH 33  533 188 HOH HOH A . 
I 6 HOH 34  534 67  HOH HOH A . 
I 6 HOH 35  535 11  HOH HOH A . 
I 6 HOH 36  536 29  HOH HOH A . 
I 6 HOH 37  537 249 HOH HOH A . 
I 6 HOH 38  538 258 HOH HOH A . 
I 6 HOH 39  539 236 HOH HOH A . 
I 6 HOH 40  540 235 HOH HOH A . 
I 6 HOH 41  541 254 HOH HOH A . 
I 6 HOH 42  542 94  HOH HOH A . 
I 6 HOH 43  543 107 HOH HOH A . 
I 6 HOH 44  544 299 HOH HOH A . 
I 6 HOH 45  545 177 HOH HOH A . 
I 6 HOH 46  546 83  HOH HOH A . 
I 6 HOH 47  547 281 HOH HOH A . 
I 6 HOH 48  548 81  HOH HOH A . 
I 6 HOH 49  549 170 HOH HOH A . 
I 6 HOH 50  550 301 HOH HOH A . 
I 6 HOH 51  551 173 HOH HOH A . 
I 6 HOH 52  552 204 HOH HOH A . 
I 6 HOH 53  553 136 HOH HOH A . 
I 6 HOH 54  554 140 HOH HOH A . 
I 6 HOH 55  555 8   HOH HOH A . 
I 6 HOH 56  556 234 HOH HOH A . 
I 6 HOH 57  557 123 HOH HOH A . 
I 6 HOH 58  558 104 HOH HOH A . 
I 6 HOH 59  559 266 HOH HOH A . 
I 6 HOH 60  560 68  HOH HOH A . 
I 6 HOH 61  561 220 HOH HOH A . 
I 6 HOH 62  562 297 HOH HOH A . 
I 6 HOH 63  563 166 HOH HOH A . 
I 6 HOH 64  564 22  HOH HOH A . 
I 6 HOH 65  565 319 HOH HOH A . 
I 6 HOH 66  566 118 HOH HOH A . 
I 6 HOH 67  567 110 HOH HOH A . 
I 6 HOH 68  568 386 HOH HOH A . 
I 6 HOH 69  569 370 HOH HOH A . 
I 6 HOH 70  570 393 HOH HOH A . 
I 6 HOH 71  571 139 HOH HOH A . 
I 6 HOH 72  572 144 HOH HOH A . 
I 6 HOH 73  573 272 HOH HOH A . 
I 6 HOH 74  574 196 HOH HOH A . 
I 6 HOH 75  575 32  HOH HOH A . 
I 6 HOH 76  576 115 HOH HOH A . 
I 6 HOH 77  577 213 HOH HOH A . 
I 6 HOH 78  578 1   HOH HOH A . 
I 6 HOH 79  579 184 HOH HOH A . 
I 6 HOH 80  580 315 HOH HOH A . 
I 6 HOH 81  581 206 HOH HOH A . 
I 6 HOH 82  582 88  HOH HOH A . 
I 6 HOH 83  583 288 HOH HOH A . 
I 6 HOH 84  584 145 HOH HOH A . 
I 6 HOH 85  585 141 HOH HOH A . 
I 6 HOH 86  586 45  HOH HOH A . 
I 6 HOH 87  587 100 HOH HOH A . 
I 6 HOH 88  588 132 HOH HOH A . 
I 6 HOH 89  589 193 HOH HOH A . 
I 6 HOH 90  590 208 HOH HOH A . 
I 6 HOH 91  591 133 HOH HOH A . 
I 6 HOH 92  592 157 HOH HOH A . 
I 6 HOH 93  593 377 HOH HOH A . 
I 6 HOH 94  594 126 HOH HOH A . 
I 6 HOH 95  595 109 HOH HOH A . 
I 6 HOH 96  596 156 HOH HOH A . 
I 6 HOH 97  597 380 HOH HOH A . 
I 6 HOH 98  598 198 HOH HOH A . 
I 6 HOH 99  599 49  HOH HOH A . 
I 6 HOH 100 600 9   HOH HOH A . 
I 6 HOH 101 601 124 HOH HOH A . 
I 6 HOH 102 602 318 HOH HOH A . 
I 6 HOH 103 603 90  HOH HOH A . 
I 6 HOH 104 604 73  HOH HOH A . 
I 6 HOH 105 605 221 HOH HOH A . 
I 6 HOH 106 606 154 HOH HOH A . 
I 6 HOH 107 607 10  HOH HOH A . 
I 6 HOH 108 608 62  HOH HOH A . 
I 6 HOH 109 609 392 HOH HOH A . 
I 6 HOH 110 610 371 HOH HOH A . 
I 6 HOH 111 611 179 HOH HOH A . 
I 6 HOH 112 612 352 HOH HOH A . 
I 6 HOH 113 613 43  HOH HOH A . 
I 6 HOH 114 614 103 HOH HOH A . 
I 6 HOH 115 615 46  HOH HOH A . 
I 6 HOH 116 616 5   HOH HOH A . 
I 6 HOH 117 617 160 HOH HOH A . 
I 6 HOH 118 618 259 HOH HOH A . 
I 6 HOH 119 619 31  HOH HOH A . 
I 6 HOH 120 620 91  HOH HOH A . 
I 6 HOH 121 621 112 HOH HOH A . 
I 6 HOH 122 622 181 HOH HOH A . 
I 6 HOH 123 623 21  HOH HOH A . 
I 6 HOH 124 624 7   HOH HOH A . 
I 6 HOH 125 625 16  HOH HOH A . 
I 6 HOH 126 626 41  HOH HOH A . 
I 6 HOH 127 627 42  HOH HOH A . 
I 6 HOH 128 628 290 HOH HOH A . 
I 6 HOH 129 629 13  HOH HOH A . 
I 6 HOH 130 630 89  HOH HOH A . 
I 6 HOH 131 631 64  HOH HOH A . 
I 6 HOH 132 632 14  HOH HOH A . 
I 6 HOH 133 633 125 HOH HOH A . 
I 6 HOH 134 634 84  HOH HOH A . 
I 6 HOH 135 635 345 HOH HOH A . 
I 6 HOH 136 636 130 HOH HOH A . 
I 6 HOH 137 637 245 HOH HOH A . 
I 6 HOH 138 638 247 HOH HOH A . 
I 6 HOH 139 639 19  HOH HOH A . 
I 6 HOH 140 640 102 HOH HOH A . 
I 6 HOH 141 641 279 HOH HOH A . 
I 6 HOH 142 642 27  HOH HOH A . 
I 6 HOH 143 643 60  HOH HOH A . 
I 6 HOH 144 644 75  HOH HOH A . 
I 6 HOH 145 645 74  HOH HOH A . 
I 6 HOH 146 646 248 HOH HOH A . 
I 6 HOH 147 647 163 HOH HOH A . 
I 6 HOH 148 648 149 HOH HOH A . 
I 6 HOH 149 649 70  HOH HOH A . 
I 6 HOH 150 650 283 HOH HOH A . 
I 6 HOH 151 651 85  HOH HOH A . 
I 6 HOH 152 652 374 HOH HOH A . 
I 6 HOH 153 653 72  HOH HOH A . 
I 6 HOH 154 654 35  HOH HOH A . 
I 6 HOH 155 655 37  HOH HOH A . 
I 6 HOH 156 656 250 HOH HOH A . 
I 6 HOH 157 657 383 HOH HOH A . 
I 6 HOH 158 658 317 HOH HOH A . 
I 6 HOH 159 659 129 HOH HOH A . 
I 6 HOH 160 660 20  HOH HOH A . 
I 6 HOH 161 661 127 HOH HOH A . 
I 6 HOH 162 662 4   HOH HOH A . 
I 6 HOH 163 663 182 HOH HOH A . 
I 6 HOH 164 664 233 HOH HOH A . 
I 6 HOH 165 665 143 HOH HOH A . 
I 6 HOH 166 666 99  HOH HOH A . 
I 6 HOH 167 667 53  HOH HOH A . 
I 6 HOH 168 668 54  HOH HOH A . 
I 6 HOH 169 669 365 HOH HOH A . 
I 6 HOH 170 670 211 HOH HOH A . 
I 6 HOH 171 671 6   HOH HOH A . 
I 6 HOH 172 672 23  HOH HOH A . 
I 6 HOH 173 673 2   HOH HOH A . 
I 6 HOH 174 674 82  HOH HOH A . 
I 6 HOH 175 675 152 HOH HOH A . 
I 6 HOH 176 676 111 HOH HOH A . 
I 6 HOH 177 677 47  HOH HOH A . 
I 6 HOH 178 678 285 HOH HOH A . 
I 6 HOH 179 679 78  HOH HOH A . 
I 6 HOH 180 680 329 HOH HOH A . 
I 6 HOH 181 681 17  HOH HOH A . 
I 6 HOH 182 682 260 HOH HOH A . 
I 6 HOH 183 683 134 HOH HOH A . 
I 6 HOH 184 684 150 HOH HOH A . 
I 6 HOH 185 685 51  HOH HOH A . 
I 6 HOH 186 686 52  HOH HOH A . 
I 6 HOH 187 687 268 HOH HOH A . 
I 6 HOH 188 688 378 HOH HOH A . 
I 6 HOH 189 689 98  HOH HOH A . 
I 6 HOH 190 690 92  HOH HOH A . 
I 6 HOH 191 691 44  HOH HOH A . 
I 6 HOH 192 692 30  HOH HOH A . 
I 6 HOH 193 693 65  HOH HOH A . 
I 6 HOH 194 694 63  HOH HOH A . 
I 6 HOH 195 695 93  HOH HOH A . 
I 6 HOH 196 696 153 HOH HOH A . 
I 6 HOH 197 697 128 HOH HOH A . 
I 6 HOH 198 698 348 HOH HOH A . 
I 6 HOH 199 699 253 HOH HOH A . 
I 6 HOH 200 700 33  HOH HOH A . 
I 6 HOH 201 701 171 HOH HOH A . 
I 6 HOH 202 702 376 HOH HOH A . 
I 6 HOH 203 703 12  HOH HOH A . 
I 6 HOH 204 704 282 HOH HOH A . 
I 6 HOH 205 705 270 HOH HOH A . 
I 6 HOH 206 706 162 HOH HOH A . 
I 6 HOH 207 707 287 HOH HOH A . 
I 6 HOH 208 708 391 HOH HOH A . 
I 6 HOH 209 709 246 HOH HOH A . 
I 6 HOH 210 710 291 HOH HOH A . 
I 6 HOH 211 711 159 HOH HOH A . 
I 6 HOH 212 712 261 HOH HOH A . 
I 6 HOH 213 713 66  HOH HOH A . 
I 6 HOH 214 714 3   HOH HOH A . 
I 6 HOH 215 715 237 HOH HOH A . 
I 6 HOH 216 716 384 HOH HOH A . 
I 6 HOH 217 717 387 HOH HOH A . 
I 6 HOH 218 718 151 HOH HOH A . 
I 6 HOH 219 719 58  HOH HOH A . 
I 6 HOH 220 720 50  HOH HOH A . 
I 6 HOH 221 721 369 HOH HOH A . 
I 6 HOH 222 722 108 HOH HOH A . 
I 6 HOH 223 723 368 HOH HOH A . 
I 6 HOH 224 724 243 HOH HOH A . 
I 6 HOH 225 725 215 HOH HOH A . 
I 6 HOH 226 726 86  HOH HOH A . 
I 6 HOH 227 727 280 HOH HOH A . 
I 6 HOH 228 728 38  HOH HOH A . 
I 6 HOH 229 729 34  HOH HOH A . 
I 6 HOH 230 730 202 HOH HOH A . 
I 6 HOH 231 731 18  HOH HOH A . 
I 6 HOH 232 732 161 HOH HOH A . 
I 6 HOH 233 733 25  HOH HOH A . 
I 6 HOH 234 734 379 HOH HOH A . 
I 6 HOH 235 735 203 HOH HOH A . 
I 6 HOH 236 736 227 HOH HOH A . 
I 6 HOH 237 737 252 HOH HOH A . 
I 6 HOH 238 738 147 HOH HOH A . 
I 6 HOH 239 739 216 HOH HOH A . 
I 6 HOH 240 740 269 HOH HOH A . 
I 6 HOH 241 741 230 HOH HOH A . 
I 6 HOH 242 742 214 HOH HOH A . 
I 6 HOH 243 743 241 HOH HOH A . 
I 6 HOH 244 744 286 HOH HOH A . 
I 6 HOH 245 745 48  HOH HOH A . 
I 6 HOH 246 746 122 HOH HOH A . 
I 6 HOH 247 747 80  HOH HOH A . 
I 6 HOH 248 748 195 HOH HOH A . 
I 6 HOH 249 749 105 HOH HOH A . 
I 6 HOH 250 750 106 HOH HOH A . 
I 6 HOH 251 751 191 HOH HOH A . 
I 6 HOH 252 752 228 HOH HOH A . 
I 6 HOH 253 753 114 HOH HOH A . 
I 6 HOH 254 754 226 HOH HOH A . 
I 6 HOH 255 755 267 HOH HOH A . 
I 6 HOH 256 756 135 HOH HOH A . 
I 6 HOH 257 757 271 HOH HOH A . 
I 6 HOH 258 758 390 HOH HOH A . 
I 6 HOH 259 759 24  HOH HOH A . 
I 6 HOH 260 760 222 HOH HOH A . 
I 6 HOH 261 761 289 HOH HOH A . 
I 6 HOH 262 762 381 HOH HOH A . 
I 6 HOH 263 763 39  HOH HOH A . 
I 6 HOH 264 764 97  HOH HOH A . 
I 6 HOH 265 765 116 HOH HOH A . 
I 6 HOH 266 766 76  HOH HOH A . 
I 6 HOH 267 767 238 HOH HOH A . 
I 6 HOH 268 768 389 HOH HOH A . 
I 6 HOH 269 769 382 HOH HOH A . 
I 6 HOH 270 770 218 HOH HOH A . 
I 6 HOH 271 771 242 HOH HOH A . 
I 6 HOH 272 772 320 HOH HOH A . 
I 6 HOH 273 773 113 HOH HOH A . 
I 6 HOH 274 774 174 HOH HOH A . 
I 6 HOH 275 775 294 HOH HOH A . 
I 6 HOH 276 776 131 HOH HOH A . 
I 6 HOH 277 777 120 HOH HOH A . 
I 6 HOH 278 778 59  HOH HOH A . 
I 6 HOH 279 779 167 HOH HOH A . 
I 6 HOH 280 780 101 HOH HOH A . 
I 6 HOH 281 781 314 HOH HOH A . 
I 6 HOH 282 782 231 HOH HOH A . 
I 6 HOH 283 783 225 HOH HOH A . 
I 6 HOH 284 784 155 HOH HOH A . 
I 6 HOH 285 785 327 HOH HOH A . 
I 6 HOH 286 786 332 HOH HOH A . 
I 6 HOH 287 787 325 HOH HOH A . 
I 6 HOH 288 788 217 HOH HOH A . 
I 6 HOH 289 789 337 HOH HOH A . 
I 6 HOH 290 790 310 HOH HOH A . 
I 6 HOH 291 791 187 HOH HOH A . 
I 6 HOH 292 792 61  HOH HOH A . 
I 6 HOH 293 793 307 HOH HOH A . 
I 6 HOH 294 794 296 HOH HOH A . 
I 6 HOH 295 795 200 HOH HOH A . 
I 6 HOH 296 796 330 HOH HOH A . 
I 6 HOH 297 797 385 HOH HOH A . 
I 6 HOH 298 798 311 HOH HOH A . 
I 6 HOH 299 799 326 HOH HOH A . 
I 6 HOH 300 800 313 HOH HOH A . 
I 6 HOH 301 801 178 HOH HOH A . 
I 6 HOH 302 802 333 HOH HOH A . 
I 6 HOH 303 803 96  HOH HOH A . 
I 6 HOH 304 804 189 HOH HOH A . 
I 6 HOH 305 805 158 HOH HOH A . 
I 6 HOH 306 806 334 HOH HOH A . 
I 6 HOH 307 807 358 HOH HOH A . 
I 6 HOH 308 808 77  HOH HOH A . 
I 6 HOH 309 809 223 HOH HOH A . 
I 6 HOH 310 810 321 HOH HOH A . 
I 6 HOH 311 811 57  HOH HOH A . 
I 6 HOH 312 812 229 HOH HOH A . 
I 6 HOH 313 813 303 HOH HOH A . 
I 6 HOH 314 814 316 HOH HOH A . 
I 6 HOH 315 815 338 HOH HOH A . 
I 6 HOH 316 816 224 HOH HOH A . 
I 6 HOH 317 817 209 HOH HOH A . 
I 6 HOH 318 818 309 HOH HOH A . 
I 6 HOH 319 819 119 HOH HOH A . 
I 6 HOH 320 820 308 HOH HOH A . 
I 6 HOH 321 821 394 HOH HOH A . 
I 6 HOH 322 822 186 HOH HOH A . 
I 6 HOH 323 823 201 HOH HOH A . 
I 6 HOH 324 824 176 HOH HOH A . 
I 6 HOH 325 825 306 HOH HOH A . 
I 6 HOH 326 826 197 HOH HOH A . 
I 6 HOH 327 827 190 HOH HOH A . 
I 6 HOH 328 828 192 HOH HOH A . 
I 6 HOH 329 829 312 HOH HOH A . 
I 6 HOH 330 830 276 HOH HOH A . 
I 6 HOH 331 831 265 HOH HOH A . 
I 6 HOH 332 832 322 HOH HOH A . 
I 6 HOH 333 833 357 HOH HOH A . 
I 6 HOH 334 834 180 HOH HOH A . 
I 6 HOH 335 835 328 HOH HOH A . 
I 6 HOH 336 836 165 HOH HOH A . 
I 6 HOH 337 837 373 HOH HOH A . 
I 6 HOH 338 838 331 HOH HOH A . 
I 6 HOH 339 839 324 HOH HOH A . 
I 6 HOH 340 840 142 HOH HOH A . 
I 6 HOH 341 841 273 HOH HOH A . 
I 6 HOH 342 842 28  HOH HOH A . 
I 6 HOH 343 843 278 HOH HOH A . 
I 6 HOH 344 844 367 HOH HOH A . 
I 6 HOH 345 845 304 HOH HOH A . 
I 6 HOH 346 846 212 HOH HOH A . 
I 6 HOH 347 847 359 HOH HOH A . 
I 6 HOH 348 848 210 HOH HOH A . 
I 6 HOH 349 849 350 HOH HOH A . 
I 6 HOH 350 850 183 HOH HOH A . 
I 6 HOH 351 851 343 HOH HOH A . 
I 6 HOH 352 852 360 HOH HOH A . 
I 6 HOH 353 853 305 HOH HOH A . 
I 6 HOH 354 854 341 HOH HOH A . 
I 6 HOH 355 855 300 HOH HOH A . 
I 6 HOH 356 856 264 HOH HOH A . 
I 6 HOH 357 857 169 HOH HOH A . 
I 6 HOH 358 858 263 HOH HOH A . 
I 6 HOH 359 859 146 HOH HOH A . 
I 6 HOH 360 860 349 HOH HOH A . 
I 6 HOH 361 861 275 HOH HOH A . 
I 6 HOH 362 862 185 HOH HOH A . 
I 6 HOH 363 863 295 HOH HOH A . 
I 6 HOH 364 864 355 HOH HOH A . 
I 6 HOH 365 865 356 HOH HOH A . 
I 6 HOH 366 866 342 HOH HOH A . 
I 6 HOH 367 867 293 HOH HOH A . 
I 6 HOH 368 868 117 HOH HOH A . 
I 6 HOH 369 869 207 HOH HOH A . 
I 6 HOH 370 870 205 HOH HOH A . 
I 6 HOH 371 871 256 HOH HOH A . 
I 6 HOH 372 872 148 HOH HOH A . 
I 6 HOH 373 873 194 HOH HOH A . 
I 6 HOH 374 874 346 HOH HOH A . 
I 6 HOH 375 875 361 HOH HOH A . 
I 6 HOH 376 876 277 HOH HOH A . 
I 6 HOH 377 877 339 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A TYR 3   ? CG  ? A TYR 3   CG  
2  1 Y 1 A TYR 3   ? CD1 ? A TYR 3   CD1 
3  1 Y 1 A TYR 3   ? CD2 ? A TYR 3   CD2 
4  1 Y 1 A TYR 3   ? CE1 ? A TYR 3   CE1 
5  1 Y 1 A TYR 3   ? CE2 ? A TYR 3   CE2 
6  1 Y 1 A TYR 3   ? CZ  ? A TYR 3   CZ  
7  1 Y 1 A TYR 3   ? OH  ? A TYR 3   OH  
8  1 Y 1 A LYS 289 ? CG  ? A LYS 289 CG  
9  1 Y 1 A LYS 289 ? CD  ? A LYS 289 CD  
10 1 Y 1 A LYS 289 ? CE  ? A LYS 289 CE  
11 1 Y 1 A LYS 289 ? NZ  ? A LYS 289 NZ  
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0257 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AXJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     116.946 
_cell.length_a_esd                 ? 
_cell.length_b                     116.946 
_cell.length_b_esd                 ? 
_cell.length_c                     116.946 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9AXJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                195 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 2 3' 
_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                   9AXJ 
_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             3.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.07 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    
;Well solution comprising 20-30% PEG300, 0.1 M HEPES, 0.2 M MgCl2. 2 uL drops were laid with a 1:1 mixture of well solution and 8 mg/mL protein in 0.1 M HEPES buffer pH 7.0. Crystals were grown overnight and were soaked with S-methylmethionine iodide
;
_exptl_crystal_grow.pdbx_pH_range   7.0-7.5 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX300HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-28 
_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   0.978720 
_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        0.978720 
_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                                       9AXJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.5 
_reflns.d_resolution_low                               40 
_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                                     84295 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                21.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.2 
_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                                0.02 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.50 
_reflns_shell.d_res_low                                     1.53 
_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                             4184 
_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                               15.7 
_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                               0.930 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.333 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.000 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.000 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.288 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.983 
_refine.correlation_coeff_Fo_to_Fc_free          0.979 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_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                                 9AXJ 
_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                            1.500 
_refine.ls_d_res_low                             39.012 
_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                     84276 
_refine.ls_number_reflns_R_free                  4113 
_refine.ls_number_reflns_R_work                  80163 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.991 
_refine.ls_percent_reflns_R_free                 4.880 
_refine.ls_R_factor_all                          0.138 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1560 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1371 
_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                    'MASK BULK SOLVENT' 
_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                          ? 
_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       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.047 
_refine.pdbx_overall_ESU_R_Free                  0.049 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_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                             2.171 
_refine.overall_SU_ML                            0.039 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2820 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             377 
_refine_hist.number_atoms_total               3231 
_refine_hist.d_res_high                       1.500 
_refine_hist.d_res_low                        39.012 
# 
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' ? 0.018  0.013  3068 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  2870 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.890  1.638  4206 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.609  1.571  6613 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 6.637  5.000  412  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 27.499 20.364 165  ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 13.067 15.000 471  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 18.567 15.000 28   ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.109  0.200  396  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  3623 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  669  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.225  0.200  628  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.178  0.200  2642 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.170  0.200  1489 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.086  0.200  1334 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.151  0.200  229  ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.087  0.200  2    ? r_metal_ion_refined            ? ? 
'X-RAY DIFFRACTION' ? 0.163  0.200  20   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.192  0.200  111  ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.180  0.200  38   ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 0.895  1.429  1594 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 0.893  1.428  1593 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 1.229  2.142  2018 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 1.229  2.142  2019 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 1.794  1.617  1474 ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 1.794  1.619  1475 ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 2.615  2.357  2186 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 2.614  2.359  2187 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 5.071  18.907 3472 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 4.891  17.994 3393 ? r_lrange_other                 ? ? 
# 
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' 1.500 1.539 . . 307 5910 100.0000 . . . . 0.299 . . . . . . . . . . . 0.307 
'X-RAY DIFFRACTION' 1.539 1.581 . . 299 5815 100.0000 . . . . 0.255 . . . . . . . . . . . 0.259 
'X-RAY DIFFRACTION' 1.581 1.627 . . 322 5571 100.0000 . . . . 0.223 . . . . . . . . . . . 0.238 
'X-RAY DIFFRACTION' 1.627 1.677 . . 290 5469 100.0000 . . . . 0.205 . . . . . . . . . . . 0.254 
'X-RAY DIFFRACTION' 1.677 1.732 . . 277 5294 100.0000 . . . . 0.179 . . . . . . . . . . . 0.198 
'X-RAY DIFFRACTION' 1.732 1.792 . . 247 5147 100.0000 . . . . 0.159 . . . . . . . . . . . 0.176 
'X-RAY DIFFRACTION' 1.792 1.860 . . 266 4954 100.0000 . . . . 0.147 . . . . . . . . . . . 0.158 
'X-RAY DIFFRACTION' 1.860 1.936 . . 228 4773 100.0000 . . . . 0.129 . . . . . . . . . . . 0.161 
'X-RAY DIFFRACTION' 1.936 2.021 . . 196 4624 99.9793  . . . . 0.125 . . . . . . . . . . . 0.176 
'X-RAY DIFFRACTION' 2.021 2.120 . . 217 4391 100.0000 . . . . 0.115 . . . . . . . . . . . 0.150 
'X-RAY DIFFRACTION' 2.120 2.234 . . 220 4196 100.0000 . . . . 0.116 . . . . . . . . . . . 0.147 
'X-RAY DIFFRACTION' 2.234 2.369 . . 137 3196 80.5462  . . . . 0.117 . . . . . . . . . . . 0.133 
'X-RAY DIFFRACTION' 2.369 2.532 . . 189 3741 100.0000 . . . . 0.114 . . . . . . . . . . . 0.142 
'X-RAY DIFFRACTION' 2.532 2.734 . . 176 3465 100.0000 . . . . 0.112 . . . . . . . . . . . 0.127 
'X-RAY DIFFRACTION' 2.734 2.994 . . 157 3212 100.0000 . . . . 0.124 . . . . . . . . . . . 0.148 
'X-RAY DIFFRACTION' 2.994 3.345 . . 202 2879 100.0000 . . . . 0.136 . . . . . . . . . . . 0.150 
'X-RAY DIFFRACTION' 3.345 3.858 . . 125 2596 100.0000 . . . . 0.131 . . . . . . . . . . . 0.148 
'X-RAY DIFFRACTION' 3.858 4.714 . . 108 2166 98.1018  . . . . 0.112 . . . . . . . . . . . 0.119 
'X-RAY DIFFRACTION' 4.714 6.620 . . 87  1744 100.0000 . . . . 0.136 . . . . . . . . . . . 0.157 
'X-RAY DIFFRACTION' 6.620 39    . . 63  1020 99.9078  . . . . 0.145 . . . . . . . . . . . 0.130 
# 
_struct.entry_id                     9AXJ 
_struct.title                        'Cystathionine gamma lyase from Thermobifida fusca in an amino crotonate form' 
_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        9AXJ 
_struct_keywords.text            'PLP, amino crotonate, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A9P2TCP3_THEFU 
_struct_ref.pdbx_db_accession          A0A9P2TCP3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSYEGFETLAIHAGQEADAETGAVVVPIYQTSTYRQDGVGGLRGGYEYSRTANPTRTALEECLAALEGGVRGLAFASGMA
AEDTLLRTIARPGDHLIIPNDAYGGTFRLVSKVFERWGVSWDAVDLSNPEAVRTAIRPETVAIWVETPTNPLLNIADIAA
LADIAHAADALLVVDNTFASPYLQRPLSLGADVVVHSTTKYLGGHSDVVGGALVVADAELGERLAFHQNSMGAVAGPFDA
WLTLRGIKTLGVRMDRHCANAERVVEALVGHPEVAEVLYPGLPDHPGHKVAVDQMRAFGGMVSFRMRGGEEAALRVCAKT
KVFTLAESLGGVESLIEHPGKMTHASTAGSLLEVPSDLVRLSVGIETVDDLVNDLLQALEP
;
_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              9AXJ 
_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                 381 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A9P2TCP3 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  381 
_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       381 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9AXJ LEU A 382 ? UNP A0A9P2TCP3 ? ? 'expression tag' 382 1 
1 9AXJ GLU A 383 ? UNP A0A9P2TCP3 ? ? 'expression tag' 383 2 
1 9AXJ HIS A 384 ? UNP A0A9P2TCP3 ? ? 'expression tag' 384 3 
1 9AXJ HIS A 385 ? UNP A0A9P2TCP3 ? ? 'expression tag' 385 4 
1 9AXJ HIS A 386 ? UNP A0A9P2TCP3 ? ? 'expression tag' 386 5 
1 9AXJ HIS A 387 ? UNP A0A9P2TCP3 ? ? 'expression tag' 387 6 
1 9AXJ HIS A 388 ? UNP A0A9P2TCP3 ? ? 'expression tag' 388 7 
1 9AXJ HIS A 389 ? UNP A0A9P2TCP3 ? ? 'expression tag' 389 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 23240 ? 
1 MORE         -163  ? 
1 'SSA (A^2)'  41420 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000    
2 'crystal symmetry operation' 2_555 -x,-y,z   -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000    
3 'crystal symmetry operation' 3_554 -x,y,-z-1 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -116.9460000000 
4 'crystal symmetry operation' 4_554 x,-y,-z-1 1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -116.9460000000 
# 
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 GLY A 5   ? ALA A 13  ? GLY A 5   ALA A 13  1 ? 9  
HELX_P HELX_P2  AA2 ASN A 53  ? GLY A 68  ? ASN A 53  GLY A 68  1 ? 16 
HELX_P HELX_P3  AA3 SER A 77  ? ALA A 90  ? SER A 77  ALA A 90  1 ? 14 
HELX_P HELX_P4  AA4 TYR A 103 ? VAL A 113 ? TYR A 103 VAL A 113 1 ? 11 
HELX_P HELX_P5  AA5 ASN A 128 ? ILE A 136 ? ASN A 128 ILE A 136 1 ? 9  
HELX_P HELX_P6  AA6 ASP A 157 ? ALA A 168 ? ASP A 157 ALA A 168 1 ? 12 
HELX_P HELX_P7  AA7 ALA A 179 ? GLN A 184 ? ALA A 179 GLN A 184 1 ? 6  
HELX_P HELX_P8  AA8 ARG A 185 ? GLY A 190 ? ARG A 185 GLY A 190 5 ? 6  
HELX_P HELX_P9  AA9 ASP A 217 ? GLY A 232 ? ASP A 217 GLY A 232 1 ? 16 
HELX_P HELX_P10 AB1 GLY A 236 ? LYS A 248 ? GLY A 236 LYS A 248 1 ? 13 
HELX_P HELX_P11 AB2 THR A 249 ? VAL A 269 ? THR A 249 VAL A 269 1 ? 21 
HELX_P HELX_P12 AB3 GLY A 287 ? MET A 295 ? GLY A 287 MET A 295 1 ? 9  
HELX_P HELX_P13 AB4 GLY A 308 ? THR A 320 ? GLY A 308 THR A 320 1 ? 13 
HELX_P HELX_P14 AB5 HIS A 344 ? ALA A 348 ? HIS A 344 ALA A 348 5 ? 5  
HELX_P HELX_P15 AB6 THR A 367 ? GLU A 380 ? THR A 367 GLU A 380 1 ? 14 
# 
_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 
metalc1  metalc ? ? F MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 405 A HOH 506 4_554 ? ? ? ? ? ? ? 2.301 ? ? 
metalc2  metalc ? ? F MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 405 A HOH 519 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc3  metalc ? ? F MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 405 A HOH 544 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
metalc4  metalc ? ? F MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 405 A HOH 550 4_554 ? ? ? ? ? ? ? 2.217 ? ? 
metalc5  metalc ? ? F MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 405 A HOH 813 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc6  metalc ? ? F MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 405 A HOH 855 4_554 ? ? ? ? ? ? ? 2.027 ? ? 
metalc7  metalc ? ? G MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 406 A HOH 579 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc8  metalc ? ? G MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 406 A HOH 740 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
metalc9  metalc ? ? G MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 406 A HOH 827 1_555 ? ? ? ? ? ? ? 2.253 ? ? 
metalc10 metalc ? ? G MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 406 A HOH 840 6_555 ? ? ? ? ? ? ? 2.180 ? ? 
metalc11 metalc ? ? G MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 406 A HOH 873 6_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc12 metalc ? ? H MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 407 A HOH 506 4_554 ? ? ? ? ? ? ? 2.108 ? ? 
metalc13 metalc ? ? H MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 407 A HOH 526 1_555 ? ? ? ? ? ? ? 1.867 ? ? 
metalc14 metalc ? ? H MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 407 A HOH 544 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc15 metalc ? ? H MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 407 A HOH 855 4_554 ? ? ? ? ? ? ? 2.479 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  O ? I HOH . ? A HOH 506 ? 4_554 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 519 ? 1_555 86.9  ? 
2  O ? I HOH . ? A HOH 506 ? 4_554 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 544 ? 1_555 93.0  ? 
3  O ? I HOH . ? A HOH 519 ? 1_555 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 544 ? 1_555 100.0 ? 
4  O ? I HOH . ? A HOH 506 ? 4_554 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 550 ? 4_554 84.3  ? 
5  O ? I HOH . ? A HOH 519 ? 1_555 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 550 ? 4_554 83.8  ? 
6  O ? I HOH . ? A HOH 544 ? 1_555 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 550 ? 4_554 175.2 ? 
7  O ? I HOH . ? A HOH 506 ? 4_554 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 813 ? 1_555 168.8 ? 
8  O ? I HOH . ? A HOH 519 ? 1_555 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 813 ? 1_555 93.1  ? 
9  O ? I HOH . ? A HOH 544 ? 1_555 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 813 ? 1_555 98.1  ? 
10 O ? I HOH . ? A HOH 550 ? 4_554 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 813 ? 1_555 84.5  ? 
11 O ? I HOH . ? A HOH 506 ? 4_554 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 855 ? 4_554 88.2  ? 
12 O ? I HOH . ? A HOH 519 ? 1_555 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 855 ? 4_554 174.0 ? 
13 O ? I HOH . ? A HOH 544 ? 1_555 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 855 ? 4_554 83.8  ? 
14 O ? I HOH . ? A HOH 550 ? 4_554 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 855 ? 4_554 92.2  ? 
15 O ? I HOH . ? A HOH 813 ? 1_555 MG ? F MG . ? A MG 405 ? 1_555 O ? I HOH . ? A HOH 855 ? 4_554 91.0  ? 
16 O ? I HOH . ? A HOH 579 ? 1_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 740 ? 1_555 86.7  ? 
17 O ? I HOH . ? A HOH 579 ? 1_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 827 ? 1_555 84.6  ? 
18 O ? I HOH . ? A HOH 740 ? 1_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 827 ? 1_555 96.4  ? 
19 O ? I HOH . ? A HOH 579 ? 1_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 840 ? 6_555 90.5  ? 
20 O ? I HOH . ? A HOH 740 ? 1_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 840 ? 6_555 172.7 ? 
21 O ? I HOH . ? A HOH 827 ? 1_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 840 ? 6_555 90.0  ? 
22 O ? I HOH . ? A HOH 579 ? 1_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 873 ? 6_555 89.9  ? 
23 O ? I HOH . ? A HOH 740 ? 1_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 873 ? 6_555 88.0  ? 
24 O ? I HOH . ? A HOH 827 ? 1_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 873 ? 6_555 172.8 ? 
25 O ? I HOH . ? A HOH 840 ? 6_555 MG ? G MG . ? A MG 406 ? 1_555 O ? I HOH . ? A HOH 873 ? 6_555 85.3  ? 
26 O ? I HOH . ? A HOH 506 ? 4_554 MG ? H MG . ? A MG 407 ? 1_555 O ? I HOH . ? A HOH 526 ? 1_555 93.7  ? 
27 O ? I HOH . ? A HOH 506 ? 4_554 MG ? H MG . ? A MG 407 ? 1_555 O ? I HOH . ? A HOH 544 ? 1_555 91.0  ? 
28 O ? I HOH . ? A HOH 526 ? 1_555 MG ? H MG . ? A MG 407 ? 1_555 O ? I HOH . ? A HOH 544 ? 1_555 130.2 ? 
29 O ? I HOH . ? A HOH 506 ? 4_554 MG ? H MG . ? A MG 407 ? 1_555 O ? I HOH . ? A HOH 855 ? 4_554 81.8  ? 
30 O ? I HOH . ? A HOH 526 ? 1_555 MG ? H MG . ? A MG 407 ? 1_555 O ? I HOH . ? A HOH 855 ? 4_554 160.2 ? 
31 O ? I HOH . ? A HOH 544 ? 1_555 MG ? H MG . ? A MG 407 ? 1_555 O ? I HOH . ? A HOH 855 ? 4_554 69.4  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 THR 147 A . ? THR 147 A PRO 148 A ? PRO 148 A 1 -12.64 
2 ASN 150 A . ? ASN 150 A PRO 151 A ? PRO 151 A 1 15.20  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 71  ? PHE A 75  ? ARG A 71  PHE A 75  
AA1 2 GLY A 211 ? VAL A 215 ? GLY A 211 VAL A 215 
AA1 3 VAL A 193 ? SER A 197 ? VAL A 193 SER A 197 
AA1 4 LEU A 171 ? ASP A 175 ? LEU A 171 ASP A 175 
AA1 5 THR A 140 ? GLU A 146 ? THR A 140 GLU A 146 
AA1 6 HIS A 95  ? PRO A 99  ? HIS A 95  PRO A 99  
AA1 7 SER A 120 ? VAL A 124 ? SER A 120 VAL A 124 
AA2 1 VAL A 274 ? LEU A 278 ? VAL A 274 LEU A 278 
AA2 2 MET A 301 ? MET A 306 ? MET A 301 MET A 306 
AA2 3 LEU A 358 ? SER A 362 ? LEU A 358 SER A 362 
AA2 4 LEU A 335 ? GLU A 337 ? LEU A 335 GLU A 337 
AA2 5 THR A 324 ? LEU A 325 ? THR A 324 LEU A 325 
# 
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 PHE A 75  ? N PHE A 75  O GLY A 211 ? O GLY A 211 
AA1 2 3 O VAL A 214 ? O VAL A 214 N VAL A 194 ? N VAL A 194 
AA1 3 4 O VAL A 193 ? O VAL A 193 N VAL A 174 ? N VAL A 174 
AA1 4 5 O ASP A 175 ? O ASP A 175 N VAL A 145 ? N VAL A 145 
AA1 5 6 O TRP A 144 ? O TRP A 144 N ILE A 97  ? N ILE A 97  
AA1 6 7 N ILE A 98  ? N ILE A 98  O ASP A 122 ? O ASP A 122 
AA2 1 2 N ALA A 275 ? N ALA A 275 O ARG A 305 ? O ARG A 305 
AA2 2 3 N VAL A 302 ? N VAL A 302 O LEU A 361 ? O LEU A 361 
AA2 3 4 O SER A 362 ? O SER A 362 N LEU A 335 ? N LEU A 335 
AA2 4 5 O ILE A 336 ? O ILE A 336 N THR A 324 ? N THR A 324 
# 
_pdbx_entry_details.entry_id                   9AXJ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 676 ? ? O A HOH 717 ? ? 2.11 
2 1 O A HOH 739 ? ? O A HOH 865 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     542 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_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     841 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_554 
_pdbx_validate_symm_contact.dist              2.15 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD A GLU 20  ? ? OE2 A GLU 20  ? ? 1.127 1.252 -0.125 0.011 N 
2 1 CD A GLU 47  ? ? OE2 A GLU 47  ? ? 1.171 1.252 -0.081 0.011 N 
3 1 NE A ARG 137 ? ? CZ  A ARG 137 ? ? 1.408 1.326 0.082  0.013 N 
4 1 CD A GLU 222 ? ? OE2 A GLU 222 ? ? 1.161 1.252 -0.091 0.011 N 
5 1 CD A GLU 333 ? ? OE1 A GLU 333 ? ? 1.356 1.252 0.104  0.011 N 
6 1 CD A GLU 333 ? ? OE2 A GLU 333 ? ? 1.338 1.252 0.086  0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 71  ? ? CZ A ARG 71  ? ? NH2 A ARG 71  ? ? 116.60 120.30 -3.70  0.50 N 
2 1 CG A ARG 87  ? B CD A ARG 87  ? B NE  A ARG 87  ? B 95.41  111.80 -16.39 2.10 N 
3 1 NE A ARG 87  ? A CZ A ARG 87  ? A NH1 A ARG 87  ? A 115.56 120.30 -4.74  0.50 N 
4 1 NE A ARG 87  ? B CZ A ARG 87  ? B NH1 A ARG 87  ? B 116.56 120.30 -3.74  0.50 N 
5 1 NE A ARG 87  ? B CZ A ARG 87  ? B NH2 A ARG 87  ? B 123.42 120.30 3.12   0.50 N 
6 1 NE A ARG 91  ? A CZ A ARG 91  ? A NH2 A ARG 91  ? A 117.16 120.30 -3.14  0.50 N 
7 1 NE A ARG 116 ? B CZ A ARG 116 ? B NH2 A ARG 116 ? B 117.02 120.30 -3.28  0.50 N 
8 1 NE A ARG 223 ? A CZ A ARG 223 ? A NH2 A ARG 223 ? A 124.58 120.30 4.28   0.50 N 
9 1 NE A ARG 263 ? B CZ A ARG 263 ? B NH2 A ARG 263 ? B 116.85 120.30 -3.45  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 47  ? ? -144.25 -38.86  
2 1 SER A 180 ? ? 70.09   162.39  
3 1 LYS A 200 ? ? -90.08  -121.41 
4 1 VAL A 208 ? A -160.82 117.41  
5 1 ALA A 233 ? ? -91.87  57.71   
6 1 SER A 328 ? ? 89.75   175.35  
7 1 MET A 342 ? ? -116.02 -104.96 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   HIS 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    196 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   SER 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    197 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            147.58 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     719 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   I 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 13.4956  24.2633 -51.9815 0.1333 ? -0.0107 ? -0.0367 ? 0.0908 ? -0.0212 ? 0.0985 ? 0.4066 ? 
1.6963  ? -1.5428 ? 13.3182 ? -1.1002 ? 10.6340 ? 0.0530  ? -0.1028 ? -0.0538 ? 0.0832  ? -0.0513 ? -0.5686 ? -0.5025 ? 0.6832  ? 
-0.0017 ? 
2  'X-RAY DIFFRACTION' ? refined 14.0766  16.2017 -54.0648 0.0536 ? -0.0176 ? -0.0053 ? 0.0644 ? -0.0058 ? 0.0209 ? 2.1055 ? 
-2.8248 ? 0.4586  ? 10.7595 ? 0.3083  ? 4.5696  ? 0.0339  ? 0.0614  ? 0.0027  ? -0.0408 ? -0.0545 ? -0.1964 ? 0.0495  ? 0.2127  ? 
0.0206  ? 
3  'X-RAY DIFFRACTION' ? refined 14.6075  4.6456  -59.6669 0.0580 ? -0.0073 ? -0.0200 ? 0.0657 ? -0.0073 ? 0.0272 ? 3.4773 ? 
2.5115  ? -3.0113 ? 1.8154  ? -2.1929 ? 3.2199  ? 0.0193  ? -0.0312 ? -0.0813 ? 0.0195  ? -0.0323 ? -0.0611 ? 0.0306  ? 0.2124  ? 
0.0130  ? 
4  'X-RAY DIFFRACTION' ? refined 19.0345  -7.5717 -48.6523 0.0505 ? 0.0028  ? -0.0113 ? 0.0800 ? -0.0123 ? 0.0513 ? 6.3660 ? 
-3.2951 ? 1.7940  ? 4.1265  ? -1.6700 ? 1.2522  ? 0.0144  ? 0.0851  ? 0.0097  ? 0.1140  ? -0.0772 ? -0.3410 ? -0.0154 ? 0.2357  ? 
0.0628  ? 
5  'X-RAY DIFFRACTION' ? refined 3.0174   8.5175  -34.8893 0.0565 ? 0.0030  ? -0.0093 ? 0.0504 ? -0.0136 ? 0.0054 ? 0.3646 ? 
-0.1106 ? -0.1687 ? 0.5900  ? 0.1126  ? 0.5810  ? -0.0128 ? -0.1119 ? 0.0302  ? 0.0971  ? 0.0078  ? -0.0034 ? -0.0293 ? 0.0281  ? 
0.0050  ? 
6  'X-RAY DIFFRACTION' ? refined -5.1627  11.5606 -22.3703 0.0693 ? 0.0075  ? 0.0096  ? 0.1189 ? -0.0222 ? 0.0321 ? 0.6531 ? 
-1.8465 ? 0.1570  ? 8.9737  ? -0.5321 ? 0.8213  ? -0.0651 ? -0.1856 ? 0.0186  ? 0.2046  ? 0.0944  ? 0.2023  ? 0.0103  ? -0.0483 ? 
-0.0293 ? 
7  'X-RAY DIFFRACTION' ? refined -0.6022  25.0449 -18.2644 0.1602 ? 0.0370  ? -0.0104 ? 0.1535 ? -0.1018 ? 0.1203 ? 4.6609 ? 
-2.1566 ? 3.0435  ? 6.2155  ? -5.2392 ? 6.9358  ? -0.1851 ? -0.3613 ? 0.3716  ? 0.4466  ? 0.2249  ? 0.1379  ? -0.2427 ? -0.2174 ? 
-0.0398 ? 
8  'X-RAY DIFFRACTION' ? refined 1.2298   22.0055 -30.8672 0.0882 ? 0.0027  ? -0.0047 ? 0.0529 ? -0.0452 ? 0.0406 ? 0.6900 ? 
-0.0289 ? 0.0315  ? 0.8591  ? 0.1013  ? 1.0763  ? -0.0105 ? -0.1574 ? 0.1154  ? 0.1393  ? 0.0268  ? -0.0455 ? -0.0806 ? 0.0062  ? 
-0.0163 ? 
9  'X-RAY DIFFRACTION' ? refined 8.3174   21.0164 -35.5132 0.0564 ? 0.0017  ? 0.0071  ? 0.0582 ? -0.0264 ? 0.0498 ? 5.2751 ? 
0.2872  ? 2.7819  ? 6.3135  ? 1.0430  ? 4.1131  ? -0.0204 ? 0.0445  ? 0.2347  ? -0.1659 ? -0.0015 ? -0.3850 ? -0.1587 ? 0.1411  ? 
0.0219  ? 
10 'X-RAY DIFFRACTION' ? refined 1.5479   12.8679 -43.8240 0.0429 ? 0.0025  ? 0.0012  ? 0.0107 ? -0.0088 ? 0.0101 ? 0.9969 ? 
-0.4658 ? 0.7294  ? 1.2222  ? -0.4542 ? 1.6608  ? -0.0116 ? -0.0608 ? 0.0749  ? 0.0609  ? 0.0115  ? -0.0274 ? -0.0294 ? -0.0254 ? 
0.0001  ? 
11 'X-RAY DIFFRACTION' ? refined 11.6581  3.8647  -32.3473 0.0904 ? 0.0248  ? -0.0219 ? 0.0819 ? -0.0146 ? 0.0107 ? 1.8222 ? 
3.9954  ? 1.8434  ? 9.7131  ? 3.2346  ? 2.6412  ? 0.0953  ? -0.0502 ? -0.0257 ? 0.3246  ? -0.1015 ? -0.1194 ? 0.0558  ? 0.0209  ? 
0.0063  ? 
12 'X-RAY DIFFRACTION' ? refined 3.3317   10.5398 -52.2211 0.0387 ? -0.0011 ? 0.0076  ? 0.0238 ? -0.0043 ? 0.0213 ? 0.3249 ? 
-0.6743 ? 0.3527  ? 2.0629  ? -1.3669 ? 1.0591  ? -0.0144 ? 0.0051  ? 0.0380  ? -0.0380 ? 0.0061  ? -0.0805 ? 0.0150  ? -0.0091 ? 
0.0083  ? 
13 'X-RAY DIFFRACTION' ? refined -7.3002  29.7205 -52.0589 0.1146 ? 0.0204  ? -0.0028 ? 0.0110 ? -0.0004 ? 0.0636 ? 6.4888 ? 
-2.5863 ? -0.3788 ? 2.1118  ? 0.3160  ? 2.1880  ? -0.0462 ? -0.0351 ? 0.3730  ? 0.0061  ? 0.0136  ? -0.0187 ? -0.3439 ? -0.0027 ? 
0.0326  ? 
14 'X-RAY DIFFRACTION' ? refined -18.9774 33.6556 -43.4354 0.1649 ? 0.0603  ? -0.0012 ? 0.0847 ? -0.0373 ? 0.1718 ? 7.8964 ? 
1.0930  ? 0.5664  ? 1.2744  ? -0.4704 ? 2.6110  ? 0.0731  ? 0.0929  ? 0.3371  ? -0.0225 ? 0.0471  ? 0.2909  ? -0.2670 ? -0.3628 ? 
-0.1202 ? 
15 'X-RAY DIFFRACTION' ? refined -3.4778  34.3606 -38.2388 0.1748 ? 0.0061  ? 0.0000  ? 0.0367 ? -0.0361 ? 0.1215 ? 5.1672 ? 
-1.0639 ? 1.1540  ? 3.2164  ? -0.2549 ? 3.3906  ? -0.1358 ? -0.1578 ? 0.4410  ? 0.0153  ? 0.0690  ? -0.0566 ? -0.3393 ? -0.0455 ? 
0.0668  ? 
16 'X-RAY DIFFRACTION' ? refined -19.3751 27.4746 -40.7616 0.1245 ? 0.0387  ? 0.0143  ? 0.0847 ? -0.0403 ? 0.1112 ? 6.8202 ? 
0.4153  ? -1.5540 ? 1.2663  ? -0.4201 ? 1.8527  ? 0.1197  ? -0.1054 ? 0.3236  ? 0.1314  ? -0.0588 ? 0.2992  ? -0.1926 ? -0.2753 ? 
-0.0610 ? 
17 'X-RAY DIFFRACTION' ? refined -20.3392 19.1172 -49.1185 0.0766 ? 0.0238  ? 0.0064  ? 0.0730 ? -0.0172 ? 0.0776 ? 3.9453 ? 
0.5273  ? -0.8978 ? 2.0128  ? -0.2070 ? 2.4032  ? -0.0016 ? -0.0077 ? 0.1672  ? 0.0179  ? 0.0094  ? 0.3527  ? -0.0889 ? -0.3655 ? 
-0.0077 ? 
18 'X-RAY DIFFRACTION' ? refined -17.2331 16.3855 -36.8753 0.0818 ? 0.0179  ? 0.0279  ? 0.0727 ? -0.0115 ? 0.0780 ? 0.7778 ? 
0.1781  ? 0.1431  ? 0.9254  ? -2.2759 ? 6.4323  ? -0.0041 ? -0.1451 ? 0.0180  ? 0.0164  ? 0.0234  ? 0.0670  ? 0.0694  ? -0.1355 ? 
-0.0193 ? 
19 'X-RAY DIFFRACTION' ? refined -15.5821 24.3935 -47.5530 0.0766 ? 0.0300  ? 0.0040  ? 0.0309 ? -0.0229 ? 0.0709 ? 1.7068 ? 
-0.1208 ? -0.9535 ? 0.9160  ? 0.0007  ? 3.5031  ? 0.0453  ? -0.0632 ? 0.1459  ? 0.0470  ? -0.0079 ? 0.1337  ? -0.2921 ? -0.1105 ? 
-0.0373 ? 
20 'X-RAY DIFFRACTION' ? refined -24.3991 29.0736 -52.0925 0.1373 ? 0.0688  ? 0.0030  ? 0.1349 ? -0.0063 ? 0.1733 ? 7.9589 ? 
2.1325  ? -3.7489 ? 3.7061  ? -0.2096 ? 6.3574  ? 0.3481  ? -0.1673 ? 0.4928  ? 0.0787  ? -0.1198 ? 0.5068  ? -0.4627 ? -0.4354 ? 
-0.2283 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? A 3   ? ? ? A 8   ? ALL ? 
2  'X-RAY DIFFRACTION' 2  ? ? A 9   ? ? ? A 16  ? ALL ? 
3  'X-RAY DIFFRACTION' 3  ? ? A 17  ? ? ? A 29  ? ALL ? 
4  'X-RAY DIFFRACTION' 4  ? ? A 30  ? ? ? A 47  ? ALL ? 
5  'X-RAY DIFFRACTION' 5  ? ? A 48  ? ? ? A 113 ? ALL ? 
6  'X-RAY DIFFRACTION' 6  ? ? A 114 ? ? ? A 127 ? ALL ? 
7  'X-RAY DIFFRACTION' 7  ? ? A 128 ? ? ? A 137 ? ALL ? 
8  'X-RAY DIFFRACTION' 8  ? ? A 138 ? ? ? A 184 ? ALL ? 
9  'X-RAY DIFFRACTION' 9  ? ? A 185 ? ? ? A 195 ? ALL ? 
10 'X-RAY DIFFRACTION' 10 ? ? A 196 ? ? ? A 218 ? ALL ? 
11 'X-RAY DIFFRACTION' 11 ? ? A 219 ? ? ? A 231 ? ALL ? 
12 'X-RAY DIFFRACTION' 12 ? ? A 232 ? ? ? A 253 ? ALL ? 
13 'X-RAY DIFFRACTION' 13 ? ? A 254 ? ? ? A 264 ? ALL ? 
14 'X-RAY DIFFRACTION' 14 ? ? A 265 ? ? ? A 279 ? ALL ? 
15 'X-RAY DIFFRACTION' 15 ? ? A 280 ? ? ? A 296 ? ALL ? 
16 'X-RAY DIFFRACTION' 16 ? ? A 297 ? ? ? A 313 ? ALL ? 
17 'X-RAY DIFFRACTION' 17 ? ? A 314 ? ? ? A 332 ? ALL ? 
18 'X-RAY DIFFRACTION' 18 ? ? A 333 ? ? ? A 353 ? ALL ? 
19 'X-RAY DIFFRACTION' 19 ? ? A 354 ? ? ? A 371 ? ALL ? 
20 'X-RAY DIFFRACTION' 20 ? ? A 372 ? ? ? A 381 ? ALL ? 
# 
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 382 ? A LEU 382 
4  1 Y 1 A GLU 383 ? A GLU 383 
5  1 Y 1 A HIS 384 ? A HIS 384 
6  1 Y 1 A HIS 385 ? A HIS 385 
7  1 Y 1 A HIS 386 ? A HIS 386 
8  1 Y 1 A HIS 387 ? A HIS 387 
9  1 Y 1 A HIS 388 ? A HIS 388 
10 1 Y 1 A HIS 389 ? A HIS 389 
# 
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 
4LM C    C  N N 1   
4LM N    N  N N 2   
4LM O1   O  N N 3   
4LM P    P  N N 4   
4LM N1   N  Y N 5   
4LM C2   C  Y N 6   
4LM C3   C  Y N 7   
4LM O3   O  N N 8   
4LM C4   C  Y N 9   
4LM C5   C  Y N 10  
4LM C6   C  Y N 11  
4LM CA   C  N N 12  
4LM CB   C  N N 13  
4LM CG   C  N N 14  
4LM C2A  C  N N 15  
4LM C4A  C  N N 16  
4LM C5A  C  N N 17  
4LM OP1  O  N N 18  
4LM OP2  O  N N 19  
4LM OP3  O  N N 20  
4LM OP4  O  N N 21  
4LM O2   O  N N 22  
4LM HO3  H  N N 23  
4LM H6   H  N N 24  
4LM HB   H  N N 25  
4LM HG   H  N N 26  
4LM HGA  H  N N 27  
4LM HGB  H  N N 28  
4LM H2A  H  N N 29  
4LM H2A1 H  N N 30  
4LM H2A2 H  N N 31  
4LM H4A  H  N N 32  
4LM H5A  H  N N 33  
4LM H5A1 H  N N 34  
4LM HOP2 H  N N 35  
4LM HOP3 H  N N 36  
4LM H2   H  N N 37  
ALA N    N  N N 38  
ALA CA   C  N S 39  
ALA C    C  N N 40  
ALA O    O  N N 41  
ALA CB   C  N N 42  
ALA OXT  O  N N 43  
ALA H    H  N N 44  
ALA H2   H  N N 45  
ALA HA   H  N N 46  
ALA HB1  H  N N 47  
ALA HB2  H  N N 48  
ALA HB3  H  N N 49  
ALA HXT  H  N N 50  
ARG N    N  N N 51  
ARG CA   C  N S 52  
ARG C    C  N N 53  
ARG O    O  N N 54  
ARG CB   C  N N 55  
ARG CG   C  N N 56  
ARG CD   C  N N 57  
ARG NE   N  N N 58  
ARG CZ   C  N N 59  
ARG NH1  N  N N 60  
ARG NH2  N  N N 61  
ARG OXT  O  N N 62  
ARG H    H  N N 63  
ARG H2   H  N N 64  
ARG HA   H  N N 65  
ARG HB2  H  N N 66  
ARG HB3  H  N N 67  
ARG HG2  H  N N 68  
ARG HG3  H  N N 69  
ARG HD2  H  N N 70  
ARG HD3  H  N N 71  
ARG HE   H  N N 72  
ARG HH11 H  N N 73  
ARG HH12 H  N N 74  
ARG HH21 H  N N 75  
ARG HH22 H  N N 76  
ARG HXT  H  N N 77  
ASN N    N  N N 78  
ASN CA   C  N S 79  
ASN C    C  N N 80  
ASN O    O  N N 81  
ASN CB   C  N N 82  
ASN CG   C  N N 83  
ASN OD1  O  N N 84  
ASN ND2  N  N N 85  
ASN OXT  O  N N 86  
ASN H    H  N N 87  
ASN H2   H  N N 88  
ASN HA   H  N N 89  
ASN HB2  H  N N 90  
ASN HB3  H  N N 91  
ASN HD21 H  N N 92  
ASN HD22 H  N N 93  
ASN HXT  H  N N 94  
ASP N    N  N N 95  
ASP CA   C  N S 96  
ASP C    C  N N 97  
ASP O    O  N N 98  
ASP CB   C  N N 99  
ASP CG   C  N N 100 
ASP OD1  O  N N 101 
ASP OD2  O  N N 102 
ASP OXT  O  N N 103 
ASP H    H  N N 104 
ASP H2   H  N N 105 
ASP HA   H  N N 106 
ASP HB2  H  N N 107 
ASP HB3  H  N N 108 
ASP HD2  H  N N 109 
ASP HXT  H  N N 110 
CYS N    N  N N 111 
CYS CA   C  N R 112 
CYS C    C  N N 113 
CYS O    O  N N 114 
CYS CB   C  N N 115 
CYS SG   S  N N 116 
CYS OXT  O  N N 117 
CYS H    H  N N 118 
CYS H2   H  N N 119 
CYS HA   H  N N 120 
CYS HB2  H  N N 121 
CYS HB3  H  N N 122 
CYS HG   H  N N 123 
CYS HXT  H  N N 124 
GLN N    N  N N 125 
GLN CA   C  N S 126 
GLN C    C  N N 127 
GLN O    O  N N 128 
GLN CB   C  N N 129 
GLN CG   C  N N 130 
GLN CD   C  N N 131 
GLN OE1  O  N N 132 
GLN NE2  N  N N 133 
GLN OXT  O  N N 134 
GLN H    H  N N 135 
GLN H2   H  N N 136 
GLN HA   H  N N 137 
GLN HB2  H  N N 138 
GLN HB3  H  N N 139 
GLN HG2  H  N N 140 
GLN HG3  H  N N 141 
GLN HE21 H  N N 142 
GLN HE22 H  N N 143 
GLN HXT  H  N N 144 
GLU N    N  N N 145 
GLU CA   C  N S 146 
GLU C    C  N N 147 
GLU O    O  N N 148 
GLU CB   C  N N 149 
GLU CG   C  N N 150 
GLU CD   C  N N 151 
GLU OE1  O  N N 152 
GLU OE2  O  N N 153 
GLU OXT  O  N N 154 
GLU H    H  N N 155 
GLU H2   H  N N 156 
GLU HA   H  N N 157 
GLU HB2  H  N N 158 
GLU HB3  H  N N 159 
GLU HG2  H  N N 160 
GLU HG3  H  N N 161 
GLU HE2  H  N N 162 
GLU HXT  H  N N 163 
GLY N    N  N N 164 
GLY CA   C  N N 165 
GLY C    C  N N 166 
GLY O    O  N N 167 
GLY OXT  O  N N 168 
GLY H    H  N N 169 
GLY H2   H  N N 170 
GLY HA2  H  N N 171 
GLY HA3  H  N N 172 
GLY HXT  H  N N 173 
HIS N    N  N N 174 
HIS CA   C  N S 175 
HIS C    C  N N 176 
HIS O    O  N N 177 
HIS CB   C  N N 178 
HIS CG   C  Y N 179 
HIS ND1  N  Y N 180 
HIS CD2  C  Y N 181 
HIS CE1  C  Y N 182 
HIS NE2  N  Y N 183 
HIS OXT  O  N N 184 
HIS H    H  N N 185 
HIS H2   H  N N 186 
HIS HA   H  N N 187 
HIS HB2  H  N N 188 
HIS HB3  H  N N 189 
HIS HD1  H  N N 190 
HIS HD2  H  N N 191 
HIS HE1  H  N N 192 
HIS HE2  H  N N 193 
HIS HXT  H  N N 194 
HOH O    O  N N 195 
HOH H1   H  N N 196 
HOH H2   H  N N 197 
ILE N    N  N N 198 
ILE CA   C  N S 199 
ILE C    C  N N 200 
ILE O    O  N N 201 
ILE CB   C  N S 202 
ILE CG1  C  N N 203 
ILE CG2  C  N N 204 
ILE CD1  C  N N 205 
ILE OXT  O  N N 206 
ILE H    H  N N 207 
ILE H2   H  N N 208 
ILE HA   H  N N 209 
ILE HB   H  N N 210 
ILE HG12 H  N N 211 
ILE HG13 H  N N 212 
ILE HG21 H  N N 213 
ILE HG22 H  N N 214 
ILE HG23 H  N N 215 
ILE HD11 H  N N 216 
ILE HD12 H  N N 217 
ILE HD13 H  N N 218 
ILE HXT  H  N N 219 
IOD I    I  N N 220 
LEU N    N  N N 221 
LEU CA   C  N S 222 
LEU C    C  N N 223 
LEU O    O  N N 224 
LEU CB   C  N N 225 
LEU CG   C  N N 226 
LEU CD1  C  N N 227 
LEU CD2  C  N N 228 
LEU OXT  O  N N 229 
LEU H    H  N N 230 
LEU H2   H  N N 231 
LEU HA   H  N N 232 
LEU HB2  H  N N 233 
LEU HB3  H  N N 234 
LEU HG   H  N N 235 
LEU HD11 H  N N 236 
LEU HD12 H  N N 237 
LEU HD13 H  N N 238 
LEU HD21 H  N N 239 
LEU HD22 H  N N 240 
LEU HD23 H  N N 241 
LEU HXT  H  N N 242 
LYS N    N  N N 243 
LYS CA   C  N S 244 
LYS C    C  N N 245 
LYS O    O  N N 246 
LYS CB   C  N N 247 
LYS CG   C  N N 248 
LYS CD   C  N N 249 
LYS CE   C  N N 250 
LYS NZ   N  N N 251 
LYS OXT  O  N N 252 
LYS H    H  N N 253 
LYS H2   H  N N 254 
LYS HA   H  N N 255 
LYS HB2  H  N N 256 
LYS HB3  H  N N 257 
LYS HG2  H  N N 258 
LYS HG3  H  N N 259 
LYS HD2  H  N N 260 
LYS HD3  H  N N 261 
LYS HE2  H  N N 262 
LYS HE3  H  N N 263 
LYS HZ1  H  N N 264 
LYS HZ2  H  N N 265 
LYS HZ3  H  N N 266 
LYS HXT  H  N N 267 
MET N    N  N N 268 
MET CA   C  N S 269 
MET C    C  N N 270 
MET O    O  N N 271 
MET CB   C  N N 272 
MET CG   C  N N 273 
MET SD   S  N N 274 
MET CE   C  N N 275 
MET OXT  O  N N 276 
MET H    H  N N 277 
MET H2   H  N N 278 
MET HA   H  N N 279 
MET HB2  H  N N 280 
MET HB3  H  N N 281 
MET HG2  H  N N 282 
MET HG3  H  N N 283 
MET HE1  H  N N 284 
MET HE2  H  N N 285 
MET HE3  H  N N 286 
MET HXT  H  N N 287 
MG  MG   MG N N 288 
PEG C1   C  N N 289 
PEG O1   O  N N 290 
PEG C2   C  N N 291 
PEG O2   O  N N 292 
PEG C3   C  N N 293 
PEG C4   C  N N 294 
PEG O4   O  N N 295 
PEG H11  H  N N 296 
PEG H12  H  N N 297 
PEG HO1  H  N N 298 
PEG H21  H  N N 299 
PEG H22  H  N N 300 
PEG H31  H  N N 301 
PEG H32  H  N N 302 
PEG H41  H  N N 303 
PEG H42  H  N N 304 
PEG HO4  H  N N 305 
PHE N    N  N N 306 
PHE CA   C  N S 307 
PHE C    C  N N 308 
PHE O    O  N N 309 
PHE CB   C  N N 310 
PHE CG   C  Y N 311 
PHE CD1  C  Y N 312 
PHE CD2  C  Y N 313 
PHE CE1  C  Y N 314 
PHE CE2  C  Y N 315 
PHE CZ   C  Y N 316 
PHE OXT  O  N N 317 
PHE H    H  N N 318 
PHE H2   H  N N 319 
PHE HA   H  N N 320 
PHE HB2  H  N N 321 
PHE HB3  H  N N 322 
PHE HD1  H  N N 323 
PHE HD2  H  N N 324 
PHE HE1  H  N N 325 
PHE HE2  H  N N 326 
PHE HZ   H  N N 327 
PHE HXT  H  N N 328 
PRO N    N  N N 329 
PRO CA   C  N S 330 
PRO C    C  N N 331 
PRO O    O  N N 332 
PRO CB   C  N N 333 
PRO CG   C  N N 334 
PRO CD   C  N N 335 
PRO OXT  O  N N 336 
PRO H    H  N N 337 
PRO HA   H  N N 338 
PRO HB2  H  N N 339 
PRO HB3  H  N N 340 
PRO HG2  H  N N 341 
PRO HG3  H  N N 342 
PRO HD2  H  N N 343 
PRO HD3  H  N N 344 
PRO HXT  H  N N 345 
SER N    N  N N 346 
SER CA   C  N S 347 
SER C    C  N N 348 
SER O    O  N N 349 
SER CB   C  N N 350 
SER OG   O  N N 351 
SER OXT  O  N N 352 
SER H    H  N N 353 
SER H2   H  N N 354 
SER HA   H  N N 355 
SER HB2  H  N N 356 
SER HB3  H  N N 357 
SER HG   H  N N 358 
SER HXT  H  N N 359 
THR N    N  N N 360 
THR CA   C  N S 361 
THR C    C  N N 362 
THR O    O  N N 363 
THR CB   C  N R 364 
THR OG1  O  N N 365 
THR CG2  C  N N 366 
THR OXT  O  N N 367 
THR H    H  N N 368 
THR H2   H  N N 369 
THR HA   H  N N 370 
THR HB   H  N N 371 
THR HG1  H  N N 372 
THR HG21 H  N N 373 
THR HG22 H  N N 374 
THR HG23 H  N N 375 
THR HXT  H  N N 376 
TRP N    N  N N 377 
TRP CA   C  N S 378 
TRP C    C  N N 379 
TRP O    O  N N 380 
TRP CB   C  N N 381 
TRP CG   C  Y N 382 
TRP CD1  C  Y N 383 
TRP CD2  C  Y N 384 
TRP NE1  N  Y N 385 
TRP CE2  C  Y N 386 
TRP CE3  C  Y N 387 
TRP CZ2  C  Y N 388 
TRP CZ3  C  Y N 389 
TRP CH2  C  Y N 390 
TRP OXT  O  N N 391 
TRP H    H  N N 392 
TRP H2   H  N N 393 
TRP HA   H  N N 394 
TRP HB2  H  N N 395 
TRP HB3  H  N N 396 
TRP HD1  H  N N 397 
TRP HE1  H  N N 398 
TRP HE3  H  N N 399 
TRP HZ2  H  N N 400 
TRP HZ3  H  N N 401 
TRP HH2  H  N N 402 
TRP HXT  H  N N 403 
TYR N    N  N N 404 
TYR CA   C  N S 405 
TYR C    C  N N 406 
TYR O    O  N N 407 
TYR CB   C  N N 408 
TYR CG   C  Y N 409 
TYR CD1  C  Y N 410 
TYR CD2  C  Y N 411 
TYR CE1  C  Y N 412 
TYR CE2  C  Y N 413 
TYR CZ   C  Y N 414 
TYR OH   O  N N 415 
TYR OXT  O  N N 416 
TYR H    H  N N 417 
TYR H2   H  N N 418 
TYR HA   H  N N 419 
TYR HB2  H  N N 420 
TYR HB3  H  N N 421 
TYR HD1  H  N N 422 
TYR HD2  H  N N 423 
TYR HE1  H  N N 424 
TYR HE2  H  N N 425 
TYR HH   H  N N 426 
TYR HXT  H  N N 427 
VAL N    N  N N 428 
VAL CA   C  N S 429 
VAL C    C  N N 430 
VAL O    O  N N 431 
VAL CB   C  N N 432 
VAL CG1  C  N N 433 
VAL CG2  C  N N 434 
VAL OXT  O  N N 435 
VAL H    H  N N 436 
VAL H2   H  N N 437 
VAL HA   H  N N 438 
VAL HB   H  N N 439 
VAL HG11 H  N N 440 
VAL HG12 H  N N 441 
VAL HG13 H  N N 442 
VAL HG21 H  N N 443 
VAL HG22 H  N N 444 
VAL HG23 H  N N 445 
VAL HXT  H  N N 446 
# 
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 
4LM C   O1   doub N N 1   
4LM C   CA   sing N N 2   
4LM C   O2   sing N N 3   
4LM N   CA   sing N N 4   
4LM N   C4A  doub N N 5   
4LM P   OP1  doub N N 6   
4LM P   OP2  sing N N 7   
4LM P   OP3  sing N N 8   
4LM P   OP4  sing N N 9   
4LM N1  C2   doub Y N 10  
4LM N1  C6   sing Y N 11  
4LM C2  C3   sing Y N 12  
4LM C2  C2A  sing N N 13  
4LM C3  O3   sing N N 14  
4LM C3  C4   doub Y N 15  
4LM C4  C5   sing Y N 16  
4LM C4  C4A  sing N N 17  
4LM C5  C6   doub Y N 18  
4LM C5  C5A  sing N N 19  
4LM CA  CB   doub N N 20  
4LM CB  CG   sing N N 21  
4LM C5A OP4  sing N E 22  
4LM O3  HO3  sing N N 23  
4LM C6  H6   sing N N 24  
4LM CB  HB   sing N N 25  
4LM CG  HG   sing N N 26  
4LM CG  HGA  sing N N 27  
4LM CG  HGB  sing N N 28  
4LM C2A H2A  sing N N 29  
4LM C2A H2A1 sing N N 30  
4LM C2A H2A2 sing N N 31  
4LM C4A H4A  sing N N 32  
4LM C5A H5A  sing N N 33  
4LM C5A H5A1 sing N N 34  
4LM OP2 HOP2 sing N N 35  
4LM OP3 HOP3 sing N N 36  
4LM O2  H2   sing N N 37  
ALA N   CA   sing N N 38  
ALA N   H    sing N N 39  
ALA N   H2   sing N N 40  
ALA CA  C    sing N N 41  
ALA CA  CB   sing N N 42  
ALA CA  HA   sing N N 43  
ALA C   O    doub N N 44  
ALA C   OXT  sing N N 45  
ALA CB  HB1  sing N N 46  
ALA CB  HB2  sing N N 47  
ALA CB  HB3  sing N N 48  
ALA OXT HXT  sing N N 49  
ARG N   CA   sing N N 50  
ARG N   H    sing N N 51  
ARG N   H2   sing N N 52  
ARG CA  C    sing N N 53  
ARG CA  CB   sing N N 54  
ARG CA  HA   sing N N 55  
ARG C   O    doub N N 56  
ARG C   OXT  sing N N 57  
ARG CB  CG   sing N N 58  
ARG CB  HB2  sing N N 59  
ARG CB  HB3  sing N N 60  
ARG CG  CD   sing N N 61  
ARG CG  HG2  sing N N 62  
ARG CG  HG3  sing N N 63  
ARG CD  NE   sing N N 64  
ARG CD  HD2  sing N N 65  
ARG CD  HD3  sing N N 66  
ARG NE  CZ   sing N N 67  
ARG NE  HE   sing N N 68  
ARG CZ  NH1  sing N N 69  
ARG CZ  NH2  doub N N 70  
ARG NH1 HH11 sing N N 71  
ARG NH1 HH12 sing N N 72  
ARG NH2 HH21 sing N N 73  
ARG NH2 HH22 sing N N 74  
ARG OXT HXT  sing N N 75  
ASN N   CA   sing N N 76  
ASN N   H    sing N N 77  
ASN N   H2   sing N N 78  
ASN CA  C    sing N N 79  
ASN CA  CB   sing N N 80  
ASN CA  HA   sing N N 81  
ASN C   O    doub N N 82  
ASN C   OXT  sing N N 83  
ASN CB  CG   sing N N 84  
ASN CB  HB2  sing N N 85  
ASN CB  HB3  sing N N 86  
ASN CG  OD1  doub N N 87  
ASN CG  ND2  sing N N 88  
ASN ND2 HD21 sing N N 89  
ASN ND2 HD22 sing N N 90  
ASN OXT HXT  sing N N 91  
ASP N   CA   sing N N 92  
ASP N   H    sing N N 93  
ASP N   H2   sing N N 94  
ASP CA  C    sing N N 95  
ASP CA  CB   sing N N 96  
ASP CA  HA   sing N N 97  
ASP C   O    doub N N 98  
ASP C   OXT  sing N N 99  
ASP CB  CG   sing N N 100 
ASP CB  HB2  sing N N 101 
ASP CB  HB3  sing N N 102 
ASP CG  OD1  doub N N 103 
ASP CG  OD2  sing N N 104 
ASP OD2 HD2  sing N N 105 
ASP OXT HXT  sing N N 106 
CYS N   CA   sing N N 107 
CYS N   H    sing N N 108 
CYS N   H2   sing N N 109 
CYS CA  C    sing N N 110 
CYS CA  CB   sing N N 111 
CYS CA  HA   sing N N 112 
CYS C   O    doub N N 113 
CYS C   OXT  sing N N 114 
CYS CB  SG   sing N N 115 
CYS CB  HB2  sing N N 116 
CYS CB  HB3  sing N N 117 
CYS SG  HG   sing N N 118 
CYS OXT HXT  sing N N 119 
GLN N   CA   sing N N 120 
GLN N   H    sing N N 121 
GLN N   H2   sing N N 122 
GLN CA  C    sing N N 123 
GLN CA  CB   sing N N 124 
GLN CA  HA   sing N N 125 
GLN C   O    doub N N 126 
GLN C   OXT  sing N N 127 
GLN CB  CG   sing N N 128 
GLN CB  HB2  sing N N 129 
GLN CB  HB3  sing N N 130 
GLN CG  CD   sing N N 131 
GLN CG  HG2  sing N N 132 
GLN CG  HG3  sing N N 133 
GLN CD  OE1  doub N N 134 
GLN CD  NE2  sing N N 135 
GLN NE2 HE21 sing N N 136 
GLN NE2 HE22 sing N N 137 
GLN OXT HXT  sing N N 138 
GLU N   CA   sing N N 139 
GLU N   H    sing N N 140 
GLU N   H2   sing N N 141 
GLU CA  C    sing N N 142 
GLU CA  CB   sing N N 143 
GLU CA  HA   sing N N 144 
GLU C   O    doub N N 145 
GLU C   OXT  sing N N 146 
GLU CB  CG   sing N N 147 
GLU CB  HB2  sing N N 148 
GLU CB  HB3  sing N N 149 
GLU CG  CD   sing N N 150 
GLU CG  HG2  sing N N 151 
GLU CG  HG3  sing N N 152 
GLU CD  OE1  doub N N 153 
GLU CD  OE2  sing N N 154 
GLU OE2 HE2  sing N N 155 
GLU OXT HXT  sing N N 156 
GLY N   CA   sing N N 157 
GLY N   H    sing N N 158 
GLY N   H2   sing N N 159 
GLY CA  C    sing N N 160 
GLY CA  HA2  sing N N 161 
GLY CA  HA3  sing N N 162 
GLY C   O    doub N N 163 
GLY C   OXT  sing N N 164 
GLY OXT HXT  sing N N 165 
HIS N   CA   sing N N 166 
HIS N   H    sing N N 167 
HIS N   H2   sing N N 168 
HIS CA  C    sing N N 169 
HIS CA  CB   sing N N 170 
HIS CA  HA   sing N N 171 
HIS C   O    doub N N 172 
HIS C   OXT  sing N N 173 
HIS CB  CG   sing N N 174 
HIS CB  HB2  sing N N 175 
HIS CB  HB3  sing N N 176 
HIS CG  ND1  sing Y N 177 
HIS CG  CD2  doub Y N 178 
HIS ND1 CE1  doub Y N 179 
HIS ND1 HD1  sing N N 180 
HIS CD2 NE2  sing Y N 181 
HIS CD2 HD2  sing N N 182 
HIS CE1 NE2  sing Y N 183 
HIS CE1 HE1  sing N N 184 
HIS NE2 HE2  sing N N 185 
HIS OXT HXT  sing N N 186 
HOH O   H1   sing N N 187 
HOH O   H2   sing N N 188 
ILE N   CA   sing N N 189 
ILE N   H    sing N N 190 
ILE N   H2   sing N N 191 
ILE CA  C    sing N N 192 
ILE CA  CB   sing N N 193 
ILE CA  HA   sing N N 194 
ILE C   O    doub N N 195 
ILE C   OXT  sing N N 196 
ILE CB  CG1  sing N N 197 
ILE CB  CG2  sing N N 198 
ILE CB  HB   sing N N 199 
ILE CG1 CD1  sing N N 200 
ILE CG1 HG12 sing N N 201 
ILE CG1 HG13 sing N N 202 
ILE CG2 HG21 sing N N 203 
ILE CG2 HG22 sing N N 204 
ILE CG2 HG23 sing N N 205 
ILE CD1 HD11 sing N N 206 
ILE CD1 HD12 sing N N 207 
ILE CD1 HD13 sing N N 208 
ILE OXT HXT  sing N N 209 
LEU N   CA   sing N N 210 
LEU N   H    sing N N 211 
LEU N   H2   sing N N 212 
LEU CA  C    sing N N 213 
LEU CA  CB   sing N N 214 
LEU CA  HA   sing N N 215 
LEU C   O    doub N N 216 
LEU C   OXT  sing N N 217 
LEU CB  CG   sing N N 218 
LEU CB  HB2  sing N N 219 
LEU CB  HB3  sing N N 220 
LEU CG  CD1  sing N N 221 
LEU CG  CD2  sing N N 222 
LEU CG  HG   sing N N 223 
LEU CD1 HD11 sing N N 224 
LEU CD1 HD12 sing N N 225 
LEU CD1 HD13 sing N N 226 
LEU CD2 HD21 sing N N 227 
LEU CD2 HD22 sing N N 228 
LEU CD2 HD23 sing N N 229 
LEU OXT HXT  sing N N 230 
LYS N   CA   sing N N 231 
LYS N   H    sing N N 232 
LYS N   H2   sing N N 233 
LYS CA  C    sing N N 234 
LYS CA  CB   sing N N 235 
LYS CA  HA   sing N N 236 
LYS C   O    doub N N 237 
LYS C   OXT  sing N N 238 
LYS CB  CG   sing N N 239 
LYS CB  HB2  sing N N 240 
LYS CB  HB3  sing N N 241 
LYS CG  CD   sing N N 242 
LYS CG  HG2  sing N N 243 
LYS CG  HG3  sing N N 244 
LYS CD  CE   sing N N 245 
LYS CD  HD2  sing N N 246 
LYS CD  HD3  sing N N 247 
LYS CE  NZ   sing N N 248 
LYS CE  HE2  sing N N 249 
LYS CE  HE3  sing N N 250 
LYS NZ  HZ1  sing N N 251 
LYS NZ  HZ2  sing N N 252 
LYS NZ  HZ3  sing N N 253 
LYS OXT HXT  sing N N 254 
MET N   CA   sing N N 255 
MET N   H    sing N N 256 
MET N   H2   sing N N 257 
MET CA  C    sing N N 258 
MET CA  CB   sing N N 259 
MET CA  HA   sing N N 260 
MET C   O    doub N N 261 
MET C   OXT  sing N N 262 
MET CB  CG   sing N N 263 
MET CB  HB2  sing N N 264 
MET CB  HB3  sing N N 265 
MET CG  SD   sing N N 266 
MET CG  HG2  sing N N 267 
MET CG  HG3  sing N N 268 
MET SD  CE   sing N N 269 
MET CE  HE1  sing N N 270 
MET CE  HE2  sing N N 271 
MET CE  HE3  sing N N 272 
MET OXT HXT  sing N N 273 
PEG C1  O1   sing N N 274 
PEG C1  C2   sing N N 275 
PEG C1  H11  sing N N 276 
PEG C1  H12  sing N N 277 
PEG O1  HO1  sing N N 278 
PEG C2  O2   sing N N 279 
PEG C2  H21  sing N N 280 
PEG C2  H22  sing N N 281 
PEG O2  C3   sing N N 282 
PEG C3  C4   sing N N 283 
PEG C3  H31  sing N N 284 
PEG C3  H32  sing N N 285 
PEG C4  O4   sing N N 286 
PEG C4  H41  sing N N 287 
PEG C4  H42  sing N N 288 
PEG O4  HO4  sing N N 289 
PHE N   CA   sing N N 290 
PHE N   H    sing N N 291 
PHE N   H2   sing N N 292 
PHE CA  C    sing N N 293 
PHE CA  CB   sing N N 294 
PHE CA  HA   sing N N 295 
PHE C   O    doub N N 296 
PHE C   OXT  sing N N 297 
PHE CB  CG   sing N N 298 
PHE CB  HB2  sing N N 299 
PHE CB  HB3  sing N N 300 
PHE CG  CD1  doub Y N 301 
PHE CG  CD2  sing Y N 302 
PHE CD1 CE1  sing Y N 303 
PHE CD1 HD1  sing N N 304 
PHE CD2 CE2  doub Y N 305 
PHE CD2 HD2  sing N N 306 
PHE CE1 CZ   doub Y N 307 
PHE CE1 HE1  sing N N 308 
PHE CE2 CZ   sing Y N 309 
PHE CE2 HE2  sing N N 310 
PHE CZ  HZ   sing N N 311 
PHE OXT HXT  sing N N 312 
PRO N   CA   sing N N 313 
PRO N   CD   sing N N 314 
PRO N   H    sing N N 315 
PRO CA  C    sing N N 316 
PRO CA  CB   sing N N 317 
PRO CA  HA   sing N N 318 
PRO C   O    doub N N 319 
PRO C   OXT  sing N N 320 
PRO CB  CG   sing N N 321 
PRO CB  HB2  sing N N 322 
PRO CB  HB3  sing N N 323 
PRO CG  CD   sing N N 324 
PRO CG  HG2  sing N N 325 
PRO CG  HG3  sing N N 326 
PRO CD  HD2  sing N N 327 
PRO CD  HD3  sing N N 328 
PRO OXT HXT  sing N N 329 
SER N   CA   sing N N 330 
SER N   H    sing N N 331 
SER N   H2   sing N N 332 
SER CA  C    sing N N 333 
SER CA  CB   sing N N 334 
SER CA  HA   sing N N 335 
SER C   O    doub N N 336 
SER C   OXT  sing N N 337 
SER CB  OG   sing N N 338 
SER CB  HB2  sing N N 339 
SER CB  HB3  sing N N 340 
SER OG  HG   sing N N 341 
SER OXT HXT  sing N N 342 
THR N   CA   sing N N 343 
THR N   H    sing N N 344 
THR N   H2   sing N N 345 
THR CA  C    sing N N 346 
THR CA  CB   sing N N 347 
THR CA  HA   sing N N 348 
THR C   O    doub N N 349 
THR C   OXT  sing N N 350 
THR CB  OG1  sing N N 351 
THR CB  CG2  sing N N 352 
THR CB  HB   sing N N 353 
THR OG1 HG1  sing N N 354 
THR CG2 HG21 sing N N 355 
THR CG2 HG22 sing N N 356 
THR CG2 HG23 sing N N 357 
THR OXT HXT  sing N N 358 
TRP N   CA   sing N N 359 
TRP N   H    sing N N 360 
TRP N   H2   sing N N 361 
TRP CA  C    sing N N 362 
TRP CA  CB   sing N N 363 
TRP CA  HA   sing N N 364 
TRP C   O    doub N N 365 
TRP C   OXT  sing N N 366 
TRP CB  CG   sing N N 367 
TRP CB  HB2  sing N N 368 
TRP CB  HB3  sing N N 369 
TRP CG  CD1  doub Y N 370 
TRP CG  CD2  sing Y N 371 
TRP CD1 NE1  sing Y N 372 
TRP CD1 HD1  sing N N 373 
TRP CD2 CE2  doub Y N 374 
TRP CD2 CE3  sing Y N 375 
TRP NE1 CE2  sing Y N 376 
TRP NE1 HE1  sing N N 377 
TRP CE2 CZ2  sing Y N 378 
TRP CE3 CZ3  doub Y N 379 
TRP CE3 HE3  sing N N 380 
TRP CZ2 CH2  doub Y N 381 
TRP CZ2 HZ2  sing N N 382 
TRP CZ3 CH2  sing Y N 383 
TRP CZ3 HZ3  sing N N 384 
TRP CH2 HH2  sing N N 385 
TRP OXT HXT  sing N N 386 
TYR N   CA   sing N N 387 
TYR N   H    sing N N 388 
TYR N   H2   sing N N 389 
TYR CA  C    sing N N 390 
TYR CA  CB   sing N N 391 
TYR CA  HA   sing N N 392 
TYR C   O    doub N N 393 
TYR C   OXT  sing N N 394 
TYR CB  CG   sing N N 395 
TYR CB  HB2  sing N N 396 
TYR CB  HB3  sing N N 397 
TYR CG  CD1  doub Y N 398 
TYR CG  CD2  sing Y N 399 
TYR CD1 CE1  sing Y N 400 
TYR CD1 HD1  sing N N 401 
TYR CD2 CE2  doub Y N 402 
TYR CD2 HD2  sing N N 403 
TYR CE1 CZ   doub Y N 404 
TYR CE1 HE1  sing N N 405 
TYR CE2 CZ   sing Y N 406 
TYR CE2 HE2  sing N N 407 
TYR CZ  OH   sing N N 408 
TYR OH  HH   sing N N 409 
TYR OXT HXT  sing N N 410 
VAL N   CA   sing N N 411 
VAL N   H    sing N N 412 
VAL N   H2   sing N N 413 
VAL CA  C    sing N N 414 
VAL CA  CB   sing N N 415 
VAL CA  HA   sing N N 416 
VAL C   O    doub N N 417 
VAL C   OXT  sing N N 418 
VAL CB  CG1  sing N N 419 
VAL CB  CG2  sing N N 420 
VAL CB  HB   sing N N 421 
VAL CG1 HG11 sing N N 422 
VAL CG1 HG12 sing N N 423 
VAL CG1 HG13 sing N N 424 
VAL CG2 HG21 sing N N 425 
VAL CG2 HG22 sing N N 426 
VAL CG2 HG23 sing N N 427 
VAL OXT HXT  sing N N 428 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1DP2GM137417-01 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8SF4 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9AXJ 
_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]   0.008551 
_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]   0.008551 
_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]   0.008551 
_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 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C  6  6  2.310  20.844 1.020  10.208 1.589 0.569  0.865 51.651 0.216   
H  1  1  0.493  10.511 0.323  26.126 0.140 3.142  0.041 57.800 0.003   
I  53 53 20.147 4.347  18.995 0.381  7.514 27.766 2.273 66.878 3.748   
MG 12 12 5.427  2.828  2.176  79.261 1.228 0.381  2.310 7.194  0.935   
N  7  7  12.222 0.006  3.135  9.893  2.014 28.997 1.167 0.583  -11.538 
O  8  8  3.049  13.277 2.287  5.701  1.546 0.324  0.867 32.909 0.251   
P  15 15 6.435  1.907  4.179  27.157 1.780 0.526  1.491 68.164 1.268   
S  16 16 6.905  1.468  5.203  22.215 1.438 0.254  1.586 56.172 1.049   
# 
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_site.calc_flag 
_atom_site.pdbx_tls_group_id 
ATOM   1    N  N   . TYR A 1 3   ? 21.283  26.305  -49.765 1.000 64.812 ? 3   TYR A N   1 ? 1  
ATOM   2    C  CA  . TYR A 1 3   ? 20.033  26.973  -49.333 1.000 58.629 ? 3   TYR A CA  1 ? 1  
ATOM   3    C  C   . TYR A 1 3   ? 18.966  26.721  -50.401 1.000 54.034 ? 3   TYR A C   1 ? 1  
ATOM   4    O  O   . TYR A 1 3   ? 18.399  27.680  -50.952 1.000 56.021 ? 3   TYR A O   1 ? 1  
ATOM   5    C  CB  . TYR A 1 3   ? 20.252  28.476  -49.123 1.000 62.517 ? 3   TYR A CB  1 ? 1  
ATOM   6    N  N   . GLU A 1 4   ? 18.644  25.448  -50.656 1.000 48.784 ? 4   GLU A N   1 ? 1  
ATOM   7    C  CA  . GLU A 1 4   ? 17.658  25.088  -51.665 1.000 39.773 ? 4   GLU A CA  1 ? 1  
ATOM   8    C  C   . GLU A 1 4   ? 16.264  25.466  -51.108 1.000 34.017 ? 4   GLU A C   1 ? 1  
ATOM   9    O  O   . GLU A 1 4   ? 15.971  25.276  -49.884 1.000 34.935 ? 4   GLU A O   1 ? 1  
ATOM   10   C  CB  . GLU A 1 4   ? 17.753  23.603  -52.001 1.000 43.224 ? 4   GLU A CB  1 ? 1  
ATOM   11   C  CG  . GLU A 1 4   ? 18.922  23.295  -52.874 1.000 53.113 ? 4   GLU A CG  1 ? 1  
ATOM   12   C  CD  . GLU A 1 4   ? 18.820  22.021  -53.666 1.000 56.489 ? 4   GLU A CD  1 ? 1  
ATOM   13   O  OE1 . GLU A 1 4   ? 18.055  21.103  -53.223 1.000 54.639 ? 4   GLU A OE1 1 ? 1  
ATOM   14   O  OE2 . GLU A 1 4   ? 19.516  21.952  -54.768 1.000 59.314 ? 4   GLU A OE2 1 ? 1  
ATOM   15   N  N   . GLY A 1 5   ? 15.403  25.846  -51.992 1.000 26.819 ? 5   GLY A N   1 ? 1  
ATOM   16   C  CA  . GLY A 1 5   ? 14.065  26.268  -51.639 1.000 24.393 ? 5   GLY A CA  1 ? 1  
ATOM   17   C  C   . GLY A 1 5   ? 13.133  25.086  -51.459 1.000 22.221 ? 5   GLY A C   1 ? 1  
ATOM   18   O  O   . GLY A 1 5   ? 13.486  23.944  -51.792 1.000 20.646 ? 5   GLY A O   1 ? 1  
ATOM   19   N  N   . PHE A 1 6   ? 12.013  25.383  -50.818 1.000 21.450 ? 6   PHE A N   1 ? 1  
ATOM   20   C  CA  . PHE A 1 6   ? 11.042  24.343  -50.425 1.000 19.966 ? 6   PHE A CA  1 ? 1  
ATOM   21   C  C   . PHE A 1 6   ? 10.620  23.539  -51.660 1.000 18.392 ? 6   PHE A C   1 ? 1  
ATOM   22   O  O   . PHE A 1 6   ? 10.634  22.304  -51.552 1.000 19.263 ? 6   PHE A O   1 ? 1  
ATOM   23   C  CB  . PHE A 1 6   ? 9.839   25.017  -49.795 1.000 20.286 ? 6   PHE A CB  1 ? 1  
ATOM   24   C  CG  . PHE A 1 6   ? 8.863   24.002  -49.246 1.000 20.449 ? 6   PHE A CG  1 ? 1  
ATOM   25   C  CD1 . PHE A 1 6   ? 7.946   23.367  -50.054 1.000 20.825 ? 6   PHE A CD1 1 ? 1  
ATOM   26   C  CD2 . PHE A 1 6   ? 8.916   23.674  -47.929 1.000 22.022 ? 6   PHE A CD2 1 ? 1  
ATOM   27   C  CE1 . PHE A 1 6   ? 7.096   22.379  -49.574 1.000 21.962 ? 6   PHE A CE1 1 ? 1  
ATOM   28   C  CE2 . PHE A 1 6   ? 8.030   22.754  -47.418 1.000 22.282 ? 6   PHE A CE2 1 ? 1  
ATOM   29   C  CZ  . PHE A 1 6   ? 7.133   22.094  -48.229 1.000 22.383 ? 6   PHE A CZ  1 ? 1  
ATOM   30   N  N   . GLU A 1 7   ? 10.231  24.199  -52.740 1.000 19.623 ? 7   GLU A N   1 ? 1  
ATOM   31   C  CA  . GLU A 1 7   ? 9.656   23.482  -53.903 1.000 19.645 ? 7   GLU A CA  1 ? 1  
ATOM   32   C  C   . GLU A 1 7   ? 10.741  22.581  -54.500 1.000 19.353 ? 7   GLU A C   1 ? 1  
ATOM   33   O  O   . GLU A 1 7   ? 10.439  21.529  -55.027 1.000 18.929 ? 7   GLU A O   1 ? 1  
ATOM   34   C  CB  . GLU A 1 7   ? 9.084   24.511  -54.872 1.000 21.838 ? 7   GLU A CB  1 ? 1  
ATOM   35   C  CG  . GLU A 1 7   ? 7.934   25.329  -54.297 1.000 23.601 ? 7   GLU A CG  1 ? 1  
ATOM   36   C  CD  . GLU A 1 7   ? 8.288   26.614  -53.578 1.000 24.780 ? 7   GLU A CD  1 ? 1  
ATOM   37   O  OE1 . GLU A 1 7   ? 7.344   27.363  -53.307 1.000 27.955 ? 7   GLU A OE1 1 ? 1  
ATOM   38   O  OE2 . GLU A 1 7   ? 9.515   26.882  -53.272 1.000 24.624 ? 7   GLU A OE2 1 ? 1  
ATOM   39   N  N   . THR A 1 8   ? 12.013  23.046  -54.481 1.000 18.622 ? 8   THR A N   1 ? 1  
ATOM   40   C  CA  . THR A 1 8   ? 13.129  22.235  -54.953 1.000 19.523 ? 8   THR A CA  1 ? 1  
ATOM   41   C  C   . THR A 1 8   ? 13.291  20.986  -54.111 1.000 19.165 ? 8   THR A C   1 ? 1  
ATOM   42   O  O   . THR A 1 8   ? 13.406  19.876  -54.637 1.000 19.601 ? 8   THR A O   1 ? 1  
ATOM   43   C  CB  . THR A 1 8   ? 14.427  23.069  -54.994 1.000 20.902 ? 8   THR A CB  1 ? 1  
ATOM   44   O  OG1 . THR A 1 8   ? 14.134  24.292  -55.694 1.000 20.629 ? 8   THR A OG1 1 ? 1  
ATOM   45   C  CG2 . THR A 1 8   ? 15.569  22.298  -55.587 1.000 22.462 ? 8   THR A CG2 1 ? 1  
ATOM   46   N  N   . LEU A 1 9   ? 13.304  21.165  -52.792 1.000 18.309 ? 9   LEU A N   1 ? 2  
ATOM   47   C  CA  . LEU A 1 9   ? 13.404  20.011  -51.879 1.000 17.654 ? 9   LEU A CA  1 ? 2  
ATOM   48   C  C   . LEU A 1 9   ? 12.257  19.033  -52.056 1.000 17.983 ? 9   LEU A C   1 ? 2  
ATOM   49   O  O   . LEU A 1 9   ? 12.453  17.798  -51.937 1.000 18.550 ? 9   LEU A O   1 ? 2  
ATOM   50   C  CB  . LEU A 1 9   ? 13.466  20.496  -50.429 1.000 19.051 ? 9   LEU A CB  1 ? 2  
ATOM   51   C  CG  . LEU A 1 9   ? 14.743  21.255  -50.051 1.000 20.903 ? 9   LEU A CG  1 ? 2  
ATOM   52   C  CD1 . LEU A 1 9   ? 14.565  21.849  -48.646 1.000 23.705 ? 9   LEU A CD1 1 ? 2  
ATOM   53   C  CD2 . LEU A 1 9   ? 15.989  20.377  -50.045 1.000 23.294 ? 9   LEU A CD2 1 ? 2  
ATOM   54   N  N   . ALA A 1 10  ? 11.040  19.516  -52.242 1.000 17.664 ? 10  ALA A N   1 ? 2  
ATOM   55   C  CA  . ALA A 1 10  ? 9.874   18.629  -52.316 1.000 18.386 ? 10  ALA A CA  1 ? 2  
ATOM   56   C  C   . ALA A 1 10  ? 10.064  17.680  -53.499 1.000 19.182 ? 10  ALA A C   1 ? 2  
ATOM   57   O  O   . ALA A 1 10  ? 9.445   16.604  -53.487 1.000 20.724 ? 10  ALA A O   1 ? 2  
ATOM   58   C  CB  . ALA A 1 10  ? 8.600   19.446  -52.426 1.000 17.798 ? 10  ALA A CB  1 ? 2  
ATOM   59   N  N   . ILE A 1 11  ? 10.749  18.112  -54.567 1.000 18.130 ? 11  ILE A N   1 ? 2  
ATOM   60   C  CA  . ILE A 1 11  ? 10.926  17.306  -55.777 1.000 18.031 ? 11  ILE A CA  1 ? 2  
ATOM   61   C  C   . ILE A 1 11  ? 12.186  16.457  -55.682 1.000 18.745 ? 11  ILE A C   1 ? 2  
ATOM   62   O  O   . ILE A 1 11  ? 12.210  15.385  -56.331 1.000 20.054 ? 11  ILE A O   1 ? 2  
ATOM   63   C  CB  . ILE A 1 11  ? 10.859  18.225  -57.018 1.000 18.418 ? 11  ILE A CB  1 ? 2  
ATOM   64   C  CG1 . ILE A 1 11  ? 9.418   18.731  -57.144 1.000 19.375 ? 11  ILE A CG1 1 ? 2  
ATOM   65   C  CG2 . ILE A 1 11  ? 11.323  17.540  -58.270 1.000 19.984 ? 11  ILE A CG2 1 ? 2  
ATOM   66   C  CD1 . ILE A 1 11  ? 9.282   19.956  -58.039 1.000 20.402 ? 11  ILE A CD1 1 ? 2  
ATOM   67   N  N   . HIS A 1 12  ? 13.226  16.939  -55.019 1.000 17.446 ? 12  HIS A N   1 ? 2  
ATOM   68   C  CA  . HIS A 1 12  ? 14.579  16.353  -55.110 1.000 18.929 ? 12  HIS A CA  1 ? 2  
ATOM   69   C  C   . HIS A 1 12  ? 15.046  15.673  -53.835 1.000 19.854 ? 12  HIS A C   1 ? 2  
ATOM   70   O  O   . HIS A 1 12  ? 15.949  14.817  -53.939 1.000 20.340 ? 12  HIS A O   1 ? 2  
ATOM   71   C  CB  . HIS A 1 12  ? 15.592  17.378  -55.605 1.000 20.135 ? 12  HIS A CB  1 ? 2  
ATOM   72   C  CG  . HIS A 1 12  ? 15.305  17.826  -57.004 1.000 21.287 ? 12  HIS A CG  1 ? 2  
ATOM   73   N  ND1 . HIS A 1 12  ? 15.643  17.061  -58.129 1.000 23.738 ? 12  HIS A ND1 1 ? 2  
ATOM   74   C  CD2 . HIS A 1 12  ? 14.644  18.909  -57.478 1.000 19.061 ? 12  HIS A CD2 1 ? 2  
ATOM   75   C  CE1 . HIS A 1 12  ? 15.244  17.716  -59.225 1.000 24.317 ? 12  HIS A CE1 1 ? 2  
ATOM   76   N  NE2 . HIS A 1 12  ? 14.682  18.878  -58.879 1.000 20.392 ? 12  HIS A NE2 1 ? 2  
ATOM   77   N  N   . ALA A 1 13  ? 14.627  16.120  -52.627 1.000 18.240 ? 13  ALA A N   1 ? 2  
ATOM   78   C  CA  . ALA A 1 13  ? 15.204  15.583  -51.396 1.000 18.601 ? 13  ALA A CA  1 ? 2  
ATOM   79   C  C   . ALA A 1 13  ? 14.800  14.118  -51.292 1.000 19.115 ? 13  ALA A C   1 ? 2  
ATOM   80   O  O   . ALA A 1 13  ? 13.592  13.806  -51.428 1.000 19.795 ? 13  ALA A O   1 ? 2  
ATOM   81   C  CB  . ALA A 1 13  ? 14.773  16.372  -50.184 1.000 19.770 ? 13  ALA A CB  1 ? 2  
ATOM   82   N  N   . GLY A 1 14  ? 15.774  13.264  -51.011 1.000 19.816 ? 14  GLY A N   1 ? 2  
ATOM   83   C  CA  . GLY A 1 14  ? 15.552  11.806  -50.907 1.000 21.078 ? 14  GLY A CA  1 ? 2  
ATOM   84   C  C   . GLY A 1 14  ? 15.372  11.166  -52.257 1.000 19.743 ? 14  GLY A C   1 ? 2  
ATOM   85   O  O   . GLY A 1 14  ? 15.070  9.931   -52.317 1.000 21.319 ? 14  GLY A O   1 ? 2  
ATOM   86   N  N   . GLN A 1 15  ? 15.482  11.920  -53.344 1.000 18.435 ? 15  GLN A N   1 ? 2  
ATOM   87   C  CA  . GLN A 1 15  ? 14.977  11.499  -54.671 1.000 19.193 ? 15  GLN A CA  1 ? 2  
ATOM   88   C  C   . GLN A 1 15  ? 16.029  11.744  -55.738 1.000 19.926 ? 15  GLN A C   1 ? 2  
ATOM   89   O  O   . GLN A 1 15  ? 15.678  12.045  -56.892 1.000 21.180 ? 15  GLN A O   1 ? 2  
ATOM   90   C  CB  . GLN A 1 15  ? 13.686  12.236  -54.952 1.000 19.989 ? 15  GLN A CB  1 ? 2  
ATOM   91   C  CG  . GLN A 1 15  ? 12.569  11.913  -53.963 1.000 19.446 ? 15  GLN A CG  1 ? 2  
ATOM   92   C  CD  . GLN A 1 15  ? 11.374  12.800  -54.193 1.000 20.142 ? 15  GLN A CD  1 ? 2  
ATOM   93   O  OE1 . GLN A 1 15  ? 10.511  12.435  -55.058 1.000 22.398 ? 15  GLN A OE1 1 ? 2  
ATOM   94   N  NE2 . GLN A 1 15  ? 11.257  13.906  -53.441 1.000 19.395 ? 15  GLN A NE2 1 ? 2  
ATOM   95   N  N   . GLU A 1 16  ? 17.280  11.460  -55.424 1.000 21.134 ? 16  GLU A N   1 ? 2  
ATOM   96   C  CA  . GLU A 1 16  ? 18.322  11.388  -56.463 1.000 23.927 ? 16  GLU A CA  1 ? 2  
ATOM   97   C  C   . GLU A 1 16  ? 17.952  10.340  -57.510 1.000 23.656 ? 16  GLU A C   1 ? 2  
ATOM   98   O  O   . GLU A 1 16  ? 17.381  9.272   -57.146 1.000 22.133 ? 16  GLU A O   1 ? 2  
ATOM   99   C  CB  . GLU A 1 16  ? 19.648  11.089  -55.816 1.000 28.342 ? 16  GLU A CB  1 ? 2  
ATOM   100  C  CG  . GLU A 1 16  ? 20.723  11.256  -56.873 1.000 38.551 ? 16  GLU A CG  1 ? 2  
ATOM   101  C  CD  . GLU A 1 16  ? 22.177  11.157  -56.461 1.000 47.085 ? 16  GLU A CD  1 ? 2  
ATOM   102  O  OE1 . GLU A 1 16  ? 22.444  10.909  -55.212 1.000 52.328 ? 16  GLU A OE1 1 ? 2  
ATOM   103  O  OE2 . GLU A 1 16  ? 23.043  11.291  -57.410 1.000 49.258 ? 16  GLU A OE2 1 ? 2  
ATOM   104  N  N   . ALA A 1 17  ? 18.349  10.549  -58.750 1.000 20.725 ? 17  ALA A N   1 ? 3  
ATOM   105  C  CA  . ALA A 1 17  ? 18.048  9.560   -59.788 1.000 19.630 ? 17  ALA A CA  1 ? 3  
ATOM   106  C  C   . ALA A 1 17  ? 18.658  8.198   -59.415 1.000 19.150 ? 17  ALA A C   1 ? 3  
ATOM   107  O  O   . ALA A 1 17  ? 19.743  8.105   -58.772 1.000 20.439 ? 17  ALA A O   1 ? 3  
ATOM   108  C  CB  . ALA A 1 17  ? 18.541  10.006  -61.123 1.000 21.420 ? 17  ALA A CB  1 ? 3  
ATOM   109  N  N   . ASP A 1 18  ? 17.991  7.143   -59.868 1.000 19.104 ? 18  ASP A N   1 ? 3  
ATOM   110  C  CA  . ASP A 1 18  ? 18.448  5.770   -59.511 1.000 19.769 ? 18  ASP A CA  1 ? 3  
ATOM   111  C  C   . ASP A 1 18  ? 19.895  5.588   -59.956 1.000 19.290 ? 18  ASP A C   1 ? 3  
ATOM   112  O  O   . ASP A 1 18  ? 20.241  5.887   -61.082 1.000 19.652 ? 18  ASP A O   1 ? 3  
ATOM   113  C  CB  . ASP A 1 18  ? 17.541  4.783   -60.188 1.000 18.659 ? 18  ASP A CB  1 ? 3  
ATOM   114  C  CG  . ASP A 1 18  ? 17.885  3.322   -59.927 1.000 20.399 ? 18  ASP A CG  1 ? 3  
ATOM   115  O  OD1 . ASP A 1 18  ? 17.933  2.986   -58.715 1.000 21.751 ? 18  ASP A OD1 1 ? 3  
ATOM   116  O  OD2 . ASP A 1 18  ? 18.054  2.527   -60.917 1.000 20.052 ? 18  ASP A OD2 1 ? 3  
ATOM   117  N  N   . ALA A 1 19  ? 20.690  4.972   -59.123 1.000 20.365 ? 19  ALA A N   1 ? 3  
ATOM   118  C  CA  . ALA A 1 19  ? 22.125  4.767   -59.394 1.000 22.489 ? 19  ALA A CA  1 ? 3  
ATOM   119  C  C   . ALA A 1 19  ? 22.322  3.850   -60.630 1.000 22.138 ? 19  ALA A C   1 ? 3  
ATOM   120  O  O   . ALA A 1 19  ? 23.138  4.174   -61.504 1.000 24.073 ? 19  ALA A O   1 ? 3  
ATOM   121  C  CB  . ALA A 1 19  ? 22.769  4.173   -58.201 1.000 24.603 ? 19  ALA A CB  1 ? 3  
ATOM   122  N  N   . GLU A 1 20  ? 21.625  2.713   -60.707 1.000 21.827 ? 20  GLU A N   1 ? 3  
ATOM   123  C  CA  . GLU A 1 20  ? 21.884  1.685   -61.734 1.000 22.398 ? 20  GLU A CA  1 ? 3  
ATOM   124  C  C   . GLU A 1 20  ? 21.348  2.141   -63.086 1.000 20.984 ? 20  GLU A C   1 ? 3  
ATOM   125  O  O   . GLU A 1 20  ? 22.012  1.852   -64.119 1.000 22.486 ? 20  GLU A O   1 ? 3  
ATOM   126  C  CB  . GLU A 1 20  ? 21.333  0.289   -61.349 1.000 24.116 ? 20  GLU A CB  1 ? 3  
ATOM   127  C  CG  . GLU A 1 20  ? 21.702  -0.790  -62.399 1.000 27.908 ? 20  GLU A CG  1 ? 3  
ATOM   128  C  CD  . GLU A 1 20  ? 21.553  -2.318  -62.125 1.000 33.221 ? 20  GLU A CD  1 ? 3  
ATOM   129  O  OE1 . GLU A 1 20  ? 22.356  -3.135  -62.670 1.000 44.239 ? 20  GLU A OE1 1 ? 3  
ATOM   130  O  OE2 . GLU A 1 20  ? 20.801  -2.645  -61.352 1.000 33.949 ? 20  GLU A OE2 1 ? 3  
ATOM   131  N  N   . THR A 1 21  ? 20.135  2.704   -63.111 1.000 20.155 ? 21  THR A N   1 ? 3  
ATOM   132  C  CA  . THR A 1 21  ? 19.384  2.922   -64.367 1.000 19.056 ? 21  THR A CA  1 ? 3  
ATOM   133  C  C   . THR A 1 21  ? 19.225  4.414   -64.688 1.000 19.252 ? 21  THR A C   1 ? 3  
ATOM   134  O  O   . THR A 1 21  ? 18.843  4.694   -65.821 1.000 19.363 ? 21  THR A O   1 ? 3  
ATOM   135  C  CB  . THR A 1 21  ? 17.969  2.324   -64.332 1.000 19.162 ? 21  THR A CB  1 ? 3  
ATOM   136  O  OG1 . THR A 1 21  ? 17.180  3.069   -63.405 1.000 18.114 ? 21  THR A OG1 1 ? 3  
ATOM   137  C  CG2 . THR A 1 21  ? 18.017  0.842   -64.003 1.000 21.349 ? 21  THR A CG2 1 ? 3  
ATOM   138  N  N   . GLY A 1 22  ? 19.488  5.303   -63.727 1.000 18.797 ? 22  GLY A N   1 ? 3  
ATOM   139  C  CA  . GLY A 1 22  ? 19.171  6.714   -63.881 1.000 18.649 ? 22  GLY A CA  1 ? 3  
ATOM   140  C  C   . GLY A 1 22  ? 17.703  7.040   -63.763 1.000 18.533 ? 22  GLY A C   1 ? 3  
ATOM   141  O  O   . GLY A 1 22  ? 17.334  8.226   -63.917 1.000 18.419 ? 22  GLY A O   1 ? 3  
ATOM   142  N  N   . ALA A 1 23  ? 16.807  6.087   -63.514 1.000 17.932 ? 23  ALA A N   1 ? 3  
ATOM   143  C  CA  . ALA A 1 23  ? 15.364  6.415   -63.405 1.000 18.014 ? 23  ALA A CA  1 ? 3  
ATOM   144  C  C   . ALA A 1 23  ? 15.153  7.690   -62.567 1.000 17.844 ? 23  ALA A C   1 ? 3  
ATOM   145  O  O   . ALA A 1 23  ? 15.618  7.800   -61.416 1.000 18.801 ? 23  ALA A O   1 ? 3  
ATOM   146  C  CB  . ALA A 1 23  ? 14.608  5.274   -62.748 1.000 18.243 ? 23  ALA A CB  1 ? 3  
ATOM   147  N  N   . VAL A 1 24  ? 14.499  8.661   -63.176 1.000 17.177 ? 24  VAL A N   1 ? 3  
ATOM   148  C  CA  . VAL A 1 24  ? 14.356  9.979   -62.526 1.000 18.479 ? 24  VAL A CA  1 ? 3  
ATOM   149  C  C   . VAL A 1 24  ? 13.376  9.937   -61.378 1.000 18.901 ? 24  VAL A C   1 ? 3  
ATOM   150  O  O   . VAL A 1 24  ? 13.425  10.840  -60.517 1.000 19.007 ? 24  VAL A O   1 ? 3  
ATOM   151  C  CB  . VAL A 1 24  ? 14.100  11.129  -63.512 1.000 18.786 ? 24  VAL A CB  1 ? 3  
ATOM   152  C  CG1 . VAL A 1 24  ? 15.177  11.254  -64.537 1.000 19.174 ? 24  VAL A CG1 1 ? 3  
ATOM   153  C  CG2 . VAL A 1 24  ? 12.737  11.103  -64.138 1.000 21.868 ? 24  VAL A CG2 1 ? 3  
ATOM   154  N  N   . VAL A 1 25  ? 12.443  9.026   -61.364 1.000 17.240 ? 25  VAL A N   1 ? 3  
ATOM   155  C  CA  . VAL A 1 25  ? 11.477  8.872   -60.282 1.000 17.808 ? 25  VAL A CA  1 ? 3  
ATOM   156  C  C   . VAL A 1 25  ? 11.885  7.650   -59.494 1.000 17.599 ? 25  VAL A C   1 ? 3  
ATOM   157  O  O   . VAL A 1 25  ? 12.294  6.618   -60.078 1.000 17.652 ? 25  VAL A O   1 ? 3  
ATOM   158  C  CB  . VAL A 1 25  ? 10.043  8.738   -60.857 1.000 17.875 ? 25  VAL A CB  1 ? 3  
ATOM   159  C  CG1 . VAL A 1 25  ? 9.050   8.439   -59.786 1.000 18.622 ? 25  VAL A CG1 1 ? 3  
ATOM   160  C  CG2 . VAL A 1 25  ? 9.707   10.038  -61.600 1.000 20.739 ? 25  VAL A CG2 1 ? 3  
ATOM   161  N  N   A VAL A 1 26  ? 11.757  7.752   -58.174 0.500 17.384 ? 26  VAL A N   1 ? 3  
ATOM   162  N  N   B VAL A 1 26  ? 11.790  7.731   -58.181 0.500 18.348 ? 26  VAL A N   1 ? 3  
ATOM   163  C  CA  A VAL A 1 26  ? 12.048  6.609   -57.268 0.500 16.983 ? 26  VAL A CA  1 ? 3  
ATOM   164  C  CA  B VAL A 1 26  ? 12.168  6.568   -57.338 0.500 18.858 ? 26  VAL A CA  1 ? 3  
ATOM   165  C  C   A VAL A 1 26  ? 11.237  5.382   -57.697 0.500 16.173 ? 26  VAL A C   1 ? 3  
ATOM   166  C  C   B VAL A 1 26  ? 11.267  5.382   -57.660 0.500 16.993 ? 26  VAL A C   1 ? 3  
ATOM   167  O  O   A VAL A 1 26  ? 10.011  5.472   -57.857 0.500 16.162 ? 26  VAL A O   1 ? 3  
ATOM   168  O  O   B VAL A 1 26  ? 10.037  5.519   -57.727 0.500 16.627 ? 26  VAL A O   1 ? 3  
ATOM   169  C  CB  A VAL A 1 26  ? 11.741  6.918   -55.803 0.500 16.523 ? 26  VAL A CB  1 ? 3  
ATOM   170  C  CB  B VAL A 1 26  ? 12.090  6.908   -55.861 0.500 20.110 ? 26  VAL A CB  1 ? 3  
ATOM   171  C  CG1 A VAL A 1 26  ? 12.249  5.758   -54.945 0.500 15.178 ? 26  VAL A CG1 1 ? 3  
ATOM   172  C  CG1 B VAL A 1 26  ? 12.981  8.103   -55.528 0.500 22.565 ? 26  VAL A CG1 1 ? 3  
ATOM   173  C  CG2 A VAL A 1 26  ? 12.264  8.262   -55.276 0.500 19.054 ? 26  VAL A CG2 1 ? 3  
ATOM   174  C  CG2 B VAL A 1 26  ? 10.647  7.109   -55.454 0.500 21.961 ? 26  VAL A CG2 1 ? 3  
ATOM   175  N  N   . PRO A 1 27  ? 11.864  4.211   -57.920 1.000 15.798 ? 27  PRO A N   1 ? 3  
ATOM   176  C  CA  . PRO A 1 27  ? 11.110  3.010   -58.196 1.000 16.724 ? 27  PRO A CA  1 ? 3  
ATOM   177  C  C   . PRO A 1 27  ? 10.144  2.682   -57.027 1.000 15.916 ? 27  PRO A C   1 ? 3  
ATOM   178  O  O   . PRO A 1 27  ? 10.427  3.059   -55.861 1.000 17.077 ? 27  PRO A O   1 ? 3  
ATOM   179  C  CB  . PRO A 1 27  ? 12.178  1.930   -58.360 1.000 18.523 ? 27  PRO A CB  1 ? 3  
ATOM   180  C  CG  . PRO A 1 27  ? 13.403  2.701   -58.734 1.000 18.729 ? 27  PRO A CG  1 ? 3  
ATOM   181  C  CD  . PRO A 1 27  ? 13.328  3.970   -57.946 1.000 18.224 ? 27  PRO A CD  1 ? 3  
ATOM   182  N  N   . ILE A 1 28  ? 9.146   1.876   -57.348 1.000 16.108 ? 28  ILE A N   1 ? 3  
ATOM   183  C  CA  . ILE A 1 28  ? 8.235   1.268   -56.339 1.000 15.321 ? 28  ILE A CA  1 ? 3  
ATOM   184  C  C   . ILE A 1 28  ? 8.870   -0.066  -56.004 1.000 15.634 ? 28  ILE A C   1 ? 3  
ATOM   185  O  O   . ILE A 1 28  ? 8.827   -1.003  -56.813 1.000 15.921 ? 28  ILE A O   1 ? 3  
ATOM   186  C  CB  . ILE A 1 28  ? 6.781   1.161   -56.843 1.000 15.556 ? 28  ILE A CB  1 ? 3  
ATOM   187  C  CG1 . ILE A 1 28  ? 6.226   2.469   -57.428 1.000 17.355 ? 28  ILE A CG1 1 ? 3  
ATOM   188  C  CG2 . ILE A 1 28  ? 5.924   0.646   -55.710 1.000 17.063 ? 28  ILE A CG2 1 ? 3  
ATOM   189  C  CD1 . ILE A 1 28  ? 4.955   2.288   -58.234 1.000 18.441 ? 28  ILE A CD1 1 ? 3  
ATOM   190  N  N   . TYR A 1 29  ? 9.444   -0.156  -54.824 1.000 15.369 ? 29  TYR A N   1 ? 3  
ATOM   191  C  CA  . TYR A 1 29  ? 10.107  -1.389  -54.363 1.000 15.388 ? 29  TYR A CA  1 ? 3  
ATOM   192  C  C   . TYR A 1 29  ? 9.040   -2.247  -53.716 1.000 16.405 ? 29  TYR A C   1 ? 3  
ATOM   193  O  O   . TYR A 1 29  ? 9.002   -2.395  -52.505 1.000 16.232 ? 29  TYR A O   1 ? 3  
ATOM   194  C  CB  . TYR A 1 29  ? 11.307  -1.114  -53.465 1.000 16.366 ? 29  TYR A CB  1 ? 3  
ATOM   195  C  CG  . TYR A 1 29  ? 12.496  -0.543  -54.190 1.000 17.178 ? 29  TYR A CG  1 ? 3  
ATOM   196  C  CD1 . TYR A 1 29  ? 12.596  0.826   -54.380 1.000 18.868 ? 29  TYR A CD1 1 ? 3  
ATOM   197  C  CD2 . TYR A 1 29  ? 13.518  -1.362  -54.674 1.000 19.617 ? 29  TYR A CD2 1 ? 3  
ATOM   198  C  CE1 . TYR A 1 29  ? 13.687  1.394   -55.002 1.000 19.422 ? 29  TYR A CE1 1 ? 3  
ATOM   199  C  CE2 . TYR A 1 29  ? 14.606  -0.767  -55.319 1.000 19.628 ? 29  TYR A CE2 1 ? 3  
ATOM   200  C  CZ  . TYR A 1 29  ? 14.639  0.597   -55.544 1.000 20.306 ? 29  TYR A CZ  1 ? 3  
ATOM   201  O  OH  . TYR A 1 29  ? 15.684  1.298   -56.154 1.000 22.844 ? 29  TYR A OH  1 ? 3  
ATOM   202  N  N   . GLN A 1 30  ? 8.250   -2.901  -54.542 1.000 15.064 ? 30  GLN A N   1 ? 4  
ATOM   203  C  CA  . GLN A 1 30  ? 7.202   -3.805  -54.133 1.000 16.292 ? 30  GLN A CA  1 ? 4  
ATOM   204  C  C   . GLN A 1 30  ? 7.824   -5.175  -53.871 1.000 16.287 ? 30  GLN A C   1 ? 4  
ATOM   205  O  O   . GLN A 1 30  ? 7.816   -6.078  -54.699 1.000 16.846 ? 30  GLN A O   1 ? 4  
ATOM   206  C  CB  . GLN A 1 30  ? 6.079   -3.766  -55.196 1.000 18.189 ? 30  GLN A CB  1 ? 4  
ATOM   207  C  CG  . GLN A 1 30  ? 4.795   -4.417  -54.775 1.000 19.122 ? 30  GLN A CG  1 ? 4  
ATOM   208  C  CD  . GLN A 1 30  ? 4.084   -3.603  -53.685 1.000 19.214 ? 30  GLN A CD  1 ? 4  
ATOM   209  O  OE1 . GLN A 1 30  ? 3.863   -2.411  -53.822 1.000 20.381 ? 30  GLN A OE1 1 ? 4  
ATOM   210  N  NE2 . GLN A 1 30  ? 3.629   -4.312  -52.657 1.000 19.420 ? 30  GLN A NE2 1 ? 4  
ATOM   211  N  N   . THR A 1 31  ? 8.480   -5.265  -52.723 1.000 15.562 ? 31  THR A N   1 ? 4  
ATOM   212  C  CA  . THR A 1 31  ? 9.312   -6.402  -52.321 1.000 16.928 ? 31  THR A CA  1 ? 4  
ATOM   213  C  C   . THR A 1 31  ? 9.132   -6.567  -50.813 1.000 16.068 ? 31  THR A C   1 ? 4  
ATOM   214  O  O   . THR A 1 31  ? 8.995   -5.533  -50.106 1.000 16.770 ? 31  THR A O   1 ? 4  
ATOM   215  C  CB  . THR A 1 31  ? 10.805  -6.211  -52.677 1.000 16.925 ? 31  THR A CB  1 ? 4  
ATOM   216  O  OG1 . THR A 1 31  ? 11.457  -7.482  -52.567 1.000 17.810 ? 31  THR A OG1 1 ? 4  
ATOM   217  C  CG2 . THR A 1 31  ? 11.499  -5.165  -51.860 1.000 17.052 ? 31  THR A CG2 1 ? 4  
ATOM   218  N  N   . SER A 1 32  ? 9.196   -7.798  -50.326 1.000 15.328 ? 32  SER A N   1 ? 4  
ATOM   219  C  CA  . SER A 1 32  ? 9.232   -7.993  -48.864 1.000 15.809 ? 32  SER A CA  1 ? 4  
ATOM   220  C  C   . SER A 1 32  ? 10.665  -8.053  -48.369 1.000 16.916 ? 32  SER A C   1 ? 4  
ATOM   221  O  O   . SER A 1 32  ? 10.913  -7.698  -47.216 1.000 17.717 ? 32  SER A O   1 ? 4  
ATOM   222  C  CB  . SER A 1 32  ? 8.514   -9.234  -48.503 1.000 17.386 ? 32  SER A CB  1 ? 4  
ATOM   223  O  OG  . SER A 1 32  ? 9.140   -10.402 -48.968 1.000 17.459 ? 32  SER A OG  1 ? 4  
ATOM   224  N  N   . THR A 1 33  ? 11.587  -8.539  -49.177 1.000 16.793 ? 33  THR A N   1 ? 4  
ATOM   225  C  CA  . THR A 1 33  ? 12.927  -8.899  -48.652 1.000 16.589 ? 33  THR A CA  1 ? 4  
ATOM   226  C  C   . THR A 1 33  ? 14.014  -8.644  -49.667 1.000 17.135 ? 33  THR A C   1 ? 4  
ATOM   227  O  O   . THR A 1 33  ? 13.707  -8.209  -50.835 1.000 17.160 ? 33  THR A O   1 ? 4  
ATOM   228  C  CB  . THR A 1 33  ? 12.889  -10.345 -48.137 1.000 18.315 ? 33  THR A CB  1 ? 4  
ATOM   229  O  OG1 . THR A 1 33  ? 14.058  -10.543 -47.331 1.000 18.708 ? 33  THR A OG1 1 ? 4  
ATOM   230  C  CG2 . THR A 1 33  ? 12.764  -11.389 -49.242 1.000 18.487 ? 33  THR A CG2 1 ? 4  
ATOM   231  N  N   . TYR A 1 34  ? 15.235  -8.855  -49.241 1.000 17.161 ? 34  TYR A N   1 ? 4  
ATOM   232  C  CA  . TYR A 1 34  ? 16.472  -8.352  -49.917 1.000 16.849 ? 34  TYR A CA  1 ? 4  
ATOM   233  C  C   . TYR A 1 34  ? 17.557  -9.387  -49.766 1.000 18.113 ? 34  TYR A C   1 ? 4  
ATOM   234  O  O   . TYR A 1 34  ? 17.821  -9.863  -48.655 1.000 18.388 ? 34  TYR A O   1 ? 4  
ATOM   235  C  CB  . TYR A 1 34  ? 16.924  -7.015  -49.334 1.000 17.746 ? 34  TYR A CB  1 ? 4  
ATOM   236  C  CG  . TYR A 1 34  ? 15.816  -5.981  -49.304 1.000 16.152 ? 34  TYR A CG  1 ? 4  
ATOM   237  C  CD1 . TYR A 1 34  ? 14.853  -5.977  -48.296 1.000 17.302 ? 34  TYR A CD1 1 ? 4  
ATOM   238  C  CD2 . TYR A 1 34  ? 15.725  -5.002  -50.259 1.000 15.728 ? 34  TYR A CD2 1 ? 4  
ATOM   239  C  CE1 . TYR A 1 34  ? 13.827  -5.044  -48.282 1.000 17.253 ? 34  TYR A CE1 1 ? 4  
ATOM   240  C  CE2 . TYR A 1 34  ? 14.720  -4.073  -50.286 1.000 16.461 ? 34  TYR A CE2 1 ? 4  
ATOM   241  C  CZ  . TYR A 1 34  ? 13.736  -4.110  -49.323 1.000 16.677 ? 34  TYR A CZ  1 ? 4  
ATOM   242  O  OH  . TYR A 1 34  ? 12.661  -3.243  -49.363 1.000 17.068 ? 34  TYR A OH  1 ? 4  
ATOM   243  N  N   . ARG A 1 35  ? 18.194  -9.724  -50.867 1.000 18.100 ? 35  ARG A N   1 ? 4  
ATOM   244  C  CA  . ARG A 1 35  ? 19.314  -10.643 -50.877 1.000 18.697 ? 35  ARG A CA  1 ? 4  
ATOM   245  C  C   . ARG A 1 35  ? 20.501  -10.028 -50.139 1.000 19.900 ? 35  ARG A C   1 ? 4  
ATOM   246  O  O   . ARG A 1 35  ? 20.819  -8.879  -50.342 1.000 19.028 ? 35  ARG A O   1 ? 4  
ATOM   247  C  CB  . ARG A 1 35  ? 19.764  -10.899 -52.316 1.000 21.133 ? 35  ARG A CB  1 ? 4  
ATOM   248  C  CG  . ARG A 1 35  ? 20.983  -11.827 -52.414 1.000 23.558 ? 35  ARG A CG  1 ? 4  
ATOM   249  C  CD  . ARG A 1 35  ? 21.328  -12.048 -53.888 1.000 27.245 ? 35  ARG A CD  1 ? 4  
ATOM   250  N  NE  . ARG A 1 35  ? 22.598  -12.685 -54.020 1.000 33.339 ? 35  ARG A NE  1 ? 4  
ATOM   251  C  CZ  . ARG A 1 35  ? 23.138  -12.965 -55.203 1.000 36.523 ? 35  ARG A CZ  1 ? 4  
ATOM   252  N  NH1 . ARG A 1 35  ? 24.345  -13.503 -55.265 1.000 40.726 ? 35  ARG A NH1 1 ? 4  
ATOM   253  N  NH2 . ARG A 1 35  ? 22.403  -12.777 -56.307 1.000 36.820 ? 35  ARG A NH2 1 ? 4  
ATOM   254  N  N   . GLN A 1 36  ? 21.145  -10.799 -49.282 1.000 18.999 ? 36  GLN A N   1 ? 4  
ATOM   255  C  CA  . GLN A 1 36  ? 22.356  -10.421 -48.521 1.000 19.946 ? 36  GLN A CA  1 ? 4  
ATOM   256  C  C   . GLN A 1 36  ? 23.563  -11.141 -49.118 1.000 20.744 ? 36  GLN A C   1 ? 4  
ATOM   257  O  O   . GLN A 1 36  ? 23.457  -12.295 -49.560 1.000 21.134 ? 36  GLN A O   1 ? 4  
ATOM   258  C  CB  . GLN A 1 36  ? 22.186  -10.800 -47.046 1.000 20.099 ? 36  GLN A CB  1 ? 4  
ATOM   259  C  CG  . GLN A 1 36  ? 20.961  -10.139 -46.419 1.000 19.277 ? 36  GLN A CG  1 ? 4  
ATOM   260  C  CD  . GLN A 1 36  ? 20.840  -10.342 -44.931 1.000 19.693 ? 36  GLN A CD  1 ? 4  
ATOM   261  O  OE1 . GLN A 1 36  ? 21.856  -10.587 -44.236 1.000 22.427 ? 36  GLN A OE1 1 ? 4  
ATOM   262  N  NE2 . GLN A 1 36  ? 19.612  -10.111 -44.411 1.000 18.739 ? 36  GLN A NE2 1 ? 4  
ATOM   263  N  N   . ASP A 1 37  ? 24.706  -10.469 -49.123 1.000 21.807 ? 37  ASP A N   1 ? 4  
ATOM   264  C  CA  . ASP A 1 37  ? 25.968  -11.018 -49.644 1.000 23.365 ? 37  ASP A CA  1 ? 4  
ATOM   265  C  C   . ASP A 1 37  ? 26.736  -11.653 -48.456 1.000 23.458 ? 37  ASP A C   1 ? 4  
ATOM   266  O  O   . ASP A 1 37  ? 27.536  -10.981 -47.756 1.000 24.610 ? 37  ASP A O   1 ? 4  
ATOM   267  C  CB  . ASP A 1 37  ? 26.777  -9.948  -50.364 1.000 26.245 ? 37  ASP A CB  1 ? 4  
ATOM   268  C  CG  . ASP A 1 37  ? 25.982  -9.384  -51.543 1.000 28.784 ? 37  ASP A CG  1 ? 4  
ATOM   269  O  OD1 . ASP A 1 37  ? 25.623  -10.212 -52.390 1.000 30.730 ? 37  ASP A OD1 1 ? 4  
ATOM   270  O  OD2 . ASP A 1 37  ? 25.868  -8.172  -51.627 1.000 29.549 ? 37  ASP A OD2 1 ? 4  
ATOM   271  N  N   . GLY A 1 38  ? 26.431  -12.908 -48.210 1.000 24.189 ? 38  GLY A N   1 ? 4  
ATOM   272  C  CA  . GLY A 1 38  ? 26.817  -13.580 -46.953 1.000 24.051 ? 38  GLY A CA  1 ? 4  
ATOM   273  C  C   . GLY A 1 38  ? 25.894  -13.090 -45.829 1.000 23.426 ? 38  GLY A C   1 ? 4  
ATOM   274  O  O   . GLY A 1 38  ? 25.207  -12.056 -45.934 1.000 21.207 ? 38  GLY A O   1 ? 4  
ATOM   275  N  N   . VAL A 1 39  ? 25.850  -13.846 -44.753 1.000 23.528 ? 39  VAL A N   1 ? 4  
ATOM   276  C  CA  . VAL A 1 39  ? 24.948  -13.504 -43.630 1.000 23.689 ? 39  VAL A CA  1 ? 4  
ATOM   277  C  C   . VAL A 1 39  ? 25.346  -12.139 -43.044 1.000 23.191 ? 39  VAL A C   1 ? 4  
ATOM   278  O  O   . VAL A 1 39  ? 26.490  -12.007 -42.605 1.000 26.202 ? 39  VAL A O   1 ? 4  
ATOM   279  C  CB  . VAL A 1 39  ? 25.018  -14.638 -42.590 1.000 25.006 ? 39  VAL A CB  1 ? 4  
ATOM   280  C  CG1 . VAL A 1 39  ? 24.294  -14.229 -41.331 1.000 26.109 ? 39  VAL A CG1 1 ? 4  
ATOM   281  C  CG2 . VAL A 1 39  ? 24.428  -15.911 -43.178 1.000 24.844 ? 39  VAL A CG2 1 ? 4  
ATOM   282  N  N   . GLY A 1 40  ? 24.411  -11.197 -43.007 1.000 25.518 ? 40  GLY A N   1 ? 4  
ATOM   283  C  CA  . GLY A 1 40  ? 24.628  -9.812  -42.526 1.000 25.611 ? 40  GLY A CA  1 ? 4  
ATOM   284  C  C   . GLY A 1 40  ? 25.281  -8.916  -43.556 1.000 26.860 ? 40  GLY A C   1 ? 4  
ATOM   285  O  O   . GLY A 1 40  ? 25.526  -7.710  -43.241 1.000 28.672 ? 40  GLY A O   1 ? 4  
ATOM   286  N  N   . GLY A 1 41  ? 25.554  -9.411  -44.784 1.000 24.924 ? 41  GLY A N   1 ? 4  
ATOM   287  C  CA  . GLY A 1 41  ? 26.143  -8.576  -45.841 1.000 25.282 ? 41  GLY A CA  1 ? 4  
ATOM   288  C  C   . GLY A 1 41  ? 25.067  -7.759  -46.514 1.000 25.149 ? 41  GLY A C   1 ? 4  
ATOM   289  O  O   . GLY A 1 41  ? 24.742  -8.076  -47.695 1.000 25.191 ? 41  GLY A O   1 ? 4  
ATOM   290  N  N   . LEU A 1 42  ? 24.581  -6.677  -45.872 1.000 24.495 ? 42  LEU A N   1 ? 4  
ATOM   291  C  CA  . LEU A 1 42  ? 23.380  -6.005  -46.426 1.000 22.684 ? 42  LEU A CA  1 ? 4  
ATOM   292  C  C   . LEU A 1 42  ? 23.798  -5.244  -47.674 1.000 24.314 ? 42  LEU A C   1 ? 4  
ATOM   293  O  O   . LEU A 1 42  ? 24.929  -4.765  -47.758 1.000 28.355 ? 42  LEU A O   1 ? 4  
ATOM   294  C  CB  . LEU A 1 42  ? 22.757  -5.061  -45.423 1.000 24.321 ? 42  LEU A CB  1 ? 4  
ATOM   295  C  CG  . LEU A 1 42  ? 22.354  -5.712  -44.096 1.000 24.619 ? 42  LEU A CG  1 ? 4  
ATOM   296  C  CD1 . LEU A 1 42  ? 21.565  -4.735  -43.265 1.000 27.280 ? 42  LEU A CD1 1 ? 4  
ATOM   297  C  CD2 . LEU A 1 42  ? 21.601  -6.982  -44.309 1.000 24.217 ? 42  LEU A CD2 1 ? 4  
ATOM   298  N  N   . ARG A 1 43  ? 22.941  -5.239  -48.657 1.000 22.101 ? 43  ARG A N   1 ? 4  
ATOM   299  C  CA  . ARG A 1 43  ? 23.123  -4.356  -49.814 1.000 25.036 ? 43  ARG A CA  1 ? 4  
ATOM   300  C  C   . ARG A 1 43  ? 22.408  -3.046  -49.586 1.000 22.509 ? 43  ARG A C   1 ? 4  
ATOM   301  O  O   . ARG A 1 43  ? 21.124  -3.054  -49.439 1.000 24.147 ? 43  ARG A O   1 ? 4  
ATOM   302  C  CB  . ARG A 1 43  ? 22.468  -4.956  -51.046 1.000 26.113 ? 43  ARG A CB  1 ? 4  
ATOM   303  C  CG  . ARG A 1 43  ? 23.148  -6.171  -51.518 1.000 26.466 ? 43  ARG A CG  1 ? 4  
ATOM   304  C  CD  . ARG A 1 43  ? 22.605  -6.670  -52.813 1.000 28.649 ? 43  ARG A CD  1 ? 4  
ATOM   305  N  NE  . ARG A 1 43  ? 23.436  -7.792  -53.263 1.000 30.963 ? 43  ARG A NE  1 ? 4  
ATOM   306  C  CZ  . ARG A 1 43  ? 23.255  -8.407  -54.425 1.000 30.717 ? 43  ARG A CZ  1 ? 4  
ATOM   307  N  NH1 . ARG A 1 43  ? 22.206  -8.080  -55.193 1.000 28.469 ? 43  ARG A NH1 1 ? 4  
ATOM   308  N  NH2 . ARG A 1 43  ? 24.018  -9.443  -54.709 1.000 33.113 ? 43  ARG A NH2 1 ? 4  
ATOM   309  N  N   . GLY A 1 44  ? 23.137  -1.971  -49.594 1.000 24.829 ? 44  GLY A N   1 ? 4  
ATOM   310  C  CA  . GLY A 1 44  ? 22.573  -0.656  -49.407 1.000 26.949 ? 44  GLY A CA  1 ? 4  
ATOM   311  C  C   . GLY A 1 44  ? 21.860  -0.512  -48.093 1.000 27.028 ? 44  GLY A C   1 ? 4  
ATOM   312  O  O   . GLY A 1 44  ? 21.041  0.372   -48.010 1.000 30.282 ? 44  GLY A O   1 ? 4  
ATOM   313  N  N   . GLY A 1 45  ? 22.138  -1.385  -47.125 1.000 24.384 ? 45  GLY A N   1 ? 4  
ATOM   314  C  CA  . GLY A 1 45  ? 21.547  -1.281  -45.791 1.000 24.571 ? 45  GLY A CA  1 ? 4  
ATOM   315  C  C   . GLY A 1 45  ? 20.156  -1.900  -45.704 1.000 23.016 ? 45  GLY A C   1 ? 4  
ATOM   316  O  O   . GLY A 1 45  ? 19.560  -1.830  -44.587 1.000 25.204 ? 45  GLY A O   1 ? 4  
ATOM   317  N  N   . TYR A 1 46  ? 19.681  -2.608  -46.727 1.000 19.425 ? 46  TYR A N   1 ? 4  
ATOM   318  C  CA  . TYR A 1 46  ? 18.311  -3.162  -46.707 1.000 18.227 ? 46  TYR A CA  1 ? 4  
ATOM   319  C  C   . TYR A 1 46  ? 18.305  -4.638  -46.338 1.000 20.201 ? 46  TYR A C   1 ? 4  
ATOM   320  O  O   . TYR A 1 46  ? 19.228  -5.408  -46.674 1.000 20.355 ? 46  TYR A O   1 ? 4  
ATOM   321  C  CB  . TYR A 1 46  ? 17.622  -2.934  -48.066 1.000 17.702 ? 46  TYR A CB  1 ? 4  
ATOM   322  C  CG  . TYR A 1 46  ? 17.297  -1.474  -48.243 1.000 18.664 ? 46  TYR A CG  1 ? 4  
ATOM   323  C  CD1 . TYR A 1 46  ? 16.191  -0.937  -47.574 1.000 18.095 ? 46  TYR A CD1 1 ? 4  
ATOM   324  C  CD2 . TYR A 1 46  ? 18.111  -0.584  -48.936 1.000 19.251 ? 46  TYR A CD2 1 ? 4  
ATOM   325  C  CE1 . TYR A 1 46  ? 15.890  0.396   -47.605 1.000 18.393 ? 46  TYR A CE1 1 ? 4  
ATOM   326  C  CE2 . TYR A 1 46  ? 17.821  0.782   -48.971 1.000 20.043 ? 46  TYR A CE2 1 ? 4  
ATOM   327  C  CZ  . TYR A 1 46  ? 16.708  1.293   -48.297 1.000 19.978 ? 46  TYR A CZ  1 ? 4  
ATOM   328  O  OH  . TYR A 1 46  ? 16.460  2.650   -48.297 1.000 20.043 ? 46  TYR A OH  1 ? 4  
ATOM   329  N  N   . GLU A 1 47  ? 17.257  -5.034  -45.627 1.000 19.656 ? 47  GLU A N   1 ? 4  
ATOM   330  C  CA  . GLU A 1 47  ? 17.137  -6.419  -45.126 1.000 20.216 ? 47  GLU A CA  1 ? 4  
ATOM   331  C  C   . GLU A 1 47  ? 15.704  -6.907  -45.145 1.000 18.713 ? 47  GLU A C   1 ? 4  
ATOM   332  O  O   . GLU A 1 47  ? 15.473  -8.114  -45.429 1.000 19.882 ? 47  GLU A O   1 ? 4  
ATOM   333  C  CB  . GLU A 1 47  ? 17.786  -6.594  -43.759 1.000 23.275 ? 47  GLU A CB  1 ? 4  
ATOM   334  C  CG  . GLU A 1 47  ? 17.202  -5.833  -42.641 1.000 24.704 ? 47  GLU A CG  1 ? 4  
ATOM   335  C  CD  . GLU A 1 47  ? 17.955  -5.914  -41.316 1.000 31.145 ? 47  GLU A CD  1 ? 4  
ATOM   336  O  OE1 . GLU A 1 47  ? 18.633  -6.871  -41.069 1.000 32.899 ? 47  GLU A OE1 1 ? 4  
ATOM   337  O  OE2 . GLU A 1 47  ? 17.933  -4.954  -40.646 1.000 35.695 ? 47  GLU A OE2 1 ? 4  
ATOM   338  N  N   . TYR A 1 48  ? 14.731  -6.070  -44.813 1.000 16.724 ? 48  TYR A N   1 ? 5  
ATOM   339  C  CA  . TYR A 1 48  ? 13.329  -6.544  -44.752 1.000 16.256 ? 48  TYR A CA  1 ? 5  
ATOM   340  C  C   . TYR A 1 48  ? 12.440  -5.306  -44.802 1.000 16.941 ? 48  TYR A C   1 ? 5  
ATOM   341  O  O   . TYR A 1 48  ? 12.691  -4.337  -44.047 1.000 16.938 ? 48  TYR A O   1 ? 5  
ATOM   342  C  CB  . TYR A 1 48  ? 13.079  -7.366  -43.477 1.000 17.420 ? 48  TYR A CB  1 ? 5  
ATOM   343  C  CG  . TYR A 1 48  ? 11.713  -7.954  -43.429 1.000 17.006 ? 48  TYR A CG  1 ? 5  
ATOM   344  C  CD1 . TYR A 1 48  ? 11.352  -8.950  -44.350 1.000 18.666 ? 48  TYR A CD1 1 ? 5  
ATOM   345  C  CD2 . TYR A 1 48  ? 10.775  -7.507  -42.539 1.000 17.099 ? 48  TYR A CD2 1 ? 5  
ATOM   346  C  CE1 . TYR A 1 48  ? 10.060  -9.424  -44.399 1.000 19.160 ? 48  TYR A CE1 1 ? 5  
ATOM   347  C  CE2 . TYR A 1 48  ? 9.472   -8.027  -42.534 1.000 17.905 ? 48  TYR A CE2 1 ? 5  
ATOM   348  C  CZ  . TYR A 1 48  ? 9.126   -9.008  -43.448 1.000 18.455 ? 48  TYR A CZ  1 ? 5  
ATOM   349  O  OH  . TYR A 1 48  ? 7.826   -9.513  -43.427 1.000 19.819 ? 48  TYR A OH  1 ? 5  
ATOM   350  N  N   . SER A 1 49  ? 11.375  -5.342  -45.616 1.000 16.504 ? 49  SER A N   1 ? 5  
ATOM   351  C  CA  . SER A 1 49  ? 10.629  -4.102  -45.912 1.000 16.407 ? 49  SER A CA  1 ? 5  
ATOM   352  C  C   . SER A 1 49  ? 9.972   -3.471  -44.689 1.000 16.794 ? 49  SER A C   1 ? 5  
ATOM   353  O  O   . SER A 1 49  ? 9.913   -2.237  -44.650 1.000 16.784 ? 49  SER A O   1 ? 5  
ATOM   354  C  CB  . SER A 1 49  ? 9.647   -4.248  -47.034 1.000 16.121 ? 49  SER A CB  1 ? 5  
ATOM   355  O  OG  . SER A 1 49  ? 10.361  -4.250  -48.288 1.000 16.292 ? 49  SER A OG  1 ? 5  
ATOM   356  N  N   . ARG A 1 50  ? 9.495   -4.237  -43.725 1.000 16.584 ? 50  ARG A N   1 ? 5  
ATOM   357  C  CA  . ARG A 1 50  ? 8.948   -3.596  -42.489 1.000 16.888 ? 50  ARG A CA  1 ? 5  
ATOM   358  C  C   . ARG A 1 50  ? 10.026  -2.709  -41.851 1.000 17.437 ? 50  ARG A C   1 ? 5  
ATOM   359  O  O   . ARG A 1 50  ? 9.746   -1.588  -41.445 1.000 17.542 ? 50  ARG A O   1 ? 5  
ATOM   360  C  CB  . ARG A 1 50  ? 8.450   -4.667  -41.534 1.000 16.566 ? 50  ARG A CB  1 ? 5  
ATOM   361  C  CG  . ARG A 1 50  ? 8.003   -4.091  -40.196 1.000 16.850 ? 50  ARG A CG  1 ? 5  
ATOM   362  C  CD  . ARG A 1 50  ? 7.127   -5.072  -39.410 1.000 17.173 ? 50  ARG A CD  1 ? 5  
ATOM   363  N  NE  . ARG A 1 50  ? 7.447   -6.469  -39.472 1.000 16.990 ? 50  ARG A NE  1 ? 5  
ATOM   364  C  CZ  . ARG A 1 50  ? 8.562   -7.033  -39.021 1.000 17.576 ? 50  ARG A CZ  1 ? 5  
ATOM   365  N  NH1 . ARG A 1 50  ? 8.767   -8.320  -39.203 1.000 18.043 ? 50  ARG A NH1 1 ? 5  
ATOM   366  N  NH2 . ARG A 1 50  ? 9.484   -6.307  -38.383 1.000 18.190 ? 50  ARG A NH2 1 ? 5  
ATOM   367  N  N   . THR A 1 51  ? 11.238  -3.220  -41.774 1.000 17.449 ? 51  THR A N   1 ? 5  
ATOM   368  C  CA  . THR A 1 51  ? 12.375  -2.534  -41.136 1.000 18.642 ? 51  THR A CA  1 ? 5  
ATOM   369  C  C   . THR A 1 51  ? 12.735  -1.243  -41.915 1.000 18.408 ? 51  THR A C   1 ? 5  
ATOM   370  O  O   . THR A 1 51  ? 12.834  -0.128  -41.373 1.000 17.888 ? 51  THR A O   1 ? 5  
ATOM   371  C  CB  . THR A 1 51  ? 13.540  -3.484  -41.032 1.000 19.283 ? 51  THR A CB  1 ? 5  
ATOM   372  O  OG1 . THR A 1 51  ? 13.118  -4.726  -40.412 1.000 18.723 ? 51  THR A OG1 1 ? 5  
ATOM   373  C  CG2 . THR A 1 51  ? 14.648  -2.827  -40.223 1.000 21.120 ? 51  THR A CG2 1 ? 5  
ATOM   374  N  N   . ALA A 1 52  ? 12.893  -1.399  -43.218 1.000 17.678 ? 52  ALA A N   1 ? 5  
ATOM   375  C  CA  . ALA A 1 52  ? 13.132  -0.270  -44.141 1.000 16.882 ? 52  ALA A CA  1 ? 5  
ATOM   376  C  C   . ALA A 1 52  ? 12.893  -0.752  -45.569 1.000 16.208 ? 52  ALA A C   1 ? 5  
ATOM   377  O  O   . ALA A 1 52  ? 13.233  -1.904  -45.924 1.000 16.331 ? 52  ALA A O   1 ? 5  
ATOM   378  C  CB  . ALA A 1 52  ? 14.545  0.285   -44.024 1.000 17.078 ? 52  ALA A CB  1 ? 5  
ATOM   379  N  N   . ASN A 1 53  ? 12.328  0.141   -46.358 1.000 15.817 ? 53  ASN A N   1 ? 5  
ATOM   380  C  CA  . ASN A 1 53  ? 12.033  -0.128  -47.788 1.000 15.043 ? 53  ASN A CA  1 ? 5  
ATOM   381  C  C   . ASN A 1 53  ? 12.510  1.090   -48.571 1.000 15.322 ? 53  ASN A C   1 ? 5  
ATOM   382  O  O   . ASN A 1 53  ? 12.330  2.209   -48.093 1.000 16.246 ? 53  ASN A O   1 ? 5  
ATOM   383  C  CB  . ASN A 1 53  ? 10.556  -0.339  -47.922 1.000 15.247 ? 53  ASN A CB  1 ? 5  
ATOM   384  C  CG  . ASN A 1 53  ? 10.102  -0.370  -49.364 1.000 16.069 ? 53  ASN A CG  1 ? 5  
ATOM   385  O  OD1 . ASN A 1 53  ? 10.069  0.682   -50.030 1.000 15.695 ? 53  ASN A OD1 1 ? 5  
ATOM   386  N  ND2 . ASN A 1 53  ? 9.768   -1.570  -49.871 1.000 16.546 ? 53  ASN A ND2 1 ? 5  
ATOM   387  N  N   . PRO A 1 54  ? 13.213  0.950   -49.726 1.000 14.800 ? 54  PRO A N   1 ? 5  
ATOM   388  C  CA  . PRO A 1 54  ? 13.849  2.102   -50.348 1.000 15.675 ? 54  PRO A CA  1 ? 5  
ATOM   389  C  C   . PRO A 1 54  ? 12.823  3.153   -50.781 1.000 16.375 ? 54  PRO A C   1 ? 5  
ATOM   390  O  O   . PRO A 1 54  ? 13.166  4.350   -50.770 1.000 16.768 ? 54  PRO A O   1 ? 5  
ATOM   391  C  CB  . PRO A 1 54  ? 14.627  1.529   -51.538 1.000 16.310 ? 54  PRO A CB  1 ? 5  
ATOM   392  C  CG  . PRO A 1 54  ? 14.780  0.071   -51.197 1.000 16.530 ? 54  PRO A CG  1 ? 5  
ATOM   393  C  CD  . PRO A 1 54  ? 13.565  -0.314  -50.358 1.000 16.010 ? 54  PRO A CD  1 ? 5  
ATOM   394  N  N   . THR A 1 55  ? 11.621  2.753   -51.238 1.000 15.141 ? 55  THR A N   1 ? 5  
ATOM   395  C  CA  . THR A 1 55  ? 10.638  3.766   -51.612 1.000 14.624 ? 55  THR A CA  1 ? 5  
ATOM   396  C  C   . THR A 1 55  ? 10.208  4.536   -50.324 1.000 15.130 ? 55  THR A C   1 ? 5  
ATOM   397  O  O   . THR A 1 55  ? 10.096  5.748   -50.345 1.000 15.869 ? 55  THR A O   1 ? 5  
ATOM   398  C  CB  . THR A 1 55  ? 9.407   3.153   -52.276 1.000 14.984 ? 55  THR A CB  1 ? 5  
ATOM   399  O  OG1 . THR A 1 55  ? 9.816   2.306   -53.352 1.000 15.932 ? 55  THR A OG1 1 ? 5  
ATOM   400  C  CG2 . THR A 1 55  ? 8.395   4.181   -52.711 1.000 15.627 ? 55  THR A CG2 1 ? 5  
ATOM   401  N  N   . ARG A 1 56  ? 9.942   3.817   -49.245 1.000 14.607 ? 56  ARG A N   1 ? 5  
ATOM   402  C  CA  . ARG A 1 56  ? 9.544   4.470   -47.973 1.000 15.267 ? 56  ARG A CA  1 ? 5  
ATOM   403  C  C   . ARG A 1 56  ? 10.676  5.353   -47.462 1.000 15.700 ? 56  ARG A C   1 ? 5  
ATOM   404  O  O   . ARG A 1 56  ? 10.366  6.450   -46.961 1.000 16.809 ? 56  ARG A O   1 ? 5  
ATOM   405  C  CB  . ARG A 1 56  ? 9.088   3.433   -46.943 1.000 15.577 ? 56  ARG A CB  1 ? 5  
ATOM   406  C  CG  . ARG A 1 56  ? 8.311   4.012   -45.772 1.000 16.151 ? 56  ARG A CG  1 ? 5  
ATOM   407  C  CD  . ARG A 1 56  ? 7.920   2.996   -44.713 1.000 16.575 ? 56  ARG A CD  1 ? 5  
ATOM   408  N  NE  . ARG A 1 56  ? 9.044   2.623   -43.878 1.000 17.511 ? 56  ARG A NE  1 ? 5  
ATOM   409  C  CZ  . ARG A 1 56  ? 9.325   1.361   -43.531 1.000 17.334 ? 56  ARG A CZ  1 ? 5  
ATOM   410  N  NH1 . ARG A 1 56  ? 8.741   0.341   -44.143 1.000 17.449 ? 56  ARG A NH1 1 ? 5  
ATOM   411  N  NH2 . ARG A 1 56  ? 10.233  1.126   -42.608 1.000 17.636 ? 56  ARG A NH2 1 ? 5  
ATOM   412  N  N   . THR A 1 57  ? 11.948  4.972   -47.625 1.000 16.450 ? 57  THR A N   1 ? 5  
ATOM   413  C  CA  . THR A 1 57  ? 13.084  5.795   -47.187 1.000 16.731 ? 57  THR A CA  1 ? 5  
ATOM   414  C  C   . THR A 1 57  ? 13.066  7.132   -47.935 1.000 15.547 ? 57  THR A C   1 ? 5  
ATOM   415  O  O   . THR A 1 57  ? 13.352  8.164   -47.368 1.000 16.164 ? 57  THR A O   1 ? 5  
ATOM   416  C  CB  . THR A 1 57  ? 14.381  5.028   -47.409 1.000 18.323 ? 57  THR A CB  1 ? 5  
ATOM   417  O  OG1 . THR A 1 57  ? 14.385  3.941   -46.480 1.000 20.294 ? 57  THR A OG1 1 ? 5  
ATOM   418  C  CG2 . THR A 1 57  ? 15.585  5.897   -47.165 1.000 18.840 ? 57  THR A CG2 1 ? 5  
ATOM   419  N  N   . ALA A 1 58  ? 12.791  7.084   -49.227 1.000 16.070 ? 58  ALA A N   1 ? 5  
ATOM   420  C  CA  . ALA A 1 58  ? 12.733  8.317   -50.038 1.000 16.711 ? 58  ALA A CA  1 ? 5  
ATOM   421  C  C   . ALA A 1 58  ? 11.689  9.277   -49.454 1.000 15.951 ? 58  ALA A C   1 ? 5  
ATOM   422  O  O   . ALA A 1 58  ? 11.949  10.443  -49.311 1.000 16.497 ? 58  ALA A O   1 ? 5  
ATOM   423  C  CB  . ALA A 1 58  ? 12.456  8.020   -51.502 1.000 16.590 ? 58  ALA A CB  1 ? 5  
ATOM   424  N  N   . LEU A 1 59  ? 10.498  8.770   -49.157 1.000 16.420 ? 59  LEU A N   1 ? 5  
ATOM   425  C  CA  . LEU A 1 59  ? 9.409   9.606   -48.565 1.000 16.436 ? 59  LEU A CA  1 ? 5  
ATOM   426  C  C   . LEU A 1 59  ? 9.855   10.134  -47.208 1.000 15.780 ? 59  LEU A C   1 ? 5  
ATOM   427  O  O   . LEU A 1 59  ? 9.688   11.326  -46.957 1.000 16.253 ? 59  LEU A O   1 ? 5  
ATOM   428  C  CB  . LEU A 1 59  ? 8.162   8.763   -48.384 1.000 15.805 ? 59  LEU A CB  1 ? 5  
ATOM   429  C  CG  . LEU A 1 59  ? 7.026   9.434   -47.602 1.000 15.420 ? 59  LEU A CG  1 ? 5  
ATOM   430  C  CD1 . LEU A 1 59  ? 6.561   10.760  -48.231 1.000 16.618 ? 59  LEU A CD1 1 ? 5  
ATOM   431  C  CD2 . LEU A 1 59  ? 5.855   8.495   -47.438 1.000 16.024 ? 59  LEU A CD2 1 ? 5  
ATOM   432  N  N   . GLU A 1 60  ? 10.483  9.301   -46.409 1.000 16.502 ? 60  GLU A N   1 ? 5  
ATOM   433  C  CA  . GLU A 1 60  ? 10.910  9.660   -45.027 1.000 16.852 ? 60  GLU A CA  1 ? 5  
ATOM   434  C  C   . GLU A 1 60  ? 11.974  10.768  -45.121 1.000 16.678 ? 60  GLU A C   1 ? 5  
ATOM   435  O  O   . GLU A 1 60  ? 11.897  11.738  -44.372 1.000 17.447 ? 60  GLU A O   1 ? 5  
ATOM   436  C  CB  . GLU A 1 60  ? 11.410  8.400   -44.333 1.000 17.108 ? 60  GLU A CB  1 ? 5  
ATOM   437  C  CG  . GLU A 1 60  ? 10.281  7.503   -43.909 1.000 16.017 ? 60  GLU A CG  1 ? 5  
ATOM   438  C  CD  . GLU A 1 60  ? 10.629  6.145   -43.332 1.000 17.557 ? 60  GLU A CD  1 ? 5  
ATOM   439  O  OE1 . GLU A 1 60  ? 11.844  5.827   -43.291 1.000 20.306 ? 60  GLU A OE1 1 ? 5  
ATOM   440  O  OE2 . GLU A 1 60  ? 9.692   5.432   -42.855 1.000 16.726 ? 60  GLU A OE2 1 ? 5  
ATOM   441  N  N   . GLU A 1 61  ? 12.936  10.621  -46.020 1.000 17.624 ? 61  GLU A N   1 ? 5  
ATOM   442  C  CA  . GLU A 1 61  ? 14.007  11.633  -46.205 1.000 17.048 ? 61  GLU A CA  1 ? 5  
ATOM   443  C  C   . GLU A 1 61  ? 13.448  12.931  -46.757 1.000 16.834 ? 61  GLU A C   1 ? 5  
ATOM   444  O  O   . GLU A 1 61  ? 13.865  14.025  -46.332 1.000 16.717 ? 61  GLU A O   1 ? 5  
ATOM   445  C  CB  . GLU A 1 61  ? 15.134  11.091  -47.086 1.000 18.403 ? 61  GLU A CB  1 ? 5  
ATOM   446  C  CG  . GLU A 1 61  ? 15.949  10.003  -46.385 1.000 20.030 ? 61  GLU A CG  1 ? 5  
ATOM   447  C  CD  . GLU A 1 61  ? 17.005  9.376   -47.291 1.000 26.559 ? 61  GLU A CD  1 ? 5  
ATOM   448  O  OE1 . GLU A 1 61  ? 17.049  9.702   -48.453 1.000 29.043 ? 61  GLU A OE1 1 ? 5  
ATOM   449  O  OE2 . GLU A 1 61  ? 17.788  8.581   -46.806 1.000 32.267 ? 61  GLU A OE2 1 ? 5  
ATOM   450  N  N   . CYS A 1 62  ? 12.509  12.850  -47.669 1.000 16.223 ? 62  CYS A N   1 ? 5  
ATOM   451  C  CA  . CYS A 1 62  ? 11.875  14.066  -48.219 1.000 15.581 ? 62  CYS A CA  1 ? 5  
ATOM   452  C  C   . CYS A 1 62  ? 11.139  14.829  -47.081 1.000 16.271 ? 62  CYS A C   1 ? 5  
ATOM   453  O  O   . CYS A 1 62  ? 11.333  16.040  -46.955 1.000 17.334 ? 62  CYS A O   1 ? 5  
ATOM   454  C  CB  . CYS A 1 62  ? 10.931  13.684  -49.331 1.000 16.825 ? 62  CYS A CB  1 ? 5  
ATOM   455  S  SG  . CYS A 1 62  ? 10.124  15.097  -50.105 1.000 19.491 ? 62  CYS A SG  1 ? 5  
ATOM   456  N  N   . LEU A 1 63  ? 10.297  14.138  -46.330 1.000 16.439 ? 63  LEU A N   1 ? 5  
ATOM   457  C  CA  . LEU A 1 63  ? 9.564   14.769  -45.218 1.000 17.649 ? 63  LEU A CA  1 ? 5  
ATOM   458  C  C   . LEU A 1 63  ? 10.533  15.376  -44.207 1.000 17.467 ? 63  LEU A C   1 ? 5  
ATOM   459  O  O   . LEU A 1 63  ? 10.304  16.479  -43.747 1.000 17.534 ? 63  LEU A O   1 ? 5  
ATOM   460  C  CB  . LEU A 1 63  ? 8.672   13.765  -44.564 1.000 18.957 ? 63  LEU A CB  1 ? 5  
ATOM   461  C  CG  . LEU A 1 63  ? 7.426   13.432  -45.369 1.000 20.979 ? 63  LEU A CG  1 ? 5  
ATOM   462  C  CD1 . LEU A 1 63  ? 6.742   12.209  -44.765 1.000 22.182 ? 63  LEU A CD1 1 ? 5  
ATOM   463  C  CD2 . LEU A 1 63  ? 6.502   14.602  -45.480 1.000 24.299 ? 63  LEU A CD2 1 ? 5  
ATOM   464  N  N   . ALA A 1 64  ? 11.594  14.699  -43.855 1.000 17.244 ? 64  ALA A N   1 ? 5  
ATOM   465  C  CA  . ALA A 1 64  ? 12.609  15.264  -42.943 1.000 17.674 ? 64  ALA A CA  1 ? 5  
ATOM   466  C  C   . ALA A 1 64  ? 13.144  16.555  -43.528 1.000 18.057 ? 64  ALA A C   1 ? 5  
ATOM   467  O  O   . ALA A 1 64  ? 13.288  17.548  -42.796 1.000 18.462 ? 64  ALA A O   1 ? 5  
ATOM   468  C  CB  . ALA A 1 64  ? 13.722  14.256  -42.685 1.000 19.848 ? 64  ALA A CB  1 ? 5  
ATOM   469  N  N   . ALA A 1 65  ? 13.455  16.576  -44.831 1.000 17.286 ? 65  ALA A N   1 ? 5  
ATOM   470  C  CA  . ALA A 1 65  ? 13.983  17.817  -45.443 1.000 18.370 ? 65  ALA A CA  1 ? 5  
ATOM   471  C  C   . ALA A 1 65  ? 12.955  18.954  -45.370 1.000 18.612 ? 65  ALA A C   1 ? 5  
ATOM   472  O  O   . ALA A 1 65  ? 13.324  20.112  -45.072 1.000 19.427 ? 65  ALA A O   1 ? 5  
ATOM   473  C  CB  . ALA A 1 65  ? 14.435  17.569  -46.861 1.000 19.073 ? 65  ALA A CB  1 ? 5  
ATOM   474  N  N   . LEU A 1 66  ? 11.707  18.665  -45.619 1.000 17.517 ? 66  LEU A N   1 ? 5  
ATOM   475  C  CA  . LEU A 1 66  ? 10.686  19.727  -45.703 1.000 18.353 ? 66  LEU A CA  1 ? 5  
ATOM   476  C  C   . LEU A 1 66  ? 10.363  20.338  -44.318 1.000 17.528 ? 66  LEU A C   1 ? 5  
ATOM   477  O  O   . LEU A 1 66  ? 10.169  21.522  -44.249 1.000 19.765 ? 66  LEU A O   1 ? 5  
ATOM   478  C  CB  . LEU A 1 66  ? 9.423   19.213  -46.351 1.000 18.993 ? 66  LEU A CB  1 ? 5  
ATOM   479  C  CG  . LEU A 1 66  ? 9.597   18.764  -47.819 1.000 19.515 ? 66  LEU A CG  1 ? 5  
ATOM   480  C  CD1 . LEU A 1 66  ? 8.252   18.291  -48.329 1.000 20.616 ? 66  LEU A CD1 1 ? 5  
ATOM   481  C  CD2 . LEU A 1 66  ? 10.145  19.901  -48.680 1.000 21.001 ? 66  LEU A CD2 1 ? 5  
ATOM   482  N  N   . GLU A 1 67  ? 10.423  19.516  -43.268 1.000 17.311 ? 67  GLU A N   1 ? 5  
ATOM   483  C  CA  . GLU A 1 67  ? 10.193  19.994  -41.894 1.000 17.818 ? 67  GLU A CA  1 ? 5  
ATOM   484  C  C   . GLU A 1 67  ? 11.483  20.445  -41.228 1.000 18.812 ? 67  GLU A C   1 ? 5  
ATOM   485  O  O   . GLU A 1 67  ? 11.435  21.018  -40.130 1.000 20.146 ? 67  GLU A O   1 ? 5  
ATOM   486  C  CB  . GLU A 1 67  ? 9.531   18.916  -41.062 1.000 17.617 ? 67  GLU A CB  1 ? 5  
ATOM   487  C  CG  . GLU A 1 67  ? 8.088   18.678  -41.395 1.000 17.503 ? 67  GLU A CG  1 ? 5  
ATOM   488  C  CD  . GLU A 1 67  ? 7.053   19.716  -40.970 1.000 18.601 ? 67  GLU A CD  1 ? 5  
ATOM   489  O  OE1 . GLU A 1 67  ? 7.432   20.825  -40.543 1.000 20.493 ? 67  GLU A OE1 1 ? 5  
ATOM   490  O  OE2 . GLU A 1 67  ? 5.865   19.456  -41.187 1.000 18.662 ? 67  GLU A OE2 1 ? 5  
ATOM   491  N  N   . GLY A 1 68  ? 12.631  20.247  -41.853 1.000 18.238 ? 68  GLY A N   1 ? 5  
ATOM   492  C  CA  . GLY A 1 68  ? 13.906  20.591  -41.257 1.000 20.050 ? 68  GLY A CA  1 ? 5  
ATOM   493  C  C   . GLY A 1 68  ? 14.258  19.675  -40.107 1.000 20.575 ? 68  GLY A C   1 ? 5  
ATOM   494  O  O   . GLY A 1 68  ? 14.932  20.155  -39.156 1.000 23.179 ? 68  GLY A O   1 ? 5  
ATOM   495  N  N   . GLY A 1 69  ? 13.902  18.424  -40.163 1.000 18.791 ? 69  GLY A N   1 ? 5  
ATOM   496  C  CA  . GLY A 1 69  ? 14.237  17.472  -39.101 1.000 19.825 ? 69  GLY A CA  1 ? 5  
ATOM   497  C  C   . GLY A 1 69  ? 15.404  16.568  -39.494 1.000 20.554 ? 69  GLY A C   1 ? 5  
ATOM   498  O  O   . GLY A 1 69  ? 15.877  16.618  -40.638 1.000 21.655 ? 69  GLY A O   1 ? 5  
ATOM   499  N  N   A VAL A 1 70  ? 15.830  15.718  -38.562 0.500 20.302 ? 70  VAL A N   1 ? 5  
ATOM   500  N  N   B VAL A 1 70  ? 15.846  15.701  -38.578 0.500 20.156 ? 70  VAL A N   1 ? 5  
ATOM   501  C  CA  A VAL A 1 70  ? 16.928  14.764  -38.823 0.500 20.606 ? 70  VAL A CA  1 ? 5  
ATOM   502  C  CA  B VAL A 1 70  ? 16.944  14.751  -38.887 0.500 20.350 ? 70  VAL A CA  1 ? 5  
ATOM   503  C  C   A VAL A 1 70  ? 16.395  13.430  -39.343 0.500 21.043 ? 70  VAL A C   1 ? 5  
ATOM   504  C  C   B VAL A 1 70  ? 16.418  13.371  -39.254 0.500 20.848 ? 70  VAL A C   1 ? 5  
ATOM   505  O  O   A VAL A 1 70  ? 17.157  12.732  -40.054 0.500 22.315 ? 70  VAL A O   1 ? 5  
ATOM   506  O  O   B VAL A 1 70  ? 17.224  12.551  -39.707 0.500 21.770 ? 70  VAL A O   1 ? 5  
ATOM   507  C  CB  A VAL A 1 70  ? 17.782  14.574  -37.568 0.500 22.284 ? 70  VAL A CB  1 ? 5  
ATOM   508  C  CB  B VAL A 1 70  ? 17.921  14.639  -37.718 0.500 21.863 ? 70  VAL A CB  1 ? 5  
ATOM   509  C  CG1 A VAL A 1 70  ? 17.001  13.910  -36.443 0.500 22.423 ? 70  VAL A CG1 1 ? 5  
ATOM   510  C  CG1 B VAL A 1 70  ? 18.491  15.997  -37.367 0.500 22.373 ? 70  VAL A CG1 1 ? 5  
ATOM   511  C  CG2 A VAL A 1 70  ? 19.033  13.816  -37.883 0.500 22.495 ? 70  VAL A CG2 1 ? 5  
ATOM   512  C  CG2 B VAL A 1 70  ? 17.235  14.018  -36.514 0.500 21.898 ? 70  VAL A CG2 1 ? 5  
ATOM   513  N  N   . ARG A 1 71  ? 15.141  13.076  -39.061 1.000 18.287 ? 71  ARG A N   1 ? 5  
ATOM   514  C  CA  . ARG A 1 71  ? 14.630  11.727  -39.337 1.000 19.721 ? 71  ARG A CA  1 ? 5  
ATOM   515  C  C   . ARG A 1 71  ? 13.140  11.850  -39.614 1.000 17.903 ? 71  ARG A C   1 ? 5  
ATOM   516  O  O   . ARG A 1 71  ? 12.429  12.473  -38.802 1.000 18.279 ? 71  ARG A O   1 ? 5  
ATOM   517  C  CB  . ARG A 1 71  ? 14.892  10.750  -38.177 1.000 21.100 ? 71  ARG A CB  1 ? 5  
ATOM   518  C  CG  . ARG A 1 71  ? 14.478  9.302   -38.420 1.000 21.525 ? 71  ARG A CG  1 ? 5  
ATOM   519  C  CD  . ARG A 1 71  ? 15.421  8.633   -39.313 1.000 24.895 ? 71  ARG A CD  1 ? 5  
ATOM   520  N  NE  . ARG A 1 71  ? 15.149  7.165   -39.418 1.000 26.812 ? 71  ARG A NE  1 ? 5  
ATOM   521  C  CZ  . ARG A 1 71  ? 15.565  6.205   -38.571 1.000 24.818 ? 71  ARG A CZ  1 ? 5  
ATOM   522  N  NH1 . ARG A 1 71  ? 16.322  6.466   -37.495 1.000 26.723 ? 71  ARG A NH1 1 ? 5  
ATOM   523  N  NH2 . ARG A 1 71  ? 15.391  4.950   -38.964 1.000 24.937 ? 71  ARG A NH2 1 ? 5  
ATOM   524  N  N   . GLY A 1 72  ? 12.714  11.243  -40.670 1.000 17.458 ? 72  GLY A N   1 ? 5  
ATOM   525  C  CA  . GLY A 1 72  ? 11.289  11.009  -40.948 1.000 16.651 ? 72  GLY A CA  1 ? 5  
ATOM   526  C  C   . GLY A 1 72  ? 10.933  9.552   -40.833 1.000 16.027 ? 72  GLY A C   1 ? 5  
ATOM   527  O  O   . GLY A 1 72  ? 11.778  8.722   -41.128 1.000 17.773 ? 72  GLY A O   1 ? 5  
ATOM   528  N  N   . LEU A 1 73  ? 9.676   9.258   -40.513 1.000 15.262 ? 73  LEU A N   1 ? 5  
ATOM   529  C  CA  . LEU A 1 73  ? 9.165   7.869   -40.415 1.000 15.893 ? 73  LEU A CA  1 ? 5  
ATOM   530  C  C   . LEU A 1 73  ? 7.743   7.859   -40.967 1.000 16.502 ? 73  LEU A C   1 ? 5  
ATOM   531  O  O   . LEU A 1 73  ? 6.931   8.700   -40.581 1.000 16.231 ? 73  LEU A O   1 ? 5  
ATOM   532  C  CB  . LEU A 1 73  ? 9.176   7.448   -38.942 1.000 16.934 ? 73  LEU A CB  1 ? 5  
ATOM   533  C  CG  . LEU A 1 73  ? 10.568  7.377   -38.344 1.000 19.314 ? 73  LEU A CG  1 ? 5  
ATOM   534  C  CD1 . LEU A 1 73  ? 10.483  6.948   -36.883 1.000 23.074 ? 73  LEU A CD1 1 ? 5  
ATOM   535  C  CD2 . LEU A 1 73  ? 11.410  6.261   -39.017 1.000 23.513 ? 73  LEU A CD2 1 ? 5  
ATOM   536  N  N   . ALA A 1 74  ? 7.484   6.959   -41.890 1.000 15.622 ? 74  ALA A N   1 ? 5  
ATOM   537  C  CA  . ALA A 1 74  ? 6.178   6.854   -42.556 1.000 16.328 ? 74  ALA A CA  1 ? 5  
ATOM   538  C  C   . ALA A 1 74  ? 5.377   5.664   -42.048 1.000 16.040 ? 74  ALA A C   1 ? 5  
ATOM   539  O  O   . ALA A 1 74  ? 5.917   4.543   -41.906 1.000 16.048 ? 74  ALA A O   1 ? 5  
ATOM   540  C  CB  . ALA A 1 74  ? 6.379   6.810   -44.055 1.000 15.460 ? 74  ALA A CB  1 ? 5  
ATOM   541  N  N   . PHE A 1 75  ? 4.069   5.872   -41.894 1.000 15.584 ? 75  PHE A N   1 ? 5  
ATOM   542  C  CA  . PHE A 1 75  ? 3.166   4.928   -41.236 1.000 15.511 ? 75  PHE A CA  1 ? 5  
ATOM   543  C  C   . PHE A 1 75  ? 1.930   4.688   -42.081 1.000 15.372 ? 75  PHE A C   1 ? 5  
ATOM   544  O  O   . PHE A 1 75  ? 1.606   5.457   -43.009 1.000 15.443 ? 75  PHE A O   1 ? 5  
ATOM   545  C  CB  . PHE A 1 75  ? 2.762   5.453   -39.859 1.000 15.907 ? 75  PHE A CB  1 ? 5  
ATOM   546  C  CG  . PHE A 1 75  ? 3.910   5.550   -38.911 1.000 15.124 ? 75  PHE A CG  1 ? 5  
ATOM   547  C  CD1 . PHE A 1 75  ? 4.251   4.439   -38.167 1.000 16.647 ? 75  PHE A CD1 1 ? 5  
ATOM   548  C  CD2 . PHE A 1 75  ? 4.715   6.681   -38.850 1.000 15.551 ? 75  PHE A CD2 1 ? 5  
ATOM   549  C  CE1 . PHE A 1 75  ? 5.403   4.466   -37.392 1.000 16.946 ? 75  PHE A CE1 1 ? 5  
ATOM   550  C  CE2 . PHE A 1 75  ? 5.825   6.722   -38.047 1.000 16.603 ? 75  PHE A CE2 1 ? 5  
ATOM   551  C  CZ  . PHE A 1 75  ? 6.160   5.630   -37.279 1.000 17.400 ? 75  PHE A CZ  1 ? 5  
ATOM   552  N  N   . ALA A 1 76  ? 1.171   3.682   -41.695 1.000 15.056 ? 76  ALA A N   1 ? 5  
ATOM   553  C  CA  . ALA A 1 76  ? 0.022   3.161   -42.458 1.000 16.693 ? 76  ALA A CA  1 ? 5  
ATOM   554  C  C   . ALA A 1 76  ? -1.141  4.139   -42.498 1.000 15.751 ? 76  ALA A C   1 ? 5  
ATOM   555  O  O   . ALA A 1 76  ? -2.056  4.006   -43.326 1.000 16.191 ? 76  ALA A O   1 ? 5  
ATOM   556  C  CB  . ALA A 1 76  ? -0.474  1.882   -41.786 1.000 17.073 ? 76  ALA A CB  1 ? 5  
ATOM   557  N  N   . SER A 1 77  ? -1.164  5.095   -41.596 1.000 15.491 ? 77  SER A N   1 ? 5  
ATOM   558  C  CA  . SER A 1 77  ? -2.187  6.132   -41.504 1.000 15.441 ? 77  SER A CA  1 ? 5  
ATOM   559  C  C   . SER A 1 77  ? -1.668  7.216   -40.534 1.000 16.246 ? 77  SER A C   1 ? 5  
ATOM   560  O  O   . SER A 1 77  ? -0.720  6.961   -39.787 1.000 15.214 ? 77  SER A O   1 ? 5  
ATOM   561  C  CB  . SER A 1 77  ? -3.497  5.596   -40.992 1.000 15.907 ? 77  SER A CB  1 ? 5  
ATOM   562  O  OG  . SER A 1 77  ? -3.377  5.088   -39.646 1.000 16.014 ? 77  SER A OG  1 ? 5  
ATOM   563  N  N   . GLY A 1 78  ? -2.298  8.381   -40.509 1.000 15.134 ? 78  GLY A N   1 ? 5  
ATOM   564  C  CA  . GLY A 1 78  ? -2.073  9.392   -39.484 1.000 15.619 ? 78  GLY A CA  1 ? 5  
ATOM   565  C  C   . GLY A 1 78  ? -2.239  8.775   -38.090 1.000 15.422 ? 78  GLY A C   1 ? 5  
ATOM   566  O  O   . GLY A 1 78  ? -1.404  9.015   -37.200 1.000 16.347 ? 78  GLY A O   1 ? 5  
ATOM   567  N  N   . MET A 1 79  ? -3.331  8.045   -37.905 1.000 15.892 ? 79  MET A N   1 ? 5  
ATOM   568  C  CA  . MET A 1 79  ? -3.596  7.456   -36.581 1.000 15.985 ? 79  MET A CA  1 ? 5  
ATOM   569  C  C   . MET A 1 79  ? -2.485  6.486   -36.204 1.000 16.385 ? 79  MET A C   1 ? 5  
ATOM   570  O  O   . MET A 1 79  ? -2.073  6.455   -34.999 1.000 16.849 ? 79  MET A O   1 ? 5  
ATOM   571  C  CB  . MET A 1 79  ? -4.934  6.768   -36.490 1.000 17.011 ? 79  MET A CB  1 ? 5  
ATOM   572  C  CG  . MET A 1 79  ? -6.100  7.733   -36.535 1.000 17.477 ? 79  MET A CG  1 ? 5  
ATOM   573  S  SD  . MET A 1 79  ? -6.009  9.145   -35.399 1.000 18.445 ? 79  MET A SD  1 ? 5  
ATOM   574  C  CE  . MET A 1 79  ? -5.471  8.350   -33.877 1.000 19.279 ? 79  MET A CE  1 ? 5  
ATOM   575  N  N   . ALA A 1 80  ? -1.914  5.744   -37.140 1.000 16.606 ? 80  ALA A N   1 ? 5  
ATOM   576  C  CA  . ALA A 1 80  ? -0.829  4.822   -36.795 1.000 15.417 ? 80  ALA A CA  1 ? 5  
ATOM   577  C  C   . ALA A 1 80  ? 0.462   5.564   -36.437 1.000 15.647 ? 80  ALA A C   1 ? 5  
ATOM   578  O  O   . ALA A 1 80  ? 1.204   5.149   -35.513 1.000 16.779 ? 80  ALA A O   1 ? 5  
ATOM   579  C  CB  . ALA A 1 80  ? -0.554  3.863   -37.937 1.000 15.950 ? 80  ALA A CB  1 ? 5  
ATOM   580  N  N   . ALA A 1 81  ? 0.712   6.691   -37.038 1.000 15.937 ? 81  ALA A N   1 ? 5  
ATOM   581  C  CA  . ALA A 1 81  ? 1.830   7.570   -36.636 1.000 16.364 ? 81  ALA A CA  1 ? 5  
ATOM   582  C  C   . ALA A 1 81  ? 1.597   8.024   -35.189 1.000 16.812 ? 81  ALA A C   1 ? 5  
ATOM   583  O  O   . ALA A 1 81  ? 2.505   8.012   -34.402 1.000 16.620 ? 81  ALA A O   1 ? 5  
ATOM   584  C  CB  . ALA A 1 81  ? 1.927   8.773   -37.576 1.000 16.679 ? 81  ALA A CB  1 ? 5  
ATOM   585  N  N   . GLU A 1 82  ? 0.399   8.484   -34.866 1.000 15.992 ? 82  GLU A N   1 ? 5  
ATOM   586  C  CA  . GLU A 1 82  ? 0.063   8.906   -33.505 1.000 17.026 ? 82  GLU A CA  1 ? 5  
ATOM   587  C  C   . GLU A 1 82  ? 0.282   7.750   -32.551 1.000 16.987 ? 82  GLU A C   1 ? 5  
ATOM   588  O  O   . GLU A 1 82  ? 0.874   7.934   -31.464 1.000 17.663 ? 82  GLU A O   1 ? 5  
ATOM   589  C  CB  . GLU A 1 82  ? -1.373  9.379   -33.377 1.000 17.229 ? 82  GLU A CB  1 ? 5  
ATOM   590  C  CG  . GLU A 1 82  ? -1.774  10.591  -34.199 1.000 18.943 ? 82  GLU A CG  1 ? 5  
ATOM   591  C  CD  . GLU A 1 82  ? -3.126  11.175  -33.788 1.000 20.976 ? 82  GLU A CD  1 ? 5  
ATOM   592  O  OE1 . GLU A 1 82  ? -3.711  10.752  -32.784 1.000 22.013 ? 82  GLU A OE1 1 ? 5  
ATOM   593  O  OE2 . GLU A 1 82  ? -3.548  12.064  -34.514 1.000 23.076 ? 82  GLU A OE2 1 ? 5  
ATOM   594  N  N   . ASP A 1 83  ? -0.221  6.555   -32.862 1.000 16.492 ? 83  ASP A N   1 ? 5  
ATOM   595  C  CA  . ASP A 1 83  ? -0.143  5.387   -31.974 1.000 17.259 ? 83  ASP A CA  1 ? 5  
ATOM   596  C  C   . ASP A 1 83  ? 1.293   5.002   -31.747 1.000 17.489 ? 83  ASP A C   1 ? 5  
ATOM   597  O  O   . ASP A 1 83  ? 1.686   4.769   -30.569 1.000 17.277 ? 83  ASP A O   1 ? 5  
ATOM   598  C  CB  . ASP A 1 83  ? -0.971  4.252   -32.554 1.000 17.091 ? 83  ASP A CB  1 ? 5  
ATOM   599  C  CG  . ASP A 1 83  ? -1.023  3.066   -31.639 1.000 19.357 ? 83  ASP A CG  1 ? 5  
ATOM   600  O  OD1 . ASP A 1 83  ? -1.432  3.242   -30.510 1.000 22.468 ? 83  ASP A OD1 1 ? 5  
ATOM   601  O  OD2 . ASP A 1 83  ? -0.608  1.982   -32.049 1.000 21.788 ? 83  ASP A OD2 1 ? 5  
ATOM   602  N  N   . THR A 1 84  ? 2.122   4.954   -32.772 1.000 16.815 ? 84  THR A N   1 ? 5  
ATOM   603  C  CA  . THR A 1 84  ? 3.518   4.581   -32.600 1.000 17.539 ? 84  THR A CA  1 ? 5  
ATOM   604  C  C   . THR A 1 84  ? 4.220   5.637   -31.753 1.000 17.389 ? 84  THR A C   1 ? 5  
ATOM   605  O  O   . THR A 1 84  ? 5.010   5.279   -30.890 1.000 17.715 ? 84  THR A O   1 ? 5  
ATOM   606  C  CB  . THR A 1 84  ? 4.200   4.376   -33.964 1.000 18.642 ? 84  THR A CB  1 ? 5  
ATOM   607  O  OG1 . THR A 1 84  ? 3.566   3.253   -34.582 1.000 21.860 ? 84  THR A OG1 1 ? 5  
ATOM   608  C  CG2 . THR A 1 84  ? 5.636   4.081   -33.843 1.000 19.512 ? 84  THR A CG2 1 ? 5  
ATOM   609  N  N   . LEU A 1 85  ? 3.949   6.894   -32.021 1.000 17.592 ? 85  LEU A N   1 ? 5  
ATOM   610  C  CA  . LEU A 1 85  ? 4.543   7.989   -31.208 1.000 17.061 ? 85  LEU A CA  1 ? 5  
ATOM   611  C  C   . LEU A 1 85  ? 4.245   7.795   -29.731 1.000 17.292 ? 85  LEU A C   1 ? 5  
ATOM   612  O  O   . LEU A 1 85  ? 5.125   7.816   -28.893 1.000 18.464 ? 85  LEU A O   1 ? 5  
ATOM   613  C  CB  . LEU A 1 85  ? 4.046   9.346   -31.691 1.000 16.289 ? 85  LEU A CB  1 ? 5  
ATOM   614  C  CG  . LEU A 1 85  ? 4.481   10.568  -30.892 1.000 17.969 ? 85  LEU A CG  1 ? 5  
ATOM   615  C  CD1 . LEU A 1 85  ? 5.989   10.689  -30.761 1.000 18.317 ? 85  LEU A CD1 1 ? 5  
ATOM   616  C  CD2 . LEU A 1 85  ? 3.933   11.810  -31.533 1.000 19.078 ? 85  LEU A CD2 1 ? 5  
ATOM   617  N  N   . LEU A 1 86  ? 2.967   7.657   -29.398 1.000 16.417 ? 86  LEU A N   1 ? 5  
ATOM   618  C  CA  . LEU A 1 86  ? 2.532   7.571   -27.987 1.000 17.231 ? 86  LEU A CA  1 ? 5  
ATOM   619  C  C   . LEU A 1 86  ? 3.016   6.283   -27.336 1.000 17.711 ? 86  LEU A C   1 ? 5  
ATOM   620  O  O   . LEU A 1 86  ? 3.374   6.302   -26.152 1.000 18.269 ? 86  LEU A O   1 ? 5  
ATOM   621  C  CB  . LEU A 1 86  ? 1.011   7.746   -27.895 1.000 17.889 ? 86  LEU A CB  1 ? 5  
ATOM   622  C  CG  . LEU A 1 86  ? 0.461   9.131   -28.246 1.000 19.942 ? 86  LEU A CG  1 ? 5  
ATOM   623  C  CD1 . LEU A 1 86  ? -1.071  9.125   -28.190 1.000 21.029 ? 86  LEU A CD1 1 ? 5  
ATOM   624  C  CD2 . LEU A 1 86  ? 1.055   10.230  -27.400 1.000 21.431 ? 86  LEU A CD2 1 ? 5  
ATOM   625  N  N   A ARG A 1 87  ? 3.075   5.167   -28.082 0.500 17.460 ? 87  ARG A N   1 ? 5  
ATOM   626  N  N   B ARG A 1 87  ? 3.082   5.194   -28.089 0.500 17.605 ? 87  ARG A N   1 ? 5  
ATOM   627  C  CA  A ARG A 1 87  ? 3.579   3.894   -27.503 0.500 18.200 ? 87  ARG A CA  1 ? 5  
ATOM   628  C  CA  B ARG A 1 87  ? 3.568   3.915   -27.542 0.500 18.430 ? 87  ARG A CA  1 ? 5  
ATOM   629  C  C   A ARG A 1 87  ? 5.050   4.085   -27.155 0.500 18.782 ? 87  ARG A C   1 ? 5  
ATOM   630  C  C   B ARG A 1 87  ? 5.048   4.060   -27.189 0.500 18.910 ? 87  ARG A C   1 ? 5  
ATOM   631  O  O   A ARG A 1 87  ? 5.503   3.482   -26.202 0.500 19.790 ? 87  ARG A O   1 ? 5  
ATOM   632  O  O   B ARG A 1 87  ? 5.513   3.377   -26.293 0.500 19.737 ? 87  ARG A O   1 ? 5  
ATOM   633  C  CB  A ARG A 1 87  ? 3.425   2.700   -28.445 0.500 18.848 ? 87  ARG A CB  1 ? 5  
ATOM   634  C  CB  B ARG A 1 87  ? 3.342   2.848   -28.595 0.500 19.587 ? 87  ARG A CB  1 ? 5  
ATOM   635  C  CG  A ARG A 1 87  ? 3.349   1.386   -27.722 0.500 21.743 ? 87  ARG A CG  1 ? 5  
ATOM   636  C  CG  B ARG A 1 87  ? 2.986   1.512   -28.050 0.500 22.027 ? 87  ARG A CG  1 ? 5  
ATOM   637  C  CD  A ARG A 1 87  ? 1.906   1.179   -27.219 0.500 22.519 ? 87  ARG A CD  1 ? 5  
ATOM   638  C  CD  B ARG A 1 87  ? 1.689   1.379   -27.221 0.500 22.545 ? 87  ARG A CD  1 ? 5  
ATOM   639  N  NE  A ARG A 1 87  ? 1.054   0.977   -28.376 0.500 21.283 ? 87  ARG A NE  1 ? 5  
ATOM   640  N  NE  B ARG A 1 87  ? 1.895   -0.003  -26.867 0.500 21.438 ? 87  ARG A NE  1 ? 5  
ATOM   641  C  CZ  A ARG A 1 87  ? 1.026   -0.171  -29.096 0.500 20.066 ? 87  ARG A CZ  1 ? 5  
ATOM   642  C  CZ  B ARG A 1 87  ? 1.350   -0.719  -25.874 0.500 20.996 ? 87  ARG A CZ  1 ? 5  
ATOM   643  N  NH1 A ARG A 1 87  ? 0.204   -0.173  -30.140 0.500 19.608 ? 87  ARG A NH1 1 ? 5  
ATOM   644  N  NH1 B ARG A 1 87  ? 1.748   -1.959  -25.761 0.500 17.526 ? 87  ARG A NH1 1 ? 5  
ATOM   645  N  NH2 A ARG A 1 87  ? 1.847   -1.255  -28.825 0.500 18.690 ? 87  ARG A NH2 1 ? 5  
ATOM   646  N  NH2 B ARG A 1 87  ? 0.438   -0.237  -25.042 0.500 21.939 ? 87  ARG A NH2 1 ? 5  
ATOM   647  N  N   . THR A 1 88  ? 5.769   4.893   -27.944 1.000 18.372 ? 88  THR A N   1 ? 5  
ATOM   648  C  CA  . THR A 1 88  ? 7.221   5.112   -27.769 1.000 18.454 ? 88  THR A CA  1 ? 5  
ATOM   649  C  C   . THR A 1 88  ? 7.453   6.019   -26.556 1.000 19.517 ? 88  THR A C   1 ? 5  
ATOM   650  O  O   . THR A 1 88  ? 8.357   5.721   -25.713 1.000 20.440 ? 88  THR A O   1 ? 5  
ATOM   651  C  CB  . THR A 1 88  ? 7.839   5.719   -29.022 1.000 18.081 ? 88  THR A CB  1 ? 5  
ATOM   652  O  OG1 . THR A 1 88  ? 7.669   4.842   -30.124 1.000 17.935 ? 88  THR A OG1 1 ? 5  
ATOM   653  C  CG2 . THR A 1 88  ? 9.299   6.007   -28.847 1.000 17.593 ? 88  THR A CG2 1 ? 5  
ATOM   654  N  N   . ILE A 1 89  ? 6.760   7.159   -26.462 1.000 19.235 ? 89  ILE A N   1 ? 5  
ATOM   655  C  CA  . ILE A 1 89  ? 7.162   8.227   -25.502 1.000 19.928 ? 89  ILE A CA  1 ? 5  
ATOM   656  C  C   . ILE A 1 89  ? 6.403   8.093   -24.178 1.000 21.752 ? 89  ILE A C   1 ? 5  
ATOM   657  O  O   . ILE A 1 89  ? 6.800   8.766   -23.247 1.000 24.016 ? 89  ILE A O   1 ? 5  
ATOM   658  C  CB  . ILE A 1 89  ? 6.985   9.633   -26.117 1.000 20.363 ? 89  ILE A CB  1 ? 5  
ATOM   659  C  CG1 . ILE A 1 89  ? 5.517   10.011  -26.311 1.000 20.636 ? 89  ILE A CG1 1 ? 5  
ATOM   660  C  CG2 . ILE A 1 89  ? 7.819   9.762   -27.376 1.000 20.260 ? 89  ILE A CG2 1 ? 5  
ATOM   661  C  CD1 . ILE A 1 89  ? 5.293   11.468  -26.641 1.000 22.992 ? 89  ILE A CD1 1 ? 5  
ATOM   662  N  N   . ALA A 1 90  ? 5.337   7.296   -24.087 1.000 20.203 ? 90  ALA A N   1 ? 5  
ATOM   663  C  CA  . ALA A 1 90  ? 4.508   7.164   -22.876 1.000 19.997 ? 90  ALA A CA  1 ? 5  
ATOM   664  C  C   . ALA A 1 90  ? 4.612   5.749   -22.356 1.000 21.580 ? 90  ALA A C   1 ? 5  
ATOM   665  O  O   . ALA A 1 90  ? 5.157   4.847   -23.022 1.000 21.570 ? 90  ALA A O   1 ? 5  
ATOM   666  C  CB  . ALA A 1 90  ? 3.058   7.573   -23.114 1.000 19.557 ? 90  ALA A CB  1 ? 5  
ATOM   667  N  N   A ARG A 1 91  ? 4.153   5.566   -21.133 0.500 21.303 ? 91  ARG A N   1 ? 5  
ATOM   668  N  N   B ARG A 1 91  ? 4.133   5.562   -21.141 0.500 21.456 ? 91  ARG A N   1 ? 5  
ATOM   669  C  CA  A ARG A 1 91  ? 4.022   4.247   -20.493 0.500 23.420 ? 91  ARG A CA  1 ? 5  
ATOM   670  C  CA  B ARG A 1 91  ? 4.041   4.259   -20.457 0.500 23.784 ? 91  ARG A CA  1 ? 5  
ATOM   671  C  C   A ARG A 1 91  ? 2.919   4.448   -19.452 0.500 22.450 ? 91  ARG A C   1 ? 5  
ATOM   672  C  C   B ARG A 1 91  ? 2.863   4.442   -19.498 0.500 22.332 ? 91  ARG A C   1 ? 5  
ATOM   673  O  O   A ARG A 1 91  ? 2.512   5.625   -19.269 0.500 24.442 ? 91  ARG A O   1 ? 5  
ATOM   674  O  O   B ARG A 1 91  ? 2.349   5.608   -19.356 0.500 23.983 ? 91  ARG A O   1 ? 5  
ATOM   675  C  CB  A ARG A 1 91  ? 5.402   3.814   -19.976 0.500 25.722 ? 91  ARG A CB  1 ? 5  
ATOM   676  C  CB  B ARG A 1 91  ? 5.378   3.959   -19.764 0.500 26.259 ? 91  ARG A CB  1 ? 5  
ATOM   677  C  CG  A ARG A 1 91  ? 5.903   4.586   -18.792 0.500 29.102 ? 91  ARG A CG  1 ? 5  
ATOM   678  C  CG  B ARG A 1 91  ? 5.707   4.953   -18.687 0.500 31.369 ? 91  ARG A CG  1 ? 5  
ATOM   679  C  CD  A ARG A 1 91  ? 7.304   4.125   -18.315 0.500 31.637 ? 91  ARG A CD  1 ? 5  
ATOM   680  C  CD  B ARG A 1 91  ? 7.206   5.072   -18.450 0.500 36.311 ? 91  ARG A CD  1 ? 5  
ATOM   681  N  NE  A ARG A 1 91  ? 7.245   2.766   -17.875 0.500 32.910 ? 91  ARG A NE  1 ? 5  
ATOM   682  N  NE  B ARG A 1 91  ? 7.375   5.594   -17.109 0.500 37.796 ? 91  ARG A NE  1 ? 5  
ATOM   683  C  CZ  A ARG A 1 91  ? 8.068   1.808   -18.250 0.500 30.469 ? 91  ARG A CZ  1 ? 5  
ATOM   684  C  CZ  B ARG A 1 91  ? 7.248   4.872   -16.032 0.500 35.329 ? 91  ARG A CZ  1 ? 5  
ATOM   685  N  NH1 A ARG A 1 91  ? 9.081   2.053   -19.092 0.500 32.717 ? 91  ARG A NH1 1 ? 5  
ATOM   686  N  NH1 B ARG A 1 91  ? 7.046   3.556   -16.131 0.500 37.596 ? 91  ARG A NH1 1 ? 5  
ATOM   687  N  NH2 A ARG A 1 91  ? 7.811   0.611   -17.831 0.500 28.259 ? 91  ARG A NH2 1 ? 5  
ATOM   688  N  NH2 B ARG A 1 91  ? 7.410   5.459   -14.886 0.500 34.408 ? 91  ARG A NH2 1 ? 5  
ATOM   689  N  N   . PRO A 1 92  ? 2.439   3.332   -18.793 1.000 23.216 ? 92  PRO A N   1 ? 5  
ATOM   690  C  CA  . PRO A 1 92  ? 1.455   3.459   -17.713 1.000 21.539 ? 92  PRO A CA  1 ? 5  
ATOM   691  C  C   . PRO A 1 92  ? 1.967   4.437   -16.642 1.000 23.408 ? 92  PRO A C   1 ? 5  
ATOM   692  O  O   . PRO A 1 92  ? 3.090   4.340   -16.199 1.000 24.888 ? 92  PRO A O   1 ? 5  
ATOM   693  C  CB  . PRO A 1 92  ? 1.232   2.036   -17.240 1.000 22.101 ? 92  PRO A CB  1 ? 5  
ATOM   694  C  CG  . PRO A 1 92  ? 1.629   1.178   -18.452 1.000 22.943 ? 92  PRO A CG  1 ? 5  
ATOM   695  C  CD  . PRO A 1 92  ? 2.796   1.929   -19.082 1.000 22.664 ? 92  PRO A CD  1 ? 5  
ATOM   696  N  N   . GLY A 1 93  ? 1.085   5.297   -16.184 1.000 23.340 ? 93  GLY A N   1 ? 5  
ATOM   697  C  CA  . GLY A 1 93  ? 1.370   6.272   -15.132 1.000 23.991 ? 93  GLY A CA  1 ? 5  
ATOM   698  C  C   . GLY A 1 93  ? 1.668   7.653   -15.671 1.000 23.927 ? 93  GLY A C   1 ? 5  
ATOM   699  O  O   . GLY A 1 93  ? 1.708   8.602   -14.853 1.000 24.250 ? 93  GLY A O   1 ? 5  
ATOM   700  N  N   . ASP A 1 94  ? 1.907   7.774   -16.965 1.000 22.024 ? 94  ASP A N   1 ? 5  
ATOM   701  C  CA  . ASP A 1 94  ? 2.271   9.058   -17.591 1.000 21.484 ? 94  ASP A CA  1 ? 5  
ATOM   702  C  C   . ASP A 1 94  ? 1.004   9.858   -17.835 1.000 22.449 ? 94  ASP A C   1 ? 5  
ATOM   703  O  O   . ASP A 1 94  ? -0.112  9.306   -17.758 1.000 24.913 ? 94  ASP A O   1 ? 5  
ATOM   704  C  CB  . ASP A 1 94  ? 3.054   8.870   -18.892 1.000 20.779 ? 94  ASP A CB  1 ? 5  
ATOM   705  C  CG  . ASP A 1 94  ? 4.437   8.326   -18.682 1.000 23.188 ? 94  ASP A CG  1 ? 5  
ATOM   706  O  OD1 . ASP A 1 94  ? 4.930   8.380   -17.529 1.000 23.816 ? 94  ASP A OD1 1 ? 5  
ATOM   707  O  OD2 . ASP A 1 94  ? 5.030   7.933   -19.709 1.000 24.584 ? 94  ASP A OD2 1 ? 5  
ATOM   708  N  N   . HIS A 1 95  ? 1.170   11.129  -18.122 1.000 22.550 ? 95  HIS A N   1 ? 5  
ATOM   709  C  CA  . HIS A 1 95  ? 0.068   12.087  -18.385 1.000 22.365 ? 95  HIS A CA  1 ? 5  
ATOM   710  C  C   . HIS A 1 95  ? 0.343   12.800  -19.686 1.000 21.293 ? 95  HIS A C   1 ? 5  
ATOM   711  O  O   . HIS A 1 95  ? 1.529   13.110  -20.002 1.000 21.412 ? 95  HIS A O   1 ? 5  
ATOM   712  C  CB  . HIS A 1 95  ? -0.045  13.058  -17.217 1.000 23.134 ? 95  HIS A CB  1 ? 5  
ATOM   713  C  CG  . HIS A 1 95  ? -1.010  14.163  -17.408 1.000 22.346 ? 95  HIS A CG  1 ? 5  
ATOM   714  N  ND1 . HIS A 1 95  ? -0.594  15.462  -17.736 1.000 24.066 ? 95  HIS A ND1 1 ? 5  
ATOM   715  C  CD2 . HIS A 1 95  ? -2.352  14.205  -17.291 1.000 23.270 ? 95  HIS A CD2 1 ? 5  
ATOM   716  C  CE1 . HIS A 1 95  ? -1.655  16.232  -17.816 1.000 23.327 ? 95  HIS A CE1 1 ? 5  
ATOM   717  N  NE2 . HIS A 1 95  ? -2.746  15.511  -17.518 1.000 23.106 ? 95  HIS A NE2 1 ? 5  
ATOM   718  N  N   . LEU A 1 96  ? -0.699  13.099  -20.422 1.000 21.326 ? 96  LEU A N   1 ? 5  
ATOM   719  C  CA  . LEU A 1 96  ? -0.659  13.865  -21.693 1.000 21.596 ? 96  LEU A CA  1 ? 5  
ATOM   720  C  C   . LEU A 1 96  ? -1.565  15.080  -21.585 1.000 22.666 ? 96  LEU A C   1 ? 5  
ATOM   721  O  O   . LEU A 1 96  ? -2.694  14.940  -21.095 1.000 22.753 ? 96  LEU A O   1 ? 5  
ATOM   722  C  CB  . LEU A 1 96  ? -1.186  12.983  -22.821 1.000 23.293 ? 96  LEU A CB  1 ? 5  
ATOM   723  C  CG  . LEU A 1 96  ? -0.419  11.761  -23.173 1.000 25.844 ? 96  LEU A CG  1 ? 5  
ATOM   724  C  CD1 . LEU A 1 96  ? -1.207  10.986  -24.264 1.000 26.370 ? 96  LEU A CD1 1 ? 5  
ATOM   725  C  CD2 . LEU A 1 96  ? 0.937   12.212  -23.728 1.000 28.504 ? 96  LEU A CD2 1 ? 5  
ATOM   726  N  N   . ILE A 1 97  ? -1.126  16.227  -22.073 1.000 21.898 ? 97  ILE A N   1 ? 5  
ATOM   727  C  CA  . ILE A 1 97  ? -2.016  17.373  -22.340 1.000 21.079 ? 97  ILE A CA  1 ? 5  
ATOM   728  C  C   . ILE A 1 97  ? -2.393  17.323  -23.810 1.000 20.748 ? 97  ILE A C   1 ? 5  
ATOM   729  O  O   . ILE A 1 97  ? -1.485  17.158  -24.685 1.000 21.527 ? 97  ILE A O   1 ? 5  
ATOM   730  C  CB  . ILE A 1 97  ? -1.296  18.654  -21.988 1.000 21.713 ? 97  ILE A CB  1 ? 5  
ATOM   731  C  CG1 . ILE A 1 97  ? -1.042  18.713  -20.483 1.000 23.196 ? 97  ILE A CG1 1 ? 5  
ATOM   732  C  CG2 . ILE A 1 97  ? -2.037  19.849  -22.529 1.000 22.755 ? 97  ILE A CG2 1 ? 5  
ATOM   733  C  CD1 . ILE A 1 97  ? -0.092  19.812  -20.037 1.000 23.271 ? 97  ILE A CD1 1 ? 5  
ATOM   734  N  N   . ILE A 1 98  ? -3.684  17.342  -24.101 1.000 20.077 ? 98  ILE A N   1 ? 5  
ATOM   735  C  CA  . ILE A 1 98  ? -4.189  17.364  -25.488 1.000 19.937 ? 98  ILE A CA  1 ? 5  
ATOM   736  C  C   . ILE A 1 98  ? -5.010  18.636  -25.676 1.000 19.647 ? 98  ILE A C   1 ? 5  
ATOM   737  O  O   . ILE A 1 98  ? -5.327  19.343  -24.732 1.000 20.117 ? 98  ILE A O   1 ? 5  
ATOM   738  C  CB  . ILE A 1 98  ? -5.004  16.100  -25.801 1.000 20.939 ? 98  ILE A CB  1 ? 5  
ATOM   739  C  CG1 . ILE A 1 98  ? -6.346  16.059  -25.051 1.000 23.849 ? 98  ILE A CG1 1 ? 5  
ATOM   740  C  CG2 . ILE A 1 98  ? -4.103  14.904  -25.506 1.000 23.063 ? 98  ILE A CG2 1 ? 5  
ATOM   741  C  CD1 . ILE A 1 98  ? -7.236  14.917  -25.478 1.000 25.120 ? 98  ILE A CD1 1 ? 5  
ATOM   742  N  N   . PRO A 1 99  ? -5.287  18.997  -26.943 1.000 19.264 ? 99  PRO A N   1 ? 5  
ATOM   743  C  CA  . PRO A 1 99  ? -6.089  20.181  -27.196 1.000 19.962 ? 99  PRO A CA  1 ? 5  
ATOM   744  C  C   . PRO A 1 99  ? -7.557  20.003  -26.809 1.000 20.727 ? 99  PRO A C   1 ? 5  
ATOM   745  O  O   . PRO A 1 99  ? -8.015  18.907  -26.733 1.000 22.030 ? 99  PRO A O   1 ? 5  
ATOM   746  C  CB  . PRO A 1 99  ? -6.012  20.411  -28.715 1.000 20.109 ? 99  PRO A CB  1 ? 5  
ATOM   747  C  CG  . PRO A 1 99  ? -4.913  19.449  -29.223 1.000 19.693 ? 99  PRO A CG  1 ? 5  
ATOM   748  C  CD  . PRO A 1 99  ? -4.931  18.311  -28.214 1.000 19.640 ? 99  PRO A CD  1 ? 5  
ATOM   749  N  N   . ASN A 1 100 ? -8.212  21.137  -26.565 1.000 21.458 ? 100 ASN A N   1 ? 5  
ATOM   750  C  CA  . ASN A 1 100 ? -9.670  21.146  -26.301 1.000 21.539 ? 100 ASN A CA  1 ? 5  
ATOM   751  C  C   . ASN A 1 100 ? -10.462 21.232  -27.606 1.000 20.210 ? 100 ASN A C   1 ? 5  
ATOM   752  O  O   . ASN A 1 100 ? -11.682 21.302  -27.514 1.000 22.021 ? 100 ASN A O   1 ? 5  
ATOM   753  C  CB  . ASN A 1 100 ? -10.077 22.274  -25.362 1.000 21.677 ? 100 ASN A CB  1 ? 5  
ATOM   754  C  CG  . ASN A 1 100 ? -9.966  23.654  -25.969 1.000 21.396 ? 100 ASN A CG  1 ? 5  
ATOM   755  O  OD1 . ASN A 1 100 ? -9.405  23.853  -27.057 1.000 22.664 ? 100 ASN A OD1 1 ? 5  
ATOM   756  N  ND2 . ASN A 1 100 ? -10.572 24.630  -25.283 1.000 23.361 ? 100 ASN A ND2 1 ? 5  
ATOM   757  N  N   . ASP A 1 101 ? -9.801  21.205  -28.739 1.000 20.855 ? 101 ASP A N   1 ? 5  
ATOM   758  C  CA  . ASP A 1 101 ? -10.433 21.069  -30.079 1.000 21.549 ? 101 ASP A CA  1 ? 5  
ATOM   759  C  C   . ASP A 1 101 ? -9.473  20.331  -30.967 1.000 20.442 ? 101 ASP A C   1 ? 5  
ATOM   760  O  O   . ASP A 1 101 ? -8.308  20.787  -31.106 1.000 20.815 ? 101 ASP A O   1 ? 5  
ATOM   761  C  CB  . ASP A 1 101 ? -10.741 22.439  -30.682 1.000 21.778 ? 101 ASP A CB  1 ? 5  
ATOM   762  C  CG  . ASP A 1 101 ? -11.595 22.349  -31.953 1.000 24.500 ? 101 ASP A CG  1 ? 5  
ATOM   763  O  OD1 . ASP A 1 101 ? -12.756 21.851  -31.819 1.000 24.054 ? 101 ASP A OD1 1 ? 5  
ATOM   764  O  OD2 . ASP A 1 101 ? -11.148 22.824  -33.073 1.000 22.907 ? 101 ASP A OD2 1 ? 5  
ATOM   765  N  N   . ALA A 1 102 ? -9.789  19.144  -31.398 1.000 21.376 ? 102 ALA A N   1 ? 5  
ATOM   766  C  CA  . ALA A 1 102 ? -8.815  18.284  -32.075 1.000 19.874 ? 102 ALA A CA  1 ? 5  
ATOM   767  C  C   . ALA A 1 102 ? -9.527  17.255  -32.898 1.000 19.892 ? 102 ALA A C   1 ? 5  
ATOM   768  O  O   . ALA A 1 102 ? -10.717 16.973  -32.659 1.000 19.936 ? 102 ALA A O   1 ? 5  
ATOM   769  C  CB  . ALA A 1 102 ? -7.910  17.544  -31.094 1.000 20.086 ? 102 ALA A CB  1 ? 5  
ATOM   770  N  N   . TYR A 1 103 ? -8.815  16.666  -33.844 1.000 19.936 ? 103 TYR A N   1 ? 5  
ATOM   771  C  CA  . TYR A 1 103 ? -9.397  15.579  -34.653 1.000 18.986 ? 103 TYR A CA  1 ? 5  
ATOM   772  C  C   . TYR A 1 103 ? -10.026 14.528  -33.699 1.000 19.870 ? 103 TYR A C   1 ? 5  
ATOM   773  O  O   . TYR A 1 103 ? -9.375  14.069  -32.748 1.000 19.528 ? 103 TYR A O   1 ? 5  
ATOM   774  C  CB  . TYR A 1 103 ? -8.354  14.914  -35.589 1.000 18.758 ? 103 TYR A CB  1 ? 5  
ATOM   775  C  CG  . TYR A 1 103 ? -8.911  13.714  -36.289 1.000 19.433 ? 103 TYR A CG  1 ? 5  
ATOM   776  C  CD1 . TYR A 1 103 ? -10.165 13.741  -36.894 1.000 21.298 ? 103 TYR A CD1 1 ? 5  
ATOM   777  C  CD2 . TYR A 1 103 ? -8.277  12.499  -36.228 1.000 19.171 ? 103 TYR A CD2 1 ? 5  
ATOM   778  C  CE1 . TYR A 1 103 ? -10.740 12.598  -37.472 1.000 20.910 ? 103 TYR A CE1 1 ? 5  
ATOM   779  C  CE2 . TYR A 1 103 ? -8.801  11.365  -36.838 1.000 18.803 ? 103 TYR A CE2 1 ? 5  
ATOM   780  C  CZ  . TYR A 1 103 ? -10.068 11.395  -37.398 1.000 20.638 ? 103 TYR A CZ  1 ? 5  
ATOM   781  O  OH  . TYR A 1 103 ? -10.664 10.253  -37.913 1.000 21.753 ? 103 TYR A OH  1 ? 5  
ATOM   782  N  N   . GLY A 1 104 ? -11.267 14.107  -33.963 1.000 19.565 ? 104 GLY A N   1 ? 5  
ATOM   783  C  CA  . GLY A 1 104 ? -11.947 13.142  -33.078 1.000 19.985 ? 104 GLY A CA  1 ? 5  
ATOM   784  C  C   . GLY A 1 104 ? -11.169 11.862  -32.945 1.000 19.603 ? 104 GLY A C   1 ? 5  
ATOM   785  O  O   . GLY A 1 104 ? -11.178 11.298  -31.850 1.000 19.008 ? 104 GLY A O   1 ? 5  
ATOM   786  N  N   . GLY A 1 105 ? -10.453 11.406  -33.974 1.000 18.116 ? 105 GLY A N   1 ? 5  
ATOM   787  C  CA  . GLY A 1 105 ? -9.636  10.182  -33.829 1.000 18.532 ? 105 GLY A CA  1 ? 5  
ATOM   788  C  C   . GLY A 1 105 ? -8.511  10.315  -32.839 1.000 18.911 ? 105 GLY A C   1 ? 5  
ATOM   789  O  O   . GLY A 1 105 ? -8.127  9.340   -32.223 1.000 18.427 ? 105 GLY A O   1 ? 5  
ATOM   790  N  N   . THR A 1 106 ? -7.879  11.480  -32.781 1.000 18.283 ? 106 THR A N   1 ? 5  
ATOM   791  C  CA  . THR A 1 106 ? -6.851  11.735  -31.783 1.000 18.414 ? 106 THR A CA  1 ? 5  
ATOM   792  C  C   . THR A 1 106 ? -7.467  11.562  -30.393 1.000 19.653 ? 106 THR A C   1 ? 5  
ATOM   793  O  O   . THR A 1 106 ? -6.908  10.866  -29.523 1.000 18.979 ? 106 THR A O   1 ? 5  
ATOM   794  C  CB  . THR A 1 106 ? -6.253  13.128  -31.940 1.000 19.384 ? 106 THR A CB  1 ? 5  
ATOM   795  O  OG1 . THR A 1 106 ? -5.697  13.213  -33.265 1.000 19.944 ? 106 THR A OG1 1 ? 5  
ATOM   796  C  CG2 . THR A 1 106 ? -5.142  13.334  -30.942 1.000 19.910 ? 106 THR A CG2 1 ? 5  
ATOM   797  N  N   . PHE A 1 107 ? -8.573  12.219  -30.143 1.000 18.467 ? 107 PHE A N   1 ? 5  
ATOM   798  C  CA  . PHE A 1 107 ? -9.296  12.143  -28.861 1.000 19.543 ? 107 PHE A CA  1 ? 5  
ATOM   799  C  C   . PHE A 1 107 ? -9.595  10.665  -28.586 1.000 19.894 ? 107 PHE A C   1 ? 5  
ATOM   800  O  O   . PHE A 1 107 ? -9.440  10.202  -27.460 1.000 19.535 ? 107 PHE A O   1 ? 5  
ATOM   801  C  CB  . PHE A 1 107 ? -10.561 12.997  -28.916 1.000 20.466 ? 107 PHE A CB  1 ? 5  
ATOM   802  C  CG  . PHE A 1 107 ? -11.412 12.809  -27.691 1.000 20.965 ? 107 PHE A CG  1 ? 5  
ATOM   803  C  CD1 . PHE A 1 107 ? -11.013 13.361  -26.461 1.000 23.305 ? 107 PHE A CD1 1 ? 5  
ATOM   804  C  CD2 . PHE A 1 107 ? -12.606 12.110  -27.776 1.000 21.759 ? 107 PHE A CD2 1 ? 5  
ATOM   805  C  CE1 . PHE A 1 107 ? -11.809 13.164  -25.327 1.000 23.316 ? 107 PHE A CE1 1 ? 5  
ATOM   806  C  CE2 . PHE A 1 107 ? -13.372 11.890  -26.622 1.000 24.085 ? 107 PHE A CE2 1 ? 5  
ATOM   807  C  CZ  . PHE A 1 107 ? -12.967 12.435  -25.426 1.000 22.362 ? 107 PHE A CZ  1 ? 5  
ATOM   808  N  N   . ARG A 1 108 ? -10.162 9.984   -29.557 1.000 20.531 ? 108 ARG A N   1 ? 5  
ATOM   809  C  CA  . ARG A 1 108 ? -10.582 8.568   -29.390 1.000 19.801 ? 108 ARG A CA  1 ? 5  
ATOM   810  C  C   . ARG A 1 108 ? -9.355  7.730   -29.022 1.000 19.545 ? 108 ARG A C   1 ? 5  
ATOM   811  O  O   . ARG A 1 108 ? -9.463  6.864   -28.102 1.000 19.711 ? 108 ARG A O   1 ? 5  
ATOM   812  C  CB  . ARG A 1 108 ? -11.241 8.085   -30.667 1.000 19.767 ? 108 ARG A CB  1 ? 5  
ATOM   813  C  CG  . ARG A 1 108 ? -11.673 6.619   -30.659 1.000 20.968 ? 108 ARG A CG  1 ? 5  
ATOM   814  C  CD  . ARG A 1 108 ? -12.499 6.263   -31.851 1.000 22.423 ? 108 ARG A CD  1 ? 5  
ATOM   815  N  NE  . ARG A 1 108 ? -11.600 6.461   -32.999 1.000 21.123 ? 108 ARG A NE  1 ? 5  
ATOM   816  C  CZ  . ARG A 1 108 ? -11.989 6.806   -34.220 1.000 22.514 ? 108 ARG A CZ  1 ? 5  
ATOM   817  N  NH1 . ARG A 1 108 ? -13.269 6.911   -34.476 1.000 24.221 ? 108 ARG A NH1 1 ? 5  
ATOM   818  N  NH2 . ARG A 1 108 ? -11.081 7.108   -35.151 1.000 21.656 ? 108 ARG A NH2 1 ? 5  
ATOM   819  N  N   . LEU A 1 109 ? -8.217  7.887   -29.711 1.000 18.673 ? 109 LEU A N   1 ? 5  
ATOM   820  C  CA  . LEU A 1 109 ? -7.042  7.038   -29.405 1.000 18.690 ? 109 LEU A CA  1 ? 5  
ATOM   821  C  C   . LEU A 1 109 ? -6.575  7.283   -27.975 1.000 19.356 ? 109 LEU A C   1 ? 5  
ATOM   822  O  O   . LEU A 1 109 ? -6.328  6.337   -27.192 1.000 18.562 ? 109 LEU A O   1 ? 5  
ATOM   823  C  CB  . LEU A 1 109 ? -5.954  7.346   -30.404 1.000 18.700 ? 109 LEU A CB  1 ? 5  
ATOM   824  C  CG  . LEU A 1 109 ? -4.651  6.579   -30.203 1.000 18.321 ? 109 LEU A CG  1 ? 5  
ATOM   825  C  CD1 . LEU A 1 109 ? -4.905  5.102   -30.450 1.000 19.590 ? 109 LEU A CD1 1 ? 5  
ATOM   826  C  CD2 . LEU A 1 109 ? -3.546  7.106   -31.084 1.000 19.850 ? 109 LEU A CD2 1 ? 5  
ATOM   827  N  N   . VAL A 1 110 ? -6.493  8.541   -27.578 1.000 18.874 ? 110 VAL A N   1 ? 5  
ATOM   828  C  CA  . VAL A 1 110 ? -5.993  8.876   -26.228 1.000 19.603 ? 110 VAL A CA  1 ? 5  
ATOM   829  C  C   . VAL A 1 110 ? -7.014  8.390   -25.169 1.000 21.547 ? 110 VAL A C   1 ? 5  
ATOM   830  O  O   . VAL A 1 110 ? -6.623  7.755   -24.204 1.000 20.395 ? 110 VAL A O   1 ? 5  
ATOM   831  C  CB  . VAL A 1 110 ? -5.747  10.371  -26.126 1.000 19.968 ? 110 VAL A CB  1 ? 5  
ATOM   832  C  CG1 . VAL A 1 110 ? -5.474  10.771  -24.693 1.000 21.771 ? 110 VAL A CG1 1 ? 5  
ATOM   833  C  CG2 . VAL A 1 110 ? -4.578  10.808  -26.993 1.000 20.622 ? 110 VAL A CG2 1 ? 5  
ATOM   834  N  N   . SER A 1 111 ? -8.285  8.743   -25.293 1.000 20.591 ? 111 SER A N   1 ? 5  
ATOM   835  C  CA  . SER A 1 111 ? -9.287  8.507   -24.224 1.000 21.090 ? 111 SER A CA  1 ? 5  
ATOM   836  C  C   . SER A 1 111 ? -9.759  7.068   -24.221 1.000 21.518 ? 111 SER A C   1 ? 5  
ATOM   837  O  O   . SER A 1 111 ? -10.138 6.594   -23.120 1.000 21.939 ? 111 SER A O   1 ? 5  
ATOM   838  C  CB  . SER A 1 111 ? -10.463 9.488   -24.331 1.000 22.630 ? 111 SER A CB  1 ? 5  
ATOM   839  O  OG  . SER A 1 111 ? -11.237 9.240   -25.495 1.000 21.366 ? 111 SER A OG  1 ? 5  
ATOM   840  N  N   . LYS A 1 112 ? -9.840  6.389   -25.364 1.000 20.022 ? 112 LYS A N   1 ? 5  
ATOM   841  C  CA  . LYS A 1 112 ? -10.477 5.057   -25.436 1.000 20.380 ? 112 LYS A CA  1 ? 5  
ATOM   842  C  C   . LYS A 1 112 ? -9.438  3.948   -25.501 1.000 22.219 ? 112 LYS A C   1 ? 5  
ATOM   843  O  O   . LYS A 1 112 ? -9.853  2.763   -25.346 1.000 24.347 ? 112 LYS A O   1 ? 5  
ATOM   844  C  CB  . LYS A 1 112 ? -11.417 4.980   -26.637 1.000 20.956 ? 112 LYS A CB  1 ? 5  
ATOM   845  C  CG  . LYS A 1 112 ? -12.482 6.048   -26.610 1.000 21.513 ? 112 LYS A CG  1 ? 5  
ATOM   846  C  CD  . LYS A 1 112 ? -13.222 6.192   -25.331 1.000 23.505 ? 112 LYS A CD  1 ? 5  
ATOM   847  C  CE  . LYS A 1 112 ? -14.425 7.123   -25.449 1.000 25.248 ? 112 LYS A CE  1 ? 5  
ATOM   848  N  NZ  . LYS A 1 112 ? -14.077 8.537   -25.721 1.000 25.226 ? 112 LYS A NZ  1 ? 5  
ATOM   849  N  N   . VAL A 1 113 ? -8.197  4.254   -25.845 1.000 20.492 ? 113 VAL A N   1 ? 5  
ATOM   850  C  CA  . VAL A 1 113 ? -7.130  3.206   -25.897 1.000 20.502 ? 113 VAL A CA  1 ? 5  
ATOM   851  C  C   . VAL A 1 113 ? -6.034  3.530   -24.864 1.000 20.639 ? 113 VAL A C   1 ? 5  
ATOM   852  O  O   . VAL A 1 113 ? -5.801  2.716   -23.957 1.000 20.473 ? 113 VAL A O   1 ? 5  
ATOM   853  C  CB  . VAL A 1 113 ? -6.523  3.043   -27.286 1.000 19.540 ? 113 VAL A CB  1 ? 5  
ATOM   854  C  CG1 . VAL A 1 113 ? -5.469  1.930   -27.294 1.000 20.177 ? 113 VAL A CG1 1 ? 5  
ATOM   855  C  CG2 . VAL A 1 113 ? -7.608  2.772   -28.319 1.000 21.261 ? 113 VAL A CG2 1 ? 5  
ATOM   856  N  N   . PHE A 1 114 ? -5.428  4.694   -24.918 1.000 19.275 ? 114 PHE A N   1 ? 6  
ATOM   857  C  CA  . PHE A 1 114 ? -4.277  4.899   -24.048 1.000 19.006 ? 114 PHE A CA  1 ? 6  
ATOM   858  C  C   . PHE A 1 114 ? -4.703  5.046   -22.563 1.000 19.553 ? 114 PHE A C   1 ? 6  
ATOM   859  O  O   . PHE A 1 114 ? -3.975  4.691   -21.672 1.000 20.580 ? 114 PHE A O   1 ? 6  
ATOM   860  C  CB  . PHE A 1 114 ? -3.428  6.054   -24.534 1.000 20.402 ? 114 PHE A CB  1 ? 6  
ATOM   861  C  CG  . PHE A 1 114 ? -2.434  5.635   -25.592 1.000 19.441 ? 114 PHE A CG  1 ? 6  
ATOM   862  C  CD1 . PHE A 1 114 ? -2.854  5.530   -26.919 1.000 21.145 ? 114 PHE A CD1 1 ? 6  
ATOM   863  C  CD2 . PHE A 1 114 ? -1.139  5.261   -25.276 1.000 20.751 ? 114 PHE A CD2 1 ? 6  
ATOM   864  C  CE1 . PHE A 1 114 ? -2.016  5.037   -27.899 1.000 20.003 ? 114 PHE A CE1 1 ? 6  
ATOM   865  C  CE2 . PHE A 1 114 ? -0.272  4.829   -26.281 1.000 20.885 ? 114 PHE A CE2 1 ? 6  
ATOM   866  C  CZ  . PHE A 1 114 ? -0.707  4.728   -27.578 1.000 20.027 ? 114 PHE A CZ  1 ? 6  
ATOM   867  N  N   . GLU A 1 115 ? -5.882  5.559   -22.298 1.000 20.972 ? 115 GLU A N   1 ? 6  
ATOM   868  C  CA  . GLU A 1 115 ? -6.358  5.683   -20.882 1.000 22.100 ? 115 GLU A CA  1 ? 6  
ATOM   869  C  C   . GLU A 1 115 ? -6.463  4.304   -20.266 1.000 23.196 ? 115 GLU A C   1 ? 6  
ATOM   870  O  O   . GLU A 1 115 ? -6.046  4.145   -19.113 1.000 23.889 ? 115 GLU A O   1 ? 6  
ATOM   871  C  CB  . GLU A 1 115 ? -7.669  6.478   -20.819 1.000 23.387 ? 115 GLU A CB  1 ? 6  
ATOM   872  C  CG  . GLU A 1 115 ? -8.076  6.745   -19.370 1.000 27.095 ? 115 GLU A CG  1 ? 6  
ATOM   873  C  CD  . GLU A 1 115 ? -9.416  7.445   -19.229 1.000 31.737 ? 115 GLU A CD  1 ? 6  
ATOM   874  O  OE1 . GLU A 1 115 ? -10.180 6.993   -18.416 1.000 38.549 ? 115 GLU A OE1 1 ? 6  
ATOM   875  O  OE2 . GLU A 1 115 ? -9.688  8.390   -19.964 1.000 31.531 ? 115 GLU A OE2 1 ? 6  
ATOM   876  N  N   A ARG A 1 116 ? -7.017  3.333   -20.994 0.500 22.938 ? 116 ARG A N   1 ? 6  
ATOM   877  N  N   B ARG A 1 116 ? -7.037  3.338   -20.982 0.500 22.572 ? 116 ARG A N   1 ? 6  
ATOM   878  C  CA  A ARG A 1 116 ? -7.200  1.908   -20.574 0.500 24.816 ? 116 ARG A CA  1 ? 6  
ATOM   879  C  CA  B ARG A 1 116 ? -7.178  1.929   -20.516 0.500 24.035 ? 116 ARG A CA  1 ? 6  
ATOM   880  C  C   A ARG A 1 116 ? -5.811  1.299   -20.318 0.500 23.028 ? 116 ARG A C   1 ? 6  
ATOM   881  C  C   B ARG A 1 116 ? -5.788  1.372   -20.228 0.500 22.675 ? 116 ARG A C   1 ? 6  
ATOM   882  O  O   A ARG A 1 116 ? -5.686  0.387   -19.488 0.500 23.486 ? 116 ARG A O   1 ? 6  
ATOM   883  O  O   B ARG A 1 116 ? -5.659  0.538   -19.311 0.500 23.298 ? 116 ARG A O   1 ? 6  
ATOM   884  C  CB  A ARG A 1 116 ? -8.042  1.247   -21.678 0.500 26.896 ? 116 ARG A CB  1 ? 6  
ATOM   885  C  CB  B ARG A 1 116 ? -7.907  1.103   -21.578 0.500 25.166 ? 116 ARG A CB  1 ? 6  
ATOM   886  C  CG  A ARG A 1 116 ? -8.374  -0.232  -21.535 0.500 31.688 ? 116 ARG A CG  1 ? 6  
ATOM   887  C  CG  B ARG A 1 116 ? -7.705  -0.403  -21.462 0.500 28.066 ? 116 ARG A CG  1 ? 6  
ATOM   888  C  CD  A ARG A 1 116 ? -9.221  -0.795  -22.702 0.500 33.335 ? 116 ARG A CD  1 ? 6  
ATOM   889  C  CD  B ARG A 1 116 ? -8.595  -1.245  -22.414 0.500 30.620 ? 116 ARG A CD  1 ? 6  
ATOM   890  N  NE  A ARG A 1 116 ? -8.438  -1.801  -23.469 0.500 37.096 ? 116 ARG A NE  1 ? 6  
ATOM   891  N  NE  B ARG A 1 116 ? -9.103  -0.546  -23.606 0.500 29.371 ? 116 ARG A NE  1 ? 6  
ATOM   892  C  CZ  A ARG A 1 116 ? -8.171  -2.987  -22.983 0.500 35.175 ? 116 ARG A CZ  1 ? 6  
ATOM   893  C  CZ  B ARG A 1 116 ? -8.615  -0.598  -24.877 0.500 28.690 ? 116 ARG A CZ  1 ? 6  
ATOM   894  N  NH1 A ARG A 1 116 ? -8.757  -3.339  -21.866 0.500 40.053 ? 116 ARG A NH1 1 ? 6  
ATOM   895  N  NH1 B ARG A 1 116 ? -7.530  -1.343  -25.203 0.500 27.957 ? 116 ARG A NH1 1 ? 6  
ATOM   896  N  NH2 A ARG A 1 116 ? -7.458  -3.861  -23.649 0.500 34.004 ? 116 ARG A NH2 1 ? 6  
ATOM   897  N  NH2 B ARG A 1 116 ? -9.267  0.100   -25.804 0.500 24.163 ? 116 ARG A NH2 1 ? 6  
ATOM   898  N  N   . TRP A 1 117 ? -4.796  1.810   -20.988 1.000 21.042 ? 117 TRP A N   1 ? 6  
ATOM   899  C  CA  . TRP A 1 117 ? -3.393  1.353   -20.889 1.000 21.042 ? 117 TRP A CA  1 ? 6  
ATOM   900  C  C   . TRP A 1 117 ? -2.617  2.212   -19.891 1.000 21.802 ? 117 TRP A C   1 ? 6  
ATOM   901  O  O   . TRP A 1 117 ? -1.376  2.121   -19.835 1.000 23.733 ? 117 TRP A O   1 ? 6  
ATOM   902  C  CB  . TRP A 1 117 ? -2.763  1.286   -22.285 1.000 20.877 ? 117 TRP A CB  1 ? 6  
ATOM   903  C  CG  . TRP A 1 117 ? -3.106  0.045   -23.038 1.000 20.030 ? 117 TRP A CG  1 ? 6  
ATOM   904  C  CD1 . TRP A 1 117 ? -4.151  -0.202  -23.860 1.000 20.195 ? 117 TRP A CD1 1 ? 6  
ATOM   905  C  CD2 . TRP A 1 117 ? -2.402  -1.185  -22.926 1.000 19.709 ? 117 TRP A CD2 1 ? 6  
ATOM   906  N  NE1 . TRP A 1 117 ? -4.124  -1.495  -24.312 1.000 19.801 ? 117 TRP A NE1 1 ? 6  
ATOM   907  C  CE2 . TRP A 1 117 ? -3.052  -2.121  -23.749 1.000 19.571 ? 117 TRP A CE2 1 ? 6  
ATOM   908  C  CE3 . TRP A 1 117 ? -1.251  -1.563  -22.207 1.000 20.043 ? 117 TRP A CE3 1 ? 6  
ATOM   909  C  CZ2 . TRP A 1 117 ? -2.624  -3.437  -23.843 1.000 20.010 ? 117 TRP A CZ2 1 ? 6  
ATOM   910  C  CZ3 . TRP A 1 117 ? -0.825  -2.872  -22.300 1.000 20.460 ? 117 TRP A CZ3 1 ? 6  
ATOM   911  C  CH2 . TRP A 1 117 ? -1.510  -3.777  -23.111 1.000 20.905 ? 117 TRP A CH2 1 ? 6  
ATOM   912  N  N   . GLY A 1 118 ? -3.313  2.998   -19.076 1.000 21.831 ? 118 GLY A N   1 ? 6  
ATOM   913  C  CA  . GLY A 1 118 ? -2.776  3.673   -17.900 1.000 23.208 ? 118 GLY A CA  1 ? 6  
ATOM   914  C  C   . GLY A 1 118 ? -2.241  5.077   -18.108 1.000 22.967 ? 118 GLY A C   1 ? 6  
ATOM   915  O  O   . GLY A 1 118 ? -1.606  5.570   -17.150 1.000 23.429 ? 118 GLY A O   1 ? 6  
ATOM   916  N  N   . VAL A 1 119 ? -2.556  5.734   -19.238 1.000 21.129 ? 119 VAL A N   1 ? 6  
ATOM   917  C  CA  . VAL A 1 119 ? -2.102  7.117   -19.496 1.000 21.222 ? 119 VAL A CA  1 ? 6  
ATOM   918  C  C   . VAL A 1 119 ? -3.213  8.068   -19.145 1.000 22.286 ? 119 VAL A C   1 ? 6  
ATOM   919  O  O   . VAL A 1 119 ? -4.318  7.917   -19.668 1.000 23.890 ? 119 VAL A O   1 ? 6  
ATOM   920  C  CB  . VAL A 1 119 ? -1.645  7.313   -20.951 1.000 20.414 ? 119 VAL A CB  1 ? 6  
ATOM   921  C  CG1 . VAL A 1 119 ? -1.198  8.752   -21.203 1.000 21.619 ? 119 VAL A CG1 1 ? 6  
ATOM   922  C  CG2 . VAL A 1 119 ? -0.535  6.346   -21.304 1.000 22.133 ? 119 VAL A CG2 1 ? 6  
ATOM   923  N  N   . SER A 1 120 ? -2.965  8.974   -18.218 1.000 23.241 ? 120 SER A N   1 ? 6  
ATOM   924  C  CA  . SER A 1 120 ? -3.937  10.020  -17.860 1.000 24.701 ? 120 SER A CA  1 ? 6  
ATOM   925  C  C   . SER A 1 120 ? -3.814  11.164  -18.880 1.000 23.592 ? 120 SER A C   1 ? 6  
ATOM   926  O  O   . SER A 1 120 ? -2.773  11.305  -19.546 1.000 22.647 ? 120 SER A O   1 ? 6  
ATOM   927  C  CB  . SER A 1 120 ? -3.760  10.478  -16.409 1.000 27.745 ? 120 SER A CB  1 ? 6  
ATOM   928  O  OG  . SER A 1 120 ? -2.498  11.069  -16.247 1.000 32.397 ? 120 SER A OG  1 ? 6  
ATOM   929  N  N   . TRP A 1 121 ? -4.839  11.978  -18.949 1.000 22.114 ? 121 TRP A N   1 ? 6  
ATOM   930  C  CA  . TRP A 1 121 ? -4.881  13.086  -19.891 1.000 22.158 ? 121 TRP A CA  1 ? 6  
ATOM   931  C  C   . TRP A 1 121 ? -5.799  14.188  -19.400 1.000 22.760 ? 121 TRP A C   1 ? 6  
ATOM   932  O  O   . TRP A 1 121 ? -6.782  13.895  -18.669 1.000 23.789 ? 121 TRP A O   1 ? 6  
ATOM   933  C  CB  . TRP A 1 121 ? -5.246  12.556  -21.292 1.000 21.418 ? 121 TRP A CB  1 ? 6  
ATOM   934  C  CG  . TRP A 1 121 ? -6.629  11.969  -21.396 1.000 21.422 ? 121 TRP A CG  1 ? 6  
ATOM   935  C  CD1 . TRP A 1 121 ? -6.969  10.676  -21.088 1.000 22.634 ? 121 TRP A CD1 1 ? 6  
ATOM   936  C  CD2 . TRP A 1 121 ? -7.875  12.649  -21.669 1.000 22.201 ? 121 TRP A CD2 1 ? 6  
ATOM   937  N  NE1 . TRP A 1 121 ? -8.309  10.497  -21.216 1.000 23.467 ? 121 TRP A NE1 1 ? 6  
ATOM   938  C  CE2 . TRP A 1 121 ? -8.894  11.686  -21.544 1.000 22.729 ? 121 TRP A CE2 1 ? 6  
ATOM   939  C  CE3 . TRP A 1 121 ? -8.238  13.949  -21.965 1.000 22.730 ? 121 TRP A CE3 1 ? 6  
ATOM   940  C  CZ2 . TRP A 1 121 ? -10.233 12.011  -21.670 1.000 25.128 ? 121 TRP A CZ2 1 ? 6  
ATOM   941  C  CZ3 . TRP A 1 121 ? -9.560  14.282  -22.133 1.000 26.231 ? 121 TRP A CZ3 1 ? 6  
ATOM   942  C  CH2 . TRP A 1 121 ? -10.545 13.311  -21.983 1.000 25.436 ? 121 TRP A CH2 1 ? 6  
ATOM   943  N  N   . ASP A 1 122 ? -5.546  15.366  -19.916 1.000 23.263 ? 122 ASP A N   1 ? 6  
ATOM   944  C  CA  . ASP A 1 122 ? -6.424  16.535  -19.781 1.000 23.390 ? 122 ASP A CA  1 ? 6  
ATOM   945  C  C   . ASP A 1 122 ? -6.473  17.272  -21.093 1.000 22.086 ? 122 ASP A C   1 ? 6  
ATOM   946  O  O   . ASP A 1 122 ? -5.432  17.389  -21.731 1.000 21.679 ? 122 ASP A O   1 ? 6  
ATOM   947  C  CB  . ASP A 1 122 ? -5.905  17.470  -18.680 1.000 24.614 ? 122 ASP A CB  1 ? 6  
ATOM   948  C  CG  . ASP A 1 122 ? -6.172  16.865  -17.313 1.000 27.759 ? 122 ASP A CG  1 ? 6  
ATOM   949  O  OD1 . ASP A 1 122 ? -7.351  16.908  -16.882 1.000 28.797 ? 122 ASP A OD1 1 ? 6  
ATOM   950  O  OD2 . ASP A 1 122 ? -5.238  16.322  -16.701 1.000 28.380 ? 122 ASP A OD2 1 ? 6  
ATOM   951  N  N   . ALA A 1 123 ? -7.637  17.773  -21.463 1.000 21.540 ? 123 ALA A N   1 ? 6  
ATOM   952  C  CA  . ALA A 1 123 ? -7.810  18.626  -22.643 1.000 21.203 ? 123 ALA A CA  1 ? 6  
ATOM   953  C  C   . ALA A 1 123 ? -7.767  20.094  -22.170 1.000 21.873 ? 123 ALA A C   1 ? 6  
ATOM   954  O  O   . ALA A 1 123 ? -8.498  20.462  -21.217 1.000 23.478 ? 123 ALA A O   1 ? 6  
ATOM   955  C  CB  . ALA A 1 123 ? -9.145  18.308  -23.276 1.000 23.322 ? 123 ALA A CB  1 ? 6  
ATOM   956  N  N   . VAL A 1 124 ? -6.965  20.884  -22.817 1.000 20.966 ? 124 VAL A N   1 ? 6  
ATOM   957  C  CA  . VAL A 1 124 ? -6.632  22.260  -22.409 1.000 22.835 ? 124 VAL A CA  1 ? 6  
ATOM   958  C  C   . VAL A 1 124 ? -6.840  23.151  -23.609 1.000 21.540 ? 124 VAL A C   1 ? 6  
ATOM   959  O  O   . VAL A 1 124 ? -6.498  22.768  -24.744 1.000 21.144 ? 124 VAL A O   1 ? 6  
ATOM   960  C  CB  . VAL A 1 124 ? -5.176  22.283  -21.865 1.000 23.134 ? 124 VAL A CB  1 ? 6  
ATOM   961  C  CG1 . VAL A 1 124 ? -4.749  23.632  -21.457 1.000 27.130 ? 124 VAL A CG1 1 ? 6  
ATOM   962  C  CG2 . VAL A 1 124 ? -5.016  21.291  -20.694 1.000 24.140 ? 124 VAL A CG2 1 ? 6  
ATOM   963  N  N   . ASP A 1 125 ? -7.191  24.387  -23.353 1.000 21.068 ? 125 ASP A N   1 ? 6  
ATOM   964  C  CA  . ASP A 1 125 ? -7.171  25.442  -24.378 1.000 21.701 ? 125 ASP A CA  1 ? 6  
ATOM   965  C  C   . ASP A 1 125 ? -5.705  25.831  -24.688 1.000 20.769 ? 125 ASP A C   1 ? 6  
ATOM   966  O  O   . ASP A 1 125 ? -5.130  26.596  -23.944 1.000 22.435 ? 125 ASP A O   1 ? 6  
ATOM   967  C  CB  . ASP A 1 125 ? -7.942  26.650  -23.848 1.000 23.083 ? 125 ASP A CB  1 ? 6  
ATOM   968  C  CG  . ASP A 1 125 ? -7.945  27.790  -24.857 1.000 24.946 ? 125 ASP A CG  1 ? 6  
ATOM   969  O  OD1 . ASP A 1 125 ? -7.453  27.587  -26.014 1.000 23.801 ? 125 ASP A OD1 1 ? 6  
ATOM   970  O  OD2 . ASP A 1 125 ? -8.480  28.859  -24.471 1.000 25.457 ? 125 ASP A OD2 1 ? 6  
ATOM   971  N  N   . LEU A 1 126 ? -5.135  25.293  -25.761 1.000 21.249 ? 126 LEU A N   1 ? 6  
ATOM   972  C  CA  . LEU A 1 126 ? -3.712  25.557  -26.086 1.000 20.960 ? 126 LEU A CA  1 ? 6  
ATOM   973  C  C   . LEU A 1 126 ? -3.505  26.985  -26.566 1.000 22.510 ? 126 LEU A C   1 ? 6  
ATOM   974  O  O   . LEU A 1 126 ? -2.362  27.351  -26.718 1.000 23.963 ? 126 LEU A O   1 ? 6  
ATOM   975  C  CB  . LEU A 1 126 ? -3.244  24.545  -27.129 1.000 22.787 ? 126 LEU A CB  1 ? 6  
ATOM   976  C  CG  . LEU A 1 126 ? -3.413  23.094  -26.686 1.000 23.067 ? 126 LEU A CG  1 ? 6  
ATOM   977  C  CD1 . LEU A 1 126 ? -2.914  22.200  -27.773 1.000 26.123 ? 126 LEU A CD1 1 ? 6  
ATOM   978  C  CD2 . LEU A 1 126 ? -2.694  22.783  -25.400 1.000 26.027 ? 126 LEU A CD2 1 ? 6  
ATOM   979  N  N   . SER A 1 127 ? -4.556  27.715  -26.878 1.000 22.532 ? 127 SER A N   1 ? 6  
ATOM   980  C  CA  . SER A 1 127 ? -4.483  29.150  -27.240 1.000 23.754 ? 127 SER A CA  1 ? 6  
ATOM   981  C  C   . SER A 1 127 ? -4.221  29.954  -25.967 1.000 24.856 ? 127 SER A C   1 ? 6  
ATOM   982  O  O   . SER A 1 127 ? -3.978  31.160  -26.120 1.000 27.340 ? 127 SER A O   1 ? 6  
ATOM   983  C  CB  . SER A 1 127 ? -5.767  29.585  -27.956 1.000 24.681 ? 127 SER A CB  1 ? 6  
ATOM   984  O  OG  . SER A 1 127 ? -5.990  28.765  -29.114 1.000 26.373 ? 127 SER A OG  1 ? 6  
ATOM   985  N  N   . ASN A 1 128 ? -4.327  29.345  -24.788 1.000 26.297 ? 128 ASN A N   1 ? 7  
ATOM   986  C  CA  . ASN A 1 128 ? -4.145  30.040  -23.462 1.000 27.138 ? 128 ASN A CA  1 ? 7  
ATOM   987  C  C   . ASN A 1 128 ? -2.918  29.468  -22.780 1.000 26.130 ? 128 ASN A C   1 ? 7  
ATOM   988  O  O   . ASN A 1 128 ? -2.964  28.420  -22.128 1.000 26.347 ? 128 ASN A O   1 ? 7  
ATOM   989  C  CB  . ASN A 1 128 ? -5.408  29.785  -22.626 1.000 28.013 ? 128 ASN A CB  1 ? 7  
ATOM   990  C  CG  . ASN A 1 128 ? -5.420  30.466  -21.275 1.000 31.786 ? 128 ASN A CG  1 ? 7  
ATOM   991  O  OD1 . ASN A 1 128 ? -4.356  30.945  -20.846 1.000 31.584 ? 128 ASN A OD1 1 ? 7  
ATOM   992  N  ND2 . ASN A 1 128 ? -6.573  30.426  -20.641 1.000 31.658 ? 128 ASN A ND2 1 ? 7  
ATOM   993  N  N   . PRO A 1 129 ? -1.722  30.054  -22.973 1.000 28.101 ? 129 PRO A N   1 ? 7  
ATOM   994  C  CA  . PRO A 1 129 ? -0.517  29.468  -22.395 1.000 28.646 ? 129 PRO A CA  1 ? 7  
ATOM   995  C  C   . PRO A 1 129 ? -0.566  29.273  -20.872 1.000 29.156 ? 129 PRO A C   1 ? 7  
ATOM   996  O  O   . PRO A 1 129 ? 0.096   28.360  -20.348 1.000 27.814 ? 129 PRO A O   1 ? 7  
ATOM   997  C  CB  . PRO A 1 129 ? 0.578   30.457  -22.895 1.000 30.508 ? 129 PRO A CB  1 ? 7  
ATOM   998  C  CG  . PRO A 1 129 ? 0.016   31.007  -24.187 1.000 31.005 ? 129 PRO A CG  1 ? 7  
ATOM   999  C  CD  . PRO A 1 129 ? -1.455  31.192  -23.863 1.000 30.203 ? 129 PRO A CD  1 ? 7  
ATOM   1000 N  N   . GLU A 1 130 ? -1.287  30.138  -20.124 1.000 31.325 ? 130 GLU A N   1 ? 7  
ATOM   1001 C  CA  . GLU A 1 130 ? -1.473  29.957  -18.664 1.000 33.137 ? 130 GLU A CA  1 ? 7  
ATOM   1002 C  C   . GLU A 1 130 ? -2.167  28.642  -18.365 1.000 32.243 ? 130 GLU A C   1 ? 7  
ATOM   1003 O  O   . GLU A 1 130 ? -1.768  27.990  -17.434 1.000 31.806 ? 130 GLU A O   1 ? 7  
ATOM   1004 C  CB  . GLU A 1 130 ? -2.343  31.046  -18.007 1.000 37.618 ? 130 GLU A CB  1 ? 7  
ATOM   1005 C  CG  . GLU A 1 130 ? -1.598  32.283  -17.766 1.000 42.654 ? 130 GLU A CG  1 ? 7  
ATOM   1006 C  CD  . GLU A 1 130 ? -2.415  33.395  -17.097 1.000 49.808 ? 130 GLU A CD  1 ? 7  
ATOM   1007 O  OE1 . GLU A 1 130 ? -3.095  33.154  -16.082 1.000 50.763 ? 130 GLU A OE1 1 ? 7  
ATOM   1008 O  OE2 . GLU A 1 130 ? -2.324  34.521  -17.596 1.000 63.125 ? 130 GLU A OE2 1 ? 7  
ATOM   1009 N  N   . ALA A 1 131 ? -3.216  28.292  -19.118 1.000 29.718 ? 131 ALA A N   1 ? 7  
ATOM   1010 C  CA  . ALA A 1 131 ? -3.947  27.067  -18.878 1.000 29.786 ? 131 ALA A CA  1 ? 7  
ATOM   1011 C  C   . ALA A 1 131 ? -2.949  25.940  -19.150 1.000 26.615 ? 131 ALA A C   1 ? 7  
ATOM   1012 O  O   . ALA A 1 131 ? -3.043  24.928  -18.478 1.000 29.145 ? 131 ALA A O   1 ? 7  
ATOM   1013 C  CB  . ALA A 1 131 ? -5.183  27.044  -19.755 1.000 30.056 ? 131 ALA A CB  1 ? 7  
ATOM   1014 N  N   . VAL A 1 132 ? -2.136  26.055  -20.204 1.000 24.667 ? 132 VAL A N   1 ? 7  
ATOM   1015 C  CA  . VAL A 1 132 ? -1.200  24.951  -20.548 1.000 23.749 ? 132 VAL A CA  1 ? 7  
ATOM   1016 C  C   . VAL A 1 132 ? -0.188  24.794  -19.394 1.000 24.827 ? 132 VAL A C   1 ? 7  
ATOM   1017 O  O   . VAL A 1 132 ? 0.060   23.666  -18.889 1.000 26.051 ? 132 VAL A O   1 ? 7  
ATOM   1018 C  CB  . VAL A 1 132 ? -0.495  25.222  -21.890 1.000 24.065 ? 132 VAL A CB  1 ? 7  
ATOM   1019 C  CG1 . VAL A 1 132 ? 0.491   24.097  -22.218 1.000 24.909 ? 132 VAL A CG1 1 ? 7  
ATOM   1020 C  CG2 . VAL A 1 132 ? -1.508  25.406  -23.015 1.000 23.731 ? 132 VAL A CG2 1 ? 7  
ATOM   1021 N  N   . ARG A 1 133 ? 0.421   25.895  -18.946 1.000 25.896 ? 133 ARG A N   1 ? 7  
ATOM   1022 C  CA  . ARG A 1 133 ? 1.445   25.851  -17.879 1.000 26.285 ? 133 ARG A CA  1 ? 7  
ATOM   1023 C  C   . ARG A 1 133 ? 0.832   25.239  -16.620 1.000 27.602 ? 133 ARG A C   1 ? 7  
ATOM   1024 O  O   . ARG A 1 133 ? 1.453   24.343  -15.956 1.000 25.997 ? 133 ARG A O   1 ? 7  
ATOM   1025 C  CB  . ARG A 1 133 ? 1.945   27.302  -17.719 1.000 28.812 ? 133 ARG A CB  1 ? 7  
ATOM   1026 C  CG  . ARG A 1 133 ? 3.370   27.500  -17.368 1.000 31.828 ? 133 ARG A CG  1 ? 7  
ATOM   1027 C  CD  . ARG A 1 133 ? 3.707   28.933  -17.202 1.000 32.270 ? 133 ARG A CD  1 ? 7  
ATOM   1028 N  NE  . ARG A 1 133 ? 4.311   29.468  -18.430 1.000 30.595 ? 133 ARG A NE  1 ? 7  
ATOM   1029 C  CZ  . ARG A 1 133 ? 3.738   30.328  -19.261 1.000 30.689 ? 133 ARG A CZ  1 ? 7  
ATOM   1030 N  NH1 . ARG A 1 133 ? 4.418   30.732  -20.312 1.000 30.650 ? 133 ARG A NH1 1 ? 7  
ATOM   1031 N  NH2 . ARG A 1 133 ? 2.578   30.919  -18.953 1.000 30.381 ? 133 ARG A NH2 1 ? 7  
ATOM   1032 N  N   . THR A 1 134 ? -0.409  25.596  -16.247 1.000 29.070 ? 134 THR A N   1 ? 7  
ATOM   1033 C  CA  . THR A 1 134 ? -0.957  25.050  -14.972 1.000 31.482 ? 134 THR A CA  1 ? 7  
ATOM   1034 C  C   . THR A 1 134 ? -1.444  23.626  -15.130 1.000 29.524 ? 134 THR A C   1 ? 7  
ATOM   1035 O  O   . THR A 1 134 ? -1.849  22.988  -14.116 1.000 31.615 ? 134 THR A O   1 ? 7  
ATOM   1036 C  CB  . THR A 1 134 ? -2.058  25.959  -14.383 1.000 36.317 ? 134 THR A CB  1 ? 7  
ATOM   1037 O  OG1 . THR A 1 134 ? -3.186  26.007  -15.224 1.000 35.875 ? 134 THR A OG1 1 ? 7  
ATOM   1038 C  CG2 . THR A 1 134 ? -1.579  27.386  -14.240 1.000 43.048 ? 134 THR A CG2 1 ? 7  
ATOM   1039 N  N   . ALA A 1 135 ? -1.589  23.119  -16.368 1.000 26.282 ? 135 ALA A N   1 ? 7  
ATOM   1040 C  CA  . ALA A 1 135 ? -2.091  21.751  -16.590 1.000 26.870 ? 135 ALA A CA  1 ? 7  
ATOM   1041 C  C   . ALA A 1 135 ? -0.930  20.751  -16.453 1.000 24.676 ? 135 ALA A C   1 ? 7  
ATOM   1042 O  O   . ALA A 1 135 ? -1.186  19.598  -16.368 1.000 25.895 ? 135 ALA A O   1 ? 7  
ATOM   1043 C  CB  . ALA A 1 135 ? -2.732  21.639  -17.962 1.000 26.499 ? 135 ALA A CB  1 ? 7  
ATOM   1044 N  N   . ILE A 1 136 ? 0.296   21.219  -16.479 1.000 25.490 ? 136 ILE A N   1 ? 7  
ATOM   1045 C  CA  . ILE A 1 136 ? 1.486   20.347  -16.338 1.000 26.245 ? 136 ILE A CA  1 ? 7  
ATOM   1046 C  C   . ILE A 1 136 ? 1.374   19.655  -14.974 1.000 26.314 ? 136 ILE A C   1 ? 7  
ATOM   1047 O  O   . ILE A 1 136 ? 1.188   20.320  -13.894 1.000 27.728 ? 136 ILE A O   1 ? 7  
ATOM   1048 C  CB  . ILE A 1 136 ? 2.778   21.171  -16.442 1.000 28.947 ? 136 ILE A CB  1 ? 7  
ATOM   1049 C  CG1 . ILE A 1 136 ? 2.959   21.853  -17.798 1.000 31.557 ? 136 ILE A CG1 1 ? 7  
ATOM   1050 C  CG2 . ILE A 1 136 ? 3.990   20.356  -15.999 1.000 30.286 ? 136 ILE A CG2 1 ? 7  
ATOM   1051 C  CD1 . ILE A 1 136 ? 3.410   21.029  -18.803 1.000 34.277 ? 136 ILE A CD1 1 ? 7  
ATOM   1052 N  N   . ARG A 1 137 ? 1.582   18.387  -14.990 1.000 26.001 ? 137 ARG A N   1 ? 7  
ATOM   1053 C  CA  . ARG A 1 137 ? 1.696   17.531  -13.817 1.000 28.640 ? 137 ARG A CA  1 ? 7  
ATOM   1054 C  C   . ARG A 1 137 ? 3.104   16.940  -13.772 1.000 28.521 ? 137 ARG A C   1 ? 7  
ATOM   1055 O  O   . ARG A 1 137 ? 3.844   16.886  -14.753 1.000 26.262 ? 137 ARG A O   1 ? 7  
ATOM   1056 C  CB  . ARG A 1 137 ? 0.656   16.424  -13.872 1.000 30.819 ? 137 ARG A CB  1 ? 7  
ATOM   1057 C  CG  . ARG A 1 137 ? -0.783  16.866  -14.002 1.000 33.161 ? 137 ARG A CG  1 ? 7  
ATOM   1058 C  CD  . ARG A 1 137 ? -1.575  15.597  -13.838 1.000 37.287 ? 137 ARG A CD  1 ? 7  
ATOM   1059 N  NE  . ARG A 1 137 ? -2.979  15.594  -14.259 1.000 40.338 ? 137 ARG A NE  1 ? 7  
ATOM   1060 C  CZ  . ARG A 1 137 ? -3.818  14.465  -14.203 1.000 45.079 ? 137 ARG A CZ  1 ? 7  
ATOM   1061 N  NH1 . ARG A 1 137 ? -3.430  13.285  -13.667 1.000 45.436 ? 137 ARG A NH1 1 ? 7  
ATOM   1062 N  NH2 . ARG A 1 137 ? -5.050  14.541  -14.708 1.000 45.957 ? 137 ARG A NH2 1 ? 7  
ATOM   1063 N  N   . PRO A 1 138 ? 3.527   16.428  -12.619 1.000 31.873 ? 138 PRO A N   1 ? 8  
ATOM   1064 C  CA  . PRO A 1 138 ? 4.856   15.831  -12.526 1.000 32.342 ? 138 PRO A CA  1 ? 8  
ATOM   1065 C  C   . PRO A 1 138 ? 5.020   14.654  -13.487 1.000 30.941 ? 138 PRO A C   1 ? 8  
ATOM   1066 O  O   . PRO A 1 138 ? 6.105   14.475  -14.017 1.000 31.186 ? 138 PRO A O   1 ? 8  
ATOM   1067 C  CB  . PRO A 1 138 ? 4.894   15.352  -11.083 1.000 34.232 ? 138 PRO A CB  1 ? 8  
ATOM   1068 C  CG  . PRO A 1 138 ? 3.995   16.348  -10.372 1.000 35.964 ? 138 PRO A CG  1 ? 8  
ATOM   1069 C  CD  . PRO A 1 138 ? 2.843   16.562  -11.330 1.000 34.255 ? 138 PRO A CD  1 ? 8  
ATOM   1070 N  N   A GLU A 1 139 ? 3.900   13.975  -13.805 0.500 31.206 ? 139 GLU A N   1 ? 8  
ATOM   1071 N  N   B GLU A 1 139 ? 3.917   14.003  -13.851 0.500 29.507 ? 139 GLU A N   1 ? 8  
ATOM   1072 C  CA  A GLU A 1 139 ? 3.839   12.817  -14.743 0.500 30.232 ? 139 GLU A CA  1 ? 8  
ATOM   1073 C  CA  B GLU A 1 139 ? 3.952   12.829  -14.751 0.500 27.631 ? 139 GLU A CA  1 ? 8  
ATOM   1074 C  C   A GLU A 1 139 ? 3.743   13.238  -16.225 0.500 26.740 ? 139 GLU A C   1 ? 8  
ATOM   1075 C  C   B GLU A 1 139 ? 3.703   13.227  -16.223 0.500 25.428 ? 139 GLU A C   1 ? 8  
ATOM   1076 O  O   A GLU A 1 139 ? 3.740   12.324  -17.087 0.500 25.175 ? 139 GLU A O   1 ? 8  
ATOM   1077 O  O   B GLU A 1 139 ? 3.650   12.305  -17.080 0.500 24.242 ? 139 GLU A O   1 ? 8  
ATOM   1078 C  CB  A GLU A 1 139 ? 2.579   11.967  -14.510 0.500 32.881 ? 139 GLU A CB  1 ? 8  
ATOM   1079 C  CB  B GLU A 1 139 ? 2.905   11.832  -14.256 0.500 28.294 ? 139 GLU A CB  1 ? 8  
ATOM   1080 C  CG  A GLU A 1 139 ? 2.200   11.720  -13.068 0.500 37.031 ? 139 GLU A CG  1 ? 8  
ATOM   1081 C  CG  B GLU A 1 139 ? 3.045   11.457  -12.786 0.500 29.419 ? 139 GLU A CG  1 ? 8  
ATOM   1082 C  CD  A GLU A 1 139 ? 1.156   12.701  -12.546 0.500 38.471 ? 139 GLU A CD  1 ? 8  
ATOM   1083 C  CD  B GLU A 1 139 ? 2.288   12.389  -11.836 0.500 29.607 ? 139 GLU A CD  1 ? 8  
ATOM   1084 O  OE1 A GLU A 1 139 ? -0.045  12.637  -12.977 0.500 41.385 ? 139 GLU A OE1 1 ? 8  
ATOM   1085 O  OE1 B GLU A 1 139 ? 1.686   13.364  -12.343 0.500 27.951 ? 139 GLU A OE1 1 ? 8  
ATOM   1086 O  OE2 A GLU A 1 139 ? 1.534   13.489  -11.722 0.500 40.763 ? 139 GLU A OE2 1 ? 8  
ATOM   1087 O  OE2 B GLU A 1 139 ? 2.211   12.075  -10.627 0.500 30.795 ? 139 GLU A OE2 1 ? 8  
ATOM   1088 N  N   . THR A 1 140 ? 3.517   14.515  -16.557 1.000 24.231 ? 140 THR A N   1 ? 8  
ATOM   1089 C  CA  . THR A 1 140 ? 3.309   14.943  -17.965 1.000 23.630 ? 140 THR A CA  1 ? 8  
ATOM   1090 C  C   . THR A 1 140 ? 4.531   14.631  -18.837 1.000 24.351 ? 140 THR A C   1 ? 8  
ATOM   1091 O  O   . THR A 1 140 ? 5.637   15.106  -18.525 1.000 24.975 ? 140 THR A O   1 ? 8  
ATOM   1092 C  CB  . THR A 1 140 ? 2.967   16.436  -18.074 1.000 23.878 ? 140 THR A CB  1 ? 8  
ATOM   1093 O  OG1 . THR A 1 140 ? 1.822   16.681  -17.228 1.000 23.420 ? 140 THR A OG1 1 ? 8  
ATOM   1094 C  CG2 . THR A 1 140 ? 2.698   16.823  -19.503 1.000 23.035 ? 140 THR A CG2 1 ? 8  
ATOM   1095 N  N   . VAL A 1 141 ? 4.353   13.828  -19.857 1.000 22.465 ? 141 VAL A N   1 ? 8  
ATOM   1096 C  CA  . VAL A 1 141 ? 5.460   13.476  -20.811 1.000 22.592 ? 141 VAL A CA  1 ? 8  
ATOM   1097 C  C   . VAL A 1 141 ? 5.395   14.292  -22.068 1.000 22.459 ? 141 VAL A C   1 ? 8  
ATOM   1098 O  O   . VAL A 1 141 ? 6.420   14.372  -22.756 1.000 22.066 ? 141 VAL A O   1 ? 8  
ATOM   1099 C  CB  . VAL A 1 141 ? 5.519   11.968  -21.098 1.000 23.446 ? 141 VAL A CB  1 ? 8  
ATOM   1100 C  CG1 . VAL A 1 141 ? 5.804   11.239  -19.823 1.000 27.637 ? 141 VAL A CG1 1 ? 8  
ATOM   1101 C  CG2 . VAL A 1 141 ? 4.271   11.472  -21.769 1.000 23.841 ? 141 VAL A CG2 1 ? 8  
ATOM   1102 N  N   . ALA A 1 142 ? 4.232   14.819  -22.467 1.000 21.539 ? 142 ALA A N   1 ? 8  
ATOM   1103 C  CA  . ALA A 1 142 ? 4.093   15.535  -23.724 1.000 20.200 ? 142 ALA A CA  1 ? 8  
ATOM   1104 C  C   . ALA A 1 142 ? 2.887   16.456  -23.696 1.000 21.118 ? 142 ALA A C   1 ? 8  
ATOM   1105 O  O   . ALA A 1 142 ? 1.938   16.167  -22.974 1.000 20.918 ? 142 ALA A O   1 ? 8  
ATOM   1106 C  CB  . ALA A 1 142 ? 4.018   14.581  -24.907 1.000 20.581 ? 142 ALA A CB  1 ? 8  
ATOM   1107 N  N   . ILE A 1 143 ? 3.027   17.541  -24.461 1.000 20.848 ? 143 ILE A N   1 ? 8  
ATOM   1108 C  CA  . ILE A 1 143 ? 1.927   18.428  -24.836 1.000 20.128 ? 143 ILE A CA  1 ? 8  
ATOM   1109 C  C   . ILE A 1 143 ? 1.647   18.192  -26.318 1.000 19.109 ? 143 ILE A C   1 ? 8  
ATOM   1110 O  O   . ILE A 1 143 ? 2.587   18.346  -27.148 1.000 19.330 ? 143 ILE A O   1 ? 8  
ATOM   1111 C  CB  . ILE A 1 143 ? 2.298   19.897  -24.535 1.000 21.077 ? 143 ILE A CB  1 ? 8  
ATOM   1112 C  CG1 . ILE A 1 143 ? 2.677   20.038  -23.071 1.000 24.423 ? 143 ILE A CG1 1 ? 8  
ATOM   1113 C  CG2 . ILE A 1 143 ? 1.144   20.778  -24.968 1.000 21.654 ? 143 ILE A CG2 1 ? 8  
ATOM   1114 C  CD1 . ILE A 1 143 ? 3.073   21.444  -22.641 1.000 26.359 ? 143 ILE A CD1 1 ? 8  
ATOM   1115 N  N   . TRP A 1 144 ? 0.427   17.809  -26.613 1.000 18.328 ? 144 TRP A N   1 ? 8  
ATOM   1116 C  CA  . TRP A 1 144 ? -0.013  17.482  -27.990 1.000 19.319 ? 144 TRP A CA  1 ? 8  
ATOM   1117 C  C   . TRP A 1 144 ? -0.757  18.683  -28.560 1.000 19.532 ? 144 TRP A C   1 ? 8  
ATOM   1118 O  O   . TRP A 1 144 ? -1.847  18.983  -28.068 1.000 19.764 ? 144 TRP A O   1 ? 8  
ATOM   1119 C  CB  . TRP A 1 144 ? -0.926  16.260  -27.977 1.000 19.603 ? 144 TRP A CB  1 ? 8  
ATOM   1120 C  CG  . TRP A 1 144 ? -1.241  15.754  -29.356 1.000 18.854 ? 144 TRP A CG  1 ? 8  
ATOM   1121 C  CD1 . TRP A 1 144 ? -2.101  16.291  -30.253 1.000 19.299 ? 144 TRP A CD1 1 ? 8  
ATOM   1122 C  CD2 . TRP A 1 144 ? -0.694  14.580  -29.957 1.000 18.447 ? 144 TRP A CD2 1 ? 8  
ATOM   1123 N  NE1 . TRP A 1 144 ? -2.142  15.492  -31.400 1.000 19.347 ? 144 TRP A NE1 1 ? 8  
ATOM   1124 C  CE2 . TRP A 1 144 ? -1.273  14.454  -31.225 1.000 18.886 ? 144 TRP A CE2 1 ? 8  
ATOM   1125 C  CE3 . TRP A 1 144 ? 0.130   13.580  -29.488 1.000 20.429 ? 144 TRP A CE3 1 ? 8  
ATOM   1126 C  CZ2 . TRP A 1 144 ? -0.937  13.418  -32.085 1.000 19.428 ? 144 TRP A CZ2 1 ? 8  
ATOM   1127 C  CZ3 . TRP A 1 144 ? 0.450   12.536  -30.326 1.000 19.735 ? 144 TRP A CZ3 1 ? 8  
ATOM   1128 C  CH2 . TRP A 1 144 ? -0.074  12.470  -31.599 1.000 19.119 ? 144 TRP A CH2 1 ? 8  
ATOM   1129 N  N   . VAL A 1 145 ? -0.208  19.304  -29.579 1.000 19.465 ? 145 VAL A N   1 ? 8  
ATOM   1130 C  CA  . VAL A 1 145 ? -0.729  20.548  -30.186 1.000 18.640 ? 145 VAL A CA  1 ? 8  
ATOM   1131 C  C   . VAL A 1 145 ? -1.238  20.299  -31.589 1.000 19.113 ? 145 VAL A C   1 ? 8  
ATOM   1132 O  O   . VAL A 1 145 ? -0.529  19.652  -32.370 1.000 20.121 ? 145 VAL A O   1 ? 8  
ATOM   1133 C  CB  . VAL A 1 145 ? 0.393   21.626  -30.251 1.000 20.709 ? 145 VAL A CB  1 ? 8  
ATOM   1134 C  CG1 . VAL A 1 145 ? -0.132  22.912  -30.875 1.000 22.102 ? 145 VAL A CG1 1 ? 8  
ATOM   1135 C  CG2 . VAL A 1 145 ? 0.981   21.874  -28.879 1.000 23.748 ? 145 VAL A CG2 1 ? 8  
ATOM   1136 N  N   . GLU A 1 146 ? -2.468  20.709  -31.873 1.000 17.719 ? 146 GLU A N   1 ? 8  
ATOM   1137 C  CA  . GLU A 1 146 ? -2.889  20.934  -33.279 1.000 18.723 ? 146 GLU A CA  1 ? 8  
ATOM   1138 C  C   . GLU A 1 146 ? -2.933  22.448  -33.435 1.000 18.626 ? 146 GLU A C   1 ? 8  
ATOM   1139 O  O   . GLU A 1 146 ? -3.520  23.135  -32.576 1.000 19.673 ? 146 GLU A O   1 ? 8  
ATOM   1140 C  CB  . GLU A 1 146 ? -4.300  20.410  -33.574 1.000 18.501 ? 146 GLU A CB  1 ? 8  
ATOM   1141 C  CG  . GLU A 1 146 ? -4.436  18.936  -33.717 1.000 20.211 ? 146 GLU A CG  1 ? 8  
ATOM   1142 C  CD  . GLU A 1 146 ? -5.825  18.431  -34.069 1.000 19.360 ? 146 GLU A CD  1 ? 8  
ATOM   1143 O  OE1 . GLU A 1 146 ? -6.628  19.232  -34.567 1.000 19.081 ? 146 GLU A OE1 1 ? 8  
ATOM   1144 O  OE2 . GLU A 1 146 ? -6.063  17.206  -33.926 1.000 20.482 ? 146 GLU A OE2 1 ? 8  
ATOM   1145 N  N   . THR A 1 147 ? -2.459  22.982  -34.552 1.000 18.772 ? 147 THR A N   1 ? 8  
ATOM   1146 C  CA  . THR A 1 147 ? -2.691  24.408  -34.892 1.000 18.598 ? 147 THR A CA  1 ? 8  
ATOM   1147 C  C   . THR A 1 147 ? -2.524  24.554  -36.397 1.000 18.644 ? 147 THR A C   1 ? 8  
ATOM   1148 O  O   . THR A 1 147 ? -1.483  24.168  -36.944 1.000 18.709 ? 147 THR A O   1 ? 8  
ATOM   1149 C  CB  . THR A 1 147 ? -1.760  25.352  -34.088 1.000 19.622 ? 147 THR A CB  1 ? 8  
ATOM   1150 O  OG1 . THR A 1 147 ? -2.116  26.690  -34.394 1.000 19.757 ? 147 THR A OG1 1 ? 8  
ATOM   1151 C  CG2 . THR A 1 147 ? -0.285  25.145  -34.315 1.000 19.369 ? 147 THR A CG2 1 ? 8  
ATOM   1152 N  N   . PRO A 1 148 ? -3.520  25.090  -37.107 1.000 19.468 ? 148 PRO A N   1 ? 8  
ATOM   1153 C  CA  . PRO A 1 148 ? -4.875  25.318  -36.608 1.000 18.921 ? 148 PRO A CA  1 ? 8  
ATOM   1154 C  C   . PRO A 1 148 ? -5.601  24.036  -36.157 1.000 19.711 ? 148 PRO A C   1 ? 8  
ATOM   1155 O  O   . PRO A 1 148 ? -5.317  22.946  -36.677 1.000 18.789 ? 148 PRO A O   1 ? 8  
ATOM   1156 C  CB  . PRO A 1 148 ? -5.605  25.923  -37.817 1.000 20.498 ? 148 PRO A CB  1 ? 8  
ATOM   1157 C  CG  . PRO A 1 148 ? -4.480  26.426  -38.756 1.000 19.382 ? 148 PRO A CG  1 ? 8  
ATOM   1158 C  CD  . PRO A 1 148 ? -3.432  25.374  -38.533 1.000 20.212 ? 148 PRO A CD  1 ? 8  
ATOM   1159 N  N   . THR A 1 149 ? -6.541  24.149  -35.201 1.000 18.295 ? 149 THR A N   1 ? 8  
ATOM   1160 C  CA  . THR A 1 149 ? -7.246  22.959  -34.653 1.000 18.604 ? 149 THR A CA  1 ? 8  
ATOM   1161 C  C   . THR A 1 149 ? -8.287  22.464  -35.640 1.000 17.826 ? 149 THR A C   1 ? 8  
ATOM   1162 O  O   . THR A 1 149 ? -8.849  23.257  -36.417 1.000 18.448 ? 149 THR A O   1 ? 8  
ATOM   1163 C  CB  . THR A 1 149 ? -7.886  23.227  -33.297 1.000 18.988 ? 149 THR A CB  1 ? 8  
ATOM   1164 O  OG1 . THR A 1 149 ? -8.923  24.200  -33.385 1.000 19.389 ? 149 THR A OG1 1 ? 8  
ATOM   1165 C  CG2 . THR A 1 149 ? -6.857  23.633  -32.270 1.000 20.396 ? 149 THR A CG2 1 ? 8  
ATOM   1166 N  N   . ASN A 1 150 ? -8.603  21.180  -35.543 1.000 18.298 ? 150 ASN A N   1 ? 8  
ATOM   1167 C  CA  . ASN A 1 150 ? -9.639  20.537  -36.362 1.000 17.936 ? 150 ASN A CA  1 ? 8  
ATOM   1168 C  C   . ASN A 1 150 ? -10.885 20.366  -35.489 1.000 18.379 ? 150 ASN A C   1 ? 8  
ATOM   1169 O  O   . ASN A 1 150 ? -10.853 19.560  -34.533 1.000 19.707 ? 150 ASN A O   1 ? 8  
ATOM   1170 C  CB  . ASN A 1 150 ? -9.128  19.210  -36.879 1.000 18.079 ? 150 ASN A CB  1 ? 8  
ATOM   1171 C  CG  . ASN A 1 150 ? -10.120 18.474  -37.726 1.000 18.040 ? 150 ASN A CG  1 ? 8  
ATOM   1172 O  OD1 . ASN A 1 150 ? -11.232 18.955  -37.957 1.000 18.974 ? 150 ASN A OD1 1 ? 8  
ATOM   1173 N  ND2 . ASN A 1 150 ? -9.713  17.236  -38.160 1.000 18.935 ? 150 ASN A ND2 1 ? 8  
ATOM   1174 N  N   . PRO A 1 151 ? -12.010 21.087  -35.703 1.000 18.996 ? 151 PRO A N   1 ? 8  
ATOM   1175 C  CA  . PRO A 1 151 ? -12.317 21.856  -36.925 1.000 18.789 ? 151 PRO A CA  1 ? 8  
ATOM   1176 C  C   . PRO A 1 151 ? -12.448 23.382  -36.753 1.000 18.791 ? 151 PRO A C   1 ? 8  
ATOM   1177 O  O   . PRO A 1 151 ? -12.830 24.075  -37.683 1.000 20.138 ? 151 PRO A O   1 ? 8  
ATOM   1178 C  CB  . PRO A 1 151 ? -13.716 21.305  -37.297 1.000 19.718 ? 151 PRO A CB  1 ? 8  
ATOM   1179 C  CG  . PRO A 1 151 ? -14.414 21.197  -35.910 1.000 20.798 ? 151 PRO A CG  1 ? 8  
ATOM   1180 C  CD  . PRO A 1 151 ? -13.274 20.790  -34.981 1.000 20.578 ? 151 PRO A CD  1 ? 8  
ATOM   1181 N  N   . LEU A 1 152 ? -12.258 23.886  -35.531 1.000 19.479 ? 152 LEU A N   1 ? 8  
ATOM   1182 C  CA  . LEU A 1 152 ? -12.510 25.327  -35.269 1.000 19.843 ? 152 LEU A CA  1 ? 8  
ATOM   1183 C  C   . LEU A 1 152 ? -11.389 26.228  -35.811 1.000 20.883 ? 152 LEU A C   1 ? 8  
ATOM   1184 O  O   . LEU A 1 152 ? -11.585 27.498  -35.815 1.000 20.934 ? 152 LEU A O   1 ? 8  
ATOM   1185 C  CB  . LEU A 1 152 ? -12.692 25.551  -33.766 1.000 20.703 ? 152 LEU A CB  1 ? 8  
ATOM   1186 C  CG  . LEU A 1 152 ? -13.876 24.807  -33.133 1.000 22.853 ? 152 LEU A CG  1 ? 8  
ATOM   1187 C  CD1 . LEU A 1 152 ? -13.922 25.044  -31.631 1.000 23.325 ? 152 LEU A CD1 1 ? 8  
ATOM   1188 C  CD2 . LEU A 1 152 ? -15.195 25.166  -33.811 1.000 24.919 ? 152 LEU A CD2 1 ? 8  
ATOM   1189 N  N   . LEU A 1 153 ? -10.235 25.675  -36.146 1.000 20.338 ? 153 LEU A N   1 ? 8  
ATOM   1190 C  CA  . LEU A 1 153 ? -9.082  26.451  -36.650 1.000 20.514 ? 153 LEU A CA  1 ? 8  
ATOM   1191 C  C   . LEU A 1 153 ? -8.581  27.431  -35.605 1.000 22.064 ? 153 LEU A C   1 ? 8  
ATOM   1192 O  O   . LEU A 1 153 ? -8.082  28.525  -35.963 1.000 21.751 ? 153 LEU A O   1 ? 8  
ATOM   1193 C  CB  . LEU A 1 153 ? -9.470  27.148  -37.943 1.000 20.479 ? 153 LEU A CB  1 ? 8  
ATOM   1194 C  CG  . LEU A 1 153 ? -10.099 26.211  -38.979 1.000 20.786 ? 153 LEU A CG  1 ? 8  
ATOM   1195 C  CD1 . LEU A 1 153 ? -10.556 26.966  -40.187 1.000 21.270 ? 153 LEU A CD1 1 ? 8  
ATOM   1196 C  CD2 . LEU A 1 153 ? -9.173  25.039  -39.377 1.000 21.254 ? 153 LEU A CD2 1 ? 8  
ATOM   1197 N  N   . ASN A 1 154 ? -8.582  27.015  -34.334 1.000 20.932 ? 154 ASN A N   1 ? 8  
ATOM   1198 C  CA  . ASN A 1 154 ? -7.933  27.817  -33.278 1.000 22.061 ? 154 ASN A CA  1 ? 8  
ATOM   1199 C  C   . ASN A 1 154 ? -6.430  27.676  -33.407 1.000 21.118 ? 154 ASN A C   1 ? 8  
ATOM   1200 O  O   . ASN A 1 154 ? -5.931  26.684  -33.916 1.000 20.259 ? 154 ASN A O   1 ? 8  
ATOM   1201 C  CB  . ASN A 1 154 ? -8.471  27.474  -31.899 1.000 21.598 ? 154 ASN A CB  1 ? 8  
ATOM   1202 C  CG  . ASN A 1 154 ? -9.908  27.968  -31.732 1.000 23.833 ? 154 ASN A CG  1 ? 8  
ATOM   1203 O  OD1 . ASN A 1 154 ? -10.253 29.019  -32.279 1.000 24.738 ? 154 ASN A OD1 1 ? 8  
ATOM   1204 N  ND2 . ASN A 1 154 ? -10.758 27.260  -30.991 1.000 23.701 ? 154 ASN A ND2 1 ? 8  
ATOM   1205 N  N   . ILE A 1 155 ? -5.732  28.678  -32.904 1.000 21.009 ? 155 ILE A N   1 ? 8  
ATOM   1206 C  CA  . ILE A 1 155 ? -4.278  28.869  -33.081 1.000 21.097 ? 155 ILE A CA  1 ? 8  
ATOM   1207 C  C   . ILE A 1 155 ? -3.552  28.762  -31.741 1.000 20.998 ? 155 ILE A C   1 ? 8  
ATOM   1208 O  O   . ILE A 1 155 ? -3.982  29.379  -30.725 1.000 22.436 ? 155 ILE A O   1 ? 8  
ATOM   1209 C  CB  . ILE A 1 155 ? -4.017  30.201  -33.772 1.000 20.797 ? 155 ILE A CB  1 ? 8  
ATOM   1210 C  CG1 . ILE A 1 155 ? -4.800  30.333  -35.089 1.000 22.058 ? 155 ILE A CG1 1 ? 8  
ATOM   1211 C  CG2 . ILE A 1 155 ? -2.550  30.379  -33.948 1.000 22.220 ? 155 ILE A CG2 1 ? 8  
ATOM   1212 C  CD1 . ILE A 1 155 ? -4.386  29.337  -36.167 1.000 22.338 ? 155 ILE A CD1 1 ? 8  
ATOM   1213 N  N   . ALA A 1 156 ? -2.426  28.054  -31.749 1.000 21.110 ? 156 ALA A N   1 ? 8  
ATOM   1214 C  CA  . ALA A 1 156 ? -1.551  27.856  -30.589 1.000 21.149 ? 156 ALA A CA  1 ? 8  
ATOM   1215 C  C   . ALA A 1 156 ? -0.173  28.393  -30.978 1.000 20.606 ? 156 ALA A C   1 ? 8  
ATOM   1216 O  O   . ALA A 1 156 ? 0.331   28.053  -32.069 1.000 22.296 ? 156 ALA A O   1 ? 8  
ATOM   1217 C  CB  . ALA A 1 156 ? -1.424  26.417  -30.236 1.000 22.362 ? 156 ALA A CB  1 ? 8  
ATOM   1218 N  N   . ASP A 1 157 ? 0.435   29.103  -30.070 1.000 21.441 ? 157 ASP A N   1 ? 8  
ATOM   1219 C  CA  . ASP A 1 157 ? 1.797   29.681  -30.274 1.000 21.850 ? 157 ASP A CA  1 ? 8  
ATOM   1220 C  C   . ASP A 1 157 ? 2.842   28.581  -29.994 1.000 20.761 ? 157 ASP A C   1 ? 8  
ATOM   1221 O  O   . ASP A 1 157 ? 3.152   28.309  -28.873 1.000 21.484 ? 157 ASP A O   1 ? 8  
ATOM   1222 C  CB  . ASP A 1 157 ? 1.969   30.881  -29.379 1.000 23.541 ? 157 ASP A CB  1 ? 8  
ATOM   1223 C  CG  . ASP A 1 157 ? 3.262   31.661  -29.545 1.000 25.880 ? 157 ASP A CG  1 ? 8  
ATOM   1224 O  OD1 . ASP A 1 157 ? 4.247   31.077  -29.963 1.000 25.119 ? 157 ASP A OD1 1 ? 8  
ATOM   1225 O  OD2 . ASP A 1 157 ? 3.255   32.853  -29.149 1.000 27.828 ? 157 ASP A OD2 1 ? 8  
ATOM   1226 N  N   . ILE A 1 158 ? 3.341   27.979  -31.057 1.000 20.086 ? 158 ILE A N   1 ? 8  
ATOM   1227 C  CA  . ILE A 1 158 ? 4.239   26.804  -30.976 1.000 20.024 ? 158 ILE A CA  1 ? 8  
ATOM   1228 C  C   . ILE A 1 158 ? 5.460   27.178  -30.127 1.000 20.957 ? 158 ILE A C   1 ? 8  
ATOM   1229 O  O   . ILE A 1 158 ? 5.828   26.409  -29.259 1.000 21.035 ? 158 ILE A O   1 ? 8  
ATOM   1230 C  CB  . ILE A 1 158 ? 4.592   26.292  -32.372 1.000 20.158 ? 158 ILE A CB  1 ? 8  
ATOM   1231 C  CG1 . ILE A 1 158 ? 3.331   25.817  -33.099 1.000 20.491 ? 158 ILE A CG1 1 ? 8  
ATOM   1232 C  CG2 . ILE A 1 158 ? 5.658   25.196  -32.264 1.000 20.647 ? 158 ILE A CG2 1 ? 8  
ATOM   1233 C  CD1 . ILE A 1 158 ? 3.532   25.620  -34.643 1.000 21.384 ? 158 ILE A CD1 1 ? 8  
ATOM   1234 N  N   . ALA A 1 159 ? 6.111   28.289  -30.444 1.000 22.863 ? 159 ALA A N   1 ? 8  
ATOM   1235 C  CA  . ALA A 1 159 ? 7.364   28.684  -29.756 1.000 22.792 ? 159 ALA A CA  1 ? 8  
ATOM   1236 C  C   . ALA A 1 159 ? 7.066   28.849  -28.263 1.000 22.986 ? 159 ALA A C   1 ? 8  
ATOM   1237 O  O   . ALA A 1 159 ? 7.864   28.415  -27.411 1.000 22.531 ? 159 ALA A O   1 ? 8  
ATOM   1238 C  CB  . ALA A 1 159 ? 7.988   29.921  -30.333 1.000 24.861 ? 159 ALA A CB  1 ? 8  
ATOM   1239 N  N   . ALA A 1 160 ? 5.937   29.484  -27.905 1.000 22.331 ? 160 ALA A N   1 ? 8  
ATOM   1240 C  CA  . ALA A 1 160 ? 5.583   29.667  -26.506 1.000 23.054 ? 160 ALA A CA  1 ? 8  
ATOM   1241 C  C   . ALA A 1 160 ? 5.371   28.320  -25.823 1.000 22.715 ? 160 ALA A C   1 ? 8  
ATOM   1242 O  O   . ALA A 1 160 ? 5.778   28.147  -24.659 1.000 23.097 ? 160 ALA A O   1 ? 8  
ATOM   1243 C  CB  . ALA A 1 160 ? 4.382   30.592  -26.388 1.000 22.128 ? 160 ALA A CB  1 ? 8  
ATOM   1244 N  N   . LEU A 1 161 ? 4.629   27.416  -26.454 1.000 21.705 ? 161 LEU A N   1 ? 8  
ATOM   1245 C  CA  . LEU A 1 161 ? 4.291   26.134  -25.809 1.000 21.866 ? 161 LEU A CA  1 ? 8  
ATOM   1246 C  C   . LEU A 1 161 ? 5.546   25.255  -25.746 1.000 22.249 ? 161 LEU A C   1 ? 8  
ATOM   1247 O  O   . LEU A 1 161 ? 5.662   24.451  -24.822 1.000 22.707 ? 161 LEU A O   1 ? 8  
ATOM   1248 C  CB  . LEU A 1 161 ? 3.166   25.436  -26.583 1.000 21.197 ? 161 LEU A CB  1 ? 8  
ATOM   1249 C  CG  . LEU A 1 161 ? 1.832   26.200  -26.598 1.000 23.486 ? 161 LEU A CG  1 ? 8  
ATOM   1250 C  CD1 . LEU A 1 161 ? 0.734   25.363  -27.215 1.000 25.299 ? 161 LEU A CD1 1 ? 8  
ATOM   1251 C  CD2 . LEU A 1 161 ? 1.428   26.708  -25.242 1.000 26.639 ? 161 LEU A CD2 1 ? 8  
ATOM   1252 N  N   . ALA A 1 162 ? 6.475   25.404  -26.692 1.000 22.339 ? 162 ALA A N   1 ? 8  
ATOM   1253 C  CA  . ALA A 1 162 ? 7.753   24.658  -26.646 1.000 22.608 ? 162 ALA A CA  1 ? 8  
ATOM   1254 C  C   . ALA A 1 162 ? 8.475   25.030  -25.368 1.000 22.784 ? 162 ALA A C   1 ? 8  
ATOM   1255 O  O   . ALA A 1 162 ? 8.979   24.144  -24.665 1.000 21.939 ? 162 ALA A O   1 ? 8  
ATOM   1256 C  CB  . ALA A 1 162 ? 8.618   24.914  -27.864 1.000 23.243 ? 162 ALA A CB  1 ? 8  
ATOM   1257 N  N   . ASP A 1 163 ? 8.552   26.312  -25.052 1.000 22.426 ? 163 ASP A N   1 ? 8  
ATOM   1258 C  CA  . ASP A 1 163 ? 9.246   26.718  -23.823 1.000 24.029 ? 163 ASP A CA  1 ? 8  
ATOM   1259 C  C   . ASP A 1 163 ? 8.560   26.146  -22.585 1.000 22.662 ? 163 ASP A C   1 ? 8  
ATOM   1260 O  O   . ASP A 1 163 ? 9.229   25.812  -21.626 1.000 23.767 ? 163 ASP A O   1 ? 8  
ATOM   1261 C  CB  . ASP A 1 163 ? 9.383   28.235  -23.721 1.000 26.436 ? 163 ASP A CB  1 ? 8  
ATOM   1262 C  CG  . ASP A 1 163 ? 10.363  28.818  -24.743 1.000 31.083 ? 163 ASP A CG  1 ? 8  
ATOM   1263 O  OD1 . ASP A 1 163 ? 11.109  28.040  -25.426 1.000 32.356 ? 163 ASP A OD1 1 ? 8  
ATOM   1264 O  OD2 . ASP A 1 163 ? 10.317  30.055  -24.900 1.000 35.983 ? 163 ASP A OD2 1 ? 8  
ATOM   1265 N  N   . ILE A 1 164 ? 7.232   26.124  -22.532 1.000 21.724 ? 164 ILE A N   1 ? 8  
ATOM   1266 C  CA  . ILE A 1 164 ? 6.495   25.552  -21.388 1.000 22.741 ? 164 ILE A CA  1 ? 8  
ATOM   1267 C  C   . ILE A 1 164 ? 6.792   24.037  -21.282 1.000 22.051 ? 164 ILE A C   1 ? 8  
ATOM   1268 O  O   . ILE A 1 164 ? 7.105   23.547  -20.190 1.000 23.208 ? 164 ILE A O   1 ? 8  
ATOM   1269 C  CB  . ILE A 1 164 ? 4.979   25.809  -21.563 1.000 22.677 ? 164 ILE A CB  1 ? 8  
ATOM   1270 C  CG1 . ILE A 1 164 ? 4.713   27.307  -21.432 1.000 23.957 ? 164 ILE A CG1 1 ? 8  
ATOM   1271 C  CG2 . ILE A 1 164 ? 4.193   24.964  -20.580 1.000 24.472 ? 164 ILE A CG2 1 ? 8  
ATOM   1272 C  CD1 . ILE A 1 164 ? 3.327   27.715  -21.922 1.000 25.735 ? 164 ILE A CD1 1 ? 8  
ATOM   1273 N  N   . ALA A 1 165 ? 6.703   23.324  -22.383 1.000 21.791 ? 165 ALA A N   1 ? 8  
ATOM   1274 C  CA  . ALA A 1 165 ? 6.972   21.866  -22.396 1.000 21.428 ? 165 ALA A CA  1 ? 8  
ATOM   1275 C  C   . ALA A 1 165 ? 8.393   21.623  -21.887 1.000 22.083 ? 165 ALA A C   1 ? 8  
ATOM   1276 O  O   . ALA A 1 165 ? 8.594   20.754  -21.012 1.000 22.881 ? 165 ALA A O   1 ? 8  
ATOM   1277 C  CB  . ALA A 1 165 ? 6.774   21.292  -23.785 1.000 22.375 ? 165 ALA A CB  1 ? 8  
ATOM   1278 N  N   . HIS A 1 166 ? 9.369   22.347  -22.432 1.000 22.024 ? 166 HIS A N   1 ? 8  
ATOM   1279 C  CA  . HIS A 1 166 ? 10.782  22.046  -22.166 1.000 22.815 ? 166 HIS A CA  1 ? 8  
ATOM   1280 C  C   . HIS A 1 166 ? 11.126  22.383  -20.702 1.000 24.771 ? 166 HIS A C   1 ? 8  
ATOM   1281 O  O   . HIS A 1 166 ? 11.961  21.712  -20.103 1.000 24.726 ? 166 HIS A O   1 ? 8  
ATOM   1282 C  CB  . HIS A 1 166 ? 11.674  22.755  -23.169 1.000 23.746 ? 166 HIS A CB  1 ? 8  
ATOM   1283 C  CG  . HIS A 1 166 ? 11.467  22.218  -24.547 1.000 23.280 ? 166 HIS A CG  1 ? 8  
ATOM   1284 N  ND1 . HIS A 1 166 ? 11.750  22.934  -25.707 1.000 23.572 ? 166 HIS A ND1 1 ? 8  
ATOM   1285 C  CD2 . HIS A 1 166 ? 10.916  21.023  -24.960 1.000 24.221 ? 166 HIS A CD2 1 ? 8  
ATOM   1286 C  CE1 . HIS A 1 166 ? 11.400  22.203  -26.744 1.000 23.671 ? 166 HIS A CE1 1 ? 8  
ATOM   1287 N  NE2 . HIS A 1 166 ? 10.870  21.037  -26.322 1.000 23.139 ? 166 HIS A NE2 1 ? 8  
ATOM   1288 N  N   . ALA A 1 167 ? 10.530  23.427  -20.176 1.000 24.574 ? 167 ALA A N   1 ? 8  
ATOM   1289 C  CA  . ALA A 1 167 ? 10.744  23.786  -18.759 1.000 26.168 ? 167 ALA A CA  1 ? 8  
ATOM   1290 C  C   . ALA A 1 167 ? 10.289  22.616  -17.900 1.000 26.431 ? 167 ALA A C   1 ? 8  
ATOM   1291 O  O   . ALA A 1 167 ? 10.804  22.518  -16.771 1.000 27.851 ? 167 ALA A O   1 ? 8  
ATOM   1292 C  CB  . ALA A 1 167 ? 10.021  25.072  -18.391 1.000 25.812 ? 167 ALA A CB  1 ? 8  
ATOM   1293 N  N   . ALA A 1 168 ? 9.261   21.871  -18.286 1.000 25.731 ? 168 ALA A N   1 ? 8  
ATOM   1294 C  CA  . ALA A 1 168 ? 8.756   20.706  -17.537 1.000 27.369 ? 168 ALA A CA  1 ? 8  
ATOM   1295 C  C   . ALA A 1 168 ? 9.448   19.375  -17.937 1.000 27.495 ? 168 ALA A C   1 ? 8  
ATOM   1296 O  O   . ALA A 1 168 ? 8.936   18.335  -17.558 1.000 29.176 ? 168 ALA A O   1 ? 8  
ATOM   1297 C  CB  . ALA A 1 168 ? 7.262   20.578  -17.775 1.000 28.085 ? 168 ALA A CB  1 ? 8  
ATOM   1298 N  N   A ASP A 1 169 ? 10.485  19.423  -18.771 0.500 27.445 ? 169 ASP A N   1 ? 8  
ATOM   1299 N  N   B ASP A 1 169 ? 10.512  19.424  -18.740 0.500 27.350 ? 169 ASP A N   1 ? 8  
ATOM   1300 C  CA  A ASP A 1 169 ? 11.156  18.200  -19.276 0.500 29.101 ? 169 ASP A CA  1 ? 8  
ATOM   1301 C  CA  B ASP A 1 169 ? 11.147  18.205  -19.308 0.500 28.939 ? 169 ASP A CA  1 ? 8  
ATOM   1302 C  C   A ASP A 1 169 ? 10.131  17.334  -20.042 0.500 26.628 ? 169 ASP A C   1 ? 8  
ATOM   1303 C  C   B ASP A 1 169 ? 10.075  17.333  -19.972 0.500 26.490 ? 169 ASP A C   1 ? 8  
ATOM   1304 O  O   A ASP A 1 169 ? 10.299  16.100  -20.040 0.500 28.156 ? 169 ASP A O   1 ? 8  
ATOM   1305 O  O   B ASP A 1 169 ? 10.122  16.099  -19.761 0.500 28.078 ? 169 ASP A O   1 ? 8  
ATOM   1306 C  CB  A ASP A 1 169 ? 11.773  17.467  -18.086 0.500 31.057 ? 169 ASP A CB  1 ? 8  
ATOM   1307 C  CB  B ASP A 1 169 ? 11.848  17.438  -18.194 0.500 30.905 ? 169 ASP A CB  1 ? 8  
ATOM   1308 C  CG  A ASP A 1 169 ? 12.757  16.390  -18.492 0.500 34.751 ? 169 ASP A CG  1 ? 8  
ATOM   1309 C  CG  B ASP A 1 169 ? 13.046  18.182  -17.672 0.500 34.697 ? 169 ASP A CG  1 ? 8  
ATOM   1310 O  OD1 A ASP A 1 169 ? 13.382  16.554  -19.558 0.500 36.530 ? 169 ASP A OD1 1 ? 8  
ATOM   1311 O  OD1 B ASP A 1 169 ? 13.823  18.673  -18.498 0.500 36.912 ? 169 ASP A OD1 1 ? 8  
ATOM   1312 O  OD2 A ASP A 1 169 ? 12.863  15.389  -17.763 0.500 36.505 ? 169 ASP A OD2 1 ? 8  
ATOM   1313 O  OD2 B ASP A 1 169 ? 13.128  18.335  -16.468 0.500 39.094 ? 169 ASP A OD2 1 ? 8  
ATOM   1314 N  N   . ALA A 1 170 ? 9.163   17.960  -20.730 1.000 24.752 ? 170 ALA A N   1 ? 8  
ATOM   1315 C  CA  . ALA A 1 170 ? 8.163   17.272  -21.549 1.000 23.313 ? 170 ALA A CA  1 ? 8  
ATOM   1316 C  C   . ALA A 1 170 ? 8.455   17.508  -23.033 1.000 23.790 ? 170 ALA A C   1 ? 8  
ATOM   1317 O  O   . ALA A 1 170 ? 9.169   18.468  -23.369 1.000 23.159 ? 170 ALA A O   1 ? 8  
ATOM   1318 C  CB  . ALA A 1 170 ? 6.797   17.692  -21.196 1.000 22.959 ? 170 ALA A CB  1 ? 8  
ATOM   1319 N  N   . LEU A 1 171 ? 7.934   16.652  -23.900 1.000 21.085 ? 171 LEU A N   1 ? 8  
ATOM   1320 C  CA  . LEU A 1 171 ? 8.083   16.889  -25.348 1.000 20.654 ? 171 LEU A CA  1 ? 8  
ATOM   1321 C  C   . LEU A 1 171 ? 6.939   17.740  -25.874 1.000 21.356 ? 171 LEU A C   1 ? 8  
ATOM   1322 O  O   . LEU A 1 171 ? 5.841   17.670  -25.308 1.000 21.924 ? 171 LEU A O   1 ? 8  
ATOM   1323 C  CB  . LEU A 1 171 ? 8.074   15.563  -26.075 1.000 21.577 ? 171 LEU A CB  1 ? 8  
ATOM   1324 C  CG  . LEU A 1 171 ? 9.207   14.632  -25.724 1.000 22.704 ? 171 LEU A CG  1 ? 8  
ATOM   1325 C  CD1 . LEU A 1 171 ? 8.986   13.245  -26.336 1.000 25.758 ? 171 LEU A CD1 1 ? 8  
ATOM   1326 C  CD2 . LEU A 1 171 ? 10.521  15.227  -26.170 1.000 24.537 ? 171 LEU A CD2 1 ? 8  
ATOM   1327 N  N   . LEU A 1 172 ? 7.212   18.599  -26.861 1.000 19.567 ? 172 LEU A N   1 ? 8  
ATOM   1328 C  CA  . LEU A 1 172 ? 6.157   19.276  -27.612 1.000 19.127 ? 172 LEU A CA  1 ? 8  
ATOM   1329 C  C   . LEU A 1 172 ? 5.932   18.532  -28.913 1.000 18.627 ? 172 LEU A C   1 ? 8  
ATOM   1330 O  O   . LEU A 1 172 ? 6.861   18.420  -29.747 1.000 18.843 ? 172 LEU A O   1 ? 8  
ATOM   1331 C  CB  . LEU A 1 172 ? 6.476   20.751  -27.880 1.000 20.521 ? 172 LEU A CB  1 ? 8  
ATOM   1332 C  CG  . LEU A 1 172 ? 5.269   21.485  -28.459 1.000 23.386 ? 172 LEU A CG  1 ? 8  
ATOM   1333 C  CD1 . LEU A 1 172 ? 4.291   21.795  -27.319 1.000 27.018 ? 172 LEU A CD1 1 ? 8  
ATOM   1334 C  CD2 . LEU A 1 172 ? 5.686   22.767  -29.113 1.000 25.174 ? 172 LEU A CD2 1 ? 8  
ATOM   1335 N  N   . VAL A 1 173 ? 4.722   18.006  -29.085 1.000 18.732 ? 173 VAL A N   1 ? 8  
ATOM   1336 C  CA  . VAL A 1 173 ? 4.278   17.327  -30.320 1.000 17.038 ? 173 VAL A CA  1 ? 8  
ATOM   1337 C  C   . VAL A 1 173 ? 3.357   18.284  -31.066 1.000 17.413 ? 173 VAL A C   1 ? 8  
ATOM   1338 O  O   . VAL A 1 173 ? 2.417   18.781  -30.455 1.000 18.014 ? 173 VAL A O   1 ? 8  
ATOM   1339 C  CB  . VAL A 1 173 ? 3.514   16.033  -30.032 1.000 17.859 ? 173 VAL A CB  1 ? 8  
ATOM   1340 C  CG1 . VAL A 1 173 ? 3.000   15.395  -31.328 1.000 18.436 ? 173 VAL A CG1 1 ? 8  
ATOM   1341 C  CG2 . VAL A 1 173 ? 4.343   15.084  -29.225 1.000 19.013 ? 173 VAL A CG2 1 ? 8  
ATOM   1342 N  N   . VAL A 1 174 ? 3.613   18.551  -32.352 1.000 17.373 ? 174 VAL A N   1 ? 8  
ATOM   1343 C  CA  . VAL A 1 174 ? 2.706   19.381  -33.158 1.000 17.540 ? 174 VAL A CA  1 ? 8  
ATOM   1344 C  C   . VAL A 1 174 ? 2.214   18.550  -34.327 1.000 16.241 ? 174 VAL A C   1 ? 8  
ATOM   1345 O  O   . VAL A 1 174 ? 3.019   18.106  -35.169 1.000 17.078 ? 174 VAL A O   1 ? 8  
ATOM   1346 C  CB  . VAL A 1 174 ? 3.355   20.690  -33.640 1.000 17.939 ? 174 VAL A CB  1 ? 8  
ATOM   1347 C  CG1 . VAL A 1 174 ? 2.377   21.462  -34.472 1.000 19.112 ? 174 VAL A CG1 1 ? 8  
ATOM   1348 C  CG2 . VAL A 1 174 ? 3.902   21.541  -32.438 1.000 18.837 ? 174 VAL A CG2 1 ? 8  
ATOM   1349 N  N   . ASP A 1 175 ? 0.916   18.359  -34.355 1.000 17.263 ? 175 ASP A N   1 ? 8  
ATOM   1350 C  CA  . ASP A 1 175 ? 0.199   17.774  -35.494 1.000 17.125 ? 175 ASP A CA  1 ? 8  
ATOM   1351 C  C   . ASP A 1 175 ? 0.034   18.895  -36.513 1.000 17.181 ? 175 ASP A C   1 ? 8  
ATOM   1352 O  O   . ASP A 1 175 ? -0.769  19.828  -36.283 1.000 18.161 ? 175 ASP A O   1 ? 8  
ATOM   1353 C  CB  . ASP A 1 175 ? -1.109  17.140  -35.044 1.000 18.659 ? 175 ASP A CB  1 ? 8  
ATOM   1354 C  CG  . ASP A 1 175 ? -1.860  16.454  -36.169 1.000 17.455 ? 175 ASP A CG  1 ? 8  
ATOM   1355 O  OD1 . ASP A 1 175 ? -1.668  16.834  -37.330 1.000 18.261 ? 175 ASP A OD1 1 ? 8  
ATOM   1356 O  OD2 . ASP A 1 175 ? -2.698  15.537  -35.821 1.000 18.327 ? 175 ASP A OD2 1 ? 8  
ATOM   1357 N  N   . ASN A 1 176 ? 0.875   18.830  -37.555 1.000 16.938 ? 176 ASN A N   1 ? 8  
ATOM   1358 C  CA  . ASN A 1 176 ? 0.999   19.907  -38.563 1.000 16.062 ? 176 ASN A CA  1 ? 8  
ATOM   1359 C  C   . ASN A 1 176 ? 0.215   19.528  -39.823 1.000 16.615 ? 176 ASN A C   1 ? 8  
ATOM   1360 O  O   . ASN A 1 176 ? 0.486   20.076  -40.910 1.000 17.281 ? 176 ASN A O   1 ? 8  
ATOM   1361 C  CB  . ASN A 1 176 ? 2.468   20.106  -38.900 1.000 15.959 ? 176 ASN A CB  1 ? 8  
ATOM   1362 C  CG  . ASN A 1 176 ? 2.795   21.418  -39.553 1.000 17.479 ? 176 ASN A CG  1 ? 8  
ATOM   1363 O  OD1 . ASN A 1 176 ? 2.165   22.428  -39.217 1.000 18.835 ? 176 ASN A OD1 1 ? 8  
ATOM   1364 N  ND2 . ASN A 1 176 ? 3.763   21.389  -40.474 1.000 16.924 ? 176 ASN A ND2 1 ? 8  
ATOM   1365 N  N   . THR A 1 177 ? -0.758  18.646  -39.699 1.000 16.420 ? 177 THR A N   1 ? 8  
ATOM   1366 C  CA  . THR A 1 177 ? -1.574  18.146  -40.813 1.000 16.350 ? 177 THR A CA  1 ? 8  
ATOM   1367 C  C   . THR A 1 177 ? -2.246  19.291  -41.584 1.000 17.322 ? 177 THR A C   1 ? 8  
ATOM   1368 O  O   . THR A 1 177 ? -2.072  19.369  -42.833 1.000 17.392 ? 177 THR A O   1 ? 8  
ATOM   1369 C  CB  . THR A 1 177 ? -2.640  17.163  -40.333 1.000 16.510 ? 177 THR A CB  1 ? 8  
ATOM   1370 O  OG1 . THR A 1 177 ? -2.000  16.015  -39.755 1.000 16.390 ? 177 THR A OG1 1 ? 8  
ATOM   1371 C  CG2 . THR A 1 177 ? -3.577  16.724  -41.434 1.000 17.169 ? 177 THR A CG2 1 ? 8  
ATOM   1372 N  N   . PHE A 1 178 ? -2.958  20.182  -40.905 1.000 16.515 ? 178 PHE A N   1 ? 8  
ATOM   1373 C  CA  . PHE A 1 178 ? -3.768  21.234  -41.578 1.000 17.659 ? 178 PHE A CA  1 ? 8  
ATOM   1374 C  C   . PHE A 1 178 ? -2.846  22.236  -42.261 1.000 18.506 ? 178 PHE A C   1 ? 8  
ATOM   1375 O  O   . PHE A 1 178 ? -3.165  22.683  -43.365 1.000 19.663 ? 178 PHE A O   1 ? 8  
ATOM   1376 C  CB  . PHE A 1 178 ? -4.685  21.906  -40.567 1.000 18.601 ? 178 PHE A CB  1 ? 8  
ATOM   1377 C  CG  . PHE A 1 178 ? -6.022  21.224  -40.357 1.000 17.893 ? 178 PHE A CG  1 ? 8  
ATOM   1378 C  CD1 . PHE A 1 178 ? -6.165  19.850  -40.365 1.000 17.510 ? 178 PHE A CD1 1 ? 8  
ATOM   1379 C  CD2 . PHE A 1 178 ? -7.105  21.997  -40.095 1.000 18.346 ? 178 PHE A CD2 1 ? 8  
ATOM   1380 C  CE1 . PHE A 1 178 ? -7.430  19.267  -40.204 1.000 18.699 ? 178 PHE A CE1 1 ? 8  
ATOM   1381 C  CE2 . PHE A 1 178 ? -8.377  21.453  -39.968 1.000 19.832 ? 178 PHE A CE2 1 ? 8  
ATOM   1382 C  CZ  . PHE A 1 178 ? -8.533  20.074  -40.019 1.000 18.846 ? 178 PHE A CZ  1 ? 8  
ATOM   1383 N  N   . ALA A 1 179 ? -1.758  22.649  -41.633 1.000 17.619 ? 179 ALA A N   1 ? 8  
ATOM   1384 C  CA  . ALA A 1 179 ? -0.916  23.689  -42.221 1.000 17.903 ? 179 ALA A CA  1 ? 8  
ATOM   1385 C  C   . ALA A 1 179 ? -0.026  23.137  -43.327 1.000 17.489 ? 179 ALA A C   1 ? 8  
ATOM   1386 O  O   . ALA A 1 179 ? 0.230   23.815  -44.315 1.000 18.284 ? 179 ALA A O   1 ? 8  
ATOM   1387 C  CB  . ALA A 1 179 ? -0.075  24.319  -41.130 1.000 18.032 ? 179 ALA A CB  1 ? 8  
ATOM   1388 N  N   . SER A 1 180 ? 0.504   21.926  -43.105 1.000 17.084 ? 180 SER A N   1 ? 8  
ATOM   1389 C  CA  . SER A 1 180 ? 1.559   21.318  -43.916 1.000 17.404 ? 180 SER A CA  1 ? 8  
ATOM   1390 C  C   . SER A 1 180 ? 2.888   22.039  -43.706 1.000 17.694 ? 180 SER A C   1 ? 8  
ATOM   1391 O  O   . SER A 1 180 ? 2.965   23.194  -43.268 1.000 17.109 ? 180 SER A O   1 ? 8  
ATOM   1392 C  CB  . SER A 1 180 ? 1.203   21.306  -45.450 1.000 17.386 ? 180 SER A CB  1 ? 8  
ATOM   1393 O  OG  . SER A 1 180 ? 1.644   22.503  -46.085 1.000 17.780 ? 180 SER A OG  1 ? 8  
ATOM   1394 N  N   . PRO A 1 181 ? 4.000   21.381  -44.090 1.000 18.157 ? 181 PRO A N   1 ? 8  
ATOM   1395 C  CA  . PRO A 1 181 ? 5.328   21.969  -43.946 1.000 18.528 ? 181 PRO A CA  1 ? 8  
ATOM   1396 C  C   . PRO A 1 181 ? 5.508   23.190  -44.808 1.000 19.005 ? 181 PRO A C   1 ? 8  
ATOM   1397 O  O   . PRO A 1 181 ? 6.409   24.009  -44.542 1.000 18.935 ? 181 PRO A O   1 ? 8  
ATOM   1398 C  CB  . PRO A 1 181 ? 6.301   20.916  -44.404 1.000 19.293 ? 181 PRO A CB  1 ? 8  
ATOM   1399 C  CG  . PRO A 1 181 ? 5.504   19.687  -44.566 1.000 22.192 ? 181 PRO A CG  1 ? 8  
ATOM   1400 C  CD  . PRO A 1 181 ? 4.046   19.986  -44.542 1.000 19.768 ? 181 PRO A CD  1 ? 8  
ATOM   1401 N  N   . TYR A 1 182 ? 4.661   23.341  -45.851 1.000 18.302 ? 182 TYR A N   1 ? 8  
ATOM   1402 C  CA  . TYR A 1 182 ? 4.755   24.540  -46.720 1.000 18.423 ? 182 TYR A CA  1 ? 8  
ATOM   1403 C  C   . TYR A 1 182 ? 4.334   25.777  -45.950 1.000 19.318 ? 182 TYR A C   1 ? 8  
ATOM   1404 O  O   . TYR A 1 182 ? 4.850   26.858  -46.296 1.000 19.812 ? 182 TYR A O   1 ? 8  
ATOM   1405 C  CB  . TYR A 1 182 ? 3.960   24.303  -47.998 1.000 18.090 ? 182 TYR A CB  1 ? 8  
ATOM   1406 C  CG  . TYR A 1 182 ? 4.007   25.433  -48.980 1.000 18.607 ? 182 TYR A CG  1 ? 8  
ATOM   1407 C  CD1 . TYR A 1 182 ? 5.159   25.751  -49.650 1.000 19.815 ? 182 TYR A CD1 1 ? 8  
ATOM   1408 C  CD2 . TYR A 1 182 ? 2.886   26.226  -49.187 1.000 18.715 ? 182 TYR A CD2 1 ? 8  
ATOM   1409 C  CE1 . TYR A 1 182 ? 5.195   26.769  -50.585 1.000 19.737 ? 182 TYR A CE1 1 ? 8  
ATOM   1410 C  CE2 . TYR A 1 182 ? 2.910   27.242  -50.097 1.000 19.345 ? 182 TYR A CE2 1 ? 8  
ATOM   1411 C  CZ  . TYR A 1 182 ? 4.052   27.517  -50.817 1.000 19.518 ? 182 TYR A CZ  1 ? 8  
ATOM   1412 O  OH  . TYR A 1 182 ? 4.087   28.526  -51.742 1.000 21.309 ? 182 TYR A OH  1 ? 8  
ATOM   1413 N  N   . LEU A 1 183 ? 3.381   25.672  -45.054 1.000 18.309 ? 183 LEU A N   1 ? 8  
ATOM   1414 C  CA  . LEU A 1 183 ? 2.864   26.886  -44.340 1.000 19.157 ? 183 LEU A CA  1 ? 8  
ATOM   1415 C  C   . LEU A 1 183 ? 3.488   27.033  -42.950 1.000 19.327 ? 183 LEU A C   1 ? 8  
ATOM   1416 O  O   . LEU A 1 183 ? 3.532   28.168  -42.481 1.000 20.634 ? 183 LEU A O   1 ? 8  
ATOM   1417 C  CB  . LEU A 1 183 ? 1.342   26.903  -44.228 1.000 19.348 ? 183 LEU A CB  1 ? 8  
ATOM   1418 C  CG  . LEU A 1 183 ? 0.585   26.848  -45.555 1.000 18.490 ? 183 LEU A CG  1 ? 8  
ATOM   1419 C  CD1 . LEU A 1 183 ? -0.902  26.905  -45.304 1.000 18.926 ? 183 LEU A CD1 1 ? 8  
ATOM   1420 C  CD2 . LEU A 1 183 ? 1.033   27.930  -46.480 1.000 20.750 ? 183 LEU A CD2 1 ? 8  
ATOM   1421 N  N   . GLN A 1 184 ? 3.918   25.956  -42.314 1.000 18.066 ? 184 GLN A N   1 ? 8  
ATOM   1422 C  CA  . GLN A 1 184 ? 4.309   26.043  -40.899 1.000 18.380 ? 184 GLN A CA  1 ? 8  
ATOM   1423 C  C   . GLN A 1 184 ? 5.372   24.987  -40.637 1.000 19.000 ? 184 GLN A C   1 ? 8  
ATOM   1424 O  O   . GLN A 1 184 ? 5.208   23.871  -41.155 1.000 18.177 ? 184 GLN A O   1 ? 8  
ATOM   1425 C  CB  . GLN A 1 184 ? 3.068   25.783  -40.071 1.000 18.279 ? 184 GLN A CB  1 ? 8  
ATOM   1426 C  CG  . GLN A 1 184 ? 3.251   25.882  -38.569 1.000 18.930 ? 184 GLN A CG  1 ? 8  
ATOM   1427 C  CD  . GLN A 1 184 ? 1.914   25.847  -37.871 1.000 19.855 ? 184 GLN A CD  1 ? 8  
ATOM   1428 O  OE1 . GLN A 1 184 ? 1.410   26.884  -37.447 1.000 20.655 ? 184 GLN A OE1 1 ? 8  
ATOM   1429 N  NE2 . GLN A 1 184 ? 1.290   24.664  -37.753 1.000 18.606 ? 184 GLN A NE2 1 ? 8  
ATOM   1430 N  N   . ARG A 1 185 ? 6.404   25.335  -39.875 1.000 20.754 ? 185 ARG A N   1 ? 9  
ATOM   1431 C  CA  . ARG A 1 185 ? 7.531   24.407  -39.628 1.000 21.154 ? 185 ARG A CA  1 ? 9  
ATOM   1432 C  C   . ARG A 1 185 ? 7.754   24.319  -38.123 1.000 19.462 ? 185 ARG A C   1 ? 9  
ATOM   1433 O  O   . ARG A 1 185 ? 8.615   25.008  -37.582 1.000 20.037 ? 185 ARG A O   1 ? 9  
ATOM   1434 C  CB  . ARG A 1 185 ? 8.774   24.781  -40.469 1.000 27.147 ? 185 ARG A CB  1 ? 9  
ATOM   1435 C  CG  . ARG A 1 185 ? 8.646   24.279  -41.945 1.000 33.126 ? 185 ARG A CG  1 ? 9  
ATOM   1436 C  CD  . ARG A 1 185 ? 9.634   24.841  -42.942 1.000 42.264 ? 185 ARG A CD  1 ? 9  
ATOM   1437 N  NE  . ARG A 1 185 ? 10.885  24.195  -42.753 1.000 49.735 ? 185 ARG A NE  1 ? 9  
ATOM   1438 C  CZ  . ARG A 1 185 ? 12.054  24.665  -43.190 1.000 64.027 ? 185 ARG A CZ  1 ? 9  
ATOM   1439 N  NH1 . ARG A 1 185 ? 13.177  23.967  -43.015 1.000 65.017 ? 185 ARG A NH1 1 ? 9  
ATOM   1440 N  NH2 . ARG A 1 185 ? 12.096  25.844  -43.788 1.000 70.296 ? 185 ARG A NH2 1 ? 9  
ATOM   1441 N  N   . PRO A 1 186 ? 7.005   23.473  -37.421 1.000 18.304 ? 186 PRO A N   1 ? 9  
ATOM   1442 C  CA  . PRO A 1 186 ? 7.073   23.463  -35.965 1.000 18.558 ? 186 PRO A CA  1 ? 9  
ATOM   1443 C  C   . PRO A 1 186 ? 8.455   23.182  -35.397 1.000 18.881 ? 186 PRO A C   1 ? 9  
ATOM   1444 O  O   . PRO A 1 186 ? 8.766   23.725  -34.281 1.000 19.597 ? 186 PRO A O   1 ? 9  
ATOM   1445 C  CB  . PRO A 1 186 ? 6.071   22.401  -35.541 1.000 18.039 ? 186 PRO A CB  1 ? 9  
ATOM   1446 C  CG  . PRO A 1 186 ? 5.045   22.384  -36.711 1.000 17.605 ? 186 PRO A CG  1 ? 9  
ATOM   1447 C  CD  . PRO A 1 186 ? 5.903   22.592  -37.939 1.000 18.148 ? 186 PRO A CD  1 ? 9  
ATOM   1448 N  N   . LEU A 1 187 ? 9.247   22.319  -36.021 1.000 18.159 ? 187 LEU A N   1 ? 9  
ATOM   1449 C  CA  . LEU A 1 187 ? 10.599  22.031  -35.442 1.000 20.170 ? 187 LEU A CA  1 ? 9  
ATOM   1450 C  C   . LEU A 1 187 ? 11.397  23.325  -35.349 1.000 21.563 ? 187 LEU A C   1 ? 9  
ATOM   1451 O  O   . LEU A 1 187 ? 12.234  23.463  -34.423 1.000 22.240 ? 187 LEU A O   1 ? 9  
ATOM   1452 C  CB  . LEU A 1 187 ? 11.369  20.989  -36.236 1.000 20.569 ? 187 LEU A CB  1 ? 9  
ATOM   1453 C  CG  . LEU A 1 187 ? 10.668  19.625  -36.390 1.000 20.366 ? 187 LEU A CG  1 ? 9  
ATOM   1454 C  CD1 . LEU A 1 187 ? 11.508  18.701  -37.205 1.000 21.611 ? 187 LEU A CD1 1 ? 9  
ATOM   1455 C  CD2 . LEU A 1 187 ? 10.361  18.998  -35.014 1.000 20.757 ? 187 LEU A CD2 1 ? 9  
ATOM   1456 N  N   . SER A 1 188 ? 11.254  24.257  -36.287 1.000 21.713 ? 188 SER A N   1 ? 9  
ATOM   1457 C  CA  . SER A 1 188 ? 12.002  25.519  -36.333 1.000 23.686 ? 188 SER A CA  1 ? 9  
ATOM   1458 C  C   . SER A 1 188 ? 11.612  26.426  -35.141 1.000 22.944 ? 188 SER A C   1 ? 9  
ATOM   1459 O  O   . SER A 1 188 ? 12.403  27.336  -34.840 1.000 25.454 ? 188 SER A O   1 ? 9  
ATOM   1460 C  CB  . SER A 1 188 ? 11.835  26.266  -37.654 1.000 25.340 ? 188 SER A CB  1 ? 9  
ATOM   1461 O  OG  . SER A 1 188 ? 10.553  26.889  -37.725 1.000 24.475 ? 188 SER A OG  1 ? 9  
ATOM   1462 N  N   . LEU A 1 189 ? 10.480  26.149  -34.493 1.000 21.944 ? 189 LEU A N   1 ? 9  
ATOM   1463 C  CA  . LEU A 1 189 ? 9.939   26.939  -33.344 1.000 23.499 ? 189 LEU A CA  1 ? 9  
ATOM   1464 C  C   . LEU A 1 189 ? 10.107  26.148  -32.034 1.000 23.583 ? 189 LEU A C   1 ? 9  
ATOM   1465 O  O   . LEU A 1 189 ? 9.599   26.598  -31.006 1.000 26.183 ? 189 LEU A O   1 ? 9  
ATOM   1466 C  CB  . LEU A 1 189 ? 8.477   27.250  -33.662 1.000 23.747 ? 189 LEU A CB  1 ? 9  
ATOM   1467 C  CG  . LEU A 1 189 ? 8.298   28.137  -34.888 1.000 26.550 ? 189 LEU A CG  1 ? 9  
ATOM   1468 C  CD1 . LEU A 1 189 ? 6.827   28.295  -35.203 1.000 28.208 ? 189 LEU A CD1 1 ? 9  
ATOM   1469 C  CD2 . LEU A 1 189 ? 8.990   29.459  -34.766 1.000 31.798 ? 189 LEU A CD2 1 ? 9  
ATOM   1470 N  N   . GLY A 1 190 ? 10.821  25.040  -32.053 1.000 21.804 ? 190 GLY A N   1 ? 9  
ATOM   1471 C  CA  . GLY A 1 190 ? 11.163  24.265  -30.848 1.000 23.547 ? 190 GLY A CA  1 ? 9  
ATOM   1472 C  C   . GLY A 1 190 ? 10.311  23.042  -30.611 1.000 21.679 ? 190 GLY A C   1 ? 9  
ATOM   1473 O  O   . GLY A 1 190 ? 10.543  22.372  -29.644 1.000 22.511 ? 190 GLY A O   1 ? 9  
ATOM   1474 N  N   . ALA A 1 191 ? 9.397   22.666  -31.496 1.000 20.086 ? 191 ALA A N   1 ? 9  
ATOM   1475 C  CA  . ALA A 1 191 ? 8.720   21.366  -31.384 1.000 19.541 ? 191 ALA A CA  1 ? 9  
ATOM   1476 C  C   . ALA A 1 191 ? 9.737   20.249  -31.423 1.000 19.543 ? 191 ALA A C   1 ? 9  
ATOM   1477 O  O   . ALA A 1 191 ? 10.783  20.357  -32.072 1.000 20.140 ? 191 ALA A O   1 ? 9  
ATOM   1478 C  CB  . ALA A 1 191 ? 7.678   21.166  -32.442 1.000 19.187 ? 191 ALA A CB  1 ? 9  
ATOM   1479 N  N   . ASP A 1 192 ? 9.458   19.167  -30.687 1.000 19.753 ? 192 ASP A N   1 ? 9  
ATOM   1480 C  CA  . ASP A 1 192 ? 10.269  17.954  -30.698 1.000 19.170 ? 192 ASP A CA  1 ? 9  
ATOM   1481 C  C   . ASP A 1 192 ? 9.819   16.983  -31.805 1.000 18.671 ? 192 ASP A C   1 ? 9  
ATOM   1482 O  O   . ASP A 1 192 ? 10.650  16.239  -32.306 1.000 18.672 ? 192 ASP A O   1 ? 9  
ATOM   1483 C  CB  . ASP A 1 192 ? 10.188  17.252  -29.350 1.000 20.714 ? 192 ASP A CB  1 ? 9  
ATOM   1484 C  CG  . ASP A 1 192 ? 10.736  18.161  -28.242 1.000 23.064 ? 192 ASP A CG  1 ? 9  
ATOM   1485 O  OD1 . ASP A 1 192 ? 11.951  18.318  -28.143 1.000 23.627 ? 192 ASP A OD1 1 ? 9  
ATOM   1486 O  OD2 . ASP A 1 192 ? 9.903   18.813  -27.557 1.000 22.508 ? 192 ASP A OD2 1 ? 9  
ATOM   1487 N  N   . VAL A 1 193 ? 8.545   16.902  -32.037 1.000 19.735 ? 193 VAL A N   1 ? 9  
ATOM   1488 C  CA  . VAL A 1 193 ? 7.958   15.918  -32.969 1.000 18.665 ? 193 VAL A CA  1 ? 9  
ATOM   1489 C  C   . VAL A 1 193 ? 6.933   16.647  -33.782 1.000 18.527 ? 193 VAL A C   1 ? 9  
ATOM   1490 O  O   . VAL A 1 193 ? 6.093   17.349  -33.204 1.000 18.170 ? 193 VAL A O   1 ? 9  
ATOM   1491 C  CB  . VAL A 1 193 ? 7.342   14.708  -32.265 1.000 20.229 ? 193 VAL A CB  1 ? 9  
ATOM   1492 C  CG1 . VAL A 1 193 ? 6.936   13.670  -33.353 1.000 21.136 ? 193 VAL A CG1 1 ? 9  
ATOM   1493 C  CG2 . VAL A 1 193 ? 8.275   14.096  -31.267 1.000 21.929 ? 193 VAL A CG2 1 ? 9  
ATOM   1494 N  N   . VAL A 1 194 ? 6.925   16.390  -35.096 1.000 17.952 ? 194 VAL A N   1 ? 9  
ATOM   1495 C  CA  . VAL A 1 194 ? 5.827   16.794  -35.980 1.000 17.219 ? 194 VAL A CA  1 ? 9  
ATOM   1496 C  C   . VAL A 1 194 ? 5.100   15.517  -36.381 1.000 16.326 ? 194 VAL A C   1 ? 9  
ATOM   1497 O  O   . VAL A 1 194 ? 5.761   14.541  -36.824 1.000 16.978 ? 194 VAL A O   1 ? 9  
ATOM   1498 C  CB  . VAL A 1 194 ? 6.337   17.546  -37.213 1.000 18.333 ? 194 VAL A CB  1 ? 9  
ATOM   1499 C  CG1 . VAL A 1 194 ? 5.235   17.740  -38.225 1.000 19.991 ? 194 VAL A CG1 1 ? 9  
ATOM   1500 C  CG2 . VAL A 1 194 ? 6.905   18.880  -36.758 1.000 19.896 ? 194 VAL A CG2 1 ? 9  
ATOM   1501 N  N   . VAL A 1 195 ? 3.796   15.541  -36.302 1.000 17.177 ? 195 VAL A N   1 ? 9  
ATOM   1502 C  CA  . VAL A 1 195 ? 2.896   14.487  -36.777 1.000 16.919 ? 195 VAL A CA  1 ? 9  
ATOM   1503 C  C   . VAL A 1 195 ? 2.189   14.982  -38.003 1.000 17.442 ? 195 VAL A C   1 ? 9  
ATOM   1504 O  O   . VAL A 1 195 ? 1.707   16.131  -37.999 1.000 16.913 ? 195 VAL A O   1 ? 9  
ATOM   1505 C  CB  . VAL A 1 195 ? 1.870   14.117  -35.688 1.000 19.637 ? 195 VAL A CB  1 ? 9  
ATOM   1506 C  CG1 . VAL A 1 195 ? 0.832   13.116  -36.195 1.000 23.069 ? 195 VAL A CG1 1 ? 9  
ATOM   1507 C  CG2 . VAL A 1 195 ? 2.545   13.622  -34.447 1.000 20.992 ? 195 VAL A CG2 1 ? 9  
ATOM   1508 N  N   . HIS A 1 196 ? 2.010   14.114  -38.998 1.000 16.036 ? 196 HIS A N   1 ? 10 
ATOM   1509 C  CA  . HIS A 1 196 ? 1.091   14.370  -40.116 1.000 16.726 ? 196 HIS A CA  1 ? 10 
ATOM   1510 C  C   . HIS A 1 196 ? 0.200   13.187  -40.370 1.000 16.169 ? 196 HIS A C   1 ? 10 
ATOM   1511 O  O   . HIS A 1 196 ? 0.705   12.048  -40.358 1.000 15.861 ? 196 HIS A O   1 ? 10 
ATOM   1512 C  CB  . HIS A 1 196 ? 1.842   14.597  -41.426 1.000 16.799 ? 196 HIS A CB  1 ? 10 
ATOM   1513 C  CG  . HIS A 1 196 ? 2.587   15.873  -41.497 1.000 16.840 ? 196 HIS A CG  1 ? 10 
ATOM   1514 N  ND1 . HIS A 1 196 ? 1.955   17.046  -41.783 1.000 16.971 ? 196 HIS A ND1 1 ? 10 
ATOM   1515 C  CD2 . HIS A 1 196 ? 3.909   16.144  -41.306 1.000 17.861 ? 196 HIS A CD2 1 ? 10 
ATOM   1516 C  CE1 . HIS A 1 196 ? 2.864   18.012  -41.747 1.000 16.909 ? 196 HIS A CE1 1 ? 10 
ATOM   1517 N  NE2 . HIS A 1 196 ? 4.073   17.480  -41.433 1.000 17.921 ? 196 HIS A NE2 1 ? 10 
ATOM   1518 N  N   . SER A 1 197 ? -1.056  13.466  -40.696 1.000 16.372 ? 197 SER A N   1 ? 10 
ATOM   1519 C  CA  . SER A 1 197 ? -1.835  12.604  -41.612 1.000 16.150 ? 197 SER A CA  1 ? 10 
ATOM   1520 C  C   . SER A 1 197 ? -1.398  12.988  -43.007 1.000 15.174 ? 197 SER A C   1 ? 10 
ATOM   1521 O  O   . SER A 1 197 ? -1.759  14.065  -43.473 1.000 16.451 ? 197 SER A O   1 ? 10 
ATOM   1522 C  CB  . SER A 1 197 ? -3.283  12.826  -41.455 1.000 16.108 ? 197 SER A CB  1 ? 10 
ATOM   1523 O  OG  . SER A 1 197 ? -3.988  12.069  -42.434 1.000 16.922 ? 197 SER A OG  1 ? 10 
ATOM   1524 N  N   . THR A 1 198 ? -0.582  12.193  -43.672 1.000 15.929 ? 198 THR A N   1 ? 10 
ATOM   1525 C  CA  . THR A 1 198 ? -0.207  12.435  -45.080 1.000 15.984 ? 198 THR A CA  1 ? 10 
ATOM   1526 C  C   . THR A 1 198 ? -1.395  12.207  -46.005 1.000 16.215 ? 198 THR A C   1 ? 10 
ATOM   1527 O  O   . THR A 1 198 ? -1.303  12.603  -47.169 1.000 16.553 ? 198 THR A O   1 ? 10 
ATOM   1528 C  CB  . THR A 1 198 ? 1.053   11.666  -45.456 1.000 16.117 ? 198 THR A CB  1 ? 10 
ATOM   1529 O  OG1 . THR A 1 198 ? 0.751   10.275  -45.402 1.000 15.841 ? 198 THR A OG1 1 ? 10 
ATOM   1530 C  CG2 . THR A 1 198 ? 2.228   11.993  -44.590 1.000 17.577 ? 198 THR A CG2 1 ? 10 
ATOM   1531 N  N   . THR A 1 199 ? -2.472  11.656  -45.500 1.000 15.733 ? 199 THR A N   1 ? 10 
ATOM   1532 C  CA  . THR A 1 199 ? -3.713  11.457  -46.239 1.000 16.022 ? 199 THR A CA  1 ? 10 
ATOM   1533 C  C   . THR A 1 199 ? -4.187  12.809  -46.756 1.000 16.864 ? 199 THR A C   1 ? 10 
ATOM   1534 O  O   . THR A 1 199 ? -4.982  12.874  -47.702 1.000 17.734 ? 199 THR A O   1 ? 10 
ATOM   1535 C  CB  . THR A 1 199 ? -4.726  10.849  -45.313 1.000 16.567 ? 199 THR A CB  1 ? 10 
ATOM   1536 O  OG1 . THR A 1 199 ? -4.214  9.706   -44.628 1.000 16.184 ? 199 THR A OG1 1 ? 10 
ATOM   1537 C  CG2 . THR A 1 199 ? -6.005  10.495  -46.010 1.000 17.703 ? 199 THR A CG2 1 ? 10 
ATOM   1538 N  N   . LYS A 1 200 ? -3.868  13.885  -46.036 1.000 16.001 ? 200 LYS A N   1 ? 10 
ATOM   1539 C  CA  . LYS A 1 200 ? -4.491  15.209  -46.288 1.000 16.600 ? 200 LYS A CA  1 ? 10 
ATOM   1540 C  C   . LYS A 1 200 ? -3.636  15.965  -47.315 1.000 17.379 ? 200 LYS A C   1 ? 10 
ATOM   1541 O  O   . LYS A 1 200 ? -3.514  15.478  -48.453 1.000 17.904 ? 200 LYS A O   1 ? 10 
ATOM   1542 C  CB  . LYS A 1 200 ? -4.740  15.920  -44.947 1.000 17.454 ? 200 LYS A CB  1 ? 10 
ATOM   1543 C  CG  . LYS A 1 200 ? -5.390  15.054  -43.885 1.000 17.473 ? 200 LYS A CG  1 ? 10 
ATOM   1544 C  CD  . LYS A 1 200 ? -6.542  14.218  -44.347 1.000 18.670 ? 200 LYS A CD  1 ? 10 
ATOM   1545 C  CE  . LYS A 1 200 ? -7.253  13.534  -43.210 1.000 21.273 ? 200 LYS A CE  1 ? 10 
ATOM   1546 N  NZ  . LYS A 1 200 ? -8.162  12.470  -43.705 1.000 24.662 ? 200 LYS A NZ  1 ? 10 
ATOM   1547 N  N   . TYR A 1 201 ? -3.118  17.122  -47.021 1.000 15.869 ? 201 TYR A N   1 ? 10 
ATOM   1548 C  CA  . TYR A 1 201 ? -2.450  17.965  -48.011 1.000 15.486 ? 201 TYR A CA  1 ? 10 
ATOM   1549 C  C   . TYR A 1 201 ? -1.185  17.348  -48.634 1.000 15.753 ? 201 TYR A C   1 ? 10 
ATOM   1550 O  O   . TYR A 1 201 ? -0.853  17.682  -49.754 1.000 17.048 ? 201 TYR A O   1 ? 10 
ATOM   1551 C  CB  . TYR A 1 201 ? -2.093  19.307  -47.401 1.000 16.400 ? 201 TYR A CB  1 ? 10 
ATOM   1552 C  CG  . TYR A 1 201 ? -3.282  20.197  -47.159 1.000 17.781 ? 201 TYR A CG  1 ? 10 
ATOM   1553 C  CD1 . TYR A 1 201 ? -3.938  20.859  -48.178 1.000 17.596 ? 201 TYR A CD1 1 ? 10 
ATOM   1554 C  CD2 . TYR A 1 201 ? -3.810  20.303  -45.883 1.000 18.196 ? 201 TYR A CD2 1 ? 10 
ATOM   1555 C  CE1 . TYR A 1 201 ? -5.028  21.683  -47.954 1.000 17.875 ? 201 TYR A CE1 1 ? 10 
ATOM   1556 C  CE2 . TYR A 1 201 ? -4.877  21.156  -45.625 1.000 19.418 ? 201 TYR A CE2 1 ? 10 
ATOM   1557 C  CZ  . TYR A 1 201 ? -5.525  21.839  -46.654 1.000 18.888 ? 201 TYR A CZ  1 ? 10 
ATOM   1558 O  OH  . TYR A 1 201 ? -6.600  22.651  -46.414 1.000 19.994 ? 201 TYR A OH  1 ? 10 
ATOM   1559 N  N   . LEU A 1 202 ? -0.419  16.534  -47.880 1.000 16.020 ? 202 LEU A N   1 ? 10 
ATOM   1560 C  CA  . LEU A 1 202 ? 0.851   16.005  -48.434 1.000 15.303 ? 202 LEU A CA  1 ? 10 
ATOM   1561 C  C   . LEU A 1 202 ? 0.552   15.084  -49.634 1.000 15.249 ? 202 LEU A C   1 ? 10 
ATOM   1562 O  O   . LEU A 1 202 ? 1.082   15.354  -50.739 1.000 16.032 ? 202 LEU A O   1 ? 10 
ATOM   1563 C  CB  . LEU A 1 202 ? 1.641   15.360  -47.307 1.000 16.504 ? 202 LEU A CB  1 ? 10 
ATOM   1564 C  CG  . LEU A 1 202 ? 2.305   16.365  -46.398 1.000 16.746 ? 202 LEU A CG  1 ? 10 
ATOM   1565 C  CD1 . LEU A 1 202 ? 2.655   15.755  -45.050 1.000 17.781 ? 202 LEU A CD1 1 ? 10 
ATOM   1566 C  CD2 . LEU A 1 202 ? 3.498   17.016  -47.015 1.000 17.799 ? 202 LEU A CD2 1 ? 10 
ATOM   1567 N  N   . GLY A 1 203 ? -0.231  14.008  -49.449 1.000 15.926 ? 203 GLY A N   1 ? 10 
ATOM   1568 C  CA  . GLY A 1 203 ? -0.644  13.207  -50.602 1.000 15.199 ? 203 GLY A CA  1 ? 10 
ATOM   1569 C  C   . GLY A 1 203 ? -1.451  14.047  -51.575 1.000 16.703 ? 203 GLY A C   1 ? 10 
ATOM   1570 O  O   . GLY A 1 203 ? -1.254  13.915  -52.794 1.000 16.152 ? 203 GLY A O   1 ? 10 
ATOM   1571 N  N   . GLY A 1 204 ? -2.422  14.817  -51.063 1.000 16.220 ? 204 GLY A N   1 ? 10 
ATOM   1572 C  CA  . GLY A 1 204 ? -3.058  15.897  -51.797 1.000 16.113 ? 204 GLY A CA  1 ? 10 
ATOM   1573 C  C   . GLY A 1 204 ? -4.202  15.501  -52.720 1.000 15.910 ? 204 GLY A C   1 ? 10 
ATOM   1574 O  O   . GLY A 1 204 ? -4.823  16.440  -53.302 1.000 16.417 ? 204 GLY A O   1 ? 10 
ATOM   1575 N  N   . HIS A 1 205 ? -4.486  14.211  -52.875 1.000 15.203 ? 205 HIS A N   1 ? 10 
ATOM   1576 C  CA  . HIS A 1 205 ? -5.432  13.786  -53.963 1.000 16.330 ? 205 HIS A CA  1 ? 10 
ATOM   1577 C  C   . HIS A 1 205 ? -6.494  12.830  -53.456 1.000 15.843 ? 205 HIS A C   1 ? 10 
ATOM   1578 O  O   . HIS A 1 205 ? -7.126  12.171  -54.281 1.000 15.813 ? 205 HIS A O   1 ? 10 
ATOM   1579 C  CB  . HIS A 1 205 ? -4.620  13.210  -55.153 1.000 16.460 ? 205 HIS A CB  1 ? 10 
ATOM   1580 C  CG  . HIS A 1 205 ? -3.710  14.221  -55.785 1.000 16.023 ? 205 HIS A CG  1 ? 10 
ATOM   1581 N  ND1 . HIS A 1 205 ? -2.520  14.616  -55.194 1.000 16.214 ? 205 HIS A ND1 1 ? 10 
ATOM   1582 C  CD2 . HIS A 1 205 ? -3.787  14.848  -56.969 1.000 17.776 ? 205 HIS A CD2 1 ? 10 
ATOM   1583 C  CE1 . HIS A 1 205 ? -1.933  15.500  -56.016 1.000 17.196 ? 205 HIS A CE1 1 ? 10 
ATOM   1584 N  NE2 . HIS A 1 205 ? -2.694  15.656  -57.119 1.000 17.580 ? 205 HIS A NE2 1 ? 10 
ATOM   1585 N  N   . SER A 1 206 ? -6.721  12.794  -52.124 1.000 16.545 ? 206 SER A N   1 ? 10 
ATOM   1586 C  CA  . SER A 1 206 ? -7.762  11.940  -51.512 1.000 17.005 ? 206 SER A CA  1 ? 10 
ATOM   1587 C  C   . SER A 1 206 ? -7.681  10.501  -52.003 1.000 16.023 ? 206 SER A C   1 ? 10 
ATOM   1588 O  O   . SER A 1 206 ? -8.730  9.860   -52.180 1.000 16.701 ? 206 SER A O   1 ? 10 
ATOM   1589 C  CB  . SER A 1 206 ? -9.126  12.464  -51.809 1.000 19.089 ? 206 SER A CB  1 ? 10 
ATOM   1590 O  OG  . SER A 1 206 ? -9.216  13.781  -51.291 1.000 22.097 ? 206 SER A OG  1 ? 10 
ATOM   1591 N  N   . ASP A 1 207 ? -6.451  9.981   -52.172 1.000 16.129 ? 207 ASP A N   1 ? 10 
ATOM   1592 C  CA  . ASP A 1 207 ? -6.274  8.661   -52.783 1.000 16.305 ? 207 ASP A CA  1 ? 10 
ATOM   1593 C  C   . ASP A 1 207 ? -5.219  7.829   -52.057 1.000 16.687 ? 207 ASP A C   1 ? 10 
ATOM   1594 O  O   . ASP A 1 207 ? -4.902  6.746   -52.552 1.000 18.645 ? 207 ASP A O   1 ? 10 
ATOM   1595 C  CB  . ASP A 1 207 ? -5.979  8.783   -54.262 1.000 16.596 ? 207 ASP A CB  1 ? 10 
ATOM   1596 C  CG  . ASP A 1 207 ? -4.735  9.555   -54.628 1.000 16.485 ? 207 ASP A CG  1 ? 10 
ATOM   1597 O  OD1 . ASP A 1 207 ? -3.971  9.884   -53.723 1.000 17.541 ? 207 ASP A OD1 1 ? 10 
ATOM   1598 O  OD2 . ASP A 1 207 ? -4.609  9.805   -55.872 1.000 17.841 ? 207 ASP A OD2 1 ? 10 
ATOM   1599 N  N   A VAL A 1 208 ? -4.769  8.196   -50.861 0.500 16.090 ? 208 VAL A N   1 ? 10 
ATOM   1600 N  N   B VAL A 1 208 ? -4.760  8.271   -50.894 0.500 17.295 ? 208 VAL A N   1 ? 10 
ATOM   1601 C  CA  A VAL A 1 208 ? -3.768  7.357   -50.123 0.500 15.840 ? 208 VAL A CA  1 ? 10 
ATOM   1602 C  CA  B VAL A 1 208 ? -3.824  7.499   -50.027 0.500 17.959 ? 208 VAL A CA  1 ? 10 
ATOM   1603 C  C   A VAL A 1 208 ? -3.791  7.732   -48.631 0.500 16.214 ? 208 VAL A C   1 ? 10 
ATOM   1604 C  C   B VAL A 1 208 ? -4.208  7.772   -48.590 0.500 17.310 ? 208 VAL A C   1 ? 10 
ATOM   1605 O  O   A VAL A 1 208 ? -3.423  8.919   -48.281 0.500 16.874 ? 208 VAL A O   1 ? 10 
ATOM   1606 O  O   B VAL A 1 208 ? -4.575  8.914   -48.259 0.500 17.635 ? 208 VAL A O   1 ? 10 
ATOM   1607 C  CB  A VAL A 1 208 ? -2.341  7.446   -50.754 0.500 16.074 ? 208 VAL A CB  1 ? 10 
ATOM   1608 C  CB  B VAL A 1 208 ? -2.348  7.880   -50.242 0.500 21.151 ? 208 VAL A CB  1 ? 10 
ATOM   1609 C  CG1 A VAL A 1 208 ? -1.870  8.880   -50.959 0.500 16.025 ? 208 VAL A CG1 1 ? 10 
ATOM   1610 C  CG1 B VAL A 1 208 ? -1.415  7.068   -49.354 0.500 23.712 ? 208 VAL A CG1 1 ? 10 
ATOM   1611 C  CG2 A VAL A 1 208 ? -1.329  6.667   -49.932 0.500 18.221 ? 208 VAL A CG2 1 ? 10 
ATOM   1612 C  CG2 B VAL A 1 208 ? -1.971  7.708   -51.660 0.500 23.793 ? 208 VAL A CG2 1 ? 10 
ATOM   1613 N  N   . VAL A 1 209 ? -4.155  6.756   -47.793 1.000 16.238 ? 209 VAL A N   1 ? 10 
ATOM   1614 C  CA  . VAL A 1 209 ? -4.174  6.958   -46.330 1.000 16.524 ? 209 VAL A CA  1 ? 10 
ATOM   1615 C  C   . VAL A 1 209 ? -2.759  6.685   -45.864 1.000 16.238 ? 209 VAL A C   1 ? 10 
ATOM   1616 O  O   . VAL A 1 209 ? -2.234  5.616   -46.138 1.000 16.316 ? 209 VAL A O   1 ? 10 
ATOM   1617 C  CB  . VAL A 1 209 ? -5.230  6.083   -45.689 1.000 16.364 ? 209 VAL A CB  1 ? 10 
ATOM   1618 C  CG1 . VAL A 1 209 ? -5.075  6.023   -44.175 1.000 16.330 ? 209 VAL A CG1 1 ? 10 
ATOM   1619 C  CG2 . VAL A 1 209 ? -6.649  6.507   -46.070 1.000 17.576 ? 209 VAL A CG2 1 ? 10 
ATOM   1620 N  N   . GLY A 1 210 ? -2.227  7.602   -45.078 1.000 15.690 ? 210 GLY A N   1 ? 10 
ATOM   1621 C  CA  . GLY A 1 210 ? -0.875  7.459   -44.576 1.000 15.497 ? 210 GLY A CA  1 ? 10 
ATOM   1622 C  C   . GLY A 1 210 ? -0.591  8.446   -43.482 1.000 16.346 ? 210 GLY A C   1 ? 10 
ATOM   1623 O  O   . GLY A 1 210 ? -1.354  9.411   -43.329 1.000 15.217 ? 210 GLY A O   1 ? 10 
ATOM   1624 N  N   . GLY A 1 211 ? 0.479   8.177   -42.736 1.000 16.465 ? 211 GLY A N   1 ? 10 
ATOM   1625 C  CA  . GLY A 1 211 ? 0.938   9.078   -41.664 1.000 14.642 ? 211 GLY A CA  1 ? 10 
ATOM   1626 C  C   . GLY A 1 211 ? 2.432   9.280   -41.684 1.000 15.281 ? 211 GLY A C   1 ? 10 
ATOM   1627 O  O   . GLY A 1 211 ? 3.175   8.514   -42.337 1.000 15.702 ? 211 GLY A O   1 ? 10 
ATOM   1628 N  N   . ALA A 1 212 ? 2.900   10.238  -40.930 1.000 15.791 ? 212 ALA A N   1 ? 10 
ATOM   1629 C  CA  . ALA A 1 212 ? 4.335   10.443  -40.782 1.000 15.490 ? 212 ALA A CA  1 ? 10 
ATOM   1630 C  C   . ALA A 1 212 ? 4.649   11.090  -39.446 1.000 15.718 ? 212 ALA A C   1 ? 10 
ATOM   1631 O  O   . ALA A 1 212 ? 3.843   11.833  -38.883 1.000 15.794 ? 212 ALA A O   1 ? 10 
ATOM   1632 C  CB  . ALA A 1 212 ? 4.861   11.300  -41.898 1.000 17.068 ? 212 ALA A CB  1 ? 10 
ATOM   1633 N  N   . LEU A 1 213 ? 5.881   10.846  -39.007 1.000 15.984 ? 213 LEU A N   1 ? 10 
ATOM   1634 C  CA  . LEU A 1 213 ? 6.517   11.555  -37.875 1.000 16.326 ? 213 LEU A CA  1 ? 10 
ATOM   1635 C  C   . LEU A 1 213 ? 7.819   12.177  -38.421 1.000 16.888 ? 213 LEU A C   1 ? 10 
ATOM   1636 O  O   . LEU A 1 213 ? 8.515   11.501  -39.189 1.000 17.552 ? 213 LEU A O   1 ? 10 
ATOM   1637 C  CB  . LEU A 1 213 ? 6.855   10.580  -36.748 1.000 16.694 ? 213 LEU A CB  1 ? 10 
ATOM   1638 C  CG  . LEU A 1 213 ? 5.640   9.852   -36.120 1.000 16.729 ? 213 LEU A CG  1 ? 10 
ATOM   1639 C  CD1 . LEU A 1 213 ? 6.169   8.862   -35.100 1.000 17.870 ? 213 LEU A CD1 1 ? 10 
ATOM   1640 C  CD2 . LEU A 1 213 ? 4.652   10.836  -35.550 1.000 17.523 ? 213 LEU A CD2 1 ? 10 
ATOM   1641 N  N   . VAL A 1 214 ? 8.145   13.366  -37.987 1.000 16.736 ? 214 VAL A N   1 ? 10 
ATOM   1642 C  CA  . VAL A 1 214 ? 9.484   13.930  -38.223 1.000 16.352 ? 214 VAL A CA  1 ? 10 
ATOM   1643 C  C   . VAL A 1 214 ? 10.021  14.460  -36.897 1.000 17.694 ? 214 VAL A C   1 ? 10 
ATOM   1644 O  O   . VAL A 1 214 ? 9.238   15.137  -36.152 1.000 18.155 ? 214 VAL A O   1 ? 10 
ATOM   1645 C  CB  . VAL A 1 214 ? 9.438   15.055  -39.270 1.000 17.096 ? 214 VAL A CB  1 ? 10 
ATOM   1646 C  CG1 . VAL A 1 214 ? 10.847  15.557  -39.513 1.000 19.328 ? 214 VAL A CG1 1 ? 10 
ATOM   1647 C  CG2 . VAL A 1 214 ? 8.835   14.585  -40.575 1.000 18.960 ? 214 VAL A CG2 1 ? 10 
ATOM   1648 N  N   . VAL A 1 215 ? 11.296  14.210  -36.620 1.000 17.394 ? 215 VAL A N   1 ? 10 
ATOM   1649 C  CA  . VAL A 1 215 ? 11.898  14.650  -35.348 1.000 18.101 ? 215 VAL A CA  1 ? 10 
ATOM   1650 C  C   . VAL A 1 215 ? 13.167  15.439  -35.580 1.000 20.308 ? 215 VAL A C   1 ? 10 
ATOM   1651 O  O   . VAL A 1 215 ? 13.791  15.306  -36.613 1.000 20.564 ? 215 VAL A O   1 ? 10 
ATOM   1652 C  CB  . VAL A 1 215 ? 12.180  13.479  -34.415 1.000 20.184 ? 215 VAL A CB  1 ? 10 
ATOM   1653 C  CG1 . VAL A 1 215 ? 10.861  12.832  -34.037 1.000 22.127 ? 215 VAL A CG1 1 ? 10 
ATOM   1654 C  CG2 . VAL A 1 215 ? 13.158  12.498  -35.001 1.000 19.750 ? 215 VAL A CG2 1 ? 10 
ATOM   1655 N  N   . ALA A 1 216 ? 13.495  16.242  -34.569 1.000 20.966 ? 216 ALA A N   1 ? 10 
ATOM   1656 C  CA  . ALA A 1 216 ? 14.749  17.023  -34.509 1.000 23.297 ? 216 ALA A CA  1 ? 10 
ATOM   1657 C  C   . ALA A 1 216 ? 15.905  16.209  -33.925 1.000 23.049 ? 216 ALA A C   1 ? 10 
ATOM   1658 O  O   . ALA A 1 216 ? 17.078  16.514  -34.194 1.000 25.910 ? 216 ALA A O   1 ? 10 
ATOM   1659 C  CB  . ALA A 1 216 ? 14.501  18.281  -33.684 1.000 24.952 ? 216 ALA A CB  1 ? 10 
ATOM   1660 N  N   . ASP A 1 217 ? 15.602  15.288  -33.036 1.000 21.843 ? 217 ASP A N   1 ? 10 
ATOM   1661 C  CA  . ASP A 1 217 ? 16.602  14.590  -32.219 1.000 23.307 ? 217 ASP A CA  1 ? 10 
ATOM   1662 C  C   . ASP A 1 217 ? 16.810  13.165  -32.730 1.000 22.719 ? 217 ASP A C   1 ? 10 
ATOM   1663 O  O   . ASP A 1 217 ? 15.841  12.380  -32.817 1.000 22.040 ? 217 ASP A O   1 ? 10 
ATOM   1664 C  CB  . ASP A 1 217 ? 16.213  14.559  -30.750 1.000 24.602 ? 217 ASP A CB  1 ? 10 
ATOM   1665 C  CG  . ASP A 1 217 ? 17.288  13.870  -29.949 1.000 28.415 ? 217 ASP A CG  1 ? 10 
ATOM   1666 O  OD1 . ASP A 1 217 ? 18.169  14.531  -29.472 1.000 33.501 ? 217 ASP A OD1 1 ? 10 
ATOM   1667 O  OD2 . ASP A 1 217 ? 17.187  12.728  -29.756 1.000 28.416 ? 217 ASP A OD2 1 ? 10 
ATOM   1668 N  N   . ALA A 1 218 ? 18.035  12.851  -33.123 1.000 22.762 ? 218 ALA A N   1 ? 10 
ATOM   1669 C  CA  . ALA A 1 218 ? 18.315  11.544  -33.780 1.000 23.019 ? 218 ALA A CA  1 ? 10 
ATOM   1670 C  C   . ALA A 1 218 ? 18.008  10.386  -32.813 1.000 21.921 ? 218 ALA A C   1 ? 10 
ATOM   1671 O  O   . ALA A 1 218 ? 17.531  9.359   -33.272 1.000 20.462 ? 218 ALA A O   1 ? 10 
ATOM   1672 C  CB  . ALA A 1 218 ? 19.732  11.499  -34.260 1.000 24.198 ? 218 ALA A CB  1 ? 10 
ATOM   1673 N  N   . GLU A 1 219 ? 18.251  10.527  -31.508 1.000 21.726 ? 219 GLU A N   1 ? 11 
ATOM   1674 C  CA  . GLU A 1 219 ? 17.942  9.427   -30.572 1.000 21.640 ? 219 GLU A CA  1 ? 11 
ATOM   1675 C  C   . GLU A 1 219 ? 16.469  9.182   -30.456 1.000 20.815 ? 219 GLU A C   1 ? 11 
ATOM   1676 O  O   . GLU A 1 219 ? 16.046  7.990   -30.501 1.000 21.427 ? 219 GLU A O   1 ? 11 
ATOM   1677 C  CB  . GLU A 1 219 ? 18.476  9.695   -29.169 1.000 24.342 ? 219 GLU A CB  1 ? 11 
ATOM   1678 C  CG  . GLU A 1 219 ? 19.765  9.108   -28.945 1.000 27.993 ? 219 GLU A CG  1 ? 11 
ATOM   1679 C  CD  . GLU A 1 219 ? 19.841  7.606   -29.182 1.000 27.217 ? 219 GLU A CD  1 ? 11 
ATOM   1680 O  OE1 . GLU A 1 219 ? 19.084  6.837   -28.514 1.000 28.993 ? 219 GLU A OE1 1 ? 11 
ATOM   1681 O  OE2 . GLU A 1 219 ? 20.639  7.229   -30.067 1.000 32.039 ? 219 GLU A OE2 1 ? 11 
ATOM   1682 N  N   . LEU A 1 220 ? 15.657  10.236  -30.376 1.000 20.185 ? 220 LEU A N   1 ? 11 
ATOM   1683 C  CA  . LEU A 1 220 ? 14.209  9.993   -30.342 1.000 20.054 ? 220 LEU A CA  1 ? 11 
ATOM   1684 C  C   . LEU A 1 220 ? 13.829  9.320   -31.675 1.000 19.244 ? 220 LEU A C   1 ? 11 
ATOM   1685 O  O   . LEU A 1 220 ? 12.926  8.477   -31.686 1.000 20.060 ? 220 LEU A O   1 ? 11 
ATOM   1686 C  CB  . LEU A 1 220 ? 13.479  11.335  -30.156 1.000 19.783 ? 220 LEU A CB  1 ? 11 
ATOM   1687 C  CG  . LEU A 1 220 ? 11.976  11.279  -30.186 1.000 22.042 ? 220 LEU A CG  1 ? 11 
ATOM   1688 C  CD1 . LEU A 1 220 ? 11.454  10.284  -29.142 1.000 24.692 ? 220 LEU A CD1 1 ? 11 
ATOM   1689 C  CD2 . LEU A 1 220 ? 11.420  12.694  -29.941 1.000 22.996 ? 220 LEU A CD2 1 ? 11 
ATOM   1690 N  N   . GLY A 1 221 ? 14.409  9.758   -32.809 1.000 18.444 ? 221 GLY A N   1 ? 11 
ATOM   1691 C  CA  . GLY A 1 221 ? 14.161  9.131   -34.080 1.000 18.465 ? 221 GLY A CA  1 ? 11 
ATOM   1692 C  C   . GLY A 1 221 ? 14.436  7.619   -34.030 1.000 18.158 ? 221 GLY A C   1 ? 11 
ATOM   1693 O  O   . GLY A 1 221 ? 13.635  6.860   -34.603 1.000 18.170 ? 221 GLY A O   1 ? 11 
ATOM   1694 N  N   . GLU A 1 222 ? 15.540  7.211   -33.429 1.000 18.486 ? 222 GLU A N   1 ? 11 
ATOM   1695 C  CA  . GLU A 1 222 ? 15.860  5.763   -33.289 1.000 19.939 ? 222 GLU A CA  1 ? 11 
ATOM   1696 C  C   . GLU A 1 222 ? 14.889  5.074   -32.379 1.000 19.373 ? 222 GLU A C   1 ? 11 
ATOM   1697 O  O   . GLU A 1 222 ? 14.523  3.932   -32.664 1.000 19.837 ? 222 GLU A O   1 ? 11 
ATOM   1698 C  CB  . GLU A 1 222 ? 17.272  5.583   -32.767 1.000 23.263 ? 222 GLU A CB  1 ? 11 
ATOM   1699 C  CG  . GLU A 1 222 ? 18.308  5.957   -33.756 1.000 26.625 ? 222 GLU A CG  1 ? 11 
ATOM   1700 C  CD  . GLU A 1 222 ? 18.387  5.122   -35.002 1.000 34.621 ? 222 GLU A CD  1 ? 11 
ATOM   1701 O  OE1 . GLU A 1 222 ? 17.641  4.146   -35.185 1.000 36.330 ? 222 GLU A OE1 1 ? 11 
ATOM   1702 O  OE2 . GLU A 1 222 ? 19.121  5.510   -35.813 1.000 45.512 ? 222 GLU A OE2 1 ? 11 
ATOM   1703 N  N   . ARG A 1 223 ? 14.417  5.680   -31.304 1.000 20.799 ? 223 ARG A N   1 ? 11 
ATOM   1704 C  CA  A ARG A 1 223 ? 13.377  5.014   -30.456 0.500 20.457 ? 223 ARG A CA  1 ? 11 
ATOM   1705 C  CA  B ARG A 1 223 ? 13.362  5.058   -30.450 0.500 20.743 ? 223 ARG A CA  1 ? 11 
ATOM   1706 C  C   . ARG A 1 223 ? 12.088  4.849   -31.233 1.000 20.936 ? 223 ARG A C   1 ? 11 
ATOM   1707 O  O   . ARG A 1 223 ? 11.427  3.802   -31.090 1.000 21.409 ? 223 ARG A O   1 ? 11 
ATOM   1708 C  CB  A ARG A 1 223 ? 13.087  5.764   -29.137 0.500 21.663 ? 223 ARG A CB  1 ? 11 
ATOM   1709 C  CB  B ARG A 1 223 ? 13.050  5.940   -29.224 0.500 22.383 ? 223 ARG A CB  1 ? 11 
ATOM   1710 C  CG  A ARG A 1 223 ? 14.316  6.164   -28.391 0.500 22.678 ? 223 ARG A CG  1 ? 11 
ATOM   1711 C  CG  B ARG A 1 223 ? 13.977  5.700   -28.084 0.500 23.959 ? 223 ARG A CG  1 ? 11 
ATOM   1712 C  CD  A ARG A 1 223 ? 14.013  6.523   -26.953 0.500 23.379 ? 223 ARG A CD  1 ? 11 
ATOM   1713 C  CD  B ARG A 1 223 ? 13.403  6.030   -26.709 0.500 25.073 ? 223 ARG A CD  1 ? 11 
ATOM   1714 N  NE  A ARG A 1 223 ? 13.393  7.809   -26.725 0.500 24.818 ? 223 ARG A NE  1 ? 11 
ATOM   1715 N  NE  B ARG A 1 223 ? 14.469  5.637   -25.813 0.500 28.579 ? 223 ARG A NE  1 ? 11 
ATOM   1716 C  CZ  A ARG A 1 223 ? 14.006  9.036   -26.719 0.500 24.207 ? 223 ARG A CZ  1 ? 11 
ATOM   1717 C  CZ  B ARG A 1 223 ? 14.609  4.468   -25.182 0.500 29.100 ? 223 ARG A CZ  1 ? 11 
ATOM   1718 N  NH1 A ARG A 1 223 ? 13.284  10.089  -26.369 0.500 26.711 ? 223 ARG A NH1 1 ? 11 
ATOM   1719 N  NH1 B ARG A 1 223 ? 15.686  4.289   -24.447 0.500 28.526 ? 223 ARG A NH1 1 ? 11 
ATOM   1720 N  NH2 A ARG A 1 223 ? 15.285  9.244   -27.030 0.500 19.432 ? 223 ARG A NH2 1 ? 11 
ATOM   1721 N  NH2 B ARG A 1 223 ? 13.714  3.505   -25.308 0.500 31.326 ? 223 ARG A NH2 1 ? 11 
ATOM   1722 N  N   . LEU A 1 224 ? 11.654  5.873   -31.975 1.000 18.820 ? 224 LEU A N   1 ? 11 
ATOM   1723 C  CA  . LEU A 1 224 ? 10.479  5.744   -32.819 1.000 18.748 ? 224 LEU A CA  1 ? 11 
ATOM   1724 C  C   . LEU A 1 224 ? 10.711  4.671   -33.848 1.000 18.469 ? 224 LEU A C   1 ? 11 
ATOM   1725 O  O   . LEU A 1 224 ? 9.756   3.953   -34.174 1.000 20.052 ? 224 LEU A O   1 ? 11 
ATOM   1726 C  CB  . LEU A 1 224 ? 10.145  7.100   -33.427 1.000 18.092 ? 224 LEU A CB  1 ? 11 
ATOM   1727 C  CG  . LEU A 1 224 ? 9.674   8.139   -32.442 1.000 19.556 ? 224 LEU A CG  1 ? 11 
ATOM   1728 C  CD1 . LEU A 1 224 ? 9.694   9.501   -33.059 1.000 20.584 ? 224 LEU A CD1 1 ? 11 
ATOM   1729 C  CD2 . LEU A 1 224 ? 8.266   7.873   -31.901 1.000 20.190 ? 224 LEU A CD2 1 ? 11 
ATOM   1730 N  N   . ALA A 1 225 ? 11.888  4.628   -34.487 1.000 17.590 ? 225 ALA A N   1 ? 11 
ATOM   1731 C  CA  . ALA A 1 225 ? 12.129  3.657   -35.567 1.000 18.175 ? 225 ALA A CA  1 ? 11 
ATOM   1732 C  C   . ALA A 1 225 ? 12.039  2.250   -34.991 1.000 18.423 ? 225 ALA A C   1 ? 11 
ATOM   1733 O  O   . ALA A 1 225 ? 11.589  1.333   -35.660 1.000 17.789 ? 225 ALA A O   1 ? 11 
ATOM   1734 C  CB  . ALA A 1 225 ? 13.488  3.854   -36.199 1.000 18.878 ? 225 ALA A CB  1 ? 11 
ATOM   1735 N  N   . PHE A 1 226 ? 12.507  2.050   -33.769 1.000 18.060 ? 226 PHE A N   1 ? 11 
ATOM   1736 C  CA  . PHE A 1 226 ? 12.399  0.715   -33.127 1.000 19.684 ? 226 PHE A CA  1 ? 11 
ATOM   1737 C  C   . PHE A 1 226 ? 10.928  0.296   -33.064 1.000 18.351 ? 226 PHE A C   1 ? 11 
ATOM   1738 O  O   . PHE A 1 226 ? 10.601  -0.890  -33.311 1.000 19.276 ? 226 PHE A O   1 ? 11 
ATOM   1739 C  CB  . PHE A 1 226 ? 12.914  0.748   -31.687 1.000 19.716 ? 226 PHE A CB  1 ? 11 
ATOM   1740 C  CG  . PHE A 1 226 ? 12.720  -0.561  -30.960 1.000 20.746 ? 226 PHE A CG  1 ? 11 
ATOM   1741 C  CD1 . PHE A 1 226 ? 13.646  -1.566  -31.096 1.000 23.130 ? 226 PHE A CD1 1 ? 11 
ATOM   1742 C  CD2 . PHE A 1 226 ? 11.599  -0.782  -30.152 1.000 21.306 ? 226 PHE A CD2 1 ? 11 
ATOM   1743 C  CE1 . PHE A 1 226 ? 13.458  -2.805  -30.489 1.000 25.543 ? 226 PHE A CE1 1 ? 11 
ATOM   1744 C  CE2 . PHE A 1 226 ? 11.405  -2.003  -29.519 1.000 22.992 ? 226 PHE A CE2 1 ? 11 
ATOM   1745 C  CZ  . PHE A 1 226 ? 12.307  -3.031  -29.741 1.000 25.561 ? 226 PHE A CZ  1 ? 11 
ATOM   1746 N  N   . HIS A 1 227 ? 10.029  1.217   -32.778 1.000 17.067 ? 227 HIS A N   1 ? 11 
ATOM   1747 C  CA  . HIS A 1 227 ? 8.570   0.926   -32.689 1.000 18.046 ? 227 HIS A CA  1 ? 11 
ATOM   1748 C  C   . HIS A 1 227 ? 7.958   0.791   -34.087 1.000 17.949 ? 227 HIS A C   1 ? 11 
ATOM   1749 O  O   . HIS A 1 227 ? 7.018   -0.004  -34.277 1.000 17.964 ? 227 HIS A O   1 ? 11 
ATOM   1750 C  CB  . HIS A 1 227 ? 7.871   1.903   -31.773 1.000 18.903 ? 227 HIS A CB  1 ? 11 
ATOM   1751 C  CG  . HIS A 1 227 ? 8.256   1.729   -30.349 1.000 21.743 ? 227 HIS A CG  1 ? 11 
ATOM   1752 N  ND1 . HIS A 1 227 ? 9.407   2.299   -29.800 1.000 20.105 ? 227 HIS A ND1 1 ? 11 
ATOM   1753 C  CD2 . HIS A 1 227 ? 7.634   1.078   -29.345 1.000 25.994 ? 227 HIS A CD2 1 ? 11 
ATOM   1754 C  CE1 . HIS A 1 227 ? 9.478   1.922   -28.505 1.000 22.741 ? 227 HIS A CE1 1 ? 11 
ATOM   1755 N  NE2 . HIS A 1 227 ? 8.405   1.235   -28.203 1.000 26.672 ? 227 HIS A NE2 1 ? 11 
ATOM   1756 N  N   . GLN A 1 228 ? 8.407   1.598   -35.049 1.000 17.603 ? 228 GLN A N   1 ? 11 
ATOM   1757 C  CA  . GLN A 1 228 ? 8.004   1.416   -36.458 1.000 17.501 ? 228 GLN A CA  1 ? 11 
ATOM   1758 C  C   . GLN A 1 228 ? 8.267   -0.045  -36.875 1.000 17.377 ? 228 GLN A C   1 ? 11 
ATOM   1759 O  O   . GLN A 1 228 ? 7.397   -0.740  -37.454 1.000 18.112 ? 228 GLN A O   1 ? 11 
ATOM   1760 C  CB  . GLN A 1 228 ? 8.754   2.418   -37.329 1.000 17.789 ? 228 GLN A CB  1 ? 11 
ATOM   1761 C  CG  . GLN A 1 228 ? 8.284   2.334   -38.783 1.000 18.199 ? 228 GLN A CG  1 ? 11 
ATOM   1762 C  CD  . GLN A 1 228 ? 9.171   3.122   -39.737 1.000 19.808 ? 228 GLN A CD  1 ? 11 
ATOM   1763 O  OE1 . GLN A 1 228 ? 10.401  3.039   -39.599 1.000 19.697 ? 228 GLN A OE1 1 ? 11 
ATOM   1764 N  NE2 . GLN A 1 228 ? 8.603   3.905   -40.626 1.000 19.672 ? 228 GLN A NE2 1 ? 11 
ATOM   1765 N  N   . ASN A 1 229 ? 9.480   -0.535  -36.626 1.000 17.141 ? 229 ASN A N   1 ? 11 
ATOM   1766 C  CA  . ASN A 1 229 ? 9.870   -1.911  -36.986 1.000 16.715 ? 229 ASN A CA  1 ? 11 
ATOM   1767 C  C   . ASN A 1 229 ? 9.099   -2.941  -36.154 1.000 18.161 ? 229 ASN A C   1 ? 11 
ATOM   1768 O  O   . ASN A 1 229 ? 8.681   -3.968  -36.669 1.000 18.464 ? 229 ASN A O   1 ? 11 
ATOM   1769 C  CB  . ASN A 1 229 ? 11.379  -2.102  -36.875 1.000 17.615 ? 229 ASN A CB  1 ? 11 
ATOM   1770 C  CG  . ASN A 1 229 ? 11.843  -3.434  -37.336 1.000 18.572 ? 229 ASN A CG  1 ? 11 
ATOM   1771 O  OD1 . ASN A 1 229 ? 11.489  -3.862  -38.444 1.000 19.864 ? 229 ASN A OD1 1 ? 11 
ATOM   1772 N  ND2 . ASN A 1 229 ? 12.699  -4.073  -36.517 1.000 21.278 ? 229 ASN A ND2 1 ? 11 
ATOM   1773 N  N   A SER A 1 230 ? 9.003   -2.701  -34.857 0.500 17.864 ? 230 SER A N   1 ? 11 
ATOM   1774 N  N   B SER A 1 230 ? 8.981   -2.719  -34.848 0.500 18.816 ? 230 SER A N   1 ? 11 
ATOM   1775 C  CA  A SER A 1 230 ? 8.564   -3.742  -33.895 0.500 18.142 ? 230 SER A CA  1 ? 11 
ATOM   1776 C  CA  B SER A 1 230 ? 8.571   -3.809  -33.918 0.500 19.725 ? 230 SER A CA  1 ? 11 
ATOM   1777 C  C   A SER A 1 230 ? 7.043   -3.904  -33.943 0.500 17.845 ? 230 SER A C   1 ? 11 
ATOM   1778 C  C   B SER A 1 230 ? 7.035   -3.900  -33.782 0.500 18.870 ? 230 SER A C   1 ? 11 
ATOM   1779 O  O   A SER A 1 230 ? 6.566   -5.061  -33.941 0.500 18.469 ? 230 SER A O   1 ? 11 
ATOM   1780 O  O   B SER A 1 230 ? 6.537   -4.991  -33.462 0.500 19.347 ? 230 SER A O   1 ? 11 
ATOM   1781 C  CB  A SER A 1 230 ? 9.040   -3.459  -32.547 0.500 18.487 ? 230 SER A CB  1 ? 11 
ATOM   1782 C  CB  B SER A 1 230 ? 9.259   -3.737  -32.594 0.500 21.158 ? 230 SER A CB  1 ? 11 
ATOM   1783 O  OG  A SER A 1 230 ? 10.453  -3.567  -32.502 0.500 18.289 ? 230 SER A OG  1 ? 11 
ATOM   1784 O  OG  B SER A 1 230 ? 8.949   -2.552  -31.887 0.500 22.157 ? 230 SER A OG  1 ? 11 
ATOM   1785 N  N   . MET A 1 231 ? 6.331   -2.775  -33.970 1.000 17.455 ? 231 MET A N   1 ? 11 
ATOM   1786 C  CA  . MET A 1 231 ? 4.861   -2.751  -34.054 1.000 18.444 ? 231 MET A CA  1 ? 11 
ATOM   1787 C  C   . MET A 1 231 ? 4.411   -2.850  -35.529 1.000 18.168 ? 231 MET A C   1 ? 11 
ATOM   1788 O  O   . MET A 1 231 ? 3.277   -3.288  -35.790 1.000 19.312 ? 231 MET A O   1 ? 11 
ATOM   1789 C  CB  . MET A 1 231 ? 4.297   -1.503  -33.435 1.000 19.665 ? 231 MET A CB  1 ? 11 
ATOM   1790 C  CG  . MET A 1 231 ? 4.495   -1.454  -31.896 1.000 21.885 ? 231 MET A CG  1 ? 11 
ATOM   1791 S  SD  . MET A 1 231 ? 4.385   0.178   -31.197 1.000 25.716 ? 231 MET A SD  1 ? 11 
ATOM   1792 C  CE  . MET A 1 231 ? 2.880   0.737   -31.927 1.000 25.369 ? 231 MET A CE  1 ? 11 
ATOM   1793 N  N   . GLY A 1 232 ? 5.257   -2.426  -36.469 1.000 17.351 ? 232 GLY A N   1 ? 12 
ATOM   1794 C  CA  . GLY A 1 232 ? 5.021   -2.705  -37.883 1.000 16.001 ? 232 GLY A CA  1 ? 12 
ATOM   1795 C  C   . GLY A 1 232 ? 3.907   -1.935  -38.532 1.000 16.198 ? 232 GLY A C   1 ? 12 
ATOM   1796 O  O   . GLY A 1 232 ? 3.477   -2.393  -39.610 1.000 16.359 ? 232 GLY A O   1 ? 12 
ATOM   1797 N  N   . ALA A 1 233 ? 3.555   -0.752  -38.108 1.000 16.240 ? 233 ALA A N   1 ? 12 
ATOM   1798 C  CA  . ALA A 1 233 ? 2.433   -0.021  -38.700 1.000 15.962 ? 233 ALA A CA  1 ? 12 
ATOM   1799 C  C   . ALA A 1 233 ? 2.974   0.873   -39.828 1.000 15.969 ? 233 ALA A C   1 ? 12 
ATOM   1800 O  O   . ALA A 1 233 ? 2.641   2.092   -39.864 1.000 16.891 ? 233 ALA A O   1 ? 12 
ATOM   1801 C  CB  . ALA A 1 233 ? 1.682   0.747   -37.655 1.000 17.178 ? 233 ALA A CB  1 ? 12 
ATOM   1802 N  N   . VAL A 1 234 ? 3.618   0.264   -40.784 1.000 16.455 ? 234 VAL A N   1 ? 12 
ATOM   1803 C  CA  . VAL A 1 234 ? 4.386   0.975   -41.828 1.000 16.548 ? 234 VAL A CA  1 ? 12 
ATOM   1804 C  C   . VAL A 1 234 ? 3.451   1.365   -42.989 1.000 15.076 ? 234 VAL A C   1 ? 12 
ATOM   1805 O  O   . VAL A 1 234 ? 2.476   0.712   -43.293 1.000 16.216 ? 234 VAL A O   1 ? 12 
ATOM   1806 C  CB  . VAL A 1 234 ? 5.587   0.171   -42.326 1.000 17.552 ? 234 VAL A CB  1 ? 12 
ATOM   1807 C  CG1 . VAL A 1 234 ? 6.594   -0.008  -41.194 1.000 18.827 ? 234 VAL A CG1 1 ? 12 
ATOM   1808 C  CG2 . VAL A 1 234 ? 5.182   -1.185  -42.936 1.000 18.121 ? 234 VAL A CG2 1 ? 12 
ATOM   1809 N  N   . ALA A 1 235 ? 3.827   2.446   -43.659 1.000 15.184 ? 235 ALA A N   1 ? 12 
ATOM   1810 C  CA  . ALA A 1 235 ? 3.333   2.764   -45.001 1.000 15.975 ? 235 ALA A CA  1 ? 12 
ATOM   1811 C  C   . ALA A 1 235 ? 3.907   1.731   -45.980 1.000 16.232 ? 235 ALA A C   1 ? 12 
ATOM   1812 O  O   . ALA A 1 235 ? 5.110   1.547   -46.032 1.000 16.611 ? 235 ALA A O   1 ? 12 
ATOM   1813 C  CB  . ALA A 1 235 ? 3.732   4.150   -45.413 1.000 16.759 ? 235 ALA A CB  1 ? 12 
ATOM   1814 N  N   . GLY A 1 236 ? 3.037   1.141   -46.792 1.000 15.615 ? 236 GLY A N   1 ? 12 
ATOM   1815 C  CA  . GLY A 1 236 ? 3.510   0.265   -47.847 1.000 16.229 ? 236 GLY A CA  1 ? 12 
ATOM   1816 C  C   . GLY A 1 236 ? 4.136   1.086   -48.983 1.000 16.034 ? 236 GLY A C   1 ? 12 
ATOM   1817 O  O   . GLY A 1 236 ? 3.944   2.304   -49.086 1.000 16.232 ? 236 GLY A O   1 ? 12 
ATOM   1818 N  N   . PRO A 1 237 ? 4.979   0.456   -49.814 1.000 15.762 ? 237 PRO A N   1 ? 12 
ATOM   1819 C  CA  . PRO A 1 237 ? 5.762   1.200   -50.780 1.000 15.942 ? 237 PRO A CA  1 ? 12 
ATOM   1820 C  C   . PRO A 1 237 ? 4.944   1.943   -51.840 1.000 15.760 ? 237 PRO A C   1 ? 12 
ATOM   1821 O  O   . PRO A 1 237 ? 5.294   3.054   -52.207 1.000 16.489 ? 237 PRO A O   1 ? 12 
ATOM   1822 C  CB  . PRO A 1 237 ? 6.685   0.165   -51.377 1.000 17.889 ? 237 PRO A CB  1 ? 12 
ATOM   1823 C  CG  . PRO A 1 237 ? 6.094   -1.123  -51.072 1.000 18.732 ? 237 PRO A CG  1 ? 12 
ATOM   1824 C  CD  . PRO A 1 237 ? 5.348   -0.952  -49.751 1.000 16.989 ? 237 PRO A CD  1 ? 12 
ATOM   1825 N  N   . PHE A 1 238 ? 3.831   1.337   -52.307 1.000 16.833 ? 238 PHE A N   1 ? 12 
ATOM   1826 C  CA  A PHE A 1 238 ? 3.044   2.052   -53.349 0.500 17.094 ? 238 PHE A CA  1 ? 12 
ATOM   1827 C  CA  B PHE A 1 238 ? 2.971   1.973   -53.321 0.500 17.312 ? 238 PHE A CA  1 ? 12 
ATOM   1828 C  C   . PHE A 1 238 ? 2.349   3.263   -52.735 1.000 17.075 ? 238 PHE A C   1 ? 12 
ATOM   1829 O  O   . PHE A 1 238 ? 2.314   4.365   -53.322 1.000 17.082 ? 238 PHE A O   1 ? 12 
ATOM   1830 C  CB  A PHE A 1 238 ? 2.016   1.214   -54.093 0.500 17.576 ? 238 PHE A CB  1 ? 12 
ATOM   1831 C  CB  B PHE A 1 238 ? 2.001   0.882   -53.758 0.500 18.084 ? 238 PHE A CB  1 ? 12 
ATOM   1832 C  CG  A PHE A 1 238 ? 1.190   2.051   -55.047 0.500 18.223 ? 238 PHE A CG  1 ? 12 
ATOM   1833 C  CG  B PHE A 1 238 ? 1.082   1.268   -54.871 0.500 19.469 ? 238 PHE A CG  1 ? 12 
ATOM   1834 C  CD1 A PHE A 1 238 ? 1.773   2.698   -56.136 0.500 18.811 ? 238 PHE A CD1 1 ? 12 
ATOM   1835 C  CD1 B PHE A 1 238 ? 1.468   1.060   -56.186 0.500 21.102 ? 238 PHE A CD1 1 ? 12 
ATOM   1836 C  CD2 A PHE A 1 238 ? -0.176  2.173   -54.893 0.500 20.696 ? 238 PHE A CD2 1 ? 12 
ATOM   1837 C  CD2 B PHE A 1 238 ? -0.213  1.641   -54.621 0.500 21.318 ? 238 PHE A CD2 1 ? 12 
ATOM   1838 C  CE1 A PHE A 1 238 ? 1.016   3.454   -57.012 0.500 19.098 ? 238 PHE A CE1 1 ? 12 
ATOM   1839 C  CE1 B PHE A 1 238 ? 0.615   1.380   -57.227 0.500 22.972 ? 238 PHE A CE1 1 ? 12 
ATOM   1840 C  CE2 A PHE A 1 238 ? -0.939  2.862   -55.821 0.500 20.364 ? 238 PHE A CE2 1 ? 12 
ATOM   1841 C  CE2 B PHE A 1 238 ? -1.063  1.952   -55.674 0.500 21.563 ? 238 PHE A CE2 1 ? 12 
ATOM   1842 C  CZ  A PHE A 1 238 ? -0.361  3.484   -56.893 0.500 20.432 ? 238 PHE A CZ  1 ? 12 
ATOM   1843 C  CZ  B PHE A 1 238 ? -0.656  1.822   -56.962 0.500 21.781 ? 238 PHE A CZ  1 ? 12 
ATOM   1844 N  N   . ASP A 1 239 ? 1.771   3.116   -51.514 1.000 16.130 ? 239 ASP A N   1 ? 12 
ATOM   1845 C  CA  . ASP A 1 239 ? 1.155   4.267   -50.838 1.000 16.808 ? 239 ASP A CA  1 ? 12 
ATOM   1846 C  C   . ASP A 1 239 ? 2.225   5.320   -50.573 1.000 16.061 ? 239 ASP A C   1 ? 12 
ATOM   1847 O  O   . ASP A 1 239 ? 2.005   6.529   -50.790 1.000 16.261 ? 239 ASP A O   1 ? 12 
ATOM   1848 C  CB  . ASP A 1 239 ? 0.475   3.849   -49.514 1.000 16.967 ? 239 ASP A CB  1 ? 12 
ATOM   1849 C  CG  . ASP A 1 239 ? -0.820  3.084   -49.718 1.000 19.611 ? 239 ASP A CG  1 ? 12 
ATOM   1850 O  OD1 . ASP A 1 239 ? -1.639  3.547   -50.565 1.000 22.363 ? 239 ASP A OD1 1 ? 12 
ATOM   1851 O  OD2 . ASP A 1 239 ? -0.998  2.061   -49.095 1.000 18.983 ? 239 ASP A OD2 1 ? 12 
ATOM   1852 N  N   . ALA A 1 240 ? 3.422   4.953   -50.096 1.000 15.079 ? 240 ALA A N   1 ? 12 
ATOM   1853 C  CA  . ALA A 1 240 ? 4.495   5.894   -49.854 1.000 14.965 ? 240 ALA A CA  1 ? 12 
ATOM   1854 C  C   . ALA A 1 240 ? 4.839   6.631   -51.142 1.000 15.720 ? 240 ALA A C   1 ? 12 
ATOM   1855 O  O   . ALA A 1 240 ? 5.080   7.845   -51.121 1.000 15.825 ? 240 ALA A O   1 ? 12 
ATOM   1856 C  CB  . ALA A 1 240 ? 5.704   5.179   -49.322 1.000 15.339 ? 240 ALA A CB  1 ? 12 
ATOM   1857 N  N   . TRP A 1 241 ? 4.862   5.883   -52.240 1.000 15.773 ? 241 TRP A N   1 ? 12 
ATOM   1858 C  CA  . TRP A 1 241 ? 5.205   6.436   -53.570 1.000 15.474 ? 241 TRP A CA  1 ? 12 
ATOM   1859 C  C   . TRP A 1 241 ? 4.173   7.470   -54.014 1.000 15.413 ? 241 TRP A C   1 ? 12 
ATOM   1860 O  O   . TRP A 1 241 ? 4.553   8.516   -54.521 1.000 15.697 ? 241 TRP A O   1 ? 12 
ATOM   1861 C  CB  . TRP A 1 241 ? 5.357   5.310   -54.557 1.000 15.620 ? 241 TRP A CB  1 ? 12 
ATOM   1862 C  CG  . TRP A 1 241 ? 5.866   5.740   -55.887 1.000 15.932 ? 241 TRP A CG  1 ? 12 
ATOM   1863 C  CD1 . TRP A 1 241 ? 7.177   5.819   -56.252 1.000 16.345 ? 241 TRP A CD1 1 ? 12 
ATOM   1864 C  CD2 . TRP A 1 241 ? 5.094   6.075   -57.050 1.000 15.905 ? 241 TRP A CD2 1 ? 12 
ATOM   1865 N  NE1 . TRP A 1 241 ? 7.279   6.219   -57.545 1.000 18.119 ? 241 TRP A NE1 1 ? 12 
ATOM   1866 C  CE2 . TRP A 1 241 ? 6.014   6.356   -58.078 1.000 16.677 ? 241 TRP A CE2 1 ? 12 
ATOM   1867 C  CE3 . TRP A 1 241 ? 3.714   6.195   -57.308 1.000 17.305 ? 241 TRP A CE3 1 ? 12 
ATOM   1868 C  CZ2 . TRP A 1 241 ? 5.594   6.746   -59.339 1.000 17.756 ? 241 TRP A CZ2 1 ? 12 
ATOM   1869 C  CZ3 . TRP A 1 241 ? 3.310   6.575   -58.575 1.000 17.706 ? 241 TRP A CZ3 1 ? 12 
ATOM   1870 C  CH2 . TRP A 1 241 ? 4.240   6.813   -59.562 1.000 17.880 ? 241 TRP A CH2 1 ? 12 
ATOM   1871 N  N   . LEU A 1 242 ? 2.902   7.197   -53.803 1.000 15.927 ? 242 LEU A N   1 ? 12 
ATOM   1872 C  CA  . LEU A 1 242 ? 1.848   8.159   -54.185 1.000 15.703 ? 242 LEU A CA  1 ? 12 
ATOM   1873 C  C   . LEU A 1 242 ? 1.905   9.362   -53.277 1.000 15.871 ? 242 LEU A C   1 ? 12 
ATOM   1874 O  O   . LEU A 1 242 ? 1.642   10.497  -53.721 1.000 17.103 ? 242 LEU A O   1 ? 12 
ATOM   1875 C  CB  . LEU A 1 242 ? 0.466   7.503   -54.095 1.000 17.421 ? 242 LEU A CB  1 ? 12 
ATOM   1876 C  CG  . LEU A 1 242 ? 0.090   6.504   -55.161 1.000 20.085 ? 242 LEU A CG  1 ? 12 
ATOM   1877 C  CD1 . LEU A 1 242 ? -1.284  5.895   -54.826 1.000 21.508 ? 242 LEU A CD1 1 ? 12 
ATOM   1878 C  CD2 . LEU A 1 242 ? 0.028   7.192   -56.521 1.000 20.373 ? 242 LEU A CD2 1 ? 12 
ATOM   1879 N  N   . THR A 1 243 ? 2.185   9.161   -51.990 1.000 16.492 ? 243 THR A N   1 ? 12 
ATOM   1880 C  CA  . THR A 1 243 ? 2.311   10.316  -51.056 1.000 16.912 ? 243 THR A CA  1 ? 12 
ATOM   1881 C  C   . THR A 1 243 ? 3.445   11.192  -51.554 1.000 16.395 ? 243 THR A C   1 ? 12 
ATOM   1882 O  O   . THR A 1 243 ? 3.315   12.433  -51.670 1.000 16.756 ? 243 THR A O   1 ? 12 
ATOM   1883 C  CB  . THR A 1 243 ? 2.548   9.778   -49.635 1.000 16.409 ? 243 THR A CB  1 ? 12 
ATOM   1884 O  OG1 . THR A 1 243 ? 1.485   8.909   -49.284 1.000 16.616 ? 243 THR A OG1 1 ? 12 
ATOM   1885 C  CG2 . THR A 1 243 ? 2.734   10.962  -48.696 1.000 16.627 ? 243 THR A CG2 1 ? 12 
ATOM   1886 N  N   . LEU A 1 244 ? 4.592   10.617  -51.880 1.000 16.325 ? 244 LEU A N   1 ? 12 
ATOM   1887 C  CA  . LEU A 1 244 ? 5.760   11.343  -52.362 1.000 17.149 ? 244 LEU A CA  1 ? 12 
ATOM   1888 C  C   . LEU A 1 244 ? 5.386   12.055  -53.677 1.000 16.957 ? 244 LEU A C   1 ? 12 
ATOM   1889 O  O   . LEU A 1 244 ? 5.757   13.219  -53.875 1.000 16.706 ? 244 LEU A O   1 ? 12 
ATOM   1890 C  CB  . LEU A 1 244 ? 6.891   10.361  -52.578 1.000 20.147 ? 244 LEU A CB  1 ? 12 
ATOM   1891 C  CG  . LEU A 1 244 ? 8.231   10.940  -52.893 1.000 23.153 ? 244 LEU A CG  1 ? 12 
ATOM   1892 C  CD1 . LEU A 1 244 ? 8.637   12.032  -51.878 1.000 23.648 ? 244 LEU A CD1 1 ? 12 
ATOM   1893 C  CD2 . LEU A 1 244 ? 9.248   9.828   -52.899 1.000 24.390 ? 244 LEU A CD2 1 ? 12 
ATOM   1894 N  N   . ARG A 1 245 ? 4.664   11.403  -54.577 1.000 15.758 ? 245 ARG A N   1 ? 12 
ATOM   1895 C  CA  . ARG A 1 245 ? 4.216   12.088  -55.817 1.000 16.242 ? 245 ARG A CA  1 ? 12 
ATOM   1896 C  C   . ARG A 1 245 ? 3.385   13.310  -55.489 1.000 15.515 ? 245 ARG A C   1 ? 12 
ATOM   1897 O  O   . ARG A 1 245 ? 3.615   14.397  -56.046 1.000 16.206 ? 245 ARG A O   1 ? 12 
ATOM   1898 C  CB  . ARG A 1 245 ? 3.407   11.128  -56.653 1.000 16.138 ? 245 ARG A CB  1 ? 12 
ATOM   1899 C  CG  . ARG A 1 245 ? 3.084   11.685  -58.050 1.000 15.921 ? 245 ARG A CG  1 ? 12 
ATOM   1900 C  CD  . ARG A 1 245 ? 2.226   10.681  -58.836 1.000 16.812 ? 245 ARG A CD  1 ? 12 
ATOM   1901 N  NE  . ARG A 1 245 ? 2.291   10.841  -60.260 1.000 17.240 ? 245 ARG A NE  1 ? 12 
ATOM   1902 C  CZ  . ARG A 1 245 ? 1.340   11.286  -61.084 1.000 17.406 ? 245 ARG A CZ  1 ? 12 
ATOM   1903 N  NH1 . ARG A 1 245 ? 1.524   11.120  -62.381 1.000 17.571 ? 245 ARG A NH1 1 ? 12 
ATOM   1904 N  NH2 . ARG A 1 245 ? 0.262   11.881  -60.648 1.000 17.910 ? 245 ARG A NH2 1 ? 12 
ATOM   1905 N  N   . GLY A 1 246 ? 2.457   13.190  -54.558 1.000 16.066 ? 246 GLY A N   1 ? 12 
ATOM   1906 C  CA  . GLY A 1 246 ? 1.624   14.309  -54.113 1.000 16.154 ? 246 GLY A CA  1 ? 12 
ATOM   1907 C  C   . GLY A 1 246 ? 2.460   15.451  -53.588 1.000 15.810 ? 246 GLY A C   1 ? 12 
ATOM   1908 O  O   . GLY A 1 246 ? 2.219   16.670  -53.906 1.000 15.567 ? 246 GLY A O   1 ? 12 
ATOM   1909 N  N   . ILE A 1 247 ? 3.487   15.130  -52.801 1.000 15.787 ? 247 ILE A N   1 ? 12 
ATOM   1910 C  CA  . ILE A 1 247 ? 4.340   16.168  -52.150 1.000 16.619 ? 247 ILE A CA  1 ? 12 
ATOM   1911 C  C   . ILE A 1 247 ? 4.978   17.075  -53.183 1.000 16.561 ? 247 ILE A C   1 ? 12 
ATOM   1912 O  O   . ILE A 1 247 ? 5.162   18.295  -52.905 1.000 17.213 ? 247 ILE A O   1 ? 12 
ATOM   1913 C  CB  . ILE A 1 247 ? 5.370   15.498  -51.227 1.000 17.116 ? 247 ILE A CB  1 ? 12 
ATOM   1914 C  CG1 . ILE A 1 247 ? 4.662   14.946  -49.992 1.000 17.072 ? 247 ILE A CG1 1 ? 12 
ATOM   1915 C  CG2 . ILE A 1 247 ? 6.527   16.431  -50.918 1.000 18.274 ? 247 ILE A CG2 1 ? 12 
ATOM   1916 C  CD1 . ILE A 1 247 ? 5.516   14.000  -49.161 1.000 17.677 ? 247 ILE A CD1 1 ? 12 
ATOM   1917 N  N   . LYS A 1 248 ? 5.271   16.561  -54.375 1.000 16.269 ? 248 LYS A N   1 ? 12 
ATOM   1918 C  CA  . LYS A 1 248 ? 5.891   17.359  -55.428 1.000 16.338 ? 248 LYS A CA  1 ? 12 
ATOM   1919 C  C   . LYS A 1 248 ? 5.095   18.583  -55.800 1.000 15.749 ? 248 LYS A C   1 ? 12 
ATOM   1920 O  O   . LYS A 1 248 ? 5.695   19.525  -56.294 1.000 17.757 ? 248 LYS A O   1 ? 12 
ATOM   1921 C  CB  . LYS A 1 248 ? 6.175   16.477  -56.659 1.000 17.219 ? 248 LYS A CB  1 ? 12 
ATOM   1922 C  CG  . LYS A 1 248 ? 7.148   15.350  -56.306 1.000 19.611 ? 248 LYS A CG  1 ? 12 
ATOM   1923 C  CD  . LYS A 1 248 ? 7.493   14.443  -57.502 1.000 22.816 ? 248 LYS A CD  1 ? 12 
ATOM   1924 C  CE  . LYS A 1 248 ? 8.225   13.184  -57.088 1.000 24.079 ? 248 LYS A CE  1 ? 12 
ATOM   1925 N  NZ  . LYS A 1 248 ? 8.538   12.387  -58.298 1.000 25.826 ? 248 LYS A NZ  1 ? 12 
ATOM   1926 N  N   . THR A 1 249 ? 3.787   18.564  -55.662 1.000 15.799 ? 249 THR A N   1 ? 12 
ATOM   1927 C  CA  . THR A 1 249 ? 2.941   19.708  -56.014 1.000 16.839 ? 249 THR A CA  1 ? 12 
ATOM   1928 C  C   . THR A 1 249 ? 2.398   20.414  -54.750 1.000 16.303 ? 249 THR A C   1 ? 12 
ATOM   1929 O  O   . THR A 1 249 ? 1.486   21.223  -54.886 1.000 16.356 ? 249 THR A O   1 ? 12 
ATOM   1930 C  CB  . THR A 1 249 ? 1.771   19.325  -56.917 1.000 16.682 ? 249 THR A CB  1 ? 12 
ATOM   1931 O  OG1 . THR A 1 249 ? 1.010   18.266  -56.364 1.000 15.865 ? 249 THR A OG1 1 ? 12 
ATOM   1932 C  CG2 . THR A 1 249 ? 2.268   18.940  -58.289 1.000 17.425 ? 249 THR A CG2 1 ? 12 
ATOM   1933 N  N   . LEU A 1 250 ? 2.873   20.106  -53.559 1.000 16.740 ? 250 LEU A N   1 ? 12 
ATOM   1934 C  CA  . LEU A 1 250 ? 2.310   20.747  -52.351 1.000 15.923 ? 250 LEU A CA  1 ? 12 
ATOM   1935 C  C   . LEU A 1 250 ? 2.320   22.274  -52.484 1.000 16.747 ? 250 LEU A C   1 ? 12 
ATOM   1936 O  O   . LEU A 1 250 ? 1.325   22.909  -52.133 1.000 17.033 ? 250 LEU A O   1 ? 12 
ATOM   1937 C  CB  . LEU A 1 250 ? 3.051   20.283  -51.089 1.000 16.498 ? 250 LEU A CB  1 ? 12 
ATOM   1938 C  CG  . LEU A 1 250 ? 2.621   20.952  -49.801 1.000 17.051 ? 250 LEU A CG  1 ? 12 
ATOM   1939 C  CD1 . LEU A 1 250 ? 1.163   20.625  -49.466 1.000 19.215 ? 250 LEU A CD1 1 ? 12 
ATOM   1940 C  CD2 . LEU A 1 250 ? 3.497   20.512  -48.690 1.000 19.260 ? 250 LEU A CD2 1 ? 12 
ATOM   1941 N  N   . GLY A 1 251 ? 3.446   22.850  -52.862 1.000 17.529 ? 251 GLY A N   1 ? 12 
ATOM   1942 C  CA  . GLY A 1 251 ? 3.527   24.317  -52.938 1.000 17.729 ? 251 GLY A CA  1 ? 12 
ATOM   1943 C  C   . GLY A 1 251 ? 2.465   24.920  -53.843 1.000 18.288 ? 251 GLY A C   1 ? 12 
ATOM   1944 O  O   . GLY A 1 251 ? 1.735   25.849  -53.449 1.000 18.251 ? 251 GLY A O   1 ? 12 
ATOM   1945 N  N   . VAL A 1 252 ? 2.387   24.432  -55.081 1.000 17.342 ? 252 VAL A N   1 ? 12 
ATOM   1946 C  CA  . VAL A 1 252 ? 1.442   25.020  -56.033 1.000 17.557 ? 252 VAL A CA  1 ? 12 
ATOM   1947 C  C   . VAL A 1 252 ? 0.015   24.712  -55.619 1.000 17.627 ? 252 VAL A C   1 ? 12 
ATOM   1948 O  O   . VAL A 1 252 ? -0.848  25.574  -55.793 1.000 18.820 ? 252 VAL A O   1 ? 12 
ATOM   1949 C  CB  . VAL A 1 252 ? 1.720   24.620  -57.487 1.000 18.191 ? 252 VAL A CB  1 ? 12 
ATOM   1950 C  CG1 . VAL A 1 252 ? 3.026   25.223  -57.985 1.000 19.244 ? 252 VAL A CG1 1 ? 12 
ATOM   1951 C  CG2 . VAL A 1 252 ? 1.699   23.116  -57.723 1.000 17.685 ? 252 VAL A CG2 1 ? 12 
ATOM   1952 N  N   . ARG A 1 253 ? -0.256  23.563  -55.045 1.000 16.571 ? 253 ARG A N   1 ? 12 
ATOM   1953 C  CA  . ARG A 1 253 ? -1.603  23.269  -54.572 1.000 16.599 ? 253 ARG A CA  1 ? 12 
ATOM   1954 C  C   . ARG A 1 253 ? -1.959  24.201  -53.416 1.000 17.609 ? 253 ARG A C   1 ? 12 
ATOM   1955 O  O   . ARG A 1 253 ? -3.041  24.797  -53.430 1.000 17.512 ? 253 ARG A O   1 ? 12 
ATOM   1956 C  CB  . ARG A 1 253 ? -1.773  21.798  -54.180 1.000 16.388 ? 253 ARG A CB  1 ? 12 
ATOM   1957 C  CG  . ARG A 1 253 ? -1.723  20.802  -55.327 1.000 15.916 ? 253 ARG A CG  1 ? 12 
ATOM   1958 C  CD  . ARG A 1 253 ? -1.975  19.378  -54.905 1.000 15.971 ? 253 ARG A CD  1 ? 12 
ATOM   1959 N  NE  . ARG A 1 253 ? -0.851  18.804  -54.216 1.000 16.134 ? 253 ARG A NE  1 ? 12 
ATOM   1960 C  CZ  . ARG A 1 253 ? -0.729  18.629  -52.893 1.000 16.493 ? 253 ARG A CZ  1 ? 12 
ATOM   1961 N  NH1 . ARG A 1 253 ? -1.687  19.012  -52.074 1.000 15.780 ? 253 ARG A NH1 1 ? 12 
ATOM   1962 N  NH2 . ARG A 1 253 ? 0.338   18.011  -52.389 1.000 16.799 ? 253 ARG A NH2 1 ? 12 
ATOM   1963 N  N   A MET A 1 254 ? -1.099  24.249  -52.393 0.600 16.004 ? 254 MET A N   1 ? 13 
ATOM   1964 N  N   B MET A 1 254 ? -1.101  24.262  -52.387 0.400 17.781 ? 254 MET A N   1 ? 13 
ATOM   1965 C  CA  A MET A 1 254 ? -1.421  25.047  -51.194 0.600 16.118 ? 254 MET A CA  1 ? 13 
ATOM   1966 C  CA  B MET A 1 254 ? -1.445  24.986  -51.138 0.400 19.150 ? 254 MET A CA  1 ? 13 
ATOM   1967 C  C   A MET A 1 254 ? -1.618  26.507  -51.605 0.600 17.894 ? 254 MET A C   1 ? 13 
ATOM   1968 C  C   B MET A 1 254 ? -1.460  26.519  -51.422 0.400 19.298 ? 254 MET A C   1 ? 13 
ATOM   1969 O  O   A MET A 1 254 ? -2.599  27.156  -51.129 0.600 17.749 ? 254 MET A O   1 ? 13 
ATOM   1970 O  O   B MET A 1 254 ? -2.265  27.209  -50.760 0.400 18.785 ? 254 MET A O   1 ? 13 
ATOM   1971 C  CB  A MET A 1 254 ? -0.362  24.906  -50.112 0.600 15.292 ? 254 MET A CB  1 ? 13 
ATOM   1972 C  CB  B MET A 1 254 ? -0.558  24.540  -49.950 0.400 21.066 ? 254 MET A CB  1 ? 13 
ATOM   1973 C  CG  A MET A 1 254 ? -0.840  25.439  -48.773 0.600 15.268 ? 254 MET A CG  1 ? 13 
ATOM   1974 C  CG  B MET A 1 254 ? -1.110  23.216  -49.123 0.400 22.455 ? 254 MET A CG  1 ? 13 
ATOM   1975 S  SD  A MET A 1 254 ? -2.426  24.916  -48.163 0.600 15.671 ? 254 MET A SD  1 ? 13 
ATOM   1976 S  SD  B MET A 1 254 ? -1.740  23.694  -47.502 0.400 31.210 ? 254 MET A SD  1 ? 13 
ATOM   1977 C  CE  A MET A 1 254 ? -2.083  23.689  -46.895 0.600 17.951 ? 254 MET A CE  1 ? 13 
ATOM   1978 C  CE  B MET A 1 254 ? -2.735  25.086  -48.017 0.400 26.786 ? 254 MET A CE  1 ? 13 
ATOM   1979 N  N   . ASP A 1 255 ? -0.750  27.038  -52.451 1.000 17.700 ? 255 ASP A N   1 ? 13 
ATOM   1980 C  CA  . ASP A 1 255 ? -0.955  28.439  -52.945 1.000 19.609 ? 255 ASP A CA  1 ? 13 
ATOM   1981 C  C   . ASP A 1 255 ? -2.398  28.602  -53.392 1.000 19.244 ? 255 ASP A C   1 ? 13 
ATOM   1982 O  O   . ASP A 1 255 ? -3.052  29.652  -53.062 1.000 20.289 ? 255 ASP A O   1 ? 13 
ATOM   1983 C  CB  . ASP A 1 255 ? 0.036   28.874  -54.032 1.000 19.597 ? 255 ASP A CB  1 ? 13 
ATOM   1984 C  CG  . ASP A 1 255 ? 1.430   29.089  -53.547 1.000 21.633 ? 255 ASP A CG  1 ? 13 
ATOM   1985 O  OD1 . ASP A 1 255 ? 1.633   29.315  -52.288 1.000 21.203 ? 255 ASP A OD1 1 ? 13 
ATOM   1986 O  OD2 . ASP A 1 255 ? 2.311   29.171  -54.403 1.000 24.336 ? 255 ASP A OD2 1 ? 13 
ATOM   1987 N  N   . ARG A 1 256 ? -2.895  27.691  -54.179 1.000 18.512 ? 256 ARG A N   1 ? 13 
ATOM   1988 C  CA  . ARG A 1 256 ? -4.242  27.847  -54.745 1.000 18.748 ? 256 ARG A CA  1 ? 13 
ATOM   1989 C  C   . ARG A 1 256 ? -5.292  27.559  -53.672 1.000 18.939 ? 256 ARG A C   1 ? 13 
ATOM   1990 O  O   . ARG A 1 256 ? -6.344  28.232  -53.683 1.000 19.704 ? 256 ARG A O   1 ? 13 
ATOM   1991 C  CB  . ARG A 1 256 ? -4.416  26.916  -55.949 1.000 18.429 ? 256 ARG A CB  1 ? 13 
ATOM   1992 C  CG  . ARG A 1 256 ? -5.741  27.100  -56.676 1.000 19.532 ? 256 ARG A CG  1 ? 13 
ATOM   1993 C  CD  . ARG A 1 256 ? -5.970  28.489  -57.226 1.000 20.243 ? 256 ARG A CD  1 ? 13 
ATOM   1994 N  NE  . ARG A 1 256 ? -4.822  28.922  -58.025 1.000 21.817 ? 256 ARG A NE  1 ? 13 
ATOM   1995 C  CZ  . ARG A 1 256 ? -4.589  28.616  -59.306 1.000 22.869 ? 256 ARG A CZ  1 ? 13 
ATOM   1996 N  NH1 . ARG A 1 256 ? -5.457  27.926  -60.013 1.000 22.954 ? 256 ARG A NH1 1 ? 13 
ATOM   1997 N  NH2 . ARG A 1 256 ? -3.455  28.962  -59.869 1.000 23.526 ? 256 ARG A NH2 1 ? 13 
ATOM   1998 N  N   . HIS A 1 257 ? -5.082  26.580  -52.776 1.000 17.989 ? 257 HIS A N   1 ? 13 
ATOM   1999 C  CA  . HIS A 1 257 ? -6.015  26.343  -51.663 1.000 18.263 ? 257 HIS A CA  1 ? 13 
ATOM   2000 C  C   . HIS A 1 257 ? -6.182  27.651  -50.875 1.000 18.524 ? 257 HIS A C   1 ? 13 
ATOM   2001 O  O   . HIS A 1 257 ? -7.319  27.988  -50.472 1.000 19.132 ? 257 HIS A O   1 ? 13 
ATOM   2002 C  CB  . HIS A 1 257 ? -5.499  25.273  -50.730 1.000 17.588 ? 257 HIS A CB  1 ? 13 
ATOM   2003 C  CG  . HIS A 1 257 ? -5.578  23.855  -51.211 1.000 16.978 ? 257 HIS A CG  1 ? 13 
ATOM   2004 N  ND1 . HIS A 1 257 ? -6.795  23.226  -51.414 1.000 18.107 ? 257 HIS A ND1 1 ? 13 
ATOM   2005 C  CD2 . HIS A 1 257 ? -4.614  22.935  -51.431 1.000 17.622 ? 257 HIS A CD2 1 ? 13 
ATOM   2006 C  CE1 . HIS A 1 257 ? -6.550  21.948  -51.706 1.000 19.306 ? 257 HIS A CE1 1 ? 13 
ATOM   2007 N  NE2 . HIS A 1 257 ? -5.243  21.737  -51.757 1.000 18.288 ? 257 HIS A NE2 1 ? 13 
ATOM   2008 N  N   . CYS A 1 258 ? -5.101  28.339  -50.583 1.000 18.462 ? 258 CYS A N   1 ? 13 
ATOM   2009 C  CA  . CYS A 1 258 ? -5.134  29.571  -49.725 1.000 19.836 ? 258 CYS A CA  1 ? 13 
ATOM   2010 C  C   . CYS A 1 258 ? -5.866  30.685  -50.458 1.000 21.729 ? 258 CYS A C   1 ? 13 
ATOM   2011 O  O   . CYS A 1 258 ? -6.753  31.355  -49.875 1.000 22.012 ? 258 CYS A O   1 ? 13 
ATOM   2012 C  CB  . CYS A 1 258 ? -3.725  30.013  -49.322 1.000 21.604 ? 258 CYS A CB  1 ? 13 
ATOM   2013 S  SG  . CYS A 1 258 ? -2.938  28.890  -48.128 1.000 22.645 ? 258 CYS A SG  1 ? 13 
ATOM   2014 N  N   . ALA A 1 259 ? -5.566  30.857  -51.732 1.000 20.135 ? 259 ALA A N   1 ? 13 
ATOM   2015 C  CA  . ALA A 1 259 ? -6.253  31.916  -52.517 1.000 21.310 ? 259 ALA A CA  1 ? 13 
ATOM   2016 C  C   . ALA A 1 259 ? -7.749  31.592  -52.645 1.000 21.151 ? 259 ALA A C   1 ? 13 
ATOM   2017 O  O   . ALA A 1 259 ? -8.541  32.498  -52.463 1.000 22.428 ? 259 ALA A O   1 ? 13 
ATOM   2018 C  CB  . ALA A 1 259 ? -5.612  32.059  -53.860 1.000 23.917 ? 259 ALA A CB  1 ? 13 
ATOM   2019 N  N   . ASN A 1 260 ? -8.110  30.345  -52.911 1.000 19.811 ? 260 ASN A N   1 ? 13 
ATOM   2020 C  CA  . ASN A 1 260 ? -9.538  29.969  -53.055 1.000 18.953 ? 260 ASN A CA  1 ? 13 
ATOM   2021 C  C   . ASN A 1 260 ? -10.252 30.098  -51.710 1.000 19.839 ? 260 ASN A C   1 ? 13 
ATOM   2022 O  O   . ASN A 1 260 ? -11.383 30.653  -51.674 1.000 20.599 ? 260 ASN A O   1 ? 13 
ATOM   2023 C  CB  . ASN A 1 260 ? -9.673  28.557  -53.580 1.000 18.889 ? 260 ASN A CB  1 ? 13 
ATOM   2024 C  CG  . ASN A 1 260 ? -9.448  28.403  -55.059 1.000 19.368 ? 260 ASN A CG  1 ? 13 
ATOM   2025 O  OD1 . ASN A 1 260 ? -9.211  29.386  -55.777 1.000 21.373 ? 260 ASN A OD1 1 ? 13 
ATOM   2026 N  ND2 . ASN A 1 260 ? -9.601  27.164  -55.546 1.000 19.696 ? 260 ASN A ND2 1 ? 13 
ATOM   2027 N  N   . ALA A 1 261 ? -9.598  29.713  -50.622 1.000 19.559 ? 261 ALA A N   1 ? 13 
ATOM   2028 C  CA  . ALA A 1 261 ? -10.197 29.815  -49.282 1.000 19.725 ? 261 ALA A CA  1 ? 13 
ATOM   2029 C  C   . ALA A 1 261 ? -10.430 31.290  -48.959 1.000 21.855 ? 261 ALA A C   1 ? 13 
ATOM   2030 O  O   . ALA A 1 261 ? -11.472 31.613  -48.394 1.000 21.514 ? 261 ALA A O   1 ? 13 
ATOM   2031 C  CB  . ALA A 1 261 ? -9.314  29.194  -48.255 1.000 20.164 ? 261 ALA A CB  1 ? 13 
ATOM   2032 N  N   . GLU A 1 262 ? -9.505  32.188  -49.289 1.000 22.294 ? 262 GLU A N   1 ? 13 
ATOM   2033 C  CA  . GLU A 1 262 ? -9.720  33.624  -48.980 1.000 24.459 ? 262 GLU A CA  1 ? 13 
ATOM   2034 C  C   . GLU A 1 262 ? -10.966 34.167  -49.688 1.000 23.979 ? 262 GLU A C   1 ? 13 
ATOM   2035 O  O   . GLU A 1 262 ? -11.726 34.943  -49.095 1.000 24.389 ? 262 GLU A O   1 ? 13 
ATOM   2036 C  CB  . GLU A 1 262 ? -8.460  34.403  -49.298 1.000 27.100 ? 262 GLU A CB  1 ? 13 
ATOM   2037 C  CG  . GLU A 1 262 ? -7.349  34.069  -48.335 1.000 31.059 ? 262 GLU A CG  1 ? 13 
ATOM   2038 C  CD  . GLU A 1 262 ? -6.005  34.672  -48.661 1.000 40.402 ? 262 GLU A CD  1 ? 13 
ATOM   2039 O  OE1 . GLU A 1 262 ? -5.841  35.146  -49.765 1.000 45.277 ? 262 GLU A OE1 1 ? 13 
ATOM   2040 O  OE2 . GLU A 1 262 ? -5.160  34.713  -47.758 1.000 44.608 ? 262 GLU A OE2 1 ? 13 
ATOM   2041 N  N   A ARG A 1 263 ? -11.187 33.741  -50.928 0.500 22.730 ? 263 ARG A N   1 ? 13 
ATOM   2042 N  N   B ARG A 1 263 ? -11.210 33.705  -50.911 0.500 23.869 ? 263 ARG A N   1 ? 13 
ATOM   2043 C  CA  A ARG A 1 263 ? -12.360 34.121  -51.716 0.500 22.902 ? 263 ARG A CA  1 ? 13 
ATOM   2044 C  CA  B ARG A 1 263 ? -12.346 34.140  -51.724 0.500 24.834 ? 263 ARG A CA  1 ? 13 
ATOM   2045 C  C   A ARG A 1 263 ? -13.635 33.537  -51.085 0.500 22.609 ? 263 ARG A C   1 ? 13 
ATOM   2046 C  C   B ARG A 1 263 ? -13.645 33.518  -51.161 0.500 23.594 ? 263 ARG A C   1 ? 13 
ATOM   2047 O  O   A ARG A 1 263 ? -14.686 34.224  -51.027 0.500 23.812 ? 263 ARG A O   1 ? 13 
ATOM   2048 O  O   B ARG A 1 263 ? -14.705 34.196  -51.148 0.500 24.432 ? 263 ARG A O   1 ? 13 
ATOM   2049 C  CB  A ARG A 1 263 ? -12.162 33.673  -53.164 0.500 23.027 ? 263 ARG A CB  1 ? 13 
ATOM   2050 C  CB  B ARG A 1 263 ? -12.001 33.877  -53.199 0.500 26.782 ? 263 ARG A CB  1 ? 13 
ATOM   2051 C  CG  A ARG A 1 263 ? -13.357 34.007  -54.026 0.500 24.771 ? 263 ARG A CG  1 ? 13 
ATOM   2052 C  CG  B ARG A 1 263 ? -12.095 35.145  -54.033 0.500 32.800 ? 263 ARG A CG  1 ? 13 
ATOM   2053 C  CD  A ARG A 1 263 ? -13.449 35.513  -54.285 0.500 28.194 ? 263 ARG A CD  1 ? 13 
ATOM   2054 C  CD  B ARG A 1 263 ? -10.854 35.977  -54.226 0.500 33.979 ? 263 ARG A CD  1 ? 13 
ATOM   2055 N  NE  A ARG A 1 263 ? -14.667 35.753  -54.972 0.500 30.203 ? 263 ARG A NE  1 ? 13 
ATOM   2056 N  NE  B ARG A 1 263 ? -10.321 36.638  -53.046 0.500 34.468 ? 263 ARG A NE  1 ? 13 
ATOM   2057 C  CZ  A ARG A 1 263 ? -15.815 35.897  -54.335 0.500 30.235 ? 263 ARG A CZ  1 ? 13 
ATOM   2058 C  CZ  B ARG A 1 263 ? -9.118  36.405  -52.537 0.500 34.394 ? 263 ARG A CZ  1 ? 13 
ATOM   2059 N  NH1 A ARG A 1 263 ? -15.842 35.817  -53.009 0.500 25.782 ? 263 ARG A NH1 1 ? 13 
ATOM   2060 N  NH1 B ARG A 1 263 ? -8.317  35.438  -53.039 0.500 30.307 ? 263 ARG A NH1 1 ? 13 
ATOM   2061 N  NH2 A ARG A 1 263 ? -16.904 36.207  -55.028 0.500 31.186 ? 263 ARG A NH2 1 ? 13 
ATOM   2062 N  NH2 B ARG A 1 263 ? -8.753  37.145  -51.505 0.500 36.412 ? 263 ARG A NH2 1 ? 13 
ATOM   2063 N  N   . VAL A 1 264 ? -13.592 32.287  -50.680 1.000 21.995 ? 264 VAL A N   1 ? 13 
ATOM   2064 C  CA  . VAL A 1 264 ? -14.756 31.630  -50.043 1.000 21.921 ? 264 VAL A CA  1 ? 13 
ATOM   2065 C  C   . VAL A 1 264 ? -15.095 32.355  -48.735 1.000 22.166 ? 264 VAL A C   1 ? 13 
ATOM   2066 O  O   . VAL A 1 264 ? -16.298 32.619  -48.473 1.000 24.568 ? 264 VAL A O   1 ? 13 
ATOM   2067 C  CB  . VAL A 1 264 ? -14.478 30.137  -49.821 1.000 21.972 ? 264 VAL A CB  1 ? 13 
ATOM   2068 C  CG1 . VAL A 1 264 ? -15.404 29.497  -48.799 1.000 24.093 ? 264 VAL A CG1 1 ? 13 
ATOM   2069 C  CG2 . VAL A 1 264 ? -14.515 29.415  -51.142 1.000 22.617 ? 264 VAL A CG2 1 ? 13 
ATOM   2070 N  N   . VAL A 1 265 ? -14.094 32.735  -47.963 1.000 23.659 ? 265 VAL A N   1 ? 14 
ATOM   2071 C  CA  . VAL A 1 265 ? -14.321 33.466  -46.688 1.000 22.836 ? 265 VAL A CA  1 ? 14 
ATOM   2072 C  C   . VAL A 1 265 ? -15.044 34.789  -47.015 1.000 25.111 ? 265 VAL A C   1 ? 14 
ATOM   2073 O  O   . VAL A 1 265 ? -16.060 35.135  -46.307 1.000 26.277 ? 265 VAL A O   1 ? 14 
ATOM   2074 C  CB  . VAL A 1 265 ? -13.011 33.707  -45.967 1.000 23.045 ? 265 VAL A CB  1 ? 14 
ATOM   2075 C  CG1 . VAL A 1 265 ? -13.136 34.781  -44.927 1.000 23.683 ? 265 VAL A CG1 1 ? 14 
ATOM   2076 C  CG2 . VAL A 1 265 ? -12.495 32.402  -45.353 1.000 23.264 ? 265 VAL A CG2 1 ? 14 
ATOM   2077 N  N   . GLU A 1 266 ? -14.598 35.502  -48.033 1.000 25.634 ? 266 GLU A N   1 ? 14 
ATOM   2078 C  CA  . GLU A 1 266 ? -15.285 36.772  -48.463 1.000 28.678 ? 266 GLU A CA  1 ? 14 
ATOM   2079 C  C   . GLU A 1 266 ? -16.768 36.496  -48.756 1.000 29.836 ? 266 GLU A C   1 ? 14 
ATOM   2080 O  O   . GLU A 1 266 ? -17.657 37.365  -48.455 1.000 30.753 ? 266 GLU A O   1 ? 14 
ATOM   2081 C  CB  . GLU A 1 266 ? -14.608 37.411  -49.654 1.000 32.538 ? 266 GLU A CB  1 ? 14 
ATOM   2082 C  CG  . GLU A 1 266 ? -13.243 37.973  -49.314 1.000 35.931 ? 266 GLU A CG  1 ? 14 
ATOM   2083 C  CD  . GLU A 1 266 ? -12.281 38.273  -50.478 1.000 42.251 ? 266 GLU A CD  1 ? 14 
ATOM   2084 O  OE1 . GLU A 1 266 ? -11.111 38.646  -50.197 1.000 45.814 ? 266 GLU A OE1 1 ? 14 
ATOM   2085 O  OE2 . GLU A 1 266 ? -12.694 38.129  -51.654 1.000 48.955 ? 266 GLU A OE2 1 ? 14 
ATOM   2086 N  N   . ALA A 1 267 ? -17.102 35.410  -49.430 1.000 27.777 ? 267 ALA A N   1 ? 14 
ATOM   2087 C  CA  . ALA A 1 267 ? -18.497 35.060  -49.757 1.000 29.157 ? 267 ALA A CA  1 ? 14 
ATOM   2088 C  C   . ALA A 1 267 ? -19.278 34.729  -48.485 1.000 28.387 ? 267 ALA A C   1 ? 14 
ATOM   2089 O  O   . ALA A 1 267 ? -20.491 35.040  -48.442 1.000 30.270 ? 267 ALA A O   1 ? 14 
ATOM   2090 C  CB  . ALA A 1 267 ? -18.593 33.923  -50.763 1.000 28.795 ? 267 ALA A CB  1 ? 14 
ATOM   2091 N  N   . LEU A 1 268 ? -18.678 34.110  -47.504 1.000 27.524 ? 268 LEU A N   1 ? 14 
ATOM   2092 C  CA  . LEU A 1 268 ? -19.387 33.644  -46.298 1.000 28.194 ? 268 LEU A CA  1 ? 14 
ATOM   2093 C  C   . LEU A 1 268 ? -19.612 34.819  -45.341 1.000 29.860 ? 268 LEU A C   1 ? 14 
ATOM   2094 O  O   . LEU A 1 268 ? -20.680 34.837  -44.720 1.000 30.640 ? 268 LEU A O   1 ? 14 
ATOM   2095 C  CB  . LEU A 1 268 ? -18.595 32.531  -45.619 1.000 28.173 ? 268 LEU A CB  1 ? 14 
ATOM   2096 C  CG  . LEU A 1 268 ? -18.543 31.227  -46.409 1.000 28.664 ? 268 LEU A CG  1 ? 14 
ATOM   2097 C  CD1 . LEU A 1 268 ? -17.549 30.258  -45.790 1.000 28.218 ? 268 LEU A CD1 1 ? 14 
ATOM   2098 C  CD2 . LEU A 1 268 ? -19.894 30.554  -46.465 1.000 31.011 ? 268 LEU A CD2 1 ? 14 
ATOM   2099 N  N   . VAL A 1 269 ? -18.633 35.698  -45.179 1.000 29.505 ? 269 VAL A N   1 ? 14 
ATOM   2100 C  CA  . VAL A 1 269 ? -18.697 36.833  -44.214 1.000 31.325 ? 269 VAL A CA  1 ? 14 
ATOM   2101 C  C   . VAL A 1 269 ? -19.851 37.764  -44.624 1.000 35.539 ? 269 VAL A C   1 ? 14 
ATOM   2102 O  O   . VAL A 1 269 ? -19.945 38.135  -45.758 1.000 37.750 ? 269 VAL A O   1 ? 14 
ATOM   2103 C  CB  . VAL A 1 269 ? -17.360 37.557  -44.122 1.000 31.723 ? 269 VAL A CB  1 ? 14 
ATOM   2104 C  CG1 . VAL A 1 269 ? -17.442 38.870  -43.378 1.000 33.904 ? 269 VAL A CG1 1 ? 14 
ATOM   2105 C  CG2 . VAL A 1 269 ? -16.342 36.669  -43.425 1.000 29.644 ? 269 VAL A CG2 1 ? 14 
ATOM   2106 N  N   . GLY A 1 270 ? -20.747 38.035  -43.704 1.000 35.808 ? 270 GLY A N   1 ? 14 
ATOM   2107 C  CA  . GLY A 1 270 ? -21.937 38.844  -44.015 1.000 39.407 ? 270 GLY A CA  1 ? 14 
ATOM   2108 C  C   . GLY A 1 270 ? -23.038 38.123  -44.797 1.000 40.815 ? 270 GLY A C   1 ? 14 
ATOM   2109 O  O   . GLY A 1 270 ? -24.065 38.741  -44.884 1.000 40.652 ? 270 GLY A O   1 ? 14 
ATOM   2110 N  N   . HIS A 1 271 ? -22.876 36.869  -45.318 1.000 35.799 ? 271 HIS A N   1 ? 14 
ATOM   2111 C  CA  . HIS A 1 271 ? -24.018 36.107  -45.901 1.000 34.533 ? 271 HIS A CA  1 ? 14 
ATOM   2112 C  C   . HIS A 1 271 ? -25.070 36.071  -44.789 1.000 34.790 ? 271 HIS A C   1 ? 14 
ATOM   2113 O  O   . HIS A 1 271 ? -24.768 35.765  -43.645 1.000 33.473 ? 271 HIS A O   1 ? 14 
ATOM   2114 C  CB  . HIS A 1 271 ? -23.629 34.670  -46.370 1.000 32.054 ? 271 HIS A CB  1 ? 14 
ATOM   2115 C  CG  . HIS A 1 271 ? -24.685 34.011  -47.165 1.000 32.424 ? 271 HIS A CG  1 ? 14 
ATOM   2116 N  ND1 . HIS A 1 271 ? -25.852 33.526  -46.594 1.000 33.167 ? 271 HIS A ND1 1 ? 14 
ATOM   2117 C  CD2 . HIS A 1 271 ? -24.796 33.819  -48.490 1.000 33.637 ? 271 HIS A CD2 1 ? 14 
ATOM   2118 C  CE1 . HIS A 1 271 ? -26.621 33.029  -47.551 1.000 34.201 ? 271 HIS A CE1 1 ? 14 
ATOM   2119 N  NE2 . HIS A 1 271 ? -25.998 33.245  -48.736 1.000 35.677 ? 271 HIS A NE2 1 ? 14 
ATOM   2120 N  N   . PRO A 1 272 ? -26.337 36.423  -45.074 1.000 35.591 ? 272 PRO A N   1 ? 14 
ATOM   2121 C  CA  . PRO A 1 272 ? -27.358 36.482  -44.030 1.000 36.983 ? 272 PRO A CA  1 ? 14 
ATOM   2122 C  C   . PRO A 1 272 ? -27.680 35.158  -43.322 1.000 36.119 ? 272 PRO A C   1 ? 14 
ATOM   2123 O  O   . PRO A 1 272 ? -28.178 35.199  -42.231 1.000 37.075 ? 272 PRO A O   1 ? 14 
ATOM   2124 C  CB  . PRO A 1 272 ? -28.608 36.996  -44.739 1.000 39.843 ? 272 PRO A CB  1 ? 14 
ATOM   2125 C  CG  . PRO A 1 272 ? -28.299 36.998  -46.218 1.000 39.638 ? 272 PRO A CG  1 ? 14 
ATOM   2126 C  CD  . PRO A 1 272 ? -26.813 36.853  -46.388 1.000 37.790 ? 272 PRO A CD  1 ? 14 
ATOM   2127 N  N   . GLU A 1 273 ? -27.324 33.997  -43.895 1.000 33.177 ? 273 GLU A N   1 ? 14 
ATOM   2128 C  CA  . GLU A 1 273 ? -27.646 32.703  -43.229 1.000 33.351 ? 273 GLU A CA  1 ? 14 
ATOM   2129 C  C   . GLU A 1 273 ? -26.443 32.267  -42.353 1.000 30.519 ? 273 GLU A C   1 ? 14 
ATOM   2130 O  O   . GLU A 1 273 ? -26.609 31.330  -41.552 1.000 30.746 ? 273 GLU A O   1 ? 14 
ATOM   2131 C  CB  . GLU A 1 273 ? -27.962 31.632  -44.270 1.000 35.315 ? 273 GLU A CB  1 ? 14 
ATOM   2132 C  CG  . GLU A 1 273 ? -29.173 31.980  -45.148 1.000 38.611 ? 273 GLU A CG  1 ? 14 
ATOM   2133 C  CD  . GLU A 1 273 ? -30.439 32.153  -44.337 1.000 46.146 ? 273 GLU A CD  1 ? 14 
ATOM   2134 O  OE1 . GLU A 1 273 ? -30.729 31.284  -43.538 1.000 51.972 ? 273 GLU A OE1 1 ? 14 
ATOM   2135 O  OE2 . GLU A 1 273 ? -31.108 33.166  -44.516 1.000 49.088 ? 273 GLU A OE2 1 ? 14 
ATOM   2136 N  N   . VAL A 1 274 ? -25.327 32.968  -42.428 1.000 29.439 ? 274 VAL A N   1 ? 14 
ATOM   2137 C  CA  . VAL A 1 274 ? -24.089 32.519  -41.757 1.000 29.362 ? 274 VAL A CA  1 ? 14 
ATOM   2138 C  C   . VAL A 1 274 ? -23.901 33.324  -40.483 1.000 30.450 ? 274 VAL A C   1 ? 14 
ATOM   2139 O  O   . VAL A 1 274 ? -23.888 34.567  -40.574 1.000 32.484 ? 274 VAL A O   1 ? 14 
ATOM   2140 C  CB  . VAL A 1 274 ? -22.898 32.676  -42.694 1.000 28.107 ? 274 VAL A CB  1 ? 14 
ATOM   2141 C  CG1 . VAL A 1 274 ? -21.591 32.406  -41.952 1.000 28.751 ? 274 VAL A CG1 1 ? 14 
ATOM   2142 C  CG2 . VAL A 1 274 ? -23.090 31.775  -43.872 1.000 28.619 ? 274 VAL A CG2 1 ? 14 
ATOM   2143 N  N   . ALA A 1 275 ? -23.802 32.674  -39.343 1.000 30.058 ? 275 ALA A N   1 ? 14 
ATOM   2144 C  CA  . ALA A 1 275 ? -23.678 33.355  -38.032 1.000 31.870 ? 275 ALA A CA  1 ? 14 
ATOM   2145 C  C   . ALA A 1 275 ? -22.232 33.742  -37.787 1.000 30.697 ? 275 ALA A C   1 ? 14 
ATOM   2146 O  O   . ALA A 1 275 ? -22.023 34.693  -37.075 1.000 32.308 ? 275 ALA A O   1 ? 14 
ATOM   2147 C  CB  . ALA A 1 275 ? -24.183 32.476  -36.917 1.000 33.729 ? 275 ALA A CB  1 ? 14 
ATOM   2148 N  N   . GLU A 1 276 ? -21.278 32.906  -38.191 1.000 27.800 ? 276 GLU A N   1 ? 14 
ATOM   2149 C  CA  . GLU A 1 276 ? -19.857 33.076  -37.814 1.000 27.814 ? 276 GLU A CA  1 ? 14 
ATOM   2150 C  C   . GLU A 1 276 ? -18.981 32.366  -38.841 1.000 25.336 ? 276 GLU A C   1 ? 14 
ATOM   2151 O  O   . GLU A 1 276 ? -19.360 31.264  -39.251 1.000 25.764 ? 276 GLU A O   1 ? 14 
ATOM   2152 C  CB  . GLU A 1 276 ? -19.644 32.542  -36.398 1.000 30.774 ? 276 GLU A CB  1 ? 14 
ATOM   2153 C  CG  . GLU A 1 276 ? -18.321 32.961  -35.824 1.000 32.290 ? 276 GLU A CG  1 ? 14 
ATOM   2154 C  CD  . GLU A 1 276 ? -17.983 32.407  -34.457 1.000 35.443 ? 276 GLU A CD  1 ? 14 
ATOM   2155 O  OE1 . GLU A 1 276 ? -18.701 31.505  -33.990 1.000 36.892 ? 276 GLU A OE1 1 ? 14 
ATOM   2156 O  OE2 . GLU A 1 276 ? -17.020 32.955  -33.841 1.000 38.844 ? 276 GLU A OE2 1 ? 14 
ATOM   2157 N  N   . VAL A 1 277 ? -17.866 32.996  -39.228 1.000 25.643 ? 277 VAL A N   1 ? 14 
ATOM   2158 C  CA  . VAL A 1 277 ? -16.872 32.363  -40.142 1.000 24.165 ? 277 VAL A CA  1 ? 14 
ATOM   2159 C  C   . VAL A 1 277 ? -15.546 32.237  -39.377 1.000 23.549 ? 277 VAL A C   1 ? 14 
ATOM   2160 O  O   . VAL A 1 277 ? -15.093 33.202  -38.726 1.000 24.275 ? 277 VAL A O   1 ? 14 
ATOM   2161 C  CB  . VAL A 1 277 ? -16.679 33.186  -41.421 1.000 24.683 ? 277 VAL A CB  1 ? 14 
ATOM   2162 C  CG1 . VAL A 1 277 ? -15.692 32.510  -42.355 1.000 24.930 ? 277 VAL A CG1 1 ? 14 
ATOM   2163 C  CG2 . VAL A 1 277 ? -18.028 33.430  -42.060 1.000 26.108 ? 277 VAL A CG2 1 ? 14 
ATOM   2164 N  N   . LEU A 1 278 ? -14.973 31.021  -39.441 1.000 22.945 ? 278 LEU A N   1 ? 14 
ATOM   2165 C  CA  . LEU A 1 278 ? -13.737 30.662  -38.725 1.000 22.344 ? 278 LEU A CA  1 ? 14 
ATOM   2166 C  C   . LEU A 1 278 ? -12.669 30.485  -39.802 1.000 22.235 ? 278 LEU A C   1 ? 14 
ATOM   2167 O  O   . LEU A 1 278 ? -12.779 29.606  -40.630 1.000 22.163 ? 278 LEU A O   1 ? 14 
ATOM   2168 C  CB  . LEU A 1 278 ? -13.949 29.392  -37.888 1.000 21.868 ? 278 LEU A CB  1 ? 14 
ATOM   2169 C  CG  . LEU A 1 278 ? -15.143 29.427  -36.925 1.000 23.062 ? 278 LEU A CG  1 ? 14 
ATOM   2170 C  CD1 . LEU A 1 278 ? -15.312 28.153  -36.188 1.000 24.313 ? 278 LEU A CD1 1 ? 14 
ATOM   2171 C  CD2 . LEU A 1 278 ? -14.981 30.600  -35.938 1.000 24.124 ? 278 LEU A CD2 1 ? 14 
ATOM   2172 N  N   . TYR A 1 279 ? -11.696 31.350  -39.773 1.000 21.854 ? 279 TYR A N   1 ? 14 
ATOM   2173 C  CA  . TYR A 1 279 ? -10.571 31.293  -40.711 1.000 22.319 ? 279 TYR A CA  1 ? 14 
ATOM   2174 C  C   . TYR A 1 279 ? -9.419  32.024  -40.074 1.000 22.276 ? 279 TYR A C   1 ? 14 
ATOM   2175 O  O   . TYR A 1 279 ? -9.564  33.217  -39.744 1.000 23.861 ? 279 TYR A O   1 ? 14 
ATOM   2176 C  CB  . TYR A 1 279 ? -10.909 31.915  -42.070 1.000 21.924 ? 279 TYR A CB  1 ? 14 
ATOM   2177 C  CG  . TYR A 1 279 ? -9.829  31.687  -43.095 1.000 21.470 ? 279 TYR A CG  1 ? 14 
ATOM   2178 C  CD1 . TYR A 1 279 ? -9.554  30.427  -43.539 1.000 20.887 ? 279 TYR A CD1 1 ? 14 
ATOM   2179 C  CD2 . TYR A 1 279 ? -9.074  32.741  -43.643 1.000 21.699 ? 279 TYR A CD2 1 ? 14 
ATOM   2180 C  CE1 . TYR A 1 279 ? -8.543  30.171  -44.455 1.000 21.737 ? 279 TYR A CE1 1 ? 14 
ATOM   2181 C  CE2 . TYR A 1 279 ? -8.052  32.499  -44.558 1.000 21.981 ? 279 TYR A CE2 1 ? 14 
ATOM   2182 C  CZ  . TYR A 1 279 ? -7.803  31.217  -44.996 1.000 22.221 ? 279 TYR A CZ  1 ? 14 
ATOM   2183 O  OH  . TYR A 1 279 ? -6.799  30.974  -45.908 1.000 22.229 ? 279 TYR A OH  1 ? 14 
ATOM   2184 N  N   . PRO A 1 280 ? -8.205  31.457  -40.004 1.000 22.297 ? 280 PRO A N   1 ? 15 
ATOM   2185 C  CA  . PRO A 1 280 ? -7.120  32.156  -39.294 1.000 22.851 ? 280 PRO A CA  1 ? 15 
ATOM   2186 C  C   . PRO A 1 280 ? -6.689  33.468  -39.921 1.000 23.502 ? 280 PRO A C   1 ? 15 
ATOM   2187 O  O   . PRO A 1 280 ? -6.113  34.292  -39.234 1.000 24.002 ? 280 PRO A O   1 ? 15 
ATOM   2188 C  CB  . PRO A 1 280 ? -5.966  31.122  -39.348 1.000 22.645 ? 280 PRO A CB  1 ? 15 
ATOM   2189 C  CG  . PRO A 1 280 ? -6.697  29.758  -39.434 1.000 22.890 ? 280 PRO A CG  1 ? 15 
ATOM   2190 C  CD  . PRO A 1 280 ? -7.862  30.066  -40.337 1.000 22.786 ? 280 PRO A CD  1 ? 15 
ATOM   2191 N  N   . GLY A 1 281 ? -7.027  33.704  -41.179 1.000 23.746 ? 281 GLY A N   1 ? 15 
ATOM   2192 C  CA  . GLY A 1 281 ? -6.655  34.948  -41.878 1.000 24.189 ? 281 GLY A CA  1 ? 15 
ATOM   2193 C  C   . GLY A 1 281 ? -7.576  36.119  -41.564 1.000 25.083 ? 281 GLY A C   1 ? 15 
ATOM   2194 O  O   . GLY A 1 281 ? -7.213  37.248  -41.873 1.000 26.179 ? 281 GLY A O   1 ? 15 
ATOM   2195 N  N   . LEU A 1 282 ? -8.704  35.870  -40.906 1.000 24.830 ? 282 LEU A N   1 ? 15 
ATOM   2196 C  CA  . LEU A 1 282 ? -9.612  36.987  -40.572 1.000 26.341 ? 282 LEU A CA  1 ? 15 
ATOM   2197 C  C   . LEU A 1 282 ? -8.969  37.742  -39.427 1.000 27.110 ? 282 LEU A C   1 ? 15 
ATOM   2198 O  O   . LEU A 1 282 ? -8.537  37.167  -38.429 1.000 25.807 ? 282 LEU A O   1 ? 15 
ATOM   2199 C  CB  . LEU A 1 282 ? -10.978 36.454  -40.164 1.000 27.507 ? 282 LEU A CB  1 ? 15 
ATOM   2200 C  CG  . LEU A 1 282 ? -11.873 35.957  -41.291 1.000 27.805 ? 282 LEU A CG  1 ? 15 
ATOM   2201 C  CD1 . LEU A 1 282 ? -13.012 35.111  -40.762 1.000 27.392 ? 282 LEU A CD1 1 ? 15 
ATOM   2202 C  CD2 . LEU A 1 282 ? -12.385 37.081  -42.157 1.000 28.819 ? 282 LEU A CD2 1 ? 15 
ATOM   2203 N  N   . PRO A 1 283 ? -8.877  39.078  -39.509 1.000 28.988 ? 283 PRO A N   1 ? 15 
ATOM   2204 C  CA  . PRO A 1 283 ? -8.164  39.794  -38.467 1.000 31.091 ? 283 PRO A CA  1 ? 15 
ATOM   2205 C  C   . PRO A 1 283 ? -8.751  39.621  -37.046 1.000 31.824 ? 283 PRO A C   1 ? 15 
ATOM   2206 O  O   . PRO A 1 283 ? -7.997  39.661  -36.068 1.000 32.239 ? 283 PRO A O   1 ? 15 
ATOM   2207 C  CB  . PRO A 1 283 ? -8.267  41.269  -38.894 1.000 34.393 ? 283 PRO A CB  1 ? 15 
ATOM   2208 C  CG  . PRO A 1 283 ? -8.715  41.246  -40.354 1.000 35.692 ? 283 PRO A CG  1 ? 15 
ATOM   2209 C  CD  . PRO A 1 283 ? -9.212  39.860  -40.691 1.000 31.574 ? 283 PRO A CD  1 ? 15 
ATOM   2210 N  N   . ASP A 1 284 ? -10.061 39.384  -36.963 1.000 31.540 ? 284 ASP A N   1 ? 15 
ATOM   2211 C  CA  . ASP A 1 284 ? -10.718 39.214  -35.649 1.000 33.649 ? 284 ASP A CA  1 ? 15 
ATOM   2212 C  C   . ASP A 1 284 ? -10.755 37.748  -35.243 1.000 30.536 ? 284 ASP A C   1 ? 15 
ATOM   2213 O  O   . ASP A 1 284 ? -11.327 37.454  -34.225 1.000 31.066 ? 284 ASP A O   1 ? 15 
ATOM   2214 C  CB  . ASP A 1 284 ? -12.131 39.794  -35.600 1.000 37.643 ? 284 ASP A CB  1 ? 15 
ATOM   2215 C  CG  . ASP A 1 284 ? -12.185 41.294  -35.848 1.000 46.545 ? 284 ASP A CG  1 ? 15 
ATOM   2216 O  OD1 . ASP A 1 284 ? -11.152 42.009  -35.559 1.000 48.004 ? 284 ASP A OD1 1 ? 15 
ATOM   2217 O  OD2 . ASP A 1 284 ? -13.294 41.766  -36.265 1.000 54.623 ? 284 ASP A OD2 1 ? 15 
ATOM   2218 N  N   . HIS A 1 285 ? -10.221 36.834  -36.026 1.000 27.699 ? 285 HIS A N   1 ? 15 
ATOM   2219 C  CA  . HIS A 1 285 ? -10.199 35.431  -35.601 1.000 27.184 ? 285 HIS A CA  1 ? 15 
ATOM   2220 C  C   . HIS A 1 285 ? -9.307  35.328  -34.387 1.000 27.173 ? 285 HIS A C   1 ? 15 
ATOM   2221 O  O   . HIS A 1 285 ? -8.212  35.951  -34.346 1.000 27.830 ? 285 HIS A O   1 ? 15 
ATOM   2222 C  CB  . HIS A 1 285 ? -9.663  34.564  -36.747 1.000 25.489 ? 285 HIS A CB  1 ? 15 
ATOM   2223 C  CG  . HIS A 1 285 ? -9.711  33.100  -36.444 1.000 25.075 ? 285 HIS A CG  1 ? 15 
ATOM   2224 N  ND1 . HIS A 1 285 ? -10.868 32.366  -36.633 1.000 25.774 ? 285 HIS A ND1 1 ? 15 
ATOM   2225 C  CD2 . HIS A 1 285 ? -8.753  32.250  -36.053 1.000 24.185 ? 285 HIS A CD2 1 ? 15 
ATOM   2226 C  CE1 . HIS A 1 285 ? -10.605 31.095  -36.306 1.000 24.854 ? 285 HIS A CE1 1 ? 15 
ATOM   2227 N  NE2 . HIS A 1 285 ? -9.305  31.004  -36.001 1.000 24.417 ? 285 HIS A NE2 1 ? 15 
ATOM   2228 N  N   . PRO A 1 286 ? -9.703  34.552  -33.370 1.000 28.966 ? 286 PRO A N   1 ? 15 
ATOM   2229 C  CA  . PRO A 1 286 ? -8.874  34.417  -32.173 1.000 32.143 ? 286 PRO A CA  1 ? 15 
ATOM   2230 C  C   . PRO A 1 286 ? -7.511  33.856  -32.577 1.000 30.342 ? 286 PRO A C   1 ? 15 
ATOM   2231 O  O   . PRO A 1 286 ? -7.437  32.819  -33.243 1.000 29.639 ? 286 PRO A O   1 ? 15 
ATOM   2232 C  CB  . PRO A 1 286 ? -9.621  33.408  -31.285 1.000 32.769 ? 286 PRO A CB  1 ? 15 
ATOM   2233 C  CG  . PRO A 1 286 ? -10.502 32.634  -32.298 1.000 31.892 ? 286 PRO A CG  1 ? 15 
ATOM   2234 C  CD  . PRO A 1 286 ? -10.917 33.706  -33.310 1.000 30.850 ? 286 PRO A CD  1 ? 15 
ATOM   2235 N  N   . GLY A 1 287 ? -6.440  34.537  -32.208 1.000 31.165 ? 287 GLY A N   1 ? 15 
ATOM   2236 C  CA  . GLY A 1 287 ? -5.089  34.026  -32.541 1.000 29.307 ? 287 GLY A CA  1 ? 15 
ATOM   2237 C  C   . GLY A 1 287 ? -4.580  34.434  -33.904 1.000 26.799 ? 287 GLY A C   1 ? 15 
ATOM   2238 O  O   . GLY A 1 287 ? -3.531  33.948  -34.303 1.000 25.988 ? 287 GLY A O   1 ? 15 
ATOM   2239 N  N   . HIS A 1 288 ? -5.288  35.302  -34.613 1.000 26.046 ? 288 HIS A N   1 ? 15 
ATOM   2240 C  CA  . HIS A 1 288 ? -4.836  35.844  -35.923 1.000 25.509 ? 288 HIS A CA  1 ? 15 
ATOM   2241 C  C   . HIS A 1 288 ? -3.370  36.291  -35.876 1.000 26.028 ? 288 HIS A C   1 ? 15 
ATOM   2242 O  O   . HIS A 1 288 ? -2.651  35.913  -36.788 1.000 26.995 ? 288 HIS A O   1 ? 15 
ATOM   2243 C  CB  . HIS A 1 288 ? -5.725  36.962  -36.404 1.000 27.310 ? 288 HIS A CB  1 ? 15 
ATOM   2244 C  CG  . HIS A 1 288 ? -5.217  37.573  -37.652 1.000 26.744 ? 288 HIS A CG  1 ? 15 
ATOM   2245 N  ND1 . HIS A 1 288 ? -5.320  36.898  -38.889 1.000 25.599 ? 288 HIS A ND1 1 ? 15 
ATOM   2246 C  CD2 . HIS A 1 288 ? -4.650  38.780  -37.883 1.000 28.308 ? 288 HIS A CD2 1 ? 15 
ATOM   2247 C  CE1 . HIS A 1 288 ? -4.804  37.708  -39.806 1.000 27.611 ? 288 HIS A CE1 1 ? 15 
ATOM   2248 N  NE2 . HIS A 1 288 ? -4.341  38.865  -39.213 1.000 28.708 ? 288 HIS A NE2 1 ? 15 
ATOM   2249 N  N   . LYS A 1 289 ? -2.954  37.083  -34.902 1.000 26.446 ? 289 LYS A N   1 ? 15 
ATOM   2250 C  CA  . LYS A 1 289 ? -1.564  37.649  -34.844 1.000 27.815 ? 289 LYS A CA  1 ? 15 
ATOM   2251 C  C   . LYS A 1 289 ? -0.547  36.531  -34.671 1.000 27.830 ? 289 LYS A C   1 ? 15 
ATOM   2252 O  O   . LYS A 1 289 ? 0.536   36.603  -35.289 1.000 28.420 ? 289 LYS A O   1 ? 15 
ATOM   2253 C  CB  . LYS A 1 289 ? -1.375  38.703  -33.742 1.000 29.681 ? 289 LYS A CB  1 ? 15 
ATOM   2254 N  N   . VAL A 1 290 ? -0.890  35.487  -33.916 1.000 25.824 ? 290 VAL A N   1 ? 15 
ATOM   2255 C  CA  . VAL A 1 290 ? 0.018   34.318  -33.778 1.000 24.800 ? 290 VAL A CA  1 ? 15 
ATOM   2256 C  C   . VAL A 1 290 ? 0.102   33.645  -35.137 1.000 24.155 ? 290 VAL A C   1 ? 15 
ATOM   2257 O  O   . VAL A 1 290 ? 1.234   33.231  -35.580 1.000 25.926 ? 290 VAL A O   1 ? 15 
ATOM   2258 C  CB  . VAL A 1 290 ? -0.437  33.373  -32.661 1.000 25.171 ? 290 VAL A CB  1 ? 15 
ATOM   2259 C  CG1 . VAL A 1 290 ? 0.357   32.074  -32.660 1.000 24.214 ? 290 VAL A CG1 1 ? 15 
ATOM   2260 C  CG2 . VAL A 1 290 ? -0.338  34.053  -31.308 1.000 27.782 ? 290 VAL A CG2 1 ? 15 
ATOM   2261 N  N   . ALA A 1 291 ? -1.024  33.463  -35.840 1.000 23.895 ? 291 ALA A N   1 ? 15 
ATOM   2262 C  CA  . ALA A 1 291 ? -1.015  32.808  -37.160 1.000 23.291 ? 291 ALA A CA  1 ? 15 
ATOM   2263 C  C   . ALA A 1 291 ? -0.126  33.589  -38.107 1.000 24.513 ? 291 ALA A C   1 ? 15 
ATOM   2264 O  O   . ALA A 1 291 ? 0.590   32.994  -38.914 1.000 24.287 ? 291 ALA A O   1 ? 15 
ATOM   2265 C  CB  . ALA A 1 291 ? -2.405  32.679  -37.701 1.000 23.294 ? 291 ALA A CB  1 ? 15 
ATOM   2266 N  N   . VAL A 1 292 ? -0.204  34.935  -38.093 1.000 24.778 ? 292 VAL A N   1 ? 15 
ATOM   2267 C  CA  . VAL A 1 292 ? 0.623   35.759  -38.986 1.000 26.467 ? 292 VAL A CA  1 ? 15 
ATOM   2268 C  C   . VAL A 1 292 ? 2.098   35.491  -38.689 1.000 27.285 ? 292 VAL A C   1 ? 15 
ATOM   2269 O  O   . VAL A 1 292 ? 2.899   35.486  -39.625 1.000 28.099 ? 292 VAL A O   1 ? 15 
ATOM   2270 C  CB  . VAL A 1 292 ? 0.293   37.244  -38.835 1.000 27.077 ? 292 VAL A CB  1 ? 15 
ATOM   2271 C  CG1 . VAL A 1 292 ? 1.264   38.121  -39.566 1.000 29.116 ? 292 VAL A CG1 1 ? 15 
ATOM   2272 C  CG2 . VAL A 1 292 ? -1.155  37.587  -39.247 1.000 26.695 ? 292 VAL A CG2 1 ? 15 
ATOM   2273 N  N   A ASP A 1 293 ? 2.482   35.298  -37.450 0.500 27.694 ? 293 ASP A N   1 ? 15 
ATOM   2274 N  N   B ASP A 1 293 ? 2.433   35.318  -37.404 0.500 27.496 ? 293 ASP A N   1 ? 15 
ATOM   2275 C  CA  A ASP A 1 293 ? 3.928   35.174  -37.173 0.500 29.224 ? 293 ASP A CA  1 ? 15 
ATOM   2276 C  CA  B ASP A 1 293 ? 3.819   35.103  -36.893 0.500 28.964 ? 293 ASP A CA  1 ? 15 
ATOM   2277 C  C   A ASP A 1 293 ? 4.421   33.741  -37.462 0.500 27.718 ? 293 ASP A C   1 ? 15 
ATOM   2278 C  C   B ASP A 1 293 ? 4.381   33.760  -37.398 0.500 27.574 ? 293 ASP A C   1 ? 15 
ATOM   2279 O  O   A ASP A 1 293 ? 5.609   33.603  -37.792 0.500 28.498 ? 293 ASP A O   1 ? 15 
ATOM   2280 O  O   B ASP A 1 293 ? 5.561   33.707  -37.789 0.500 28.616 ? 293 ASP A O   1 ? 15 
ATOM   2281 C  CB  A ASP A 1 293 ? 4.223   35.590  -35.744 0.500 31.339 ? 293 ASP A CB  1 ? 15 
ATOM   2282 C  CB  B ASP A 1 293 ? 3.836   35.094  -35.354 0.500 29.805 ? 293 ASP A CB  1 ? 15 
ATOM   2283 C  CG  A ASP A 1 293 ? 4.231   37.091  -35.484 0.500 34.565 ? 293 ASP A CG  1 ? 15 
ATOM   2284 C  CG  B ASP A 1 293 ? 5.211   35.284  -34.725 0.500 33.016 ? 293 ASP A CG  1 ? 15 
ATOM   2285 O  OD1 A ASP A 1 293 ? 4.153   37.948  -36.460 0.500 35.894 ? 293 ASP A OD1 1 ? 15 
ATOM   2286 O  OD1 B ASP A 1 293 ? 6.019   35.999  -35.348 0.500 35.130 ? 293 ASP A OD1 1 ? 15 
ATOM   2287 O  OD2 A ASP A 1 293 ? 4.320   37.391  -34.328 0.500 38.129 ? 293 ASP A OD2 1 ? 15 
ATOM   2288 O  OD2 B ASP A 1 293 ? 5.417   34.829  -33.550 0.500 35.274 ? 293 ASP A OD2 1 ? 15 
ATOM   2289 N  N   . GLN A 1 294 ? 3.569   32.712  -37.381 1.000 24.649 ? 294 GLN A N   1 ? 15 
ATOM   2290 C  CA  . GLN A 1 294 ? 4.098   31.335  -37.536 1.000 24.301 ? 294 GLN A CA  1 ? 15 
ATOM   2291 C  C   . GLN A 1 294 ? 3.628   30.626  -38.815 1.000 22.527 ? 294 GLN A C   1 ? 15 
ATOM   2292 O  O   . GLN A 1 294 ? 4.155   29.523  -39.073 1.000 22.595 ? 294 GLN A O   1 ? 15 
ATOM   2293 C  CB  . GLN A 1 294 ? 3.884   30.523  -36.253 1.000 25.674 ? 294 GLN A CB  1 ? 15 
ATOM   2294 C  CG  . GLN A 1 294 ? 2.526   29.973  -36.063 1.000 24.710 ? 294 GLN A CG  1 ? 15 
ATOM   2295 C  CD  . GLN A 1 294 ? 2.254   29.304  -34.712 1.000 22.786 ? 294 GLN A CD  1 ? 15 
ATOM   2296 O  OE1 . GLN A 1 294 ? 3.056   29.323  -33.772 1.000 23.602 ? 294 GLN A OE1 1 ? 15 
ATOM   2297 N  NE2 . GLN A 1 294 ? 1.049   28.732  -34.608 1.000 22.032 ? 294 GLN A NE2 1 ? 15 
ATOM   2298 N  N   . MET A 1 295 ? 2.689   31.171  -39.566 1.000 21.988 ? 295 MET A N   1 ? 15 
ATOM   2299 C  CA  . MET A 1 295 ? 2.195   30.537  -40.817 1.000 21.819 ? 295 MET A CA  1 ? 15 
ATOM   2300 C  C   . MET A 1 295 ? 2.519   31.445  -41.996 1.000 23.371 ? 295 MET A C   1 ? 15 
ATOM   2301 O  O   . MET A 1 295 ? 2.332   32.641  -41.901 1.000 24.820 ? 295 MET A O   1 ? 15 
ATOM   2302 C  CB  . MET A 1 295 ? 0.674   30.326  -40.754 1.000 20.531 ? 295 MET A CB  1 ? 15 
ATOM   2303 C  CG  . MET A 1 295 ? 0.206   29.501  -39.585 1.000 21.121 ? 295 MET A CG  1 ? 15 
ATOM   2304 S  SD  . MET A 1 295 ? -1.593  29.264  -39.556 1.000 22.524 ? 295 MET A SD  1 ? 15 
ATOM   2305 C  CE  . MET A 1 295 ? -1.779  28.087  -40.890 1.000 22.348 ? 295 MET A CE  1 ? 15 
ATOM   2306 N  N   . ARG A 1 296 ? 2.968   30.865  -43.120 1.000 22.825 ? 296 ARG A N   1 ? 15 
ATOM   2307 C  CA  . ARG A 1 296 ? 3.260   31.595  -44.387 1.000 24.149 ? 296 ARG A CA  1 ? 15 
ATOM   2308 C  C   . ARG A 1 296 ? 1.928   32.148  -44.927 1.000 23.520 ? 296 ARG A C   1 ? 15 
ATOM   2309 O  O   . ARG A 1 296 ? 1.959   33.203  -45.595 1.000 24.844 ? 296 ARG A O   1 ? 15 
ATOM   2310 C  CB  . ARG A 1 296 ? 3.967   30.616  -45.371 1.000 26.926 ? 296 ARG A CB  1 ? 15 
ATOM   2311 C  CG  . ARG A 1 296 ? 4.250   31.107  -46.798 1.000 32.181 ? 296 ARG A CG  1 ? 15 
ATOM   2312 C  CD  . ARG A 1 296 ? 5.072   30.078  -47.629 1.000 35.693 ? 296 ARG A CD  1 ? 15 
ATOM   2313 N  NE  . ARG A 1 296 ? 5.241   30.648  -48.960 1.000 40.581 ? 296 ARG A NE  1 ? 15 
ATOM   2314 C  CZ  . ARG A 1 296 ? 6.200   30.313  -49.823 1.000 43.520 ? 296 ARG A CZ  1 ? 15 
ATOM   2315 N  NH1 . ARG A 1 296 ? 6.263   30.895  -51.008 1.000 45.168 ? 296 ARG A NH1 1 ? 15 
ATOM   2316 N  NH2 . ARG A 1 296 ? 7.148   29.452  -49.458 1.000 47.909 ? 296 ARG A NH2 1 ? 15 
ATOM   2317 N  N   . ALA A 1 297 ? 0.842   31.407  -44.754 1.000 20.983 ? 297 ALA A N   1 ? 16 
ATOM   2318 C  CA  . ALA A 1 297 ? -0.529  31.724  -45.242 1.000 20.631 ? 297 ALA A CA  1 ? 16 
ATOM   2319 C  C   . ALA A 1 297 ? -1.484  30.935  -44.406 1.000 20.356 ? 297 ALA A C   1 ? 16 
ATOM   2320 O  O   . ALA A 1 297 ? -1.046  30.125  -43.608 1.000 21.429 ? 297 ALA A O   1 ? 16 
ATOM   2321 C  CB  . ALA A 1 297 ? -0.707  31.506  -46.755 1.000 21.247 ? 297 ALA A CB  1 ? 16 
ATOM   2322 N  N   . PHE A 1 298 ? -2.774  31.107  -44.585 1.000 21.878 ? 298 PHE A N   1 ? 16 
ATOM   2323 C  CA  . PHE A 1 298 ? -3.743  30.714  -43.529 1.000 21.997 ? 298 PHE A CA  1 ? 16 
ATOM   2324 C  C   . PHE A 1 298 ? -4.520  29.459  -43.828 1.000 21.135 ? 298 PHE A C   1 ? 16 
ATOM   2325 O  O   . PHE A 1 298 ? -5.338  29.093  -42.992 1.000 22.459 ? 298 PHE A O   1 ? 16 
ATOM   2326 C  CB  . PHE A 1 298 ? -4.671  31.900  -43.289 1.000 22.385 ? 298 PHE A CB  1 ? 16 
ATOM   2327 C  CG  . PHE A 1 298 ? -3.903  33.129  -42.893 1.000 24.388 ? 298 PHE A CG  1 ? 16 
ATOM   2328 C  CD1 . PHE A 1 298 ? -3.292  33.216  -41.670 1.000 28.677 ? 298 PHE A CD1 1 ? 16 
ATOM   2329 C  CD2 . PHE A 1 298 ? -3.827  34.208  -43.747 1.000 26.438 ? 298 PHE A CD2 1 ? 16 
ATOM   2330 C  CE1 . PHE A 1 298 ? -2.707  34.398  -41.264 1.000 32.021 ? 298 PHE A CE1 1 ? 16 
ATOM   2331 C  CE2 . PHE A 1 298 ? -3.143  35.361  -43.392 1.000 31.185 ? 298 PHE A CE2 1 ? 16 
ATOM   2332 C  CZ  . PHE A 1 298 ? -2.573  35.453  -42.150 1.000 32.911 ? 298 PHE A CZ  1 ? 16 
ATOM   2333 N  N   . GLY A 1 299 ? -4.196  28.782  -44.934 1.000 19.679 ? 299 GLY A N   1 ? 16 
ATOM   2334 C  CA  . GLY A 1 299 ? -4.684  27.445  -45.193 1.000 21.038 ? 299 GLY A CA  1 ? 16 
ATOM   2335 C  C   . GLY A 1 299 ? -5.918  27.372  -46.055 1.000 18.797 ? 299 GLY A C   1 ? 16 
ATOM   2336 O  O   . GLY A 1 299 ? -6.470  28.407  -46.447 1.000 20.590 ? 299 GLY A O   1 ? 16 
ATOM   2337 N  N   . GLY A 1 300 ? -6.286  26.132  -46.398 1.000 18.401 ? 300 GLY A N   1 ? 16 
ATOM   2338 C  CA  . GLY A 1 300 ? -7.419  25.831  -47.259 1.000 18.173 ? 300 GLY A CA  1 ? 16 
ATOM   2339 C  C   . GLY A 1 300 ? -8.696  25.530  -46.494 1.000 18.449 ? 300 GLY A C   1 ? 16 
ATOM   2340 O  O   . GLY A 1 300 ? -9.745  25.335  -47.160 1.000 20.208 ? 300 GLY A O   1 ? 16 
ATOM   2341 N  N   . MET A 1 301 ? -8.608  25.400  -45.183 1.000 18.317 ? 301 MET A N   1 ? 16 
ATOM   2342 C  CA  . MET A 1 301 ? -9.764  25.011  -44.348 1.000 18.605 ? 301 MET A CA  1 ? 16 
ATOM   2343 C  C   . MET A 1 301 ? -10.532 26.235  -43.923 1.000 18.898 ? 301 MET A C   1 ? 16 
ATOM   2344 O  O   . MET A 1 301 ? -9.945  27.263  -43.553 1.000 19.530 ? 301 MET A O   1 ? 16 
ATOM   2345 C  CB  . MET A 1 301 ? -9.296  24.205  -43.129 1.000 18.830 ? 301 MET A CB  1 ? 16 
ATOM   2346 C  CG  . MET A 1 301 ? -8.556  22.939  -43.487 1.000 19.605 ? 301 MET A CG  1 ? 16 
ATOM   2347 S  SD  . MET A 1 301 ? -9.410  21.752  -44.542 1.000 19.577 ? 301 MET A SD  1 ? 16 
ATOM   2348 C  CE  . MET A 1 301 ? -10.739 21.238  -43.430 1.000 19.498 ? 301 MET A CE  1 ? 16 
ATOM   2349 N  N   . VAL A 1 302 ? -11.859 26.110  -43.995 1.000 20.491 ? 302 VAL A N   1 ? 16 
ATOM   2350 C  CA  . VAL A 1 302 ? -12.762 27.218  -43.559 1.000 20.405 ? 302 VAL A CA  1 ? 16 
ATOM   2351 C  C   . VAL A 1 302 ? -13.916 26.540  -42.811 1.000 21.015 ? 302 VAL A C   1 ? 16 
ATOM   2352 O  O   . VAL A 1 302 ? -14.517 25.623  -43.375 1.000 20.543 ? 302 VAL A O   1 ? 16 
ATOM   2353 C  CB  . VAL A 1 302 ? -13.304 27.995  -44.762 1.000 21.314 ? 302 VAL A CB  1 ? 16 
ATOM   2354 C  CG1 . VAL A 1 302 ? -14.238 29.135  -44.286 1.000 22.450 ? 302 VAL A CG1 1 ? 16 
ATOM   2355 C  CG2 . VAL A 1 302 ? -12.179 28.518  -45.665 1.000 21.577 ? 302 VAL A CG2 1 ? 16 
ATOM   2356 N  N   . SER A 1 303 ? -14.253 27.008  -41.624 1.000 20.397 ? 303 SER A N   1 ? 16 
ATOM   2357 C  CA  . SER A 1 303 ? -15.435 26.508  -40.910 1.000 21.152 ? 303 SER A CA  1 ? 16 
ATOM   2358 C  C   . SER A 1 303 ? -16.410 27.649  -40.717 1.000 21.055 ? 303 SER A C   1 ? 16 
ATOM   2359 O  O   . SER A 1 303 ? -15.989 28.787  -40.666 1.000 22.607 ? 303 SER A O   1 ? 16 
ATOM   2360 C  CB  . SER A 1 303 ? -15.083 25.833  -39.612 1.000 20.901 ? 303 SER A CB  1 ? 16 
ATOM   2361 O  OG  . SER A 1 303 ? -14.399 24.569  -39.872 1.000 20.216 ? 303 SER A OG  1 ? 16 
ATOM   2362 N  N   . PHE A 1 304 ? -17.658 27.332  -40.584 1.000 21.570 ? 304 PHE A N   1 ? 16 
ATOM   2363 C  CA  . PHE A 1 304 ? -18.691 28.376  -40.342 1.000 23.126 ? 304 PHE A CA  1 ? 16 
ATOM   2364 C  C   . PHE A 1 304 ? -19.900 27.781  -39.648 1.000 23.793 ? 304 PHE A C   1 ? 16 
ATOM   2365 O  O   . PHE A 1 304 ? -20.189 26.589  -39.741 1.000 22.609 ? 304 PHE A O   1 ? 16 
ATOM   2366 C  CB  . PHE A 1 304 ? -19.068 29.089  -41.640 1.000 22.695 ? 304 PHE A CB  1 ? 16 
ATOM   2367 C  CG  . PHE A 1 304 ? -19.684 28.252  -42.710 1.000 23.311 ? 304 PHE A CG  1 ? 16 
ATOM   2368 C  CD1 . PHE A 1 304 ? -18.916 27.520  -43.594 1.000 22.935 ? 304 PHE A CD1 1 ? 16 
ATOM   2369 C  CD2 . PHE A 1 304 ? -21.059 28.143  -42.838 1.000 24.241 ? 304 PHE A CD2 1 ? 16 
ATOM   2370 C  CE1 . PHE A 1 304 ? -19.515 26.753  -44.581 1.000 23.041 ? 304 PHE A CE1 1 ? 16 
ATOM   2371 C  CE2 . PHE A 1 304 ? -21.641 27.368  -43.819 1.000 25.338 ? 304 PHE A CE2 1 ? 16 
ATOM   2372 C  CZ  . PHE A 1 304 ? -20.870 26.657  -44.674 1.000 23.615 ? 304 PHE A CZ  1 ? 16 
ATOM   2373 N  N   A ARG A 1 305 ? -20.613 28.647  -38.921 0.500 24.734 ? 305 ARG A N   1 ? 16 
ATOM   2374 N  N   B ARG A 1 305 ? -20.571 28.625  -38.868 0.500 24.417 ? 305 ARG A N   1 ? 16 
ATOM   2375 C  CA  A ARG A 1 305 ? -21.813 28.283  -38.132 0.500 25.926 ? 305 ARG A CA  1 ? 16 
ATOM   2376 C  CA  B ARG A 1 305 ? -21.813 28.263  -38.158 0.500 25.360 ? 305 ARG A CA  1 ? 16 
ATOM   2377 C  C   A ARG A 1 305 ? -23.066 28.929  -38.777 0.500 26.486 ? 305 ARG A C   1 ? 16 
ATOM   2378 C  C   B ARG A 1 305 ? -23.010 28.870  -38.917 0.500 26.115 ? 305 ARG A C   1 ? 16 
ATOM   2379 O  O   A ARG A 1 305 ? -23.084 30.185  -39.027 0.500 26.583 ? 305 ARG A O   1 ? 16 
ATOM   2380 O  O   B ARG A 1 305 ? -22.908 30.035  -39.414 0.500 26.466 ? 305 ARG A O   1 ? 16 
ATOM   2381 C  CB  A ARG A 1 305 ? -21.661 28.730  -36.678 0.500 27.538 ? 305 ARG A CB  1 ? 16 
ATOM   2382 C  CB  B ARG A 1 305 ? -21.796 28.793  -36.728 0.500 26.543 ? 305 ARG A CB  1 ? 16 
ATOM   2383 C  CG  A ARG A 1 305 ? -20.454 28.136  -35.937 0.500 28.272 ? 305 ARG A CG  1 ? 16 
ATOM   2384 C  CG  B ARG A 1 305 ? -20.705 28.201  -35.834 0.500 27.095 ? 305 ARG A CG  1 ? 16 
ATOM   2385 C  CD  A ARG A 1 305 ? -20.433 28.443  -34.428 0.500 29.842 ? 305 ARG A CD  1 ? 16 
ATOM   2386 C  CD  B ARG A 1 305 ? -20.961 28.512  -34.358 0.500 28.609 ? 305 ARG A CD  1 ? 16 
ATOM   2387 N  NE  A ARG A 1 305 ? -21.535 27.805  -33.673 0.500 31.312 ? 305 ARG A NE  1 ? 16 
ATOM   2388 N  NE  B ARG A 1 305 ? -21.003 29.946  -34.052 0.500 29.298 ? 305 ARG A NE  1 ? 16 
ATOM   2389 C  CZ  A ARG A 1 305 ? -21.855 27.973  -32.366 0.500 32.359 ? 305 ARG A CZ  1 ? 16 
ATOM   2390 C  CZ  B ARG A 1 305 ? -22.098 30.665  -33.833 0.500 31.025 ? 305 ARG A CZ  1 ? 16 
ATOM   2391 N  NH1 A ARG A 1 305 ? -21.174 28.791  -31.581 0.500 34.977 ? 305 ARG A NH1 1 ? 16 
ATOM   2392 N  NH1 B ARG A 1 305 ? -23.293 30.098  -33.826 0.500 30.151 ? 305 ARG A NH1 1 ? 16 
ATOM   2393 N  NH2 A ARG A 1 305 ? -22.887 27.319  -31.839 0.500 32.118 ? 305 ARG A NH2 1 ? 16 
ATOM   2394 N  NH2 B ARG A 1 305 ? -21.998 31.961  -33.568 0.500 33.450 ? 305 ARG A NH2 1 ? 16 
ATOM   2395 N  N   . MET A 1 306 ? -24.087 28.098  -38.997 1.000 26.112 ? 306 MET A N   1 ? 16 
ATOM   2396 C  CA  . MET A 1 306 ? -25.356 28.517  -39.626 1.000 27.222 ? 306 MET A CA  1 ? 16 
ATOM   2397 C  C   . MET A 1 306 ? -26.254 29.158  -38.584 1.000 29.931 ? 306 MET A C   1 ? 16 
ATOM   2398 O  O   . MET A 1 306 ? -26.475 28.562  -37.529 1.000 30.092 ? 306 MET A O   1 ? 16 
ATOM   2399 C  CB  . MET A 1 306 ? -26.054 27.311  -40.240 1.000 27.120 ? 306 MET A CB  1 ? 16 
ATOM   2400 C  CG  . MET A 1 306 ? -25.297 26.692  -41.399 1.000 27.227 ? 306 MET A CG  1 ? 16 
ATOM   2401 S  SD  . MET A 1 306 ? -25.063 27.853  -42.758 1.000 30.155 ? 306 MET A SD  1 ? 16 
ATOM   2402 C  CE  . MET A 1 306 ? -26.713 28.041  -43.404 1.000 32.414 ? 306 MET A CE  1 ? 16 
ATOM   2403 N  N   . ARG A 1 307 ? -26.908 30.245  -38.930 1.000 32.606 ? 307 ARG A N   1 ? 16 
ATOM   2404 C  CA  . ARG A 1 307 ? -27.921 30.869  -38.020 1.000 35.020 ? 307 ARG A CA  1 ? 16 
ATOM   2405 C  C   . ARG A 1 307 ? -29.044 29.896  -37.680 1.000 35.698 ? 307 ARG A C   1 ? 16 
ATOM   2406 O  O   . ARG A 1 307 ? -29.583 29.978  -36.524 1.000 37.191 ? 307 ARG A O   1 ? 16 
ATOM   2407 C  CB  . ARG A 1 307 ? -28.539 32.124  -38.649 1.000 38.669 ? 307 ARG A CB  1 ? 16 
ATOM   2408 C  CG  . ARG A 1 307 ? -27.515 33.224  -38.832 1.000 40.492 ? 307 ARG A CG  1 ? 16 
ATOM   2409 C  CD  . ARG A 1 307 ? -28.147 34.582  -39.034 1.000 44.729 ? 307 ARG A CD  1 ? 16 
ATOM   2410 N  NE  . ARG A 1 307 ? -27.089 35.571  -39.228 1.000 47.668 ? 307 ARG A NE  1 ? 16 
ATOM   2411 C  CZ  . ARG A 1 307 ? -26.458 36.199  -38.240 1.000 49.673 ? 307 ARG A CZ  1 ? 16 
ATOM   2412 N  NH1 . ARG A 1 307 ? -25.551 37.116  -38.508 1.000 52.492 ? 307 ARG A NH1 1 ? 16 
ATOM   2413 N  NH2 . ARG A 1 307 ? -26.786 35.955  -36.987 1.000 50.985 ? 307 ARG A NH2 1 ? 16 
ATOM   2414 N  N   . GLY A 1 308 ? -29.474 29.097  -38.647 1.000 33.305 ? 308 GLY A N   1 ? 16 
ATOM   2415 C  CA  . GLY A 1 308 ? -30.626 28.201  -38.463 1.000 34.322 ? 308 GLY A CA  1 ? 16 
ATOM   2416 C  C   . GLY A 1 308 ? -30.267 26.896  -37.758 1.000 32.931 ? 308 GLY A C   1 ? 16 
ATOM   2417 O  O   . GLY A 1 308 ? -31.076 25.963  -37.827 1.000 34.128 ? 308 GLY A O   1 ? 16 
ATOM   2418 N  N   . GLY A 1 309 ? -29.086 26.787  -37.140 1.000 30.484 ? 309 GLY A N   1 ? 16 
ATOM   2419 C  CA  . GLY A 1 309 ? -28.802 25.668  -36.247 1.000 31.280 ? 309 GLY A CA  1 ? 16 
ATOM   2420 C  C   . GLY A 1 309 ? -28.365 24.410  -37.001 1.000 28.652 ? 309 GLY A C   1 ? 16 
ATOM   2421 O  O   . GLY A 1 309 ? -28.065 24.478  -38.217 1.000 27.255 ? 309 GLY A O   1 ? 16 
ATOM   2422 N  N   . GLU A 1 310 ? -28.469 23.301  -36.321 1.000 29.734 ? 310 GLU A N   1 ? 16 
ATOM   2423 C  CA  . GLU A 1 310 ? -28.096 21.978  -36.870 1.000 30.143 ? 310 GLU A CA  1 ? 16 
ATOM   2424 C  C   . GLU A 1 310 ? -28.901 21.737  -38.152 1.000 30.209 ? 310 GLU A C   1 ? 16 
ATOM   2425 O  O   . GLU A 1 310 ? -28.352 21.215  -39.121 1.000 28.151 ? 310 GLU A O   1 ? 16 
ATOM   2426 C  CB  . GLU A 1 310 ? -28.359 20.888  -35.857 1.000 32.289 ? 310 GLU A CB  1 ? 16 
ATOM   2427 C  CG  . GLU A 1 310 ? -27.914 19.512  -36.321 1.000 34.960 ? 310 GLU A CG  1 ? 16 
ATOM   2428 C  CD  . GLU A 1 310 ? -28.210 18.379  -35.359 1.000 38.489 ? 310 GLU A CD  1 ? 16 
ATOM   2429 O  OE1 . GLU A 1 310 ? -29.309 17.881  -35.389 1.000 43.146 ? 310 GLU A OE1 1 ? 16 
ATOM   2430 O  OE2 . GLU A 1 310 ? -27.305 17.994  -34.613 1.000 45.892 ? 310 GLU A OE2 1 ? 16 
ATOM   2431 N  N   . GLU A 1 311 ? -30.208 22.019  -38.127 1.000 31.466 ? 311 GLU A N   1 ? 16 
ATOM   2432 C  CA  . GLU A 1 311 ? -31.086 21.740  -39.277 1.000 33.160 ? 311 GLU A CA  1 ? 16 
ATOM   2433 C  C   . GLU A 1 311 ? -30.498 22.436  -40.517 1.000 30.469 ? 311 GLU A C   1 ? 16 
ATOM   2434 O  O   . GLU A 1 311 ? -30.409 21.783  -41.573 1.000 30.605 ? 311 GLU A O   1 ? 16 
ATOM   2435 C  CB  . GLU A 1 311 ? -32.500 22.166  -38.877 1.000 37.173 ? 311 GLU A CB  1 ? 16 
ATOM   2436 C  CG  . GLU A 1 311 ? -33.539 22.074  -39.944 1.000 43.055 ? 311 GLU A CG  1 ? 16 
ATOM   2437 C  CD  . GLU A 1 311 ? -34.905 22.599  -39.436 1.000 48.021 ? 311 GLU A CD  1 ? 16 
ATOM   2438 O  OE1 . GLU A 1 311 ? -35.005 23.778  -39.064 1.000 50.779 ? 311 GLU A OE1 1 ? 16 
ATOM   2439 O  OE2 . GLU A 1 311 ? -35.806 21.804  -39.276 1.000 57.749 ? 311 GLU A OE2 1 ? 16 
ATOM   2440 N  N   . ALA A 1 312 ? -30.100 23.698  -40.414 1.000 28.894 ? 312 ALA A N   1 ? 16 
ATOM   2441 C  CA  . ALA A 1 312 ? -29.586 24.490  -41.551 1.000 29.365 ? 312 ALA A CA  1 ? 16 
ATOM   2442 C  C   . ALA A 1 312 ? -28.238 23.934  -41.981 1.000 27.578 ? 312 ALA A C   1 ? 16 
ATOM   2443 O  O   . ALA A 1 312 ? -27.969 23.862  -43.200 1.000 27.795 ? 312 ALA A O   1 ? 16 
ATOM   2444 C  CB  . ALA A 1 312 ? -29.501 25.979  -41.193 1.000 30.037 ? 312 ALA A CB  1 ? 16 
ATOM   2445 N  N   . ALA A 1 313 ? -27.381 23.605  -41.030 1.000 25.888 ? 313 ALA A N   1 ? 16 
ATOM   2446 C  CA  . ALA A 1 313 ? -26.033 23.047  -41.369 1.000 25.872 ? 313 ALA A CA  1 ? 16 
ATOM   2447 C  C   . ALA A 1 313 ? -26.178 21.736  -42.166 1.000 26.777 ? 313 ALA A C   1 ? 16 
ATOM   2448 O  O   . ALA A 1 313 ? -25.395 21.543  -43.120 1.000 25.946 ? 313 ALA A O   1 ? 16 
ATOM   2449 C  CB  . ALA A 1 313 ? -25.192 22.835  -40.119 1.000 25.618 ? 313 ALA A CB  1 ? 16 
ATOM   2450 N  N   . LEU A 1 314 ? -27.024 20.826  -41.734 1.000 27.703 ? 314 LEU A N   1 ? 17 
ATOM   2451 C  CA  . LEU A 1 314 ? -27.212 19.544  -42.426 1.000 27.907 ? 314 LEU A CA  1 ? 17 
ATOM   2452 C  C   . LEU A 1 314 ? -27.754 19.804  -43.840 1.000 27.594 ? 314 LEU A C   1 ? 17 
ATOM   2453 O  O   . LEU A 1 314 ? -27.317 19.099  -44.771 1.000 26.388 ? 314 LEU A O   1 ? 17 
ATOM   2454 C  CB  . LEU A 1 314 ? -28.132 18.616  -41.650 1.000 29.227 ? 314 LEU A CB  1 ? 17 
ATOM   2455 C  CG  . LEU A 1 314 ? -27.668 18.204  -40.252 1.000 30.878 ? 314 LEU A CG  1 ? 17 
ATOM   2456 C  CD1 . LEU A 1 314 ? -28.743 17.366  -39.548 1.000 32.947 ? 314 LEU A CD1 1 ? 17 
ATOM   2457 C  CD2 . LEU A 1 314 ? -26.353 17.500  -40.295 1.000 29.541 ? 314 LEU A CD2 1 ? 17 
ATOM   2458 N  N   . ARG A 1 315 ? -28.605 20.786  -43.997 1.000 28.713 ? 315 ARG A N   1 ? 17 
ATOM   2459 C  CA  . ARG A 1 315 ? -29.171 21.109  -45.350 1.000 31.669 ? 315 ARG A CA  1 ? 17 
ATOM   2460 C  C   . ARG A 1 315 ? -28.079 21.605  -46.276 1.000 29.453 ? 315 ARG A C   1 ? 17 
ATOM   2461 O  O   . ARG A 1 315 ? -27.998 21.091  -47.415 1.000 27.422 ? 315 ARG A O   1 ? 17 
ATOM   2462 C  CB  . ARG A 1 315 ? -30.279 22.154  -45.318 1.000 35.160 ? 315 ARG A CB  1 ? 17 
ATOM   2463 C  CG  . ARG A 1 315 ? -31.623 21.517  -45.080 1.000 43.392 ? 315 ARG A CG  1 ? 17 
ATOM   2464 C  CD  . ARG A 1 315 ? -32.761 22.527  -45.274 1.000 50.208 ? 315 ARG A CD  1 ? 17 
ATOM   2465 N  NE  . ARG A 1 315 ? -32.323 23.890  -45.003 1.000 52.785 ? 315 ARG A NE  1 ? 17 
ATOM   2466 C  CZ  . ARG A 1 315 ? -32.603 24.595  -43.903 1.000 57.957 ? 315 ARG A CZ  1 ? 17 
ATOM   2467 N  NH1 . ARG A 1 315 ? -32.166 25.847  -43.846 1.000 58.701 ? 315 ARG A NH1 1 ? 17 
ATOM   2468 N  NH2 . ARG A 1 315 ? -33.330 24.075  -42.895 1.000 58.683 ? 315 ARG A NH2 1 ? 17 
ATOM   2469 N  N   . VAL A 1 316 ? -27.182 22.481  -45.786 1.000 28.032 ? 316 VAL A N   1 ? 17 
ATOM   2470 C  CA  . VAL A 1 316 ? -26.081 23.003  -46.640 1.000 27.337 ? 316 VAL A CA  1 ? 17 
ATOM   2471 C  C   . VAL A 1 316 ? -25.206 21.816  -47.100 1.000 25.729 ? 316 VAL A C   1 ? 17 
ATOM   2472 O  O   . VAL A 1 316 ? -24.836 21.697  -48.284 1.000 25.052 ? 316 VAL A O   1 ? 17 
ATOM   2473 C  CB  . VAL A 1 316 ? -25.268 24.075  -45.889 1.000 27.998 ? 316 VAL A CB  1 ? 17 
ATOM   2474 C  CG1 . VAL A 1 316 ? -24.068 24.467  -46.714 1.000 29.168 ? 316 VAL A CG1 1 ? 17 
ATOM   2475 C  CG2 . VAL A 1 316 ? -26.090 25.278  -45.576 1.000 31.949 ? 316 VAL A CG2 1 ? 17 
ATOM   2476 N  N   . CYS A 1 317 ? -24.816 20.975  -46.150 1.000 24.992 ? 317 CYS A N   1 ? 17 
ATOM   2477 C  CA  . CYS A 1 317 ? -23.965 19.828  -46.407 1.000 23.654 ? 317 CYS A CA  1 ? 17 
ATOM   2478 C  C   . CYS A 1 317 ? -24.546 18.981  -47.561 1.000 24.426 ? 317 CYS A C   1 ? 17 
ATOM   2479 O  O   . CYS A 1 317 ? -23.739 18.412  -48.304 1.000 24.704 ? 317 CYS A O   1 ? 17 
ATOM   2480 C  CB  . CYS A 1 317 ? -23.810 18.987  -45.147 1.000 24.123 ? 317 CYS A CB  1 ? 17 
ATOM   2481 S  SG  . CYS A 1 317 ? -22.665 19.730  -43.979 1.000 25.205 ? 317 CYS A SG  1 ? 17 
ATOM   2482 N  N   . ALA A 1 318 ? -25.855 18.781  -47.599 1.000 25.304 ? 318 ALA A N   1 ? 17 
ATOM   2483 C  CA  . ALA A 1 318 ? -26.525 17.893  -48.585 1.000 26.687 ? 318 ALA A CA  1 ? 17 
ATOM   2484 C  C   . ALA A 1 318 ? -26.687 18.550  -49.949 1.000 27.502 ? 318 ALA A C   1 ? 17 
ATOM   2485 O  O   . ALA A 1 318 ? -27.007 17.825  -50.881 1.000 29.170 ? 318 ALA A O   1 ? 17 
ATOM   2486 C  CB  . ALA A 1 318 ? -27.847 17.466  -48.079 1.000 28.511 ? 318 ALA A CB  1 ? 17 
ATOM   2487 N  N   . LYS A 1 319 ? -26.589 19.882  -50.021 1.000 26.634 ? 319 LYS A N   1 ? 17 
ATOM   2488 C  CA  . LYS A 1 319 ? -27.040 20.684  -51.173 1.000 27.442 ? 319 LYS A CA  1 ? 17 
ATOM   2489 C  C   . LYS A 1 319 ? -25.881 21.056  -52.123 1.000 25.476 ? 319 LYS A C   1 ? 17 
ATOM   2490 O  O   . LYS A 1 319 ? -26.166 21.356  -53.277 1.000 25.958 ? 319 LYS A O   1 ? 17 
ATOM   2491 C  CB  . LYS A 1 319 ? -27.764 21.915  -50.660 1.000 29.158 ? 319 LYS A CB  1 ? 17 
ATOM   2492 C  CG  . LYS A 1 319 ? -28.655 22.560  -51.667 1.000 34.907 ? 319 LYS A CG  1 ? 17 
ATOM   2493 C  CD  . LYS A 1 319 ? -29.713 23.458  -51.048 1.000 37.563 ? 319 LYS A CD  1 ? 17 
ATOM   2494 C  CE  . LYS A 1 319 ? -30.349 24.323  -52.097 1.000 40.536 ? 319 LYS A CE  1 ? 17 
ATOM   2495 N  NZ  . LYS A 1 319 ? -30.859 25.579  -51.509 1.000 43.548 ? 319 LYS A NZ  1 ? 17 
ATOM   2496 N  N   . THR A 1 320 ? -24.632 21.020  -51.673 1.000 24.492 ? 320 THR A N   1 ? 17 
ATOM   2497 C  CA  . THR A 1 320 ? -23.481 21.345  -52.545 1.000 24.074 ? 320 THR A CA  1 ? 17 
ATOM   2498 C  C   . THR A 1 320 ? -23.388 20.331  -53.695 1.000 25.529 ? 320 THR A C   1 ? 17 
ATOM   2499 O  O   . THR A 1 320 ? -23.630 19.116  -53.489 1.000 25.116 ? 320 THR A O   1 ? 17 
ATOM   2500 C  CB  . THR A 1 320 ? -22.165 21.445  -51.792 1.000 23.688 ? 320 THR A CB  1 ? 17 
ATOM   2501 O  OG1 . THR A 1 320 ? -21.931 20.208  -51.123 1.000 24.314 ? 320 THR A OG1 1 ? 17 
ATOM   2502 C  CG2 . THR A 1 320 ? -22.166 22.622  -50.840 1.000 23.425 ? 320 THR A CG2 1 ? 17 
ATOM   2503 N  N   A LYS A 1 321 ? -23.009 20.823  -54.873 0.500 26.485 ? 321 LYS A N   1 ? 17 
ATOM   2504 N  N   B LYS A 1 321 ? -23.025 20.826  -54.875 0.500 26.067 ? 321 LYS A N   1 ? 17 
ATOM   2505 C  CA  A LYS A 1 321 ? -22.885 20.002  -56.100 0.500 28.734 ? 321 LYS A CA  1 ? 17 
ATOM   2506 C  CA  B LYS A 1 321 ? -22.898 20.004  -56.099 0.500 27.962 ? 321 LYS A CA  1 ? 17 
ATOM   2507 C  C   A LYS A 1 321 ? -21.440 19.926  -56.571 0.500 28.016 ? 321 LYS A C   1 ? 17 
ATOM   2508 C  C   B LYS A 1 321 ? -21.425 19.868  -56.490 0.500 27.546 ? 321 LYS A C   1 ? 17 
ATOM   2509 O  O   A LYS A 1 321 ? -21.196 19.123  -57.494 0.500 29.343 ? 321 LYS A O   1 ? 17 
ATOM   2510 O  O   B LYS A 1 321 ? -21.116 18.898  -57.191 0.500 29.276 ? 321 LYS A O   1 ? 17 
ATOM   2511 C  CB  A LYS A 1 321 ? -23.759 20.567  -57.209 0.500 32.558 ? 321 LYS A CB  1 ? 17 
ATOM   2512 C  CB  B LYS A 1 321 ? -23.777 20.585  -57.202 0.500 30.965 ? 321 LYS A CB  1 ? 17 
ATOM   2513 C  CG  A LYS A 1 321 ? -25.227 20.240  -57.047 0.500 36.696 ? 321 LYS A CG  1 ? 17 
ATOM   2514 C  CG  B LYS A 1 321 ? -25.267 20.550  -56.887 0.500 34.086 ? 321 LYS A CG  1 ? 17 
ATOM   2515 C  CD  A LYS A 1 321 ? -26.069 20.710  -58.205 0.500 39.837 ? 321 LYS A CD  1 ? 17 
ATOM   2516 C  CD  B LYS A 1 321 ? -25.797 19.147  -56.555 0.500 34.015 ? 321 LYS A CD  1 ? 17 
ATOM   2517 C  CE  A LYS A 1 321 ? -27.506 20.930  -57.809 0.500 42.522 ? 321 LYS A CE  1 ? 17 
ATOM   2518 C  CE  B LYS A 1 321 ? -27.319 19.052  -56.573 0.500 36.789 ? 321 LYS A CE  1 ? 17 
ATOM   2519 N  NZ  A LYS A 1 321 ? -28.191 21.763  -58.811 0.500 45.801 ? 321 LYS A NZ  1 ? 17 
ATOM   2520 N  NZ  B LYS A 1 321 ? -27.920 19.419  -55.252 0.500 36.817 ? 321 LYS A NZ  1 ? 17 
ATOM   2521 N  N   . VAL A 1 322 ? -20.558 20.777  -56.060 1.000 24.752 ? 322 VAL A N   1 ? 17 
ATOM   2522 C  CA  . VAL A 1 322 ? -19.108 20.765  -56.431 1.000 23.677 ? 322 VAL A CA  1 ? 17 
ATOM   2523 C  C   . VAL A 1 322 ? -18.302 20.337  -55.207 1.000 23.026 ? 322 VAL A C   1 ? 17 
ATOM   2524 O  O   . VAL A 1 322 ? -17.577 19.320  -55.287 1.000 23.208 ? 322 VAL A O   1 ? 17 
ATOM   2525 C  CB  . VAL A 1 322 ? -18.613 22.129  -56.993 1.000 23.767 ? 322 VAL A CB  1 ? 17 
ATOM   2526 C  CG1 . VAL A 1 322 ? -17.160 21.995  -57.394 1.000 23.251 ? 322 VAL A CG1 1 ? 17 
ATOM   2527 C  CG2 . VAL A 1 322 ? -19.449 22.663  -58.125 1.000 26.210 ? 322 VAL A CG2 1 ? 17 
ATOM   2528 N  N   . PHE A 1 323 ? -18.492 20.986  -54.052 1.000 20.301 ? 323 PHE A N   1 ? 17 
ATOM   2529 C  CA  . PHE A 1 323 ? -18.026 20.440  -52.778 1.000 19.059 ? 323 PHE A CA  1 ? 17 
ATOM   2530 C  C   . PHE A 1 323 ? -18.690 19.065  -52.578 1.000 20.000 ? 323 PHE A C   1 ? 17 
ATOM   2531 O  O   . PHE A 1 323 ? -19.965 18.938  -52.664 1.000 21.796 ? 323 PHE A O   1 ? 17 
ATOM   2532 C  CB  . PHE A 1 323 ? -18.403 21.309  -51.611 1.000 18.819 ? 323 PHE A CB  1 ? 17 
ATOM   2533 C  CG  . PHE A 1 323 ? -17.641 22.602  -51.487 1.000 19.981 ? 323 PHE A CG  1 ? 17 
ATOM   2534 C  CD1 . PHE A 1 323 ? -18.002 23.716  -52.218 1.000 21.227 ? 323 PHE A CD1 1 ? 17 
ATOM   2535 C  CD2 . PHE A 1 323 ? -16.582 22.700  -50.611 1.000 19.643 ? 323 PHE A CD2 1 ? 17 
ATOM   2536 C  CE1 . PHE A 1 323 ? -17.299 24.897  -52.104 1.000 21.170 ? 323 PHE A CE1 1 ? 17 
ATOM   2537 C  CE2 . PHE A 1 323 ? -15.888 23.890  -50.481 1.000 19.404 ? 323 PHE A CE2 1 ? 17 
ATOM   2538 C  CZ  . PHE A 1 323 ? -16.241 24.995  -51.219 1.000 20.815 ? 323 PHE A CZ  1 ? 17 
ATOM   2539 N  N   . THR A 1 324 ? -17.904 18.036  -52.301 1.000 18.784 ? 324 THR A N   1 ? 17 
ATOM   2540 C  CA  . THR A 1 324 ? -18.404 16.669  -52.078 1.000 18.399 ? 324 THR A CA  1 ? 17 
ATOM   2541 C  C   . THR A 1 324 ? -18.579 16.439  -50.564 1.000 18.569 ? 324 THR A C   1 ? 17 
ATOM   2542 O  O   . THR A 1 324 ? -17.615 16.696  -49.800 1.000 17.814 ? 324 THR A O   1 ? 17 
ATOM   2543 C  CB  . THR A 1 324 ? -17.472 15.624  -52.637 1.000 19.742 ? 324 THR A CB  1 ? 17 
ATOM   2544 O  OG1 . THR A 1 324 ? -17.405 15.788  -54.067 1.000 20.087 ? 324 THR A OG1 1 ? 17 
ATOM   2545 C  CG2 . THR A 1 324 ? -17.958 14.210  -52.357 1.000 20.843 ? 324 THR A CG2 1 ? 17 
ATOM   2546 N  N   . LEU A 1 325 ? -19.737 15.921  -50.157 1.000 18.577 ? 325 LEU A N   1 ? 17 
ATOM   2547 C  CA  . LEU A 1 325 ? -20.004 15.614  -48.734 1.000 19.400 ? 325 LEU A CA  1 ? 17 
ATOM   2548 C  C   . LEU A 1 325 ? -19.301 14.300  -48.382 1.000 18.454 ? 325 LEU A C   1 ? 17 
ATOM   2549 O  O   . LEU A 1 325 ? -19.670 13.239  -48.882 1.000 18.972 ? 325 LEU A O   1 ? 17 
ATOM   2550 C  CB  . LEU A 1 325 ? -21.498 15.454  -48.515 1.000 19.340 ? 325 LEU A CB  1 ? 17 
ATOM   2551 C  CG  . LEU A 1 325 ? -21.932 15.101  -47.080 1.000 20.708 ? 325 LEU A CG  1 ? 17 
ATOM   2552 C  CD1 . LEU A 1 325 ? -21.426 16.095  -46.105 1.000 21.587 ? 325 LEU A CD1 1 ? 17 
ATOM   2553 C  CD2 . LEU A 1 325 ? -23.446 15.004  -47.043 1.000 21.013 ? 325 LEU A CD2 1 ? 17 
ATOM   2554 N  N   . ALA A 1 326 ? -18.256 14.415  -47.578 1.000 18.671 ? 326 ALA A N   1 ? 17 
ATOM   2555 C  CA  . ALA A 1 326 ? -17.392 13.262  -47.235 1.000 18.031 ? 326 ALA A CA  1 ? 17 
ATOM   2556 C  C   . ALA A 1 326 ? -16.472 13.664  -46.096 1.000 18.491 ? 326 ALA A C   1 ? 17 
ATOM   2557 O  O   . ALA A 1 326 ? -16.253 14.879  -45.903 1.000 19.442 ? 326 ALA A O   1 ? 17 
ATOM   2558 C  CB  . ALA A 1 326 ? -16.542 12.880  -48.409 1.000 18.246 ? 326 ALA A CB  1 ? 17 
ATOM   2559 N  N   . GLU A 1 327 ? -15.992 12.698  -45.353 1.000 18.258 ? 327 GLU A N   1 ? 17 
ATOM   2560 C  CA  . GLU A 1 327 ? -14.889 12.921  -44.409 1.000 17.984 ? 327 GLU A CA  1 ? 17 
ATOM   2561 C  C   . GLU A 1 327 ? -13.610 13.246  -45.205 1.000 18.917 ? 327 GLU A C   1 ? 17 
ATOM   2562 O  O   . GLU A 1 327 ? -13.548 13.068  -46.450 1.000 18.349 ? 327 GLU A O   1 ? 17 
ATOM   2563 C  CB  . GLU A 1 327 ? -14.738 11.714  -43.505 1.000 20.499 ? 327 GLU A CB  1 ? 17 
ATOM   2564 C  CG  . GLU A 1 327 ? -15.947 11.498  -42.609 1.000 22.786 ? 327 GLU A CG  1 ? 17 
ATOM   2565 C  CD  . GLU A 1 327 ? -15.681 10.676  -41.350 1.000 27.165 ? 327 GLU A CD  1 ? 17 
ATOM   2566 O  OE1 . GLU A 1 327 ? -14.523 10.080  -41.197 1.000 29.704 ? 327 GLU A OE1 1 ? 17 
ATOM   2567 O  OE2 . GLU A 1 327 ? -16.640 10.518  -40.567 1.000 27.594 ? 327 GLU A OE2 1 ? 17 
ATOM   2568 N  N   . SER A 1 328 ? -12.621 13.703  -44.479 1.000 18.206 ? 328 SER A N   1 ? 17 
ATOM   2569 C  CA  . SER A 1 328 ? -11.288 13.994  -45.002 1.000 18.291 ? 328 SER A CA  1 ? 17 
ATOM   2570 C  C   . SER A 1 328 ? -11.141 15.417  -45.504 1.000 18.703 ? 328 SER A C   1 ? 17 
ATOM   2571 O  O   . SER A 1 328 ? -12.088 16.261  -45.394 1.000 19.876 ? 328 SER A O   1 ? 17 
ATOM   2572 C  CB  . SER A 1 328 ? -10.837 12.977  -46.036 1.000 19.392 ? 328 SER A CB  1 ? 17 
ATOM   2573 O  OG  . SER A 1 328 ? -9.391  13.022  -46.078 1.000 19.735 ? 328 SER A OG  1 ? 17 
ATOM   2574 N  N   . LEU A 1 329 ? -9.927  15.769  -45.902 1.000 18.654 ? 329 LEU A N   1 ? 17 
ATOM   2575 C  CA  . LEU A 1 329 ? -9.578  17.166  -46.252 1.000 18.115 ? 329 LEU A CA  1 ? 17 
ATOM   2576 C  C   . LEU A 1 329 ? -8.246  17.154  -46.995 1.000 17.829 ? 329 LEU A C   1 ? 17 
ATOM   2577 O  O   . LEU A 1 329 ? -7.575  16.103  -47.035 1.000 18.120 ? 329 LEU A O   1 ? 17 
ATOM   2578 C  CB  . LEU A 1 329 ? -9.486  18.033  -44.978 1.000 17.694 ? 329 LEU A CB  1 ? 17 
ATOM   2579 C  CG  . LEU A 1 329 ? -8.423  17.565  -43.974 1.000 18.940 ? 329 LEU A CG  1 ? 17 
ATOM   2580 C  CD1 . LEU A 1 329 ? -7.322  18.617  -43.754 1.000 18.517 ? 329 LEU A CD1 1 ? 17 
ATOM   2581 C  CD2 . LEU A 1 329 ? -9.024  17.127  -42.693 1.000 21.647 ? 329 LEU A CD2 1 ? 17 
ATOM   2582 N  N   . GLY A 1 330 ? -7.862  18.299  -47.545 1.000 16.945 ? 330 GLY A N   1 ? 17 
ATOM   2583 C  CA  . GLY A 1 330 ? -6.557  18.478  -48.144 1.000 16.998 ? 330 GLY A CA  1 ? 17 
ATOM   2584 C  C   . GLY A 1 330 ? -6.428  17.893  -49.518 1.000 17.616 ? 330 GLY A C   1 ? 17 
ATOM   2585 O  O   . GLY A 1 330 ? -5.271  17.899  -49.996 1.000 20.707 ? 330 GLY A O   1 ? 17 
ATOM   2586 N  N   . GLY A 1 331 ? -7.513  17.468  -50.142 1.000 17.893 ? 331 GLY A N   1 ? 17 
ATOM   2587 C  CA  . GLY A 1 331 ? -7.481  17.047  -51.510 1.000 18.297 ? 331 GLY A CA  1 ? 17 
ATOM   2588 C  C   . GLY A 1 331 ? -7.669  18.190  -52.490 1.000 17.716 ? 331 GLY A C   1 ? 17 
ATOM   2589 O  O   . GLY A 1 331 ? -8.151  19.272  -52.164 1.000 17.856 ? 331 GLY A O   1 ? 17 
ATOM   2590 N  N   . VAL A 1 332 ? -7.295  17.915  -53.718 1.000 17.164 ? 332 VAL A N   1 ? 17 
ATOM   2591 C  CA  . VAL A 1 332 ? -7.505  18.870  -54.816 1.000 17.238 ? 332 VAL A CA  1 ? 17 
ATOM   2592 C  C   . VAL A 1 332 ? -9.014  19.095  -54.945 1.000 17.325 ? 332 VAL A C   1 ? 17 
ATOM   2593 O  O   . VAL A 1 332 ? -9.415  20.201  -55.352 1.000 17.364 ? 332 VAL A O   1 ? 17 
ATOM   2594 C  CB  . VAL A 1 332 ? -6.881  18.415  -56.115 1.000 17.620 ? 332 VAL A CB  1 ? 17 
ATOM   2595 C  CG1 . VAL A 1 332 ? -5.337  18.437  -55.987 1.000 18.224 ? 332 VAL A CG1 1 ? 17 
ATOM   2596 C  CG2 . VAL A 1 332 ? -7.359  17.019  -56.534 1.000 18.480 ? 332 VAL A CG2 1 ? 17 
ATOM   2597 N  N   . GLU A 1 333 ? -9.803  18.077  -54.688 1.000 19.782 ? 333 GLU A N   1 ? 18 
ATOM   2598 C  CA  . GLU A 1 333 ? -11.245 18.239  -54.773 1.000 19.836 ? 333 GLU A CA  1 ? 18 
ATOM   2599 C  C   . GLU A 1 333 ? -11.801 18.838  -53.487 1.000 20.125 ? 333 GLU A C   1 ? 18 
ATOM   2600 O  O   . GLU A 1 333 ? -11.401 18.437  -52.400 1.000 19.542 ? 333 GLU A O   1 ? 18 
ATOM   2601 C  CB  . GLU A 1 333 ? -11.886 16.915  -55.128 1.000 22.068 ? 333 GLU A CB  1 ? 18 
ATOM   2602 C  CG  . GLU A 1 333 ? -12.008 15.962  -53.998 1.000 24.381 ? 333 GLU A CG  1 ? 18 
ATOM   2603 C  CD  . GLU A 1 333 ? -10.752 15.442  -53.304 1.000 30.725 ? 333 GLU A CD  1 ? 18 
ATOM   2604 O  OE1 . GLU A 1 333 ? -9.525  15.355  -53.874 1.000 32.053 ? 333 GLU A OE1 1 ? 18 
ATOM   2605 O  OE2 . GLU A 1 333 ? -11.036 14.956  -52.090 1.000 40.249 ? 333 GLU A OE2 1 ? 18 
ATOM   2606 N  N   . SER A 1 334 ? -12.717 19.763  -53.607 1.000 18.367 ? 334 SER A N   1 ? 18 
ATOM   2607 C  CA  . SER A 1 334 ? -13.377 20.402  -52.439 1.000 19.095 ? 334 SER A CA  1 ? 18 
ATOM   2608 C  C   . SER A 1 334 ? -14.241 19.395  -51.670 1.000 18.810 ? 334 SER A C   1 ? 18 
ATOM   2609 O  O   . SER A 1 334 ? -15.003 18.603  -52.291 1.000 19.401 ? 334 SER A O   1 ? 18 
ATOM   2610 C  CB  . SER A 1 334 ? -14.180 21.568  -52.848 1.000 19.249 ? 334 SER A CB  1 ? 18 
ATOM   2611 O  OG  . SER A 1 334 ? -13.344 22.609  -53.348 1.000 18.318 ? 334 SER A OG  1 ? 18 
ATOM   2612 N  N   . LEU A 1 335 ? -14.152 19.436  -50.337 1.000 18.924 ? 335 LEU A N   1 ? 18 
ATOM   2613 C  CA  . LEU A 1 335 ? -14.964 18.573  -49.465 1.000 19.343 ? 335 LEU A CA  1 ? 18 
ATOM   2614 C  C   . LEU A 1 335 ? -15.691 19.448  -48.449 1.000 19.069 ? 335 LEU A C   1 ? 18 
ATOM   2615 O  O   . LEU A 1 335 ? -15.223 20.537  -48.053 1.000 19.531 ? 335 LEU A O   1 ? 18 
ATOM   2616 C  CB  . LEU A 1 335 ? -14.090 17.553  -48.744 1.000 19.331 ? 335 LEU A CB  1 ? 18 
ATOM   2617 C  CG  . LEU A 1 335 ? -13.275 16.628  -49.635 1.000 20.128 ? 335 LEU A CG  1 ? 18 
ATOM   2618 C  CD1 . LEU A 1 335 ? -12.276 15.776  -48.837 1.000 21.189 ? 335 LEU A CD1 1 ? 18 
ATOM   2619 C  CD2 . LEU A 1 335 ? -14.157 15.665  -50.454 1.000 22.148 ? 335 LEU A CD2 1 ? 18 
ATOM   2620 N  N   . ILE A 1 336 ? -16.869 18.954  -48.087 1.000 18.657 ? 336 ILE A N   1 ? 18 
ATOM   2621 C  CA  . ILE A 1 336 ? -17.714 19.591  -47.045 1.000 18.456 ? 336 ILE A CA  1 ? 18 
ATOM   2622 C  C   . ILE A 1 336 ? -18.113 18.479  -46.074 1.000 18.405 ? 336 ILE A C   1 ? 18 
ATOM   2623 O  O   . ILE A 1 336 ? -18.336 17.321  -46.466 1.000 18.667 ? 336 ILE A O   1 ? 18 
ATOM   2624 C  CB  . ILE A 1 336 ? -18.929 20.298  -47.705 1.000 19.753 ? 336 ILE A CB  1 ? 18 
ATOM   2625 C  CG1 . ILE A 1 336 ? -19.792 20.966  -46.635 1.000 21.104 ? 336 ILE A CG1 1 ? 18 
ATOM   2626 C  CG2 . ILE A 1 336 ? -19.771 19.321  -48.539 1.000 21.912 ? 336 ILE A CG2 1 ? 18 
ATOM   2627 C  CD1 . ILE A 1 336 ? -20.761 21.997  -47.207 1.000 22.261 ? 336 ILE A CD1 1 ? 18 
ATOM   2628 N  N   . GLU A 1 337 ? -18.251 18.825  -44.784 1.000 19.148 ? 337 GLU A N   1 ? 18 
ATOM   2629 C  CA  . GLU A 1 337 ? -18.800 17.867  -43.808 1.000 19.330 ? 337 GLU A CA  1 ? 18 
ATOM   2630 C  C   . GLU A 1 337 ? -19.412 18.604  -42.621 1.000 19.338 ? 337 GLU A C   1 ? 18 
ATOM   2631 O  O   . GLU A 1 337 ? -19.233 19.800  -42.452 1.000 18.801 ? 337 GLU A O   1 ? 18 
ATOM   2632 C  CB  . GLU A 1 337 ? -17.742 16.869  -43.294 1.000 19.307 ? 337 GLU A CB  1 ? 18 
ATOM   2633 C  CG  . GLU A 1 337 ? -16.647 17.509  -42.473 1.000 19.883 ? 337 GLU A CG  1 ? 18 
ATOM   2634 C  CD  . GLU A 1 337 ? -16.317 16.796  -41.158 1.000 20.646 ? 337 GLU A CD  1 ? 18 
ATOM   2635 O  OE1 . GLU A 1 337 ? -15.422 17.282  -40.389 1.000 20.616 ? 337 GLU A OE1 1 ? 18 
ATOM   2636 O  OE2 . GLU A 1 337 ? -16.902 15.731  -40.887 1.000 24.144 ? 337 GLU A OE2 1 ? 18 
ATOM   2637 N  N   . HIS A 1 338 ? -20.146 17.812  -41.835 1.000 19.720 ? 338 HIS A N   1 ? 18 
ATOM   2638 C  CA  . HIS A 1 338 ? -20.719 18.212  -40.538 1.000 20.537 ? 338 HIS A CA  1 ? 18 
ATOM   2639 C  C   . HIS A 1 338 ? -19.918 17.503  -39.460 1.000 21.075 ? 338 HIS A C   1 ? 18 
ATOM   2640 O  O   . HIS A 1 338 ? -20.124 16.319  -39.223 1.000 20.986 ? 338 HIS A O   1 ? 18 
ATOM   2641 C  CB  . HIS A 1 338 ? -22.168 17.833  -40.512 1.000 21.605 ? 338 HIS A CB  1 ? 18 
ATOM   2642 C  CG  . HIS A 1 338 ? -22.837 18.273  -39.267 1.000 22.790 ? 338 HIS A CG  1 ? 18 
ATOM   2643 N  ND1 . HIS A 1 338 ? -22.986 17.443  -38.166 1.000 22.077 ? 338 HIS A ND1 1 ? 18 
ATOM   2644 C  CD2 . HIS A 1 338 ? -23.416 19.474  -38.966 1.000 23.725 ? 338 HIS A CD2 1 ? 18 
ATOM   2645 C  CE1 . HIS A 1 338 ? -23.631 18.139  -37.247 1.000 24.793 ? 338 HIS A CE1 1 ? 18 
ATOM   2646 N  NE2 . HIS A 1 338 ? -23.937 19.353  -37.705 1.000 23.505 ? 338 HIS A NE2 1 ? 18 
ATOM   2647 N  N   . PRO A 1 339 ? -18.936 18.174  -38.825 1.000 20.997 ? 339 PRO A N   1 ? 18 
ATOM   2648 C  CA  . PRO A 1 339 ? -18.128 17.488  -37.824 1.000 21.080 ? 339 PRO A CA  1 ? 18 
ATOM   2649 C  C   . PRO A 1 339 ? -18.943 16.825  -36.724 1.000 21.471 ? 339 PRO A C   1 ? 18 
ATOM   2650 O  O   . PRO A 1 339 ? -18.576 15.723  -36.288 1.000 21.162 ? 339 PRO A O   1 ? 18 
ATOM   2651 C  CB  . PRO A 1 339 ? -17.238 18.611  -37.229 1.000 22.451 ? 339 PRO A CB  1 ? 18 
ATOM   2652 C  CG  . PRO A 1 339 ? -17.106 19.605  -38.450 1.000 23.522 ? 339 PRO A CG  1 ? 18 
ATOM   2653 C  CD  . PRO A 1 339 ? -18.515 19.575  -39.077 1.000 21.948 ? 339 PRO A CD  1 ? 18 
ATOM   2654 N  N   . GLY A 1 340 ? -20.024 17.456  -36.280 1.000 22.645 ? 340 GLY A N   1 ? 18 
ATOM   2655 C  CA  . GLY A 1 340 ? -20.756 16.917  -35.112 1.000 23.052 ? 340 GLY A CA  1 ? 18 
ATOM   2656 C  C   . GLY A 1 340 ? -21.252 15.488  -35.351 1.000 23.346 ? 340 GLY A C   1 ? 18 
ATOM   2657 O  O   . GLY A 1 340 ? -21.263 14.681  -34.413 1.000 22.948 ? 340 GLY A O   1 ? 18 
ATOM   2658 N  N   . LYS A 1 341 ? -21.671 15.181  -36.581 1.000 22.209 ? 341 LYS A N   1 ? 18 
ATOM   2659 C  CA  . LYS A 1 341 ? -22.208 13.836  -36.923 1.000 23.734 ? 341 LYS A CA  1 ? 18 
ATOM   2660 C  C   . LYS A 1 341 ? -21.205 12.974  -37.726 1.000 23.343 ? 341 LYS A C   1 ? 18 
ATOM   2661 O  O   . LYS A 1 341 ? -21.451 11.746  -37.848 1.000 23.130 ? 341 LYS A O   1 ? 18 
ATOM   2662 C  CB  . LYS A 1 341 ? -23.502 14.007  -37.700 1.000 26.624 ? 341 LYS A CB  1 ? 18 
ATOM   2663 C  CG  . LYS A 1 341 ? -24.681 14.439  -36.836 1.000 31.154 ? 341 LYS A CG  1 ? 18 
ATOM   2664 C  CD  . LYS A 1 341 ? -25.909 14.789  -37.630 1.000 36.022 ? 341 LYS A CD  1 ? 18 
ATOM   2665 C  CE  . LYS A 1 341 ? -27.251 14.556  -36.957 1.000 44.225 ? 341 LYS A CE  1 ? 18 
ATOM   2666 N  NZ  . LYS A 1 341 ? -27.189 14.584  -35.493 1.000 48.189 ? 341 LYS A NZ  1 ? 18 
ATOM   2667 N  N   . MET A 1 342 ? -20.116 13.546  -38.174 1.000 21.609 ? 342 MET A N   1 ? 18 
ATOM   2668 C  CA  . MET A 1 342 ? -19.121 12.866  -39.046 1.000 21.143 ? 342 MET A CA  1 ? 18 
ATOM   2669 C  C   . MET A 1 342 ? -17.790 12.764  -38.291 1.000 20.630 ? 342 MET A C   1 ? 18 
ATOM   2670 O  O   . MET A 1 342 ? -17.715 11.891  -37.381 1.000 21.689 ? 342 MET A O   1 ? 18 
ATOM   2671 C  CB  . MET A 1 342 ? -19.067 13.535  -40.427 1.000 21.179 ? 342 MET A CB  1 ? 18 
ATOM   2672 C  CG  . MET A 1 342 ? -20.420 13.450  -41.164 1.000 21.593 ? 342 MET A CG  1 ? 18 
ATOM   2673 S  SD  . MET A 1 342 ? -20.572 14.385  -42.691 1.000 21.719 ? 342 MET A SD  1 ? 18 
ATOM   2674 C  CE  . MET A 1 342 ? -19.308 13.605  -43.705 1.000 22.554 ? 342 MET A CE  1 ? 18 
ATOM   2675 N  N   . THR A 1 343 ? -16.781 13.567  -38.611 1.000 20.437 ? 343 THR A N   1 ? 18 
ATOM   2676 C  CA  . THR A 1 343 ? -15.417 13.332  -38.087 1.000 20.689 ? 343 THR A CA  1 ? 18 
ATOM   2677 C  C   . THR A 1 343 ? -15.372 13.435  -36.563 1.000 20.784 ? 343 THR A C   1 ? 18 
ATOM   2678 O  O   . THR A 1 343 ? -14.400 12.910  -35.986 1.000 22.481 ? 343 THR A O   1 ? 18 
ATOM   2679 C  CB  . THR A 1 343 ? -14.435 14.382  -38.657 1.000 21.303 ? 343 THR A CB  1 ? 18 
ATOM   2680 O  OG1 . THR A 1 343 ? -14.929 15.700  -38.454 1.000 21.222 ? 343 THR A OG1 1 ? 18 
ATOM   2681 C  CG2 . THR A 1 343 ? -14.201 14.083  -40.121 1.000 22.922 ? 343 THR A CG2 1 ? 18 
ATOM   2682 N  N   . HIS A 1 344 ? -16.290 14.183  -35.969 1.000 20.226 ? 344 HIS A N   1 ? 18 
ATOM   2683 C  CA  . HIS A 1 344 ? -16.221 14.462  -34.518 1.000 20.123 ? 344 HIS A CA  1 ? 18 
ATOM   2684 C  C   . HIS A 1 344 ? -17.426 13.897  -33.784 1.000 20.581 ? 344 HIS A C   1 ? 18 
ATOM   2685 O  O   . HIS A 1 344 ? -17.699 14.247  -32.612 1.000 21.598 ? 344 HIS A O   1 ? 18 
ATOM   2686 C  CB  . HIS A 1 344 ? -16.026 15.946  -34.252 1.000 20.375 ? 344 HIS A CB  1 ? 18 
ATOM   2687 C  CG  . HIS A 1 344 ? -14.699 16.485  -34.662 1.000 20.208 ? 344 HIS A CG  1 ? 18 
ATOM   2688 N  ND1 . HIS A 1 344 ? -14.351 16.602  -36.012 1.000 20.311 ? 344 HIS A ND1 1 ? 18 
ATOM   2689 C  CD2 . HIS A 1 344 ? -13.631 16.934  -33.926 1.000 21.332 ? 344 HIS A CD2 1 ? 18 
ATOM   2690 C  CE1 . HIS A 1 344 ? -13.102 17.071  -36.068 1.000 20.768 ? 344 HIS A CE1 1 ? 18 
ATOM   2691 N  NE2 . HIS A 1 344 ? -12.661 17.353  -34.768 1.000 19.814 ? 344 HIS A NE2 1 ? 18 
ATOM   2692 N  N   . ALA A 1 345 ? -18.133 12.950  -34.362 1.000 21.435 ? 345 ALA A N   1 ? 18 
ATOM   2693 C  CA  . ALA A 1 345 ? -19.119 12.172  -33.600 1.000 22.230 ? 345 ALA A CA  1 ? 18 
ATOM   2694 C  C   . ALA A 1 345 ? -18.427 11.541  -32.361 1.000 22.301 ? 345 ALA A C   1 ? 18 
ATOM   2695 O  O   . ALA A 1 345 ? -19.072 11.436  -31.310 1.000 23.601 ? 345 ALA A O   1 ? 18 
ATOM   2696 C  CB  . ALA A 1 345 ? -19.708 11.082  -34.488 1.000 23.309 ? 345 ALA A CB  1 ? 18 
ATOM   2697 N  N   . SER A 1 346 ? -17.130 11.168  -32.496 1.000 21.976 ? 346 SER A N   1 ? 18 
ATOM   2698 C  CA  . SER A 1 346 ? -16.314 10.524  -31.435 1.000 22.632 ? 346 SER A CA  1 ? 18 
ATOM   2699 C  C   . SER A 1 346 ? -16.043 11.522  -30.290 1.000 22.309 ? 346 SER A C   1 ? 18 
ATOM   2700 O  O   . SER A 1 346 ? -15.564 11.065  -29.206 1.000 24.802 ? 346 SER A O   1 ? 18 
ATOM   2701 C  CB  . SER A 1 346 ? -14.988 10.061  -32.040 1.000 22.791 ? 346 SER A CB  1 ? 18 
ATOM   2702 O  OG  . SER A 1 346 ? -14.423 11.140  -32.788 1.000 24.896 ? 346 SER A OG  1 ? 18 
ATOM   2703 N  N   . THR A 1 347 ? -16.334 12.815  -30.447 1.000 21.101 ? 347 THR A N   1 ? 18 
ATOM   2704 C  CA  . THR A 1 347 ? -16.094 13.785  -29.337 1.000 21.220 ? 347 THR A CA  1 ? 18 
ATOM   2705 C  C   . THR A 1 347 ? -17.396 14.224  -28.656 1.000 21.862 ? 347 THR A C   1 ? 18 
ATOM   2706 O  O   . THR A 1 347 ? -17.311 15.027  -27.715 1.000 22.043 ? 347 THR A O   1 ? 18 
ATOM   2707 C  CB  . THR A 1 347 ? -15.253 15.014  -29.783 1.000 21.201 ? 347 THR A CB  1 ? 18 
ATOM   2708 O  OG1 . THR A 1 347 ? -16.040 15.869  -30.613 1.000 22.248 ? 347 THR A OG1 1 ? 18 
ATOM   2709 C  CG2 . THR A 1 347 ? -13.954 14.568  -30.428 1.000 21.712 ? 347 THR A CG2 1 ? 18 
ATOM   2710 N  N   . ALA A 1 348 ? -18.556 13.768  -29.135 1.000 23.508 ? 348 ALA A N   1 ? 18 
ATOM   2711 C  CA  . ALA A 1 348 ? -19.832 14.093  -28.518 1.000 24.341 ? 348 ALA A CA  1 ? 18 
ATOM   2712 C  C   . ALA A 1 348 ? -19.754 13.777  -27.019 1.000 24.830 ? 348 ALA A C   1 ? 18 
ATOM   2713 O  O   . ALA A 1 348 ? -19.265 12.717  -26.629 1.000 23.868 ? 348 ALA A O   1 ? 18 
ATOM   2714 C  CB  . ALA A 1 348 ? -20.919 13.349  -29.234 1.000 24.745 ? 348 ALA A CB  1 ? 18 
ATOM   2715 N  N   . GLY A 1 349 ? -20.242 14.668  -26.170 1.000 23.240 ? 349 GLY A N   1 ? 18 
ATOM   2716 C  CA  . GLY A 1 349 ? -20.258 14.443  -24.727 1.000 24.438 ? 349 GLY A CA  1 ? 18 
ATOM   2717 C  C   . GLY A 1 349 ? -18.951 14.725  -24.008 1.000 25.432 ? 349 GLY A C   1 ? 18 
ATOM   2718 O  O   . GLY A 1 349 ? -18.852 14.510  -22.772 1.000 29.837 ? 349 GLY A O   1 ? 18 
ATOM   2719 N  N   . SER A 1 350 ? -17.935 15.159  -24.720 1.000 22.504 ? 350 SER A N   1 ? 18 
ATOM   2720 C  CA  . SER A 1 350 ? -16.593 15.439  -24.131 1.000 23.009 ? 350 SER A CA  1 ? 18 
ATOM   2721 C  C   . SER A 1 350 ? -16.335 16.951  -24.163 1.000 23.509 ? 350 SER A C   1 ? 18 
ATOM   2722 O  O   . SER A 1 350 ? -17.084 17.711  -24.834 1.000 24.295 ? 350 SER A O   1 ? 18 
ATOM   2723 C  CB  . SER A 1 350 ? -15.510 14.697  -24.914 1.000 23.534 ? 350 SER A CB  1 ? 18 
ATOM   2724 O  OG  . SER A 1 350 ? -15.180 15.400  -26.119 1.000 22.900 ? 350 SER A OG  1 ? 18 
ATOM   2725 N  N   . LEU A 1 351 ? -15.201 17.371  -23.615 1.000 25.308 ? 351 LEU A N   1 ? 18 
ATOM   2726 C  CA  . LEU A 1 351 ? -14.751 18.762  -23.733 1.000 27.031 ? 351 LEU A CA  1 ? 18 
ATOM   2727 C  C   . LEU A 1 351 ? -14.467 19.157  -25.173 1.000 25.949 ? 351 LEU A C   1 ? 18 
ATOM   2728 O  O   . LEU A 1 351 ? -14.382 20.367  -25.462 1.000 27.489 ? 351 LEU A O   1 ? 18 
ATOM   2729 C  CB  . LEU A 1 351 ? -13.477 18.865  -22.897 1.000 28.925 ? 351 LEU A CB  1 ? 18 
ATOM   2730 C  CG  . LEU A 1 351 ? -13.694 18.794  -21.399 1.000 33.204 ? 351 LEU A CG  1 ? 18 
ATOM   2731 C  CD1 . LEU A 1 351 ? -12.361 18.515  -20.658 1.000 35.472 ? 351 LEU A CD1 1 ? 18 
ATOM   2732 C  CD2 . LEU A 1 351 ? -14.362 20.084  -20.899 1.000 35.785 ? 351 LEU A CD2 1 ? 18 
ATOM   2733 N  N   . LEU A 1 352 ? -14.302 18.167  -26.082 1.000 23.097 ? 352 LEU A N   1 ? 18 
ATOM   2734 C  CA  . LEU A 1 352 ? -13.999 18.446  -27.508 1.000 22.616 ? 352 LEU A CA  1 ? 18 
ATOM   2735 C  C   . LEU A 1 352 ? -15.244 18.401  -28.396 1.000 22.964 ? 352 LEU A C   1 ? 18 
ATOM   2736 O  O   . LEU A 1 352 ? -15.055 18.423  -29.616 1.000 23.031 ? 352 LEU A O   1 ? 18 
ATOM   2737 C  CB  . LEU A 1 352 ? -12.948 17.436  -28.019 1.000 21.950 ? 352 LEU A CB  1 ? 18 
ATOM   2738 C  CG  . LEU A 1 352 ? -11.497 17.724  -27.617 1.000 23.173 ? 352 LEU A CG  1 ? 18 
ATOM   2739 C  CD1 . LEU A 1 352 ? -11.303 17.604  -26.128 1.000 24.306 ? 352 LEU A CD1 1 ? 18 
ATOM   2740 C  CD2 . LEU A 1 352 ? -10.547 16.801  -28.371 1.000 23.308 ? 352 LEU A CD2 1 ? 18 
ATOM   2741 N  N   . GLU A 1 353 ? -16.470 18.331  -27.822 1.000 21.920 ? 353 GLU A N   1 ? 18 
ATOM   2742 C  CA  . GLU A 1 353 ? -17.705 18.347  -28.604 1.000 22.511 ? 353 GLU A CA  1 ? 18 
ATOM   2743 C  C   . GLU A 1 353 ? -17.711 19.595  -29.485 1.000 23.145 ? 353 GLU A C   1 ? 18 
ATOM   2744 O  O   . GLU A 1 353 ? -17.426 20.718  -28.981 1.000 24.150 ? 353 GLU A O   1 ? 18 
ATOM   2745 C  CB  . GLU A 1 353 ? -18.910 18.292  -27.694 1.000 24.868 ? 353 GLU A CB  1 ? 18 
ATOM   2746 C  CG  . GLU A 1 353 ? -20.209 18.225  -28.452 1.000 26.408 ? 353 GLU A CG  1 ? 18 
ATOM   2747 C  CD  . GLU A 1 353 ? -21.434 17.951  -27.598 1.000 30.158 ? 353 GLU A CD  1 ? 18 
ATOM   2748 O  OE1 . GLU A 1 353 ? -21.370 17.083  -26.711 1.000 29.909 ? 353 GLU A OE1 1 ? 18 
ATOM   2749 O  OE2 . GLU A 1 353 ? -22.449 18.702  -27.736 1.000 37.346 ? 353 GLU A OE2 1 ? 18 
ATOM   2750 N  N   A VAL A 1 354 ? -18.097 19.434  -30.731 0.500 24.300 ? 354 VAL A N   1 ? 19 
ATOM   2751 N  N   B VAL A 1 354 ? -18.079 19.435  -30.751 0.500 24.682 ? 354 VAL A N   1 ? 19 
ATOM   2752 C  CA  A VAL A 1 354 ? -18.130 20.562  -31.693 0.500 24.429 ? 354 VAL A CA  1 ? 19 
ATOM   2753 C  CA  B VAL A 1 354 ? -18.117 20.543  -31.754 0.500 25.063 ? 354 VAL A CA  1 ? 19 
ATOM   2754 C  C   A VAL A 1 354 ? -19.554 21.091  -31.723 0.500 26.349 ? 354 VAL A C   1 ? 19 
ATOM   2755 C  C   B VAL A 1 354 ? -19.543 21.063  -31.817 0.500 26.662 ? 354 VAL A C   1 ? 19 
ATOM   2756 O  O   A VAL A 1 354 ? -20.501 20.390  -31.387 0.500 28.413 ? 354 VAL A O   1 ? 19 
ATOM   2757 O  O   B VAL A 1 354 ? -20.483 20.285  -31.727 0.500 28.421 ? 354 VAL A O   1 ? 19 
ATOM   2758 C  CB  A VAL A 1 354 ? -17.652 20.089  -33.066 0.500 22.978 ? 354 VAL A CB  1 ? 19 
ATOM   2759 C  CB  B VAL A 1 354 ? -17.678 20.045  -33.140 0.500 24.176 ? 354 VAL A CB  1 ? 19 
ATOM   2760 C  CG1 A VAL A 1 354 ? -16.241 19.496  -32.938 0.500 23.275 ? 354 VAL A CG1 1 ? 19 
ATOM   2761 C  CG1 B VAL A 1 354 ? -17.795 21.117  -34.224 0.500 24.184 ? 354 VAL A CG1 1 ? 19 
ATOM   2762 C  CG2 A VAL A 1 354 ? -18.610 19.075  -33.675 0.500 22.652 ? 354 VAL A CG2 1 ? 19 
ATOM   2763 C  CG2 B VAL A 1 354 ? -16.263 19.458  -33.084 0.500 24.573 ? 354 VAL A CG2 1 ? 19 
ATOM   2764 N  N   . PRO A 1 355 ? -19.752 22.370  -32.049 1.000 27.112 ? 355 PRO A N   1 ? 19 
ATOM   2765 C  CA  . PRO A 1 355 ? -21.125 22.897  -32.189 1.000 27.411 ? 355 PRO A CA  1 ? 19 
ATOM   2766 C  C   . PRO A 1 355 ? -21.911 22.210  -33.327 1.000 26.465 ? 355 PRO A C   1 ? 19 
ATOM   2767 O  O   . PRO A 1 355 ? -21.371 21.920  -34.388 1.000 26.232 ? 355 PRO A O   1 ? 19 
ATOM   2768 C  CB  . PRO A 1 355 ? -20.876 24.370  -32.535 1.000 29.507 ? 355 PRO A CB  1 ? 19 
ATOM   2769 C  CG  . PRO A 1 355 ? -19.436 24.630  -32.138 1.000 30.529 ? 355 PRO A CG  1 ? 19 
ATOM   2770 C  CD  . PRO A 1 355 ? -18.696 23.331  -32.352 1.000 29.155 ? 355 PRO A CD  1 ? 19 
ATOM   2771 N  N   . SER A 1 356 ? -23.179 21.939  -33.074 1.000 26.891 ? 356 SER A N   1 ? 19 
ATOM   2772 C  CA  . SER A 1 356 ? -24.023 21.180  -34.016 1.000 27.177 ? 356 SER A CA  1 ? 19 
ATOM   2773 C  C   . SER A 1 356 ? -24.392 22.069  -35.196 1.000 27.549 ? 356 SER A C   1 ? 19 
ATOM   2774 O  O   . SER A 1 356 ? -24.894 21.532  -36.191 1.000 26.794 ? 356 SER A O   1 ? 19 
ATOM   2775 C  CB  . SER A 1 356 ? -25.239 20.668  -33.334 1.000 30.023 ? 356 SER A CB  1 ? 19 
ATOM   2776 O  OG  . SER A 1 356 ? -26.029 21.787  -32.874 1.000 32.788 ? 356 SER A OG  1 ? 19 
ATOM   2777 N  N   . ASP A 1 357 ? -24.161 23.381  -35.103 1.000 26.849 ? 357 ASP A N   1 ? 19 
ATOM   2778 C  CA  . ASP A 1 357 ? -24.498 24.286  -36.237 1.000 26.090 ? 357 ASP A CA  1 ? 19 
ATOM   2779 C  C   . ASP A 1 357 ? -23.289 24.540  -37.132 1.000 24.657 ? 357 ASP A C   1 ? 19 
ATOM   2780 O  O   . ASP A 1 357 ? -23.388 25.408  -38.024 1.000 24.522 ? 357 ASP A O   1 ? 19 
ATOM   2781 C  CB  . ASP A 1 357 ? -25.041 25.621  -35.766 1.000 27.321 ? 357 ASP A CB  1 ? 19 
ATOM   2782 C  CG  . ASP A 1 357 ? -24.127 26.362  -34.781 1.000 30.982 ? 357 ASP A CG  1 ? 19 
ATOM   2783 O  OD1 . ASP A 1 357 ? -23.055 25.879  -34.481 1.000 32.294 ? 357 ASP A OD1 1 ? 19 
ATOM   2784 O  OD2 . ASP A 1 357 ? -24.489 27.466  -34.369 1.000 32.285 ? 357 ASP A OD2 1 ? 19 
ATOM   2785 N  N   . LEU A 1 358 ? -22.211 23.782  -36.958 1.000 22.873 ? 358 LEU A N   1 ? 19 
ATOM   2786 C  CA  . LEU A 1 358 ? -20.960 24.052  -37.680 1.000 22.832 ? 358 LEU A CA  1 ? 19 
ATOM   2787 C  C   . LEU A 1 358 ? -20.840 23.192  -38.925 1.000 22.470 ? 358 LEU A C   1 ? 19 
ATOM   2788 O  O   . LEU A 1 358 ? -21.093 21.944  -38.863 1.000 22.508 ? 358 LEU A O   1 ? 19 
ATOM   2789 C  CB  . LEU A 1 358 ? -19.808 23.874  -36.711 1.000 25.757 ? 358 LEU A CB  1 ? 19 
ATOM   2790 C  CG  . LEU A 1 358 ? -18.482 24.301  -37.316 1.000 27.754 ? 358 LEU A CG  1 ? 19 
ATOM   2791 C  CD1 . LEU A 1 358 ? -17.819 25.384  -36.548 1.000 32.237 ? 358 LEU A CD1 1 ? 19 
ATOM   2792 C  CD2 . LEU A 1 358 ? -17.588 23.129  -37.492 1.000 35.139 ? 358 LEU A CD2 1 ? 19 
ATOM   2793 N  N   . VAL A 1 359 ? -20.362 23.818  -39.993 1.000 21.072 ? 359 VAL A N   1 ? 19 
ATOM   2794 C  CA  . VAL A 1 359 ? -19.982 23.153  -41.250 1.000 20.337 ? 359 VAL A CA  1 ? 19 
ATOM   2795 C  C   . VAL A 1 359 ? -18.468 23.354  -41.450 1.000 20.314 ? 359 VAL A C   1 ? 19 
ATOM   2796 O  O   . VAL A 1 359 ? -17.989 24.487  -41.207 1.000 20.246 ? 359 VAL A O   1 ? 19 
ATOM   2797 C  CB  . VAL A 1 359 ? -20.739 23.779  -42.409 1.000 21.468 ? 359 VAL A CB  1 ? 19 
ATOM   2798 C  CG1 . VAL A 1 359 ? -20.281 23.175  -43.765 1.000 21.021 ? 359 VAL A CG1 1 ? 19 
ATOM   2799 C  CG2 . VAL A 1 359 ? -22.231 23.612  -42.231 1.000 23.011 ? 359 VAL A CG2 1 ? 19 
ATOM   2800 N  N   . ARG A 1 360 ? -17.767 22.322  -41.857 1.000 19.272 ? 360 ARG A N   1 ? 19 
ATOM   2801 C  CA  . ARG A 1 360 ? -16.326 22.416  -42.149 1.000 18.456 ? 360 ARG A CA  1 ? 19 
ATOM   2802 C  C   . ARG A 1 360 ? -16.153 22.283  -43.672 1.000 19.472 ? 360 ARG A C   1 ? 19 
ATOM   2803 O  O   . ARG A 1 360 ? -16.682 21.278  -44.244 1.000 19.381 ? 360 ARG A O   1 ? 19 
ATOM   2804 C  CB  . ARG A 1 360 ? -15.503 21.349  -41.433 1.000 19.163 ? 360 ARG A CB  1 ? 19 
ATOM   2805 C  CG  . ARG A 1 360 ? -14.040 21.561  -41.551 1.000 19.077 ? 360 ARG A CG  1 ? 19 
ATOM   2806 C  CD  . ARG A 1 360 ? -13.260 20.400  -40.962 1.000 19.299 ? 360 ARG A CD  1 ? 19 
ATOM   2807 N  NE  . ARG A 1 360 ? -13.307 19.274  -41.910 1.000 19.291 ? 360 ARG A NE  1 ? 19 
ATOM   2808 C  CZ  . ARG A 1 360 ? -12.812 18.059  -41.628 1.000 19.808 ? 360 ARG A CZ  1 ? 19 
ATOM   2809 N  NH1 . ARG A 1 360 ? -12.178 17.801  -40.479 1.000 19.471 ? 360 ARG A NH1 1 ? 19 
ATOM   2810 N  NH2 . ARG A 1 360 ? -12.839 17.100  -42.558 1.000 20.223 ? 360 ARG A NH2 1 ? 19 
ATOM   2811 N  N   . LEU A 1 361 ? -15.394 23.181  -44.259 1.000 19.029 ? 361 LEU A N   1 ? 19 
ATOM   2812 C  CA  . LEU A 1 361 ? -14.965 23.114  -45.668 1.000 19.444 ? 361 LEU A CA  1 ? 19 
ATOM   2813 C  C   . LEU A 1 361 ? -13.486 22.823  -45.788 1.000 19.034 ? 361 LEU A C   1 ? 19 
ATOM   2814 O  O   . LEU A 1 361 ? -12.690 23.481  -45.128 1.000 18.704 ? 361 LEU A O   1 ? 19 
ATOM   2815 C  CB  . LEU A 1 361 ? -15.210 24.422  -46.414 1.000 19.372 ? 361 LEU A CB  1 ? 19 
ATOM   2816 C  CG  . LEU A 1 361 ? -16.624 24.990  -46.353 1.000 21.111 ? 361 LEU A CG  1 ? 19 
ATOM   2817 C  CD1 . LEU A 1 361 ? -16.671 26.337  -47.109 1.000 23.661 ? 361 LEU A CD1 1 ? 19 
ATOM   2818 C  CD2 . LEU A 1 361 ? -17.653 24.013  -46.899 1.000 21.590 ? 361 LEU A CD2 1 ? 19 
ATOM   2819 N  N   . SER A 1 362 ? -13.164 21.893  -46.696 1.000 18.256 ? 362 SER A N   1 ? 19 
ATOM   2820 C  CA  . SER A 1 362 ? -11.820 21.800  -47.298 1.000 17.838 ? 362 SER A CA  1 ? 19 
ATOM   2821 C  C   . SER A 1 362 ? -11.954 22.394  -48.693 1.000 17.062 ? 362 SER A C   1 ? 19 
ATOM   2822 O  O   . SER A 1 362 ? -12.474 21.733  -49.582 1.000 18.569 ? 362 SER A O   1 ? 19 
ATOM   2823 C  CB  . SER A 1 362 ? -11.346 20.367  -47.315 1.000 18.387 ? 362 SER A CB  1 ? 19 
ATOM   2824 O  OG  . SER A 1 362 ? -10.029 20.295  -47.904 1.000 18.190 ? 362 SER A OG  1 ? 19 
ATOM   2825 N  N   . VAL A 1 363 ? -11.505 23.621  -48.832 1.000 18.596 ? 363 VAL A N   1 ? 19 
ATOM   2826 C  CA  . VAL A 1 363 ? -11.611 24.331  -50.122 1.000 17.709 ? 363 VAL A CA  1 ? 19 
ATOM   2827 C  C   . VAL A 1 363 ? -10.540 23.768  -51.041 1.000 18.820 ? 363 VAL A C   1 ? 19 
ATOM   2828 O  O   . VAL A 1 363 ? -9.395  23.838  -50.654 1.000 19.571 ? 363 VAL A O   1 ? 19 
ATOM   2829 C  CB  . VAL A 1 363 ? -11.499 25.835  -49.949 1.000 18.860 ? 363 VAL A CB  1 ? 19 
ATOM   2830 C  CG1 . VAL A 1 363 ? -11.622 26.524  -51.287 1.000 19.443 ? 363 VAL A CG1 1 ? 19 
ATOM   2831 C  CG2 . VAL A 1 363 ? -12.543 26.373  -48.953 1.000 20.376 ? 363 VAL A CG2 1 ? 19 
ATOM   2832 N  N   . GLY A 1 364 ? -10.956 23.240  -52.173 1.000 19.037 ? 364 GLY A N   1 ? 19 
ATOM   2833 C  CA  . GLY A 1 364 ? -10.067 22.578  -53.134 1.000 18.369 ? 364 GLY A CA  1 ? 19 
ATOM   2834 C  C   . GLY A 1 364 ? -9.487  23.593  -54.102 1.000 19.210 ? 364 GLY A C   1 ? 19 
ATOM   2835 O  O   . GLY A 1 364 ? -9.513  24.822  -53.861 1.000 19.694 ? 364 GLY A O   1 ? 19 
ATOM   2836 N  N   . ILE A 1 365 ? -8.929  23.085  -55.199 1.000 18.191 ? 365 ILE A N   1 ? 19 
ATOM   2837 C  CA  . ILE A 1 365 ? -8.245  23.917  -56.211 1.000 18.743 ? 365 ILE A CA  1 ? 19 
ATOM   2838 C  C   . ILE A 1 365 ? -9.066  24.036  -57.492 1.000 18.999 ? 365 ILE A C   1 ? 19 
ATOM   2839 O  O   . ILE A 1 365 ? -8.522  24.520  -58.525 1.000 20.070 ? 365 ILE A O   1 ? 19 
ATOM   2840 C  CB  . ILE A 1 365 ? -6.804  23.439  -56.444 1.000 17.825 ? 365 ILE A CB  1 ? 19 
ATOM   2841 C  CG1 . ILE A 1 365 ? -6.736  22.094  -57.148 1.000 17.454 ? 365 ILE A CG1 1 ? 19 
ATOM   2842 C  CG2 . ILE A 1 365 ? -6.025  23.445  -55.146 1.000 18.732 ? 365 ILE A CG2 1 ? 19 
ATOM   2843 C  CD1 . ILE A 1 365 ? -5.369  21.737  -57.648 1.000 18.754 ? 365 ILE A CD1 1 ? 19 
ATOM   2844 N  N   . GLU A 1 366 ? -10.348 23.727  -57.425 1.000 18.901 ? 366 GLU A N   1 ? 19 
ATOM   2845 C  CA  . GLU A 1 366 ? -11.273 24.002  -58.536 1.000 19.123 ? 366 GLU A CA  1 ? 19 
ATOM   2846 C  C   . GLU A 1 366 ? -11.322 25.515  -58.812 1.000 20.048 ? 366 GLU A C   1 ? 19 
ATOM   2847 O  O   . GLU A 1 366 ? -10.813 26.325  -58.067 1.000 19.896 ? 366 GLU A O   1 ? 19 
ATOM   2848 C  CB  . GLU A 1 366 ? -12.696 23.474  -58.279 1.000 20.565 ? 366 GLU A CB  1 ? 19 
ATOM   2849 C  CG  . GLU A 1 366 ? -12.837 21.949  -58.053 1.000 19.425 ? 366 GLU A CG  1 ? 19 
ATOM   2850 C  CD  . GLU A 1 366 ? -12.836 21.543  -56.570 1.000 19.034 ? 366 GLU A CD  1 ? 19 
ATOM   2851 O  OE1 . GLU A 1 366 ? -12.265 22.306  -55.757 1.000 18.702 ? 366 GLU A OE1 1 ? 19 
ATOM   2852 O  OE2 . GLU A 1 366 ? -13.407 20.447  -56.267 1.000 19.386 ? 366 GLU A OE2 1 ? 19 
ATOM   2853 N  N   . THR A 1 367 ? -11.840 25.846  -59.987 1.000 20.076 ? 367 THR A N   1 ? 19 
ATOM   2854 C  CA  . THR A 1 367 ? -12.022 27.273  -60.392 1.000 21.102 ? 367 THR A CA  1 ? 19 
ATOM   2855 C  C   . THR A 1 367 ? -12.873 27.973  -59.330 1.000 21.418 ? 367 THR A C   1 ? 19 
ATOM   2856 O  O   . THR A 1 367 ? -14.020 27.537  -59.054 1.000 21.639 ? 367 THR A O   1 ? 19 
ATOM   2857 C  CB  . THR A 1 367 ? -12.670 27.342  -61.773 1.000 22.959 ? 367 THR A CB  1 ? 19 
ATOM   2858 O  OG1 . THR A 1 367 ? -12.014 26.417  -62.673 1.000 21.937 ? 367 THR A OG1 1 ? 19 
ATOM   2859 C  CG2 . THR A 1 367 ? -12.608 28.750  -62.365 1.000 24.735 ? 367 THR A CG2 1 ? 19 
ATOM   2860 N  N   . VAL A 1 368 ? -12.387 29.056  -58.779 1.000 21.265 ? 368 VAL A N   1 ? 19 
ATOM   2861 C  CA  . VAL A 1 368 ? -12.958 29.625  -57.547 1.000 23.637 ? 368 VAL A CA  1 ? 19 
ATOM   2862 C  C   . VAL A 1 368 ? -14.427 30.046  -57.762 1.000 23.730 ? 368 VAL A C   1 ? 19 
ATOM   2863 O  O   . VAL A 1 368 ? -15.233 29.819  -56.849 1.000 23.325 ? 368 VAL A O   1 ? 19 
ATOM   2864 C  CB  . VAL A 1 368 ? -12.073 30.783  -57.038 1.000 27.385 ? 368 VAL A CB  1 ? 19 
ATOM   2865 C  CG1 . VAL A 1 368 ? -12.018 31.961  -57.971 1.000 31.104 ? 368 VAL A CG1 1 ? 19 
ATOM   2866 C  CG2 . VAL A 1 368 ? -12.482 31.136  -55.628 1.000 32.600 ? 368 VAL A CG2 1 ? 19 
ATOM   2867 N  N   . ASP A 1 369 ? -14.777 30.586  -58.918 1.000 25.084 ? 369 ASP A N   1 ? 19 
ATOM   2868 C  CA  . ASP A 1 369 ? -16.156 31.061  -59.090 1.000 26.854 ? 369 ASP A CA  1 ? 19 
ATOM   2869 C  C   . ASP A 1 369 ? -17.074 29.857  -58.962 1.000 24.072 ? 369 ASP A C   1 ? 19 
ATOM   2870 O  O   . ASP A 1 369 ? -18.207 30.018  -58.511 1.000 25.482 ? 369 ASP A O   1 ? 19 
ATOM   2871 C  CB  . ASP A 1 369 ? -16.355 31.752  -60.433 1.000 28.941 ? 369 ASP A CB  1 ? 19 
ATOM   2872 C  CG  . ASP A 1 369 ? -15.794 33.146  -60.527 1.000 34.243 ? 369 ASP A CG  1 ? 19 
ATOM   2873 O  OD1 . ASP A 1 369 ? -15.475 33.740  -59.498 1.000 36.574 ? 369 ASP A OD1 1 ? 19 
ATOM   2874 O  OD2 . ASP A 1 369 ? -15.837 33.683  -61.619 1.000 40.856 ? 369 ASP A OD2 1 ? 19 
ATOM   2875 N  N   . ASP A 1 370 ? -16.667 28.683  -59.416 1.000 23.924 ? 370 ASP A N   1 ? 19 
ATOM   2876 C  CA  . ASP A 1 370 ? -17.551 27.502  -59.327 1.000 22.815 ? 370 ASP A CA  1 ? 19 
ATOM   2877 C  C   . ASP A 1 370 ? -17.777 27.138  -57.862 1.000 22.471 ? 370 ASP A C   1 ? 19 
ATOM   2878 O  O   . ASP A 1 370 ? -18.902 26.691  -57.524 1.000 24.007 ? 370 ASP A O   1 ? 19 
ATOM   2879 C  CB  . ASP A 1 370 ? -16.976 26.304  -60.082 1.000 22.314 ? 370 ASP A CB  1 ? 19 
ATOM   2880 C  CG  . ASP A 1 370 ? -16.851 26.525  -61.590 1.000 24.034 ? 370 ASP A CG  1 ? 19 
ATOM   2881 O  OD1 . ASP A 1 370 ? -17.646 27.356  -62.141 1.000 26.783 ? 370 ASP A OD1 1 ? 19 
ATOM   2882 O  OD2 . ASP A 1 370 ? -15.978 25.869  -62.214 1.000 23.625 ? 370 ASP A OD2 1 ? 19 
ATOM   2883 N  N   . LEU A 1 371 ? -16.761 27.269  -57.024 1.000 22.237 ? 371 LEU A N   1 ? 19 
ATOM   2884 C  CA  . LEU A 1 371 ? -16.857 26.952  -55.582 1.000 21.846 ? 371 LEU A CA  1 ? 19 
ATOM   2885 C  C   . LEU A 1 371 ? -17.737 27.977  -54.883 1.000 23.023 ? 371 LEU A C   1 ? 19 
ATOM   2886 O  O   . LEU A 1 371 ? -18.603 27.572  -54.093 1.000 22.681 ? 371 LEU A O   1 ? 19 
ATOM   2887 C  CB  . LEU A 1 371 ? -15.472 26.910  -54.956 1.000 20.846 ? 371 LEU A CB  1 ? 19 
ATOM   2888 C  CG  . LEU A 1 371 ? -14.595 25.797  -55.526 1.000 20.454 ? 371 LEU A CG  1 ? 19 
ATOM   2889 C  CD1 . LEU A 1 371 ? -13.225 25.868  -54.836 1.000 20.234 ? 371 LEU A CD1 1 ? 19 
ATOM   2890 C  CD2 . LEU A 1 371 ? -15.257 24.420  -55.383 1.000 20.139 ? 371 LEU A CD2 1 ? 19 
ATOM   2891 N  N   . VAL A 1 372 ? -17.526 29.264  -55.154 1.000 22.146 ? 372 VAL A N   1 ? 20 
ATOM   2892 C  CA  . VAL A 1 372 ? -18.343 30.322  -54.525 1.000 23.392 ? 372 VAL A CA  1 ? 20 
ATOM   2893 C  C   . VAL A 1 372 ? -19.802 30.144  -54.951 1.000 24.082 ? 372 VAL A C   1 ? 20 
ATOM   2894 O  O   . VAL A 1 372 ? -20.705 30.171  -54.082 1.000 24.644 ? 372 VAL A O   1 ? 20 
ATOM   2895 C  CB  . VAL A 1 372 ? -17.801 31.694  -54.893 1.000 25.377 ? 372 VAL A CB  1 ? 20 
ATOM   2896 C  CG1 . VAL A 1 372 ? -18.748 32.822  -54.521 1.000 27.779 ? 372 VAL A CG1 1 ? 20 
ATOM   2897 C  CG2 . VAL A 1 372 ? -16.457 31.951  -54.248 1.000 25.925 ? 372 VAL A CG2 1 ? 20 
ATOM   2898 N  N   . ASN A 1 373 ? -20.039 29.950  -56.237 1.000 23.847 ? 373 ASN A N   1 ? 20 
ATOM   2899 C  CA  . ASN A 1 373 ? -21.418 29.810  -56.722 1.000 25.832 ? 373 ASN A CA  1 ? 20 
ATOM   2900 C  C   . ASN A 1 373 ? -22.069 28.571  -56.090 1.000 24.565 ? 373 ASN A C   1 ? 20 
ATOM   2901 O  O   . ASN A 1 373 ? -23.303 28.631  -55.817 1.000 25.405 ? 373 ASN A O   1 ? 20 
ATOM   2902 C  CB  . ASN A 1 373 ? -21.498 29.803  -58.238 1.000 27.667 ? 373 ASN A CB  1 ? 20 
ATOM   2903 C  CG  . ASN A 1 373 ? -21.212 31.152  -58.861 1.000 29.668 ? 373 ASN A CG  1 ? 20 
ATOM   2904 O  OD1 . ASN A 1 373 ? -21.396 32.178  -58.231 1.000 33.613 ? 373 ASN A OD1 1 ? 20 
ATOM   2905 N  ND2 . ASN A 1 373 ? -20.739 31.133  -60.083 1.000 31.328 ? 373 ASN A ND2 1 ? 20 
ATOM   2906 N  N   . ASP A 1 374 ? -21.339 27.469  -55.918 1.000 23.217 ? 374 ASP A N   1 ? 20 
ATOM   2907 C  CA  . ASP A 1 374 ? -21.877 26.251  -55.323 1.000 22.357 ? 374 ASP A CA  1 ? 20 
ATOM   2908 C  C   . ASP A 1 374 ? -22.270 26.543  -53.880 1.000 24.264 ? 374 ASP A C   1 ? 20 
ATOM   2909 O  O   . ASP A 1 374 ? -23.338 26.169  -53.483 1.000 23.857 ? 374 ASP A O   1 ? 20 
ATOM   2910 C  CB  . ASP A 1 374 ? -20.853 25.130  -55.420 1.000 22.331 ? 374 ASP A CB  1 ? 20 
ATOM   2911 C  CG  . ASP A 1 374 ? -21.445 23.813  -54.966 1.000 23.364 ? 374 ASP A CG  1 ? 20 
ATOM   2912 O  OD1 . ASP A 1 374 ? -22.654 23.487  -55.372 1.000 24.211 ? 374 ASP A OD1 1 ? 20 
ATOM   2913 O  OD2 . ASP A 1 374 ? -20.654 23.036  -54.307 1.000 23.050 ? 374 ASP A OD2 1 ? 20 
ATOM   2914 N  N   . LEU A 1 375 ? -21.421 27.199  -53.122 1.000 24.211 ? 375 LEU A N   1 ? 20 
ATOM   2915 C  CA  . LEU A 1 375 ? -21.781 27.496  -51.721 1.000 26.067 ? 375 LEU A CA  1 ? 20 
ATOM   2916 C  C   . LEU A 1 375 ? -22.999 28.417  -51.688 1.000 26.481 ? 375 LEU A C   1 ? 20 
ATOM   2917 O  O   . LEU A 1 375 ? -23.890 28.222  -50.833 1.000 27.044 ? 375 LEU A O   1 ? 20 
ATOM   2918 C  CB  . LEU A 1 375 ? -20.601 28.187  -51.056 1.000 28.067 ? 375 LEU A CB  1 ? 20 
ATOM   2919 C  CG  . LEU A 1 375 ? -19.509 27.247  -50.664 1.000 31.390 ? 375 LEU A CG  1 ? 20 
ATOM   2920 C  CD1 . LEU A 1 375 ? -18.296 28.021  -50.140 1.000 31.286 ? 375 LEU A CD1 1 ? 20 
ATOM   2921 C  CD2 . LEU A 1 375 ? -20.027 26.257  -49.608 1.000 33.365 ? 375 LEU A CD2 1 ? 20 
ATOM   2922 N  N   . LEU A 1 376 ? -22.993 29.433  -52.537 1.000 27.546 ? 376 LEU A N   1 ? 20 
ATOM   2923 C  CA  . LEU A 1 376 ? -24.115 30.410  -52.486 1.000 29.160 ? 376 LEU A CA  1 ? 20 
ATOM   2924 C  C   . LEU A 1 376 ? -25.443 29.711  -52.765 1.000 29.137 ? 376 LEU A C   1 ? 20 
ATOM   2925 O  O   . LEU A 1 376 ? -26.438 30.025  -52.068 1.000 29.640 ? 376 LEU A O   1 ? 20 
ATOM   2926 C  CB  . LEU A 1 376 ? -23.900 31.599  -53.425 1.000 31.648 ? 376 LEU A CB  1 ? 20 
ATOM   2927 C  CG  . LEU A 1 376 ? -22.763 32.544  -53.028 1.000 32.223 ? 376 LEU A CG  1 ? 20 
ATOM   2928 C  CD1 . LEU A 1 376 ? -22.523 33.575  -54.122 1.000 33.307 ? 376 LEU A CD1 1 ? 20 
ATOM   2929 C  CD2 . LEU A 1 376 ? -22.998 33.235  -51.697 1.000 33.839 ? 376 LEU A CD2 1 ? 20 
ATOM   2930 N  N   . GLN A 1 377 ? -25.526 28.788  -53.704 1.000 29.454 ? 377 GLN A N   1 ? 20 
ATOM   2931 C  CA  . GLN A 1 377 ? -26.805 28.069  -53.953 1.000 28.928 ? 377 GLN A CA  1 ? 20 
ATOM   2932 C  C   . GLN A 1 377 ? -27.121 27.125  -52.761 1.000 28.795 ? 377 GLN A C   1 ? 20 
ATOM   2933 O  O   . GLN A 1 377 ? -28.290 26.960  -52.380 1.000 29.422 ? 377 GLN A O   1 ? 20 
ATOM   2934 C  CB  . GLN A 1 377 ? -26.835 27.362  -55.311 1.000 30.641 ? 377 GLN A CB  1 ? 20 
ATOM   2935 C  CG  . GLN A 1 377 ? -25.894 26.194  -55.481 1.000 28.348 ? 377 GLN A CG  1 ? 20 
ATOM   2936 C  CD  . GLN A 1 377 ? -26.418 24.896  -54.913 1.000 29.407 ? 377 GLN A CD  1 ? 20 
ATOM   2937 O  OE1 . GLN A 1 377 ? -27.644 24.665  -54.770 1.000 30.410 ? 377 GLN A OE1 1 ? 20 
ATOM   2938 N  NE2 . GLN A 1 377 ? -25.457 24.049  -54.529 1.000 26.726 ? 377 GLN A NE2 1 ? 20 
ATOM   2939 N  N   . ALA A 1 378 ? -26.123 26.509  -52.161 1.000 26.957 ? 378 ALA A N   1 ? 20 
ATOM   2940 C  CA  . ALA A 1 378 ? -26.383 25.581  -51.052 1.000 27.074 ? 378 ALA A CA  1 ? 20 
ATOM   2941 C  C   . ALA A 1 378 ? -26.892 26.337  -49.816 1.000 27.968 ? 378 ALA A C   1 ? 20 
ATOM   2942 O  O   . ALA A 1 378 ? -27.565 25.701  -49.000 1.000 28.614 ? 378 ALA A O   1 ? 20 
ATOM   2943 C  CB  . ALA A 1 378 ? -25.138 24.749  -50.776 1.000 26.527 ? 378 ALA A CB  1 ? 20 
ATOM   2944 N  N   . LEU A 1 379 ? -26.471 27.592  -49.630 1.000 27.780 ? 379 LEU A N   1 ? 20 
ATOM   2945 C  CA  . LEU A 1 379 ? -26.776 28.402  -48.435 1.000 29.666 ? 379 LEU A CA  1 ? 20 
ATOM   2946 C  C   . LEU A 1 379 ? -28.183 28.977  -48.558 1.000 32.124 ? 379 LEU A C   1 ? 20 
ATOM   2947 O  O   . LEU A 1 379 ? -28.722 29.391  -47.527 1.000 34.734 ? 379 LEU A O   1 ? 20 
ATOM   2948 C  CB  . LEU A 1 379 ? -25.750 29.525  -48.295 1.000 30.052 ? 379 LEU A CB  1 ? 20 
ATOM   2949 C  CG  . LEU A 1 379 ? -24.350 29.118  -47.803 1.000 28.378 ? 379 LEU A CG  1 ? 20 
ATOM   2950 C  CD1 . LEU A 1 379 ? -23.395 30.276  -47.976 1.000 29.472 ? 379 LEU A CD1 1 ? 20 
ATOM   2951 C  CD2 . LEU A 1 379 ? -24.379 28.675  -46.337 1.000 30.878 ? 379 LEU A CD2 1 ? 20 
ATOM   2952 N  N   . GLU A 1 380 ? -28.690 29.082  -49.777 1.000 33.796 ? 380 GLU A N   1 ? 20 
ATOM   2953 C  CA  . GLU A 1 380 ? -30.004 29.771  -50.042 1.000 38.090 ? 380 GLU A CA  1 ? 20 
ATOM   2954 C  C   . GLU A 1 380 ? -31.095 28.922  -49.415 1.000 41.737 ? 380 GLU A C   1 ? 20 
ATOM   2955 O  O   . GLU A 1 380 ? -31.151 27.737  -49.698 1.000 44.022 ? 380 GLU A O   1 ? 20 
ATOM   2956 C  CB  . GLU A 1 380 ? -30.191 29.997  -51.550 1.000 39.924 ? 380 GLU A CB  1 ? 20 
ATOM   2957 C  CG  . GLU A 1 380 ? -31.260 31.045  -51.871 1.000 47.090 ? 380 GLU A CG  1 ? 20 
ATOM   2958 C  CD  . GLU A 1 380 ? -30.958 32.467  -51.393 1.000 50.992 ? 380 GLU A CD  1 ? 20 
ATOM   2959 O  OE1 . GLU A 1 380 ? -29.805 32.771  -50.876 1.000 48.014 ? 380 GLU A OE1 1 ? 20 
ATOM   2960 O  OE2 . GLU A 1 380 ? -31.864 33.300  -51.566 1.000 57.678 ? 380 GLU A OE2 1 ? 20 
ATOM   2961 N  N   . PRO A 1 381 ? -31.918 29.460  -48.468 1.000 45.504 ? 381 PRO A N   1 ? 20 
ATOM   2962 C  CA  . PRO A 1 381 ? -32.874 28.646  -47.695 1.000 49.275 ? 381 PRO A CA  1 ? 20 
ATOM   2963 C  C   . PRO A 1 381 ? -34.148 28.219  -48.466 1.000 50.259 ? 381 PRO A C   1 ? 20 
ATOM   2964 O  O   . PRO A 1 381 ? -34.203 28.764  -49.564 1.000 52.811 ? 381 PRO A O   1 ? 20 
ATOM   2965 C  CB  . PRO A 1 381 ? -33.258 29.566  -46.512 1.000 51.339 ? 381 PRO A CB  1 ? 20 
ATOM   2966 C  CG  . PRO A 1 381 ? -33.029 30.971  -47.037 1.000 51.855 ? 381 PRO A CG  1 ? 20 
ATOM   2967 C  CD  . PRO A 1 381 ? -31.879 30.858  -48.025 1.000 46.434 ? 381 PRO A CD  1 ? 20 
HETATM 2968 C  C   . 4LM B 2 .   ? -10.834 14.436  -41.042 1.000 20.051 ? 401 4LM A C   1 ? ?  
HETATM 2969 N  N   . 4LM B 2 .   ? -8.808  13.693  -40.098 1.000 20.073 ? 401 4LM A N   1 ? ?  
HETATM 2970 O  O1  . 4LM B 2 .   ? -10.848 15.339  -40.169 1.000 22.253 ? 401 4LM A O1  1 ? ?  
HETATM 2971 P  P   . 4LM B 2 .   ? -5.576  9.404   -40.742 1.000 17.435 ? 401 4LM A P   1 ? ?  
HETATM 2972 N  N1  . 4LM B 2 .   ? -4.580  14.425  -37.416 1.000 19.372 ? 401 4LM A N1  1 ? ?  
HETATM 2973 C  C2  . 4LM B 2 .   ? -5.494  15.327  -37.894 1.000 18.789 ? 401 4LM A C2  1 ? ?  
HETATM 2974 C  C3  . 4LM B 2 .   ? -6.562  14.856  -38.649 1.000 19.776 ? 401 4LM A C3  1 ? ?  
HETATM 2975 O  O3  . 4LM B 2 .   ? -7.470  15.653  -39.049 1.000 21.033 ? 401 4LM A O3  1 ? ?  
HETATM 2976 C  C4  . 4LM B 2 .   ? -6.647  13.451  -38.971 1.000 17.949 ? 401 4LM A C4  1 ? ?  
HETATM 2977 C  C5  . 4LM B 2 .   ? -5.665  12.580  -38.466 1.000 17.200 ? 401 4LM A C5  1 ? ?  
HETATM 2978 C  C6  . 4LM B 2 .   ? -4.652  13.102  -37.676 1.000 17.667 ? 401 4LM A C6  1 ? ?  
HETATM 2979 C  CA  . 4LM B 2 .   ? -9.926  13.370  -40.828 1.000 21.382 ? 401 4LM A CA  1 ? ?  
HETATM 2980 C  CB  . 4LM B 2 .   ? -10.119 11.920  -41.127 1.000 23.225 ? 401 4LM A CB  1 ? ?  
HETATM 2981 C  CG  . 4LM B 2 .   ? -11.387 11.363  -41.547 1.000 28.052 ? 401 4LM A CG  1 ? ?  
HETATM 2982 C  C2A . 4LM B 2 .   ? -5.326  16.786  -37.552 1.000 18.703 ? 401 4LM A C2A 1 ? ?  
HETATM 2983 C  C4A . 4LM B 2 .   ? -7.769  12.942  -39.780 1.000 20.501 ? 401 4LM A C4A 1 ? ?  
HETATM 2984 C  C5A . 4LM B 2 .   ? -5.724  11.088  -38.677 1.000 17.720 ? 401 4LM A C5A 1 ? ?  
HETATM 2985 O  OP1 . 4LM B 2 .   ? -7.070  9.563   -41.092 1.000 17.496 ? 401 4LM A OP1 1 ? ?  
HETATM 2986 O  OP2 . 4LM B 2 .   ? -5.338  8.245   -39.810 1.000 16.242 ? 401 4LM A OP2 1 ? ?  
HETATM 2987 O  OP3 . 4LM B 2 .   ? -4.632  9.394   -41.955 1.000 16.587 ? 401 4LM A OP3 1 ? ?  
HETATM 2988 O  OP4 . 4LM B 2 .   ? -5.113  10.762  -39.940 1.000 16.752 ? 401 4LM A OP4 1 ? ?  
HETATM 2989 O  O2  . 4LM B 2 .   ? -11.590 14.491  -41.940 1.000 18.818 ? 401 4LM A O2  1 ? ?  
HETATM 2990 C  C1  . PEG C 3 .   ? 6.483   31.636  -41.055 1.000 50.565 ? 402 PEG A C1  1 ? ?  
HETATM 2991 O  O1  . PEG C 3 .   ? 6.306   32.916  -41.630 1.000 54.234 ? 402 PEG A O1  1 ? ?  
HETATM 2992 C  C2  . PEG C 3 .   ? 7.525   30.810  -41.746 1.000 54.715 ? 402 PEG A C2  1 ? ?  
HETATM 2993 O  O2  . PEG C 3 .   ? 6.894   29.812  -42.550 1.000 52.688 ? 402 PEG A O2  1 ? ?  
HETATM 2994 C  C3  . PEG C 3 .   ? 7.582   28.568  -42.567 1.000 44.151 ? 402 PEG A C3  1 ? ?  
HETATM 2995 C  C4  . PEG C 3 .   ? 7.187   27.775  -43.777 1.000 46.582 ? 402 PEG A C4  1 ? ?  
HETATM 2996 O  O4  . PEG C 3 .   ? 8.303   27.177  -44.454 1.000 50.710 ? 402 PEG A O4  1 ? ?  
HETATM 2997 I  I   . IOD D 4 .   ? -6.054  29.497  -15.981 0.800 32.296 ? 403 IOD A I   1 ? ?  
HETATM 2998 I  I   . IOD E 4 .   ? 13.078  2.101   -27.463 0.500 43.469 ? 404 IOD A I   1 ? ?  
HETATM 2999 MG MG  . MG  F 5 .   ? 20.058  6.715   -54.972 1.000 39.460 ? 405 MG  A MG  1 ? ?  
HETATM 3000 MG MG  . MG  G 5 .   ? -25.242 16.159  -25.595 1.000 43.410 ? 406 MG  A MG  1 ? ?  
HETATM 3001 MG MG  . MG  H 5 .   ? 17.780  5.107   -55.310 1.000 46.402 ? 407 MG  A MG  1 ? ?  
HETATM 3002 O  O   . HOH I 6 .   ? 5.170   39.307  -33.329 1.000 60.195 ? 501 HOH A O   1 ? ?  
HETATM 3003 O  O   . HOH I 6 .   ? 18.274  -2.562  -40.784 1.000 37.267 ? 502 HOH A O   1 ? ?  
HETATM 3004 O  O   . HOH I 6 .   ? 2.262   35.536  -42.011 1.000 41.336 ? 503 HOH A O   1 ? ?  
HETATM 3005 O  O   . HOH I 6 .   ? 4.920   2.305   -15.963 1.000 33.123 ? 504 HOH A O   1 ? ?  
HETATM 3006 O  O   . HOH I 6 .   ? -14.426 21.969  -29.973 1.000 38.868 ? 505 HOH A O   1 ? ?  
HETATM 3007 O  O   . HOH I 6 .   ? 19.671  -4.801  -60.757 1.000 24.204 ? 506 HOH A O   1 ? ?  
HETATM 3008 O  O   . HOH I 6 .   ? 20.146  24.227  -55.688 1.000 47.998 ? 507 HOH A O   1 ? ?  
HETATM 3009 O  O   . HOH I 6 .   ? 1.910   38.889  -35.737 1.000 38.506 ? 508 HOH A O   1 ? ?  
HETATM 3010 O  O   . HOH I 6 .   ? -10.142 19.169  -50.198 1.000 25.090 ? 509 HOH A O   1 ? ?  
HETATM 3011 O  O   . HOH I 6 .   ? -13.622 35.493  -59.699 1.000 52.290 ? 510 HOH A O   1 ? ?  
HETATM 3012 O  O   . HOH I 6 .   ? -17.745 39.587  -47.185 1.000 47.027 ? 511 HOH A O   1 ? ?  
HETATM 3013 O  O   . HOH I 6 .   ? -29.582 25.042  -47.560 1.000 40.682 ? 512 HOH A O   1 ? ?  
HETATM 3014 O  O   . HOH I 6 .   ? -4.830  11.055  -49.654 1.000 18.952 ? 513 HOH A O   1 ? ?  
HETATM 3015 O  O   . HOH I 6 .   ? -8.218  31.228  -25.460 1.000 36.574 ? 514 HOH A O   1 ? ?  
HETATM 3016 O  O   . HOH I 6 .   ? -3.511  18.607  -15.845 1.000 41.599 ? 515 HOH A O   1 ? ?  
HETATM 3017 O  O   . HOH I 6 .   ? 7.029   29.888  -53.757 1.000 35.003 ? 516 HOH A O   1 ? ?  
HETATM 3018 O  O   . HOH I 6 .   ? 17.665  4.144   -50.028 1.000 26.942 ? 517 HOH A O   1 ? ?  
HETATM 3019 O  O   . HOH I 6 .   ? -29.624 34.172  -48.707 1.000 49.668 ? 518 HOH A O   1 ? ?  
HETATM 3020 O  O   . HOH I 6 .   ? 21.019  7.434   -56.616 1.000 32.290 ? 519 HOH A O   1 ? ?  
HETATM 3021 O  O   . HOH I 6 .   ? 26.589  -6.426  -49.842 1.000 37.974 ? 520 HOH A O   1 ? ?  
HETATM 3022 O  O   . HOH I 6 .   ? -14.596 16.938  -45.241 1.000 19.762 ? 521 HOH A O   1 ? ?  
HETATM 3023 O  O   . HOH I 6 .   ? -4.162  15.461  -33.578 1.000 19.658 ? 522 HOH A O   1 ? ?  
HETATM 3024 O  O   . HOH I 6 .   ? -16.966 11.509  -26.860 1.000 46.516 ? 523 HOH A O   1 ? ?  
HETATM 3025 O  O   . HOH I 6 .   ? -8.218  12.909  -48.411 1.000 22.252 ? 524 HOH A O   1 ? ?  
HETATM 3026 O  O   . HOH I 6 .   ? 9.146   21.665  -38.749 1.000 19.785 ? 525 HOH A O   1 ? ?  
HETATM 3027 O  O   . HOH I 6 .   ? 16.899  4.003   -56.531 1.000 26.412 ? 526 HOH A O   1 ? ?  
HETATM 3028 O  O   . HOH I 6 .   ? 7.490   7.709   -20.592 1.000 29.697 ? 527 HOH A O   1 ? ?  
HETATM 3029 O  O   . HOH I 6 .   ? -9.065  28.093  -28.025 1.000 28.613 ? 528 HOH A O   1 ? ?  
HETATM 3030 O  O   . HOH I 6 .   ? -15.473 17.600  -54.673 1.000 24.629 ? 529 HOH A O   1 ? ?  
HETATM 3031 O  O   . HOH I 6 .   ? -18.939 9.683   -41.543 1.000 26.378 ? 530 HOH A O   1 ? ?  
HETATM 3032 O  O   . HOH I 6 .   ? 17.753  -0.040  -57.085 1.000 26.900 ? 531 HOH A O   1 ? ?  
HETATM 3033 O  O   . HOH I 6 .   ? -19.740 28.891  -61.691 1.000 44.969 ? 532 HOH A O   1 ? ?  
HETATM 3034 O  O   . HOH I 6 .   ? -3.163  41.023  -40.170 1.000 42.173 ? 533 HOH A O   1 ? ?  
HETATM 3035 O  O   . HOH I 6 .   ? -8.369  22.478  -48.364 1.000 19.239 ? 534 HOH A O   1 ? ?  
HETATM 3036 O  O   . HOH I 6 .   ? -0.992  27.692  -36.707 1.000 20.376 ? 535 HOH A O   1 ? ?  
HETATM 3037 O  O   . HOH I 6 .   ? 23.922  -13.769 -51.701 1.000 26.290 ? 536 HOH A O   1 ? ?  
HETATM 3038 O  O   . HOH I 6 .   ? -0.804  10.055  -14.492 1.000 41.521 ? 537 HOH A O   1 ? ?  
HETATM 3039 O  O   . HOH I 6 .   ? -26.852 28.586  -34.744 1.000 40.661 ? 538 HOH A O   1 ? ?  
HETATM 3040 O  O   . HOH I 6 .   ? -5.674  38.245  -43.782 1.000 42.176 ? 539 HOH A O   1 ? ?  
HETATM 3041 O  O   . HOH I 6 .   ? 25.055  5.986   -61.217 1.000 36.470 ? 540 HOH A O   1 ? ?  
HETATM 3042 O  O   . HOH I 6 .   ? -22.029 36.672  -49.869 1.000 43.451 ? 541 HOH A O   1 ? ?  
HETATM 3043 O  O   . HOH I 6 .   ? 18.568  19.773  -55.961 1.000 39.068 ? 542 HOH A O   1 ? ?  
HETATM 3044 O  O   . HOH I 6 .   ? -14.188 22.361  -23.713 1.000 32.116 ? 543 HOH A O   1 ? ?  
HETATM 3045 O  O   . HOH I 6 .   ? 18.108  7.467   -55.328 1.000 36.074 ? 544 HOH A O   1 ? ?  
HETATM 3046 O  O   . HOH I 6 .   ? 12.207  25.558  -25.738 1.000 37.602 ? 545 HOH A O   1 ? ?  
HETATM 3047 O  O   . HOH I 6 .   ? 24.508  0.929   -64.257 1.000 33.288 ? 546 HOH A O   1 ? ?  
HETATM 3048 O  O   . HOH I 6 .   ? -16.710 29.116  -63.918 1.000 46.875 ? 547 HOH A O   1 ? ?  
HETATM 3049 O  O   . HOH I 6 .   ? -7.680  38.471  -33.636 1.000 34.126 ? 548 HOH A O   1 ? ?  
HETATM 3050 O  O   . HOH I 6 .   ? -23.184 10.717  -39.603 1.000 36.470 ? 549 HOH A O   1 ? ?  
HETATM 3051 O  O   . HOH I 6 .   ? 22.018  -5.776  -62.412 1.000 38.124 ? 550 HOH A O   1 ? ?  
HETATM 3052 O  O   . HOH I 6 .   ? -31.751 19.525  -42.081 1.000 35.951 ? 551 HOH A O   1 ? ?  
HETATM 3053 O  O   . HOH I 6 .   ? 17.013  7.085   -26.838 1.000 29.782 ? 552 HOH A O   1 ? ?  
HETATM 3054 O  O   . HOH I 6 .   ? 2.212   8.013   -12.292 1.000 44.475 ? 553 HOH A O   1 ? ?  
HETATM 3055 O  O   . HOH I 6 .   ? -23.646 24.101  -57.782 1.000 36.462 ? 554 HOH A O   1 ? ?  
HETATM 3056 O  O   . HOH I 6 .   ? 17.200  -10.074 -46.018 1.000 17.952 ? 555 HOH A O   1 ? ?  
HETATM 3057 O  O   . HOH I 6 .   ? -29.395 28.191  -45.228 1.000 38.521 ? 556 HOH A O   1 ? ?  
HETATM 3058 O  O   . HOH I 6 .   ? -21.641 10.669  -31.340 1.000 31.097 ? 557 HOH A O   1 ? ?  
HETATM 3059 O  O   . HOH I 6 .   ? -0.623  9.429   -47.545 1.000 27.497 ? 558 HOH A O   1 ? ?  
HETATM 3060 O  O   . HOH I 6 .   ? 5.929   10.544  -16.293 1.000 40.724 ? 559 HOH A O   1 ? ?  
HETATM 3061 O  O   . HOH I 6 .   ? -12.397 29.282  -33.875 1.000 26.347 ? 560 HOH A O   1 ? ?  
HETATM 3062 O  O   . HOH I 6 .   ? -13.222 10.404  -38.718 1.000 27.857 ? 561 HOH A O   1 ? ?  
HETATM 3063 O  O   . HOH I 6 .   ? -6.253  24.407  -59.959 1.000 35.066 ? 562 HOH A O   1 ? ?  
HETATM 3064 O  O   . HOH I 6 .   ? -10.140 22.575  -20.937 1.000 32.129 ? 563 HOH A O   1 ? ?  
HETATM 3065 O  O   . HOH I 6 .   ? -4.401  19.351  -52.675 1.000 17.831 ? 564 HOH A O   1 ? ?  
HETATM 3066 O  O   . HOH I 6 .   ? -27.432 24.029  -33.377 1.000 53.047 ? 565 HOH A O   1 ? ?  
HETATM 3067 O  O   . HOH I 6 .   ? -1.995  31.969  -52.187 1.000 30.754 ? 566 HOH A O   1 ? ?  
HETATM 3068 O  O   . HOH I 6 .   ? -27.015 32.476  -51.109 1.000 35.090 ? 567 HOH A O   1 ? ?  
HETATM 3069 O  O   . HOH I 6 .   ? -29.686 25.539  -44.860 1.000 42.016 ? 568 HOH A O   1 ? ?  
HETATM 3070 O  O   . HOH I 6 .   ? 16.069  8.142   -50.556 1.000 25.962 ? 569 HOH A O   1 ? ?  
HETATM 3071 O  O   . HOH I 6 .   ? -23.845 18.901  -30.042 1.000 52.428 ? 570 HOH A O   1 ? ?  
HETATM 3072 O  O   . HOH I 6 .   ? 1.155   0.734   -50.054 1.000 29.104 ? 571 HOH A O   1 ? ?  
HETATM 3073 O  O   . HOH I 6 .   ? -16.632 21.479  -26.476 1.000 31.656 ? 572 HOH A O   1 ? ?  
HETATM 3074 O  O   . HOH I 6 .   ? 3.364   34.530  -31.809 1.000 44.324 ? 573 HOH A O   1 ? ?  
HETATM 3075 O  O   . HOH I 6 .   ? -16.380 9.759   -24.983 1.000 39.988 ? 574 HOH A O   1 ? ?  
HETATM 3076 O  O   . HOH I 6 .   ? -1.638  15.804  -59.610 1.000 15.955 ? 575 HOH A O   1 ? ?  
HETATM 3077 O  O   . HOH I 6 .   ? 9.438   28.897  -51.462 1.000 39.027 ? 576 HOH A O   1 ? ?  
HETATM 3078 O  O   . HOH I 6 .   ? -5.167  24.324  -16.902 1.000 30.700 ? 577 HOH A O   1 ? ?  
HETATM 3079 O  O   . HOH I 6 .   ? 0.250   1.973   -46.686 1.000 17.096 ? 578 HOH A O   1 ? ?  
HETATM 3080 O  O   . HOH I 6 .   ? -23.273 16.459  -24.878 1.000 38.058 ? 579 HOH A O   1 ? ?  
HETATM 3081 O  O   . HOH I 6 .   ? -25.154 30.270  -56.943 1.000 43.533 ? 580 HOH A O   1 ? ?  
HETATM 3082 O  O   . HOH I 6 .   ? 16.466  14.352  -58.091 1.000 37.982 ? 581 HOH A O   1 ? ?  
HETATM 3083 O  O   . HOH I 6 .   ? 8.890   4.581   -60.167 1.000 19.453 ? 582 HOH A O   1 ? ?  
HETATM 3084 O  O   . HOH I 6 .   ? -28.444 22.096  -55.155 1.000 52.355 ? 583 HOH A O   1 ? ?  
HETATM 3085 O  O   . HOH I 6 .   ? -16.879 8.837   -38.443 1.000 43.447 ? 584 HOH A O   1 ? ?  
HETATM 3086 O  O   . HOH I 6 .   ? 8.266   31.840  -24.941 1.000 41.826 ? 585 HOH A O   1 ? ?  
HETATM 3087 O  O   . HOH I 6 .   ? 13.145  15.534  -31.475 1.000 25.244 ? 586 HOH A O   1 ? ?  
HETATM 3088 O  O   . HOH I 6 .   ? -22.375 18.379  -32.177 1.000 31.956 ? 587 HOH A O   1 ? ?  
HETATM 3089 O  O   . HOH I 6 .   ? -10.738 36.436  -47.043 1.000 34.420 ? 588 HOH A O   1 ? ?  
HETATM 3090 O  O   . HOH I 6 .   ? 24.847  -6.541  -40.877 1.000 43.573 ? 589 HOH A O   1 ? ?  
HETATM 3091 O  O   . HOH I 6 .   ? 21.146  8.694   -32.306 1.000 34.711 ? 590 HOH A O   1 ? ?  
HETATM 3092 O  O   . HOH I 6 .   ? 8.978   10.387  -23.034 1.000 29.597 ? 591 HOH A O   1 ? ?  
HETATM 3093 O  O   . HOH I 6 .   ? -14.519 33.906  -34.349 1.000 36.719 ? 592 HOH A O   1 ? ?  
HETATM 3094 O  O   . HOH I 6 .   ? 12.013  3.439   -41.989 1.000 22.777 ? 593 HOH A O   1 ? ?  
HETATM 3095 O  O   . HOH I 6 .   ? -1.823  23.161  -11.396 1.000 37.503 ? 594 HOH A O   1 ? ?  
HETATM 3096 O  O   . HOH I 6 .   ? 7.431   32.238  -36.293 1.000 33.933 ? 595 HOH A O   1 ? ?  
HETATM 3097 O  O   . HOH I 6 .   ? 4.856   6.344   -15.646 1.000 28.415 ? 596 HOH A O   1 ? ?  
HETATM 3098 O  O   . HOH I 6 .   ? 16.408  14.388  -45.414 1.000 28.904 ? 597 HOH A O   1 ? ?  
HETATM 3099 O  O   . HOH I 6 .   ? 1.187   31.088  -16.611 1.000 40.812 ? 598 HOH A O   1 ? ?  
HETATM 3100 O  O   . HOH I 6 .   ? -7.270  30.704  -31.525 1.000 26.178 ? 599 HOH A O   1 ? ?  
HETATM 3101 O  O   . HOH I 6 .   ? -3.473  11.813  -51.855 1.000 17.293 ? 600 HOH A O   1 ? ?  
HETATM 3102 O  O   . HOH I 6 .   ? -26.227 17.782  -53.498 1.000 36.900 ? 601 HOH A O   1 ? ?  
HETATM 3103 O  O   . HOH I 6 .   ? -33.290 25.813  -39.682 1.000 50.113 ? 602 HOH A O   1 ? ?  
HETATM 3104 O  O   . HOH I 6 .   ? 6.361   30.444  -23.299 1.000 27.063 ? 603 HOH A O   1 ? ?  
HETATM 3105 O  O   . HOH I 6 .   ? -8.796  29.202  -21.774 1.000 34.112 ? 604 HOH A O   1 ? ?  
HETATM 3106 O  O   . HOH I 6 .   ? 4.533   30.764  -54.248 1.000 27.979 ? 605 HOH A O   1 ? ?  
HETATM 3107 O  O   . HOH I 6 .   ? 15.398  19.717  -36.493 1.000 34.438 ? 606 HOH A O   1 ? ?  
HETATM 3108 O  O   . HOH I 6 .   ? 7.316   0.014   -46.565 1.000 18.493 ? 607 HOH A O   1 ? ?  
HETATM 3109 O  O   . HOH I 6 .   ? -23.680 17.635  -50.930 1.000 25.045 ? 608 HOH A O   1 ? ?  
HETATM 3110 O  O   . HOH I 6 .   ? 21.898  9.671   -59.414 1.000 43.912 ? 609 HOH A O   1 ? ?  
HETATM 3111 O  O   . HOH I 6 .   ? 15.595  5.472   -51.363 1.000 24.184 ? 610 HOH A O   1 ? ?  
HETATM 3112 O  O   . HOH I 6 .   ? 20.953  -1.080  -42.349 1.000 36.547 ? 611 HOH A O   1 ? ?  
HETATM 3113 O  O   . HOH I 6 .   ? 12.881  12.389  -24.932 1.000 48.585 ? 612 HOH A O   1 ? ?  
HETATM 3114 O  O   . HOH I 6 .   ? 5.215   30.417  -32.442 1.000 23.526 ? 613 HOH A O   1 ? ?  
HETATM 3115 O  O   . HOH I 6 .   ? -8.185  31.874  -56.302 1.000 28.421 ? 614 HOH A O   1 ? ?  
HETATM 3116 O  O   . HOH I 6 .   ? 20.226  1.518   -58.390 1.000 25.640 ? 615 HOH A O   1 ? ?  
HETATM 3117 O  O   . HOH I 6 .   ? -0.800  27.834  -57.346 1.000 21.756 ? 616 HOH A O   1 ? ?  
HETATM 3118 O  O   . HOH I 6 .   ? 1.164   33.669  -27.572 1.000 41.824 ? 617 HOH A O   1 ? ?  
HETATM 3119 O  O   . HOH I 6 .   ? -4.575  33.472  -19.801 1.000 47.570 ? 618 HOH A O   1 ? ?  
HETATM 3120 O  O   . HOH I 6 .   ? -0.942  16.093  -45.130 1.000 17.656 ? 619 HOH A O   1 ? ?  
HETATM 3121 O  O   . HOH I 6 .   ? 24.918  -2.272  -46.609 1.000 34.750 ? 620 HOH A O   1 ? ?  
HETATM 3122 O  O   . HOH I 6 .   ? 15.983  20.802  -45.068 1.000 31.723 ? 621 HOH A O   1 ? ?  
HETATM 3123 O  O   . HOH I 6 .   ? -18.812 11.875  -21.996 1.000 36.919 ? 622 HOH A O   1 ? ?  
HETATM 3124 O  O   . HOH I 6 .   ? -4.375  32.288  -46.729 1.000 24.356 ? 623 HOH A O   1 ? ?  
HETATM 3125 O  O   . HOH I 6 .   ? -5.663  20.242  -37.046 1.000 19.127 ? 624 HOH A O   1 ? ?  
HETATM 3126 O  O   . HOH I 6 .   ? 12.016  0.724   -38.887 1.000 21.781 ? 625 HOH A O   1 ? ?  
HETATM 3127 O  O   . HOH I 6 .   ? 20.837  -6.990  -48.250 1.000 19.904 ? 626 HOH A O   1 ? ?  
HETATM 3128 O  O   . HOH I 6 .   ? 4.781   27.092  -54.275 1.000 24.140 ? 627 HOH A O   1 ? ?  
HETATM 3129 O  O   . HOH I 6 .   ? 17.881  18.719  -35.639 1.000 47.777 ? 628 HOH A O   1 ? ?  
HETATM 3130 O  O   . HOH I 6 .   ? 6.441   27.996  -38.863 1.000 24.493 ? 629 HOH A O   1 ? ?  
HETATM 3131 O  O   . HOH I 6 .   ? -4.421  25.589  -31.699 1.000 24.974 ? 630 HOH A O   1 ? ?  
HETATM 3132 O  O   . HOH I 6 .   ? 17.286  -1.993  -43.036 1.000 24.443 ? 631 HOH A O   1 ? ?  
HETATM 3133 O  O   . HOH I 6 .   ? -5.154  24.216  -44.508 1.000 21.575 ? 632 HOH A O   1 ? ?  
HETATM 3134 O  O   . HOH I 6 .   ? 13.177  21.637  -32.566 1.000 32.584 ? 633 HOH A O   1 ? ?  
HETATM 3135 O  O   . HOH I 6 .   ? -9.066  25.556  -29.203 1.000 28.225 ? 634 HOH A O   1 ? ?  
HETATM 3136 O  O   . HOH I 6 .   ? 16.133  11.867  -27.184 1.000 31.261 ? 635 HOH A O   1 ? ?  
HETATM 3137 O  O   . HOH I 6 .   ? 0.639   31.028  -50.364 1.000 44.784 ? 636 HOH A O   1 ? ?  
HETATM 3138 O  O   . HOH I 6 .   ? -14.356 7.577   -40.042 1.000 43.600 ? 637 HOH A O   1 ? ?  
HETATM 3139 O  O   . HOH I 6 .   ? -0.965  20.510  -12.174 1.000 51.871 ? 638 HOH A O   1 ? ?  
HETATM 3140 O  O   . HOH I 6 .   ? 2.906   8.552   -45.254 1.000 17.884 ? 639 HOH A O   1 ? ?  
HETATM 3141 O  O   . HOH I 6 .   ? -5.908  41.446  -35.774 1.000 39.853 ? 640 HOH A O   1 ? ?  
HETATM 3142 O  O   . HOH I 6 .   ? -19.816 34.388  -57.721 1.000 48.996 ? 641 HOH A O   1 ? ?  
HETATM 3143 O  O   . HOH I 6 .   ? -7.275  27.124  -42.836 1.000 21.395 ? 642 HOH A O   1 ? ?  
HETATM 3144 O  O   . HOH I 6 .   ? 6.475   24.285  -17.597 1.000 26.416 ? 643 HOH A O   1 ? ?  
HETATM 3145 O  O   . HOH I 6 .   ? 8.848   13.121  -22.301 1.000 25.846 ? 644 HOH A O   1 ? ?  
HETATM 3146 O  O   . HOH I 6 .   ? -13.375 10.382  -35.237 1.000 30.756 ? 645 HOH A O   1 ? ?  
HETATM 3147 O  O   . HOH I 6 .   ? -30.354 20.069  -48.473 1.000 37.068 ? 646 HOH A O   1 ? ?  
HETATM 3148 O  O   . HOH I 6 .   ? -23.017 12.789  -33.382 1.000 39.040 ? 647 HOH A O   1 ? ?  
HETATM 3149 O  O   . HOH I 6 .   ? 13.198  18.395  -25.661 1.000 33.194 ? 648 HOH A O   1 ? ?  
HETATM 3150 O  O   . HOH I 6 .   ? 13.797  16.482  -29.115 1.000 31.289 ? 649 HOH A O   1 ? ?  
HETATM 3151 O  O   . HOH I 6 .   ? 1.612   22.923  -13.013 1.000 47.783 ? 650 HOH A O   1 ? ?  
HETATM 3152 O  O   . HOH I 6 .   ? -8.715  13.533  -56.113 1.000 28.708 ? 651 HOH A O   1 ? ?  
HETATM 3153 O  O   . HOH I 6 .   ? 15.704  7.780   -53.964 1.000 42.921 ? 652 HOH A O   1 ? ?  
HETATM 3154 O  O   . HOH I 6 .   ? 2.660   -1.173  -51.639 1.000 22.606 ? 653 HOH A O   1 ? ?  
HETATM 3155 O  O   . HOH I 6 .   ? -8.646  6.886   -33.430 1.000 20.874 ? 654 HOH A O   1 ? ?  
HETATM 3156 O  O   . HOH I 6 .   ? -21.344 15.799  -31.865 1.000 25.315 ? 655 HOH A O   1 ? ?  
HETATM 3157 O  O   . HOH I 6 .   ? 15.734  12.259  -59.877 1.000 39.744 ? 656 HOH A O   1 ? ?  
HETATM 3158 O  O   . HOH I 6 .   ? 16.698  2.933   -37.553 1.000 37.368 ? 657 HOH A O   1 ? ?  
HETATM 3159 O  O   . HOH I 6 .   ? 7.355   27.540  -47.310 1.000 42.505 ? 658 HOH A O   1 ? ?  
HETATM 3160 O  O   . HOH I 6 .   ? -2.985  31.890  -30.035 1.000 33.388 ? 659 HOH A O   1 ? ?  
HETATM 3161 O  O   . HOH I 6 .   ? -6.146  10.523  -58.086 1.000 21.352 ? 660 HOH A O   1 ? ?  
HETATM 3162 O  O   . HOH I 6 .   ? 6.679   32.343  -33.658 1.000 33.265 ? 661 HOH A O   1 ? ?  
HETATM 3163 O  O   . HOH I 6 .   ? 7.574   21.359  -55.350 1.000 18.175 ? 662 HOH A O   1 ? ?  
HETATM 3164 O  O   . HOH I 6 .   ? -28.806 29.572  -41.316 1.000 36.282 ? 663 HOH A O   1 ? ?  
HETATM 3165 O  O   . HOH I 6 .   ? -8.357  34.390  -55.627 1.000 39.498 ? 664 HOH A O   1 ? ?  
HETATM 3166 O  O   . HOH I 6 .   ? 11.476  13.432  -58.187 1.000 37.232 ? 665 HOH A O   1 ? ?  
HETATM 3167 O  O   . HOH I 6 .   ? -13.502 23.400  -27.807 1.000 34.711 ? 666 HOH A O   1 ? ?  
HETATM 3168 O  O   . HOH I 6 .   ? -6.205  26.018  -29.574 1.000 25.026 ? 667 HOH A O   1 ? ?  
HETATM 3169 O  O   . HOH I 6 .   ? -0.708  29.467  -27.490 1.000 23.222 ? 668 HOH A O   1 ? ?  
HETATM 3170 O  O   . HOH I 6 .   ? 26.341  -6.945  -54.093 1.000 58.146 ? 669 HOH A O   1 ? ?  
HETATM 3171 O  O   . HOH I 6 .   ? 20.236  14.572  -33.046 1.000 32.316 ? 670 HOH A O   1 ? ?  
HETATM 3172 O  O   . HOH I 6 .   ? 0.445   4.847   -46.353 1.000 18.369 ? 671 HOH A O   1 ? ?  
HETATM 3173 O  O   . HOH I 6 .   ? -1.492  22.108  -38.840 1.000 18.634 ? 672 HOH A O   1 ? ?  
HETATM 3174 O  O   . HOH I 6 .   ? 15.416  -3.185  -44.608 1.000 17.477 ? 673 HOH A O   1 ? ?  
HETATM 3175 O  O   . HOH I 6 .   ? 10.631  10.605  -57.176 1.000 34.158 ? 674 HOH A O   1 ? ?  
HETATM 3176 O  O   . HOH I 6 .   ? 12.700  23.317  -39.145 1.000 36.810 ? 675 HOH A O   1 ? ?  
HETATM 3177 O  O   . HOH I 6 .   ? -0.933  1.213   -34.726 1.000 32.838 ? 676 HOH A O   1 ? ?  
HETATM 3178 O  O   . HOH I 6 .   ? 0.264   18.212  -43.868 1.000 16.980 ? 677 HOH A O   1 ? ?  
HETATM 3179 O  O   . HOH I 6 .   ? -3.513  33.792  -50.552 1.000 54.294 ? 678 HOH A O   1 ? ?  
HETATM 3180 O  O   . HOH I 6 .   ? -13.146 33.989  -36.856 1.000 28.299 ? 679 HOH A O   1 ? ?  
HETATM 3181 O  O   . HOH I 6 .   ? -4.954  11.033  -12.973 1.000 58.689 ? 680 HOH A O   1 ? ?  
HETATM 3182 O  O   . HOH I 6 .   ? -8.185  27.108  -59.559 1.000 22.032 ? 681 HOH A O   1 ? ?  
HETATM 3183 O  O   . HOH I 6 .   ? 26.156  -5.040  -43.838 1.000 51.187 ? 682 HOH A O   1 ? ?  
HETATM 3184 O  O   . HOH I 6 .   ? 21.553  -9.951  -41.516 1.000 32.594 ? 683 HOH A O   1 ? ?  
HETATM 3185 O  O   . HOH I 6 .   ? 16.104  1.899   -33.791 1.000 36.016 ? 684 HOH A O   1 ? ?  
HETATM 3186 O  O   . HOH I 6 .   ? 11.918  26.619  -21.425 1.000 29.885 ? 685 HOH A O   1 ? ?  
HETATM 3187 O  O   . HOH I 6 .   ? 11.423  4.296   -61.411 1.000 19.905 ? 686 HOH A O   1 ? ?  
HETATM 3188 O  O   . HOH I 6 .   ? -18.686 36.894  -52.957 1.000 53.730 ? 687 HOH A O   1 ? ?  
HETATM 3189 O  O   . HOH I 6 .   ? 14.088  7.048   -42.101 1.000 29.437 ? 688 HOH A O   1 ? ?  
HETATM 3190 O  O   . HOH I 6 .   ? -27.449 16.275  -44.686 1.000 25.560 ? 689 HOH A O   1 ? ?  
HETATM 3191 O  O   . HOH I 6 .   ? 19.569  12.948  -59.626 1.000 32.033 ? 690 HOH A O   1 ? ?  
HETATM 3192 O  O   . HOH I 6 .   ? -3.945  4.070   -49.006 1.000 18.520 ? 691 HOH A O   1 ? ?  
HETATM 3193 O  O   . HOH I 6 .   ? -5.947  14.466  -49.837 1.000 17.736 ? 692 HOH A O   1 ? ?  
HETATM 3194 O  O   . HOH I 6 .   ? -14.003 8.783   -28.588 1.000 24.137 ? 693 HOH A O   1 ? ?  
HETATM 3195 O  O   . HOH I 6 .   ? -20.851 20.181  -36.656 1.000 21.307 ? 694 HOH A O   1 ? ?  
HETATM 3196 O  O   . HOH I 6 .   ? 11.994  18.299  -23.179 1.000 36.744 ? 695 HOH A O   1 ? ?  
HETATM 3197 O  O   . HOH I 6 .   ? -17.400 35.685  -38.452 1.000 38.889 ? 696 HOH A O   1 ? ?  
HETATM 3198 O  O   . HOH I 6 .   ? -17.414 13.402  -55.603 1.000 35.793 ? 697 HOH A O   1 ? ?  
HETATM 3199 O  O   . HOH I 6 .   ? 10.654  4.055   -25.797 1.000 32.568 ? 698 HOH A O   1 ? ?  
HETATM 3200 O  O   . HOH I 6 .   ? 13.024  -3.067  -33.875 1.000 33.410 ? 699 HOH A O   1 ? ?  
HETATM 3201 O  O   . HOH I 6 .   ? -12.880 19.028  -31.354 1.000 21.899 ? 700 HOH A O   1 ? ?  
HETATM 3202 O  O   . HOH I 6 .   ? 7.408   35.788  -38.404 1.000 52.846 ? 701 HOH A O   1 ? ?  
HETATM 3203 O  O   . HOH I 6 .   ? 12.214  2.775   -45.045 1.000 17.522 ? 702 HOH A O   1 ? ?  
HETATM 3204 O  O   . HOH I 6 .   ? 1.898   -1.578  -44.894 1.000 17.888 ? 703 HOH A O   1 ? ?  
HETATM 3205 O  O   . HOH I 6 .   ? -9.628  3.903   -22.320 1.000 37.676 ? 704 HOH A O   1 ? ?  
HETATM 3206 O  O   . HOH I 6 .   ? -6.766  36.716  -30.394 1.000 44.744 ? 705 HOH A O   1 ? ?  
HETATM 3207 O  O   . HOH I 6 .   ? 10.635  31.717  -22.600 1.000 37.861 ? 706 HOH A O   1 ? ?  
HETATM 3208 O  O   . HOH I 6 .   ? 6.477   17.958  -15.029 1.000 44.214 ? 707 HOH A O   1 ? ?  
HETATM 3209 O  O   . HOH I 6 .   ? -0.697  14.967  -10.719 1.000 58.145 ? 708 HOH A O   1 ? ?  
HETATM 3210 O  O   . HOH I 6 .   ? 9.181   13.400  -19.656 1.000 43.620 ? 709 HOH A O   1 ? ?  
HETATM 3211 O  O   . HOH I 6 .   ? 4.633   0.967   -35.934 1.000 17.517 ? 710 HOH A O   1 ? ?  
HETATM 3212 O  O   . HOH I 6 .   ? -19.325 16.842  -55.926 1.000 40.573 ? 711 HOH A O   1 ? ?  
HETATM 3213 O  O   . HOH I 6 .   ? -26.418 23.991  -58.395 1.000 55.212 ? 712 HOH A O   1 ? ?  
HETATM 3214 O  O   . HOH I 6 .   ? 25.894  -1.930  -50.420 1.000 33.971 ? 713 HOH A O   1 ? ?  
HETATM 3215 O  O   . HOH I 6 .   ? -14.403 19.545  -44.559 1.000 17.785 ? 714 HOH A O   1 ? ?  
HETATM 3216 O  O   . HOH I 6 .   ? -19.831 18.199  -24.115 1.000 52.158 ? 715 HOH A O   1 ? ?  
HETATM 3217 O  O   . HOH I 6 .   ? 17.126  9.021   -36.106 1.000 22.595 ? 716 HOH A O   1 ? ?  
HETATM 3218 O  O   . HOH I 6 .   ? 1.054   1.843   -34.430 1.000 39.427 ? 717 HOH A O   1 ? ?  
HETATM 3219 O  O   . HOH I 6 .   ? 8.951   29.099  -38.661 1.000 36.207 ? 718 HOH A O   1 ? ?  
HETATM 3220 O  O   . HOH I 6 .   ? 0.000   13.766  -58.473 0.500 16.961 ? 719 HOH A O   1 ? ?  
HETATM 3221 O  O   . HOH I 6 .   ? -18.761 16.678  -31.323 1.000 26.112 ? 720 HOH A O   1 ? ?  
HETATM 3222 O  O   . HOH I 6 .   ? 18.478  10.532  -52.953 1.000 33.522 ? 721 HOH A O   1 ? ?  
HETATM 3223 O  O   . HOH I 6 .   ? -21.049 25.972  -59.334 1.000 30.171 ? 722 HOH A O   1 ? ?  
HETATM 3224 O  O   . HOH I 6 .   ? 10.866  9.140   -25.082 1.000 41.361 ? 723 HOH A O   1 ? ?  
HETATM 3225 O  O   . HOH I 6 .   ? -4.245  0.433   -16.782 1.000 35.975 ? 724 HOH A O   1 ? ?  
HETATM 3226 O  O   . HOH I 6 .   ? -3.615  3.080   -46.412 1.000 20.430 ? 725 HOH A O   1 ? ?  
HETATM 3227 O  O   . HOH I 6 .   ? -9.449  29.365  -58.670 1.000 26.345 ? 726 HOH A O   1 ? ?  
HETATM 3228 O  O   . HOH I 6 .   ? 2.842   32.127  -49.676 1.000 56.470 ? 727 HOH A O   1 ? ?  
HETATM 3229 O  O   . HOH I 6 .   ? -6.615  23.840  -27.889 1.000 22.641 ? 728 HOH A O   1 ? ?  
HETATM 3230 O  O   . HOH I 6 .   ? 2.139   6.880   -47.299 1.000 18.572 ? 729 HOH A O   1 ? ?  
HETATM 3231 O  O   . HOH I 6 .   ? -21.958 15.752  -52.038 1.000 21.234 ? 730 HOH A O   1 ? ?  
HETATM 3232 O  O   . HOH I 6 .   ? 6.692   9.221   -56.379 1.000 20.392 ? 731 HOH A O   1 ? ?  
HETATM 3233 O  O   . HOH I 6 .   ? -7.896  20.789  -18.378 1.000 35.655 ? 732 HOH A O   1 ? ?  
HETATM 3234 O  O   . HOH I 6 .   ? -3.166  19.912  -37.950 1.000 18.919 ? 733 HOH A O   1 ? ?  
HETATM 3235 O  O   . HOH I 6 .   ? 14.588  10.118  -42.608 1.000 21.121 ? 734 HOH A O   1 ? ?  
HETATM 3236 O  O   . HOH I 6 .   ? 6.730   -4.026  -49.038 1.000 21.471 ? 735 HOH A O   1 ? ?  
HETATM 3237 O  O   . HOH I 6 .   ? -16.433 23.400  -29.591 1.000 40.874 ? 736 HOH A O   1 ? ?  
HETATM 3238 O  O   . HOH I 6 .   ? -25.232 14.736  -33.315 1.000 39.822 ? 737 HOH A O   1 ? ?  
HETATM 3239 O  O   . HOH I 6 .   ? -12.115 39.710  -39.031 1.000 36.986 ? 738 HOH A O   1 ? ?  
HETATM 3240 O  O   . HOH I 6 .   ? -9.433  12.810  -18.027 1.000 50.561 ? 739 HOH A O   1 ? ?  
HETATM 3241 O  O   . HOH I 6 .   ? -25.020 17.867  -26.585 1.000 45.946 ? 740 HOH A O   1 ? ?  
HETATM 3242 O  O   . HOH I 6 .   ? -24.180 22.184  -30.322 1.000 40.999 ? 741 HOH A O   1 ? ?  
HETATM 3243 O  O   . HOH I 6 .   ? 12.124  -7.519  -37.932 1.000 22.936 ? 742 HOH A O   1 ? ?  
HETATM 3244 O  O   . HOH I 6 .   ? -31.667 22.807  -35.699 1.000 38.161 ? 743 HOH A O   1 ? ?  
HETATM 3245 O  O   . HOH I 6 .   ? -22.946 16.621  -57.525 1.000 52.642 ? 744 HOH A O   1 ? ?  
HETATM 3246 O  O   . HOH I 6 .   ? -24.491 17.293  -34.120 1.000 30.547 ? 745 HOH A O   1 ? ?  
HETATM 3247 O  O   . HOH I 6 .   ? -15.674 6.049   -33.015 1.000 40.920 ? 746 HOH A O   1 ? ?  
HETATM 3248 O  O   . HOH I 6 .   ? -8.352  24.871  -20.689 1.000 23.981 ? 747 HOH A O   1 ? ?  
HETATM 3249 O  O   . HOH I 6 .   ? 13.752  19.999  -21.697 1.000 41.692 ? 748 HOH A O   1 ? ?  
HETATM 3250 O  O   . HOH I 6 .   ? -13.249 28.509  -30.023 1.000 33.011 ? 749 HOH A O   1 ? ?  
HETATM 3251 O  O   . HOH I 6 .   ? 11.513  28.199  -50.086 1.000 30.088 ? 750 HOH A O   1 ? ?  
HETATM 3252 O  O   . HOH I 6 .   ? -9.541  17.557  -19.205 1.000 38.044 ? 751 HOH A O   1 ? ?  
HETATM 3253 O  O   . HOH I 6 .   ? -12.640 35.493  -57.117 1.000 43.676 ? 752 HOH A O   1 ? ?  
HETATM 3254 O  O   . HOH I 6 .   ? -11.224 27.240  -26.527 1.000 32.826 ? 753 HOH A O   1 ? ?  
HETATM 3255 O  O   . HOH I 6 .   ? -5.371  6.003   -16.902 1.000 38.530 ? 754 HOH A O   1 ? ?  
HETATM 3256 O  O   . HOH I 6 .   ? 0.098   35.412  -46.269 1.000 44.718 ? 755 HOH A O   1 ? ?  
HETATM 3257 O  O   . HOH I 6 .   ? -13.220 31.823  -61.121 1.000 34.477 ? 756 HOH A O   1 ? ?  
HETATM 3258 O  O   . HOH I 6 .   ? -1.710  7.806   -15.199 1.000 43.141 ? 757 HOH A O   1 ? ?  
HETATM 3259 O  O   . HOH I 6 .   ? -31.579 18.533  -37.195 1.000 47.299 ? 758 HOH A O   1 ? ?  
HETATM 3260 O  O   . HOH I 6 .   ? 5.909   21.187  -53.125 1.000 18.436 ? 759 HOH A O   1 ? ?  
HETATM 3261 O  O   . HOH I 6 .   ? -4.307  36.650  -16.923 1.000 44.494 ? 760 HOH A O   1 ? ?  
HETATM 3262 O  O   . HOH I 6 .   ? -30.467 27.541  -54.341 1.000 51.588 ? 761 HOH A O   1 ? ?  
HETATM 3263 O  O   . HOH I 6 .   ? 15.628  4.639   -43.854 1.000 35.586 ? 762 HOH A O   1 ? ?  
HETATM 3264 O  O   . HOH I 6 .   ? 4.794   22.795  -55.771 1.000 22.259 ? 763 HOH A O   1 ? ?  
HETATM 3265 O  O   . HOH I 6 .   ? -16.425 10.160  -35.224 1.000 32.524 ? 764 HOH A O   1 ? ?  
HETATM 3266 O  O   . HOH I 6 .   ? 10.642  28.118  -28.494 1.000 40.870 ? 765 HOH A O   1 ? ?  
HETATM 3267 O  O   . HOH I 6 .   ? -1.508  31.935  -27.629 1.000 31.988 ? 766 HOH A O   1 ? ?  
HETATM 3268 O  O   . HOH I 6 .   ? 14.332  21.487  -17.602 1.000 56.014 ? 767 HOH A O   1 ? ?  
HETATM 3269 O  O   . HOH I 6 .   ? -29.743 23.388  -33.602 1.000 44.795 ? 768 HOH A O   1 ? ?  
HETATM 3270 O  O   . HOH I 6 .   ? 14.709  3.506   -41.515 1.000 27.469 ? 769 HOH A O   1 ? ?  
HETATM 3271 O  O   . HOH I 6 .   ? -11.964 23.662  -22.788 1.000 27.987 ? 770 HOH A O   1 ? ?  
HETATM 3272 O  O   . HOH I 6 .   ? -18.182 20.461  -24.255 1.000 46.274 ? 771 HOH A O   1 ? ?  
HETATM 3273 O  O   . HOH I 6 .   ? 12.627  15.951  -22.417 1.000 52.153 ? 772 HOH A O   1 ? ?  
HETATM 3274 O  O   . HOH I 6 .   ? -25.856 15.040  -50.508 1.000 29.718 ? 773 HOH A O   1 ? ?  
HETATM 3275 O  O   . HOH I 6 .   ? 25.215  -9.976  -57.461 1.000 51.697 ? 774 HOH A O   1 ? ?  
HETATM 3276 O  O   . HOH I 6 .   ? 8.566   16.282  -14.225 1.000 57.468 ? 775 HOH A O   1 ? ?  
HETATM 3277 O  O   . HOH I 6 .   ? 2.138   33.335  -20.781 1.000 43.354 ? 776 HOH A O   1 ? ?  
HETATM 3278 O  O   . HOH I 6 .   ? -4.959  38.248  -32.903 1.000 33.272 ? 777 HOH A O   1 ? ?  
HETATM 3279 O  O   . HOH I 6 .   ? 15.194  7.282   -58.424 1.000 26.354 ? 778 HOH A O   1 ? ?  
HETATM 3280 O  O   . HOH I 6 .   ? -21.617 16.976  -54.444 1.000 37.464 ? 779 HOH A O   1 ? ?  
HETATM 3281 O  O   . HOH I 6 .   ? 6.337   33.217  -29.155 1.000 43.688 ? 780 HOH A O   1 ? ?  
HETATM 3282 O  O   . HOH I 6 .   ? 3.980   32.365  -22.910 1.000 43.793 ? 781 HOH A O   1 ? ?  
HETATM 3283 O  O   . HOH I 6 .   ? -6.687  35.828  -45.296 1.000 46.159 ? 782 HOH A O   1 ? ?  
HETATM 3284 O  O   . HOH I 6 .   ? 7.725   13.708  -16.651 1.000 55.163 ? 783 HOH A O   1 ? ?  
HETATM 3285 O  O   . HOH I 6 .   ? 28.889  -10.952 -44.921 1.000 54.200 ? 784 HOH A O   1 ? ?  
HETATM 3286 O  O   . HOH I 6 .   ? 11.655  3.611   -20.004 1.000 57.221 ? 785 HOH A O   1 ? ?  
HETATM 3287 O  O   . HOH I 6 .   ? -14.375 31.718  -63.602 1.000 47.067 ? 786 HOH A O   1 ? ?  
HETATM 3288 O  O   . HOH I 6 .   ? -13.775 8.866   -22.590 1.000 42.706 ? 787 HOH A O   1 ? ?  
HETATM 3289 O  O   . HOH I 6 .   ? -7.164  10.873  -17.110 1.000 31.244 ? 788 HOH A O   1 ? ?  
HETATM 3290 O  O   . HOH I 6 .   ? 28.002  -13.735 -40.425 1.000 59.249 ? 789 HOH A O   1 ? ?  
HETATM 3291 O  O   . HOH I 6 .   ? -4.588  21.955  -12.866 1.000 46.440 ? 790 HOH A O   1 ? ?  
HETATM 3292 O  O   . HOH I 6 .   ? -20.689 9.885   -27.091 1.000 36.547 ? 791 HOH A O   1 ? ?  
HETATM 3293 O  O   . HOH I 6 .   ? 13.060  24.969  -46.724 1.000 44.864 ? 792 HOH A O   1 ? ?  
HETATM 3294 O  O   . HOH I 6 .   ? -19.765 9.005   -37.897 1.000 39.183 ? 793 HOH A O   1 ? ?  
HETATM 3295 O  O   . HOH I 6 .   ? 21.363  -14.395 -58.908 1.000 50.562 ? 794 HOH A O   1 ? ?  
HETATM 3296 O  O   . HOH I 6 .   ? -2.297  30.519  -56.768 1.000 23.159 ? 795 HOH A O   1 ? ?  
HETATM 3297 O  O   . HOH I 6 .   ? -5.811  32.418  -29.797 1.000 43.649 ? 796 HOH A O   1 ? ?  
HETATM 3298 O  O   . HOH I 6 .   ? 18.700  10.320  -37.790 1.000 36.310 ? 797 HOH A O   1 ? ?  
HETATM 3299 O  O   . HOH I 6 .   ? 14.525  23.007  -37.549 1.000 55.791 ? 798 HOH A O   1 ? ?  
HETATM 3300 O  O   . HOH I 6 .   ? 18.877  22.729  -48.781 1.000 58.073 ? 799 HOH A O   1 ? ?  
HETATM 3301 O  O   . HOH I 6 .   ? -20.065 22.679  -28.547 1.000 49.487 ? 800 HOH A O   1 ? ?  
HETATM 3302 O  O   . HOH I 6 .   ? 20.798  12.583  -30.862 1.000 51.252 ? 801 HOH A O   1 ? ?  
HETATM 3303 O  O   . HOH I 6 .   ? 2.186   36.913  -31.808 1.000 54.191 ? 802 HOH A O   1 ? ?  
HETATM 3304 O  O   . HOH I 6 .   ? -9.031  30.423  -29.491 1.000 28.305 ? 803 HOH A O   1 ? ?  
HETATM 3305 O  O   . HOH I 6 .   ? -3.056  36.381  -31.502 1.000 40.934 ? 804 HOH A O   1 ? ?  
HETATM 3306 O  O   . HOH I 6 .   ? 13.627  21.028  -29.538 1.000 50.935 ? 805 HOH A O   1 ? ?  
HETATM 3307 O  O   . HOH I 6 .   ? -5.286  32.227  -57.587 1.000 45.882 ? 806 HOH A O   1 ? ?  
HETATM 3308 O  O   . HOH I 6 .   ? 17.716  16.437  -26.719 1.000 67.774 ? 807 HOH A O   1 ? ?  
HETATM 3309 O  O   . HOH I 6 .   ? 15.156  7.590   -23.142 1.000 40.776 ? 808 HOH A O   1 ? ?  
HETATM 3310 O  O   . HOH I 6 .   ? -0.074  35.086  -15.132 1.000 31.947 ? 809 HOH A O   1 ? ?  
HETATM 3311 O  O   . HOH I 6 .   ? 15.106  21.677  -34.790 1.000 45.613 ? 810 HOH A O   1 ? ?  
HETATM 3312 O  O   . HOH I 6 .   ? 14.384  0.482   -37.513 1.000 29.008 ? 811 HOH A O   1 ? ?  
HETATM 3313 O  O   . HOH I 6 .   ? -22.710 12.246  -26.317 1.000 38.959 ? 812 HOH A O   1 ? ?  
HETATM 3314 O  O   . HOH I 6 .   ? 20.754  8.269   -53.743 1.000 36.280 ? 813 HOH A O   1 ? ?  
HETATM 3315 O  O   . HOH I 6 .   ? -23.318 26.318  -58.556 1.000 41.038 ? 814 HOH A O   1 ? ?  
HETATM 3316 O  O   . HOH I 6 .   ? -32.989 27.980  -41.199 1.000 62.210 ? 815 HOH A O   1 ? ?  
HETATM 3317 O  O   . HOH I 6 .   ? -14.822 8.909   -36.936 1.000 35.555 ? 816 HOH A O   1 ? ?  
HETATM 3318 O  O   . HOH I 6 .   ? -9.672  38.731  -43.941 1.000 43.402 ? 817 HOH A O   1 ? ?  
HETATM 3319 O  O   . HOH I 6 .   ? 5.682   11.652  -11.195 1.000 57.717 ? 818 HOH A O   1 ? ?  
HETATM 3320 O  O   . HOH I 6 .   ? -17.668 7.910   -33.825 1.000 35.821 ? 819 HOH A O   1 ? ?  
HETATM 3321 O  O   . HOH I 6 .   ? -5.458  31.926  -60.302 1.000 40.152 ? 820 HOH A O   1 ? ?  
HETATM 3322 O  O   . HOH I 6 .   ? -10.386 3.580   -19.619 1.000 60.188 ? 821 HOH A O   1 ? ?  
HETATM 3323 O  O   . HOH I 6 .   ? -5.809  20.171  -16.482 1.000 37.974 ? 822 HOH A O   1 ? ?  
HETATM 3324 O  O   . HOH I 6 .   ? -9.039  36.221  -44.848 1.000 25.375 ? 823 HOH A O   1 ? ?  
HETATM 3325 O  O   . HOH I 6 .   ? -23.605 10.843  -35.053 1.000 52.986 ? 824 HOH A O   1 ? ?  
HETATM 3326 O  O   . HOH I 6 .   ? 0.776   3.278   -13.136 1.000 50.318 ? 825 HOH A O   1 ? ?  
HETATM 3327 O  O   . HOH I 6 .   ? 11.400  13.867  -22.740 1.000 46.142 ? 826 HOH A O   1 ? ?  
HETATM 3328 O  O   . HOH I 6 .   ? -24.254 14.845  -27.135 1.000 42.038 ? 827 HOH A O   1 ? ?  
HETATM 3329 O  O   . HOH I 6 .   ? -26.253 34.870  -52.030 1.000 57.167 ? 828 HOH A O   1 ? ?  
HETATM 3330 O  O   . HOH I 6 .   ? -5.322  22.452  -15.236 1.000 41.938 ? 829 HOH A O   1 ? ?  
HETATM 3331 O  O   . HOH I 6 .   ? -30.863 17.886  -44.315 1.000 45.477 ? 830 HOH A O   1 ? ?  
HETATM 3332 O  O   . HOH I 6 .   ? -3.053  19.743  -12.830 1.000 54.315 ? 831 HOH A O   1 ? ?  
HETATM 3333 O  O   . HOH I 6 .   ? -20.410 36.305  -40.456 1.000 46.622 ? 832 HOH A O   1 ? ?  
HETATM 3334 O  O   . HOH I 6 .   ? -34.113 20.493  -43.462 1.000 51.625 ? 833 HOH A O   1 ? ?  
HETATM 3335 O  O   . HOH I 6 .   ? -13.801 36.610  -37.107 1.000 40.645 ? 834 HOH A O   1 ? ?  
HETATM 3336 O  O   . HOH I 6 .   ? -17.238 28.339  -32.612 1.000 50.413 ? 835 HOH A O   1 ? ?  
HETATM 3337 O  O   . HOH I 6 .   ? -11.855 30.763  -29.358 1.000 38.904 ? 836 HOH A O   1 ? ?  
HETATM 3338 O  O   . HOH I 6 .   ? 18.930  -2.863  -64.656 1.000 37.113 ? 837 HOH A O   1 ? ?  
HETATM 3339 O  O   . HOH I 6 .   ? -11.937 34.200  -60.915 1.000 48.316 ? 838 HOH A O   1 ? ?  
HETATM 3340 O  O   . HOH I 6 .   ? -7.237  34.172  -20.041 1.000 51.409 ? 839 HOH A O   1 ? ?  
HETATM 3341 O  O   . HOH I 6 .   ? -14.438 24.278  -25.481 1.000 40.012 ? 840 HOH A O   1 ? ?  
HETATM 3342 O  O   . HOH I 6 .   ? -19.360 17.800  -60.662 1.000 57.409 ? 841 HOH A O   1 ? ?  
HETATM 3343 O  O   . HOH I 6 .   ? -5.827  25.056  -41.788 1.000 22.823 ? 842 HOH A O   1 ? ?  
HETATM 3344 O  O   . HOH I 6 .   ? 27.389  -4.047  -50.701 1.000 47.680 ? 843 HOH A O   1 ? ?  
HETATM 3345 O  O   . HOH I 6 .   ? 9.852   32.146  -48.625 1.000 64.250 ? 844 HOH A O   1 ? ?  
HETATM 3346 O  O   . HOH I 6 .   ? -13.012 25.758  -28.165 1.000 37.352 ? 845 HOH A O   1 ? ?  
HETATM 3347 O  O   . HOH I 6 .   ? 6.481   -2.662  -46.530 1.000 18.450 ? 846 HOH A O   1 ? ?  
HETATM 3348 O  O   . HOH I 6 .   ? 14.008  13.951  -27.161 1.000 47.410 ? 847 HOH A O   1 ? ?  
HETATM 3349 O  O   . HOH I 6 .   ? -1.271  37.243  -30.330 1.000 53.186 ? 848 HOH A O   1 ? ?  
HETATM 3350 O  O   . HOH I 6 .   ? 22.937  22.487  -56.810 1.000 46.281 ? 849 HOH A O   1 ? ?  
HETATM 3351 O  O   . HOH I 6 .   ? -23.427 15.437  -29.917 1.000 51.084 ? 850 HOH A O   1 ? ?  
HETATM 3352 O  O   . HOH I 6 .   ? 9.495   31.188  -53.437 1.000 43.197 ? 851 HOH A O   1 ? ?  
HETATM 3353 O  O   . HOH I 6 .   ? -14.191 38.513  -38.523 1.000 48.840 ? 852 HOH A O   1 ? ?  
HETATM 3354 O  O   . HOH I 6 .   ? -31.805 33.113  -40.012 1.000 51.219 ? 853 HOH A O   1 ? ?  
HETATM 3355 O  O   . HOH I 6 .   ? 10.320  31.886  -51.142 1.000 58.311 ? 854 HOH A O   1 ? ?  
HETATM 3356 O  O   . HOH I 6 .   ? 19.179  -5.807  -63.559 1.000 40.058 ? 855 HOH A O   1 ? ?  
HETATM 3357 O  O   . HOH I 6 .   ? 0.159   36.368  -43.496 1.000 50.748 ? 856 HOH A O   1 ? ?  
HETATM 3358 O  O   . HOH I 6 .   ? -8.107  31.724  -59.109 1.000 36.834 ? 857 HOH A O   1 ? ?  
HETATM 3359 O  O   . HOH I 6 .   ? -22.432 16.706  -22.322 1.000 42.379 ? 858 HOH A O   1 ? ?  
HETATM 3360 O  O   . HOH I 6 .   ? -12.153 38.595  -46.084 1.000 47.127 ? 859 HOH A O   1 ? ?  
HETATM 3361 O  O   . HOH I 6 .   ? 1.125   33.262  -54.366 1.000 66.398 ? 860 HOH A O   1 ? ?  
HETATM 3362 O  O   . HOH I 6 .   ? -1.993  1.268   -15.328 1.000 39.614 ? 861 HOH A O   1 ? ?  
HETATM 3363 O  O   . HOH I 6 .   ? -14.587 29.216  -32.413 1.000 34.597 ? 862 HOH A O   1 ? ?  
HETATM 3364 O  O   . HOH I 6 .   ? 6.991   19.837  -13.969 1.000 58.583 ? 863 HOH A O   1 ? ?  
HETATM 3365 O  O   . HOH I 6 .   ? 30.398  -14.378 -47.044 1.000 54.655 ? 864 HOH A O   1 ? ?  
HETATM 3366 O  O   . HOH I 6 .   ? -11.135 14.152  -18.172 1.000 53.712 ? 865 HOH A O   1 ? ?  
HETATM 3367 O  O   . HOH I 6 .   ? -10.058 35.444  -57.274 1.000 47.728 ? 866 HOH A O   1 ? ?  
HETATM 3368 O  O   . HOH I 6 .   ? -30.030 29.561  -55.479 1.000 55.490 ? 867 HOH A O   1 ? ?  
HETATM 3369 O  O   . HOH I 6 .   ? -8.117  32.395  -27.801 1.000 34.176 ? 868 HOH A O   1 ? ?  
HETATM 3370 O  O   . HOH I 6 .   ? -18.155 7.541   -24.370 1.000 35.155 ? 869 HOH A O   1 ? ?  
HETATM 3371 O  O   . HOH I 6 .   ? -32.478 18.414  -39.366 1.000 42.071 ? 870 HOH A O   1 ? ?  
HETATM 3372 O  O   . HOH I 6 .   ? -31.341 18.228  -46.753 1.000 44.456 ? 871 HOH A O   1 ? ?  
HETATM 3373 O  O   . HOH I 6 .   ? 16.194  18.538  -30.031 1.000 47.290 ? 872 HOH A O   1 ? ?  
HETATM 3374 O  O   . HOH I 6 .   ? -17.229 24.053  -25.964 1.000 37.463 ? 873 HOH A O   1 ? ?  
HETATM 3375 O  O   . HOH I 6 .   ? 23.607  -1.426  -42.597 1.000 53.677 ? 874 HOH A O   1 ? ?  
HETATM 3376 O  O   . HOH I 6 .   ? 11.401  34.233  -23.530 1.000 54.944 ? 875 HOH A O   1 ? ?  
HETATM 3377 O  O   . HOH I 6 .   ? -0.989  38.630  -43.270 1.000 46.859 ? 876 HOH A O   1 ? ?  
HETATM 3378 O  O   . HOH I 6 .   ? -9.473  33.888  -60.004 1.000 42.022 ? 877 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   . TYR A 3   ? 0.637 0.922 0.904 -0.169 -0.139 0.005  3   TYR A N   
2    C CA  . TYR A 3   ? 0.643 0.809 0.776 -0.175 -0.139 -0.004 3   TYR A CA  
3    C C   . TYR A 3   ? 0.612 0.731 0.710 -0.140 -0.093 -0.012 3   TYR A C   
4    O O   . TYR A 3   ? 0.682 0.735 0.712 -0.154 -0.070 -0.020 3   TYR A O   
5    C CB  . TYR A 3   ? 0.731 0.846 0.799 -0.234 -0.144 -0.010 3   TYR A CB  
6    N N   . GLU A 4   ? 0.528 0.668 0.657 -0.096 -0.084 -0.008 4   GLU A N   
7    C CA  . GLU A 4   ? 0.440 0.537 0.535 -0.069 -0.051 -0.014 4   GLU A CA  
8    C C   . GLU A 4   ? 0.419 0.441 0.433 -0.063 -0.058 -0.018 4   GLU A C   
9    O O   . GLU A 4   ? 0.445 0.448 0.434 -0.061 -0.080 -0.016 4   GLU A O   
10   C CB  . GLU A 4   ? 0.459 0.587 0.597 -0.031 -0.042 -0.009 4   GLU A CB  
11   C CG  . GLU A 4   ? 0.539 0.727 0.752 -0.027 -0.014 -0.006 4   GLU A CG  
12   C CD  . GLU A 4   ? 0.584 0.760 0.801 0.011  0.015  -0.004 4   GLU A CD  
13   O OE1 . GLU A 4   ? 0.585 0.727 0.765 0.035  0.001  -0.002 4   GLU A OE1 
14   O OE2 . GLU A 4   ? 0.606 0.795 0.853 0.013  0.059  -0.005 4   GLU A OE2 
15   N N   . GLY A 5   ? 0.355 0.333 0.331 -0.056 -0.038 -0.023 5   GLY A N   
16   C CA  . GLY A 5   ? 0.360 0.283 0.283 -0.044 -0.038 -0.024 5   GLY A CA  
17   C C   . GLY A 5   ? 0.325 0.256 0.263 -0.018 -0.039 -0.022 5   GLY A C   
18   O O   . GLY A 5   ? 0.284 0.246 0.254 -0.007 -0.039 -0.020 5   GLY A O   
19   N N   . PHE A 6   ? 0.335 0.234 0.246 -0.009 -0.036 -0.023 6   PHE A N   
20   C CA  . PHE A 6   ? 0.310 0.214 0.235 0.008  -0.033 -0.022 6   PHE A CA  
21   C C   . PHE A 6   ? 0.274 0.200 0.225 0.016  -0.033 -0.021 6   PHE A C   
22   O O   . PHE A 6   ? 0.278 0.215 0.239 0.020  -0.034 -0.020 6   PHE A O   
23   C CB  . PHE A 6   ? 0.331 0.203 0.237 0.017  -0.018 -0.022 6   PHE A CB  
24   C CG  . PHE A 6   ? 0.323 0.205 0.249 0.025  -0.007 -0.022 6   PHE A CG  
25   C CD1 . PHE A 6   ? 0.302 0.218 0.272 0.032  -0.007 -0.020 6   PHE A CD1 
26   C CD2 . PHE A 6   ? 0.366 0.214 0.256 0.019  0.003  -0.024 6   PHE A CD2 
27   C CE1 . PHE A 6   ? 0.306 0.232 0.296 0.029  0.005  -0.020 6   PHE A CE1 
28   C CE2 . PHE A 6   ? 0.368 0.213 0.266 0.021  0.020  -0.025 6   PHE A CE2 
29   C CZ  . PHE A 6   ? 0.336 0.225 0.289 0.024  0.023  -0.024 6   PHE A CZ  
30   N N   . GLU A 7   ? 0.295 0.210 0.240 0.018  -0.035 -0.020 7   GLU A N   
31   C CA  . GLU A 7   ? 0.294 0.210 0.243 0.021  -0.043 -0.018 7   GLU A CA  
32   C C   . GLU A 7   ? 0.294 0.208 0.233 0.016  -0.035 -0.020 7   GLU A C   
33   O O   . GLU A 7   ? 0.296 0.199 0.225 0.015  -0.037 -0.019 7   GLU A O   
34   C CB  . GLU A 7   ? 0.338 0.226 0.266 0.026  -0.053 -0.014 7   GLU A CB  
35   C CG  . GLU A 7   ? 0.351 0.245 0.300 0.043  -0.056 -0.010 7   GLU A CG  
36   C CD  . GLU A 7   ? 0.387 0.248 0.306 0.047  -0.040 -0.012 7   GLU A CD  
37   O OE1 . GLU A 7   ? 0.429 0.279 0.354 0.069  -0.036 -0.007 7   GLU A OE1 
38   O OE2 . GLU A 7   ? 0.401 0.246 0.289 0.028  -0.031 -0.017 7   GLU A OE2 
39   N N   . THR A 8   ? 0.282 0.203 0.223 0.010  -0.024 -0.021 8   THR A N   
40   C CA  . THR A 8   ? 0.286 0.217 0.239 0.012  -0.008 -0.021 8   THR A CA  
41   C C   . THR A 8   ? 0.267 0.219 0.241 0.026  -0.012 -0.018 8   THR A C   
42   O O   . THR A 8   ? 0.284 0.217 0.244 0.037  -0.000 -0.017 8   THR A O   
43   C CB  . THR A 8   ? 0.287 0.243 0.264 -0.001 0.005  -0.022 8   THR A CB  
44   O OG1 . THR A 8   ? 0.312 0.226 0.246 -0.016 0.009  -0.025 8   THR A OG1 
45   C CG2 . THR A 8   ? 0.290 0.267 0.297 0.007  0.031  -0.021 8   THR A CG2 
46   N N   . LEU A 9   ? 0.258 0.234 0.203 -0.031 -0.015 -0.005 9   LEU A N   
47   C CA  . LEU A 9   ? 0.248 0.229 0.193 -0.027 -0.017 -0.007 9   LEU A CA  
48   C C   . LEU A 9   ? 0.250 0.236 0.197 -0.022 -0.007 -0.007 9   LEU A C   
49   O O   . LEU A 9   ? 0.255 0.245 0.205 -0.021 -0.006 -0.006 9   LEU A O   
50   C CB  . LEU A 9   ? 0.284 0.238 0.202 -0.023 -0.026 -0.011 9   LEU A CB  
51   C CG  . LEU A 9   ? 0.307 0.254 0.233 -0.030 -0.047 -0.015 9   LEU A CG  
52   C CD1 . LEU A 9   ? 0.372 0.276 0.252 -0.021 -0.061 -0.021 9   LEU A CD1 
53   C CD2 . LEU A 9   ? 0.320 0.289 0.277 -0.032 -0.058 -0.016 9   LEU A CD2 
54   N N   . ALA A 10  ? 0.246 0.230 0.196 -0.018 -0.002 -0.008 10  ALA A N   
55   C CA  . ALA A 10  ? 0.244 0.238 0.216 -0.016 0.005  -0.008 10  ALA A CA  
56   C C   . ALA A 10  ? 0.248 0.250 0.231 -0.019 -0.004 -0.010 10  ALA A C   
57   O O   . ALA A 10  ? 0.259 0.266 0.262 -0.021 -0.002 -0.012 10  ALA A O   
58   C CB  . ALA A 10  ? 0.229 0.227 0.219 -0.010 0.008  -0.011 10  ALA A CB  
59   N N   . ILE A 11  ? 0.240 0.239 0.209 -0.018 -0.011 -0.011 11  ILE A N   
60   C CA  . ILE A 11  ? 0.244 0.237 0.205 -0.014 -0.018 -0.014 11  ILE A CA  
61   C C   . ILE A 11  ? 0.254 0.249 0.209 -0.015 -0.011 -0.011 11  ILE A C   
62   O O   . ILE A 11  ? 0.276 0.263 0.223 -0.010 -0.014 -0.014 11  ILE A O   
63   C CB  . ILE A 11  ? 0.264 0.238 0.198 -0.007 -0.024 -0.014 11  ILE A CB  
64   C CG1 . ILE A 11  ? 0.271 0.245 0.220 -0.001 -0.040 -0.020 11  ILE A CG1 
65   C CG2 . ILE A 11  ? 0.301 0.254 0.204 0.002  -0.026 -0.015 11  ILE A CG2 
66   C CD1 . ILE A 11  ? 0.304 0.252 0.219 0.009  -0.047 -0.019 11  ILE A CD1 
67   N N   . HIS A 12  ? 0.233 0.237 0.192 -0.018 -0.005 -0.006 12  HIS A N   
68   C CA  . HIS A 12  ? 0.246 0.260 0.213 -0.015 0.001  -0.004 12  HIS A CA  
69   C C   . HIS A 12  ? 0.254 0.272 0.229 -0.014 -0.006 -0.005 12  HIS A C   
70   O O   . HIS A 12  ? 0.255 0.279 0.238 -0.007 -0.006 -0.006 12  HIS A O   
71   C CB  . HIS A 12  ? 0.255 0.276 0.234 -0.019 0.011  0.001  12  HIS A CB  
72   C CG  . HIS A 12  ? 0.286 0.286 0.237 -0.014 0.022  0.004  12  HIS A CG  
73   N ND1 . HIS A 12  ? 0.329 0.316 0.258 -0.002 0.034  0.005  12  HIS A ND1 
74   C CD2 . HIS A 12  ? 0.271 0.252 0.201 -0.016 0.021  0.006  12  HIS A CD2 
75   C CE1 . HIS A 12  ? 0.361 0.315 0.248 0.005  0.040  0.008  12  HIS A CE1 
76   N NE2 . HIS A 12  ? 0.311 0.263 0.201 -0.004 0.032  0.009  12  HIS A NE2 
77   N N   . ALA A 13  ? 0.239 0.248 0.206 -0.017 -0.012 -0.006 13  ALA A N   
78   C CA  . ALA A 13  ? 0.251 0.248 0.208 -0.011 -0.022 -0.007 13  ALA A CA  
79   C C   . ALA A 13  ? 0.267 0.250 0.209 -0.005 -0.017 -0.005 13  ALA A C   
80   O O   . ALA A 13  ? 0.280 0.254 0.218 -0.010 -0.006 -0.004 13  ALA A O   
81   C CB  . ALA A 13  ? 0.282 0.256 0.213 -0.011 -0.027 -0.008 13  ALA A CB  
82   N N   . GLY A 14  ? 0.277 0.258 0.218 0.004  -0.026 -0.007 14  GLY A N   
83   C CA  . GLY A 14  ? 0.308 0.266 0.228 0.011  -0.023 -0.005 14  GLY A CA  
84   C C   . GLY A 14  ? 0.284 0.250 0.216 0.010  -0.016 -0.007 14  GLY A C   
85   O O   . GLY A 14  ? 0.317 0.259 0.233 0.014  -0.014 -0.007 14  GLY A O   
86   N N   . GLN A 15  ? 0.254 0.242 0.204 0.007  -0.012 -0.008 15  GLN A N   
87   C CA  . GLN A 15  ? 0.269 0.249 0.211 0.008  -0.008 -0.012 15  GLN A CA  
88   C C   . GLN A 15  ? 0.274 0.265 0.219 0.018  0.002  -0.011 15  GLN A C   
89   O O   . GLN A 15  ? 0.300 0.279 0.226 0.021  0.006  -0.013 15  GLN A O   
90   C CB  . GLN A 15  ? 0.278 0.257 0.224 -0.003 -0.010 -0.013 15  GLN A CB  
91   C CG  . GLN A 15  ? 0.272 0.241 0.226 -0.012 -0.009 -0.011 15  GLN A CG  
92   C CD  . GLN A 15  ? 0.271 0.250 0.244 -0.020 -0.010 -0.013 15  GLN A CD  
93   O OE1 . GLN A 15  ? 0.297 0.271 0.283 -0.022 -0.021 -0.019 15  GLN A OE1 
94   N NE2 . GLN A 15  ? 0.257 0.246 0.234 -0.022 -0.003 -0.009 15  GLN A NE2 
95   N N   . GLU A 16  ? 0.277 0.285 0.241 0.028  0.005  -0.010 16  GLU A N   
96   C CA  . GLU A 16  ? 0.306 0.324 0.280 0.042  0.023  -0.008 16  GLU A CA  
97   C C   . GLU A 16  ? 0.330 0.311 0.258 0.056  0.027  -0.013 16  GLU A C   
98   O O   . GLU A 16  ? 0.326 0.282 0.232 0.058  0.012  -0.018 16  GLU A O   
99   C CB  . GLU A 16  ? 0.337 0.385 0.355 0.051  0.021  -0.008 16  GLU A CB  
100  C CG  . GLU A 16  ? 0.450 0.518 0.497 0.064  0.051  -0.004 16  GLU A CG  
101  C CD  . GLU A 16  ? 0.519 0.632 0.638 0.073  0.053  -0.003 16  GLU A CD  
102  O OE1 . GLU A 16  ? 0.574 0.698 0.717 0.074  0.022  -0.009 16  GLU A OE1 
103  O OE2 . GLU A 16  ? 0.530 0.661 0.681 0.084  0.088  0.002  16  GLU A OE2 
104  N N   . ALA A 17  ? 0.277 0.298 0.212 -0.058 -0.002 -0.020 17  ALA A N   
105  C CA  . ALA A 17  ? 0.256 0.282 0.207 -0.039 -0.010 -0.015 17  ALA A CA  
106  C C   . ALA A 17  ? 0.241 0.287 0.199 -0.034 -0.019 -0.008 17  ALA A C   
107  O O   . ALA A 17  ? 0.250 0.319 0.207 -0.042 -0.023 -0.002 17  ALA A O   
108  C CB  . ALA A 17  ? 0.276 0.306 0.233 -0.035 -0.010 -0.014 17  ALA A CB  
109  N N   . ASP A 18  ? 0.240 0.280 0.206 -0.022 -0.021 -0.006 18  ASP A N   
110  C CA  . ASP A 18  ? 0.241 0.293 0.218 -0.014 -0.023 0.001  18  ASP A CA  
111  C C   . ASP A 18  ? 0.225 0.297 0.212 -0.011 -0.023 0.009  18  ASP A C   
112  O O   . ASP A 18  ? 0.230 0.299 0.218 -0.009 -0.020 0.005  18  ASP A O   
113  C CB  . ASP A 18  ? 0.231 0.267 0.211 -0.005 -0.020 -0.002 18  ASP A CB  
114  C CG  . ASP A 18  ? 0.249 0.286 0.240 0.004  -0.016 0.006  18  ASP A CG  
115  O OD1 . ASP A 18  ? 0.261 0.309 0.256 0.004  -0.019 0.014  18  ASP A OD1 
116  O OD2 . ASP A 18  ? 0.247 0.274 0.241 0.010  -0.007 0.003  18  ASP A OD2 
117  N N   . ALA A 19  ? 0.227 0.322 0.225 -0.010 -0.026 0.023  19  ALA A N   
118  C CA  . ALA A 19  ? 0.239 0.362 0.254 -0.006 -0.025 0.037  19  ALA A CA  
119  C C   . ALA A 19  ? 0.235 0.342 0.264 0.010  -0.012 0.037  19  ALA A C   
120  O O   . ALA A 19  ? 0.256 0.369 0.289 0.012  -0.009 0.036  19  ALA A O   
121  C CB  . ALA A 19  ? 0.249 0.407 0.278 -0.008 -0.029 0.059  19  ALA A CB  
122  N N   . GLU A 20  ? 0.237 0.323 0.270 0.020  -0.003 0.035  20  GLU A N   
123  C CA  . GLU A 20  ? 0.247 0.314 0.290 0.032  0.015  0.034  20  GLU A CA  
124  C C   . GLU A 20  ? 0.243 0.287 0.267 0.024  0.017  0.014  20  GLU A C   
125  O O   . GLU A 20  ? 0.263 0.300 0.291 0.027  0.031  0.011  20  GLU A O   
126  C CB  . GLU A 20  ? 0.272 0.321 0.324 0.041  0.028  0.039  20  GLU A CB  
127  C CG  . GLU A 20  ? 0.326 0.348 0.387 0.051  0.055  0.036  20  GLU A CG  
128  C CD  . GLU A 20  ? 0.396 0.395 0.472 0.063  0.079  0.044  20  GLU A CD  
129  O OE1 . GLU A 20  ? 0.533 0.519 0.629 0.075  0.106  0.052  20  GLU A OE1 
130  O OE2 . GLU A 20  ? 0.407 0.403 0.480 0.062  0.073  0.045  20  GLU A OE2 
131  N N   . THR A 21  ? 0.242 0.276 0.247 0.014  0.008  0.002  21  THR A N   
132  C CA  . THR A 21  ? 0.239 0.257 0.227 0.005  0.010  -0.012 21  THR A CA  
133  C C   . THR A 21  ? 0.241 0.270 0.221 -0.003 -0.002 -0.014 21  THR A C   
134  O O   . THR A 21  ? 0.246 0.272 0.217 -0.011 -0.001 -0.021 21  THR A O   
135  C CB  . THR A 21  ? 0.250 0.252 0.226 -0.001 0.011  -0.019 21  THR A CB  
136  O OG1 . THR A 21  ? 0.235 0.244 0.209 -0.002 -0.002 -0.015 21  THR A OG1 
137  C CG2 . THR A 21  ? 0.282 0.267 0.263 0.006  0.026  -0.018 21  THR A CG2 
138  N N   . GLY A 22  ? 0.230 0.271 0.214 -0.004 -0.010 -0.009 22  GLY A N   
139  C CA  . GLY A 22  ? 0.229 0.273 0.207 -0.011 -0.015 -0.011 22  GLY A CA  
140  C C   . GLY A 22  ? 0.233 0.266 0.205 -0.013 -0.017 -0.012 22  GLY A C   
141  O O   . GLY A 22  ? 0.232 0.265 0.204 -0.017 -0.016 -0.010 22  GLY A O   
142  N N   . ALA A 23  ? 0.228 0.254 0.199 -0.012 -0.016 -0.012 23  ALA A N   
143  C CA  . ALA A 23  ? 0.231 0.253 0.201 -0.014 -0.018 -0.009 23  ALA A CA  
144  C C   . ALA A 23  ? 0.229 0.247 0.202 -0.015 -0.015 -0.006 23  ALA A C   
145  O O   . ALA A 23  ? 0.243 0.258 0.213 -0.016 -0.014 -0.008 23  ALA A O   
146  C CB  . ALA A 23  ? 0.237 0.251 0.205 -0.012 -0.018 -0.010 23  ALA A CB  
147  N N   . VAL A 24  ? 0.218 0.238 0.196 -0.015 -0.012 0.001  24  VAL A N   
148  C CA  . VAL A 24  ? 0.237 0.246 0.219 -0.016 -0.001 0.003  24  VAL A CA  
149  C C   . VAL A 24  ? 0.247 0.242 0.229 -0.015 0.005  0.005  24  VAL A C   
150  O O   . VAL A 24  ? 0.255 0.234 0.233 -0.019 0.017  0.001  24  VAL A O   
151  C CB  . VAL A 24  ? 0.236 0.249 0.229 -0.015 0.006  0.014  24  VAL A CB  
152  C CG1 . VAL A 24  ? 0.238 0.263 0.228 -0.018 0.000  0.011  24  VAL A CG1 
153  C CG2 . VAL A 24  ? 0.266 0.291 0.274 -0.011 0.006  0.032  24  VAL A CG2 
154  N N   . VAL A 25  ? 0.224 0.223 0.208 -0.012 -0.001 0.009  25  VAL A N   
155  C CA  . VAL A 25  ? 0.234 0.222 0.220 -0.010 0.004  0.010  25  VAL A CA  
156  C C   . VAL A 25  ? 0.235 0.223 0.210 -0.012 -0.005 0.001  25  VAL A C   
157  O O   . VAL A 25  ? 0.234 0.231 0.206 -0.011 -0.013 -0.001 25  VAL A O   
158  C CB  . VAL A 25  ? 0.227 0.226 0.227 -0.006 0.004  0.025  25  VAL A CB  
159  C CG1 . VAL A 25  ? 0.239 0.228 0.241 -0.004 0.009  0.027  25  VAL A CG1 
160  C CG2 . VAL A 25  ? 0.255 0.260 0.273 -0.002 0.015  0.042  25  VAL A CG2 
161  N N   A VAL A 26  ? 0.239 0.215 0.207 -0.016 0.000  -0.004 26  VAL A N   
162  N N   B VAL A 26  ? 0.251 0.227 0.219 -0.016 0.000  -0.004 26  VAL A N   
163  C CA  A VAL A 26  ? 0.235 0.215 0.196 -0.018 -0.008 -0.008 26  VAL A CA  
164  C CA  B VAL A 26  ? 0.258 0.239 0.219 -0.018 -0.008 -0.008 26  VAL A CA  
165  C C   A VAL A 26  ? 0.222 0.205 0.188 -0.011 -0.014 -0.004 26  VAL A C   
166  C C   B VAL A 26  ? 0.233 0.215 0.198 -0.011 -0.014 -0.005 26  VAL A C   
167  O O   A VAL A 26  ? 0.221 0.201 0.192 -0.009 -0.011 0.001  26  VAL A O   
168  O O   B VAL A 26  ? 0.228 0.206 0.198 -0.009 -0.011 0.000  26  VAL A O   
169  C CB  A VAL A 26  ? 0.236 0.205 0.187 -0.026 -0.001 -0.012 26  VAL A CB  
170  C CB  B VAL A 26  ? 0.280 0.253 0.231 -0.027 -0.003 -0.012 26  VAL A CB  
171  C CG1 A VAL A 26  ? 0.216 0.198 0.163 -0.029 -0.011 -0.011 26  VAL A CG1 
172  C CG1 B VAL A 26  ? 0.316 0.285 0.256 -0.041 0.006  -0.018 26  VAL A CG1 
173  C CG2 A VAL A 26  ? 0.275 0.233 0.215 -0.040 0.012  -0.018 26  VAL A CG2 
174  C CG2 B VAL A 26  ? 0.308 0.265 0.262 -0.025 0.006  -0.010 26  VAL A CG2 
175  N N   . PRO A 27  ? 0.216 0.204 0.180 -0.008 -0.020 -0.006 27  PRO A N   
176  C CA  . PRO A 27  ? 0.229 0.214 0.193 -0.006 -0.021 -0.006 27  PRO A CA  
177  C C   . PRO A 27  ? 0.221 0.200 0.184 -0.006 -0.021 -0.004 27  PRO A C   
178  O O   . PRO A 27  ? 0.237 0.215 0.197 -0.008 -0.021 -0.005 27  PRO A O   
179  C CB  . PRO A 27  ? 0.251 0.237 0.216 -0.002 -0.019 -0.007 27  PRO A CB  
180  C CG  . PRO A 27  ? 0.249 0.245 0.218 -0.002 -0.020 -0.006 27  PRO A CG  
181  C CD  . PRO A 27  ? 0.243 0.241 0.209 -0.008 -0.021 -0.006 27  PRO A CD  
182  N N   . ILE A 28  ? 0.226 0.201 0.186 -0.007 -0.022 -0.004 28  ILE A N   
183  C CA  . ILE A 28  ? 0.218 0.187 0.177 -0.006 -0.023 -0.003 28  ILE A CA  
184  C C   . ILE A 28  ? 0.225 0.188 0.182 -0.003 -0.022 -0.005 28  ILE A C   
185  O O   . ILE A 28  ? 0.232 0.189 0.185 -0.004 -0.017 -0.008 28  ILE A O   
186  C CB  . ILE A 28  ? 0.220 0.192 0.179 -0.010 -0.023 0.002  28  ILE A CB  
187  C CG1 . ILE A 28  ? 0.236 0.219 0.205 -0.010 -0.021 0.011  28  ILE A CG1 
188  C CG2 . ILE A 28  ? 0.242 0.207 0.199 -0.009 -0.023 0.003  28  ILE A CG2 
189  C CD1 . ILE A 28  ? 0.243 0.243 0.215 -0.017 -0.024 0.023  28  ILE A CD1 
190  N N   . TYR A 29  ? 0.219 0.186 0.179 -0.001 -0.023 -0.001 29  TYR A N   
191  C CA  . TYR A 29  ? 0.217 0.184 0.183 0.005  -0.021 0.004  29  TYR A CA  
192  C C   . TYR A 29  ? 0.234 0.192 0.197 0.005  -0.020 0.004  29  TYR A C   
193  O O   . TYR A 29  ? 0.230 0.193 0.194 0.004  -0.024 0.010  29  TYR A O   
194  C CB  . TYR A 29  ? 0.220 0.208 0.194 0.005  -0.024 0.014  29  TYR A CB  
195  C CG  . TYR A 29  ? 0.225 0.224 0.204 0.006  -0.024 0.016  29  TYR A CG  
196  C CD1 . TYR A 29  ? 0.248 0.250 0.219 -0.002 -0.027 0.010  29  TYR A CD1 
197  C CD2 . TYR A 29  ? 0.249 0.253 0.243 0.016  -0.017 0.025  29  TYR A CD2 
198  C CE1 . TYR A 29  ? 0.250 0.263 0.225 -0.003 -0.027 0.011  29  TYR A CE1 
199  C CE2 . TYR A 29  ? 0.244 0.260 0.243 0.016  -0.016 0.027  29  TYR A CE2 
200  C CZ  . TYR A 29  ? 0.254 0.275 0.242 0.006  -0.023 0.019  29  TYR A CZ  
201  O OH  . TYR A 29  ? 0.281 0.314 0.272 0.005  -0.023 0.020  29  TYR A OH  
202  N N   . GLN A 30  ? 0.206 0.203 0.164 0.003  0.003  -0.009 30  GLN A N   
203  C CA  . GLN A 30  ? 0.220 0.207 0.193 0.002  -0.004 -0.013 30  GLN A CA  
204  C C   . GLN A 30  ? 0.218 0.203 0.197 0.005  -0.010 -0.020 30  GLN A C   
205  O O   . GLN A 30  ? 0.224 0.210 0.206 0.013  -0.023 -0.032 30  GLN A O   
206  C CB  . GLN A 30  ? 0.242 0.229 0.220 0.006  -0.014 -0.016 30  GLN A CB  
207  C CG  . GLN A 30  ? 0.247 0.224 0.255 0.003  -0.022 -0.013 30  GLN A CG  
208  C CD  . GLN A 30  ? 0.246 0.220 0.263 -0.003 -0.008 0.002  30  GLN A CD  
209  O OE1 . GLN A 30  ? 0.264 0.239 0.271 -0.004 -0.001 0.006  30  GLN A OE1 
210  N NE2 . GLN A 30  ? 0.242 0.214 0.282 -0.003 -0.004 0.012  30  GLN A NE2 
211  N N   . THR A 31  ? 0.209 0.193 0.188 0.002  -0.003 -0.016 31  THR A N   
212  C CA  . THR A 31  ? 0.225 0.209 0.210 0.004  -0.007 -0.019 31  THR A CA  
213  C C   . THR A 31  ? 0.212 0.194 0.205 0.001  0.000  -0.007 31  THR A C   
214  O O   . THR A 31  ? 0.226 0.207 0.205 0.000  0.008  -0.002 31  THR A O   
215  C CB  . THR A 31  ? 0.226 0.221 0.196 0.007  -0.004 -0.024 31  THR A CB  
216  O OG1 . THR A 31  ? 0.235 0.229 0.213 0.011  -0.010 -0.030 31  THR A OG1 
217  C CG2 . THR A 31  ? 0.230 0.226 0.192 0.001  0.004  -0.017 31  THR A CG2 
218  N N   . SER A 32  ? 0.196 0.177 0.209 0.003  -0.004 -0.003 32  SER A N   
219  C CA  . SER A 32  ? 0.201 0.185 0.215 0.005  0.005  0.012  32  SER A CA  
220  C C   . SER A 32  ? 0.219 0.208 0.216 0.006  0.005  0.007  32  SER A C   
221  O O   . SER A 32  ? 0.233 0.226 0.214 0.011  0.011  0.014  32  SER A O   
222  C CB  . SER A 32  ? 0.207 0.193 0.261 0.006  0.002  0.027  32  SER A CB  
223  O OG  . SER A 32  ? 0.202 0.184 0.278 0.006  -0.011 0.020  32  SER A OG  
224  N N   . THR A 33  ? 0.217 0.205 0.216 0.005  -0.002 -0.005 33  THR A N   
225  C CA  . THR A 33  ? 0.214 0.208 0.208 0.007  -0.003 -0.006 33  THR A CA  
226  C C   . THR A 33  ? 0.222 0.221 0.209 0.007  -0.005 -0.017 33  THR A C   
227  O O   . THR A 33  ? 0.223 0.224 0.205 0.009  -0.005 -0.024 33  THR A O   
228  C CB  . THR A 33  ? 0.227 0.221 0.248 0.010  -0.007 0.003  33  THR A CB  
229  O OG1 . THR A 33  ? 0.233 0.232 0.246 0.012  -0.007 0.006  33  THR A OG1 
230  C CG2 . THR A 33  ? 0.223 0.210 0.269 0.012  -0.019 -0.008 33  THR A CG2 
231  N N   . TYR A 34  ? 0.220 0.225 0.207 0.008  -0.006 -0.017 34  TYR A N   
232  C CA  . TYR A 34  ? 0.213 0.229 0.198 0.008  -0.004 -0.020 34  TYR A CA  
233  C C   . TYR A 34  ? 0.223 0.245 0.220 0.013  -0.007 -0.021 34  TYR A C   
234  O O   . TYR A 34  ? 0.226 0.245 0.228 0.011  -0.011 -0.016 34  TYR A O   
235  C CB  . TYR A 34  ? 0.225 0.242 0.207 0.002  -0.004 -0.016 34  TYR A CB  
236  C CG  . TYR A 34  ? 0.211 0.220 0.183 -0.001 -0.003 -0.015 34  TYR A CG  
237  C CD1 . TYR A 34  ? 0.233 0.231 0.194 0.001  -0.003 -0.015 34  TYR A CD1 
238  C CD2 . TYR A 34  ? 0.203 0.217 0.178 -0.003 0.001  -0.013 34  TYR A CD2 
239  C CE1 . TYR A 34  ? 0.237 0.229 0.190 -0.000 -0.001 -0.015 34  TYR A CE1 
240  C CE2 . TYR A 34  ? 0.217 0.222 0.186 -0.006 0.002  -0.012 34  TYR A CE2 
241  C CZ  . TYR A 34  ? 0.227 0.221 0.186 -0.005 0.001  -0.015 34  TYR A CZ  
242  O OH  . TYR A 34  ? 0.236 0.222 0.190 -0.005 0.003  -0.014 34  TYR A OH  
243  N N   . ARG A 35  ? 0.218 0.252 0.218 0.021  -0.005 -0.027 35  ARG A N   
244  C CA  . ARG A 35  ? 0.218 0.261 0.232 0.028  -0.007 -0.029 35  ARG A CA  
245  C C   . ARG A 35  ? 0.227 0.279 0.250 0.022  -0.006 -0.018 35  ARG A C   
246  O O   . ARG A 35  ? 0.213 0.273 0.238 0.017  -0.002 -0.010 35  ARG A O   
247  C CB  . ARG A 35  ? 0.245 0.304 0.254 0.045  -0.002 -0.037 35  ARG A CB  
248  C CG  . ARG A 35  ? 0.268 0.338 0.290 0.056  -0.002 -0.039 35  ARG A CG  
249  C CD  . ARG A 35  ? 0.312 0.402 0.321 0.079  0.005  -0.049 35  ARG A CD  
250  N NE  . ARG A 35  ? 0.380 0.486 0.401 0.092  0.009  -0.048 35  ARG A NE  
251  C CZ  . ARG A 35  ? 0.416 0.546 0.425 0.119  0.018  -0.054 35  ARG A CZ  
252  N NH1 . ARG A 35  ? 0.459 0.607 0.482 0.132  0.024  -0.051 35  ARG A NH1 
253  N NH2 . ARG A 35  ? 0.428 0.563 0.408 0.136  0.019  -0.066 35  ARG A NH2 
254  N N   . GLN A 36  ? 0.212 0.263 0.247 0.021  -0.012 -0.016 36  GLN A N   
255  C CA  . GLN A 36  ? 0.217 0.276 0.265 0.017  -0.016 -0.008 36  GLN A CA  
256  C C   . GLN A 36  ? 0.215 0.290 0.283 0.025  -0.012 -0.006 36  GLN A C   
257  O O   . GLN A 36  ? 0.220 0.294 0.290 0.036  -0.012 -0.014 36  GLN A O   
258  C CB  . GLN A 36  ? 0.225 0.272 0.267 0.014  -0.026 -0.005 36  GLN A CB  
259  C CG  . GLN A 36  ? 0.226 0.261 0.246 0.011  -0.027 -0.006 36  GLN A CG  
260  C CD  . GLN A 36  ? 0.237 0.268 0.244 0.015  -0.034 -0.000 36  GLN A CD  
261  O OE1 . GLN A 36  ? 0.267 0.304 0.281 0.017  -0.044 0.002  36  GLN A OE1 
262  N NE2 . GLN A 36  ? 0.234 0.258 0.221 0.018  -0.031 0.002  36  GLN A NE2 
263  N N   . ASP A 37  ? 0.216 0.307 0.305 0.023  -0.012 0.005  37  ASP A N   
264  C CA  . ASP A 37  ? 0.220 0.334 0.334 0.032  -0.005 0.011  37  ASP A CA  
265  C C   . ASP A 37  ? 0.217 0.326 0.348 0.028  -0.019 0.013  37  ASP A C   
266  O O   . ASP A 37  ? 0.223 0.337 0.375 0.019  -0.029 0.023  37  ASP A O   
267  C CB  . ASP A 37  ? 0.239 0.379 0.379 0.032  0.004  0.029  37  ASP A CB  
268  C CG  . ASP A 37  ? 0.276 0.423 0.395 0.039  0.018  0.030  37  ASP A CG  
269  O OD1 . ASP A 37  ? 0.306 0.458 0.404 0.056  0.026  0.019  37  ASP A OD1 
270  O OD2 . ASP A 37  ? 0.280 0.431 0.412 0.030  0.019  0.042  37  ASP A OD2 
271  N N   . GLY A 38  ? 0.232 0.331 0.356 0.034  -0.021 0.005  38  GLY A N   
272  C CA  . GLY A 38  ? 0.230 0.322 0.363 0.031  -0.034 0.009  38  GLY A CA  
273  C C   . GLY A 38  ? 0.235 0.311 0.344 0.023  -0.043 0.010  38  GLY A C   
274  O O   . GLY A 38  ? 0.215 0.285 0.306 0.018  -0.042 0.007  38  GLY A O   
275  N N   . VAL A 39  ? 0.239 0.309 0.346 0.025  -0.051 0.015  39  VAL A N   
276  C CA  . VAL A 39  ? 0.253 0.315 0.332 0.025  -0.057 0.019  39  VAL A CA  
277  C C   . VAL A 39  ? 0.252 0.312 0.317 0.021  -0.069 0.014  39  VAL A C   
278  O O   . VAL A 39  ? 0.282 0.350 0.364 0.021  -0.082 0.015  39  VAL A O   
279  C CB  . VAL A 39  ? 0.267 0.331 0.352 0.032  -0.062 0.033  39  VAL A CB  
280  C CG1 . VAL A 39  ? 0.293 0.356 0.344 0.038  -0.066 0.040  39  VAL A CG1 
281  C CG2 . VAL A 39  ? 0.259 0.318 0.367 0.034  -0.054 0.037  39  VAL A CG2 
282  N N   . GLY A 40  ? 0.292 0.344 0.334 0.020  -0.067 0.008  40  GLY A N   
283  C CA  . GLY A 40  ? 0.298 0.344 0.330 0.018  -0.083 -0.002 40  GLY A CA  
284  C C   . GLY A 40  ? 0.302 0.352 0.366 0.008  -0.083 -0.003 40  GLY A C   
285  O O   . GLY A 40  ? 0.325 0.368 0.396 0.004  -0.099 -0.010 40  GLY A O   
286  N N   . GLY A 41  ? 0.266 0.328 0.353 0.005  -0.066 0.004  41  GLY A N   
287  C CA  . GLY A 41  ? 0.256 0.330 0.374 -0.001 -0.061 0.010  41  GLY A CA  
288  C C   . GLY A 41  ? 0.262 0.330 0.364 -0.003 -0.051 0.008  41  GLY A C   
289  O O   . GLY A 41  ? 0.260 0.337 0.360 0.001  -0.033 0.011  41  GLY A O   
290  N N   . LEU A 42  ? 0.262 0.314 0.355 -0.007 -0.064 0.000  42  LEU A N   
291  C CA  . LEU A 42  ? 0.248 0.292 0.322 -0.009 -0.055 -0.003 42  LEU A CA  
292  C C   . LEU A 42  ? 0.252 0.312 0.360 -0.014 -0.045 0.011  42  LEU A C   
293  O O   . LEU A 42  ? 0.284 0.357 0.436 -0.019 -0.053 0.023  42  LEU A O   
294  C CB  . LEU A 42  ? 0.281 0.306 0.337 -0.008 -0.071 -0.016 42  LEU A CB  
295  C CG  . LEU A 42  ? 0.300 0.316 0.319 0.002  -0.079 -0.025 42  LEU A CG  
296  C CD1 . LEU A 42  ? 0.348 0.348 0.340 0.010  -0.091 -0.039 42  LEU A CD1 
297  C CD2 . LEU A 42  ? 0.300 0.321 0.299 0.007  -0.060 -0.018 42  LEU A CD2 
298  N N   . ARG A 43  ? 0.228 0.292 0.320 -0.011 -0.029 0.014  43  ARG A N   
299  C CA  . ARG A 43  ? 0.250 0.332 0.369 -0.013 -0.018 0.030  43  ARG A CA  
300  C C   . ARG A 43  ? 0.222 0.288 0.346 -0.021 -0.027 0.028  43  ARG A C   
301  O O   . ARG A 43  ? 0.260 0.310 0.347 -0.019 -0.025 0.016  43  ARG A O   
302  C CB  . ARG A 43  ? 0.268 0.362 0.362 -0.002 0.002  0.032  43  ARG A CB  
303  C CG  . ARG A 43  ? 0.268 0.379 0.359 0.010  0.011  0.032  43  ARG A CG  
304  C CD  . ARG A 43  ? 0.300 0.423 0.365 0.026  0.026  0.029  43  ARG A CD  
305  N NE  . ARG A 43  ? 0.323 0.464 0.389 0.042  0.033  0.027  43  ARG A NE  
306  C CZ  . ARG A 43  ? 0.323 0.478 0.366 0.064  0.043  0.020  43  ARG A CZ  
307  N NH1 . ARG A 43  ? 0.304 0.457 0.321 0.070  0.045  0.014  43  ARG A NH1 
308  N NH2 . ARG A 43  ? 0.348 0.517 0.393 0.081  0.046  0.014  43  ARG A NH2 
309  N N   . GLY A 44  ? 0.233 0.305 0.406 -0.029 -0.037 0.041  44  GLY A N   
310  C CA  . GLY A 44  ? 0.260 0.315 0.449 -0.036 -0.050 0.039  44  GLY A CA  
311  C C   . GLY A 44  ? 0.283 0.307 0.437 -0.034 -0.070 0.011  44  GLY A C   
312  O O   . GLY A 44  ? 0.331 0.339 0.481 -0.035 -0.075 0.004  44  GLY A O   
313  N N   . GLY A 45  ? 0.260 0.277 0.389 -0.028 -0.078 -0.003 45  GLY A N   
314  C CA  . GLY A 45  ? 0.283 0.277 0.374 -0.020 -0.095 -0.028 45  GLY A CA  
315  C C   . GLY A 45  ? 0.283 0.271 0.320 -0.012 -0.078 -0.033 45  GLY A C   
316  O O   . GLY A 45  ? 0.327 0.302 0.329 -0.000 -0.087 -0.049 45  GLY A O   
317  N N   . TYR A 46  ? 0.235 0.236 0.266 -0.014 -0.054 -0.021 46  TYR A N   
318  C CA  . TYR A 46  ? 0.234 0.230 0.229 -0.008 -0.041 -0.025 46  TYR A CA  
319  C C   . TYR A 46  ? 0.263 0.264 0.241 -0.002 -0.034 -0.022 46  TYR A C   
320  O O   . TYR A 46  ? 0.256 0.268 0.249 -0.003 -0.033 -0.017 46  TYR A O   
321  C CB  . TYR A 46  ? 0.223 0.226 0.224 -0.012 -0.026 -0.016 46  TYR A CB  
322  C CG  . TYR A 46  ? 0.233 0.228 0.248 -0.017 -0.032 -0.016 46  TYR A CG  
323  C CD1 . TYR A 46  ? 0.239 0.217 0.232 -0.012 -0.035 -0.027 46  TYR A CD1 
324  C CD2 . TYR A 46  ? 0.224 0.228 0.280 -0.024 -0.035 -0.004 46  TYR A CD2 
325  C CE1 . TYR A 46  ? 0.241 0.208 0.250 -0.014 -0.044 -0.030 46  TYR A CE1 
326  C CE2 . TYR A 46  ? 0.230 0.223 0.308 -0.028 -0.045 -0.003 46  TYR A CE2 
327  C CZ  . TYR A 46  ? 0.244 0.217 0.298 -0.023 -0.051 -0.019 46  TYR A CZ  
328  O OH  . TYR A 46  ? 0.240 0.200 0.321 -0.027 -0.063 -0.021 46  TYR A OH  
329  N N   . GLU A 47  ? 0.266 0.262 0.219 0.006  -0.030 -0.024 47  GLU A N   
330  C CA  . GLU A 47  ? 0.274 0.275 0.220 0.012  -0.025 -0.016 47  GLU A CA  
331  C C   . GLU A 47  ? 0.257 0.257 0.197 0.016  -0.013 -0.008 47  GLU A C   
332  O O   . GLU A 47  ? 0.266 0.270 0.220 0.015  -0.008 0.000  47  GLU A O   
333  C CB  . GLU A 47  ? 0.316 0.319 0.249 0.022  -0.036 -0.018 47  GLU A CB  
334  C CG  . GLU A 47  ? 0.347 0.344 0.248 0.035  -0.042 -0.024 47  GLU A CG  
335  C CD  . GLU A 47  ? 0.434 0.435 0.314 0.050  -0.057 -0.030 47  GLU A CD  
336  O OE1 . GLU A 47  ? 0.451 0.461 0.339 0.050  -0.058 -0.021 47  GLU A OE1 
337  O OE2 . GLU A 47  ? 0.501 0.494 0.361 0.061  -0.071 -0.045 47  GLU A OE2 
338  N N   . TYR A 48  ? 0.223 0.216 0.197 0.023  -0.003 0.011  48  TYR A N   
339  C CA  . TYR A 48  ? 0.221 0.207 0.190 0.021  -0.002 0.012  48  TYR A CA  
340  C C   . TYR A 48  ? 0.229 0.216 0.199 0.017  -0.003 0.010  48  TYR A C   
341  O O   . TYR A 48  ? 0.227 0.219 0.198 0.017  -0.005 0.009  48  TYR A O   
342  C CB  . TYR A 48  ? 0.237 0.222 0.203 0.023  -0.002 0.014  48  TYR A CB  
343  C CG  . TYR A 48  ? 0.236 0.213 0.197 0.022  -0.001 0.014  48  TYR A CG  
344  C CD1 . TYR A 48  ? 0.260 0.230 0.219 0.021  0.002  0.014  48  TYR A CD1 
345  C CD2 . TYR A 48  ? 0.238 0.215 0.197 0.020  -0.002 0.014  48  TYR A CD2 
346  C CE1 . TYR A 48  ? 0.269 0.234 0.225 0.019  0.003  0.014  48  TYR A CE1 
347  C CE2 . TYR A 48  ? 0.251 0.223 0.207 0.018  0.000  0.014  48  TYR A CE2 
348  C CZ  . TYR A 48  ? 0.260 0.226 0.215 0.017  0.003  0.014  48  TYR A CZ  
349  O OH  . TYR A 48  ? 0.280 0.241 0.232 0.015  0.005  0.014  48  TYR A OH  
350  N N   . SER A 49  ? 0.226 0.208 0.193 0.015  -0.001 0.009  49  SER A N   
351  C CA  . SER A 49  ? 0.224 0.207 0.192 0.012  -0.002 0.007  49  SER A CA  
352  C C   . SER A 49  ? 0.229 0.214 0.196 0.011  -0.004 0.006  49  SER A C   
353  O O   . SER A 49  ? 0.227 0.215 0.195 0.010  -0.005 0.005  49  SER A O   
354  C CB  . SER A 49  ? 0.223 0.201 0.189 0.011  -0.001 0.006  49  SER A CB  
355  O OG  . SER A 49  ? 0.225 0.202 0.192 0.011  0.000  0.005  49  SER A OG  
356  N N   . ARG A 50  ? 0.227 0.211 0.192 0.012  -0.004 0.008  50  ARG A N   
357  C CA  . ARG A 50  ? 0.231 0.217 0.194 0.012  -0.005 0.008  50  ARG A CA  
358  C C   . ARG A 50  ? 0.235 0.227 0.200 0.012  -0.007 0.007  50  ARG A C   
359  O O   . ARG A 50  ? 0.236 0.230 0.201 0.011  -0.009 0.005  50  ARG A O   
360  C CB  . ARG A 50  ? 0.229 0.212 0.188 0.013  -0.004 0.010  50  ARG A CB  
361  C CG  . ARG A 50  ? 0.233 0.218 0.189 0.012  -0.005 0.009  50  ARG A CG  
362  C CD  . ARG A 50  ? 0.240 0.221 0.192 0.013  -0.003 0.011  50  ARG A CD  
363  N NE  . ARG A 50  ? 0.240 0.216 0.190 0.015  -0.001 0.014  50  ARG A NE  
364  C CZ  . ARG A 50  ? 0.248 0.224 0.196 0.018  -0.002 0.016  50  ARG A CZ  
365  N NH1 . ARG A 50  ? 0.256 0.227 0.202 0.020  -0.000 0.018  50  ARG A NH1 
366  N NH2 . ARG A 50  ? 0.253 0.236 0.202 0.020  -0.005 0.015  50  ARG A NH2 
367  N N   . THR A 51  ? 0.234 0.228 0.200 0.015  -0.008 0.008  51  THR A N   
368  C CA  . THR A 51  ? 0.246 0.247 0.215 0.015  -0.010 0.007  51  THR A CA  
369  C C   . THR A 51  ? 0.241 0.244 0.214 0.013  -0.011 0.005  51  THR A C   
370  O O   . THR A 51  ? 0.233 0.240 0.207 0.011  -0.012 0.003  51  THR A O   
371  C CB  . THR A 51  ? 0.253 0.256 0.224 0.019  -0.011 0.009  51  THR A CB  
372  O OG1 . THR A 51  ? 0.249 0.248 0.215 0.021  -0.010 0.012  51  THR A OG1 
373  C CG2 . THR A 51  ? 0.272 0.284 0.246 0.020  -0.014 0.008  51  THR A CG2 
374  N N   . ALA A 52  ? 0.231 0.233 0.207 0.012  -0.009 0.005  52  ALA A N   
375  C CA  . ALA A 52  ? 0.220 0.223 0.199 0.010  -0.008 0.003  52  ALA A CA  
376  C C   . ALA A 52  ? 0.213 0.211 0.191 0.010  -0.006 0.004  52  ALA A C   
377  O O   . ALA A 52  ? 0.216 0.212 0.193 0.012  -0.004 0.005  52  ALA A O   
378  C CB  . ALA A 52  ? 0.219 0.228 0.203 0.010  -0.009 0.002  52  ALA A CB  
379  N N   . ASN A 53  ? 0.210 0.205 0.187 0.008  -0.005 0.002  53  ASN A N   
380  C CA  . ASN A 53  ? 0.202 0.192 0.177 0.008  -0.003 0.002  53  ASN A CA  
381  C C   . ASN A 53  ? 0.205 0.195 0.182 0.006  -0.002 0.001  53  ASN A C   
382  O O   . ASN A 53  ? 0.216 0.208 0.194 0.004  -0.003 0.000  53  ASN A O   
383  C CB  . ASN A 53  ? 0.207 0.193 0.179 0.007  -0.003 0.002  53  ASN A CB  
384  C CG  . ASN A 53  ? 0.220 0.201 0.189 0.007  -0.002 0.002  53  ASN A CG  
385  O OD1 . ASN A 53  ? 0.216 0.196 0.185 0.006  -0.001 0.001  53  ASN A OD1 
386  N ND2 . ASN A 53  ? 0.228 0.206 0.195 0.007  -0.001 0.002  53  ASN A ND2 
387  N N   . PRO A 54  ? 0.198 0.188 0.176 0.006  0.000  0.002  54  PRO A N   
388  C CA  . PRO A 54  ? 0.209 0.198 0.189 0.005  0.002  0.001  54  PRO A CA  
389  C C   . PRO A 54  ? 0.220 0.205 0.196 0.003  0.002  -0.000 54  PRO A C   
390  O O   . PRO A 54  ? 0.225 0.210 0.202 0.001  0.002  -0.001 54  PRO A O   
391  C CB  . PRO A 54  ? 0.217 0.205 0.197 0.006  0.005  0.001  54  PRO A CB  
392  C CG  . PRO A 54  ? 0.220 0.209 0.200 0.008  0.004  0.002  54  PRO A CG  
393  C CD  . PRO A 54  ? 0.215 0.202 0.192 0.008  0.002  0.003  54  PRO A CD  
394  N N   . THR A 55  ? 0.208 0.188 0.179 0.004  0.001  0.000  55  THR A N   
395  C CA  . THR A 55  ? 0.204 0.181 0.172 0.003  0.000  -0.001 55  THR A CA  
396  C C   . THR A 55  ? 0.208 0.188 0.178 0.002  -0.002 -0.001 55  THR A C   
397  O O   . THR A 55  ? 0.218 0.197 0.188 0.001  -0.002 -0.002 55  THR A O   
398  C CB  . THR A 55  ? 0.211 0.184 0.175 0.004  -0.000 -0.001 55  THR A CB  
399  O OG1 . THR A 55  ? 0.224 0.195 0.186 0.005  0.001  -0.000 55  THR A OG1 
400  C CG2 . THR A 55  ? 0.221 0.191 0.182 0.004  -0.001 -0.001 55  THR A CG2 
401  N N   . ARG A 56  ? 0.200 0.183 0.171 0.002  -0.003 -0.001 56  ARG A N   
402  C CA  . ARG A 56  ? 0.208 0.193 0.179 0.002  -0.005 -0.002 56  ARG A CA  
403  C C   . ARG A 56  ? 0.211 0.200 0.186 0.000  -0.005 -0.003 56  ARG A C   
404  O O   . ARG A 56  ? 0.225 0.214 0.200 -0.001 -0.006 -0.004 56  ARG A O   
405  C CB  . ARG A 56  ? 0.211 0.198 0.182 0.003  -0.006 -0.002 56  ARG A CB  
406  C CG  . ARG A 56  ? 0.218 0.207 0.189 0.002  -0.007 -0.003 56  ARG A CG  
407  C CD  . ARG A 56  ? 0.223 0.214 0.193 0.003  -0.008 -0.002 56  ARG A CD  
408  N NE  . ARG A 56  ? 0.234 0.227 0.204 0.004  -0.009 -0.001 56  ARG A NE  
409  C CZ  . ARG A 56  ? 0.231 0.226 0.202 0.006  -0.008 0.001  56  ARG A CZ  
410  N NH1 . ARG A 56  ? 0.234 0.225 0.203 0.006  -0.007 0.002  56  ARG A NH1 
411  N NH2 . ARG A 56  ? 0.234 0.232 0.205 0.007  -0.010 0.001  56  ARG A NH2 
412  N N   . THR A 57  ? 0.218 0.210 0.197 0.000  -0.004 -0.003 57  THR A N   
413  C CA  . THR A 57  ? 0.219 0.215 0.202 -0.001 -0.004 -0.004 57  THR A CA  
414  C C   . THR A 57  ? 0.206 0.198 0.188 -0.003 -0.003 -0.005 57  THR A C   
415  O O   . THR A 57  ? 0.212 0.206 0.196 -0.005 -0.003 -0.006 57  THR A O   
416  C CB  . THR A 57  ? 0.236 0.237 0.223 -0.000 -0.003 -0.003 57  THR A CB  
417  O OG1 . THR A 57  ? 0.260 0.264 0.247 0.002  -0.005 -0.002 57  THR A OG1 
418  C CG2 . THR A 57  ? 0.239 0.245 0.232 -0.003 -0.003 -0.005 57  THR A CG2 
419  N N   . ALA A 58  ? 0.215 0.202 0.194 -0.003 -0.000 -0.004 58  ALA A N   
420  C CA  . ALA A 58  ? 0.225 0.207 0.203 -0.004 0.002  -0.004 58  ALA A CA  
421  C C   . ALA A 58  ? 0.218 0.197 0.192 -0.005 -0.000 -0.005 58  ALA A C   
422  O O   . ALA A 58  ? 0.225 0.202 0.200 -0.007 0.001  -0.006 58  ALA A O   
423  C CB  . ALA A 58  ? 0.227 0.203 0.200 -0.003 0.004  -0.003 58  ALA A CB  
424  N N   . LEU A 59  ? 0.225 0.203 0.196 -0.003 -0.002 -0.005 59  LEU A N   
425  C CA  . LEU A 59  ? 0.226 0.203 0.196 -0.003 -0.003 -0.006 59  LEU A CA  
426  C C   . LEU A 59  ? 0.216 0.196 0.188 -0.004 -0.004 -0.008 59  LEU A C   
427  O O   . LEU A 59  ? 0.223 0.200 0.194 -0.006 -0.004 -0.009 59  LEU A O   
428  C CB  . LEU A 59  ? 0.219 0.195 0.186 -0.001 -0.005 -0.006 59  LEU A CB  
429  C CG  . LEU A 59  ? 0.215 0.191 0.181 -0.000 -0.006 -0.007 59  LEU A CG  
430  C CD1 . LEU A 59  ? 0.233 0.203 0.196 -0.000 -0.005 -0.007 59  LEU A CD1 
431  C CD2 . LEU A 59  ? 0.222 0.199 0.187 0.001  -0.007 -0.006 59  LEU A CD2 
432  N N   . GLU A 60  ? 0.222 0.208 0.197 -0.004 -0.005 -0.008 60  GLU A N   
433  C CA  . GLU A 60  ? 0.225 0.214 0.201 -0.006 -0.007 -0.010 60  GLU A CA  
434  C C   . GLU A 60  ? 0.221 0.211 0.201 -0.008 -0.006 -0.011 60  GLU A C   
435  O O   . GLU A 60  ? 0.231 0.221 0.211 -0.010 -0.007 -0.013 60  GLU A O   
436  C CB  . GLU A 60  ? 0.225 0.221 0.204 -0.004 -0.009 -0.009 60  GLU A CB  
437  C CG  . GLU A 60  ? 0.213 0.208 0.188 -0.002 -0.009 -0.007 60  GLU A CG  
438  C CD  . GLU A 60  ? 0.231 0.229 0.207 -0.000 -0.010 -0.006 60  GLU A CD  
439  O OE1 . GLU A 60  ? 0.263 0.266 0.242 -0.000 -0.011 -0.006 60  GLU A OE1 
440  O OE2 . GLU A 60  ? 0.222 0.219 0.195 0.001  -0.011 -0.005 60  GLU A OE2 
441  N N   . GLU A 61  ? 0.232 0.223 0.215 -0.009 -0.005 -0.010 61  GLU A N   
442  C CA  . GLU A 61  ? 0.223 0.215 0.210 -0.012 -0.003 -0.012 61  GLU A CA  
443  C C   . GLU A 61  ? 0.224 0.208 0.207 -0.014 -0.001 -0.013 61  GLU A C   
444  O O   . GLU A 61  ? 0.223 0.205 0.207 -0.017 -0.001 -0.015 61  GLU A O   
445  C CB  . GLU A 61  ? 0.238 0.232 0.229 -0.013 -0.001 -0.011 61  GLU A CB  
446  C CG  . GLU A 61  ? 0.254 0.257 0.250 -0.012 -0.003 -0.011 61  GLU A CG  
447  C CD  . GLU A 61  ? 0.334 0.340 0.335 -0.011 -0.001 -0.010 61  GLU A CD  
448  O OE1 . GLU A 61  ? 0.368 0.369 0.367 -0.012 0.003  -0.009 61  GLU A OE1 
449  O OE2 . GLU A 61  ? 0.403 0.416 0.408 -0.010 -0.002 -0.010 61  GLU A OE2 
450  N N   . CYS A 62  ? 0.220 0.198 0.198 -0.012 0.000  -0.011 62  CYS A N   
451  C CA  . CYS A 62  ? 0.216 0.185 0.190 -0.012 0.002  -0.011 62  CYS A CA  
452  C C   . CYS A 62  ? 0.226 0.194 0.198 -0.012 -0.000 -0.013 62  CYS A C   
453  O O   . CYS A 62  ? 0.241 0.205 0.213 -0.014 0.001  -0.014 62  CYS A O   
454  C CB  . CYS A 62  ? 0.236 0.200 0.204 -0.009 0.002  -0.009 62  CYS A CB  
455  S SG  . CYS A 62  ? 0.275 0.228 0.237 -0.008 0.004  -0.008 62  CYS A SG  
456  N N   . LEU A 63  ? 0.227 0.199 0.198 -0.010 -0.003 -0.013 63  LEU A N   
457  C CA  . LEU A 63  ? 0.244 0.214 0.213 -0.010 -0.004 -0.015 63  LEU A CA  
458  C C   . LEU A 63  ? 0.239 0.213 0.211 -0.013 -0.005 -0.018 63  LEU A C   
459  O O   . LEU A 63  ? 0.242 0.212 0.212 -0.014 -0.004 -0.020 63  LEU A O   
460  C CB  . LEU A 63  ? 0.259 0.234 0.227 -0.007 -0.006 -0.014 63  LEU A CB  
461  C CG  . LEU A 63  ? 0.287 0.258 0.252 -0.005 -0.006 -0.012 63  LEU A CG  
462  C CD1 . LEU A 63  ? 0.301 0.276 0.266 -0.003 -0.007 -0.012 63  LEU A CD1 
463  C CD2 . LEU A 63  ? 0.332 0.297 0.294 -0.004 -0.005 -0.013 63  LEU A CD2 
464  N N   . ALA A 64  ? 0.233 0.213 0.209 -0.014 -0.006 -0.018 64  ALA A N   
465  C CA  . ALA A 64  ? 0.236 0.220 0.216 -0.017 -0.007 -0.021 64  ALA A CA  
466  C C   . ALA A 64  ? 0.242 0.221 0.223 -0.021 -0.004 -0.022 64  ALA A C   
467  O O   . ALA A 64  ? 0.248 0.225 0.229 -0.023 -0.005 -0.025 64  ALA A O   
468  C CB  . ALA A 64  ? 0.259 0.252 0.244 -0.018 -0.008 -0.021 64  ALA A CB  
469  N N   . ALA A 65  ? 0.233 0.209 0.215 -0.021 -0.001 -0.020 65  ALA A N   
470  C CA  . ALA A 65  ? 0.249 0.218 0.231 -0.024 0.002  -0.021 65  ALA A CA  
471  C C   . ALA A 65  ? 0.257 0.217 0.233 -0.024 0.003  -0.022 65  ALA A C   
472  O O   . ALA A 65  ? 0.269 0.224 0.245 -0.027 0.004  -0.025 65  ALA A O   
473  C CB  . ALA A 65  ? 0.258 0.225 0.241 -0.024 0.005  -0.019 65  ALA A CB  
474  N N   . LEU A 66  ? 0.246 0.203 0.217 -0.020 0.002  -0.020 66  LEU A N   
475  C CA  . LEU A 66  ? 0.261 0.209 0.227 -0.018 0.003  -0.020 66  LEU A CA  
476  C C   . LEU A 66  ? 0.251 0.199 0.216 -0.019 0.002  -0.024 66  LEU A C   
477  O O   . LEU A 66  ? 0.283 0.223 0.245 -0.020 0.003  -0.025 66  LEU A O   
478  C CB  . LEU A 66  ? 0.272 0.217 0.233 -0.014 0.003  -0.018 66  LEU A CB  
479  C CG  . LEU A 66  ? 0.279 0.222 0.240 -0.012 0.005  -0.015 66  LEU A CG  
480  C CD1 . LEU A 66  ? 0.295 0.237 0.251 -0.008 0.003  -0.012 66  LEU A CD1 
481  C CD2 . LEU A 66  ? 0.302 0.236 0.260 -0.014 0.008  -0.014 66  LEU A CD2 
482  N N   . GLU A 67  ? 0.245 0.201 0.212 -0.019 -0.001 -0.025 67  GLU A N   
483  C CA  . GLU A 67  ? 0.251 0.209 0.217 -0.019 -0.003 -0.028 67  GLU A CA  
484  C C   . GLU A 67  ? 0.261 0.222 0.231 -0.024 -0.004 -0.031 67  GLU A C   
485  O O   . GLU A 67  ? 0.279 0.239 0.247 -0.025 -0.005 -0.035 67  GLU A O   
486  C CB  . GLU A 67  ? 0.247 0.211 0.212 -0.016 -0.006 -0.027 67  GLU A CB  
487  C CG  . GLU A 67  ? 0.248 0.208 0.209 -0.012 -0.005 -0.025 67  GLU A CG  
488  C CD  . GLU A 67  ? 0.265 0.219 0.222 -0.011 -0.005 -0.027 67  GLU A CD  
489  O OE1 . GLU A 67  ? 0.291 0.241 0.247 -0.013 -0.004 -0.030 67  GLU A OE1 
490  O OE2 . GLU A 67  ? 0.267 0.220 0.222 -0.007 -0.004 -0.025 67  GLU A OE2 
491  N N   . GLY A 68  ? 0.251 0.215 0.226 -0.027 -0.003 -0.031 68  GLY A N   
492  C CA  . GLY A 68  ? 0.271 0.240 0.251 -0.031 -0.004 -0.034 68  GLY A CA  
493  C C   . GLY A 68  ? 0.273 0.253 0.256 -0.030 -0.008 -0.036 68  GLY A C   
494  O O   . GLY A 68  ? 0.305 0.287 0.289 -0.033 -0.010 -0.039 68  GLY A O   
495  N N   . GLY A 69  ? 0.249 0.233 0.231 -0.027 -0.010 -0.033 69  GLY A N   
496  C CA  . GLY A 69  ? 0.259 0.252 0.242 -0.026 -0.013 -0.033 69  GLY A CA  
497  C C   . GLY A 69  ? 0.263 0.264 0.253 -0.026 -0.014 -0.032 69  GLY A C   
498  O O   . GLY A 69  ? 0.276 0.276 0.270 -0.027 -0.011 -0.030 69  GLY A O   
499  N N   A VAL A 70  ? 0.257 0.266 0.248 -0.025 -0.018 -0.032 70  VAL A N   
500  N N   B VAL A 70  ? 0.255 0.265 0.246 -0.025 -0.018 -0.032 70  VAL A N   
501  C CA  A VAL A 70  ? 0.256 0.274 0.253 -0.024 -0.019 -0.031 70  VAL A CA  
502  C CA  B VAL A 70  ? 0.252 0.270 0.250 -0.024 -0.019 -0.031 70  VAL A CA  
503  C C   A VAL A 70  ? 0.262 0.280 0.258 -0.020 -0.018 -0.027 70  VAL A C   
504  C C   B VAL A 70  ? 0.259 0.278 0.255 -0.020 -0.019 -0.027 70  VAL A C   
505  O O   A VAL A 70  ? 0.275 0.297 0.276 -0.019 -0.017 -0.025 70  VAL A O   
506  O O   B VAL A 70  ? 0.267 0.292 0.268 -0.019 -0.019 -0.025 70  VAL A O   
507  C CB  A VAL A 70  ? 0.273 0.300 0.273 -0.025 -0.023 -0.034 70  VAL A CB  
508  C CB  B VAL A 70  ? 0.267 0.295 0.269 -0.025 -0.023 -0.034 70  VAL A CB  
509  C CG1 A VAL A 70  ? 0.277 0.305 0.270 -0.021 -0.026 -0.033 70  VAL A CG1 
510  C CG1 B VAL A 70  ? 0.273 0.300 0.277 -0.030 -0.023 -0.039 70  VAL A CG1 
511  C CG2 A VAL A 70  ? 0.270 0.306 0.278 -0.024 -0.024 -0.033 70  VAL A CG2 
512  C CG2 B VAL A 70  ? 0.270 0.298 0.264 -0.022 -0.026 -0.033 70  VAL A CG2 
513  N N   . ARG A 71  ? 0.231 0.244 0.220 -0.017 -0.018 -0.025 71  ARG A N   
514  C CA  . ARG A 71  ? 0.249 0.263 0.236 -0.013 -0.018 -0.021 71  ARG A CA  
515  C C   . ARG A 71  ? 0.231 0.237 0.212 -0.012 -0.016 -0.020 71  ARG A C   
516  O O   . ARG A 71  ? 0.238 0.242 0.215 -0.012 -0.017 -0.022 71  ARG A O   
517  C CB  . ARG A 71  ? 0.265 0.286 0.251 -0.011 -0.021 -0.021 71  ARG A CB  
518  C CG  . ARG A 71  ? 0.271 0.292 0.255 -0.007 -0.021 -0.017 71  ARG A CG  
519  C CD  . ARG A 71  ? 0.311 0.335 0.300 -0.006 -0.020 -0.016 71  ARG A CD  
520  N NE  . ARG A 71  ? 0.336 0.360 0.323 -0.003 -0.020 -0.012 71  ARG A NE  
521  C CZ  . ARG A 71  ? 0.309 0.338 0.296 -0.000 -0.022 -0.011 71  ARG A CZ  
522  N NH1 . ARG A 71  ? 0.331 0.365 0.319 -0.000 -0.026 -0.013 71  ARG A NH1 
523  N NH2 . ARG A 71  ? 0.312 0.339 0.297 0.003  -0.021 -0.008 71  ARG A NH2 
524  N N   . GLY A 72  ? 0.226 0.230 0.207 -0.010 -0.014 -0.017 72  GLY A N   
525  C CA  . GLY A 72  ? 0.219 0.218 0.195 -0.008 -0.013 -0.016 72  GLY A CA  
526  C C   . GLY A 72  ? 0.211 0.212 0.186 -0.005 -0.014 -0.013 72  GLY A C   
527  O O   . GLY A 72  ? 0.231 0.235 0.209 -0.005 -0.014 -0.012 72  GLY A O   
528  N N   . LEU A 73  ? 0.204 0.202 0.175 -0.004 -0.013 -0.012 73  LEU A N   
529  C CA  . LEU A 73  ? 0.212 0.211 0.181 -0.001 -0.013 -0.010 73  LEU A CA  
530  C C   . LEU A 73  ? 0.222 0.216 0.189 -0.001 -0.012 -0.009 73  LEU A C   
531  O O   . LEU A 73  ? 0.219 0.212 0.185 -0.001 -0.012 -0.011 73  LEU A O   
532  C CB  . LEU A 73  ? 0.225 0.227 0.192 -0.000 -0.015 -0.010 73  LEU A CB  
533  C CG  . LEU A 73  ? 0.252 0.260 0.222 -0.001 -0.017 -0.011 73  LEU A CG  
534  C CD1 . LEU A 73  ? 0.301 0.310 0.266 0.001  -0.019 -0.011 73  LEU A CD1 
535  C CD2 . LEU A 73  ? 0.304 0.313 0.276 0.001  -0.017 -0.009 73  LEU A CD2 
536  N N   . ALA A 74  ? 0.211 0.204 0.179 0.000  -0.011 -0.008 74  ALA A N   
537  C CA  . ALA A 74  ? 0.221 0.211 0.188 0.001  -0.010 -0.007 74  ALA A CA  
538  C C   . ALA A 74  ? 0.218 0.209 0.183 0.002  -0.009 -0.006 74  ALA A C   
539  O O   . ALA A 74  ? 0.217 0.210 0.183 0.002  -0.009 -0.004 74  ALA A O   
540  C CB  . ALA A 74  ? 0.211 0.198 0.178 0.001  -0.009 -0.006 74  ALA A CB  
541  N N   . PHE A 75  ? 0.212 0.203 0.177 0.002  -0.009 -0.007 75  PHE A N   
542  C CA  . PHE A 75  ? 0.212 0.202 0.175 0.003  -0.008 -0.006 75  PHE A CA  
543  C C   . PHE A 75  ? 0.210 0.199 0.175 0.003  -0.007 -0.006 75  PHE A C   
544  O O   . PHE A 75  ? 0.211 0.199 0.177 0.003  -0.008 -0.007 75  PHE A O   
545  C CB  . PHE A 75  ? 0.217 0.209 0.179 0.003  -0.008 -0.007 75  PHE A CB  
546  C CG  . PHE A 75  ? 0.207 0.201 0.167 0.003  -0.009 -0.007 75  PHE A CG  
547  C CD1 . PHE A 75  ? 0.227 0.221 0.185 0.004  -0.009 -0.005 75  PHE A CD1 
548  C CD2 . PHE A 75  ? 0.212 0.206 0.172 0.002  -0.010 -0.009 75  PHE A CD2 
549  C CE1 . PHE A 75  ? 0.230 0.227 0.187 0.004  -0.011 -0.005 75  PHE A CE1 
550  C CE2 . PHE A 75  ? 0.225 0.221 0.184 0.002  -0.012 -0.009 75  PHE A CE2 
551  C CZ  . PHE A 75  ? 0.235 0.233 0.193 0.003  -0.012 -0.007 75  PHE A CZ  
552  N N   . ALA A 76  ? 0.206 0.196 0.171 0.003  -0.006 -0.005 76  ALA A N   
553  C CA  . ALA A 76  ? 0.226 0.216 0.193 0.002  -0.005 -0.005 76  ALA A CA  
554  C C   . ALA A 76  ? 0.213 0.204 0.182 0.003  -0.006 -0.007 76  ALA A C   
555  O O   . ALA A 76  ? 0.217 0.209 0.189 0.003  -0.006 -0.008 76  ALA A O   
556  C CB  . ALA A 76  ? 0.230 0.221 0.198 0.002  -0.004 -0.004 76  ALA A CB  
557  N N   . SER A 77  ? 0.210 0.202 0.177 0.003  -0.005 -0.008 77  SER A N   
558  C CA  . SER A 77  ? 0.208 0.201 0.177 0.004  -0.005 -0.010 77  SER A CA  
559  C C   . SER A 77  ? 0.219 0.212 0.186 0.004  -0.005 -0.011 77  SER A C   
560  O O   . SER A 77  ? 0.207 0.199 0.171 0.004  -0.005 -0.010 77  SER A O   
561  C CB  . SER A 77  ? 0.212 0.208 0.184 0.004  -0.004 -0.010 77  SER A CB  
562  O OG  . SER A 77  ? 0.214 0.211 0.184 0.003  -0.002 -0.009 77  SER A OG  
563  N N   . GLY A 78  ? 0.205 0.197 0.172 0.006  -0.005 -0.012 78  GLY A N   
564  C CA  . GLY A 78  ? 0.213 0.204 0.177 0.006  -0.005 -0.014 78  GLY A CA  
565  C C   . GLY A 78  ? 0.210 0.203 0.173 0.006  -0.003 -0.014 78  GLY A C   
566  O O   . GLY A 78  ? 0.224 0.215 0.182 0.005  -0.004 -0.014 78  GLY A O   
567  N N   . MET A 79  ? 0.215 0.210 0.179 0.006  -0.002 -0.013 79  MET A N   
568  C CA  . MET A 79  ? 0.216 0.213 0.178 0.005  0.001  -0.013 79  MET A CA  
569  C C   . MET A 79  ? 0.223 0.218 0.181 0.004  -0.000 -0.011 79  MET A C   
570  O O   . MET A 79  ? 0.231 0.225 0.184 0.005  0.000  -0.011 79  MET A O   
571  C CB  . MET A 79  ? 0.227 0.226 0.193 0.005  0.003  -0.013 79  MET A CB  
572  C CG  . MET A 79  ? 0.232 0.232 0.200 0.007  0.004  -0.015 79  MET A CG  
573  S SD  . MET A 79  ? 0.246 0.245 0.210 0.008  0.005  -0.017 79  MET A SD  
574  C CE  . MET A 79  ? 0.259 0.257 0.216 0.007  0.007  -0.016 79  MET A CE  
575  N N   . ALA A 80  ? 0.225 0.220 0.185 0.004  -0.001 -0.009 80  ALA A N   
576  C CA  . ALA A 80  ? 0.211 0.206 0.169 0.004  -0.002 -0.007 80  ALA A CA  
577  C C   . ALA A 80  ? 0.215 0.209 0.170 0.004  -0.004 -0.008 80  ALA A C   
578  O O   . ALA A 80  ? 0.231 0.225 0.182 0.004  -0.005 -0.007 80  ALA A O   
579  C CB  . ALA A 80  ? 0.218 0.211 0.178 0.003  -0.002 -0.006 80  ALA A CB  
580  N N   . ALA A 81  ? 0.219 0.212 0.175 0.004  -0.005 -0.010 81  ALA A N   
581  C CA  . ALA A 81  ? 0.225 0.218 0.179 0.003  -0.007 -0.011 81  ALA A CA  
582  C C   . ALA A 81  ? 0.232 0.225 0.182 0.004  -0.007 -0.013 81  ALA A C   
583  O O   . ALA A 81  ? 0.230 0.224 0.177 0.004  -0.008 -0.013 81  ALA A O   
584  C CB  . ALA A 81  ? 0.229 0.220 0.185 0.003  -0.008 -0.013 81  ALA A CB  
585  N N   . GLU A 82  ? 0.222 0.214 0.172 0.004  -0.005 -0.014 82  GLU A N   
586  C CA  . GLU A 82  ? 0.237 0.229 0.182 0.005  -0.004 -0.015 82  GLU A CA  
587  C C   . GLU A 82  ? 0.237 0.230 0.178 0.005  -0.003 -0.013 82  GLU A C   
588  O O   . GLU A 82  ? 0.247 0.241 0.183 0.006  -0.004 -0.014 82  GLU A O   
589  C CB  . GLU A 82  ? 0.239 0.231 0.185 0.006  -0.001 -0.016 82  GLU A CB  
590  C CG  . GLU A 82  ? 0.260 0.250 0.209 0.006  -0.001 -0.018 82  GLU A CG  
591  C CD  . GLU A 82  ? 0.286 0.276 0.235 0.008  0.001  -0.020 82  GLU A CD  
592  O OE1 . GLU A 82  ? 0.299 0.291 0.246 0.008  0.003  -0.020 82  GLU A OE1 
593  O OE2 . GLU A 82  ? 0.312 0.301 0.264 0.009  0.001  -0.021 82  GLU A OE2 
594  N N   . ASP A 83  ? 0.230 0.224 0.173 0.005  -0.002 -0.011 83  ASP A N   
595  C CA  . ASP A 83  ? 0.241 0.235 0.180 0.006  -0.000 -0.008 83  ASP A CA  
596  C C   . ASP A 83  ? 0.245 0.239 0.181 0.006  -0.003 -0.007 83  ASP A C   
597  O O   . ASP A 83  ? 0.245 0.238 0.174 0.007  -0.004 -0.007 83  ASP A O   
598  C CB  . ASP A 83  ? 0.238 0.231 0.180 0.005  0.002  -0.006 83  ASP A CB  
599  C CG  . ASP A 83  ? 0.269 0.261 0.206 0.006  0.004  -0.004 83  ASP A CG  
600  O OD1 . ASP A 83  ? 0.310 0.301 0.242 0.006  0.006  -0.004 83  ASP A OD1 
601  O OD2 . ASP A 83  ? 0.300 0.290 0.237 0.006  0.004  -0.001 83  ASP A OD2 
602  N N   . THR A 84  ? 0.235 0.229 0.175 0.006  -0.005 -0.007 84  THR A N   
603  C CA  . THR A 84  ? 0.244 0.240 0.182 0.006  -0.008 -0.006 84  THR A CA  
604  C C   . THR A 84  ? 0.243 0.240 0.178 0.006  -0.011 -0.009 84  THR A C   
605  O O   . THR A 84  ? 0.248 0.246 0.179 0.008  -0.013 -0.008 84  THR A O   
606  C CB  . THR A 84  ? 0.256 0.253 0.200 0.006  -0.009 -0.006 84  THR A CB  
607  O OG1 . THR A 84  ? 0.297 0.292 0.242 0.006  -0.007 -0.003 84  THR A OG1 
608  C CG2 . THR A 84  ? 0.266 0.265 0.210 0.007  -0.012 -0.005 84  THR A CG2 
609  N N   . LEU A 85  ? 0.245 0.242 0.182 0.005  -0.011 -0.012 85  LEU A N   
610  C CA  . LEU A 85  ? 0.239 0.236 0.173 0.005  -0.013 -0.015 85  LEU A CA  
611  C C   . LEU A 85  ? 0.244 0.242 0.171 0.006  -0.012 -0.015 85  LEU A C   
612  O O   . LEU A 85  ? 0.260 0.259 0.183 0.007  -0.015 -0.016 85  LEU A O   
613  C CB  . LEU A 85  ? 0.229 0.224 0.166 0.003  -0.012 -0.017 85  LEU A CB  
614  C CG  . LEU A 85  ? 0.251 0.246 0.185 0.002  -0.014 -0.021 85  LEU A CG  
615  C CD1 . LEU A 85  ? 0.254 0.253 0.189 0.001  -0.017 -0.022 85  LEU A CD1 
616  C CD2 . LEU A 85  ? 0.266 0.257 0.202 0.001  -0.012 -0.023 85  LEU A CD2 
617  N N   . LEU A 86  ? 0.235 0.230 0.159 0.007  -0.009 -0.014 86  LEU A N   
618  C CA  . LEU A 86  ? 0.248 0.242 0.165 0.008  -0.008 -0.015 86  LEU A CA  
619  C C   . LEU A 86  ? 0.256 0.250 0.167 0.010  -0.008 -0.011 86  LEU A C   
620  O O   . LEU A 86  ? 0.265 0.259 0.169 0.011  -0.009 -0.012 86  LEU A O   
621  C CB  . LEU A 86  ? 0.257 0.249 0.174 0.008  -0.003 -0.015 86  LEU A CB  
622  C CG  . LEU A 86  ? 0.282 0.273 0.202 0.007  -0.003 -0.018 86  LEU A CG  
623  C CD1 . LEU A 86  ? 0.296 0.286 0.217 0.008  0.002  -0.018 86  LEU A CD1 
624  C CD2 . LEU A 86  ? 0.303 0.293 0.218 0.007  -0.005 -0.022 86  LEU A CD2 
625  N N   A ARG A 87  ? 0.251 0.246 0.166 0.010  -0.007 -0.008 87  ARG A N   
626  N N   B ARG A 87  ? 0.253 0.247 0.168 0.010  -0.007 -0.008 87  ARG A N   
627  C CA  A ARG A 87  ? 0.263 0.256 0.173 0.012  -0.008 -0.005 87  ARG A CA  
628  C CA  B ARG A 87  ? 0.265 0.259 0.176 0.012  -0.008 -0.005 87  ARG A CA  
629  C C   A ARG A 87  ? 0.269 0.266 0.178 0.013  -0.013 -0.006 87  ARG A C   
630  C C   B ARG A 87  ? 0.271 0.268 0.180 0.013  -0.013 -0.005 87  ARG A C   
631  O O   A ARG A 87  ? 0.285 0.281 0.186 0.015  -0.014 -0.004 87  ARG A O   
632  O O   B ARG A 87  ? 0.284 0.280 0.186 0.015  -0.014 -0.004 87  ARG A O   
633  C CB  A ARG A 87  ? 0.270 0.262 0.184 0.012  -0.006 -0.002 87  ARG A CB  
634  C CB  B ARG A 87  ? 0.279 0.271 0.194 0.011  -0.006 -0.002 87  ARG A CB  
635  C CG  A ARG A 87  ? 0.310 0.299 0.218 0.014  -0.004 0.002  87  ARG A CG  
636  C CG  B ARG A 87  ? 0.312 0.302 0.223 0.013  -0.003 0.002  87  ARG A CG  
637  C CD  A ARG A 87  ? 0.321 0.308 0.227 0.013  0.001  0.003  87  ARG A CD  
638  C CD  B ARG A 87  ? 0.322 0.308 0.227 0.013  0.001  0.002  87  ARG A CD  
639  N NE  A ARG A 87  ? 0.303 0.289 0.216 0.011  0.003  0.003  87  ARG A NE  
640  N NE  B ARG A 87  ? 0.310 0.293 0.211 0.014  0.003  0.006  87  ARG A NE  
641  C CZ  A ARG A 87  ? 0.287 0.272 0.204 0.011  0.005  0.005  87  ARG A CZ  
642  C CZ  B ARG A 87  ? 0.308 0.287 0.202 0.015  0.006  0.009  87  ARG A CZ  
643  N NH1 A ARG A 87  ? 0.279 0.264 0.202 0.008  0.006  0.004  87  ARG A NH1 
644  N NH1 B ARG A 87  ? 0.267 0.242 0.157 0.017  0.007  0.012  87  ARG A NH1 
645  N NH2 A ARG A 87  ? 0.272 0.254 0.184 0.013  0.004  0.008  87  ARG A NH2 
646  N NH2 B ARG A 87  ? 0.322 0.300 0.211 0.015  0.009  0.007  87  ARG A NH2 
647  N N   . THR A 88  ? 0.261 0.261 0.176 0.011  -0.015 -0.008 88  THR A N   
648  C CA  . THR A 88  ? 0.260 0.265 0.176 0.012  -0.020 -0.009 88  THR A CA  
649  C C   . THR A 88  ? 0.276 0.281 0.185 0.012  -0.022 -0.012 88  THR A C   
650  O O   . THR A 88  ? 0.288 0.296 0.193 0.013  -0.026 -0.012 88  THR A O   
651  C CB  . THR A 88  ? 0.252 0.258 0.177 0.009  -0.021 -0.011 88  THR A CB  
652  O OG1 . THR A 88  ? 0.249 0.254 0.178 0.010  -0.020 -0.008 88  THR A OG1 
653  C CG2 . THR A 88  ? 0.243 0.255 0.170 0.009  -0.026 -0.012 88  THR A CG2 
654  N N   . ILE A 89  ? 0.273 0.276 0.182 0.010  -0.021 -0.016 89  ILE A N   
655  C CA  . ILE A 89  ? 0.283 0.287 0.187 0.009  -0.024 -0.020 89  ILE A CA  
656  C C   . ILE A 89  ? 0.311 0.311 0.205 0.011  -0.022 -0.020 89  ILE A C   
657  O O   . ILE A 89  ? 0.341 0.342 0.229 0.011  -0.024 -0.023 89  ILE A O   
658  C CB  . ILE A 89  ? 0.287 0.290 0.197 0.006  -0.023 -0.024 89  ILE A CB  
659  C CG1 . ILE A 89  ? 0.292 0.290 0.201 0.006  -0.019 -0.024 89  ILE A CG1 
660  C CG2 . ILE A 89  ? 0.282 0.287 0.201 0.004  -0.025 -0.024 89  ILE A CG2 
661  C CD1 . ILE A 89  ? 0.322 0.318 0.234 0.004  -0.018 -0.028 89  ILE A CD1 
662  N N   . ALA A 90  ? 0.293 0.290 0.184 0.012  -0.018 -0.016 90  ALA A N   
663  C CA  . ALA A 90  ? 0.295 0.289 0.176 0.014  -0.015 -0.016 90  ALA A CA  
664  C C   . ALA A 90  ? 0.317 0.310 0.193 0.017  -0.014 -0.012 90  ALA A C   
665  O O   . ALA A 90  ? 0.315 0.309 0.195 0.017  -0.015 -0.009 90  ALA A O   
666  C CB  . ALA A 90  ? 0.290 0.280 0.173 0.013  -0.009 -0.017 90  ALA A CB  
667  N N   A ARG A 91  ? 0.318 0.308 0.183 0.018  -0.012 -0.011 91  ARG A N   
668  N N   B ARG A 91  ? 0.320 0.310 0.185 0.018  -0.012 -0.011 91  ARG A N   
669  C CA  A ARG A 91  ? 0.349 0.335 0.206 0.021  -0.010 -0.006 91  ARG A CA  
670  C CA  B ARG A 91  ? 0.353 0.340 0.210 0.021  -0.010 -0.006 91  ARG A CA  
671  C C   A ARG A 91  ? 0.341 0.323 0.189 0.022  -0.005 -0.007 91  ARG A C   
672  C C   B ARG A 91  ? 0.339 0.321 0.188 0.022  -0.005 -0.007 91  ARG A C   
673  O O   A ARG A 91  ? 0.366 0.348 0.214 0.020  -0.005 -0.011 91  ARG A O   
674  O O   B ARG A 91  ? 0.360 0.342 0.209 0.020  -0.004 -0.011 91  ARG A O   
675  C CB  A ARG A 91  ? 0.378 0.368 0.231 0.024  -0.016 -0.005 91  ARG A CB  
676  C CB  B ARG A 91  ? 0.386 0.375 0.237 0.024  -0.016 -0.006 91  ARG A CB  
677  C CG  A ARG A 91  ? 0.424 0.414 0.267 0.025  -0.020 -0.009 91  ARG A CG  
678  C CG  B ARG A 91  ? 0.453 0.443 0.296 0.024  -0.019 -0.010 91  ARG A CG  
679  C CD  A ARG A 91  ? 0.456 0.450 0.296 0.028  -0.026 -0.008 91  ARG A CD  
680  C CD  B ARG A 91  ? 0.514 0.509 0.356 0.025  -0.027 -0.012 91  ARG A CD  
681  N NE  A ARG A 91  ? 0.476 0.467 0.308 0.031  -0.024 -0.003 91  ARG A NE  
682  N NE  B ARG A 91  ? 0.537 0.532 0.368 0.027  -0.029 -0.014 91  ARG A NE  
683  C CZ  A ARG A 91  ? 0.443 0.436 0.278 0.034  -0.027 0.001  91  ARG A CZ  
684  C CZ  B ARG A 91  ? 0.511 0.502 0.329 0.030  -0.028 -0.012 91  ARG A CZ  
685  N NH1 A ARG A 91  ? 0.466 0.466 0.311 0.033  -0.031 -0.001 91  ARG A NH1 
686  N NH1 B ARG A 91  ? 0.541 0.530 0.357 0.033  -0.026 -0.006 91  ARG A NH1 
687  N NH2 A ARG A 91  ? 0.420 0.407 0.247 0.037  -0.024 0.006  91  ARG A NH2 
688  N NH2 B ARG A 91  ? 0.503 0.494 0.310 0.031  -0.031 -0.015 91  ARG A NH2 
689  N N   . PRO A 92  ? 0.355 0.332 0.195 0.024  -0.002 -0.003 92  PRO A N   
690  C CA  . PRO A 92  ? 0.338 0.311 0.169 0.025  0.003  -0.003 92  PRO A CA  
691  C C   . PRO A 92  ? 0.365 0.339 0.186 0.026  -0.000 -0.007 92  PRO A C   
692  O O   . PRO A 92  ? 0.385 0.360 0.201 0.028  -0.006 -0.007 92  PRO A O   
693  C CB  . PRO A 92  ? 0.349 0.318 0.173 0.027  0.007  0.003  92  PRO A CB  
694  C CG  . PRO A 92  ? 0.356 0.326 0.189 0.026  0.006  0.006  92  PRO A CG  
695  C CD  . PRO A 92  ? 0.348 0.324 0.189 0.025  -0.001 0.003  92  PRO A CD  
696  N N   . GLY A 93  ? 0.365 0.337 0.184 0.025  0.003  -0.010 93  GLY A N   
697  C CA  . GLY A 93  ? 0.377 0.348 0.186 0.026  0.001  -0.014 93  GLY A CA  
698  C C   . GLY A 93  ? 0.373 0.347 0.189 0.023  -0.003 -0.019 93  GLY A C   
699  O O   . GLY A 93  ? 0.380 0.353 0.189 0.023  -0.004 -0.024 93  GLY A O   
700  N N   . ASP A 94  ? 0.343 0.321 0.173 0.021  -0.004 -0.020 94  ASP A N   
701  C CA  . ASP A 94  ? 0.333 0.313 0.170 0.019  -0.007 -0.024 94  ASP A CA  
702  C C   . ASP A 94  ? 0.345 0.323 0.185 0.017  -0.002 -0.027 94  ASP A C   
703  O O   . ASP A 94  ? 0.377 0.353 0.217 0.018  0.004  -0.024 94  ASP A O   
704  C CB  . ASP A 94  ? 0.319 0.303 0.168 0.017  -0.011 -0.023 94  ASP A CB  
705  C CG  . ASP A 94  ? 0.349 0.337 0.196 0.018  -0.017 -0.022 94  ASP A CG  
706  O OD1 . ASP A 94  ? 0.360 0.348 0.197 0.020  -0.019 -0.024 94  ASP A OD1 
707  O OD2 . ASP A 94  ? 0.362 0.354 0.218 0.017  -0.019 -0.021 94  ASP A OD2 
708  N N   . HIS A 95  ? 0.345 0.323 0.189 0.016  -0.004 -0.031 95  HIS A N   
709  C CA  . HIS A 95  ? 0.342 0.318 0.190 0.015  0.001  -0.034 95  HIS A CA  
710  C C   . HIS A 95  ? 0.324 0.301 0.184 0.013  -0.001 -0.035 95  HIS A C   
711  O O   . HIS A 95  ? 0.324 0.303 0.186 0.011  -0.007 -0.037 95  HIS A O   
712  C CB  . HIS A 95  ? 0.357 0.328 0.194 0.016  0.001  -0.038 95  HIS A CB  
713  C CG  . HIS A 95  ? 0.347 0.315 0.187 0.015  0.005  -0.042 95  HIS A CG  
714  N ND1 . HIS A 95  ? 0.368 0.335 0.211 0.014  0.002  -0.046 95  HIS A ND1 
715  C CD2 . HIS A 95  ? 0.359 0.326 0.200 0.017  0.011  -0.041 95  HIS A CD2 
716  C CE1 . HIS A 95  ? 0.359 0.323 0.204 0.014  0.007  -0.048 95  HIS A CE1 
717  N NE2 . HIS A 95  ? 0.357 0.321 0.200 0.016  0.012  -0.045 95  HIS A NE2 
718  N N   . LEU A 96  ? 0.322 0.299 0.189 0.013  0.003  -0.035 96  LEU A N   
719  C CA  . LEU A 96  ? 0.322 0.299 0.199 0.011  0.002  -0.037 96  LEU A CA  
720  C C   . LEU A 96  ? 0.337 0.310 0.214 0.012  0.005  -0.040 96  LEU A C   
721  O O   . LEU A 96  ? 0.339 0.312 0.214 0.013  0.010  -0.040 96  LEU A O   
722  C CB  . LEU A 96  ? 0.340 0.319 0.226 0.011  0.003  -0.032 96  LEU A CB  
723  C CG  . LEU A 96  ? 0.371 0.353 0.258 0.011  0.001  -0.029 96  LEU A CG  
724  C CD1 . LEU A 96  ? 0.374 0.358 0.270 0.011  0.004  -0.025 96  LEU A CD1 
725  C CD2 . LEU A 96  ? 0.403 0.387 0.294 0.009  -0.004 -0.030 96  LEU A CD2 
726  N N   . ILE A 97  ? 0.327 0.298 0.207 0.010  0.003  -0.043 97  ILE A N   
727  C CA  . ILE A 97  ? 0.317 0.285 0.199 0.011  0.006  -0.046 97  ILE A CA  
728  C C   . ILE A 97  ? 0.309 0.278 0.202 0.011  0.006  -0.044 97  ILE A C   
729  O O   . ILE A 97  ? 0.317 0.287 0.214 0.009  0.003  -0.043 97  ILE A O   
730  C CB  . ILE A 97  ? 0.328 0.291 0.206 0.010  0.004  -0.051 97  ILE A CB  
731  C CG1 . ILE A 97  ? 0.351 0.313 0.217 0.010  0.003  -0.054 97  ILE A CG1 
732  C CG2 . ILE A 97  ? 0.342 0.300 0.223 0.010  0.006  -0.053 97  ILE A CG2 
733  C CD1 . ILE A 97  ? 0.355 0.313 0.216 0.008  -0.000 -0.059 97  ILE A CD1 
734  N N   . ILE A 98  ? 0.299 0.268 0.196 0.013  0.010  -0.043 98  ILE A N   
735  C CA  . ILE A 98  ? 0.294 0.264 0.200 0.013  0.011  -0.041 98  ILE A CA  
736  C C   . ILE A 98  ? 0.291 0.257 0.198 0.015  0.013  -0.044 98  ILE A C   
737  O O   . ILE A 98  ? 0.300 0.263 0.201 0.016  0.015  -0.047 98  ILE A O   
738  C CB  . ILE A 98  ? 0.303 0.279 0.214 0.014  0.013  -0.037 98  ILE A CB  
739  C CG1 . ILE A 98  ? 0.340 0.316 0.250 0.016  0.018  -0.038 98  ILE A CG1 
740  C CG2 . ILE A 98  ? 0.330 0.308 0.238 0.012  0.011  -0.035 98  ILE A CG2 
741  C CD1 . ILE A 98  ? 0.352 0.334 0.268 0.017  0.021  -0.034 98  ILE A CD1 
742  N N   . PRO A 99  ? 0.283 0.250 0.199 0.016  0.013  -0.043 99  PRO A N   
743  C CA  . PRO A 99  ? 0.293 0.256 0.210 0.018  0.015  -0.045 99  PRO A CA  
744  C C   . PRO A 99  ? 0.301 0.267 0.220 0.022  0.019  -0.045 99  PRO A C   
745  O O   . PRO A 99  ? 0.315 0.286 0.236 0.022  0.021  -0.042 99  PRO A O   
746  C CB  . PRO A 99  ? 0.293 0.255 0.216 0.019  0.013  -0.043 99  PRO A CB  
747  C CG  . PRO A 99  ? 0.286 0.251 0.211 0.015  0.010  -0.041 99  PRO A CG  
748  C CD  . PRO A 99  ? 0.285 0.255 0.207 0.015  0.010  -0.040 99  PRO A CD  
749  N N   . ASN A 100 ? 0.312 0.274 0.229 0.024  0.022  -0.048 100 ASN A N   
750  C CA  . ASN A 100 ? 0.311 0.276 0.232 0.028  0.026  -0.048 100 ASN A CA  
751  C C   . ASN A 100 ? 0.290 0.258 0.220 0.030  0.026  -0.046 100 ASN A C   
752  O O   . ASN A 100 ? 0.310 0.281 0.245 0.033  0.030  -0.046 100 ASN A O   
753  C CB  . ASN A 100 ? 0.317 0.275 0.231 0.030  0.030  -0.052 100 ASN A CB  
754  C CG  . ASN A 100 ? 0.316 0.267 0.230 0.032  0.029  -0.054 100 ASN A CG  
755  O OD1 . ASN A 100 ? 0.331 0.281 0.249 0.031  0.026  -0.053 100 ASN A OD1 
756  N ND2 . ASN A 100 ? 0.343 0.290 0.254 0.035  0.032  -0.057 100 ASN A ND2 
757  N N   . ASP A 101 ? 0.297 0.264 0.231 0.029  0.022  -0.044 101 ASP A N   
758  C CA  . ASP A 101 ? 0.302 0.272 0.244 0.031  0.021  -0.042 101 ASP A CA  
759  C C   . ASP A 101 ? 0.287 0.259 0.231 0.028  0.017  -0.039 101 ASP A C   
760  O O   . ASP A 101 ? 0.295 0.261 0.235 0.025  0.015  -0.040 101 ASP A O   
761  C CB  . ASP A 101 ? 0.307 0.271 0.250 0.034  0.021  -0.044 101 ASP A CB  
762  C CG  . ASP A 101 ? 0.337 0.306 0.288 0.037  0.020  -0.041 101 ASP A CG  
763  O OD1 . ASP A 101 ? 0.327 0.303 0.284 0.039  0.022  -0.041 101 ASP A OD1 
764  O OD2 . ASP A 101 ? 0.318 0.283 0.270 0.038  0.018  -0.040 101 ASP A OD2 
765  N N   . ALA A 102 ? 0.295 0.273 0.244 0.027  0.017  -0.037 102 ALA A N   
766  C CA  . ALA A 102 ? 0.275 0.255 0.225 0.023  0.014  -0.034 102 ALA A CA  
767  C C   . ALA A 102 ? 0.271 0.257 0.228 0.024  0.013  -0.032 102 ALA A C   
768  O O   . ALA A 102 ? 0.268 0.259 0.230 0.025  0.016  -0.032 102 ALA A O   
769  C CB  . ALA A 102 ? 0.280 0.259 0.224 0.020  0.013  -0.034 102 ALA A CB  
770  N N   . TYR A 103 ? 0.271 0.257 0.230 0.022  0.010  -0.030 103 TYR A N   
771  C CA  . TYR A 103 ? 0.254 0.247 0.220 0.021  0.010  -0.028 103 TYR A CA  
772  C C   . TYR A 103 ? 0.263 0.261 0.230 0.020  0.013  -0.027 103 TYR A C   
773  O O   . TYR A 103 ? 0.261 0.258 0.223 0.018  0.013  -0.027 103 TYR A O   
774  C CB  . TYR A 103 ? 0.252 0.244 0.217 0.019  0.006  -0.026 103 TYR A CB  
775  C CG  . TYR A 103 ? 0.257 0.254 0.228 0.018  0.006  -0.024 103 TYR A CG  
776  C CD1 . TYR A 103 ? 0.276 0.279 0.254 0.020  0.006  -0.024 103 TYR A CD1 
777  C CD2 . TYR A 103 ? 0.253 0.252 0.223 0.015  0.005  -0.022 103 TYR A CD2 
778  C CE1 . TYR A 103 ? 0.268 0.276 0.251 0.019  0.006  -0.023 103 TYR A CE1 
779  C CE2 . TYR A 103 ? 0.245 0.249 0.221 0.014  0.005  -0.021 103 TYR A CE2 
780  C CZ  . TYR A 103 ? 0.265 0.273 0.247 0.016  0.006  -0.022 103 TYR A CZ  
781  O OH  . TYR A 103 ? 0.275 0.288 0.263 0.014  0.006  -0.021 103 TYR A OH  
782  N N   . GLY A 104 ? 0.255 0.259 0.229 0.021  0.014  -0.027 104 GLY A N   
783  C CA  . GLY A 104 ? 0.258 0.267 0.234 0.020  0.018  -0.027 104 GLY A CA  
784  C C   . GLY A 104 ? 0.255 0.263 0.227 0.017  0.017  -0.025 104 GLY A C   
785  O O   . GLY A 104 ? 0.248 0.257 0.217 0.015  0.020  -0.024 104 GLY A O   
786  N N   . GLY A 105 ? 0.236 0.243 0.209 0.015  0.014  -0.023 105 GLY A N   
787  C CA  . GLY A 105 ? 0.242 0.249 0.213 0.012  0.013  -0.021 105 GLY A CA  
788  C C   . GLY A 105 ? 0.251 0.254 0.214 0.012  0.013  -0.021 105 GLY A C   
789  O O   . GLY A 105 ? 0.246 0.248 0.206 0.010  0.014  -0.019 105 GLY A O   
790  N N   . THR A 106 ? 0.246 0.244 0.205 0.013  0.011  -0.022 106 THR A N   
791  C CA  . THR A 106 ? 0.251 0.246 0.202 0.012  0.011  -0.023 106 THR A CA  
792  C C   . THR A 106 ? 0.268 0.263 0.215 0.012  0.015  -0.024 106 THR A C   
793  O O   . THR A 106 ? 0.262 0.256 0.203 0.011  0.015  -0.022 106 THR A O   
794  C CB  . THR A 106 ? 0.266 0.256 0.214 0.013  0.009  -0.025 106 THR A CB  
795  O OG1 . THR A 106 ? 0.272 0.262 0.224 0.012  0.006  -0.024 106 THR A OG1 
796  C CG2 . THR A 106 ? 0.276 0.264 0.217 0.012  0.008  -0.026 106 THR A CG2 
797  N N   . PHE A 107 ? 0.252 0.249 0.201 0.014  0.017  -0.025 107 PHE A N   
798  C CA  . PHE A 107 ? 0.267 0.264 0.212 0.015  0.022  -0.026 107 PHE A CA  
799  C C   . PHE A 107 ? 0.270 0.270 0.216 0.013  0.024  -0.023 107 PHE A C   
800  O O   . PHE A 107 ? 0.268 0.266 0.208 0.013  0.027  -0.023 107 PHE A O   
801  C CB  . PHE A 107 ? 0.276 0.275 0.226 0.018  0.025  -0.028 107 PHE A CB  
802  C CG  . PHE A 107 ? 0.283 0.283 0.231 0.018  0.030  -0.029 107 PHE A CG  
803  C CD1 . PHE A 107 ? 0.317 0.313 0.255 0.019  0.031  -0.031 107 PHE A CD1 
804  C CD2 . PHE A 107 ? 0.288 0.295 0.243 0.018  0.034  -0.028 107 PHE A CD2 
805  C CE1 . PHE A 107 ? 0.318 0.315 0.253 0.020  0.037  -0.031 107 PHE A CE1 
806  C CE2 . PHE A 107 ? 0.318 0.326 0.271 0.019  0.039  -0.029 107 PHE A CE2 
807  C CZ  . PHE A 107 ? 0.302 0.304 0.244 0.020  0.041  -0.030 107 PHE A CZ  
808  N N   . ARG A 108 ? 0.274 0.278 0.228 0.012  0.024  -0.022 108 ARG A N   
809  C CA  . ARG A 108 ? 0.263 0.269 0.220 0.010  0.027  -0.020 108 ARG A CA  
810  C C   . ARG A 108 ? 0.264 0.266 0.213 0.009  0.025  -0.017 108 ARG A C   
811  O O   . ARG A 108 ? 0.268 0.269 0.212 0.008  0.028  -0.016 108 ARG A O   
812  C CB  . ARG A 108 ? 0.258 0.269 0.224 0.010  0.026  -0.019 108 ARG A CB  
813  C CG  . ARG A 108 ? 0.271 0.284 0.241 0.007  0.029  -0.017 108 ARG A CG  
814  C CD  . ARG A 108 ? 0.285 0.303 0.265 0.006  0.028  -0.018 108 ARG A CD  
815  N NE  . ARG A 108 ? 0.269 0.285 0.249 0.006  0.022  -0.017 108 ARG A NE  
816  C CZ  . ARG A 108 ? 0.283 0.303 0.270 0.007  0.020  -0.018 108 ARG A CZ  
817  N NH1 . ARG A 108 ? 0.300 0.325 0.295 0.007  0.021  -0.020 108 ARG A NH1 
818  N NH2 . ARG A 108 ? 0.274 0.290 0.259 0.007  0.015  -0.018 108 ARG A NH2 
819  N N   . LEU A 109 ? 0.254 0.254 0.202 0.009  0.021  -0.017 109 LEU A N   
820  C CA  . LEU A 109 ? 0.257 0.254 0.199 0.008  0.019  -0.015 109 LEU A CA  
821  C C   . LEU A 109 ? 0.269 0.264 0.202 0.009  0.020  -0.015 109 LEU A C   
822  O O   . LEU A 109 ? 0.262 0.255 0.189 0.008  0.021  -0.013 109 LEU A O   
823  C CB  . LEU A 109 ? 0.257 0.253 0.200 0.007  0.014  -0.015 109 LEU A CB  
824  C CG  . LEU A 109 ? 0.254 0.249 0.193 0.007  0.012  -0.013 109 LEU A CG  
825  C CD1 . LEU A 109 ? 0.270 0.265 0.210 0.006  0.013  -0.010 109 LEU A CD1 
826  C CD2 . LEU A 109 ? 0.273 0.267 0.214 0.007  0.007  -0.013 109 LEU A CD2 
827  N N   . VAL A 110 ? 0.265 0.258 0.194 0.010  0.019  -0.018 110 VAL A N   
828  C CA  . VAL A 110 ? 0.278 0.269 0.198 0.011  0.019  -0.019 110 VAL A CA  
829  C C   . VAL A 110 ? 0.304 0.294 0.220 0.011  0.025  -0.018 110 VAL A C   
830  O O   . VAL A 110 ? 0.293 0.281 0.201 0.012  0.026  -0.017 110 VAL A O   
831  C CB  . VAL A 110 ? 0.284 0.273 0.202 0.012  0.017  -0.022 110 VAL A CB  
832  C CG1 . VAL A 110 ? 0.311 0.297 0.219 0.013  0.018  -0.024 110 VAL A CG1 
833  C CG2 . VAL A 110 ? 0.292 0.280 0.212 0.011  0.012  -0.023 110 VAL A CG2 
834  N N   . SER A 111 ? 0.289 0.282 0.211 0.012  0.029  -0.019 111 SER A N   
835  C CA  . SER A 111 ? 0.297 0.290 0.215 0.012  0.035  -0.019 111 SER A CA  
836  C C   . SER A 111 ? 0.301 0.295 0.221 0.011  0.038  -0.016 111 SER A C   
837  O O   . SER A 111 ? 0.309 0.301 0.223 0.011  0.043  -0.015 111 SER A O   
838  C CB  . SER A 111 ? 0.313 0.309 0.237 0.014  0.038  -0.022 111 SER A CB  
839  O OG  . SER A 111 ? 0.292 0.292 0.228 0.013  0.038  -0.022 111 SER A OG  
840  N N   . LYS A 112 ? 0.279 0.275 0.207 0.009  0.036  -0.015 112 LYS A N   
841  C CA  . LYS A 112 ? 0.282 0.279 0.214 0.007  0.040  -0.012 112 LYS A CA  
842  C C   . LYS A 112 ? 0.308 0.302 0.235 0.006  0.038  -0.009 112 LYS A C   
843  O O   . LYS A 112 ? 0.335 0.328 0.262 0.004  0.042  -0.006 112 LYS A O   
844  C CB  . LYS A 112 ? 0.283 0.286 0.228 0.006  0.041  -0.013 112 LYS A CB  
845  C CG  . LYS A 112 ? 0.286 0.294 0.237 0.007  0.043  -0.016 112 LYS A CG  
846  C CD  . LYS A 112 ? 0.313 0.320 0.259 0.008  0.049  -0.017 112 LYS A CD  
847  C CE  . LYS A 112 ? 0.331 0.343 0.285 0.010  0.051  -0.020 112 LYS A CE  
848  N NZ  . LYS A 112 ? 0.331 0.343 0.284 0.012  0.047  -0.022 112 LYS A NZ  
849  N N   . VAL A 113 ? 0.287 0.280 0.212 0.007  0.033  -0.009 113 VAL A N   
850  C CA  . VAL A 113 ? 0.290 0.279 0.210 0.007  0.030  -0.005 113 VAL A CA  
851  C C   . VAL A 113 ? 0.297 0.282 0.205 0.009  0.028  -0.005 113 VAL A C   
852  O O   . VAL A 113 ? 0.299 0.281 0.199 0.009  0.030  -0.003 113 VAL A O   
853  C CB  . VAL A 113 ? 0.275 0.266 0.202 0.006  0.026  -0.005 113 VAL A CB  
854  C CG1 . VAL A 113 ? 0.286 0.273 0.208 0.006  0.024  -0.002 113 VAL A CG1 
855  C CG2 . VAL A 113 ? 0.292 0.286 0.229 0.004  0.028  -0.006 113 VAL A CG2 
856  N N   . PHE A 114 ? 0.255 0.270 0.207 -0.002 -0.008 -0.002 114 PHE A N   
857  C CA  . PHE A 114 ? 0.251 0.276 0.195 0.001  0.001  -0.004 114 PHE A CA  
858  C C   . PHE A 114 ? 0.253 0.288 0.202 0.002  0.009  -0.002 114 PHE A C   
859  O O   . PHE A 114 ? 0.271 0.305 0.206 0.006  0.012  -0.002 114 PHE A O   
860  C CB  . PHE A 114 ? 0.270 0.294 0.210 0.003  0.003  -0.008 114 PHE A CB  
861  C CG  . PHE A 114 ? 0.269 0.275 0.195 0.006  0.006  -0.006 114 PHE A CG  
862  C CD1 . PHE A 114 ? 0.307 0.285 0.211 0.008  0.003  -0.006 114 PHE A CD1 
863  C CD2 . PHE A 114 ? 0.281 0.292 0.215 0.009  0.013  -0.005 114 PHE A CD2 
864  C CE1 . PHE A 114 ? 0.310 0.260 0.190 0.014  0.012  -0.003 114 PHE A CE1 
865  C CE2 . PHE A 114 ? 0.293 0.283 0.218 0.013  0.023  -0.002 114 PHE A CE2 
866  C CZ  . PHE A 114 ? 0.303 0.261 0.197 0.016  0.026  -0.000 114 PHE A CZ  
867  N N   . GLU A 115 ? 0.264 0.304 0.230 0.001  0.014  -0.001 115 GLU A N   
868  C CA  . GLU A 115 ? 0.280 0.318 0.242 0.006  0.030  0.002  115 GLU A CA  
869  C C   . GLU A 115 ? 0.299 0.328 0.254 0.007  0.038  0.009  115 GLU A C   
870  O O   . GLU A 115 ? 0.323 0.337 0.247 0.014  0.047  0.010  115 GLU A O   
871  C CB  . GLU A 115 ? 0.285 0.328 0.276 0.005  0.039  0.005  115 GLU A CB  
872  C CG  . GLU A 115 ? 0.342 0.371 0.317 0.014  0.062  0.009  115 GLU A CG  
873  C CD  . GLU A 115 ? 0.387 0.421 0.398 0.015  0.079  0.013  115 GLU A CD  
874  O OE1 . GLU A 115 ? 0.473 0.496 0.495 0.019  0.104  0.022  115 GLU A OE1 
875  O OE2 . GLU A 115 ? 0.373 0.419 0.406 0.012  0.068  0.009  115 GLU A OE2 
876  N N   A ARG A 116 ? 0.287 0.319 0.266 0.001  0.034  0.013  116 ARG A N   
877  N N   B ARG A 116 ? 0.282 0.314 0.262 0.001  0.034  0.013  116 ARG A N   
878  C CA  A ARG A 116 ? 0.313 0.337 0.293 0.001  0.041  0.020  116 ARG A CA  
879  C CA  B ARG A 116 ? 0.304 0.327 0.282 0.001  0.042  0.020  116 ARG A CA  
880  C C   A ARG A 116 ? 0.306 0.322 0.247 0.004  0.035  0.017  116 ARG A C   
881  C C   B ARG A 116 ? 0.302 0.318 0.241 0.005  0.036  0.017  116 ARG A C   
882  O O   A ARG A 116 ? 0.322 0.325 0.245 0.008  0.044  0.022  116 ARG A O   
883  O O   B ARG A 116 ? 0.321 0.323 0.241 0.009  0.046  0.021  116 ARG A O   
884  C CB  A ARG A 116 ? 0.325 0.352 0.345 -0.007 0.028  0.022  116 ARG A CB  
885  C CB  B ARG A 116 ? 0.305 0.331 0.320 -0.006 0.030  0.023  116 ARG A CB  
886  C CG  A ARG A 116 ? 0.384 0.404 0.417 -0.010 0.032  0.030  116 ARG A CG  
887  C CG  B ARG A 116 ? 0.347 0.364 0.355 -0.008 0.030  0.028  116 ARG A CG  
888  C CD  A ARG A 116 ? 0.392 0.409 0.466 -0.017 0.009  0.030  116 ARG A CD  
889  C CD  B ARG A 116 ? 0.368 0.380 0.415 -0.015 0.014  0.031  116 ARG A CD  
890  N NE  A ARG A 116 ? 0.456 0.457 0.497 -0.018 -0.008 0.027  116 ARG A NE  
891  N NE  B ARG A 116 ? 0.346 0.357 0.413 -0.018 -0.010 0.025  116 ARG A NE  
892  C CZ  A ARG A 116 ? 0.436 0.431 0.469 -0.018 0.000  0.032  116 ARG A CZ  
893  C CZ  B ARG A 116 ? 0.353 0.345 0.391 -0.017 -0.034 0.018  116 ARG A CZ  
894  N NH1 A ARG A 116 ? 0.489 0.489 0.544 -0.018 0.023  0.041  116 ARG A NH1 
895  N NH1 B ARG A 116 ? 0.363 0.341 0.358 -0.014 -0.036 0.017  116 ARG A NH1 
896  N NH2 A ARG A 116 ? 0.436 0.416 0.440 -0.017 -0.013 0.030  116 ARG A NH2 
897  N NH2 B ARG A 116 ? 0.295 0.277 0.347 -0.018 -0.055 0.014  116 ARG A NH2 
898  N N   . TRP A 117 ? 0.283 0.303 0.214 0.004  0.022  0.010  117 TRP A N   
899  C CA  . TRP A 117 ? 0.291 0.307 0.202 0.008  0.014  0.008  117 TRP A CA  
900  C C   . TRP A 117 ? 0.307 0.319 0.202 0.014  0.011  0.003  117 TRP A C   
901  O O   . TRP A 117 ? 0.333 0.343 0.226 0.017  -0.000 -0.001 117 TRP A O   
902  C CB  . TRP A 117 ? 0.286 0.303 0.204 0.006  0.007  0.006  117 TRP A CB  
903  C CG  . TRP A 117 ? 0.279 0.286 0.195 0.003  0.004  0.010  117 TRP A CG  
904  C CD1 . TRP A 117 ? 0.281 0.280 0.206 -0.001 -0.002 0.011  117 TRP A CD1 
905  C CD2 . TRP A 117 ? 0.282 0.281 0.186 0.005  0.004  0.012  117 TRP A CD2 
906  N NE1 . TRP A 117 ? 0.284 0.268 0.200 -0.002 -0.007 0.014  117 TRP A NE1 
907  C CE2 . TRP A 117 ? 0.285 0.271 0.188 0.002  -0.001 0.015  117 TRP A CE2 
908  C CE3 . TRP A 117 ? 0.288 0.288 0.185 0.010  0.004  0.012  117 TRP A CE3 
909  C CZ2 . TRP A 117 ? 0.299 0.273 0.189 0.004  -0.002 0.018  117 TRP A CZ2 
910  C CZ3 . TRP A 117 ? 0.300 0.290 0.188 0.012  0.003  0.015  117 TRP A CZ3 
911  C CH2 . TRP A 117 ? 0.311 0.289 0.194 0.008  0.002  0.019  117 TRP A CH2 
912  N N   . GLY A 118 ? 0.313 0.318 0.198 0.017  0.018  0.002  118 GLY A N   
913  C CA  . GLY A 118 ? 0.347 0.333 0.202 0.026  0.013  -0.002 118 GLY A CA  
914  C C   . GLY A 118 ? 0.338 0.331 0.203 0.026  0.001  -0.010 118 GLY A C   
915  O O   . GLY A 118 ? 0.360 0.331 0.199 0.034  -0.012 -0.015 118 GLY A O   
916  N N   . VAL A 119 ? 0.298 0.312 0.193 0.019  0.004  -0.011 119 VAL A N   
917  C CA  . VAL A 119 ? 0.293 0.314 0.200 0.018  -0.004 -0.017 119 VAL A CA  
918  C C   . VAL A 119 ? 0.310 0.327 0.210 0.020  0.006  -0.017 119 VAL A C   
919  O O   . VAL A 119 ? 0.322 0.349 0.237 0.016  0.018  -0.012 119 VAL A O   
920  C CB  . VAL A 119 ? 0.268 0.304 0.204 0.012  -0.004 -0.017 119 VAL A CB  
921  C CG1 . VAL A 119 ? 0.277 0.317 0.228 0.012  -0.008 -0.022 119 VAL A CG1 
922  C CG2 . VAL A 119 ? 0.286 0.323 0.232 0.012  -0.008 -0.015 119 VAL A CG2 
923  N N   . SER A 120 ? 0.335 0.336 0.213 0.026  -0.000 -0.022 120 SER A N   
924  C CA  . SER A 120 ? 0.359 0.353 0.227 0.030  0.011  -0.023 120 SER A CA  
925  C C   . SER A 120 ? 0.327 0.342 0.227 0.023  0.005  -0.027 120 SER A C   
926  O O   . SER A 120 ? 0.306 0.330 0.225 0.019  -0.007 -0.030 120 SER A O   
927  C CB  . SER A 120 ? 0.427 0.382 0.245 0.042  0.007  -0.027 120 SER A CB  
928  O OG  . SER A 120 ? 0.489 0.436 0.305 0.043  -0.021 -0.036 120 SER A OG  
929  N N   . TRP A 121 ? 0.306 0.323 0.211 0.024  0.016  -0.026 121 TRP A N   
930  C CA  . TRP A 121 ? 0.295 0.325 0.222 0.019  0.012  -0.030 121 TRP A CA  
931  C C   . TRP A 121 ? 0.307 0.330 0.228 0.024  0.021  -0.031 121 TRP A C   
932  O O   . TRP A 121 ? 0.326 0.339 0.239 0.029  0.039  -0.026 121 TRP A O   
933  C CB  . TRP A 121 ? 0.272 0.318 0.225 0.012  0.013  -0.026 121 TRP A CB  
934  C CG  . TRP A 121 ? 0.265 0.315 0.234 0.011  0.022  -0.020 121 TRP A CG  
935  C CD1 . TRP A 121 ? 0.280 0.328 0.252 0.011  0.028  -0.014 121 TRP A CD1 
936  C CD2 . TRP A 121 ? 0.265 0.320 0.259 0.011  0.026  -0.018 121 TRP A CD2 
937  N NE1 . TRP A 121 ? 0.278 0.332 0.282 0.010  0.036  -0.008 121 TRP A NE1 
938  C CE2 . TRP A 121 ? 0.262 0.320 0.281 0.010  0.034  -0.011 121 TRP A CE2 
939  C CE3 . TRP A 121 ? 0.269 0.325 0.270 0.012  0.024  -0.022 121 TRP A CE3 
940  C CZ2 . TRP A 121 ? 0.277 0.340 0.337 0.010  0.040  -0.007 121 TRP A CZ2 
941  C CZ3 . TRP A 121 ? 0.301 0.361 0.334 0.013  0.029  -0.019 121 TRP A CZ3 
942  C CH2 . TRP A 121 ? 0.278 0.343 0.346 0.012  0.036  -0.011 121 TRP A CH2 
943  N N   . ASP A 122 ? 0.308 0.337 0.239 0.022  0.014  -0.036 122 ASP A N   
944  C CA  . ASP A 122 ? 0.311 0.336 0.242 0.025  0.022  -0.037 122 ASP A CA  
945  C C   . ASP A 122 ? 0.281 0.320 0.238 0.019  0.015  -0.039 122 ASP A C   
946  O O   . ASP A 122 ? 0.274 0.315 0.235 0.015  0.006  -0.041 122 ASP A O   
947  C CB  . ASP A 122 ? 0.345 0.346 0.244 0.033  0.016  -0.044 122 ASP A CB  
948  C CG  . ASP A 122 ? 0.410 0.380 0.265 0.044  0.026  -0.041 122 ASP A CG  
949  O OD1 . ASP A 122 ? 0.427 0.388 0.278 0.050  0.050  -0.035 122 ASP A OD1 
950  O OD2 . ASP A 122 ? 0.432 0.384 0.262 0.047  0.012  -0.044 122 ASP A OD2 
951  N N   . ALA A 123 ? 0.267 0.311 0.241 0.020  0.021  -0.037 123 ALA A N   
952  C CA  . ALA A 123 ? 0.257 0.304 0.244 0.017  0.013  -0.039 123 ALA A CA  
953  C C   . ALA A 123 ? 0.271 0.311 0.249 0.020  0.015  -0.044 123 ALA A C   
954  O O   . ALA A 123 ? 0.295 0.329 0.268 0.027  0.026  -0.044 123 ALA A O   
955  C CB  . ALA A 123 ? 0.273 0.325 0.288 0.016  0.012  -0.035 123 ALA A CB  
956  N N   . VAL A 124 ? 0.262 0.298 0.236 0.018  0.007  -0.048 124 VAL A N   
957  C CA  . VAL A 124 ? 0.291 0.319 0.258 0.020  0.005  -0.054 124 VAL A CA  
958  C C   . VAL A 124 ? 0.273 0.298 0.248 0.018  0.003  -0.055 124 VAL A C   
959  O O   . VAL A 124 ? 0.269 0.290 0.245 0.015  0.002  -0.052 124 VAL A O   
960  C CB  . VAL A 124 ? 0.298 0.320 0.260 0.018  -0.004 -0.058 124 VAL A CB  
961  C CG1 . VAL A 124 ? 0.354 0.365 0.312 0.020  -0.011 -0.065 124 VAL A CG1 
962  C CG2 . VAL A 124 ? 0.319 0.335 0.263 0.022  -0.006 -0.058 124 VAL A CG2 
963  N N   . ASP A 125 ? 0.270 0.289 0.242 0.021  0.003  -0.058 125 ASP A N   
964  C CA  . ASP A 125 ? 0.280 0.291 0.253 0.020  0.001  -0.060 125 ASP A CA  
965  C C   . ASP A 125 ? 0.270 0.274 0.245 0.016  0.001  -0.061 125 ASP A C   
966  O O   . ASP A 125 ? 0.291 0.292 0.270 0.016  -0.003 -0.066 125 ASP A O   
967  C CB  . ASP A 125 ? 0.299 0.306 0.271 0.026  0.002  -0.063 125 ASP A CB  
968  C CG  . ASP A 125 ? 0.328 0.322 0.298 0.025  -0.001 -0.065 125 ASP A CG  
969  O OD1 . ASP A 125 ? 0.319 0.302 0.283 0.023  -0.001 -0.062 125 ASP A OD1 
970  O OD2 . ASP A 125 ? 0.336 0.327 0.305 0.030  -0.000 -0.068 125 ASP A OD2 
971  N N   . LEU A 126 ? 0.279 0.274 0.254 0.014  0.006  -0.056 126 LEU A N   
972  C CA  . LEU A 126 ? 0.272 0.261 0.263 0.010  0.014  -0.055 126 LEU A CA  
973  C C   . LEU A 126 ? 0.296 0.269 0.290 0.011  0.019  -0.056 126 LEU A C   
974  O O   . LEU A 126 ? 0.308 0.276 0.327 0.007  0.027  -0.054 126 LEU A O   
975  C CB  . LEU A 126 ? 0.302 0.278 0.286 0.011  0.025  -0.048 126 LEU A CB  
976  C CG  . LEU A 126 ? 0.301 0.292 0.283 0.010  0.020  -0.046 126 LEU A CG  
977  C CD1 . LEU A 126 ? 0.350 0.322 0.320 0.011  0.032  -0.040 126 LEU A CD1 
978  C CD2 . LEU A 126 ? 0.324 0.334 0.330 0.007  0.012  -0.050 126 LEU A CD2 
979  N N   . SER A 127 ? 0.306 0.271 0.280 0.015  0.016  -0.058 127 SER A N   
980  C CA  . SER A 127 ? 0.327 0.276 0.300 0.016  0.019  -0.060 127 SER A CA  
981  C C   . SER A 127 ? 0.331 0.292 0.322 0.013  0.010  -0.067 127 SER A C   
982  O O   . SER A 127 ? 0.364 0.314 0.361 0.013  0.011  -0.069 127 SER A O   
983  C CB  . SER A 127 ? 0.353 0.286 0.298 0.022  0.014  -0.060 127 SER A CB  
984  O OG  . SER A 127 ? 0.391 0.301 0.310 0.026  0.016  -0.055 127 SER A OG  
985  N N   . ASN A 128 ? 0.293 0.312 0.394 0.019  -0.027 -0.038 128 ASN A N   
986  C CA  . ASN A 128 ? 0.311 0.314 0.406 0.035  -0.021 -0.055 128 ASN A CA  
987  C C   . ASN A 128 ? 0.310 0.302 0.380 0.031  -0.023 -0.069 128 ASN A C   
988  O O   . ASN A 128 ? 0.316 0.316 0.369 0.032  -0.016 -0.073 128 ASN A O   
989  C CB  . ASN A 128 ? 0.314 0.336 0.415 0.052  -0.006 -0.050 128 ASN A CB  
990  C CG  . ASN A 128 ? 0.376 0.377 0.455 0.079  0.004  -0.068 128 ASN A CG  
991  O OD1 . ASN A 128 ? 0.394 0.357 0.449 0.078  -0.008 -0.088 128 ASN A OD1 
992  N ND2 . ASN A 128 ? 0.364 0.390 0.449 0.103  0.023  -0.057 128 ASN A ND2 
993  N N   . PRO A 129 ? 0.339 0.317 0.411 0.023  -0.035 -0.071 129 PRO A N   
994  C CA  . PRO A 129 ? 0.351 0.329 0.408 0.018  -0.038 -0.077 129 PRO A CA  
995  C C   . PRO A 129 ? 0.373 0.332 0.403 0.028  -0.037 -0.096 129 PRO A C   
996  O O   . PRO A 129 ? 0.359 0.325 0.373 0.026  -0.036 -0.099 129 PRO A O   
997  C CB  . PRO A 129 ? 0.368 0.342 0.449 0.005  -0.055 -0.064 129 PRO A CB  
998  C CG  . PRO A 129 ? 0.363 0.348 0.467 0.003  -0.053 -0.047 129 PRO A CG  
999  C CD  . PRO A 129 ? 0.359 0.331 0.457 0.016  -0.046 -0.058 129 PRO A CD  
1000 N N   . GLU A 130 ? 0.413 0.346 0.431 0.045  -0.037 -0.109 130 GLU A N   
1001 C CA  . GLU A 130 ? 0.455 0.371 0.433 0.063  -0.032 -0.126 130 GLU A CA  
1002 C C   . GLU A 130 ? 0.432 0.386 0.407 0.068  -0.011 -0.117 130 GLU A C   
1003 O O   . GLU A 130 ? 0.436 0.388 0.385 0.071  -0.009 -0.124 130 GLU A O   
1004 C CB  . GLU A 130 ? 0.532 0.413 0.485 0.093  -0.028 -0.140 130 GLU A CB  
1005 C CG  . GLU A 130 ? 0.623 0.441 0.557 0.092  -0.058 -0.156 130 GLU A CG  
1006 C CD  . GLU A 130 ? 0.745 0.510 0.638 0.130  -0.058 -0.175 130 GLU A CD  
1007 O OE1 . GLU A 130 ? 0.773 0.535 0.621 0.165  -0.036 -0.186 130 GLU A OE1 
1008 O OE2 . GLU A 130 ? 0.925 0.647 0.826 0.128  -0.079 -0.177 130 GLU A OE2 
1009 N N   . ALA A 131 ? 0.381 0.365 0.383 0.067  0.001  -0.099 131 ALA A N   
1010 C CA  . ALA A 131 ? 0.369 0.387 0.376 0.065  0.013  -0.083 131 ALA A CA  
1011 C C   . ALA A 131 ? 0.333 0.348 0.331 0.045  0.003  -0.084 131 ALA A C   
1012 O O   . ALA A 131 ? 0.365 0.390 0.352 0.044  0.007  -0.079 131 ALA A O   
1013 C CB  . ALA A 131 ? 0.350 0.397 0.395 0.060  0.017  -0.059 131 ALA A CB  
1014 N N   . VAL A 132 ? 0.310 0.314 0.313 0.033  -0.009 -0.085 132 VAL A N   
1015 C CA  . VAL A 132 ? 0.305 0.305 0.293 0.024  -0.014 -0.084 132 VAL A CA  
1016 C C   . VAL A 132 ? 0.326 0.321 0.297 0.028  -0.015 -0.095 132 VAL A C   
1017 O O   . VAL A 132 ? 0.346 0.343 0.301 0.028  -0.014 -0.093 132 VAL A O   
1018 C CB  . VAL A 132 ? 0.307 0.306 0.301 0.020  -0.019 -0.079 132 VAL A CB  
1019 C CG1 . VAL A 132 ? 0.327 0.321 0.298 0.023  -0.020 -0.077 132 VAL A CG1 
1020 C CG2 . VAL A 132 ? 0.299 0.299 0.303 0.015  -0.022 -0.068 132 VAL A CG2 
1021 N N   . ARG A 133 ? 0.342 0.326 0.315 0.030  -0.023 -0.104 133 ARG A N   
1022 C CA  . ARG A 133 ? 0.356 0.331 0.312 0.030  -0.032 -0.112 133 ARG A CA  
1023 C C   . ARG A 133 ? 0.383 0.356 0.309 0.041  -0.023 -0.119 133 ARG A C   
1024 O O   . ARG A 133 ? 0.366 0.344 0.278 0.040  -0.025 -0.117 133 ARG A O   
1025 C CB  . ARG A 133 ? 0.395 0.344 0.356 0.026  -0.052 -0.118 133 ARG A CB  
1026 C CG  . ARG A 133 ? 0.432 0.378 0.400 0.012  -0.075 -0.113 133 ARG A CG  
1027 C CD  . ARG A 133 ? 0.448 0.358 0.420 0.003  -0.103 -0.117 133 ARG A CD  
1028 N NE  . ARG A 133 ? 0.403 0.335 0.425 -0.013 -0.111 -0.091 133 ARG A NE  
1029 C CZ  . ARG A 133 ? 0.401 0.325 0.441 -0.014 -0.111 -0.087 133 ARG A CZ  
1030 N NH1 . ARG A 133 ? 0.376 0.328 0.461 -0.029 -0.117 -0.058 133 ARG A NH1 
1031 N NH2 . ARG A 133 ? 0.418 0.305 0.432 0.001  -0.107 -0.108 133 ARG A NH2 
1032 N N   . THR A 134 ? 0.404 0.378 0.323 0.056  -0.010 -0.121 134 THR A N   
1033 C CA  . THR A 134 ? 0.441 0.424 0.331 0.071  0.002  -0.121 134 THR A CA  
1034 C C   . THR A 134 ? 0.401 0.415 0.307 0.062  0.011  -0.099 134 THR A C   
1035 O O   . THR A 134 ? 0.427 0.458 0.317 0.070  0.022  -0.090 134 THR A O   
1036 C CB  . THR A 134 ? 0.509 0.489 0.382 0.099  0.018  -0.125 134 THR A CB  
1037 O OG1 . THR A 134 ? 0.481 0.490 0.392 0.100  0.031  -0.106 134 THR A OG1 
1038 C CG2 . THR A 134 ? 0.620 0.549 0.467 0.109  0.001  -0.150 134 THR A CG2 
1039 N N   . ALA A 135 ? 0.349 0.368 0.282 0.045  0.006  -0.088 135 ALA A N   
1040 C CA  . ALA A 135 ? 0.350 0.380 0.291 0.033  0.004  -0.067 135 ALA A CA  
1041 C C   . ALA A 135 ? 0.334 0.347 0.256 0.028  -0.006 -0.072 135 ALA A C   
1042 O O   . ALA A 135 ? 0.352 0.361 0.271 0.020  -0.011 -0.058 135 ALA A O   
1043 C CB  . ALA A 135 ? 0.339 0.366 0.302 0.020  -0.005 -0.057 135 ALA A CB  
1044 N N   . ILE A 136 ? 0.351 0.353 0.265 0.032  -0.010 -0.087 136 ILE A N   
1045 C CA  . ILE A 136 ? 0.368 0.361 0.268 0.032  -0.017 -0.086 136 ILE A CA  
1046 C C   . ILE A 136 ? 0.372 0.372 0.256 0.035  -0.015 -0.081 136 ILE A C   
1047 O O   . ILE A 136 ? 0.391 0.400 0.263 0.042  -0.010 -0.087 136 ILE A O   
1048 C CB  . ILE A 136 ? 0.398 0.395 0.306 0.034  -0.023 -0.093 136 ILE A CB  
1049 C CG1 . ILE A 136 ? 0.424 0.423 0.352 0.033  -0.022 -0.090 136 ILE A CG1 
1050 C CG2 . ILE A 136 ? 0.416 0.417 0.318 0.038  -0.028 -0.086 136 ILE A CG2 
1051 C CD1 . ILE A 136 ? 0.462 0.457 0.384 0.041  -0.019 -0.082 136 ILE A CD1 
1052 N N   . ARG A 137 ? 0.373 0.364 0.250 0.032  -0.020 -0.071 137 ARG A N   
1053 C CA  . ARG A 137 ? 0.409 0.406 0.273 0.033  -0.021 -0.061 137 ARG A CA  
1054 C C   . ARG A 137 ? 0.414 0.401 0.269 0.039  -0.028 -0.062 137 ARG A C   
1055 O O   . ARG A 137 ? 0.388 0.364 0.247 0.046  -0.030 -0.065 137 ARG A O   
1056 C CB  . ARG A 137 ? 0.437 0.429 0.305 0.022  -0.025 -0.039 137 ARG A CB  
1057 C CG  . ARG A 137 ? 0.452 0.466 0.342 0.015  -0.018 -0.026 137 ARG A CG  
1058 C CD  . ARG A 137 ? 0.501 0.514 0.402 -0.001 -0.030 0.006  137 ARG A CD  
1059 N NE  . ARG A 137 ? 0.521 0.555 0.457 -0.017 -0.034 0.033  137 ARG A NE  
1060 C CZ  . ARG A 137 ? 0.574 0.608 0.531 -0.040 -0.054 0.071  137 ARG A CZ  
1061 N NH1 . ARG A 137 ? 0.590 0.602 0.535 -0.048 -0.069 0.085  137 ARG A NH1 
1062 N NH2 . ARG A 137 ? 0.564 0.621 0.561 -0.058 -0.063 0.100  137 ARG A NH2 
1063 N N   . PRO A 138 ? 0.496 0.455 0.260 0.019  -0.036 -0.048 138 PRO A N   
1064 C CA  . PRO A 138 ? 0.501 0.462 0.266 0.021  -0.046 -0.045 138 PRO A CA  
1065 C C   . PRO A 138 ? 0.480 0.440 0.255 0.022  -0.046 -0.037 138 PRO A C   
1066 O O   . PRO A 138 ? 0.479 0.442 0.265 0.023  -0.053 -0.037 138 PRO A O   
1067 C CB  . PRO A 138 ? 0.534 0.491 0.275 0.024  -0.049 -0.043 138 PRO A CB  
1068 C CG  . PRO A 138 ? 0.560 0.516 0.291 0.022  -0.043 -0.050 138 PRO A CG  
1069 C CD  . PRO A 138 ? 0.534 0.491 0.277 0.020  -0.033 -0.049 138 PRO A CD  
1070 N N   A GLU A 139 ? 0.486 0.441 0.259 0.021  -0.038 -0.032 139 GLU A N   
1071 N N   B GLU A 139 ? 0.464 0.420 0.238 0.021  -0.038 -0.032 139 GLU A N   
1072 C CA  A GLU A 139 ? 0.472 0.424 0.253 0.021  -0.036 -0.024 139 GLU A CA  
1073 C CA  B GLU A 139 ? 0.438 0.391 0.220 0.021  -0.037 -0.024 139 GLU A CA  
1074 C C   A GLU A 139 ? 0.419 0.375 0.222 0.019  -0.033 -0.026 139 GLU A C   
1075 C C   B GLU A 139 ? 0.402 0.359 0.205 0.019  -0.033 -0.026 139 GLU A C   
1076 O O   A GLU A 139 ? 0.398 0.351 0.207 0.019  -0.032 -0.021 139 GLU A O   
1077 O O   B GLU A 139 ? 0.386 0.340 0.195 0.018  -0.032 -0.021 139 GLU A O   
1078 C CB  A GLU A 139 ? 0.511 0.457 0.282 0.018  -0.028 -0.017 139 GLU A CB  
1079 C CB  B GLU A 139 ? 0.454 0.400 0.221 0.019  -0.030 -0.017 139 GLU A CB  
1080 C CG  A GLU A 139 ? 0.572 0.515 0.320 0.019  -0.026 -0.015 139 GLU A CG  
1081 C CG  B GLU A 139 ? 0.477 0.419 0.222 0.021  -0.033 -0.014 139 GLU A CG  
1082 C CD  A GLU A 139 ? 0.591 0.537 0.334 0.017  -0.019 -0.021 139 GLU A CD  
1083 C CD  B GLU A 139 ? 0.483 0.426 0.216 0.020  -0.028 -0.020 139 GLU A CD  
1084 O OE1 A GLU A 139 ? 0.626 0.573 0.374 0.014  -0.010 -0.019 139 GLU A OE1 
1085 O OE1 B GLU A 139 ? 0.456 0.405 0.200 0.018  -0.023 -0.026 139 GLU A OE1 
1086 O OE2 A GLU A 139 ? 0.622 0.570 0.357 0.018  -0.022 -0.026 139 GLU A OE2 
1087 O OE2 B GLU A 139 ? 0.506 0.446 0.218 0.021  -0.029 -0.017 139 GLU A OE2 
1088 N N   . THR A 140 ? 0.383 0.344 0.194 0.017  -0.031 -0.033 140 THR A N   
1089 C CA  . THR A 140 ? 0.368 0.332 0.198 0.015  -0.028 -0.035 140 THR A CA  
1090 C C   . THR A 140 ? 0.372 0.338 0.215 0.016  -0.034 -0.034 140 THR A C   
1091 O O   . THR A 140 ? 0.378 0.348 0.223 0.017  -0.041 -0.038 140 THR A O   
1092 C CB  . THR A 140 ? 0.368 0.335 0.204 0.014  -0.025 -0.042 140 THR A CB  
1093 O OG1 . THR A 140 ? 0.367 0.332 0.191 0.014  -0.019 -0.043 140 THR A OG1 
1094 C CG2 . THR A 140 ? 0.351 0.319 0.204 0.012  -0.022 -0.043 140 THR A CG2 
1095 N N   . VAL A 141 ? 0.346 0.310 0.197 0.016  -0.031 -0.029 141 VAL A N   
1096 C CA  . VAL A 141 ? 0.343 0.309 0.206 0.017  -0.036 -0.028 141 VAL A CA  
1097 C C   . VAL A 141 ? 0.335 0.305 0.214 0.015  -0.033 -0.032 141 VAL A C   
1098 O O   . VAL A 141 ? 0.325 0.299 0.215 0.016  -0.037 -0.033 141 VAL A O   
1099 C CB  . VAL A 141 ? 0.356 0.318 0.217 0.019  -0.036 -0.021 141 VAL A CB  
1100 C CG1 . VAL A 141 ? 0.416 0.373 0.261 0.022  -0.040 -0.018 141 VAL A CG1 
1101 C CG2 . VAL A 141 ? 0.363 0.319 0.224 0.017  -0.029 -0.018 141 VAL A CG2 
1102 N N   . ALA A 142 ? 0.323 0.292 0.204 0.013  -0.027 -0.033 142 ALA A N   
1103 C CA  . ALA A 142 ? 0.300 0.272 0.195 0.011  -0.024 -0.035 142 ALA A CA  
1104 C C   . ALA A 142 ? 0.312 0.283 0.207 0.009  -0.018 -0.038 142 ALA A C   
1105 O O   . ALA A 142 ? 0.314 0.283 0.199 0.009  -0.015 -0.036 142 ALA A O   
1106 C CB  . ALA A 142 ? 0.303 0.273 0.205 0.011  -0.022 -0.030 142 ALA A CB  
1107 N N   . ILE A 143 ? 0.305 0.277 0.210 0.008  -0.018 -0.041 143 ILE A N   
1108 C CA  . ILE A 143 ? 0.295 0.267 0.203 0.007  -0.013 -0.044 143 ILE A CA  
1109 C C   . ILE A 143 ? 0.279 0.250 0.197 0.006  -0.010 -0.041 143 ILE A C   
1110 O O   . ILE A 143 ? 0.279 0.251 0.205 0.005  -0.013 -0.041 143 ILE A O   
1111 C CB  . ILE A 143 ? 0.307 0.278 0.216 0.007  -0.014 -0.050 143 ILE A CB  
1112 C CG1 . ILE A 143 ? 0.353 0.324 0.251 0.008  -0.018 -0.054 143 ILE A CG1 
1113 C CG2 . ILE A 143 ? 0.314 0.283 0.226 0.007  -0.009 -0.052 143 ILE A CG2 
1114 C CD1 . ILE A 143 ? 0.378 0.347 0.276 0.007  -0.020 -0.061 143 ILE A CD1 
1115 N N   . TRP A 144 ? 0.269 0.241 0.187 0.006  -0.006 -0.038 144 TRP A N   
1116 C CA  . TRP A 144 ? 0.279 0.250 0.205 0.005  -0.003 -0.035 144 TRP A CA  
1117 C C   . TRP A 144 ? 0.279 0.251 0.211 0.005  -0.001 -0.038 144 TRP A C   
1118 O O   . TRP A 144 ? 0.283 0.256 0.212 0.006  0.003  -0.039 144 TRP A O   
1119 C CB  . TRP A 144 ? 0.284 0.255 0.206 0.004  -0.000 -0.030 144 TRP A CB  
1120 C CG  . TRP A 144 ? 0.272 0.243 0.201 0.003  0.001  -0.027 144 TRP A CG  
1121 C CD1 . TRP A 144 ? 0.275 0.248 0.211 0.002  0.003  -0.028 144 TRP A CD1 
1122 C CD2 . TRP A 144 ? 0.267 0.236 0.197 0.002  -0.001 -0.024 144 TRP A CD2 
1123 N NE1 . TRP A 144 ? 0.274 0.246 0.215 0.001  0.003  -0.025 144 TRP A NE1 
1124 C CE2 . TRP A 144 ? 0.271 0.240 0.207 0.001  0.001  -0.022 144 TRP A CE2 
1125 C CE3 . TRP A 144 ? 0.295 0.261 0.220 0.003  -0.004 -0.021 144 TRP A CE3 
1126 C CZ2 . TRP A 144 ? 0.278 0.244 0.216 -0.000 -0.000 -0.020 144 TRP A CZ2 
1127 C CZ3 . TRP A 144 ? 0.287 0.249 0.214 0.003  -0.005 -0.019 144 TRP A CZ3 
1128 C CH2 . TRP A 144 ? 0.277 0.239 0.210 0.001  -0.003 -0.018 144 TRP A CH2 
1129 N N   . VAL A 145 ? 0.276 0.247 0.216 0.004  -0.002 -0.039 145 VAL A N   
1130 C CA  . VAL A 145 ? 0.265 0.234 0.210 0.005  -0.000 -0.041 145 VAL A CA  
1131 C C   . VAL A 145 ? 0.268 0.238 0.220 0.005  0.001  -0.038 145 VAL A C   
1132 O O   . VAL A 145 ? 0.280 0.250 0.234 0.003  -0.000 -0.035 145 VAL A O   
1133 C CB  . VAL A 145 ? 0.291 0.257 0.239 0.004  -0.003 -0.045 145 VAL A CB  
1134 C CG1 . VAL A 145 ? 0.309 0.271 0.260 0.005  -0.001 -0.047 145 VAL A CG1 
1135 C CG2 . VAL A 145 ? 0.332 0.298 0.273 0.004  -0.006 -0.049 145 VAL A CG2 
1136 N N   . GLU A 146 ? 0.250 0.221 0.203 0.006  0.004  -0.038 146 GLU A N   
1137 C CA  . GLU A 146 ? 0.261 0.231 0.220 0.006  0.005  -0.035 146 GLU A CA  
1138 C C   . GLU A 146 ? 0.260 0.226 0.222 0.008  0.005  -0.039 146 GLU A C   
1139 O O   . GLU A 146 ? 0.274 0.240 0.233 0.010  0.006  -0.042 146 GLU A O   
1140 C CB  . GLU A 146 ? 0.256 0.231 0.217 0.007  0.007  -0.033 146 GLU A CB  
1141 C CG  . GLU A 146 ? 0.277 0.255 0.236 0.004  0.007  -0.030 146 GLU A CG  
1142 C CD  . GLU A 146 ? 0.263 0.246 0.226 0.004  0.009  -0.028 146 GLU A CD  
1143 O OE1 . GLU A 146 ? 0.257 0.243 0.225 0.006  0.010  -0.028 146 GLU A OE1 
1144 O OE2 . GLU A 146 ? 0.278 0.262 0.238 0.001  0.010  -0.025 146 GLU A OE2 
1145 N N   . THR A 147 ? 0.262 0.224 0.227 0.007  0.004  -0.037 147 THR A N   
1146 C CA  . THR A 147 ? 0.261 0.217 0.228 0.009  0.004  -0.039 147 THR A CA  
1147 C C   . THR A 147 ? 0.262 0.215 0.232 0.008  0.003  -0.036 147 THR A C   
1148 O O   . THR A 147 ? 0.263 0.215 0.234 0.005  0.003  -0.035 147 THR A O   
1149 C CB  . THR A 147 ? 0.277 0.227 0.242 0.008  0.003  -0.044 147 THR A CB  
1150 O OG1 . THR A 147 ? 0.281 0.224 0.246 0.010  0.003  -0.046 147 THR A OG1 
1151 C CG2 . THR A 147 ? 0.273 0.223 0.240 0.004  0.001  -0.044 147 THR A CG2 
1152 N N   . PRO A 148 ? 0.272 0.224 0.244 0.011  0.004  -0.035 148 PRO A N   
1153 C CA  . PRO A 148 ? 0.263 0.219 0.236 0.015  0.005  -0.036 148 PRO A CA  
1154 C C   . PRO A 148 ? 0.270 0.235 0.243 0.014  0.007  -0.035 148 PRO A C   
1155 O O   . PRO A 148 ? 0.258 0.226 0.231 0.011  0.006  -0.032 148 PRO A O   
1156 C CB  . PRO A 148 ? 0.283 0.236 0.259 0.018  0.005  -0.033 148 PRO A CB  
1157 C CG  . PRO A 148 ? 0.273 0.217 0.247 0.015  0.003  -0.031 148 PRO A CG  
1158 C CD  . PRO A 148 ? 0.282 0.230 0.256 0.010  0.003  -0.031 148 PRO A CD  
1159 N N   . THR A 149 ? 0.250 0.221 0.224 0.017  0.009  -0.037 149 THR A N   
1160 C CA  . THR A 149 ? 0.251 0.231 0.225 0.016  0.010  -0.036 149 THR A CA  
1161 C C   . THR A 149 ? 0.238 0.223 0.216 0.016  0.010  -0.032 149 THR A C   
1162 O O   . THR A 149 ? 0.244 0.230 0.227 0.019  0.009  -0.032 149 THR A O   
1163 C CB  . THR A 149 ? 0.256 0.239 0.227 0.018  0.013  -0.039 149 THR A CB  
1164 O OG1 . THR A 149 ? 0.259 0.244 0.234 0.023  0.015  -0.041 149 THR A OG1 
1165 C CG2 . THR A 149 ? 0.278 0.255 0.242 0.018  0.013  -0.043 149 THR A CG2 
1166 N N   . ASN A 150 ? 0.242 0.233 0.220 0.013  0.011  -0.030 150 ASN A N   
1167 C CA  . ASN A 150 ? 0.233 0.232 0.217 0.011  0.011  -0.028 150 ASN A CA  
1168 C C   . ASN A 150 ? 0.234 0.243 0.221 0.012  0.014  -0.029 150 ASN A C   
1169 O O   . ASN A 150 ? 0.251 0.263 0.234 0.009  0.017  -0.028 150 ASN A O   
1170 C CB  . ASN A 150 ? 0.236 0.233 0.217 0.007  0.009  -0.025 150 ASN A CB  
1171 C CG  . ASN A 150 ? 0.232 0.236 0.218 0.004  0.009  -0.023 150 ASN A CG  
1172 O OD1 . ASN A 150 ? 0.239 0.250 0.231 0.007  0.009  -0.023 150 ASN A OD1 
1173 N ND2 . ASN A 150 ? 0.245 0.246 0.228 -0.000 0.007  -0.020 150 ASN A ND2 
1174 N N   . PRO A 151 ? 0.237 0.254 0.231 0.016  0.015  -0.030 151 PRO A N   
1175 C CA  . PRO A 151 ? 0.233 0.249 0.232 0.020  0.012  -0.029 151 PRO A CA  
1176 C C   . PRO A 151 ? 0.234 0.245 0.234 0.027  0.012  -0.032 151 PRO A C   
1177 O O   . PRO A 151 ? 0.251 0.261 0.254 0.031  0.009  -0.031 151 PRO A O   
1178 C CB  . PRO A 151 ? 0.238 0.267 0.245 0.020  0.012  -0.028 151 PRO A CB  
1179 C CG  . PRO A 151 ? 0.248 0.286 0.257 0.020  0.017  -0.030 151 PRO A CG  
1180 C CD  . PRO A 151 ? 0.251 0.280 0.250 0.017  0.019  -0.031 151 PRO A CD  
1181 N N   . LEU A 152 ? 0.245 0.254 0.241 0.029  0.015  -0.035 152 LEU A N   
1182 C CA  . LEU A 152 ? 0.251 0.255 0.248 0.036  0.015  -0.039 152 LEU A CA  
1183 C C   . LEU A 152 ? 0.270 0.260 0.263 0.036  0.012  -0.039 152 LEU A C   
1184 O O   . LEU A 152 ? 0.273 0.256 0.266 0.042  0.012  -0.041 152 LEU A O   
1185 C CB  . LEU A 152 ? 0.262 0.269 0.256 0.037  0.020  -0.043 152 LEU A CB  
1186 C CG  . LEU A 152 ? 0.282 0.305 0.281 0.037  0.024  -0.043 152 LEU A CG  
1187 C CD1 . LEU A 152 ? 0.289 0.314 0.283 0.039  0.029  -0.048 152 LEU A CD1 
1188 C CD2 . LEU A 152 ? 0.301 0.335 0.311 0.042  0.024  -0.043 152 LEU A CD2 
1189 N N   . LEU A 153 ? 0.267 0.251 0.255 0.031  0.011  -0.037 153 LEU A N   
1190 C CA  . LEU A 153 ? 0.275 0.245 0.259 0.030  0.008  -0.037 153 LEU A CA  
1191 C C   . LEU A 153 ? 0.299 0.261 0.278 0.032  0.010  -0.042 153 LEU A C   
1192 O O   . LEU A 153 ? 0.299 0.250 0.277 0.033  0.008  -0.043 153 LEU A O   
1193 C CB  . LEU A 153 ? 0.275 0.241 0.262 0.033  0.006  -0.034 153 LEU A CB  
1194 C CG  . LEU A 153 ? 0.275 0.249 0.265 0.032  0.004  -0.030 153 LEU A CG  
1195 C CD1 . LEU A 153 ? 0.282 0.252 0.274 0.036  0.002  -0.027 153 LEU A CD1 
1196 C CD2 . LEU A 153 ? 0.282 0.256 0.269 0.025  0.004  -0.028 153 LEU A CD2 
1197 N N   . ASN A 154 ? 0.284 0.251 0.261 0.031  0.012  -0.045 154 ASN A N   
1198 C CA  . ASN A 154 ? 0.302 0.262 0.274 0.031  0.012  -0.050 154 ASN A CA  
1199 C C   . ASN A 154 ? 0.294 0.247 0.262 0.026  0.010  -0.049 154 ASN A C   
1200 O O   . ASN A 154 ? 0.282 0.238 0.250 0.022  0.009  -0.046 154 ASN A O   
1201 C CB  . ASN A 154 ? 0.295 0.262 0.263 0.033  0.016  -0.053 154 ASN A CB  
1202 C CG  . ASN A 154 ? 0.320 0.293 0.293 0.039  0.019  -0.055 154 ASN A CG  
1203 O OD1 . ASN A 154 ? 0.332 0.300 0.308 0.044  0.018  -0.056 154 ASN A OD1 
1204 N ND2 . ASN A 154 ? 0.314 0.299 0.287 0.040  0.023  -0.055 154 ASN A ND2 
1205 N N   . ILE A 155 ? 0.297 0.240 0.261 0.026  0.009  -0.053 155 ILE A N   
1206 C CA  . ILE A 155 ? 0.301 0.237 0.263 0.021  0.007  -0.054 155 ILE A CA  
1207 C C   . ILE A 155 ? 0.302 0.238 0.258 0.019  0.006  -0.058 155 ILE A C   
1208 O O   . ILE A 155 ? 0.322 0.256 0.274 0.022  0.007  -0.063 155 ILE A O   
1209 C CB  . ILE A 155 ? 0.301 0.225 0.264 0.022  0.005  -0.054 155 ILE A CB  
1210 C CG1 . ILE A 155 ? 0.316 0.239 0.283 0.025  0.006  -0.049 155 ILE A CG1 
1211 C CG2 . ILE A 155 ? 0.321 0.239 0.284 0.016  0.003  -0.055 155 ILE A CG2 
1212 C CD1 . ILE A 155 ? 0.317 0.245 0.287 0.021  0.005  -0.044 155 ILE A CD1 
1213 N N   . ALA A 156 ? 0.302 0.241 0.259 0.014  0.004  -0.057 156 ALA A N   
1214 C CA  . ALA A 156 ? 0.304 0.244 0.256 0.011  0.002  -0.060 156 ALA A CA  
1215 C C   . ALA A 156 ? 0.298 0.232 0.252 0.007  -0.001 -0.061 156 ALA A C   
1216 O O   . ALA A 156 ? 0.318 0.252 0.277 0.004  -0.002 -0.057 156 ALA A O   
1217 C CB  . ALA A 156 ? 0.317 0.265 0.267 0.010  0.002  -0.057 156 ALA A CB  
1218 N N   . ASP A 157 ? 0.312 0.241 0.262 0.005  -0.003 -0.067 157 ASP A N   
1219 C CA  . ASP A 157 ? 0.317 0.242 0.271 0.000  -0.006 -0.069 157 ASP A CA  
1220 C C   . ASP A 157 ? 0.300 0.234 0.255 -0.003 -0.009 -0.067 157 ASP A C   
1221 O O   . ASP A 157 ? 0.310 0.247 0.259 -0.003 -0.011 -0.071 157 ASP A O   
1222 C CB  . ASP A 157 ? 0.343 0.259 0.292 -0.000 -0.008 -0.076 157 ASP A CB  
1223 C CG  . ASP A 157 ? 0.374 0.284 0.326 -0.007 -0.011 -0.079 157 ASP A CG  
1224 O OD1 . ASP A 157 ? 0.360 0.277 0.317 -0.011 -0.013 -0.076 157 ASP A OD1 
1225 O OD2 . ASP A 157 ? 0.403 0.303 0.352 -0.007 -0.011 -0.084 157 ASP A OD2 
1226 N N   . ILE A 158 ? 0.288 0.226 0.249 -0.005 -0.009 -0.063 158 ILE A N   
1227 C CA  . ILE A 158 ? 0.283 0.231 0.247 -0.007 -0.011 -0.060 158 ILE A CA  
1228 C C   . ILE A 158 ? 0.295 0.243 0.258 -0.010 -0.015 -0.065 158 ILE A C   
1229 O O   . ILE A 158 ? 0.295 0.250 0.255 -0.010 -0.018 -0.066 158 ILE A O   
1230 C CB  . ILE A 158 ? 0.282 0.232 0.252 -0.008 -0.010 -0.055 158 ILE A CB  
1231 C CG1 . ILE A 158 ? 0.287 0.236 0.256 -0.005 -0.006 -0.051 158 ILE A CG1 
1232 C CG2 . ILE A 158 ? 0.284 0.243 0.258 -0.010 -0.012 -0.054 158 ILE A CG2 
1233 C CD1 . ILE A 158 ? 0.297 0.245 0.271 -0.006 -0.004 -0.046 158 ILE A CD1 
1234 N N   . ALA A 159 ? 0.319 0.262 0.287 -0.015 -0.016 -0.068 159 ALA A N   
1235 C CA  . ALA A 159 ? 0.317 0.263 0.287 -0.019 -0.021 -0.073 159 ALA A CA  
1236 C C   . ALA A 159 ? 0.323 0.267 0.283 -0.017 -0.024 -0.078 159 ALA A C   
1237 O O   . ALA A 159 ? 0.315 0.267 0.275 -0.018 -0.028 -0.081 159 ALA A O   
1238 C CB  . ALA A 159 ? 0.343 0.282 0.319 -0.025 -0.021 -0.075 159 ALA A CB  
1239 N N   . ALA A 160 ? 0.320 0.256 0.273 -0.014 -0.021 -0.080 160 ALA A N   
1240 C CA  . ALA A 160 ? 0.333 0.267 0.276 -0.011 -0.023 -0.086 160 ALA A CA  
1241 C C   . ALA A 160 ? 0.327 0.271 0.265 -0.008 -0.023 -0.083 160 ALA A C   
1242 O O   . ALA A 160 ? 0.333 0.280 0.264 -0.008 -0.027 -0.087 160 ALA A O   
1243 C CB  . ALA A 160 ? 0.326 0.251 0.264 -0.008 -0.019 -0.088 160 ALA A CB  
1244 N N   . LEU A 161 ? 0.313 0.260 0.252 -0.005 -0.020 -0.077 161 LEU A N   
1245 C CA  . LEU A 161 ? 0.315 0.269 0.248 -0.002 -0.020 -0.074 161 LEU A CA  
1246 C C   . LEU A 161 ? 0.316 0.277 0.252 -0.004 -0.025 -0.072 161 LEU A C   
1247 O O   . LEU A 161 ? 0.323 0.288 0.252 -0.002 -0.027 -0.071 161 LEU A O   
1248 C CB  . LEU A 161 ? 0.305 0.260 0.240 0.001  -0.015 -0.068 161 LEU A CB  
1249 C CG  . LEU A 161 ? 0.337 0.287 0.269 0.004  -0.010 -0.070 161 LEU A CG  
1250 C CD1 . LEU A 161 ? 0.358 0.312 0.292 0.006  -0.006 -0.064 161 LEU A CD1 
1251 C CD2 . LEU A 161 ? 0.381 0.329 0.303 0.006  -0.010 -0.075 161 LEU A CD2 
1252 N N   . ALA A 162 ? 0.313 0.276 0.260 -0.007 -0.026 -0.071 162 ALA A N   
1253 C CA  . ALA A 162 ? 0.312 0.284 0.264 -0.009 -0.030 -0.070 162 ALA A CA  
1254 C C   . ALA A 162 ? 0.315 0.289 0.262 -0.010 -0.036 -0.075 162 ALA A C   
1255 O O   . ALA A 162 ? 0.303 0.284 0.247 -0.008 -0.040 -0.074 162 ALA A O   
1256 C CB  . ALA A 162 ? 0.314 0.289 0.279 -0.012 -0.030 -0.068 162 ALA A CB  
1257 N N   . ASP A 163 ? 0.313 0.281 0.259 -0.013 -0.037 -0.081 163 ASP A N   
1258 C CA  . ASP A 163 ? 0.334 0.304 0.275 -0.014 -0.043 -0.087 163 ASP A CA  
1259 C C   . ASP A 163 ? 0.322 0.291 0.248 -0.010 -0.044 -0.088 163 ASP A C   
1260 O O   . ASP A 163 ? 0.336 0.310 0.256 -0.010 -0.050 -0.090 163 ASP A O   
1261 C CB  . ASP A 163 ? 0.367 0.329 0.308 -0.019 -0.044 -0.094 163 ASP A CB  
1262 C CG  . ASP A 163 ? 0.421 0.384 0.376 -0.025 -0.045 -0.094 163 ASP A CG  
1263 O OD1 . ASP A 163 ? 0.430 0.403 0.396 -0.026 -0.045 -0.090 163 ASP A OD1 
1264 O OD2 . ASP A 163 ? 0.486 0.439 0.442 -0.029 -0.044 -0.099 163 ASP A OD2 
1265 N N   . ILE A 164 ? 0.315 0.278 0.233 -0.006 -0.038 -0.086 164 ILE A N   
1266 C CA  . ILE A 164 ? 0.332 0.296 0.236 -0.002 -0.038 -0.086 164 ILE A CA  
1267 C C   . ILE A 164 ? 0.322 0.292 0.224 -0.000 -0.039 -0.080 164 ILE A C   
1268 O O   . ILE A 164 ? 0.339 0.312 0.231 0.001  -0.044 -0.080 164 ILE A O   
1269 C CB  . ILE A 164 ? 0.335 0.292 0.234 0.001  -0.030 -0.085 164 ILE A CB  
1270 C CG1 . ILE A 164 ? 0.354 0.303 0.253 -0.000 -0.029 -0.092 164 ILE A CG1 
1271 C CG2 . ILE A 164 ? 0.361 0.321 0.248 0.004  -0.028 -0.083 164 ILE A CG2 
1272 C CD1 . ILE A 164 ? 0.378 0.322 0.277 0.003  -0.022 -0.091 164 ILE A CD1 
1273 N N   . ALA A 165 ? 0.315 0.288 0.226 0.000  -0.037 -0.074 165 ALA A N   
1274 C CA  . ALA A 165 ? 0.309 0.287 0.219 0.003  -0.038 -0.067 165 ALA A CA  
1275 C C   . ALA A 165 ? 0.314 0.299 0.226 0.002  -0.046 -0.069 165 ALA A C   
1276 O O   . ALA A 165 ? 0.327 0.313 0.229 0.005  -0.050 -0.067 165 ALA A O   
1277 C CB  . ALA A 165 ? 0.317 0.296 0.237 0.002  -0.034 -0.062 165 ALA A CB  
1278 N N   . HIS A 166 ? 0.308 0.296 0.232 -0.001 -0.049 -0.072 166 HIS A N   
1279 C CA  . HIS A 166 ? 0.314 0.310 0.243 -0.002 -0.057 -0.074 166 HIS A CA  
1280 C C   . HIS A 166 ? 0.342 0.339 0.260 -0.002 -0.063 -0.079 166 HIS A C   
1281 O O   . HIS A 166 ? 0.340 0.344 0.256 0.000  -0.070 -0.078 166 HIS A O   
1282 C CB  . HIS A 166 ? 0.318 0.319 0.264 -0.007 -0.057 -0.076 166 HIS A CB  
1283 C CG  . HIS A 166 ? 0.309 0.311 0.265 -0.006 -0.051 -0.070 166 HIS A CG  
1284 N ND1 . HIS A 166 ? 0.309 0.310 0.276 -0.010 -0.048 -0.071 166 HIS A ND1 
1285 C CD2 . HIS A 166 ? 0.322 0.323 0.275 -0.002 -0.048 -0.064 166 HIS A CD2 
1286 C CE1 . HIS A 166 ? 0.309 0.310 0.280 -0.008 -0.044 -0.065 166 HIS A CE1 
1287 N NE2 . HIS A 166 ? 0.305 0.306 0.268 -0.003 -0.044 -0.061 166 HIS A NE2 
1288 N N   . ALA A 167 ? 0.344 0.335 0.255 -0.004 -0.061 -0.084 167 ALA A N   
1289 C CA  . ALA A 167 ? 0.369 0.359 0.266 -0.004 -0.067 -0.090 167 ALA A CA  
1290 C C   . ALA A 167 ? 0.377 0.367 0.260 0.002  -0.068 -0.085 167 ALA A C   
1291 O O   . ALA A 167 ? 0.398 0.390 0.270 0.003  -0.074 -0.088 167 ALA A O   
1292 C CB  . ALA A 167 ? 0.370 0.350 0.261 -0.006 -0.064 -0.096 167 ALA A CB  
1293 N N   . ALA A 168 ? 0.371 0.357 0.250 0.004  -0.061 -0.079 168 ALA A N   
1294 C CA  . ALA A 168 ? 0.397 0.381 0.262 0.009  -0.060 -0.073 168 ALA A CA  
1295 C C   . ALA A 168 ? 0.395 0.384 0.265 0.011  -0.063 -0.066 168 ALA A C   
1296 O O   . ALA A 168 ? 0.421 0.407 0.281 0.014  -0.062 -0.060 168 ALA A O   
1297 C CB  . ALA A 168 ? 0.410 0.388 0.269 0.009  -0.051 -0.070 168 ALA A CB  
1298 N N   A ASP A 169 ? 0.387 0.383 0.273 0.010  -0.067 -0.067 169 ASP A N   
1299 N N   B ASP A 169 ? 0.386 0.382 0.272 0.010  -0.067 -0.067 169 ASP A N   
1300 C CA  A ASP A 169 ? 0.404 0.405 0.297 0.013  -0.069 -0.061 169 ASP A CA  
1301 C CA  B ASP A 169 ? 0.402 0.403 0.295 0.013  -0.069 -0.061 169 ASP A CA  
1302 C C   A ASP A 169 ? 0.375 0.370 0.267 0.015  -0.062 -0.054 169 ASP A C   
1303 C C   B ASP A 169 ? 0.374 0.368 0.265 0.015  -0.062 -0.054 169 ASP A C   
1304 O O   A ASP A 169 ? 0.396 0.389 0.285 0.019  -0.063 -0.048 169 ASP A O   
1305 O O   B ASP A 169 ? 0.397 0.389 0.281 0.019  -0.063 -0.048 169 ASP A O   
1306 C CB  A ASP A 169 ? 0.432 0.435 0.313 0.017  -0.077 -0.059 169 ASP A CB  
1307 C CB  B ASP A 169 ? 0.429 0.433 0.312 0.017  -0.077 -0.059 169 ASP A CB  
1308 C CG  A ASP A 169 ? 0.474 0.483 0.363 0.021  -0.082 -0.055 169 ASP A CG  
1309 C CG  B ASP A 169 ? 0.473 0.485 0.361 0.016  -0.086 -0.066 169 ASP A CG  
1310 O OD1 A ASP A 169 ? 0.489 0.504 0.395 0.020  -0.082 -0.056 169 ASP A OD1 
1311 O OD1 B ASP A 169 ? 0.493 0.512 0.398 0.013  -0.087 -0.068 169 ASP A OD1 
1312 O OD2 A ASP A 169 ? 0.501 0.508 0.379 0.026  -0.086 -0.050 169 ASP A OD2 
1313 O OD2 B ASP A 169 ? 0.533 0.545 0.407 0.017  -0.091 -0.068 169 ASP A OD2 
1314 N N   . ALA A 170 ? 0.352 0.342 0.247 0.012  -0.054 -0.055 170 ALA A N   
1315 C CA  . ALA A 170 ? 0.335 0.320 0.231 0.013  -0.047 -0.049 170 ALA A CA  
1316 C C   . ALA A 170 ? 0.334 0.322 0.247 0.011  -0.045 -0.049 170 ALA A C   
1317 O O   . ALA A 170 ? 0.322 0.314 0.244 0.008  -0.047 -0.054 170 ALA A O   
1318 C CB  . ALA A 170 ? 0.335 0.315 0.222 0.012  -0.041 -0.050 170 ALA A CB  
1319 N N   . LEU A 171 ? 0.300 0.285 0.216 0.012  -0.040 -0.044 171 LEU A N   
1320 C CA  . LEU A 171 ? 0.290 0.276 0.219 0.010  -0.037 -0.044 171 LEU A CA  
1321 C C   . LEU A 171 ? 0.300 0.282 0.230 0.007  -0.031 -0.045 171 LEU A C   
1322 O O   . LEU A 171 ? 0.311 0.290 0.232 0.008  -0.028 -0.044 171 LEU A O   
1323 C CB  . LEU A 171 ? 0.301 0.287 0.232 0.012  -0.036 -0.038 171 LEU A CB  
1324 C CG  . LEU A 171 ? 0.314 0.303 0.245 0.016  -0.042 -0.036 171 LEU A CG  
1325 C CD1 . LEU A 171 ? 0.355 0.339 0.285 0.019  -0.040 -0.031 171 LEU A CD1 
1326 C CD2 . LEU A 171 ? 0.330 0.328 0.274 0.015  -0.045 -0.040 171 LEU A CD2 
1327 N N   . LEU A 172 ? 0.273 0.257 0.214 0.005  -0.030 -0.047 172 LEU A N   
1328 C CA  . LEU A 172 ? 0.268 0.248 0.211 0.003  -0.024 -0.047 172 LEU A CA  
1329 C C   . LEU A 172 ? 0.260 0.239 0.209 0.003  -0.021 -0.043 172 LEU A C   
1330 O O   . LEU A 172 ? 0.259 0.241 0.216 0.003  -0.022 -0.042 172 LEU A O   
1331 C CB  . LEU A 172 ? 0.284 0.263 0.233 0.000  -0.024 -0.052 172 LEU A CB  
1332 C CG  . LEU A 172 ? 0.322 0.295 0.271 -0.000 -0.019 -0.052 172 LEU A CG  
1333 C CD1 . LEU A 172 ? 0.372 0.343 0.311 0.001  -0.018 -0.054 172 LEU A CD1 
1334 C CD2 . LEU A 172 ? 0.343 0.314 0.299 -0.003 -0.019 -0.055 172 LEU A CD2 
1335 N N   . VAL A 173 ? 0.264 0.240 0.208 0.004  -0.017 -0.039 173 VAL A N   
1336 C CA  . VAL A 173 ? 0.242 0.216 0.190 0.004  -0.014 -0.036 173 VAL A CA  
1337 C C   . VAL A 173 ? 0.246 0.218 0.197 0.003  -0.010 -0.037 173 VAL A C   
1338 O O   . VAL A 173 ? 0.255 0.227 0.203 0.003  -0.009 -0.038 173 VAL A O   
1339 C CB  . VAL A 173 ? 0.255 0.227 0.196 0.005  -0.013 -0.031 173 VAL A CB  
1340 C CG1 . VAL A 173 ? 0.262 0.232 0.207 0.004  -0.010 -0.028 173 VAL A CG1 
1341 C CG2 . VAL A 173 ? 0.271 0.244 0.207 0.007  -0.017 -0.030 173 VAL A CG2 
1342 N N   . VAL A 174 ? 0.243 0.215 0.202 0.001  -0.009 -0.036 174 VAL A N   
1343 C CA  . VAL A 174 ? 0.245 0.215 0.207 0.001  -0.006 -0.036 174 VAL A CA  
1344 C C   . VAL A 174 ? 0.228 0.197 0.191 0.001  -0.004 -0.032 174 VAL A C   
1345 O O   . VAL A 174 ? 0.238 0.207 0.204 0.000  -0.004 -0.031 174 VAL A O   
1346 C CB  . VAL A 174 ? 0.249 0.217 0.216 -0.001 -0.006 -0.038 174 VAL A CB  
1347 C CG1 . VAL A 174 ? 0.265 0.229 0.233 -0.001 -0.004 -0.038 174 VAL A CG1 
1348 C CG2 . VAL A 174 ? 0.261 0.229 0.226 -0.002 -0.009 -0.043 174 VAL A CG2 
1349 N N   . ASP A 175 ? 0.242 0.211 0.203 0.001  -0.002 -0.031 175 ASP A N   
1350 C CA  . ASP A 175 ? 0.240 0.208 0.202 0.001  -0.000 -0.028 175 ASP A CA  
1351 C C   . ASP A 175 ? 0.240 0.206 0.206 0.000  0.001  -0.028 175 ASP A C   
1352 O O   . ASP A 175 ? 0.253 0.218 0.219 0.001  0.001  -0.029 175 ASP A O   
1353 C CB  . ASP A 175 ? 0.260 0.230 0.219 0.001  0.001  -0.026 175 ASP A CB  
1354 C CG  . ASP A 175 ? 0.245 0.214 0.205 -0.000 0.002  -0.023 175 ASP A CG  
1355 O OD1 . ASP A 175 ? 0.254 0.222 0.218 -0.001 0.002  -0.023 175 ASP A OD1 
1356 O OD2 . ASP A 175 ? 0.256 0.227 0.214 -0.002 0.003  -0.022 175 ASP A OD2 
1357 N N   . ASN A 176 ? 0.236 0.202 0.206 -0.001 0.000  -0.027 176 ASN A N   
1358 C CA  . ASN A 176 ? 0.225 0.188 0.197 -0.001 0.001  -0.027 176 ASN A CA  
1359 C C   . ASN A 176 ? 0.233 0.194 0.204 -0.001 0.002  -0.024 176 ASN A C   
1360 O O   . ASN A 176 ? 0.242 0.200 0.214 -0.002 0.003  -0.023 176 ASN A O   
1361 C CB  . ASN A 176 ? 0.223 0.185 0.198 -0.003 0.001  -0.028 176 ASN A CB  
1362 C CG  . ASN A 176 ? 0.243 0.201 0.220 -0.005 0.002  -0.028 176 ASN A CG  
1363 O OD1 . ASN A 176 ? 0.261 0.216 0.238 -0.004 0.002  -0.029 176 ASN A OD1 
1364 N ND2 . ASN A 176 ? 0.235 0.194 0.215 -0.006 0.003  -0.027 176 ASN A ND2 
1365 N N   . THR A 177 ? 0.230 0.194 0.200 -0.001 0.002  -0.023 177 THR A N   
1366 C CA  . THR A 177 ? 0.230 0.193 0.198 -0.001 0.002  -0.021 177 THR A CA  
1367 C C   . THR A 177 ? 0.242 0.204 0.212 0.000  0.002  -0.020 177 THR A C   
1368 O O   . THR A 177 ? 0.244 0.203 0.213 -0.000 0.002  -0.019 177 THR A O   
1369 C CB  . THR A 177 ? 0.231 0.198 0.199 -0.001 0.002  -0.020 177 THR A CB  
1370 O OG1 . THR A 177 ? 0.231 0.196 0.196 -0.002 0.002  -0.020 177 THR A OG1 
1371 C CG2 . THR A 177 ? 0.239 0.206 0.207 -0.002 0.002  -0.018 177 THR A CG2 
1372 N N   . PHE A 178 ? 0.231 0.194 0.203 0.002  0.002  -0.022 178 PHE A N   
1373 C CA  . PHE A 178 ? 0.246 0.207 0.219 0.004  0.002  -0.021 178 PHE A CA  
1374 C C   . PHE A 178 ? 0.259 0.213 0.231 0.004  0.002  -0.020 178 PHE A C   
1375 O O   . PHE A 178 ? 0.275 0.226 0.246 0.005  0.002  -0.018 178 PHE A O   
1376 C CB  . PHE A 178 ? 0.256 0.220 0.231 0.007  0.002  -0.023 178 PHE A CB  
1377 C CG  . PHE A 178 ? 0.244 0.215 0.221 0.008  0.003  -0.022 178 PHE A CG  
1378 C CD1 . PHE A 178 ? 0.238 0.213 0.214 0.005  0.003  -0.021 178 PHE A CD1 
1379 C CD2 . PHE A 178 ? 0.248 0.222 0.228 0.011  0.003  -0.023 178 PHE A CD2 
1380 C CE1 . PHE A 178 ? 0.250 0.232 0.228 0.005  0.003  -0.021 178 PHE A CE1 
1381 C CE2 . PHE A 178 ? 0.262 0.245 0.246 0.012  0.003  -0.023 178 PHE A CE2 
1382 C CZ  . PHE A 178 ? 0.249 0.236 0.232 0.008  0.003  -0.021 178 PHE A CZ  
1383 N N   . ALA A 179 ? 0.249 0.200 0.221 0.002  0.003  -0.022 179 ALA A N   
1384 C CA  . ALA A 179 ? 0.254 0.199 0.227 0.001  0.003  -0.022 179 ALA A CA  
1385 C C   . ALA A 179 ? 0.250 0.194 0.221 -0.002 0.004  -0.019 179 ALA A C   
1386 O O   . ALA A 179 ? 0.262 0.201 0.231 -0.003 0.005  -0.017 179 ALA A O   
1387 C CB  . ALA A 179 ? 0.256 0.199 0.230 -0.000 0.003  -0.025 179 ALA A CB  
1388 N N   . SER A 180 ? 0.243 0.192 0.214 -0.003 0.004  -0.020 180 SER A N   
1389 C CA  . SER A 180 ? 0.246 0.197 0.218 -0.005 0.006  -0.019 180 SER A CA  
1390 C C   . SER A 180 ? 0.249 0.199 0.224 -0.007 0.007  -0.020 180 SER A C   
1391 O O   . SER A 180 ? 0.243 0.189 0.219 -0.008 0.007  -0.022 180 SER A O   
1392 C CB  . SER A 180 ? 0.249 0.196 0.216 -0.005 0.007  -0.016 180 SER A CB  
1393 O OG  . SER A 180 ? 0.256 0.197 0.222 -0.006 0.008  -0.015 180 SER A OG  
1394 N N   . PRO A 181 ? 0.253 0.207 0.230 -0.009 0.008  -0.021 181 PRO A N   
1395 C CA  . PRO A 181 ? 0.256 0.211 0.238 -0.012 0.010  -0.022 181 PRO A CA  
1396 C C   . PRO A 181 ? 0.264 0.213 0.245 -0.014 0.012  -0.020 181 PRO A C   
1397 O O   . PRO A 181 ? 0.262 0.211 0.247 -0.018 0.013  -0.021 181 PRO A O   
1398 C CB  . PRO A 181 ? 0.262 0.224 0.247 -0.012 0.011  -0.022 181 PRO A CB  
1399 C CG  . PRO A 181 ? 0.301 0.262 0.281 -0.009 0.010  -0.021 181 PRO A CG  
1400 C CD  . PRO A 181 ? 0.273 0.230 0.248 -0.007 0.009  -0.020 181 PRO A CD  
1401 N N   . TYR A 182 ? 0.259 0.203 0.234 -0.013 0.013  -0.017 182 TYR A N   
1402 C CA  . TYR A 182 ? 0.264 0.200 0.236 -0.016 0.015  -0.014 182 TYR A CA  
1403 C C   . TYR A 182 ? 0.277 0.207 0.250 -0.016 0.013  -0.015 182 TYR A C   
1404 O O   . TYR A 182 ? 0.286 0.208 0.259 -0.019 0.015  -0.014 182 TYR A O   
1405 C CB  . TYR A 182 ? 0.263 0.196 0.228 -0.014 0.015  -0.011 182 TYR A CB  
1406 C CG  . TYR A 182 ? 0.275 0.198 0.235 -0.016 0.017  -0.007 182 TYR A CG  
1407 C CD1 . TYR A 182 ? 0.290 0.213 0.250 -0.020 0.021  -0.006 182 TYR A CD1 
1408 C CD2 . TYR A 182 ? 0.280 0.195 0.236 -0.013 0.015  -0.005 182 TYR A CD2 
1409 C CE1 . TYR A 182 ? 0.294 0.207 0.249 -0.022 0.023  -0.001 182 TYR A CE1 
1410 C CE2 . TYR A 182 ? 0.293 0.199 0.243 -0.014 0.016  -0.001 182 TYR A CE2 
1411 C CZ  . TYR A 182 ? 0.296 0.200 0.245 -0.019 0.021  0.001  182 TYR A CZ  
1412 O OH  . TYR A 182 ? 0.325 0.218 0.267 -0.021 0.023  0.006  182 TYR A OH  
1413 N N   . LEU A 183 ? 0.264 0.194 0.237 -0.012 0.010  -0.017 183 LEU A N   
1414 C CA  . LEU A 183 ? 0.277 0.200 0.250 -0.011 0.009  -0.019 183 LEU A CA  
1415 C C   . LEU A 183 ? 0.277 0.203 0.254 -0.013 0.008  -0.023 183 LEU A C   
1416 O O   . LEU A 183 ? 0.296 0.215 0.273 -0.014 0.007  -0.025 183 LEU A O   
1417 C CB  . LEU A 183 ? 0.281 0.203 0.251 -0.006 0.007  -0.018 183 LEU A CB  
1418 C CG  . LEU A 183 ? 0.273 0.191 0.238 -0.004 0.007  -0.014 183 LEU A CG  
1419 C CD1 . LEU A 183 ? 0.278 0.198 0.243 0.001  0.004  -0.014 183 LEU A CD1 
1420 C CD2 . LEU A 183 ? 0.306 0.215 0.268 -0.006 0.008  -0.010 183 LEU A CD2 
1421 N N   . GLN A 184 ? 0.257 0.192 0.237 -0.013 0.007  -0.025 184 GLN A N   
1422 C CA  . GLN A 184 ? 0.259 0.197 0.242 -0.013 0.005  -0.030 184 GLN A CA  
1423 C C   . GLN A 184 ? 0.262 0.210 0.249 -0.015 0.004  -0.031 184 GLN A C   
1424 O O   . GLN A 184 ? 0.251 0.203 0.237 -0.013 0.005  -0.029 184 GLN A O   
1425 C CB  . GLN A 184 ? 0.259 0.198 0.238 -0.009 0.003  -0.031 184 GLN A CB  
1426 C CG  . GLN A 184 ? 0.266 0.207 0.246 -0.008 0.001  -0.035 184 GLN A CG  
1427 C CD  . GLN A 184 ? 0.279 0.220 0.255 -0.004 0.001  -0.036 184 GLN A CD  
1428 O OE1 . GLN A 184 ? 0.292 0.227 0.266 -0.003 0.001  -0.039 184 GLN A OE1 
1429 N NE2 . GLN A 184 ? 0.262 0.209 0.237 -0.002 0.001  -0.035 184 GLN A NE2 
1430 N N   . ARG A 185 ? 0.323 0.222 0.243 -0.010 -0.008 0.017  185 ARG A N   
1431 C CA  . ARG A 185 ? 0.314 0.243 0.247 -0.015 0.012  0.013  185 ARG A CA  
1432 C C   . ARG A 185 ? 0.276 0.222 0.241 -0.011 0.007  -0.001 185 ARG A C   
1433 O O   . ARG A 185 ? 0.275 0.222 0.264 -0.019 0.006  -0.000 185 ARG A O   
1434 C CB  . ARG A 185 ? 0.392 0.321 0.319 -0.031 0.030  0.028  185 ARG A CB  
1435 C CG  . ARG A 185 ? 0.486 0.408 0.366 -0.033 0.042  0.037  185 ARG A CG  
1436 C CD  . ARG A 185 ? 0.608 0.528 0.470 -0.052 0.064  0.056  185 ARG A CD  
1437 N NE  . ARG A 185 ? 0.678 0.640 0.572 -0.056 0.089  0.047  185 ARG A NE  
1438 C CZ  . ARG A 185 ? 0.848 0.829 0.755 -0.075 0.113  0.059  185 ARG A CZ  
1439 N NH1 . ARG A 185 ? 0.832 0.859 0.779 -0.075 0.135  0.046  185 ARG A NH1 
1440 N NH2 . ARG A 185 ? 0.944 0.898 0.829 -0.096 0.113  0.085  185 ARG A NH2 
1441 N N   . PRO A 186 ? 0.256 0.216 0.223 -0.001 0.003  -0.013 186 PRO A N   
1442 C CA  . PRO A 186 ? 0.249 0.222 0.234 0.002  -0.003 -0.024 186 PRO A CA  
1443 C C   . PRO A 186 ? 0.243 0.228 0.246 -0.004 0.001  -0.025 186 PRO A C   
1444 O O   . PRO A 186 ? 0.248 0.234 0.263 -0.004 -0.009 -0.033 186 PRO A O   
1445 C CB  . PRO A 186 ? 0.240 0.227 0.218 0.008  -0.003 -0.030 186 PRO A CB  
1446 C CG  . PRO A 186 ? 0.243 0.219 0.207 0.012  -0.006 -0.026 186 PRO A CG  
1447 C CD  . PRO A 186 ? 0.260 0.220 0.210 0.007  0.000  -0.015 186 PRO A CD  
1448 N N   . LEU A 187 ? 0.229 0.225 0.236 -0.007 0.012  -0.021 187 LEU A N   
1449 C CA  . LEU A 187 ? 0.239 0.252 0.276 -0.010 0.012  -0.025 187 LEU A CA  
1450 C C   . LEU A 187 ? 0.250 0.259 0.311 -0.021 0.010  -0.022 187 LEU A C   
1451 O O   . LEU A 187 ? 0.246 0.264 0.334 -0.023 -0.001 -0.028 187 LEU A O   
1452 C CB  . LEU A 187 ? 0.235 0.264 0.282 -0.008 0.025  -0.025 187 LEU A CB  
1453 C CG  . LEU A 187 ? 0.240 0.266 0.268 0.003  0.022  -0.030 187 LEU A CG  
1454 C CD1 . LEU A 187 ? 0.247 0.287 0.287 0.009  0.033  -0.036 187 LEU A CD1 
1455 C CD2 . LEU A 187 ? 0.246 0.269 0.274 0.006  0.004  -0.032 187 LEU A CD2 
1456 N N   . SER A 188 ? 0.259 0.254 0.312 -0.030 0.017  -0.010 188 SER A N   
1457 C CA  . SER A 188 ? 0.279 0.265 0.356 -0.045 0.014  -0.003 188 SER A CA  
1458 C C   . SER A 188 ? 0.274 0.240 0.358 -0.041 -0.011 -0.014 188 SER A C   
1459 O O   . SER A 188 ? 0.299 0.257 0.411 -0.053 -0.021 -0.013 188 SER A O   
1460 C CB  . SER A 188 ? 0.313 0.280 0.370 -0.057 0.024  0.017  188 SER A CB  
1461 O OG  . SER A 188 ? 0.323 0.256 0.351 -0.049 0.007  0.018  188 SER A OG  
1462 N N   . LEU A 189 ? 0.271 0.232 0.331 -0.025 -0.020 -0.026 189 LEU A N   
1463 C CA  . LEU A 189 ? 0.296 0.242 0.354 -0.017 -0.040 -0.043 189 LEU A CA  
1464 C C   . LEU A 189 ? 0.293 0.258 0.346 -0.010 -0.045 -0.057 189 LEU A C   
1465 O O   . LEU A 189 ? 0.331 0.291 0.373 -0.002 -0.057 -0.074 189 LEU A O   
1466 C CB  . LEU A 189 ? 0.311 0.244 0.348 -0.005 -0.042 -0.047 189 LEU A CB  
1467 C CG  . LEU A 189 ? 0.356 0.260 0.392 -0.012 -0.045 -0.031 189 LEU A CG  
1468 C CD1 . LEU A 189 ? 0.386 0.280 0.406 0.003  -0.052 -0.036 189 LEU A CD1 
1469 C CD2 . LEU A 189 ? 0.425 0.301 0.482 -0.022 -0.061 -0.028 189 LEU A CD2 
1470 N N   . GLY A 190 ? 0.261 0.246 0.321 -0.013 -0.038 -0.051 190 GLY A N   
1471 C CA  . GLY A 190 ? 0.282 0.277 0.335 -0.009 -0.049 -0.060 190 GLY A CA  
1472 C C   . GLY A 190 ? 0.266 0.269 0.288 -0.003 -0.042 -0.057 190 GLY A C   
1473 O O   . GLY A 190 ? 0.280 0.286 0.289 -0.002 -0.052 -0.059 190 GLY A O   
1474 N N   . ALA A 191 ? 0.249 0.254 0.261 -0.001 -0.028 -0.050 191 ALA A N   
1475 C CA  . ALA A 191 ? 0.246 0.258 0.238 0.001  -0.023 -0.045 191 ALA A CA  
1476 C C   . ALA A 191 ? 0.241 0.256 0.245 0.000  -0.028 -0.039 191 ALA A C   
1477 O O   . ALA A 191 ? 0.238 0.257 0.270 -0.001 -0.026 -0.039 191 ALA A O   
1478 C CB  . ALA A 191 ? 0.244 0.256 0.230 0.003  -0.012 -0.040 191 ALA A CB  
1479 N N   . ASP A 192 ? 0.251 0.264 0.236 -0.001 -0.036 -0.034 192 ASP A N   
1480 C CA  . ASP A 192 ? 0.241 0.250 0.238 0.001  -0.047 -0.029 192 ASP A CA  
1481 C C   . ASP A 192 ? 0.234 0.241 0.234 0.004  -0.038 -0.025 192 ASP A C   
1482 O O   . ASP A 192 ? 0.227 0.233 0.249 0.011  -0.043 -0.028 192 ASP A O   
1483 C CB  . ASP A 192 ? 0.273 0.271 0.243 -0.003 -0.065 -0.023 192 ASP A CB  
1484 C CG  . ASP A 192 ? 0.306 0.304 0.267 -0.004 -0.077 -0.030 192 ASP A CG  
1485 O OD1 . ASP A 192 ? 0.303 0.301 0.293 -0.000 -0.092 -0.035 192 ASP A OD1 
1486 O OD2 . ASP A 192 ? 0.309 0.309 0.238 -0.007 -0.071 -0.035 192 ASP A OD2 
1487 N N   . VAL A 193 ? 0.255 0.260 0.235 0.001  -0.030 -0.021 193 VAL A N   
1488 C CA  . VAL A 193 ? 0.244 0.242 0.223 0.002  -0.028 -0.019 193 VAL A CA  
1489 C C   . VAL A 193 ? 0.243 0.246 0.215 0.002  -0.016 -0.021 193 VAL A C   
1490 O O   . VAL A 193 ? 0.238 0.250 0.202 -0.002 -0.012 -0.021 193 VAL A O   
1491 C CB  . VAL A 193 ? 0.273 0.259 0.237 -0.006 -0.040 -0.007 193 VAL A CB  
1492 C CG1 . VAL A 193 ? 0.287 0.260 0.256 -0.003 -0.044 -0.008 193 VAL A CG1 
1493 C CG2 . VAL A 193 ? 0.299 0.273 0.262 -0.007 -0.059 -0.002 193 VAL A CG2 
1494 N N   . VAL A 194 ? 0.237 0.235 0.210 0.007  -0.011 -0.024 194 VAL A N   
1495 C CA  . VAL A 194 ? 0.232 0.227 0.195 0.008  -0.008 -0.025 194 VAL A CA  
1496 C C   . VAL A 194 ? 0.225 0.211 0.185 0.007  -0.017 -0.024 194 VAL A C   
1497 O O   . VAL A 194 ? 0.237 0.211 0.197 0.012  -0.023 -0.028 194 VAL A O   
1498 C CB  . VAL A 194 ? 0.250 0.241 0.206 0.012  0.001  -0.028 194 VAL A CB  
1499 C CG1 . VAL A 194 ? 0.280 0.261 0.219 0.014  -0.002 -0.027 194 VAL A CG1 
1500 C CG2 . VAL A 194 ? 0.265 0.261 0.230 0.009  0.007  -0.026 194 VAL A CG2 
1501 N N   . VAL A 195 ? 0.234 0.225 0.194 0.001  -0.021 -0.021 195 VAL A N   
1502 C CA  . VAL A 195 ? 0.232 0.215 0.196 -0.003 -0.033 -0.020 195 VAL A CA  
1503 C C   . VAL A 195 ? 0.243 0.220 0.200 0.003  -0.037 -0.027 195 VAL A C   
1504 O O   . VAL A 195 ? 0.231 0.220 0.191 0.006  -0.032 -0.027 195 VAL A O   
1505 C CB  . VAL A 195 ? 0.257 0.256 0.234 -0.018 -0.034 -0.011 195 VAL A CB  
1506 C CG1 . VAL A 195 ? 0.298 0.291 0.288 -0.026 -0.048 -0.009 195 VAL A CG1 
1507 C CG2 . VAL A 195 ? 0.276 0.274 0.248 -0.026 -0.033 -0.001 195 VAL A CG2 
1508 N N   . HIS A 196 ? 0.233 0.194 0.182 0.009  -0.004 -0.018 196 HIS A N   
1509 C CA  . HIS A 196 ? 0.239 0.203 0.193 0.009  -0.001 -0.017 196 HIS A CA  
1510 C C   . HIS A 196 ? 0.230 0.200 0.185 0.008  0.002  -0.013 196 HIS A C   
1511 O O   . HIS A 196 ? 0.226 0.197 0.180 0.005  0.002  -0.011 196 HIS A O   
1512 C CB  . HIS A 196 ? 0.238 0.201 0.200 0.006  -0.002 -0.015 196 HIS A CB  
1513 C CG  . HIS A 196 ? 0.240 0.196 0.203 0.005  -0.006 -0.017 196 HIS A CG  
1514 N ND1 . HIS A 196 ? 0.243 0.195 0.206 0.007  -0.007 -0.018 196 HIS A ND1 
1515 C CD2 . HIS A 196 ? 0.252 0.207 0.219 0.002  -0.010 -0.017 196 HIS A CD2 
1516 C CE1 . HIS A 196 ? 0.244 0.189 0.209 0.004  -0.012 -0.019 196 HIS A CE1 
1517 N NE2 . HIS A 196 ? 0.255 0.202 0.223 0.001  -0.014 -0.018 196 HIS A NE2 
1518 N N   . SER A 197 ? 0.230 0.205 0.187 0.009  0.005  -0.012 197 SER A N   
1519 C CA  . SER A 197 ? 0.224 0.204 0.186 0.006  0.006  -0.008 197 SER A CA  
1520 C C   . SER A 197 ? 0.212 0.187 0.177 0.005  0.005  -0.008 197 SER A C   
1521 O O   . SER A 197 ? 0.228 0.202 0.195 0.007  0.005  -0.009 197 SER A O   
1522 C CB  . SER A 197 ? 0.220 0.208 0.184 0.008  0.009  -0.006 197 SER A CB  
1523 O OG  . SER A 197 ? 0.227 0.219 0.197 0.004  0.009  -0.002 197 SER A OG  
1524 N N   . THR A 198 ? 0.222 0.195 0.188 0.003  0.003  -0.007 198 THR A N   
1525 C CA  . THR A 198 ? 0.223 0.193 0.191 0.002  0.003  -0.006 198 THR A CA  
1526 C C   . THR A 198 ? 0.225 0.197 0.194 0.002  0.003  -0.004 198 THR A C   
1527 O O   . THR A 198 ? 0.230 0.199 0.200 0.003  0.002  -0.004 198 THR A O   
1528 C CB  . THR A 198 ? 0.226 0.194 0.193 0.002  0.002  -0.006 198 THR A CB  
1529 O OG1 . THR A 198 ? 0.224 0.190 0.187 0.001  0.000  -0.005 198 THR A OG1 
1530 C CG2 . THR A 198 ? 0.244 0.212 0.212 0.002  0.001  -0.007 198 THR A CG2 
1531 N N   . THR A 199 ? 0.217 0.193 0.187 0.001  0.003  -0.003 199 THR A N   
1532 C CA  . THR A 199 ? 0.218 0.198 0.192 -0.000 0.002  -0.000 199 THR A CA  
1533 C C   . THR A 199 ? 0.227 0.209 0.204 0.003  0.002  -0.002 199 THR A C   
1534 O O   . THR A 199 ? 0.237 0.220 0.217 0.003  0.001  -0.000 199 THR A O   
1535 C CB  . THR A 199 ? 0.221 0.210 0.198 -0.002 0.002  0.003  199 THR A CB  
1536 O OG1 . THR A 199 ? 0.219 0.204 0.192 -0.005 0.001  0.004  199 THR A OG1 
1537 C CG2 . THR A 199 ? 0.232 0.226 0.215 -0.005 0.000  0.006  199 THR A CG2 
1538 N N   . LYS A 200 ? 0.217 0.198 0.193 0.006  0.004  -0.004 200 LYS A N   
1539 C CA  . LYS A 200 ? 0.224 0.205 0.202 0.010  0.004  -0.005 200 LYS A CA  
1540 C C   . LYS A 200 ? 0.237 0.209 0.214 0.010  0.003  -0.006 200 LYS A C   
1541 O O   . LYS A 200 ? 0.244 0.215 0.221 0.008  0.002  -0.004 200 LYS A O   
1542 C CB  . LYS A 200 ? 0.235 0.218 0.211 0.015  0.006  -0.008 200 LYS A CB  
1543 C CG  . LYS A 200 ? 0.231 0.225 0.208 0.015  0.009  -0.006 200 LYS A CG  
1544 C CD  . LYS A 200 ? 0.241 0.245 0.224 0.012  0.009  -0.002 200 LYS A CD  
1545 C CE  . LYS A 200 ? 0.269 0.285 0.254 0.011  0.013  0.002  200 LYS A CE  
1546 N NZ  . LYS A 200 ? 0.306 0.331 0.299 0.006  0.011  0.007  200 LYS A NZ  
1547 N N   . TYR A 201 ? 0.221 0.187 0.196 0.012  0.002  -0.008 201 TYR A N   
1548 C CA  . TYR A 201 ? 0.218 0.177 0.193 0.011  0.000  -0.006 201 TYR A CA  
1549 C C   . TYR A 201 ? 0.222 0.180 0.197 0.007  0.001  -0.004 201 TYR A C   
1550 O O   . TYR A 201 ? 0.239 0.195 0.214 0.006  0.001  -0.001 201 TYR A O   
1551 C CB  . TYR A 201 ? 0.233 0.183 0.206 0.013  -0.002 -0.008 201 TYR A CB  
1552 C CG  . TYR A 201 ? 0.252 0.200 0.224 0.019  -0.003 -0.011 201 TYR A CG  
1553 C CD1 . TYR A 201 ? 0.250 0.196 0.223 0.021  -0.005 -0.009 201 TYR A CD1 
1554 C CD2 . TYR A 201 ? 0.257 0.208 0.226 0.024  -0.002 -0.015 201 TYR A CD2 
1555 C CE1 . TYR A 201 ? 0.255 0.199 0.226 0.028  -0.006 -0.011 201 TYR A CE1 
1556 C CE2 . TYR A 201 ? 0.273 0.223 0.241 0.031  -0.003 -0.017 201 TYR A CE2 
1557 C CZ  . TYR A 201 ? 0.267 0.214 0.236 0.034  -0.005 -0.016 201 TYR A CZ  
1558 O OH  . TYR A 201 ? 0.282 0.229 0.249 0.043  -0.005 -0.018 201 TYR A OH  
1559 N N   . LEU A 202 ? 0.225 0.185 0.199 0.005  0.002  -0.005 202 LEU A N   
1560 C CA  . LEU A 202 ? 0.215 0.177 0.190 0.003  0.002  -0.002 202 LEU A CA  
1561 C C   . LEU A 202 ? 0.215 0.178 0.187 0.004  0.003  -0.001 202 LEU A C   
1562 O O   . LEU A 202 ? 0.225 0.188 0.196 0.004  0.004  0.002  202 LEU A O   
1563 C CB  . LEU A 202 ? 0.229 0.193 0.205 0.002  0.002  -0.004 202 LEU A CB  
1564 C CG  . LEU A 202 ? 0.233 0.193 0.210 0.001  -0.000 -0.006 202 LEU A CG  
1565 C CD1 . LEU A 202 ? 0.246 0.208 0.222 0.001  -0.001 -0.008 202 LEU A CD1 
1566 C CD2 . LEU A 202 ? 0.244 0.205 0.227 -0.003 -0.001 -0.002 202 LEU A CD2 
1567 N N   . GLY A 203 ? 0.224 0.188 0.193 0.004  0.003  -0.002 203 GLY A N   
1568 C CA  . GLY A 203 ? 0.217 0.179 0.182 0.005  0.002  -0.001 203 GLY A CA  
1569 C C   . GLY A 203 ? 0.236 0.197 0.201 0.007  0.001  0.001  203 GLY A C   
1570 O O   . GLY A 203 ? 0.232 0.190 0.192 0.008  0.000  0.002  203 GLY A O   
1571 N N   . GLY A 204 ? 0.228 0.191 0.197 0.007  -0.000 0.000  204 GLY A N   
1572 C CA  . GLY A 204 ? 0.227 0.188 0.197 0.009  -0.001 0.001  204 GLY A CA  
1573 C C   . GLY A 204 ? 0.225 0.187 0.193 0.010  -0.004 0.002  204 GLY A C   
1574 O O   . GLY A 204 ? 0.232 0.192 0.200 0.012  -0.006 0.003  204 GLY A O   
1575 N N   . HIS A 205 ? 0.216 0.179 0.183 0.008  -0.006 0.002  205 HIS A N   
1576 C CA  . HIS A 205 ? 0.232 0.193 0.196 0.008  -0.011 0.003  205 HIS A CA  
1577 C C   . HIS A 205 ? 0.222 0.189 0.191 0.005  -0.015 0.003  205 HIS A C   
1578 O O   . HIS A 205 ? 0.223 0.187 0.190 0.004  -0.020 0.004  205 HIS A O   
1579 C CB  . HIS A 205 ? 0.240 0.193 0.192 0.010  -0.012 0.003  205 HIS A CB  
1580 C CG  . HIS A 205 ? 0.236 0.187 0.185 0.013  -0.008 0.005  205 HIS A CG  
1581 N ND1 . HIS A 205 ? 0.237 0.190 0.189 0.012  -0.004 0.005  205 HIS A ND1 
1582 C CD2 . HIS A 205 ? 0.262 0.209 0.205 0.015  -0.009 0.007  205 HIS A CD2 
1583 C CE1 . HIS A 205 ? 0.252 0.202 0.200 0.013  -0.001 0.008  205 HIS A CE1 
1584 N NE2 . HIS A 205 ? 0.260 0.207 0.202 0.016  -0.004 0.010  205 HIS A NE2 
1585 N N   . SER A 206 ? 0.226 0.200 0.202 0.004  -0.012 0.003  206 SER A N   
1586 C CA  . SER A 206 ? 0.227 0.209 0.210 -0.000 -0.014 0.006  206 SER A CA  
1587 C C   . SER A 206 ? 0.218 0.194 0.197 -0.005 -0.020 0.006  206 SER A C   
1588 O O   . SER A 206 ? 0.224 0.203 0.208 -0.009 -0.025 0.009  206 SER A O   
1589 C CB  . SER A 206 ? 0.247 0.239 0.239 0.000  -0.016 0.008  206 SER A CB  
1590 O OG  . SER A 206 ? 0.282 0.279 0.278 0.006  -0.012 0.007  206 SER A OG  
1591 N N   . ASP A 207 ? 0.226 0.191 0.195 -0.004 -0.019 0.004  207 ASP A N   
1592 C CA  . ASP A 207 ? 0.235 0.189 0.195 -0.005 -0.025 0.003  207 ASP A CA  
1593 C C   . ASP A 207 ? 0.243 0.192 0.199 -0.006 -0.024 0.002  207 ASP A C   
1594 O O   . ASP A 207 ? 0.275 0.212 0.221 -0.005 -0.029 0.001  207 ASP A O   
1595 C CB  . ASP A 207 ? 0.245 0.190 0.195 -0.001 -0.028 0.001  207 ASP A CB  
1596 C CG  . ASP A 207 ? 0.246 0.190 0.190 0.005  -0.022 -0.000 207 ASP A CG  
1597 O OD1 . ASP A 207 ? 0.257 0.205 0.205 0.005  -0.016 -0.000 207 ASP A OD1 
1598 O OD2 . ASP A 207 ? 0.268 0.206 0.204 0.008  -0.023 -0.001 207 ASP A OD2 
1599 N N   A VAL A 208 ? 0.232 0.187 0.192 -0.006 -0.018 0.002  208 VAL A N   
1600 N N   B VAL A 208 ? 0.247 0.203 0.207 -0.006 -0.018 0.002  208 VAL A N   
1601 C CA  A VAL A 208 ? 0.232 0.182 0.187 -0.006 -0.017 0.001  208 VAL A CA  
1602 C CA  B VAL A 208 ? 0.258 0.210 0.214 -0.006 -0.017 0.002  208 VAL A CA  
1603 C C   A VAL A 208 ? 0.232 0.191 0.193 -0.008 -0.013 0.003  208 VAL A C   
1604 C C   B VAL A 208 ? 0.244 0.205 0.208 -0.009 -0.013 0.004  208 VAL A C   
1605 O O   A VAL A 208 ? 0.237 0.202 0.202 -0.005 -0.008 0.002  208 VAL A O   
1606 O O   B VAL A 208 ? 0.243 0.213 0.213 -0.007 -0.009 0.004  208 VAL A O   
1607 C CB  A VAL A 208 ? 0.240 0.184 0.187 0.000  -0.015 -0.002 208 VAL A CB  
1608 C CB  B VAL A 208 ? 0.301 0.250 0.252 -0.001 -0.013 -0.001 208 VAL A CB  
1609 C CG1 A VAL A 208 ? 0.236 0.186 0.187 0.003  -0.010 -0.002 208 VAL A CG1 
1610 C CG1 B VAL A 208 ? 0.336 0.281 0.284 -0.000 -0.012 -0.002 208 VAL A CG1 
1611 C CG2 A VAL A 208 ? 0.269 0.210 0.213 0.001  -0.015 -0.003 208 VAL A CG2 
1612 C CG2 B VAL A 208 ? 0.340 0.281 0.283 0.004  -0.015 -0.003 208 VAL A CG2 
1613 N N   . VAL A 209 ? 0.232 0.191 0.194 -0.012 -0.015 0.006  209 VAL A N   
1614 C CA  . VAL A 209 ? 0.232 0.199 0.198 -0.013 -0.010 0.007  209 VAL A CA  
1615 C C   . VAL A 209 ? 0.232 0.193 0.192 -0.010 -0.009 0.005  209 VAL A C   
1616 O O   . VAL A 209 ? 0.239 0.189 0.192 -0.010 -0.013 0.004  209 VAL A O   
1617 C CB  . VAL A 209 ? 0.227 0.198 0.197 -0.019 -0.012 0.013  209 VAL A CB  
1618 C CG1 . VAL A 209 ? 0.224 0.202 0.194 -0.020 -0.008 0.015  209 VAL A CG1 
1619 C CG2 . VAL A 209 ? 0.235 0.218 0.215 -0.022 -0.013 0.016  209 VAL A CG2 
1620 N N   . GLY A 210 ? 0.223 0.189 0.184 -0.007 -0.005 0.003  210 GLY A N   
1621 C CA  . GLY A 210 ? 0.224 0.185 0.180 -0.005 -0.004 0.001  210 GLY A CA  
1622 C C   . GLY A 210 ? 0.232 0.199 0.190 -0.003 -0.001 -0.001 210 GLY A C   
1623 O O   . GLY A 210 ? 0.214 0.188 0.176 -0.003 0.001  -0.001 210 GLY A O   
1624 N N   . GLY A 211 ? 0.235 0.200 0.190 -0.002 -0.002 -0.002 211 GLY A N   
1625 C CA  . GLY A 211 ? 0.211 0.179 0.166 -0.000 -0.000 -0.004 211 GLY A CA  
1626 C C   . GLY A 211 ? 0.220 0.186 0.175 0.002  -0.002 -0.006 211 GLY A C   
1627 O O   . GLY A 211 ? 0.226 0.189 0.181 0.003  -0.004 -0.006 211 GLY A O   
1628 N N   . ALA A 212 ? 0.226 0.193 0.181 0.003  -0.003 -0.009 212 ALA A N   
1629 C CA  . ALA A 212 ? 0.221 0.188 0.179 0.003  -0.005 -0.010 212 ALA A CA  
1630 C C   . ALA A 212 ? 0.226 0.191 0.180 0.004  -0.008 -0.013 212 ALA A C   
1631 O O   . ALA A 212 ? 0.229 0.192 0.179 0.005  -0.007 -0.014 212 ALA A O   
1632 C CB  . ALA A 212 ? 0.238 0.207 0.204 0.003  -0.005 -0.010 212 ALA A CB  
1633 N N   . LEU A 213 ? 0.229 0.194 0.184 0.004  -0.011 -0.013 213 LEU A N   
1634 C CA  . LEU A 213 ? 0.235 0.198 0.188 0.004  -0.016 -0.016 213 LEU A CA  
1635 C C   . LEU A 213 ? 0.237 0.204 0.201 0.002  -0.020 -0.016 213 LEU A C   
1636 O O   . LEU A 213 ? 0.241 0.214 0.212 0.002  -0.018 -0.013 213 LEU A O   
1637 C CB  . LEU A 213 ? 0.242 0.204 0.188 0.006  -0.019 -0.016 213 LEU A CB  
1638 C CG  . LEU A 213 ? 0.247 0.206 0.182 0.007  -0.015 -0.014 213 LEU A CG  
1639 C CD1 . LEU A 213 ? 0.265 0.222 0.192 0.009  -0.018 -0.013 213 LEU A CD1 
1640 C CD2 . LEU A 213 ? 0.259 0.218 0.189 0.009  -0.013 -0.017 213 LEU A CD2 
1641 N N   . VAL A 214 ? 0.236 0.199 0.201 0.000  -0.024 -0.018 214 VAL A N   
1642 C CA  . VAL A 214 ? 0.226 0.193 0.203 -0.003 -0.029 -0.016 214 VAL A CA  
1643 C C   . VAL A 214 ? 0.246 0.208 0.218 -0.004 -0.037 -0.020 214 VAL A C   
1644 O O   . VAL A 214 ? 0.259 0.210 0.220 -0.002 -0.039 -0.024 214 VAL A O   
1645 C CB  . VAL A 214 ? 0.232 0.200 0.217 -0.007 -0.028 -0.014 214 VAL A CB  
1646 C CG1 . VAL A 214 ? 0.254 0.228 0.253 -0.012 -0.033 -0.011 214 VAL A CG1 
1647 C CG2 . VAL A 214 ? 0.254 0.226 0.241 -0.006 -0.020 -0.011 214 VAL A CG2 
1648 N N   . VAL A 215 ? 0.238 0.205 0.218 -0.006 -0.043 -0.018 215 VAL A N   
1649 C CA  . VAL A 215 ? 0.250 0.212 0.226 -0.006 -0.052 -0.022 215 VAL A CA  
1650 C C   . VAL A 215 ? 0.271 0.238 0.262 -0.013 -0.060 -0.019 215 VAL A C   
1651 O O   . VAL A 215 ? 0.265 0.245 0.271 -0.016 -0.057 -0.014 215 VAL A O   
1652 C CB  . VAL A 215 ? 0.279 0.242 0.246 -0.002 -0.054 -0.023 215 VAL A CB  
1653 C CG1 . VAL A 215 ? 0.311 0.267 0.263 0.003  -0.047 -0.024 215 VAL A CG1 
1654 C CG2 . VAL A 215 ? 0.265 0.241 0.245 -0.002 -0.052 -0.018 215 VAL A CG2 
1655 N N   . ALA A 216 ? 0.285 0.241 0.271 -0.015 -0.070 -0.023 216 ALA A N   
1656 C CA  . ALA A 216 ? 0.308 0.268 0.309 -0.022 -0.081 -0.021 216 ALA A CA  
1657 C C   . ALA A 216 ? 0.299 0.270 0.307 -0.022 -0.086 -0.019 216 ALA A C   
1658 O O   . ALA A 216 ? 0.325 0.308 0.351 -0.028 -0.092 -0.014 216 ALA A O   
1659 C CB  . ALA A 216 ? 0.339 0.280 0.329 -0.024 -0.091 -0.027 216 ALA A CB  
1660 N N   . ASP A 217 ? 0.290 0.257 0.283 -0.015 -0.086 -0.023 217 ASP A N   
1661 C CA  . ASP A 217 ? 0.306 0.279 0.301 -0.013 -0.093 -0.023 217 ASP A CA  
1662 C C   . ASP A 217 ? 0.292 0.279 0.292 -0.008 -0.085 -0.018 217 ASP A C   
1663 O O   . ASP A 217 ? 0.289 0.272 0.276 -0.003 -0.076 -0.019 217 ASP A O   
1664 C CB  . ASP A 217 ? 0.335 0.292 0.308 -0.009 -0.100 -0.029 217 ASP A CB  
1665 C CG  . ASP A 217 ? 0.380 0.344 0.356 -0.007 -0.108 -0.029 217 ASP A CG  
1666 O OD1 . ASP A 217 ? 0.443 0.406 0.425 -0.012 -0.120 -0.029 217 ASP A OD1 
1667 O OD2 . ASP A 217 ? 0.381 0.348 0.350 -0.002 -0.103 -0.027 217 ASP A OD2 
1668 N N   . ALA A 218 ? 0.281 0.285 0.299 -0.010 -0.087 -0.013 218 ALA A N   
1669 C CA  . ALA A 218 ? 0.278 0.295 0.302 -0.003 -0.079 -0.010 218 ALA A CA  
1670 C C   . ALA A 218 ? 0.273 0.281 0.279 0.004  -0.080 -0.013 218 ALA A C   
1671 O O   . ALA A 218 ? 0.257 0.264 0.256 0.010  -0.073 -0.012 218 ALA A O   
1672 C CB  . ALA A 218 ? 0.278 0.317 0.325 -0.005 -0.082 -0.004 218 ALA A CB  
1673 N N   . GLU A 219 ? 0.286 0.289 0.251 -0.002 -0.042 -0.022 219 GLU A N   
1674 C CA  . GLU A 219 ? 0.286 0.283 0.253 0.007  -0.057 -0.018 219 GLU A CA  
1675 C C   . GLU A 219 ? 0.291 0.275 0.224 0.011  -0.050 -0.012 219 GLU A C   
1676 O O   . GLU A 219 ? 0.298 0.283 0.234 0.015  -0.051 -0.012 219 GLU A O   
1677 C CB  . GLU A 219 ? 0.331 0.306 0.288 0.006  -0.080 -0.013 219 GLU A CB  
1678 C CG  . GLU A 219 ? 0.358 0.341 0.365 0.008  -0.100 -0.020 219 GLU A CG  
1679 C CD  . GLU A 219 ? 0.337 0.324 0.373 0.016  -0.109 -0.025 219 GLU A CD  
1680 O OE1 . GLU A 219 ? 0.382 0.340 0.379 0.017  -0.121 -0.015 219 GLU A OE1 
1681 O OE2 . GLU A 219 ? 0.367 0.385 0.465 0.018  -0.100 -0.042 219 GLU A OE2 
1682 N N   . LEU A 220 ? 0.294 0.269 0.204 0.009  -0.045 -0.011 220 LEU A N   
1683 C CA  . LEU A 220 ? 0.298 0.268 0.197 0.013  -0.037 -0.013 220 LEU A CA  
1684 C C   . LEU A 220 ? 0.279 0.261 0.191 0.016  -0.032 -0.013 220 LEU A C   
1685 O O   . LEU A 220 ? 0.289 0.272 0.202 0.019  -0.028 -0.015 220 LEU A O   
1686 C CB  . LEU A 220 ? 0.300 0.260 0.192 0.013  -0.035 -0.017 220 LEU A CB  
1687 C CG  . LEU A 220 ? 0.324 0.285 0.228 0.017  -0.028 -0.026 220 LEU A CG  
1688 C CD1 . LEU A 220 ? 0.363 0.319 0.256 0.011  -0.015 -0.032 220 LEU A CD1 
1689 C CD2 . LEU A 220 ? 0.337 0.288 0.249 0.019  -0.030 -0.035 220 LEU A CD2 
1690 N N   . GLY A 221 ? 0.269 0.252 0.180 0.011  -0.030 -0.013 221 GLY A N   
1691 C CA  . GLY A 221 ? 0.270 0.253 0.179 0.008  -0.025 -0.014 221 GLY A CA  
1692 C C   . GLY A 221 ? 0.255 0.253 0.183 0.012  -0.020 -0.017 221 GLY A C   
1693 O O   . GLY A 221 ? 0.257 0.253 0.181 0.014  -0.018 -0.017 221 GLY A O   
1694 N N   . GLU A 222 ? 0.247 0.256 0.199 0.013  -0.022 -0.021 222 GLU A N   
1695 C CA  . GLU A 222 ? 0.255 0.272 0.231 0.019  -0.025 -0.026 222 GLU A CA  
1696 C C   . GLU A 222 ? 0.259 0.262 0.215 0.024  -0.035 -0.018 222 GLU A C   
1697 O O   . GLU A 222 ? 0.263 0.268 0.223 0.028  -0.035 -0.019 222 GLU A O   
1698 C CB  . GLU A 222 ? 0.280 0.307 0.297 0.020  -0.036 -0.034 222 GLU A CB  
1699 C CG  . GLU A 222 ? 0.305 0.351 0.356 0.011  -0.018 -0.050 222 GLU A CG  
1700 C CD  . GLU A 222 ? 0.398 0.454 0.463 0.005  0.004  -0.064 222 GLU A CD  
1701 O OE1 . GLU A 222 ? 0.425 0.476 0.479 0.012  0.001  -0.059 222 GLU A OE1 
1702 O OE2 . GLU A 222 ? 0.528 0.593 0.608 -0.010 0.026  -0.080 222 GLU A OE2 
1703 N N   . ARG A 223 ? 0.290 0.278 0.222 0.022  -0.040 -0.013 223 ARG A N   
1704 C CA  A ARG A 223 ? 0.301 0.271 0.205 0.018  -0.040 -0.011 223 ARG A CA  
1705 C CA  B ARG A 223 ? 0.304 0.275 0.209 0.018  -0.039 -0.011 223 ARG A CA  
1706 C C   . ARG A 223 ? 0.302 0.283 0.210 0.020  -0.025 -0.014 223 ARG A C   
1707 O O   . ARG A 223 ? 0.312 0.288 0.213 0.018  -0.023 -0.015 223 ARG A O   
1708 C CB  A ARG A 223 ? 0.335 0.281 0.207 0.008  -0.039 -0.010 223 ARG A CB  
1709 C CB  B ARG A 223 ? 0.342 0.291 0.217 0.008  -0.038 -0.011 223 ARG A CB  
1710 C CG  A ARG A 223 ? 0.355 0.285 0.221 0.004  -0.059 -0.006 223 ARG A CG  
1711 C CG  B ARG A 223 ? 0.381 0.299 0.231 0.000  -0.059 -0.005 223 ARG A CG  
1712 C CD  A ARG A 223 ? 0.395 0.285 0.209 -0.012 -0.060 -0.005 223 ARG A CD  
1713 C CD  B ARG A 223 ? 0.427 0.305 0.221 -0.019 -0.053 -0.006 223 ARG A CD  
1714 N NE  A ARG A 223 ? 0.414 0.308 0.221 -0.016 -0.041 -0.012 223 ARG A NE  
1715 N NE  B ARG A 223 ? 0.494 0.332 0.261 -0.027 -0.086 0.003  223 ARG A NE  
1716 C CZ  A ARG A 223 ? 0.402 0.301 0.217 -0.013 -0.046 -0.011 223 ARG A CZ  
1717 C CZ  B ARG A 223 ? 0.527 0.321 0.257 -0.038 -0.108 0.009  223 ARG A CZ  
1718 N NH1 A ARG A 223 ? 0.438 0.333 0.245 -0.018 -0.029 -0.020 223 ARG A NH1 
1719 N NH1 B ARG A 223 ? 0.539 0.292 0.253 -0.043 -0.149 0.018  223 ARG A NH1 
1720 N NH2 A ARG A 223 ? 0.331 0.239 0.169 -0.007 -0.064 -0.005 223 ARG A NH2 
1721 N NH2 B ARG A 223 ? 0.564 0.352 0.275 -0.044 -0.096 0.007  223 ARG A NH2 
1722 N N   . LEU A 224 ? 0.269 0.259 0.187 0.023  -0.021 -0.017 224 LEU A N   
1723 C CA  . LEU A 224 ? 0.263 0.257 0.192 0.026  -0.018 -0.020 224 LEU A CA  
1724 C C   . LEU A 224 ? 0.258 0.256 0.188 0.027  -0.019 -0.017 224 LEU A C   
1725 O O   . LEU A 224 ? 0.276 0.275 0.211 0.029  -0.018 -0.018 224 LEU A O   
1726 C CB  . LEU A 224 ? 0.254 0.243 0.190 0.028  -0.026 -0.022 224 LEU A CB  
1727 C CG  . LEU A 224 ? 0.271 0.257 0.215 0.028  -0.024 -0.030 224 LEU A CG  
1728 C CD1 . LEU A 224 ? 0.287 0.261 0.234 0.031  -0.038 -0.030 224 LEU A CD1 
1729 C CD2 . LEU A 224 ? 0.267 0.261 0.239 0.029  -0.013 -0.046 224 LEU A CD2 
1730 N N   . ALA A 225 ? 0.246 0.246 0.176 0.025  -0.018 -0.015 225 ALA A N   
1731 C CA  . ALA A 225 ? 0.253 0.254 0.183 0.023  -0.013 -0.018 225 ALA A CA  
1732 C C   . ALA A 225 ? 0.252 0.257 0.191 0.028  -0.015 -0.018 225 ALA A C   
1733 O O   . ALA A 225 ? 0.245 0.248 0.182 0.029  -0.012 -0.018 225 ALA A O   
1734 C CB  . ALA A 225 ? 0.258 0.263 0.196 0.015  -0.003 -0.025 225 ALA A CB  
1735 N N   . PHE A 226 ? 0.247 0.249 0.190 0.030  -0.023 -0.017 226 PHE A N   
1736 C CA  . PHE A 226 ? 0.274 0.264 0.211 0.031  -0.033 -0.015 226 PHE A CA  
1737 C C   . PHE A 226 ? 0.265 0.250 0.182 0.027  -0.025 -0.013 226 PHE A C   
1738 O O   . PHE A 226 ? 0.280 0.259 0.194 0.027  -0.027 -0.012 226 PHE A O   
1739 C CB  . PHE A 226 ? 0.287 0.254 0.208 0.027  -0.050 -0.011 226 PHE A CB  
1740 C CG  . PHE A 226 ? 0.318 0.255 0.215 0.022  -0.065 -0.007 226 PHE A CG  
1741 C CD1 . PHE A 226 ? 0.342 0.272 0.264 0.030  -0.087 -0.009 226 PHE A CD1 
1742 C CD2 . PHE A 226 ? 0.349 0.262 0.199 0.007  -0.057 -0.004 226 PHE A CD2 
1743 C CE1 . PHE A 226 ? 0.395 0.288 0.288 0.024  -0.108 -0.004 226 PHE A CE1 
1744 C CE2 . PHE A 226 ? 0.396 0.270 0.208 -0.004 -0.071 0.000  226 PHE A CE2 
1745 C CZ  . PHE A 226 ? 0.426 0.288 0.257 0.006  -0.100 0.003  226 PHE A CZ  
1746 N N   . HIS A 227 ? 0.250 0.236 0.163 0.023  -0.016 -0.016 227 HIS A N   
1747 C CA  . HIS A 227 ? 0.261 0.249 0.175 0.018  -0.006 -0.022 227 HIS A CA  
1748 C C   . HIS A 227 ? 0.250 0.249 0.183 0.025  -0.009 -0.022 227 HIS A C   
1749 O O   . HIS A 227 ? 0.248 0.248 0.187 0.022  -0.006 -0.025 227 HIS A O   
1750 C CB  . HIS A 227 ? 0.272 0.259 0.188 0.011  0.005  -0.032 227 HIS A CB  
1751 C CG  . HIS A 227 ? 0.330 0.291 0.206 -0.004 0.009  -0.031 227 HIS A CG  
1752 N ND1 . HIS A 227 ? 0.319 0.267 0.178 -0.004 -0.003 -0.024 227 HIS A ND1 
1753 C CD2 . HIS A 227 ? 0.403 0.340 0.245 -0.025 0.023  -0.038 227 HIS A CD2 
1754 C CE1 . HIS A 227 ? 0.382 0.291 0.192 -0.024 -0.003 -0.024 227 HIS A CE1 
1755 N NE2 . HIS A 227 ? 0.440 0.340 0.234 -0.039 0.015  -0.033 227 HIS A NE2 
1756 N N   . GLN A 228 ? 0.244 0.244 0.181 0.029  -0.016 -0.019 228 GLN A N   
1757 C CA  . GLN A 228 ? 0.246 0.238 0.181 0.029  -0.023 -0.017 228 GLN A CA  
1758 C C   . GLN A 228 ? 0.248 0.238 0.174 0.028  -0.019 -0.015 228 GLN A C   
1759 O O   . GLN A 228 ? 0.259 0.244 0.185 0.027  -0.023 -0.014 228 GLN A O   
1760 C CB  . GLN A 228 ? 0.260 0.238 0.178 0.024  -0.028 -0.013 228 GLN A CB  
1761 C CG  . GLN A 228 ? 0.282 0.232 0.177 0.017  -0.040 -0.010 228 GLN A CG  
1762 C CD  . GLN A 228 ? 0.325 0.247 0.181 0.001  -0.040 -0.008 228 GLN A CD  
1763 O OE1 . GLN A 228 ? 0.320 0.254 0.174 -0.004 -0.020 -0.013 228 GLN A OE1 
1764 N NE2 . GLN A 228 ? 0.346 0.229 0.172 -0.008 -0.063 -0.002 228 GLN A NE2 
1765 N N   . ASN A 229 ? 0.245 0.238 0.169 0.029  -0.014 -0.015 229 ASN A N   
1766 C CA  . ASN A 229 ? 0.240 0.231 0.164 0.030  -0.012 -0.017 229 ASN A CA  
1767 C C   . ASN A 229 ? 0.262 0.248 0.181 0.030  -0.016 -0.014 229 ASN A C   
1768 O O   . ASN A 229 ? 0.269 0.250 0.183 0.030  -0.017 -0.014 229 ASN A O   
1769 C CB  . ASN A 229 ? 0.243 0.240 0.187 0.032  -0.009 -0.025 229 ASN A CB  
1770 C CG  . ASN A 229 ? 0.251 0.246 0.209 0.035  -0.008 -0.032 229 ASN A CG  
1771 O OD1 . ASN A 229 ? 0.273 0.262 0.219 0.030  0.002  -0.035 229 ASN A OD1 
1772 N ND2 . ASN A 229 ? 0.276 0.271 0.261 0.043  -0.022 -0.037 229 ASN A ND2 
1773 N N   A SER A 230 ? 0.262 0.243 0.174 0.027  -0.019 -0.013 230 SER A N   
1774 N N   B SER A 230 ? 0.274 0.255 0.186 0.027  -0.019 -0.013 230 SER A N   
1775 C CA  A SER A 230 ? 0.279 0.242 0.169 0.019  -0.022 -0.011 230 SER A CA  
1776 C CA  B SER A 230 ? 0.299 0.261 0.189 0.020  -0.022 -0.011 230 SER A CA  
1777 C C   A SER A 230 ? 0.274 0.241 0.163 0.011  -0.010 -0.016 230 SER A C   
1778 C C   B SER A 230 ? 0.289 0.254 0.175 0.010  -0.009 -0.016 230 SER A C   
1779 O O   A SER A 230 ? 0.291 0.246 0.165 0.005  -0.010 -0.015 230 SER A O   
1780 O O   B SER A 230 ? 0.307 0.256 0.172 0.000  -0.009 -0.016 230 SER A O   
1781 C CB  A SER A 230 ? 0.298 0.240 0.165 0.012  -0.029 -0.009 230 SER A CB  
1782 C CB  B SER A 230 ? 0.333 0.271 0.200 0.013  -0.034 -0.008 230 SER A CB  
1783 O OG  A SER A 230 ? 0.293 0.229 0.173 0.021  -0.048 -0.007 230 SER A OG  
1784 O OG  B SER A 230 ? 0.347 0.288 0.207 0.006  -0.023 -0.011 230 SER A OG  
1785 N N   . MET A 231 ? 0.257 0.240 0.167 0.011  -0.001 -0.023 231 MET A N   
1786 C CA  . MET A 231 ? 0.257 0.252 0.192 0.005  0.009  -0.035 231 MET A CA  
1787 C C   . MET A 231 ? 0.244 0.245 0.201 0.014  -0.004 -0.032 231 MET A C   
1788 O O   . MET A 231 ? 0.249 0.256 0.228 0.011  -0.003 -0.040 231 MET A O   
1789 C CB  . MET A 231 ? 0.260 0.266 0.221 0.001  0.020  -0.049 231 MET A CB  
1790 C CG  . MET A 231 ? 0.305 0.294 0.232 -0.017 0.038  -0.055 231 MET A CG  
1791 S SD  . MET A 231 ? 0.344 0.341 0.292 -0.019 0.050  -0.069 231 MET A SD  
1792 C CE  . MET A 231 ? 0.301 0.331 0.332 -0.011 0.053  -0.092 231 MET A CE  
1793 N N   . GLY A 232 ? 0.244 0.219 0.197 0.027  0.007  -0.003 232 GLY A N   
1794 C CA  . GLY A 232 ? 0.220 0.203 0.185 0.021  0.008  -0.002 232 GLY A CA  
1795 C C   . GLY A 232 ? 0.221 0.207 0.188 0.021  0.010  0.000  232 GLY A C   
1796 O O   . GLY A 232 ? 0.219 0.209 0.193 0.016  0.010  0.002  232 GLY A O   
1797 N N   . ALA A 233 ? 0.226 0.207 0.185 0.026  0.011  0.000  233 ALA A N   
1798 C CA  . ALA A 233 ? 0.220 0.204 0.182 0.026  0.013  0.004  233 ALA A CA  
1799 C C   . ALA A 233 ? 0.220 0.203 0.184 0.021  0.010  -0.000 233 ALA A C   
1800 O O   . ALA A 233 ? 0.234 0.214 0.193 0.024  0.010  -0.000 233 ALA A O   
1801 C CB  . ALA A 233 ? 0.241 0.220 0.192 0.035  0.017  0.007  233 ALA A CB  
1802 N N   . VAL A 234 ? 0.223 0.209 0.193 0.015  0.008  -0.002 234 VAL A N   
1803 C CA  . VAL A 234 ? 0.223 0.209 0.196 0.012  0.005  -0.005 234 VAL A CA  
1804 C C   . VAL A 234 ? 0.203 0.192 0.179 0.009  0.007  -0.003 234 VAL A C   
1805 O O   . VAL A 234 ? 0.215 0.207 0.194 0.008  0.007  0.000  234 VAL A O   
1806 C CB  . VAL A 234 ? 0.235 0.221 0.211 0.009  0.005  -0.006 234 VAL A CB  
1807 C CG1 . VAL A 234 ? 0.252 0.236 0.227 0.011  0.002  -0.008 234 VAL A CG1 
1808 C CG2 . VAL A 234 ? 0.241 0.228 0.219 0.007  0.006  -0.005 234 VAL A CG2 
1809 N N   . ALA A 235 ? 0.205 0.192 0.180 0.008  0.005  -0.005 235 ALA A N   
1810 C CA  . ALA A 235 ? 0.213 0.202 0.191 0.005  0.006  -0.004 235 ALA A CA  
1811 C C   . ALA A 235 ? 0.217 0.204 0.195 0.002  0.006  -0.005 235 ALA A C   
1812 O O   . ALA A 235 ? 0.222 0.208 0.201 0.003  0.006  -0.006 235 ALA A O   
1813 C CB  . ALA A 235 ? 0.224 0.211 0.202 0.005  0.005  -0.006 235 ALA A CB  
1814 N N   . GLY A 236 ? 0.210 0.196 0.187 -0.000 0.004  -0.003 236 GLY A N   
1815 C CA  . GLY A 236 ? 0.223 0.200 0.194 -0.002 0.004  -0.004 236 GLY A CA  
1816 C C   . GLY A 236 ? 0.222 0.197 0.190 -0.001 0.006  -0.005 236 GLY A C   
1817 O O   . GLY A 236 ? 0.222 0.201 0.194 -0.001 0.006  -0.005 236 GLY A O   
1818 N N   . PRO A 237 ? 0.224 0.190 0.184 0.001  0.008  -0.006 237 PRO A N   
1819 C CA  . PRO A 237 ? 0.228 0.192 0.186 0.003  0.012  -0.005 237 PRO A CA  
1820 C C   . PRO A 237 ? 0.228 0.188 0.182 0.002  0.010  -0.005 237 PRO A C   
1821 O O   . PRO A 237 ? 0.235 0.199 0.193 0.003  0.012  -0.005 237 PRO A O   
1822 C CB  . PRO A 237 ? 0.258 0.213 0.208 0.008  0.016  -0.004 237 PRO A CB  
1823 C CG  . PRO A 237 ? 0.274 0.222 0.216 0.006  0.012  -0.006 237 PRO A CG  
1824 C CD  . PRO A 237 ? 0.244 0.204 0.198 0.002  0.008  -0.006 237 PRO A CD  
1825 N N   . PHE A 238 ? 0.247 0.199 0.193 -0.001 0.004  -0.005 238 PHE A N   
1826 C CA  A PHE A 238 ? 0.254 0.201 0.194 -0.003 0.001  -0.005 238 PHE A CA  
1827 C CA  B PHE A 238 ? 0.257 0.204 0.197 -0.003 0.001  -0.005 238 PHE A CA  
1828 C C   . PHE A 238 ? 0.245 0.205 0.199 -0.005 0.001  -0.004 238 PHE A C   
1829 O O   . PHE A 238 ? 0.244 0.206 0.199 -0.004 0.002  -0.004 238 PHE A O   
1830 C CB  A PHE A 238 ? 0.268 0.202 0.197 -0.006 -0.006 -0.004 238 PHE A CB  
1831 C CB  B PHE A 238 ? 0.274 0.209 0.204 -0.006 -0.007 -0.004 238 PHE A CB  
1832 C CG  A PHE A 238 ? 0.278 0.209 0.205 -0.008 -0.010 -0.003 238 PHE A CG  
1833 C CG  B PHE A 238 ? 0.297 0.223 0.220 -0.009 -0.013 -0.003 238 PHE A CG  
1834 C CD1 A PHE A 238 ? 0.292 0.215 0.208 -0.004 -0.007 -0.004 238 PHE A CD1 
1835 C CD1 B PHE A 238 ? 0.331 0.238 0.233 -0.006 -0.014 -0.004 238 PHE A CD1 
1836 C CD2 A PHE A 238 ? 0.305 0.241 0.240 -0.014 -0.018 0.001  238 PHE A CD2 
1837 C CD2 B PHE A 238 ? 0.314 0.248 0.248 -0.014 -0.019 0.001  238 PHE A CD2 
1838 C CE1 A PHE A 238 ? 0.298 0.217 0.211 -0.006 -0.011 -0.003 238 PHE A CE1 
1839 C CE1 B PHE A 238 ? 0.361 0.257 0.255 -0.009 -0.021 -0.003 238 PHE A CE1 
1840 C CE2 A PHE A 238 ? 0.303 0.235 0.235 -0.016 -0.022 0.003  238 PHE A CE2 
1841 C CE2 B PHE A 238 ? 0.321 0.248 0.250 -0.018 -0.026 0.003  238 PHE A CE2 
1842 C CZ  A PHE A 238 ? 0.311 0.234 0.231 -0.012 -0.019 -0.000 238 PHE A CZ  
1843 C CZ  B PHE A 238 ? 0.338 0.244 0.245 -0.015 -0.028 0.000  238 PHE A CZ  
1844 N N   . ASP A 239 ? 0.227 0.196 0.190 -0.006 -0.000 -0.002 239 ASP A N   
1845 C CA  . ASP A 239 ? 0.229 0.209 0.201 -0.006 0.000  -0.001 239 ASP A CA  
1846 C C   . ASP A 239 ? 0.218 0.200 0.192 -0.003 0.004  -0.003 239 ASP A C   
1847 O O   . ASP A 239 ? 0.219 0.203 0.195 -0.003 0.005  -0.003 239 ASP A O   
1848 C CB  . ASP A 239 ? 0.226 0.213 0.205 -0.005 0.000  0.002  239 ASP A CB  
1849 C CG  . ASP A 239 ? 0.258 0.246 0.241 -0.009 -0.004 0.008  239 ASP A CG  
1850 O OD1 . ASP A 239 ? 0.293 0.280 0.277 -0.011 -0.007 0.011  239 ASP A OD1 
1851 O OD2 . ASP A 239 ? 0.249 0.237 0.235 -0.009 -0.005 0.010  239 ASP A OD2 
1852 N N   . ALA A 240 ? 0.205 0.187 0.180 -0.001 0.006  -0.005 240 ALA A N   
1853 C CA  . ALA A 240 ? 0.202 0.186 0.181 -0.000 0.007  -0.006 240 ALA A CA  
1854 C C   . ALA A 240 ? 0.212 0.194 0.191 0.000  0.009  -0.005 240 ALA A C   
1855 O O   . ALA A 240 ? 0.211 0.195 0.195 0.000  0.009  -0.004 240 ALA A O   
1856 C CB  . ALA A 240 ? 0.205 0.190 0.188 0.001  0.008  -0.005 240 ALA A CB  
1857 N N   . TRP A 241 ? 0.217 0.193 0.189 0.001  0.011  -0.004 241 TRP A N   
1858 C CA  . TRP A 241 ? 0.216 0.188 0.184 0.003  0.014  -0.003 241 TRP A CA  
1859 C C   . TRP A 241 ? 0.215 0.188 0.183 0.001  0.012  -0.004 241 TRP A C   
1860 O O   . TRP A 241 ? 0.217 0.191 0.188 0.002  0.014  -0.002 241 TRP A O   
1861 C CB  . TRP A 241 ? 0.227 0.186 0.181 0.006  0.016  -0.003 241 TRP A CB  
1862 C CG  . TRP A 241 ? 0.235 0.188 0.182 0.010  0.021  -0.001 241 TRP A CG  
1863 C CD1 . TRP A 241 ? 0.239 0.192 0.189 0.015  0.029  0.004  241 TRP A CD1 
1864 C CD2 . TRP A 241 ? 0.242 0.185 0.177 0.010  0.019  -0.001 241 TRP A CD2 
1865 N NE1 . TRP A 241 ? 0.268 0.213 0.208 0.020  0.033  0.006  241 TRP A NE1 
1866 C CE2 . TRP A 241 ? 0.256 0.193 0.185 0.017  0.027  0.002  241 TRP A CE2 
1867 C CE3 . TRP A 241 ? 0.263 0.202 0.192 0.006  0.012  -0.003 241 TRP A CE3 
1868 C CZ2 . TRP A 241 ? 0.278 0.204 0.193 0.019  0.027  0.002  241 TRP A CZ2 
1869 C CZ3 . TRP A 241 ? 0.276 0.204 0.193 0.007  0.011  -0.003 241 TRP A CZ3 
1870 C CH2 . TRP A 241 ? 0.284 0.204 0.192 0.014  0.019  -0.001 241 TRP A CH2 
1871 N N   . LEU A 242 ? 0.223 0.195 0.188 -0.002 0.008  -0.004 242 LEU A N   
1872 C CA  . LEU A 242 ? 0.219 0.193 0.185 -0.004 0.005  -0.003 242 LEU A CA  
1873 C C   . LEU A 242 ? 0.215 0.197 0.190 -0.003 0.007  -0.003 242 LEU A C   
1874 O O   . LEU A 242 ? 0.230 0.213 0.206 -0.003 0.007  -0.003 242 LEU A O   
1875 C CB  . LEU A 242 ? 0.241 0.215 0.207 -0.007 0.000  -0.001 242 LEU A CB  
1876 C CG  . LEU A 242 ? 0.282 0.244 0.237 -0.009 -0.004 -0.000 242 LEU A CG  
1877 C CD1 . LEU A 242 ? 0.297 0.262 0.258 -0.013 -0.011 0.004  242 LEU A CD1 
1878 C CD2 . LEU A 242 ? 0.291 0.245 0.238 -0.008 -0.005 -0.000 242 LEU A CD2 
1879 N N   . THR A 243 ? 0.221 0.206 0.199 -0.002 0.006  -0.004 243 THR A N   
1880 C CA  . THR A 243 ? 0.225 0.212 0.206 -0.000 0.006  -0.004 243 THR A CA  
1881 C C   . THR A 243 ? 0.218 0.203 0.202 -0.001 0.006  -0.005 243 THR A C   
1882 O O   . THR A 243 ? 0.222 0.207 0.207 -0.000 0.006  -0.005 243 THR A O   
1883 C CB  . THR A 243 ? 0.219 0.205 0.199 0.001  0.005  -0.005 243 THR A CB  
1884 O OG1 . THR A 243 ? 0.221 0.210 0.201 0.002  0.006  -0.003 243 THR A OG1 
1885 C CG2 . THR A 243 ? 0.224 0.206 0.201 0.004  0.003  -0.006 243 THR A CG2 
1886 N N   . LEU A 244 ? 0.216 0.201 0.203 -0.001 0.008  -0.004 244 LEU A N   
1887 C CA  . LEU A 244 ? 0.223 0.210 0.218 -0.001 0.008  -0.001 244 LEU A CA  
1888 C C   . LEU A 244 ? 0.222 0.207 0.215 -0.000 0.011  -0.000 244 LEU A C   
1889 O O   . LEU A 244 ? 0.216 0.203 0.215 -0.001 0.010  0.002  244 LEU A O   
1890 C CB  . LEU A 244 ? 0.260 0.247 0.259 0.000  0.012  0.002  244 LEU A CB  
1891 C CG  . LEU A 244 ? 0.292 0.283 0.304 0.001  0.013  0.007  244 LEU A CG  
1892 C CD1 . LEU A 244 ? 0.295 0.287 0.316 -0.003 0.005  0.008  244 LEU A CD1 
1893 C CD2 . LEU A 244 ? 0.306 0.299 0.322 0.003  0.017  0.011  244 LEU A CD2 
1894 N N   . ARG A 245 ? 0.211 0.193 0.195 0.000  0.013  -0.001 245 ARG A N   
1895 C CA  . ARG A 245 ? 0.219 0.199 0.199 0.001  0.015  -0.000 245 ARG A CA  
1896 C C   . ARG A 245 ? 0.208 0.190 0.191 -0.001 0.012  -0.001 245 ARG A C   
1897 O O   . ARG A 245 ? 0.216 0.198 0.201 -0.000 0.013  0.000  245 ARG A O   
1898 C CB  . ARG A 245 ? 0.224 0.196 0.192 0.001  0.014  -0.001 245 ARG A CB  
1899 C CG  . ARG A 245 ? 0.226 0.192 0.186 0.003  0.016  0.000  245 ARG A CG  
1900 C CD  . ARG A 245 ? 0.247 0.201 0.191 0.002  0.012  -0.001 245 ARG A CD  
1901 N NE  . ARG A 245 ? 0.260 0.203 0.192 0.005  0.013  0.000  245 ARG A NE  
1902 C CZ  . ARG A 245 ? 0.267 0.204 0.191 0.004  0.009  0.000  245 ARG A CZ  
1903 N NH1 . ARG A 245 ? 0.280 0.201 0.186 0.008  0.011  0.001  245 ARG A NH1 
1904 N NH2 . ARG A 245 ? 0.267 0.213 0.201 -0.001 0.004  0.001  245 ARG A NH2 
1905 N N   . GLY A 246 ? 0.215 0.199 0.197 -0.001 0.009  -0.002 246 GLY A N   
1906 C CA  . GLY A 246 ? 0.216 0.201 0.197 -0.001 0.008  -0.002 246 GLY A CA  
1907 C C   . GLY A 246 ? 0.211 0.194 0.196 -0.000 0.007  -0.003 246 GLY A C   
1908 O O   . GLY A 246 ? 0.208 0.190 0.193 -0.000 0.007  -0.002 246 GLY A O   
1909 N N   . ILE A 247 ? 0.210 0.192 0.198 -0.001 0.005  -0.003 247 ILE A N   
1910 C CA  . ILE A 247 ? 0.221 0.198 0.212 -0.002 0.000  -0.003 247 ILE A CA  
1911 C C   . ILE A 247 ? 0.217 0.196 0.216 -0.003 0.001  0.000  247 ILE A C   
1912 O O   . ILE A 247 ? 0.227 0.201 0.227 -0.004 -0.004 0.001  247 ILE A O   
1913 C CB  . ILE A 247 ? 0.226 0.203 0.221 -0.003 -0.004 -0.002 247 ILE A CB  
1914 C CG1 . ILE A 247 ? 0.230 0.203 0.216 -0.000 -0.005 -0.006 247 ILE A CG1 
1915 C CG2 . ILE A 247 ? 0.240 0.212 0.243 -0.005 -0.010 0.000  247 ILE A CG2 
1916 C CD1 . ILE A 247 ? 0.237 0.209 0.225 -0.001 -0.007 -0.006 247 ILE A CD1 
1917 N N   . LYS A 248 ? 0.210 0.194 0.214 -0.003 0.006  0.003  248 LYS A N   
1918 C CA  . LYS A 248 ? 0.208 0.194 0.219 -0.003 0.009  0.007  248 LYS A CA  
1919 C C   . LYS A 248 ? 0.203 0.186 0.210 -0.003 0.008  0.006  248 LYS A C   
1920 O O   . LYS A 248 ? 0.225 0.209 0.240 -0.004 0.007  0.010  248 LYS A O   
1921 C CB  . LYS A 248 ? 0.219 0.207 0.228 0.000  0.016  0.010  248 LYS A CB  
1922 C CG  . LYS A 248 ? 0.247 0.237 0.261 0.001  0.018  0.012  248 LYS A CG  
1923 C CD  . LYS A 248 ? 0.290 0.278 0.299 0.006  0.026  0.015  248 LYS A CD  
1924 C CE  . LYS A 248 ? 0.306 0.294 0.315 0.008  0.028  0.017  248 LYS A CE  
1925 N NZ  . LYS A 248 ? 0.334 0.315 0.332 0.015  0.037  0.020  248 LYS A NZ  
1926 N N   . THR A 249 ? 0.207 0.189 0.204 -0.002 0.008  0.002  249 THR A N   
1927 C CA  . THR A 249 ? 0.222 0.202 0.215 -0.001 0.008  0.002  249 THR A CA  
1928 C C   . THR A 249 ? 0.220 0.193 0.206 -0.000 0.004  -0.000 249 THR A C   
1929 O O   . THR A 249 ? 0.223 0.194 0.204 0.002  0.005  -0.000 249 THR A O   
1930 C CB  . THR A 249 ? 0.222 0.203 0.209 -0.000 0.011  0.002  249 THR A CB  
1931 O OG1 . THR A 249 ? 0.212 0.195 0.195 -0.000 0.010  0.001  249 THR A OG1 
1932 C CG2 . THR A 249 ? 0.231 0.213 0.218 0.000  0.015  0.004  249 THR A CG2 
1933 N N   . LEU A 250 ? 0.228 0.196 0.212 0.000  -0.000 -0.002 250 LEU A N   
1934 C CA  . LEU A 250 ? 0.225 0.183 0.197 0.003  -0.004 -0.004 250 LEU A CA  
1935 C C   . LEU A 250 ? 0.239 0.189 0.208 0.004  -0.007 -0.004 250 LEU A C   
1936 O O   . LEU A 250 ? 0.249 0.192 0.206 0.009  -0.005 -0.004 250 LEU A O   
1937 C CB  . LEU A 250 ? 0.236 0.187 0.205 0.003  -0.009 -0.005 250 LEU A CB  
1938 C CG  . LEU A 250 ? 0.254 0.189 0.205 0.008  -0.013 -0.008 250 LEU A CG  
1939 C CD1 . LEU A 250 ? 0.284 0.221 0.226 0.015  -0.005 -0.007 250 LEU A CD1 
1940 C CD2 . LEU A 250 ? 0.286 0.212 0.233 0.007  -0.020 -0.009 250 LEU A CD2 
1941 N N   . GLY A 251 ? 0.247 0.195 0.224 -0.000 -0.011 -0.002 251 GLY A N   
1942 C CA  . GLY A 251 ? 0.254 0.192 0.228 -0.001 -0.016 -0.001 251 GLY A CA  
1943 C C   . GLY A 251 ? 0.260 0.203 0.232 0.002  -0.009 -0.001 251 GLY A C   
1944 O O   . GLY A 251 ? 0.268 0.200 0.226 0.006  -0.010 -0.002 251 GLY A O   
1945 N N   . VAL A 252 ? 0.241 0.196 0.222 0.000  -0.003 0.001  252 VAL A N   
1946 C CA  . VAL A 252 ? 0.243 0.202 0.223 0.002  0.002  0.002  252 VAL A CA  
1947 C C   . VAL A 252 ? 0.246 0.206 0.217 0.007  0.005  0.001  252 VAL A C   
1948 O O   . VAL A 252 ? 0.264 0.222 0.229 0.010  0.007  0.002  252 VAL A O   
1949 C CB  . VAL A 252 ? 0.244 0.213 0.234 0.000  0.006  0.005  252 VAL A CB  
1950 C CG1 . VAL A 252 ? 0.254 0.223 0.255 -0.002 0.005  0.008  252 VAL A CG1 
1951 C CG2 . VAL A 252 ? 0.235 0.211 0.226 0.000  0.009  0.004  252 VAL A CG2 
1952 N N   . ARG A 253 ? 0.232 0.196 0.202 0.008  0.006  0.001  253 ARG A N   
1953 C CA  . ARG A 253 ? 0.234 0.199 0.198 0.012  0.010  0.002  253 ARG A CA  
1954 C C   . ARG A 253 ? 0.255 0.208 0.206 0.019  0.010  0.002  253 ARG A C   
1955 O O   . ARG A 253 ? 0.256 0.208 0.201 0.024  0.014  0.005  253 ARG A O   
1956 C CB  . ARG A 253 ? 0.228 0.200 0.195 0.012  0.011  0.003  253 ARG A CB  
1957 C CG  . ARG A 253 ? 0.216 0.197 0.191 0.007  0.012  0.004  253 ARG A CG  
1958 C CD  . ARG A 253 ? 0.215 0.200 0.192 0.006  0.011  0.004  253 ARG A CD  
1959 N NE  . ARG A 253 ? 0.218 0.200 0.195 0.005  0.010  0.001  253 ARG A NE  
1960 C CZ  . ARG A 253 ? 0.226 0.203 0.197 0.008  0.009  0.000  253 ARG A CZ  
1961 N NH1 . ARG A 253 ? 0.220 0.195 0.185 0.013  0.011  0.002  253 ARG A NH1 
1962 N NH2 . ARG A 253 ? 0.230 0.206 0.203 0.006  0.006  -0.002 253 ARG A NH2 
1963 N N   A MET A 254 ? 0.228 0.195 0.186 0.005  0.004  0.005  254 MET A N   
1964 N N   B MET A 254 ? 0.250 0.217 0.208 0.005  0.004  0.005  254 MET A N   
1965 C CA  A MET A 254 ? 0.232 0.195 0.186 0.006  0.003  0.003  254 MET A CA  
1966 C CA  B MET A 254 ? 0.270 0.233 0.224 0.006  0.003  0.003  254 MET A CA  
1967 C C   A MET A 254 ? 0.258 0.209 0.213 -0.001 -0.000 0.000  254 MET A C   
1968 C C   B MET A 254 ? 0.276 0.227 0.230 -0.001 -0.001 -0.001 254 MET A C   
1969 O O   A MET A 254 ? 0.261 0.201 0.213 0.002  -0.001 -0.003 254 MET A O   
1970 O O   B MET A 254 ? 0.273 0.216 0.225 0.002  -0.002 -0.005 254 MET A O   
1971 C CB  A MET A 254 ? 0.217 0.195 0.169 0.008  0.001  -0.001 254 MET A CB  
1972 C CB  B MET A 254 ? 0.290 0.269 0.242 0.011  0.002  0.001  254 MET A CB  
1973 C CG  A MET A 254 ? 0.217 0.200 0.163 0.015  -0.002 -0.007 254 MET A CG  
1974 C CG  B MET A 254 ? 0.305 0.291 0.258 0.024  0.009  0.011  254 MET A CG  
1975 S SD  A MET A 254 ? 0.225 0.204 0.167 0.026  0.005  0.001  254 MET A SD  
1976 S SD  B MET A 254 ? 0.416 0.413 0.357 0.036  0.010  0.011  254 MET A SD  
1977 C CE  A MET A 254 ? 0.247 0.250 0.185 0.042  0.012  0.013  254 MET A CE  
1978 C CE  B MET A 254 ? 0.366 0.344 0.307 0.028  0.005  0.001  254 MET A CE  
1979 N N   . ASP A 255 ? 0.254 0.205 0.214 -0.008 0.000  0.004  255 ASP A N   
1980 C CA  . ASP A 255 ? 0.281 0.217 0.248 -0.013 0.001  0.008  255 ASP A CA  
1981 C C   . ASP A 255 ? 0.283 0.207 0.242 -0.006 0.001  0.011  255 ASP A C   
1982 O O   . ASP A 255 ? 0.300 0.208 0.263 -0.006 -0.000 0.009  255 ASP A O   
1983 C CB  . ASP A 255 ? 0.275 0.217 0.252 -0.020 0.006  0.019  255 ASP A CB  
1984 C CG  . ASP A 255 ? 0.292 0.244 0.286 -0.030 0.005  0.014  255 ASP A CG  
1985 O OD1 . ASP A 255 ? 0.284 0.237 0.284 -0.031 -0.002 -0.002 255 ASP A OD1 
1986 O OD2 . ASP A 255 ? 0.319 0.283 0.323 -0.034 0.011  0.025  255 ASP A OD2 
1987 N N   . ARG A 256 ? 0.273 0.206 0.225 -0.000 0.002  0.014  256 ARG A N   
1988 C CA  . ARG A 256 ? 0.279 0.207 0.226 0.007  0.001  0.016  256 ARG A CA  
1989 C C   . ARG A 256 ? 0.282 0.206 0.232 0.011  -0.000 0.008  256 ARG A C   
1990 O O   . ARG A 256 ? 0.295 0.210 0.243 0.015  -0.001 0.008  256 ARG A O   
1991 C CB  . ARG A 256 ? 0.270 0.216 0.214 0.014  0.001  0.015  256 ARG A CB  
1992 C CG  . ARG A 256 ? 0.284 0.233 0.225 0.023  -0.002 0.014  256 ARG A CG  
1993 C CD  . ARG A 256 ? 0.298 0.239 0.232 0.028  -0.000 0.027  256 ARG A CD  
1994 N NE  . ARG A 256 ? 0.317 0.265 0.247 0.027  0.006  0.042  256 ARG A NE  
1995 C CZ  . ARG A 256 ? 0.325 0.298 0.246 0.037  0.007  0.048  256 ARG A CZ  
1996 N NH1 . ARG A 256 ? 0.322 0.315 0.235 0.050  0.000  0.037  256 ARG A NH1 
1997 N NH2 . ARG A 256 ? 0.331 0.313 0.251 0.036  0.015  0.063  256 ARG A NH2 
1998 N N   . HIS A 257 ? 0.267 0.197 0.219 0.011  0.001  0.004  257 HIS A N   
1999 C CA  . HIS A 257 ? 0.269 0.200 0.224 0.016  0.003  0.002  257 HIS A CA  
2000 C C   . HIS A 257 ? 0.278 0.200 0.226 0.018  0.001  -0.002 257 HIS A C   
2001 O O   . HIS A 257 ? 0.286 0.206 0.235 0.024  0.002  -0.004 257 HIS A O   
2002 C CB  . HIS A 257 ? 0.256 0.198 0.214 0.018  0.007  0.005  257 HIS A CB  
2003 C CG  . HIS A 257 ? 0.241 0.188 0.215 0.019  0.011  0.008  257 HIS A CG  
2004 N ND1 . HIS A 257 ? 0.250 0.197 0.242 0.021  0.014  0.008  257 HIS A ND1 
2005 C CD2 . HIS A 257 ? 0.246 0.199 0.225 0.018  0.012  0.009  257 HIS A CD2 
2006 C CE1 . HIS A 257 ? 0.257 0.207 0.269 0.020  0.016  0.008  257 HIS A CE1 
2007 N NE2 . HIS A 257 ? 0.247 0.199 0.249 0.019  0.015  0.009  257 HIS A NE2 
2008 N N   . CYS A 258 ? 0.278 0.198 0.226 0.013  -0.002 -0.007 258 CYS A N   
2009 C CA  . CYS A 258 ? 0.298 0.210 0.246 0.015  -0.007 -0.018 258 CYS A CA  
2010 C C   . CYS A 258 ? 0.327 0.218 0.281 0.015  -0.007 -0.016 258 CYS A C   
2011 O O   . CYS A 258 ? 0.333 0.218 0.286 0.022  -0.009 -0.024 258 CYS A O   
2012 C CB  . CYS A 258 ? 0.316 0.232 0.272 0.008  -0.011 -0.028 258 CYS A CB  
2013 S SG  . CYS A 258 ? 0.322 0.269 0.269 0.015  -0.012 -0.032 258 CYS A SG  
2014 N N   . ALA A 259 ? 0.308 0.192 0.266 0.009  -0.005 -0.004 259 ALA A N   
2015 C CA  . ALA A 259 ? 0.327 0.194 0.289 0.012  -0.004 0.004  259 ALA A CA  
2016 C C   . ALA A 259 ? 0.326 0.198 0.280 0.024  -0.004 0.004  259 ALA A C   
2017 O O   . ALA A 259 ? 0.346 0.204 0.302 0.030  -0.005 0.002  259 ALA A O   
2018 C CB  . ALA A 259 ? 0.359 0.226 0.324 0.009  0.001  0.020  259 ALA A CB  
2019 N N   . ASN A 260 ? 0.305 0.194 0.254 0.025  -0.003 0.005  260 ASN A N   
2020 C CA  . ASN A 260 ? 0.291 0.189 0.241 0.034  -0.004 0.004  260 ASN A CA  
2021 C C   . ASN A 260 ? 0.301 0.200 0.253 0.039  -0.003 -0.004 260 ASN A C   
2022 O O   . ASN A 260 ? 0.311 0.208 0.264 0.048  -0.003 -0.005 260 ASN A O   
2023 C CB  . ASN A 260 ? 0.282 0.198 0.237 0.033  -0.004 0.002  260 ASN A CB  
2024 C CG  . ASN A 260 ? 0.286 0.212 0.238 0.035  -0.007 0.006  260 ASN A CG  
2025 O OD1 . ASN A 260 ? 0.316 0.236 0.260 0.039  -0.006 0.015  260 ASN A OD1 
2026 N ND2 . ASN A 260 ? 0.282 0.224 0.242 0.036  -0.009 -0.002 260 ASN A ND2 
2027 N N   . ALA A 261 ? 0.297 0.200 0.246 0.037  -0.001 -0.008 261 ALA A N   
2028 C CA  . ALA A 261 ? 0.297 0.209 0.243 0.046  0.001  -0.014 261 ALA A CA  
2029 C C   . ALA A 261 ? 0.329 0.227 0.274 0.052  -0.003 -0.025 261 ALA A C   
2030 O O   . ALA A 261 ? 0.324 0.226 0.267 0.063  -0.002 -0.029 261 ALA A O   
2031 C CB  . ALA A 261 ? 0.299 0.226 0.241 0.047  0.004  -0.016 261 ALA A CB  
2032 N N   . GLU A 262 ? 0.340 0.219 0.288 0.045  -0.008 -0.029 262 GLU A N   
2033 C CA  . GLU A 262 ? 0.371 0.231 0.327 0.050  -0.013 -0.041 262 GLU A CA  
2034 C C   . GLU A 262 ? 0.368 0.217 0.326 0.058  -0.011 -0.033 262 GLU A C   
2035 O O   . GLU A 262 ? 0.374 0.218 0.334 0.070  -0.013 -0.044 262 GLU A O   
2036 C CB  . GLU A 262 ? 0.406 0.247 0.377 0.038  -0.016 -0.044 262 GLU A CB  
2037 C CG  . GLU A 262 ? 0.451 0.308 0.422 0.034  -0.020 -0.059 262 GLU A CG  
2038 C CD  . GLU A 262 ? 0.566 0.410 0.559 0.020  -0.023 -0.063 262 GLU A CD  
2039 O OE1 . GLU A 262 ? 0.629 0.455 0.636 0.012  -0.019 -0.046 262 GLU A OE1 
2040 O OE2 . GLU A 262 ? 0.613 0.471 0.612 0.018  -0.030 -0.082 262 GLU A OE2 
2041 N N   A ARG A 263 ? 0.352 0.203 0.309 0.056  -0.009 -0.017 263 ARG A N   
2042 N N   B ARG A 263 ? 0.366 0.218 0.323 0.056  -0.009 -0.017 263 ARG A N   
2043 C CA  A ARG A 263 ? 0.355 0.203 0.312 0.066  -0.008 -0.008 263 ARG A CA  
2044 C CA  B ARG A 263 ? 0.379 0.228 0.337 0.066  -0.008 -0.008 263 ARG A CA  
2045 C C   A ARG A 263 ? 0.345 0.214 0.300 0.075  -0.007 -0.015 263 ARG A C   
2046 C C   B ARG A 263 ? 0.357 0.227 0.312 0.075  -0.007 -0.014 263 ARG A C   
2047 O O   A ARG A 263 ? 0.360 0.227 0.318 0.088  -0.008 -0.017 263 ARG A O   
2048 O O   B ARG A 263 ? 0.367 0.235 0.326 0.088  -0.008 -0.016 263 ARG A O   
2049 C CB  A ARG A 263 ? 0.355 0.211 0.309 0.063  -0.007 0.007  263 ARG A CB  
2050 C CB  B ARG A 263 ? 0.404 0.255 0.359 0.063  -0.007 0.008  263 ARG A CB  
2051 C CG  A ARG A 263 ? 0.376 0.238 0.328 0.077  -0.009 0.015  263 ARG A CG  
2052 C CG  B ARG A 263 ? 0.485 0.316 0.445 0.070  -0.006 0.022  263 ARG A CG  
2053 C CD  A ARG A 263 ? 0.426 0.261 0.384 0.086  -0.008 0.024  263 ARG A CD  
2054 C CD  B ARG A 263 ? 0.504 0.311 0.476 0.061  -0.002 0.031  263 ARG A CD  
2055 N NE  A ARG A 263 ? 0.449 0.295 0.403 0.102  -0.009 0.030  263 ARG A NE  
2056 N NE  B ARG A 263 ? 0.511 0.299 0.499 0.054  -0.005 0.014  263 ARG A NE  
2057 C CZ  A ARG A 263 ? 0.446 0.299 0.404 0.112  -0.012 0.019  263 ARG A CZ  
2058 C CZ  B ARG A 263 ? 0.508 0.296 0.503 0.040  -0.006 0.005  263 ARG A CZ  
2059 N NH1 A ARG A 263 ? 0.390 0.239 0.351 0.108  -0.011 0.003  263 ARG A NH1 
2060 N NH1 B ARG A 263 ? 0.453 0.259 0.440 0.031  -0.003 0.013  263 ARG A NH1 
2061 N NH2 A ARG A 263 ? 0.455 0.319 0.411 0.129  -0.014 0.026  263 ARG A NH2 
2062 N NH2 B ARG A 263 ? 0.532 0.306 0.545 0.037  -0.010 -0.015 263 ARG A NH2 
2063 N N   . VAL A 264 ? 0.330 0.221 0.285 0.071  -0.004 -0.015 264 VAL A N   
2064 C CA  . VAL A 264 ? 0.319 0.233 0.281 0.078  0.000  -0.017 264 VAL A CA  
2065 C C   . VAL A 264 ? 0.324 0.239 0.280 0.090  0.002  -0.027 264 VAL A C   
2066 O O   . VAL A 264 ? 0.349 0.275 0.310 0.101  0.004  -0.028 264 VAL A O   
2067 C CB  . VAL A 264 ? 0.311 0.243 0.281 0.070  0.006  -0.011 264 VAL A CB  
2068 C CG1 . VAL A 264 ? 0.327 0.281 0.308 0.077  0.015  -0.008 264 VAL A CG1 
2069 C CG2 . VAL A 264 ? 0.314 0.250 0.295 0.063  0.003  -0.008 264 VAL A CG2 
2070 N N   . VAL A 265 ? 0.333 0.277 0.289 0.034  -0.015 -0.041 265 VAL A N   
2071 C CA  . VAL A 265 ? 0.331 0.245 0.292 0.038  -0.010 -0.036 265 VAL A CA  
2072 C C   . VAL A 265 ? 0.358 0.270 0.326 0.044  -0.011 -0.018 265 VAL A C   
2073 O O   . VAL A 265 ? 0.372 0.274 0.353 0.052  -0.009 -0.017 265 VAL A O   
2074 C CB  . VAL A 265 ? 0.341 0.238 0.297 0.034  -0.006 -0.039 265 VAL A CB  
2075 C CG1 . VAL A 265 ? 0.356 0.229 0.315 0.036  -0.001 -0.037 265 VAL A CG1 
2076 C CG2 . VAL A 265 ? 0.343 0.240 0.301 0.030  -0.006 -0.052 265 VAL A CG2 
2077 N N   . GLU A 266 ? 0.362 0.285 0.327 0.042  -0.013 -0.002 266 GLU A N   
2078 C CA  . GLU A 266 ? 0.396 0.317 0.377 0.048  -0.016 0.022  266 GLU A CA  
2079 C C   . GLU A 266 ? 0.400 0.342 0.392 0.055  -0.021 0.026  266 GLU A C   
2080 O O   . GLU A 266 ? 0.408 0.338 0.422 0.065  -0.020 0.038  266 GLU A O   
2081 C CB  . GLU A 266 ? 0.439 0.381 0.416 0.040  -0.020 0.045  266 GLU A CB  
2082 C CG  . GLU A 266 ? 0.490 0.411 0.464 0.033  -0.016 0.046  266 GLU A CG  
2083 C CD  . GLU A 266 ? 0.562 0.516 0.528 0.022  -0.019 0.066  266 GLU A CD  
2084 O OE1 . GLU A 266 ? 0.612 0.552 0.576 0.014  -0.016 0.067  266 GLU A OE1 
2085 O OE2 . GLU A 266 ? 0.633 0.632 0.594 0.019  -0.025 0.082  266 GLU A OE2 
2086 N N   . ALA A 267 ? 0.367 0.341 0.347 0.051  -0.025 0.018  267 ALA A N   
2087 C CA  . ALA A 267 ? 0.373 0.372 0.363 0.055  -0.031 0.021  267 ALA A CA  
2088 C C   . ALA A 267 ? 0.366 0.344 0.369 0.061  -0.026 0.009  267 ALA A C   
2089 O O   . ALA A 267 ? 0.381 0.369 0.400 0.069  -0.028 0.018  267 ALA A O   
2090 C CB  . ALA A 267 ? 0.359 0.399 0.336 0.046  -0.037 0.009  267 ALA A CB  
2091 N N   . LEU A 268 ? 0.365 0.321 0.361 0.058  -0.020 -0.009 268 LEU A N   
2092 C CA  . LEU A 268 ? 0.372 0.321 0.378 0.061  -0.016 -0.019 268 LEU A CA  
2093 C C   . LEU A 268 ? 0.396 0.325 0.413 0.070  -0.009 -0.017 268 LEU A C   
2094 O O   . LEU A 268 ? 0.399 0.336 0.429 0.077  -0.006 -0.018 268 LEU A O   
2095 C CB  . LEU A 268 ? 0.378 0.317 0.376 0.052  -0.015 -0.034 268 LEU A CB  
2096 C CG  . LEU A 268 ? 0.378 0.334 0.377 0.044  -0.022 -0.043 268 LEU A CG  
2097 C CD1 . LEU A 268 ? 0.377 0.318 0.377 0.037  -0.021 -0.054 268 LEU A CD1 
2098 C CD2 . LEU A 268 ? 0.396 0.372 0.410 0.042  -0.027 -0.043 268 LEU A CD2 
2099 N N   . VAL A 269 ? 0.401 0.306 0.414 0.070  -0.005 -0.016 269 VAL A N   
2100 C CA  . VAL A 269 ? 0.427 0.309 0.454 0.078  0.003  -0.022 269 VAL A CA  
2101 C C   . VAL A 269 ? 0.469 0.356 0.525 0.092  0.002  -0.010 269 VAL A C   
2102 O O   . VAL A 269 ? 0.493 0.387 0.555 0.094  -0.005 0.012  269 VAL A O   
2103 C CB  . VAL A 269 ? 0.442 0.299 0.464 0.072  0.005  -0.024 269 VAL A CB  
2104 C CG1 . VAL A 269 ? 0.471 0.303 0.514 0.080  0.011  -0.033 269 VAL A CG1 
2105 C CG2 . VAL A 269 ? 0.423 0.280 0.423 0.061  0.007  -0.038 269 VAL A CG2 
2106 N N   . GLY A 270 ? 0.466 0.356 0.539 0.102  0.009  -0.021 270 GLY A N   
2107 C CA  . GLY A 270 ? 0.498 0.395 0.605 0.119  0.008  -0.010 270 GLY A CA  
2108 C C   . GLY A 270 ? 0.502 0.436 0.612 0.120  0.000  0.006  270 GLY A C   
2109 O O   . GLY A 270 ? 0.487 0.431 0.627 0.134  0.001  0.014  270 GLY A O   
2110 N N   . HIS A 271 ? 0.441 0.395 0.525 0.106  -0.006 0.007  271 HIS A N   
2111 C CA  . HIS A 271 ? 0.410 0.402 0.500 0.105  -0.014 0.016  271 HIS A CA  
2112 C C   . HIS A 271 ? 0.403 0.408 0.511 0.114  -0.006 0.006  271 HIS A C   
2113 O O   . HIS A 271 ? 0.392 0.389 0.491 0.110  0.003  -0.012 271 HIS A O   
2114 C CB  . HIS A 271 ? 0.382 0.389 0.447 0.088  -0.020 0.009  271 HIS A CB  
2115 C CG  . HIS A 271 ? 0.372 0.417 0.444 0.085  -0.030 0.016  271 HIS A CG  
2116 N ND1 . HIS A 271 ? 0.369 0.435 0.457 0.086  -0.029 0.014  271 HIS A ND1 
2117 C CD2 . HIS A 271 ? 0.380 0.452 0.446 0.079  -0.040 0.026  271 HIS A CD2 
2118 C CE1 . HIS A 271 ? 0.369 0.470 0.461 0.080  -0.039 0.022  271 HIS A CE1 
2119 N NE2 . HIS A 271 ? 0.390 0.497 0.469 0.076  -0.046 0.028  271 HIS A NE2 
2120 N N   . PRO A 272 ? 0.396 0.427 0.530 0.126  -0.008 0.017  272 PRO A N   
2121 C CA  . PRO A 272 ? 0.400 0.450 0.555 0.135  0.002  0.007  272 PRO A CA  
2122 C C   . PRO A 272 ? 0.386 0.460 0.526 0.121  0.003  -0.002 272 PRO A C   
2123 O O   . PRO A 272 ? 0.389 0.480 0.539 0.125  0.013  -0.014 272 PRO A O   
2124 C CB  . PRO A 272 ? 0.416 0.495 0.603 0.149  -0.004 0.026  272 PRO A CB  
2125 C CG  . PRO A 272 ? 0.414 0.498 0.594 0.143  -0.018 0.050  272 PRO A CG  
2126 C CD  . PRO A 272 ? 0.413 0.462 0.561 0.130  -0.019 0.043  272 PRO A CD  
2127 N N   . GLU A 273 ? 0.354 0.432 0.475 0.103  -0.007 0.001  273 GLU A N   
2128 C CA  . GLU A 273 ? 0.351 0.448 0.468 0.088  -0.007 -0.003 273 GLU A CA  
2129 C C   . GLU A 273 ? 0.330 0.403 0.427 0.078  -0.003 -0.013 273 GLU A C   
2130 O O   . GLU A 273 ? 0.327 0.415 0.426 0.066  -0.002 -0.013 273 GLU A O   
2131 C CB  . GLU A 273 ? 0.370 0.484 0.488 0.074  -0.021 0.004  273 GLU A CB  
2132 C CG  . GLU A 273 ? 0.394 0.542 0.531 0.081  -0.028 0.017  273 GLU A CG  
2133 C CD  . GLU A 273 ? 0.470 0.652 0.632 0.089  -0.022 0.021  273 GLU A CD  
2134 O OE1 . GLU A 273 ? 0.538 0.734 0.703 0.078  -0.020 0.018  273 GLU A OE1 
2135 O OE2 . GLU A 273 ? 0.496 0.691 0.677 0.107  -0.019 0.029  273 GLU A OE2 
2136 N N   . VAL A 274 ? 0.332 0.372 0.415 0.082  0.001  -0.020 274 VAL A N   
2137 C CA  . VAL A 274 ? 0.344 0.363 0.409 0.072  0.003  -0.028 274 VAL A CA  
2138 C C   . VAL A 274 ? 0.358 0.378 0.421 0.078  0.016  -0.040 274 VAL A C   
2139 O O   . VAL A 274 ? 0.386 0.391 0.457 0.091  0.021  -0.047 274 VAL A O   
2140 C CB  . VAL A 274 ? 0.343 0.333 0.392 0.069  -0.002 -0.028 274 VAL A CB  
2141 C CG1 . VAL A 274 ? 0.362 0.334 0.396 0.061  0.001  -0.036 274 VAL A CG1 
2142 C CG2 . VAL A 274 ? 0.345 0.346 0.396 0.061  -0.014 -0.023 274 VAL A CG2 
2143 N N   . ALA A 275 ? 0.348 0.387 0.407 0.068  0.020  -0.042 275 ALA A N   
2144 C CA  . ALA A 275 ? 0.367 0.422 0.422 0.070  0.032  -0.057 275 ALA A CA  
2145 C C   . ALA A 275 ? 0.368 0.394 0.405 0.066  0.034  -0.067 275 ALA A C   
2146 O O   . ALA A 275 ? 0.389 0.415 0.424 0.071  0.043  -0.086 275 ALA A O   
2147 C CB  . ALA A 275 ? 0.375 0.476 0.431 0.059  0.035  -0.050 275 ALA A CB  
2148 N N   . GLU A 276 ? 0.341 0.349 0.366 0.054  0.025  -0.056 276 GLU A N   
2149 C CA  . GLU A 276 ? 0.353 0.342 0.361 0.047  0.026  -0.062 276 GLU A CA  
2150 C C   . GLU A 276 ? 0.332 0.295 0.335 0.042  0.015  -0.052 276 GLU A C   
2151 O O   . GLU A 276 ? 0.332 0.303 0.345 0.037  0.008  -0.041 276 GLU A O   
2152 C CB  . GLU A 276 ? 0.381 0.406 0.382 0.035  0.029  -0.061 276 GLU A CB  
2153 C CG  . GLU A 276 ? 0.409 0.425 0.394 0.029  0.032  -0.071 276 GLU A CG  
2154 C CD  . GLU A 276 ? 0.437 0.496 0.413 0.015  0.033  -0.065 276 GLU A CD  
2155 O OE1 . GLU A 276 ? 0.441 0.535 0.426 0.008  0.031  -0.048 276 GLU A OE1 
2156 O OE2 . GLU A 276 ? 0.484 0.546 0.446 0.009  0.036  -0.078 276 GLU A OE2 
2157 N N   . VAL A 277 ? 0.348 0.285 0.341 0.043  0.016  -0.058 277 VAL A N   
2158 C CA  . VAL A 277 ? 0.337 0.257 0.325 0.038  0.008  -0.052 277 VAL A CA  
2159 C C   . VAL A 277 ? 0.333 0.251 0.311 0.029  0.009  -0.054 277 VAL A C   
2160 O O   . VAL A 277 ? 0.346 0.260 0.316 0.028  0.015  -0.064 277 VAL A O   
2161 C CB  . VAL A 277 ? 0.350 0.251 0.336 0.044  0.006  -0.052 277 VAL A CB  
2162 C CG1 . VAL A 277 ? 0.357 0.252 0.338 0.039  0.000  -0.050 277 VAL A CG1 
2163 C CG2 . VAL A 277 ? 0.361 0.272 0.359 0.053  0.005  -0.047 277 VAL A CG2 
2164 N N   . LEU A 278 ? 0.322 0.243 0.306 0.022  0.002  -0.046 278 LEU A N   
2165 C CA  . LEU A 278 ? 0.314 0.239 0.295 0.014  0.001  -0.042 278 LEU A CA  
2166 C C   . LEU A 278 ? 0.319 0.225 0.300 0.015  -0.003 -0.045 278 LEU A C   
2167 O O   . LEU A 278 ? 0.315 0.218 0.309 0.017  -0.008 -0.044 278 LEU A O   
2168 C CB  . LEU A 278 ? 0.295 0.242 0.293 0.006  -0.004 -0.025 278 LEU A CB  
2169 C CG  . LEU A 278 ? 0.300 0.277 0.299 0.003  -0.001 -0.020 278 LEU A CG  
2170 C CD1 . LEU A 278 ? 0.301 0.302 0.321 -0.007 -0.007 0.004  278 LEU A CD1 
2171 C CD2 . LEU A 278 ? 0.315 0.309 0.293 0.002  0.009  -0.033 278 LEU A CD2 
2172 N N   . TYR A 279 ? 0.321 0.220 0.289 0.014  0.001  -0.050 279 TYR A N   
2173 C CA  . TYR A 279 ? 0.331 0.220 0.297 0.014  -0.001 -0.052 279 TYR A CA  
2174 C C   . TYR A 279 ? 0.334 0.223 0.289 0.007  0.002  -0.053 279 TYR A C   
2175 O O   . TYR A 279 ? 0.360 0.242 0.305 0.005  0.006  -0.060 279 TYR A O   
2176 C CB  . TYR A 279 ? 0.330 0.211 0.292 0.020  -0.001 -0.055 279 TYR A CB  
2177 C CG  . TYR A 279 ? 0.324 0.208 0.284 0.019  -0.002 -0.058 279 TYR A CG  
2178 C CD1 . TYR A 279 ? 0.309 0.202 0.283 0.020  -0.006 -0.063 279 TYR A CD1 
2179 C CD2 . TYR A 279 ? 0.331 0.213 0.281 0.016  0.001  -0.055 279 TYR A CD2 
2180 C CE1 . TYR A 279 ? 0.315 0.219 0.291 0.021  -0.006 -0.070 279 TYR A CE1 
2181 C CE2 . TYR A 279 ? 0.331 0.226 0.279 0.014  0.000  -0.057 279 TYR A CE2 
2182 C CZ  . TYR A 279 ? 0.325 0.234 0.285 0.018  -0.002 -0.066 279 TYR A CZ  
2183 O OH  . TYR A 279 ? 0.318 0.248 0.279 0.017  -0.001 -0.073 279 TYR A OH  
2184 N N   . PRO A 280 ? 0.328 0.232 0.287 0.013  -0.001 -0.019 280 PRO A N   
2185 C CA  . PRO A 280 ? 0.341 0.235 0.292 0.015  0.003  -0.023 280 PRO A CA  
2186 C C   . PRO A 280 ? 0.356 0.233 0.304 0.016  -0.001 -0.023 280 PRO A C   
2187 O O   . PRO A 280 ? 0.365 0.233 0.313 0.018  -0.001 -0.028 280 PRO A O   
2188 C CB  . PRO A 280 ? 0.341 0.233 0.287 0.007  0.005  -0.022 280 PRO A CB  
2189 C CG  . PRO A 280 ? 0.338 0.240 0.292 0.004  0.004  -0.018 280 PRO A CG  
2190 C CD  . PRO A 280 ? 0.334 0.239 0.293 0.006  -0.001 -0.017 280 PRO A CD  
2191 N N   . GLY A 281 ? 0.362 0.233 0.307 0.016  -0.005 -0.016 281 GLY A N   
2192 C CA  . GLY A 281 ? 0.375 0.227 0.316 0.017  -0.008 -0.010 281 GLY A CA  
2193 C C   . GLY A 281 ? 0.387 0.230 0.337 0.028  -0.014 -0.012 281 GLY A C   
2194 O O   . GLY A 281 ? 0.407 0.229 0.359 0.028  -0.018 -0.007 281 GLY A O   
2195 N N   . LEU A 282 ? 0.375 0.235 0.334 0.037  -0.014 -0.018 282 LEU A N   
2196 C CA  . LEU A 282 ? 0.392 0.246 0.363 0.051  -0.019 -0.023 282 LEU A CA  
2197 C C   . LEU A 282 ? 0.406 0.247 0.377 0.055  -0.017 -0.036 282 LEU A C   
2198 O O   . LEU A 282 ? 0.387 0.240 0.354 0.052  -0.011 -0.045 282 LEU A O   
2199 C CB  . LEU A 282 ? 0.392 0.277 0.376 0.060  -0.017 -0.026 282 LEU A CB  
2200 C CG  . LEU A 282 ? 0.389 0.288 0.380 0.059  -0.024 -0.017 282 LEU A CG  
2201 C CD1 . LEU A 282 ? 0.365 0.301 0.375 0.061  -0.020 -0.019 282 LEU A CD1 
2202 C CD2 . LEU A 282 ? 0.406 0.290 0.399 0.071  -0.035 -0.010 282 LEU A CD2 
2203 N N   . PRO A 283 ? 0.437 0.250 0.414 0.061  -0.025 -0.039 283 PRO A N   
2204 C CA  . PRO A 283 ? 0.469 0.265 0.447 0.063  -0.027 -0.055 283 PRO A CA  
2205 C C   . PRO A 283 ? 0.472 0.290 0.448 0.078  -0.022 -0.075 283 PRO A C   
2206 O O   . PRO A 283 ? 0.480 0.297 0.448 0.076  -0.022 -0.089 283 PRO A O   
2207 C CB  . PRO A 283 ? 0.520 0.278 0.509 0.070  -0.038 -0.054 283 PRO A CB  
2208 C CG  . PRO A 283 ? 0.538 0.292 0.526 0.068  -0.041 -0.030 283 PRO A CG  
2209 C CD  . PRO A 283 ? 0.476 0.268 0.456 0.064  -0.033 -0.024 283 PRO A CD  
2210 N N   . ASP A 284 ? 0.457 0.301 0.440 0.091  -0.017 -0.075 284 ASP A N   
2211 C CA  . ASP A 284 ? 0.475 0.348 0.456 0.106  -0.009 -0.091 284 ASP A CA  
2212 C C   . ASP A 284 ? 0.425 0.335 0.400 0.096  0.003  -0.082 284 ASP A C   
2213 O O   . ASP A 284 ? 0.422 0.364 0.394 0.107  0.013  -0.088 284 ASP A O   
2214 C CB  . ASP A 284 ? 0.515 0.404 0.512 0.129  -0.009 -0.097 284 ASP A CB  
2215 C CG  . ASP A 284 ? 0.638 0.487 0.644 0.143  -0.022 -0.108 284 ASP A CG  
2216 O OD1 . ASP A 284 ? 0.671 0.484 0.669 0.139  -0.030 -0.119 284 ASP A OD1 
2217 O OD2 . ASP A 284 ? 0.732 0.588 0.755 0.160  -0.025 -0.106 284 ASP A OD2 
2218 N N   . HIS A 285 ? 0.391 0.298 0.363 0.078  0.003  -0.066 285 HIS A N   
2219 C CA  . HIS A 285 ? 0.376 0.311 0.345 0.068  0.012  -0.057 285 HIS A CA  
2220 C C   . HIS A 285 ? 0.381 0.318 0.333 0.069  0.015  -0.066 285 HIS A C   
2221 O O   . HIS A 285 ? 0.401 0.312 0.344 0.066  0.008  -0.075 285 HIS A O   
2222 C CB  . HIS A 285 ? 0.359 0.283 0.327 0.051  0.008  -0.043 285 HIS A CB  
2223 C CG  . HIS A 285 ? 0.346 0.290 0.316 0.041  0.015  -0.033 285 HIS A CG  
2224 N ND1 . HIS A 285 ? 0.341 0.309 0.329 0.039  0.018  -0.024 285 HIS A ND1 
2225 C CD2 . HIS A 285 ? 0.339 0.281 0.299 0.033  0.017  -0.030 285 HIS A CD2 
2226 C CE1 . HIS A 285 ? 0.327 0.303 0.315 0.029  0.022  -0.015 285 HIS A CE1 
2227 N NE2 . HIS A 285 ? 0.333 0.292 0.303 0.026  0.021  -0.018 285 HIS A NE2 
2228 N N   . PRO A 286 ? 0.395 0.364 0.341 0.072  0.026  -0.063 286 PRO A N   
2229 C CA  . PRO A 286 ? 0.440 0.415 0.366 0.075  0.027  -0.071 286 PRO A CA  
2230 C C   . PRO A 286 ? 0.426 0.381 0.346 0.059  0.020  -0.064 286 PRO A C   
2231 O O   . PRO A 286 ? 0.414 0.369 0.342 0.047  0.022  -0.048 286 PRO A O   
2232 C CB  . PRO A 286 ? 0.436 0.451 0.358 0.077  0.041  -0.057 286 PRO A CB  
2233 C CG  . PRO A 286 ? 0.414 0.436 0.362 0.066  0.044  -0.039 286 PRO A CG  
2234 C CD  . PRO A 286 ? 0.402 0.406 0.364 0.072  0.036  -0.049 286 PRO A CD  
2235 N N   . GLY A 287 ? 0.445 0.383 0.356 0.059  0.011  -0.078 287 GLY A N   
2236 C CA  . GLY A 287 ? 0.426 0.351 0.337 0.046  0.006  -0.073 287 GLY A CA  
2237 C C   . GLY A 287 ? 0.398 0.298 0.323 0.035  0.000  -0.069 287 GLY A C   
2238 O O   . GLY A 287 ? 0.388 0.284 0.316 0.025  -0.002 -0.063 287 GLY A O   
2239 N N   . HIS A 288 ? 0.390 0.276 0.324 0.038  -0.001 -0.070 288 HIS A N   
2240 C CA  . HIS A 288 ? 0.388 0.250 0.332 0.029  -0.006 -0.063 288 HIS A CA  
2241 C C   . HIS A 288 ? 0.397 0.246 0.346 0.019  -0.012 -0.067 288 HIS A C   
2242 O O   . HIS A 288 ? 0.408 0.256 0.362 0.008  -0.010 -0.055 288 HIS A O   
2243 C CB  . HIS A 288 ? 0.413 0.260 0.365 0.037  -0.010 -0.065 288 HIS A CB  
2244 C CG  . HIS A 288 ? 0.412 0.234 0.370 0.028  -0.014 -0.054 288 HIS A CG  
2245 N ND1 . HIS A 288 ? 0.396 0.224 0.352 0.021  -0.010 -0.037 288 HIS A ND1 
2246 C CD2 . HIS A 288 ? 0.438 0.232 0.406 0.024  -0.022 -0.055 288 HIS A CD2 
2247 C CE1 . HIS A 288 ? 0.427 0.235 0.387 0.014  -0.014 -0.027 288 HIS A CE1 
2248 N NE2 . HIS A 288 ? 0.445 0.230 0.415 0.014  -0.021 -0.036 288 HIS A NE2 
2249 N N   . LYS A 289 ? 0.405 0.247 0.353 0.022  -0.020 -0.084 289 LYS A N   
2250 C CA  . LYS A 289 ? 0.422 0.252 0.383 0.010  -0.030 -0.089 289 LYS A CA  
2251 C C   . LYS A 289 ? 0.415 0.267 0.375 0.003  -0.027 -0.082 289 LYS A C   
2252 O O   . LYS A 289 ? 0.418 0.269 0.394 -0.010 -0.028 -0.075 289 LYS A O   
2253 C CB  . LYS A 289 ? 0.450 0.267 0.411 0.016  -0.043 -0.113 289 LYS A CB  
2254 N N   . VAL A 290 ? 0.388 0.262 0.331 0.011  -0.022 -0.082 290 VAL A N   
2255 C CA  . VAL A 290 ? 0.369 0.261 0.312 0.007  -0.020 -0.074 290 VAL A CA  
2256 C C   . VAL A 290 ? 0.358 0.249 0.310 -0.000 -0.012 -0.058 290 VAL A C   
2257 O O   . VAL A 290 ? 0.374 0.273 0.338 -0.007 -0.011 -0.053 290 VAL A O   
2258 C CB  . VAL A 290 ? 0.373 0.286 0.297 0.017  -0.018 -0.074 290 VAL A CB  
2259 C CG1 . VAL A 290 ? 0.356 0.282 0.282 0.015  -0.016 -0.062 290 VAL A CG1 
2260 C CG2 . VAL A 290 ? 0.409 0.328 0.319 0.026  -0.027 -0.092 290 VAL A CG2 
2261 N N   . ALA A 291 ? 0.359 0.244 0.305 0.002  -0.005 -0.051 291 ALA A N   
2262 C CA  . ALA A 291 ? 0.350 0.235 0.300 -0.002 0.001  -0.039 291 ALA A CA  
2263 C C   . ALA A 291 ? 0.365 0.242 0.325 -0.011 0.001  -0.035 291 ALA A C   
2264 O O   . ALA A 291 ? 0.358 0.244 0.321 -0.015 0.007  -0.029 291 ALA A O   
2265 C CB  . ALA A 291 ? 0.353 0.234 0.297 0.002  0.004  -0.035 291 ALA A CB  
2266 N N   . VAL A 292 ? 0.371 0.232 0.338 -0.014 -0.004 -0.038 292 VAL A N   
2267 C CA  . VAL A 292 ? 0.390 0.244 0.372 -0.026 -0.003 -0.028 292 VAL A CA  
2268 C C   . VAL A 292 ? 0.390 0.260 0.387 -0.034 -0.003 -0.030 292 VAL A C   
2269 O O   . VAL A 292 ? 0.393 0.273 0.401 -0.042 0.004  -0.018 292 VAL A O   
2270 C CB  . VAL A 292 ? 0.404 0.231 0.394 -0.028 -0.012 -0.031 292 VAL A CB  
2271 C CG1 . VAL A 292 ? 0.426 0.244 0.436 -0.043 -0.012 -0.019 292 VAL A CG1 
2272 C CG2 . VAL A 292 ? 0.408 0.220 0.386 -0.017 -0.012 -0.028 292 VAL A CG2 
2273 N N   A ASP A 293 ? 0.392 0.270 0.391 -0.031 -0.011 -0.043 293 ASP A N   
2274 N N   B ASP A 293 ? 0.389 0.267 0.388 -0.031 -0.012 -0.044 293 ASP A N   
2275 C CA  A ASP A 293 ? 0.398 0.295 0.418 -0.039 -0.015 -0.044 293 ASP A CA  
2276 C CA  B ASP A 293 ? 0.396 0.292 0.413 -0.037 -0.016 -0.047 293 ASP A CA  
2277 C C   A ASP A 293 ? 0.372 0.292 0.389 -0.034 -0.006 -0.039 293 ASP A C   
2278 C C   B ASP A 293 ? 0.370 0.290 0.387 -0.034 -0.007 -0.039 293 ASP A C   
2279 O O   A ASP A 293 ? 0.368 0.309 0.406 -0.040 -0.004 -0.035 293 ASP A O   
2280 O O   B ASP A 293 ? 0.370 0.309 0.408 -0.041 -0.004 -0.035 293 ASP A O   
2281 C CB  A ASP A 293 ? 0.423 0.320 0.447 -0.038 -0.030 -0.062 293 ASP A CB  
2282 C CB  B ASP A 293 ? 0.407 0.308 0.417 -0.030 -0.029 -0.065 293 ASP A CB  
2283 C CG  A ASP A 293 ? 0.468 0.341 0.505 -0.046 -0.042 -0.072 293 ASP A CG  
2284 C CG  B ASP A 293 ? 0.435 0.352 0.467 -0.038 -0.041 -0.072 293 ASP A CG  
2285 O OD1 A ASP A 293 ? 0.486 0.340 0.537 -0.056 -0.038 -0.060 293 ASP A OD1 
2286 O OD1 B ASP A 293 ? 0.452 0.369 0.513 -0.052 -0.042 -0.067 293 ASP A OD1 
2287 O OD2 A ASP A 293 ? 0.514 0.386 0.548 -0.041 -0.055 -0.090 293 ASP A OD2 
2288 O OD2 B ASP A 293 ? 0.463 0.393 0.485 -0.029 -0.051 -0.083 293 ASP A OD2 
2289 N N   . GLN A 294 ? 0.340 0.260 0.337 -0.023 -0.002 -0.038 294 GLN A N   
2290 C CA  . GLN A 294 ? 0.330 0.266 0.327 -0.016 0.002  -0.035 294 GLN A CA  
2291 C C   . GLN A 294 ? 0.312 0.245 0.299 -0.012 0.012  -0.029 294 GLN A C   
2292 O O   . GLN A 294 ? 0.309 0.252 0.298 -0.006 0.015  -0.029 294 GLN A O   
2293 C CB  . GLN A 294 ? 0.350 0.289 0.336 -0.007 -0.005 -0.040 294 GLN A CB  
2294 C CG  . GLN A 294 ? 0.348 0.276 0.315 -0.001 -0.003 -0.037 294 GLN A CG  
2295 C CD  . GLN A 294 ? 0.325 0.259 0.281 0.007  -0.008 -0.036 294 GLN A CD  
2296 O OE1 . GLN A 294 ? 0.331 0.277 0.289 0.010  -0.016 -0.039 294 GLN A OE1 
2297 N NE2 . GLN A 294 ? 0.322 0.249 0.266 0.010  -0.004 -0.029 294 GLN A NE2 
2298 N N   . MET A 295 ? 0.314 0.232 0.290 -0.015 0.016  -0.025 295 MET A N   
2299 C CA  . MET A 295 ? 0.317 0.233 0.280 -0.011 0.022  -0.022 295 MET A CA  
2300 C C   . MET A 295 ? 0.335 0.254 0.298 -0.017 0.029  -0.013 295 MET A C   
2301 O O   . MET A 295 ? 0.355 0.264 0.324 -0.024 0.027  -0.007 295 MET A O   
2302 C CB  . MET A 295 ? 0.310 0.211 0.259 -0.007 0.018  -0.023 295 MET A CB  
2303 C CG  . MET A 295 ? 0.318 0.218 0.267 -0.003 0.013  -0.026 295 MET A CG  
2304 S SD  . MET A 295 ? 0.341 0.232 0.283 -0.001 0.011  -0.025 295 MET A SD  
2305 C CE  . MET A 295 ? 0.342 0.229 0.279 0.001  0.010  -0.027 295 MET A CE  
2306 N N   . ARG A 296 ? 0.326 0.259 0.282 -0.013 0.038  -0.010 296 ARG A N   
2307 C CA  . ARG A 296 ? 0.342 0.283 0.292 -0.017 0.048  0.002  296 ARG A CA  
2308 C C   . ARG A 296 ? 0.347 0.268 0.278 -0.017 0.043  0.008  296 ARG A C   
2309 O O   . ARG A 296 ? 0.366 0.284 0.294 -0.023 0.046  0.023  296 ARG A O   
2310 C CB  . ARG A 296 ? 0.372 0.337 0.314 -0.008 0.059  -0.001 296 ARG A CB  
2311 C CG  . ARG A 296 ? 0.438 0.420 0.365 -0.008 0.072  0.012  296 ARG A CG  
2312 C CD  . ARG A 296 ? 0.475 0.487 0.394 0.005  0.084  0.003  296 ARG A CD  
2313 N NE  . ARG A 296 ? 0.537 0.568 0.436 0.005  0.098  0.018  296 ARG A NE  
2314 C CZ  . ARG A 296 ? 0.564 0.632 0.458 0.013  0.115  0.020  296 ARG A CZ  
2315 N NH1 . ARG A 296 ? 0.586 0.673 0.457 0.013  0.128  0.038  296 ARG A NH1 
2316 N NH2 . ARG A 296 ? 0.606 0.695 0.520 0.022  0.120  0.006  296 ARG A NH2 
2317 N N   . ALA A 297 ? 0.302 0.222 0.273 -0.027 -0.014 0.011  297 ALA A N   
2318 C CA  . ALA A 297 ? 0.303 0.207 0.274 -0.018 -0.010 0.013  297 ALA A CA  
2319 C C   . ALA A 297 ? 0.304 0.210 0.260 -0.016 -0.014 0.003  297 ALA A C   
2320 O O   . ALA A 297 ? 0.315 0.236 0.263 -0.019 -0.018 -0.001 297 ALA A O   
2321 C CB  . ALA A 297 ? 0.310 0.218 0.280 -0.007 -0.009 0.030  297 ALA A CB  
2322 N N   . PHE A 298 ? 0.326 0.222 0.283 -0.009 -0.011 0.002  298 PHE A N   
2323 C CA  . PHE A 298 ? 0.330 0.227 0.278 -0.009 -0.012 -0.011 298 PHE A CA  
2324 C C   . PHE A 298 ? 0.321 0.225 0.257 -0.001 -0.015 -0.006 298 PHE A C   
2325 O O   . PHE A 298 ? 0.339 0.245 0.270 -0.001 -0.015 -0.013 298 PHE A O   
2326 C CB  . PHE A 298 ? 0.336 0.217 0.298 -0.009 -0.005 -0.019 298 PHE A CB  
2327 C CG  . PHE A 298 ? 0.358 0.230 0.339 -0.020 0.001  -0.029 298 PHE A CG  
2328 C CD1 . PHE A 298 ? 0.410 0.294 0.386 -0.033 -0.000 -0.048 298 PHE A CD1 
2329 C CD2 . PHE A 298 ? 0.381 0.237 0.387 -0.017 0.008  -0.019 298 PHE A CD2 
2330 C CE1 . PHE A 298 ? 0.447 0.324 0.445 -0.045 0.006  -0.064 298 PHE A CE1 
2331 C CE2 . PHE A 298 ? 0.437 0.280 0.468 -0.028 0.015  -0.030 298 PHE A CE2 
2332 C CZ  . PHE A 298 ? 0.456 0.310 0.484 -0.043 0.014  -0.055 298 PHE A CZ  
2333 N N   . GLY A 299 ? 0.301 0.211 0.236 0.004  -0.016 0.004  299 GLY A N   
2334 C CA  . GLY A 299 ? 0.318 0.234 0.247 0.009  -0.017 0.004  299 GLY A CA  
2335 C C   . GLY A 299 ? 0.289 0.207 0.218 0.016  -0.017 0.003  299 GLY A C   
2336 O O   . GLY A 299 ? 0.311 0.226 0.245 0.019  -0.016 0.007  299 GLY A O   
2337 N N   . GLY A 300 ? 0.281 0.208 0.210 0.018  -0.017 -0.001 300 GLY A N   
2338 C CA  . GLY A 300 ? 0.275 0.211 0.204 0.022  -0.017 -0.005 300 GLY A CA  
2339 C C   . GLY A 300 ? 0.279 0.212 0.211 0.021  -0.017 -0.011 300 GLY A C   
2340 O O   . GLY A 300 ? 0.296 0.241 0.230 0.024  -0.018 -0.015 300 GLY A O   
2341 N N   . MET A 301 ? 0.280 0.204 0.212 0.018  -0.016 -0.012 301 MET A N   
2342 C CA  . MET A 301 ? 0.283 0.206 0.218 0.018  -0.014 -0.016 301 MET A CA  
2343 C C   . MET A 301 ? 0.288 0.208 0.222 0.020  -0.013 -0.017 301 MET A C   
2344 O O   . MET A 301 ? 0.299 0.211 0.231 0.018  -0.012 -0.017 301 MET A O   
2345 C CB  . MET A 301 ? 0.285 0.209 0.222 0.014  -0.012 -0.012 301 MET A CB  
2346 C CG  . MET A 301 ? 0.291 0.216 0.239 0.014  -0.010 -0.008 301 MET A CG  
2347 S SD  . MET A 301 ? 0.284 0.211 0.249 0.014  -0.006 -0.019 301 MET A SD  
2348 C CE  . MET A 301 ? 0.280 0.207 0.254 0.013  -0.003 -0.017 301 MET A CE  
2349 N N   . VAL A 302 ? 0.305 0.230 0.244 0.022  -0.012 -0.020 302 VAL A N   
2350 C CA  . VAL A 302 ? 0.304 0.225 0.247 0.026  -0.009 -0.022 302 VAL A CA  
2351 C C   . VAL A 302 ? 0.308 0.236 0.255 0.025  -0.006 -0.026 302 VAL A C   
2352 O O   . VAL A 302 ? 0.297 0.235 0.249 0.025  -0.008 -0.027 302 VAL A O   
2353 C CB  . VAL A 302 ? 0.310 0.237 0.262 0.034  -0.010 -0.014 302 VAL A CB  
2354 C CG1 . VAL A 302 ? 0.322 0.244 0.288 0.039  -0.004 -0.014 302 VAL A CG1 
2355 C CG2 . VAL A 302 ? 0.315 0.240 0.265 0.034  -0.012 -0.006 302 VAL A CG2 
2356 N N   . SER A 303 ? 0.301 0.228 0.247 0.024  -0.001 -0.032 303 SER A N   
2357 C CA  . SER A 303 ? 0.306 0.242 0.256 0.023  0.003  -0.034 303 SER A CA  
2358 C C   . SER A 303 ? 0.302 0.237 0.261 0.029  0.008  -0.040 303 SER A C   
2359 O O   . SER A 303 ? 0.324 0.248 0.287 0.031  0.011  -0.044 303 SER A O   
2360 C CB  . SER A 303 ? 0.302 0.248 0.244 0.017  0.005  -0.034 303 SER A CB  
2361 O OG  . SER A 303 ? 0.293 0.239 0.236 0.014  0.002  -0.024 303 SER A OG  
2362 N N   . PHE A 304 ? 0.302 0.248 0.270 0.032  0.011  -0.041 304 PHE A N   
2363 C CA  . PHE A 304 ? 0.316 0.264 0.299 0.039  0.018  -0.045 304 PHE A CA  
2364 C C   . PHE A 304 ? 0.317 0.281 0.306 0.038  0.023  -0.048 304 PHE A C   
2365 O O   . PHE A 304 ? 0.299 0.273 0.287 0.034  0.019  -0.043 304 PHE A O   
2366 C CB  . PHE A 304 ? 0.305 0.253 0.304 0.049  0.015  -0.036 304 PHE A CB  
2367 C CG  . PHE A 304 ? 0.306 0.272 0.308 0.050  0.007  -0.027 304 PHE A CG  
2368 C CD1 . PHE A 304 ? 0.303 0.273 0.295 0.045  -0.001 -0.024 304 PHE A CD1 
2369 C CD2 . PHE A 304 ? 0.306 0.292 0.323 0.054  0.008  -0.025 304 PHE A CD2 
2370 C CE1 . PHE A 304 ? 0.295 0.289 0.292 0.044  -0.007 -0.023 304 PHE A CE1 
2371 C CE2 . PHE A 304 ? 0.310 0.321 0.332 0.053  0.000  -0.022 304 PHE A CE2 
2372 C CZ  . PHE A 304 ? 0.290 0.305 0.302 0.047  -0.007 -0.023 304 PHE A CZ  
2373 N N   A ARG A 305 ? 0.325 0.291 0.323 0.042  0.032  -0.057 305 ARG A N   
2374 N N   B ARG A 305 ? 0.322 0.287 0.318 0.042  0.032  -0.057 305 ARG A N   
2375 C CA  A ARG A 305 ? 0.332 0.316 0.337 0.043  0.039  -0.060 305 ARG A CA  
2376 C CA  B ARG A 305 ? 0.325 0.309 0.329 0.043  0.039  -0.060 305 ARG A CA  
2377 C C   A ARG A 305 ? 0.329 0.318 0.359 0.054  0.043  -0.057 305 ARG A C   
2378 C C   B ARG A 305 ? 0.324 0.314 0.354 0.054  0.041  -0.055 305 ARG A C   
2379 O O   A ARG A 305 ? 0.329 0.306 0.375 0.063  0.048  -0.059 305 ARG A O   
2380 O O   B ARG A 305 ? 0.328 0.305 0.373 0.063  0.044  -0.054 305 ARG A O   
2381 C CB  A ARG A 305 ? 0.354 0.344 0.349 0.038  0.050  -0.075 305 ARG A CB  
2382 C CB  B ARG A 305 ? 0.340 0.330 0.338 0.039  0.051  -0.075 305 ARG A CB  
2383 C CG  A ARG A 305 ? 0.369 0.365 0.340 0.027  0.047  -0.075 305 ARG A CG  
2384 C CG  B ARG A 305 ? 0.353 0.351 0.326 0.028  0.049  -0.077 305 ARG A CG  
2385 C CD  A ARG A 305 ? 0.386 0.404 0.344 0.021  0.057  -0.091 305 ARG A CD  
2386 C CD  B ARG A 305 ? 0.367 0.389 0.331 0.023  0.060  -0.092 305 ARG A CD  
2387 N NE  A ARG A 305 ? 0.395 0.440 0.355 0.020  0.064  -0.087 305 ARG A NE  
2388 N NE  B ARG A 305 ? 0.376 0.388 0.349 0.025  0.071  -0.116 305 ARG A NE  
2389 C CZ  A ARG A 305 ? 0.401 0.476 0.352 0.016  0.074  -0.098 305 ARG A CZ  
2390 C CZ  B ARG A 305 ? 0.390 0.405 0.384 0.032  0.083  -0.128 305 ARG A CZ  
2391 N NH1 A ARG A 305 ? 0.435 0.520 0.373 0.010  0.080  -0.120 305 ARG A NH1 
2392 N NH1 B ARG A 305 ? 0.371 0.401 0.374 0.037  0.085  -0.119 305 ARG A NH1 
2393 N NH2 A ARG A 305 ? 0.388 0.488 0.344 0.016  0.080  -0.090 305 ARG A NH2 
2394 N NH2 B ARG A 305 ? 0.420 0.422 0.429 0.034  0.094  -0.152 305 ARG A NH2 
2395 N N   . MET A 306 ? 0.315 0.324 0.354 0.054  0.040  -0.050 306 MET A N   
2396 C CA  . MET A 306 ? 0.315 0.340 0.380 0.064  0.041  -0.044 306 MET A CA  
2397 C C   . MET A 306 ? 0.342 0.373 0.421 0.069  0.056  -0.053 306 MET A C   
2398 O O   . MET A 306 ? 0.344 0.385 0.414 0.062  0.062  -0.060 306 MET A O   
2399 C CB  . MET A 306 ? 0.304 0.352 0.374 0.059  0.033  -0.038 306 MET A CB  
2400 C CG  . MET A 306 ? 0.309 0.356 0.370 0.053  0.020  -0.033 306 MET A CG  
2401 S SD  . MET A 306 ? 0.342 0.392 0.411 0.066  0.014  -0.021 306 MET A SD  
2402 C CE  . MET A 306 ? 0.348 0.438 0.446 0.074  0.012  -0.012 306 MET A CE  
2403 N N   . ARG A 307 ? 0.367 0.399 0.473 0.082  0.062  -0.051 307 ARG A N   
2404 C CA  . ARG A 307 ? 0.388 0.428 0.515 0.089  0.078  -0.061 307 ARG A CA  
2405 C C   . ARG A 307 ? 0.386 0.455 0.516 0.086  0.078  -0.058 307 ARG A C   
2406 O O   . ARG A 307 ? 0.401 0.480 0.532 0.085  0.092  -0.070 307 ARG A O   
2407 C CB  . ARG A 307 ? 0.422 0.459 0.588 0.107  0.085  -0.052 307 ARG A CB  
2408 C CG  . ARG A 307 ? 0.454 0.459 0.626 0.110  0.090  -0.056 307 ARG A CG  
2409 C CD  . ARG A 307 ? 0.494 0.491 0.714 0.128  0.105  -0.051 307 ARG A CD  
2410 N NE  . ARG A 307 ? 0.538 0.503 0.770 0.129  0.111  -0.054 307 ARG A NE  
2411 C CZ  . ARG A 307 ? 0.572 0.513 0.803 0.123  0.125  -0.083 307 ARG A CZ  
2412 N NH1 . ARG A 307 ? 0.612 0.523 0.859 0.123  0.130  -0.084 307 ARG A NH1 
2413 N NH2 . ARG A 307 ? 0.590 0.540 0.807 0.115  0.135  -0.110 307 ARG A NH2 
2414 N N   . GLY A 308 ? 0.348 0.435 0.483 0.084  0.066  -0.044 308 GLY A N   
2415 C CA  . GLY A 308 ? 0.347 0.464 0.493 0.079  0.066  -0.041 308 GLY A CA  
2416 C C   . GLY A 308 ? 0.336 0.454 0.462 0.064  0.065  -0.044 308 GLY A C   
2417 O O   . GLY A 308 ? 0.340 0.479 0.478 0.057  0.063  -0.040 308 GLY A O   
2418 N N   . GLY A 309 ? 0.321 0.418 0.420 0.057  0.066  -0.049 309 GLY A N   
2419 C CA  . GLY A 309 ? 0.333 0.437 0.419 0.045  0.069  -0.047 309 GLY A CA  
2420 C C   . GLY A 309 ? 0.301 0.400 0.387 0.035  0.057  -0.039 309 GLY A C   
2421 O O   . GLY A 309 ? 0.286 0.377 0.373 0.037  0.047  -0.038 309 GLY A O   
2422 N N   . GLU A 310 ? 0.311 0.419 0.399 0.025  0.062  -0.031 310 GLU A N   
2423 C CA  . GLU A 310 ? 0.315 0.417 0.413 0.015  0.056  -0.025 310 GLU A CA  
2424 C C   . GLU A 310 ? 0.305 0.417 0.425 0.014  0.048  -0.030 310 GLU A C   
2425 O O   . GLU A 310 ? 0.281 0.385 0.403 0.008  0.039  -0.034 310 GLU A O   
2426 C CB  . GLU A 310 ? 0.334 0.449 0.443 0.007  0.066  -0.012 310 GLU A CB  
2427 C CG  . GLU A 310 ? 0.366 0.469 0.493 -0.004 0.063  -0.005 310 GLU A CG  
2428 C CD  . GLU A 310 ? 0.399 0.515 0.548 -0.012 0.075  0.014  310 GLU A CD  
2429 O OE1 . GLU A 310 ? 0.444 0.574 0.621 -0.017 0.080  0.015  310 GLU A OE1 
2430 O OE2 . GLU A 310 ? 0.497 0.609 0.637 -0.013 0.079  0.030  310 GLU A OE2 
2431 N N   . GLU A 311 ? 0.307 0.443 0.446 0.017  0.051  -0.031 311 GLU A N   
2432 C CA  . GLU A 311 ? 0.313 0.471 0.476 0.014  0.043  -0.036 311 GLU A CA  
2433 C C   . GLU A 311 ? 0.284 0.438 0.435 0.020  0.031  -0.040 311 GLU A C   
2434 O O   . GLU A 311 ? 0.280 0.444 0.438 0.012  0.022  -0.047 311 GLU A O   
2435 C CB  . GLU A 311 ? 0.347 0.534 0.531 0.020  0.050  -0.034 311 GLU A CB  
2436 C CG  . GLU A 311 ? 0.402 0.622 0.611 0.018  0.042  -0.037 311 GLU A CG  
2437 C CD  . GLU A 311 ? 0.448 0.697 0.679 0.026  0.050  -0.032 311 GLU A CD  
2438 O OE1 . GLU A 311 ? 0.486 0.731 0.712 0.042  0.056  -0.029 311 GLU A OE1 
2439 O OE2 . GLU A 311 ? 0.555 0.827 0.812 0.016  0.053  -0.033 311 GLU A OE2 
2440 N N   . ALA A 312 ? 0.273 0.415 0.409 0.034  0.032  -0.037 312 ALA A N   
2441 C CA  . ALA A 312 ? 0.282 0.423 0.411 0.042  0.022  -0.035 312 ALA A CA  
2442 C C   . ALA A 312 ? 0.273 0.393 0.382 0.034  0.015  -0.039 312 ALA A C   
2443 O O   . ALA A 312 ? 0.273 0.404 0.380 0.033  0.005  -0.040 312 ALA A O   
2444 C CB  . ALA A 312 ? 0.295 0.424 0.422 0.057  0.028  -0.030 312 ALA A CB  
2445 N N   . ALA A 313 ? 0.266 0.359 0.359 0.030  0.021  -0.040 313 ALA A N   
2446 C CA  . ALA A 313 ? 0.278 0.350 0.355 0.023  0.017  -0.042 313 ALA A CA  
2447 C C   . ALA A 313 ? 0.280 0.364 0.373 0.011  0.012  -0.050 313 ALA A C   
2448 O O   . ALA A 313 ? 0.273 0.353 0.359 0.009  0.005  -0.055 313 ALA A O   
2449 C CB  . ALA A 313 ? 0.286 0.338 0.349 0.021  0.024  -0.038 313 ALA A CB  
2450 N N   . LEU A 314 ? 0.288 0.396 0.369 0.046  0.088  -0.054 314 LEU A N   
2451 C CA  . LEU A 314 ? 0.287 0.402 0.371 0.036  0.079  -0.042 314 LEU A CA  
2452 C C   . LEU A 314 ? 0.273 0.394 0.382 0.041  0.066  -0.036 314 LEU A C   
2453 O O   . LEU A 314 ? 0.262 0.376 0.364 0.034  0.054  -0.030 314 LEU A O   
2454 C CB  . LEU A 314 ? 0.292 0.433 0.386 0.027  0.090  -0.039 314 LEU A CB  
2455 C CG  . LEU A 314 ? 0.322 0.462 0.389 0.020  0.102  -0.040 314 LEU A CG  
2456 C CD1 . LEU A 314 ? 0.335 0.502 0.415 0.012  0.114  -0.035 314 LEU A CD1 
2457 C CD2 . LEU A 314 ? 0.322 0.440 0.361 0.012  0.093  -0.033 314 LEU A CD2 
2458 N N   . ARG A 315 ? 0.274 0.408 0.409 0.054  0.070  -0.039 315 ARG A N   
2459 C CA  . ARG A 315 ? 0.300 0.445 0.458 0.062  0.056  -0.030 315 ARG A CA  
2460 C C   . ARG A 315 ? 0.287 0.404 0.428 0.064  0.044  -0.026 315 ARG A C   
2461 O O   . ARG A 315 ? 0.260 0.382 0.400 0.059  0.030  -0.018 315 ARG A O   
2462 C CB  . ARG A 315 ? 0.326 0.490 0.520 0.078  0.063  -0.031 315 ARG A CB  
2463 C CG  . ARG A 315 ? 0.408 0.611 0.630 0.075  0.068  -0.029 315 ARG A CG  
2464 C CD  . ARG A 315 ? 0.472 0.700 0.736 0.094  0.072  -0.027 315 ARG A CD  
2465 N NE  . ARG A 315 ? 0.513 0.715 0.777 0.110  0.079  -0.033 315 ARG A NE  
2466 C CZ  . ARG A 315 ? 0.577 0.777 0.848 0.120  0.099  -0.046 315 ARG A CZ  
2467 N NH1 . ARG A 315 ? 0.595 0.767 0.868 0.134  0.105  -0.052 315 ARG A NH1 
2468 N NH2 . ARG A 315 ? 0.575 0.800 0.854 0.114  0.115  -0.054 315 ARG A NH2 
2469 N N   . VAL A 316 ? 0.283 0.374 0.408 0.070  0.050  -0.033 316 VAL A N   
2470 C CA  . VAL A 316 ? 0.288 0.352 0.398 0.072  0.040  -0.029 316 VAL A CA  
2471 C C   . VAL A 316 ? 0.278 0.336 0.364 0.057  0.030  -0.025 316 VAL A C   
2472 O O   . VAL A 316 ? 0.272 0.326 0.354 0.055  0.018  -0.017 316 VAL A O   
2473 C CB  . VAL A 316 ? 0.309 0.347 0.408 0.076  0.049  -0.039 316 VAL A CB  
2474 C CG1 . VAL A 316 ? 0.337 0.350 0.421 0.075  0.040  -0.034 316 VAL A CG1 
2475 C CG2 . VAL A 316 ? 0.350 0.389 0.475 0.092  0.059  -0.044 316 VAL A CG2 
2476 N N   . CYS A 317 ? 0.275 0.331 0.344 0.047  0.037  -0.030 317 CYS A N   
2477 C CA  . CYS A 317 ? 0.267 0.314 0.317 0.035  0.031  -0.026 317 CYS A CA  
2478 C C   . CYS A 317 ? 0.269 0.330 0.330 0.029  0.021  -0.020 317 CYS A C   
2479 O O   . CYS A 317 ? 0.281 0.330 0.328 0.023  0.014  -0.018 317 CYS A O   
2480 C CB  . CYS A 317 ? 0.276 0.326 0.314 0.027  0.040  -0.029 317 CYS A CB  
2481 S SG  . CYS A 317 ? 0.303 0.337 0.318 0.029  0.047  -0.037 317 CYS A SG  
2482 N N   . ALA A 318 ? 0.264 0.350 0.348 0.029  0.022  -0.019 318 ALA A N   
2483 C CA  . ALA A 318 ? 0.272 0.376 0.367 0.020  0.013  -0.016 318 ALA A CA  
2484 C C   . ALA A 318 ? 0.277 0.389 0.379 0.027  -0.000 -0.011 318 ALA A C   
2485 O O   . ALA A 318 ? 0.293 0.418 0.397 0.017  -0.009 -0.010 318 ALA A O   
2486 C CB  . ALA A 318 ? 0.277 0.410 0.397 0.017  0.019  -0.017 318 ALA A CB  
2487 N N   . LYS A 319 ? 0.267 0.373 0.373 0.041  -0.000 -0.007 319 LYS A N   
2488 C CA  . LYS A 319 ? 0.268 0.387 0.387 0.051  -0.012 0.002  319 LYS A CA  
2489 C C   . LYS A 319 ? 0.258 0.356 0.354 0.051  -0.020 0.008  319 LYS A C   
2490 O O   . LYS A 319 ? 0.259 0.370 0.358 0.054  -0.031 0.017  319 LYS A O   
2491 C CB  . LYS A 319 ? 0.279 0.405 0.423 0.068  -0.005 0.005  319 LYS A CB  
2492 C CG  . LYS A 319 ? 0.335 0.487 0.504 0.079  -0.016 0.018  319 LYS A CG  
2493 C CD  . LYS A 319 ? 0.352 0.519 0.556 0.096  -0.007 0.020  319 LYS A CD  
2494 C CE  . LYS A 319 ? 0.375 0.562 0.603 0.111  -0.018 0.038  319 LYS A CE  
2495 N NZ  . LYS A 319 ? 0.405 0.586 0.663 0.132  -0.006 0.040  319 LYS A NZ  
2496 N N   . THR A 320 ? 0.263 0.331 0.336 0.048  -0.014 0.002  320 THR A N   
2497 C CA  . THR A 320 ? 0.271 0.320 0.324 0.047  -0.019 0.007  320 THR A CA  
2498 C C   . THR A 320 ? 0.290 0.350 0.330 0.035  -0.029 0.007  320 THR A C   
2499 O O   . THR A 320 ? 0.283 0.350 0.322 0.024  -0.028 -0.000 320 THR A O   
2500 C CB  . THR A 320 ? 0.282 0.302 0.316 0.044  -0.011 0.000  320 THR A CB  
2501 O OG1 . THR A 320 ? 0.293 0.312 0.318 0.034  -0.007 -0.007 320 THR A OG1 
2502 C CG2 . THR A 320 ? 0.280 0.287 0.323 0.054  -0.002 -0.002 320 THR A CG2 
2503 N N   A LYS A 321 ? 0.306 0.365 0.336 0.037  -0.038 0.016  321 LYS A N   
2504 N N   B LYS A 321 ? 0.300 0.360 0.331 0.037  -0.038 0.016  321 LYS A N   
2505 C CA  A LYS A 321 ? 0.335 0.407 0.350 0.026  -0.047 0.015  321 LYS A CA  
2506 C CA  B LYS A 321 ? 0.325 0.397 0.340 0.026  -0.047 0.015  321 LYS A CA  
2507 C C   A LYS A 321 ? 0.342 0.391 0.331 0.022  -0.045 0.014  321 LYS A C   
2508 C C   B LYS A 321 ? 0.336 0.384 0.326 0.022  -0.044 0.013  321 LYS A C   
2509 O O   A LYS A 321 ? 0.362 0.418 0.336 0.012  -0.049 0.009  321 LYS A O   
2510 O O   B LYS A 321 ? 0.362 0.414 0.337 0.011  -0.047 0.006  321 LYS A O   
2511 C CB  A LYS A 321 ? 0.371 0.472 0.394 0.031  -0.060 0.028  321 LYS A CB  
2512 C CB  B LYS A 321 ? 0.351 0.452 0.374 0.032  -0.060 0.028  321 LYS A CB  
2513 C CG  A LYS A 321 ? 0.404 0.538 0.453 0.031  -0.065 0.027  321 LYS A CG  
2514 C CG  B LYS A 321 ? 0.370 0.502 0.423 0.035  -0.064 0.030  321 LYS A CG  
2515 C CD  A LYS A 321 ? 0.429 0.598 0.486 0.035  -0.081 0.041  321 LYS A CD  
2516 C CD  B LYS A 321 ? 0.363 0.508 0.421 0.020  -0.063 0.015  321 LYS A CD  
2517 C CE  A LYS A 321 ? 0.441 0.642 0.533 0.043  -0.084 0.046  321 LYS A CE  
2518 C CE  B LYS A 321 ? 0.375 0.560 0.462 0.020  -0.069 0.017  321 LYS A CE  
2519 N NZ  A LYS A 321 ? 0.468 0.700 0.572 0.053  -0.098 0.066  321 LYS A NZ  
2520 N NZ  B LYS A 321 ? 0.368 0.552 0.480 0.029  -0.058 0.017  321 LYS A NZ  
2521 N N   . VAL A 322 ? 0.310 0.335 0.296 0.029  -0.038 0.017  322 VAL A N   
2522 C CA  . VAL A 322 ? 0.310 0.315 0.275 0.025  -0.035 0.016  322 VAL A CA  
2523 C C   . VAL A 322 ? 0.308 0.295 0.272 0.022  -0.025 0.006  322 VAL A C   
2524 O O   . VAL A 322 ? 0.316 0.297 0.269 0.014  -0.022 -0.001 322 VAL A O   
2525 C CB  . VAL A 322 ? 0.315 0.311 0.277 0.032  -0.036 0.030  322 VAL A CB  
2526 C CG1 . VAL A 322 ? 0.320 0.300 0.263 0.026  -0.031 0.028  322 VAL A CG1 
2527 C CG2 . VAL A 322 ? 0.338 0.354 0.303 0.037  -0.046 0.045  322 VAL A CG2 
2528 N N   . PHE A 323 ? 0.272 0.252 0.248 0.029  -0.019 0.005  323 PHE A N   
2529 C CA  . PHE A 323 ? 0.260 0.230 0.234 0.025  -0.012 -0.003 323 PHE A CA  
2530 C C   . PHE A 323 ? 0.267 0.249 0.244 0.019  -0.012 -0.008 323 PHE A C   
2531 O O   . PHE A 323 ? 0.279 0.279 0.270 0.019  -0.015 -0.008 323 PHE A O   
2532 C CB  . PHE A 323 ? 0.254 0.221 0.239 0.032  -0.006 -0.006 323 PHE A CB  
2533 C CG  . PHE A 323 ? 0.275 0.225 0.259 0.036  -0.003 -0.005 323 PHE A CG  
2534 C CD1 . PHE A 323 ? 0.290 0.235 0.282 0.044  -0.006 0.004  323 PHE A CD1 
2535 C CD2 . PHE A 323 ? 0.278 0.216 0.253 0.032  0.002  -0.012 323 PHE A CD2 
2536 C CE1 . PHE A 323 ? 0.295 0.221 0.289 0.046  -0.001 0.005  323 PHE A CE1 
2537 C CE2 . PHE A 323 ? 0.280 0.202 0.256 0.033  0.005  -0.013 323 PHE A CE2 
2538 C CZ  . PHE A 323 ? 0.297 0.211 0.283 0.040  0.004  -0.005 323 PHE A CZ  
2539 N N   . THR A 324 ? 0.257 0.232 0.225 0.012  -0.008 -0.013 324 THR A N   
2540 C CA  . THR A 324 ? 0.249 0.229 0.222 0.005  -0.006 -0.017 324 THR A CA  
2541 C C   . THR A 324 ? 0.249 0.229 0.227 0.006  0.001  -0.017 324 THR A C   
2542 O O   . THR A 324 ? 0.246 0.215 0.216 0.008  0.005  -0.016 324 THR A O   
2543 C CB  . THR A 324 ? 0.273 0.242 0.236 -0.001 -0.004 -0.020 324 THR A CB  
2544 O OG1 . THR A 324 ? 0.278 0.252 0.233 -0.003 -0.010 -0.022 324 THR A OG1 
2545 C CG2 . THR A 324 ? 0.284 0.253 0.255 -0.009 -0.000 -0.025 324 THR A CG2 
2546 N N   . LEU A 325 ? 0.241 0.233 0.231 0.003  0.003  -0.017 325 LEU A N   
2547 C CA  . LEU A 325 ? 0.250 0.244 0.243 0.002  0.011  -0.016 325 LEU A CA  
2548 C C   . LEU A 325 ? 0.243 0.226 0.231 -0.004 0.016  -0.013 325 LEU A C   
2549 O O   . LEU A 325 ? 0.248 0.230 0.243 -0.011 0.016  -0.014 325 LEU A O   
2550 C CB  . LEU A 325 ? 0.237 0.250 0.248 -0.000 0.014  -0.017 325 LEU A CB  
2551 C CG  . LEU A 325 ? 0.251 0.271 0.265 -0.002 0.024  -0.014 325 LEU A CG  
2552 C CD1 . LEU A 325 ? 0.266 0.284 0.270 0.006  0.028  -0.016 325 LEU A CD1 
2553 C CD2 . LEU A 325 ? 0.240 0.283 0.275 -0.005 0.026  -0.015 325 LEU A CD2 
2554 N N   . ALA A 326 ? 0.252 0.227 0.230 -0.001 0.018  -0.009 326 ALA A N   
2555 C CA  . ALA A 326 ? 0.249 0.213 0.223 -0.003 0.022  -0.003 326 ALA A CA  
2556 C C   . ALA A 326 ? 0.258 0.224 0.221 0.001  0.023  0.002  326 ALA A C   
2557 O O   . ALA A 326 ? 0.271 0.241 0.227 0.005  0.020  -0.003 326 ALA A O   
2558 C CB  . ALA A 326 ? 0.257 0.208 0.228 -0.003 0.019  -0.006 326 ALA A CB  
2559 N N   . GLU A 327 ? 0.256 0.220 0.218 0.001  0.027  0.012  327 GLU A N   
2560 C CA  . GLU A 327 ? 0.254 0.223 0.206 0.004  0.025  0.019  327 GLU A CA  
2561 C C   . GLU A 327 ? 0.269 0.231 0.219 0.008  0.020  0.016  327 GLU A C   
2562 O O   . GLU A 327 ? 0.264 0.214 0.219 0.007  0.019  0.010  327 GLU A O   
2563 C CB  . GLU A 327 ? 0.286 0.255 0.238 0.004  0.030  0.034  327 GLU A CB  
2564 C CG  . GLU A 327 ? 0.311 0.291 0.263 -0.001 0.037  0.038  327 GLU A CG  
2565 C CD  . GLU A 327 ? 0.366 0.354 0.312 -0.001 0.041  0.057  327 GLU A CD  
2566 O OE1 . GLU A 327 ? 0.400 0.383 0.346 0.004  0.038  0.069  327 GLU A OE1 
2567 O OE2 . GLU A 327 ? 0.369 0.367 0.313 -0.006 0.048  0.061  327 GLU A OE2 
2568 N N   . SER A 328 ? 0.260 0.230 0.202 0.010  0.017  0.019  328 SER A N   
2569 C CA  . SER A 328 ? 0.261 0.230 0.204 0.012  0.012  0.018  328 SER A CA  
2570 C C   . SER A 328 ? 0.268 0.237 0.206 0.011  0.009  0.006  328 SER A C   
2571 O O   . SER A 328 ? 0.284 0.253 0.219 0.009  0.010  -0.002 328 SER A O   
2572 C CB  . SER A 328 ? 0.276 0.232 0.229 0.015  0.015  0.021  328 SER A CB  
2573 O OG  . SER A 328 ? 0.277 0.238 0.234 0.019  0.012  0.025  328 SER A OG  
2574 N N   . LEU A 329 ? 0.266 0.236 0.206 0.012  0.006  0.005  329 LEU A N   
2575 C CA  . LEU A 329 ? 0.261 0.230 0.198 0.009  0.003  -0.004 329 LEU A CA  
2576 C C   . LEU A 329 ? 0.255 0.224 0.198 0.009  0.002  -0.002 329 LEU A C   
2577 O O   . LEU A 329 ? 0.256 0.228 0.205 0.013  0.003  0.006  329 LEU A O   
2578 C CB  . LEU A 329 ? 0.254 0.235 0.183 0.005  0.001  -0.009 329 LEU A CB  
2579 C CG  . LEU A 329 ? 0.265 0.264 0.190 0.004  -0.003 -0.002 329 LEU A CG  
2580 C CD1 . LEU A 329 ? 0.256 0.266 0.181 -0.002 -0.007 -0.010 329 LEU A CD1 
2581 C CD2 . LEU A 329 ? 0.298 0.310 0.214 0.004  -0.002 0.002  329 LEU A CD2 
2582 N N   . GLY A 330 ? 0.246 0.211 0.187 0.006  0.001  -0.008 330 GLY A N   
2583 C CA  . GLY A 330 ? 0.243 0.212 0.191 0.004  0.000  -0.007 330 GLY A CA  
2584 C C   . GLY A 330 ? 0.253 0.213 0.204 0.007  0.004  -0.005 330 GLY A C   
2585 O O   . GLY A 330 ? 0.287 0.254 0.245 0.006  0.006  -0.003 330 GLY A O   
2586 N N   . GLY A 331 ? 0.261 0.211 0.208 0.009  0.006  -0.006 331 GLY A N   
2587 C CA  . GLY A 331 ? 0.268 0.212 0.215 0.009  0.010  -0.007 331 GLY A CA  
2588 C C   . GLY A 331 ? 0.265 0.204 0.205 0.006  0.009  -0.008 331 GLY A C   
2589 O O   . GLY A 331 ? 0.268 0.204 0.206 0.005  0.006  -0.008 331 GLY A O   
2590 N N   . VAL A 332 ? 0.259 0.197 0.196 0.005  0.013  -0.009 332 VAL A N   
2591 C CA  . VAL A 332 ? 0.264 0.199 0.192 0.003  0.013  -0.007 332 VAL A CA  
2592 C C   . VAL A 332 ? 0.268 0.200 0.191 0.004  0.008  -0.006 332 VAL A C   
2593 O O   . VAL A 332 ? 0.270 0.199 0.190 0.004  0.005  -0.001 332 VAL A O   
2594 C CB  . VAL A 332 ? 0.270 0.208 0.191 0.001  0.018  -0.008 332 VAL A CB  
2595 C CG1 . VAL A 332 ? 0.272 0.217 0.203 -0.000 0.024  -0.007 332 VAL A CG1 
2596 C CG2 . VAL A 332 ? 0.282 0.220 0.200 0.002  0.021  -0.015 332 VAL A CG2 
2597 N N   . GLU A 333 ? 0.258 0.280 0.214 0.071  0.032  0.023  333 GLU A N   
2598 C CA  . GLU A 333 ? 0.269 0.260 0.225 0.055  0.026  0.012  333 GLU A CA  
2599 C C   . GLU A 333 ? 0.265 0.259 0.241 0.042  0.021  0.009  333 GLU A C   
2600 O O   . GLU A 333 ? 0.256 0.255 0.231 0.047  0.024  0.011  333 GLU A O   
2601 C CB  . GLU A 333 ? 0.323 0.270 0.245 0.060  0.030  0.006  333 GLU A CB  
2602 C CG  . GLU A 333 ? 0.364 0.290 0.272 0.066  0.033  0.003  333 GLU A CG  
2603 C CD  . GLU A 333 ? 0.442 0.382 0.343 0.087  0.042  0.011  333 GLU A CD  
2604 O OE1 . GLU A 333 ? 0.453 0.417 0.348 0.108  0.049  0.020  333 GLU A OE1 
2605 O OE2 . GLU A 333 ? 0.567 0.496 0.466 0.086  0.042  0.008  333 GLU A OE2 
2606 N N   . SER A 334 ? 0.239 0.231 0.228 0.028  0.015  0.006  334 SER A N   
2607 C CA  . SER A 334 ? 0.244 0.235 0.246 0.020  0.012  0.003  334 SER A CA  
2608 C C   . SER A 334 ? 0.250 0.223 0.242 0.021  0.014  -0.002 334 SER A C   
2609 O O   . SER A 334 ? 0.267 0.223 0.247 0.018  0.014  -0.004 334 SER A O   
2610 C CB  . SER A 334 ? 0.243 0.234 0.255 0.012  0.007  0.002  334 SER A CB  
2611 O OG  . SER A 334 ? 0.226 0.229 0.242 0.007  0.003  0.007  334 SER A OG  
2612 N N   . LEU A 335 ? 0.248 0.225 0.246 0.021  0.015  -0.003 335 LEU A N   
2613 C CA  . LEU A 335 ? 0.260 0.223 0.251 0.020  0.016  -0.006 335 LEU A CA  
2614 C C   . LEU A 335 ? 0.250 0.220 0.254 0.016  0.014  -0.008 335 LEU A C   
2615 O O   . LEU A 335 ? 0.252 0.228 0.262 0.015  0.013  -0.007 335 LEU A O   
2616 C CB  . LEU A 335 ? 0.266 0.224 0.245 0.029  0.021  -0.005 335 LEU A CB  
2617 C CG  . LEU A 335 ? 0.287 0.234 0.244 0.041  0.025  -0.002 335 LEU A CG  
2618 C CD1 . LEU A 335 ? 0.304 0.252 0.249 0.056  0.031  0.002  335 LEU A CD1 
2619 C CD2 . LEU A 335 ? 0.332 0.245 0.264 0.037  0.025  -0.006 335 LEU A CD2 
2620 N N   . ILE A 336 ? 0.246 0.213 0.249 0.012  0.014  -0.008 336 ILE A N   
2621 C CA  . ILE A 336 ? 0.238 0.214 0.250 0.013  0.014  -0.008 336 ILE A CA  
2622 C C   . ILE A 336 ? 0.240 0.214 0.246 0.010  0.016  -0.008 336 ILE A C   
2623 O O   . ILE A 336 ? 0.251 0.214 0.244 0.003  0.014  -0.007 336 ILE A O   
2624 C CB  . ILE A 336 ? 0.248 0.235 0.267 0.012  0.013  -0.004 336 ILE A CB  
2625 C CG1 . ILE A 336 ? 0.260 0.258 0.284 0.020  0.016  -0.002 336 ILE A CG1 
2626 C CG2 . ILE A 336 ? 0.275 0.267 0.290 0.001  0.010  0.000  336 ILE A CG2 
2627 C CD1 . ILE A 336 ? 0.269 0.279 0.298 0.027  0.017  0.004  336 ILE A CD1 
2628 N N   . GLU A 337 ? 0.246 0.226 0.256 0.014  0.018  -0.009 337 GLU A N   
2629 C CA  . GLU A 337 ? 0.249 0.231 0.255 0.010  0.019  -0.007 337 GLU A CA  
2630 C C   . GLU A 337 ? 0.242 0.238 0.255 0.016  0.021  -0.007 337 GLU A C   
2631 O O   . GLU A 337 ? 0.236 0.229 0.250 0.024  0.023  -0.009 337 GLU A O   
2632 C CB  . GLU A 337 ? 0.257 0.225 0.252 0.011  0.020  -0.009 337 GLU A CB  
2633 C CG  . GLU A 337 ? 0.262 0.233 0.261 0.018  0.022  -0.011 337 GLU A CG  
2634 C CD  . GLU A 337 ? 0.273 0.244 0.268 0.019  0.023  -0.011 337 GLU A CD  
2635 O OE1 . GLU A 337 ? 0.269 0.247 0.266 0.021  0.024  -0.011 337 GLU A OE1 
2636 O OE2 . GLU A 337 ? 0.322 0.287 0.309 0.015  0.024  -0.009 337 GLU A OE2 
2637 N N   . HIS A 338 ? 0.244 0.250 0.256 0.012  0.022  -0.003 338 HIS A N   
2638 C CA  . HIS A 338 ? 0.248 0.268 0.264 0.019  0.025  -0.002 338 HIS A CA  
2639 C C   . HIS A 338 ? 0.260 0.270 0.270 0.017  0.026  -0.006 338 HIS A C   
2640 O O   . HIS A 338 ? 0.261 0.270 0.266 0.008  0.024  -0.002 338 HIS A O   
2641 C CB  . HIS A 338 ? 0.250 0.300 0.271 0.014  0.025  0.008  338 HIS A CB  
2642 C CG  . HIS A 338 ? 0.257 0.327 0.282 0.025  0.030  0.012  338 HIS A CG  
2643 N ND1 . HIS A 338 ? 0.246 0.324 0.269 0.019  0.030  0.014  338 HIS A ND1 
2644 C CD2 . HIS A 338 ? 0.265 0.347 0.290 0.045  0.037  0.014  338 HIS A CD2 
2645 C CE1 . HIS A 338 ? 0.273 0.371 0.298 0.034  0.037  0.017  338 HIS A CE1 
2646 N NE2 . HIS A 338 ? 0.256 0.356 0.281 0.051  0.041  0.017  338 HIS A NE2 
2647 N N   . PRO A 339 ? 0.264 0.263 0.271 0.022  0.027  -0.011 339 PRO A N   
2648 C CA  . PRO A 339 ? 0.268 0.262 0.270 0.020  0.028  -0.013 339 PRO A CA  
2649 C C   . PRO A 339 ? 0.269 0.275 0.271 0.019  0.029  -0.009 339 PRO A C   
2650 O O   . PRO A 339 ? 0.268 0.270 0.266 0.014  0.028  -0.008 339 PRO A O   
2651 C CB  . PRO A 339 ? 0.290 0.277 0.286 0.023  0.028  -0.017 339 PRO A CB  
2652 C CG  . PRO A 339 ? 0.307 0.285 0.302 0.024  0.026  -0.018 339 PRO A CG  
2653 C CD  . PRO A 339 ? 0.282 0.269 0.283 0.028  0.028  -0.015 339 PRO A CD  
2654 N N   . GLY A 340 ? 0.278 0.300 0.283 0.024  0.032  -0.007 340 GLY A N   
2655 C CA  . GLY A 340 ? 0.277 0.316 0.283 0.024  0.034  -0.003 340 GLY A CA  
2656 C C   . GLY A 340 ? 0.278 0.325 0.284 0.009  0.030  0.005  340 GLY A C   
2657 O O   . GLY A 340 ? 0.273 0.323 0.275 0.003  0.029  0.007  340 GLY A O   
2658 N N   . LYS A 341 ? 0.264 0.311 0.270 0.000  0.026  0.009  341 LYS A N   
2659 C CA  . LYS A 341 ? 0.288 0.332 0.282 -0.019 0.019  0.016  341 LYS A CA  
2660 C C   . LYS A 341 ? 0.304 0.305 0.278 -0.024 0.016  0.011  341 LYS A C   
2661 O O   . LYS A 341 ? 0.315 0.297 0.267 -0.040 0.011  0.016  341 LYS A O   
2662 C CB  . LYS A 341 ? 0.312 0.386 0.313 -0.028 0.016  0.027  341 LYS A CB  
2663 C CG  . LYS A 341 ? 0.348 0.471 0.364 -0.024 0.019  0.038  341 LYS A CG  
2664 C CD  . LYS A 341 ? 0.393 0.558 0.418 -0.028 0.018  0.052  341 LYS A CD  
2665 C CE  . LYS A 341 ? 0.474 0.698 0.509 -0.035 0.017  0.071  341 LYS A CE  
2666 N NZ  . LYS A 341 ? 0.521 0.753 0.557 -0.024 0.023  0.069  341 LYS A NZ  
2667 N N   . MET A 342 ? 0.286 0.273 0.263 -0.011 0.020  0.004  342 MET A N   
2668 C CA  . MET A 342 ? 0.297 0.250 0.256 -0.010 0.019  0.001  342 MET A CA  
2669 C C   . MET A 342 ? 0.294 0.240 0.251 0.004  0.024  -0.002 342 MET A C   
2670 O O   . MET A 342 ? 0.314 0.251 0.259 0.002  0.024  0.000  342 MET A O   
2671 C CB  . MET A 342 ? 0.297 0.249 0.259 -0.008 0.018  -0.001 342 MET A CB  
2672 C CG  . MET A 342 ? 0.299 0.262 0.260 -0.023 0.013  0.005  342 MET A CG  
2673 S SD  . MET A 342 ? 0.295 0.265 0.266 -0.022 0.012  0.004  342 MET A SD  
2674 C CE  . MET A 342 ? 0.329 0.256 0.273 -0.017 0.012  -0.001 342 MET A CE  
2675 N N   . THR A 343 ? 0.286 0.238 0.252 0.014  0.026  -0.005 343 THR A N   
2676 C CA  . THR A 343 ? 0.290 0.243 0.253 0.025  0.029  -0.004 343 THR A CA  
2677 C C   . THR A 343 ? 0.284 0.251 0.254 0.024  0.030  -0.003 343 THR A C   
2678 O O   . THR A 343 ? 0.307 0.276 0.272 0.031  0.033  0.001  343 THR A O   
2679 C CB  . THR A 343 ? 0.289 0.257 0.264 0.030  0.030  -0.004 343 THR A CB  
2680 O OG1 . THR A 343 ? 0.280 0.259 0.268 0.024  0.027  -0.008 343 THR A OG1 
2681 C CG2 . THR A 343 ? 0.317 0.271 0.282 0.035  0.030  -0.003 343 THR A CG2 
2682 N N   . HIS A 344 ? 0.269 0.249 0.250 0.018  0.029  -0.006 344 HIS A N   
2683 C CA  . HIS A 344 ? 0.262 0.255 0.248 0.017  0.030  -0.006 344 HIS A CA  
2684 C C   . HIS A 344 ? 0.266 0.264 0.251 0.012  0.030  -0.004 344 HIS A C   
2685 O O   . HIS A 344 ? 0.274 0.285 0.262 0.012  0.032  -0.005 344 HIS A O   
2686 C CB  . HIS A 344 ? 0.261 0.261 0.252 0.018  0.030  -0.011 344 HIS A CB  
2687 C CG  . HIS A 344 ? 0.259 0.260 0.249 0.018  0.028  -0.010 344 HIS A CG  
2688 N ND1 . HIS A 344 ? 0.261 0.258 0.252 0.019  0.027  -0.009 344 HIS A ND1 
2689 C CD2 . HIS A 344 ? 0.272 0.281 0.258 0.013  0.026  -0.007 344 HIS A CD2 
2690 C CE1 . HIS A 344 ? 0.263 0.271 0.254 0.017  0.025  -0.005 344 HIS A CE1 
2691 N NE2 . HIS A 344 ? 0.250 0.266 0.237 0.011  0.024  -0.003 344 HIS A NE2 
2692 N N   . ALA A 345 ? 0.283 0.272 0.259 0.005  0.028  -0.000 345 ALA A N   
2693 C CA  . ALA A 345 ? 0.292 0.288 0.264 -0.005 0.026  0.005  345 ALA A CA  
2694 C C   . ALA A 345 ? 0.297 0.288 0.262 -0.002 0.028  0.006  345 ALA A C   
2695 O O   . ALA A 345 ? 0.306 0.315 0.276 -0.007 0.028  0.009  345 ALA A O   
2696 C CB  . ALA A 345 ? 0.319 0.295 0.272 -0.019 0.021  0.010  345 ALA A CB  
2697 N N   . SER A 346 ? 0.301 0.276 0.258 0.007  0.029  0.006  346 SER A N   
2698 C CA  . SER A 346 ? 0.312 0.286 0.262 0.012  0.032  0.009  346 SER A CA  
2699 C C   . SER A 346 ? 0.293 0.294 0.260 0.013  0.033  0.007  346 SER A C   
2700 O O   . SER A 346 ? 0.323 0.331 0.288 0.015  0.034  0.010  346 SER A O   
2701 C CB  . SER A 346 ? 0.323 0.281 0.262 0.026  0.035  0.012  346 SER A CB  
2702 O OG  . SER A 346 ? 0.340 0.313 0.293 0.030  0.035  0.009  346 SER A OG  
2703 N N   . THR A 347 ? 0.270 0.283 0.248 0.013  0.033  0.001  347 THR A N   
2704 C CA  . THR A 347 ? 0.266 0.292 0.248 0.013  0.034  -0.002 347 THR A CA  
2705 C C   . THR A 347 ? 0.271 0.307 0.253 0.012  0.036  -0.004 347 THR A C   
2706 O O   . THR A 347 ? 0.274 0.313 0.251 0.014  0.038  -0.008 347 THR A O   
2707 C CB  . THR A 347 ? 0.267 0.291 0.248 0.013  0.033  -0.006 347 THR A CB  
2708 O OG1 . THR A 347 ? 0.282 0.299 0.264 0.015  0.033  -0.011 347 THR A OG1 
2709 C CG2 . THR A 347 ? 0.272 0.299 0.254 0.015  0.031  -0.000 347 THR A CG2 
2710 N N   . ALA A 348 ? 0.288 0.330 0.275 0.010  0.036  -0.001 348 ALA A N   
2711 C CA  . ALA A 348 ? 0.291 0.354 0.280 0.012  0.039  0.002  348 ALA A CA  
2712 C C   . ALA A 348 ? 0.295 0.368 0.281 0.011  0.040  0.003  348 ALA A C   
2713 O O   . ALA A 348 ? 0.285 0.354 0.269 0.004  0.038  0.007  348 ALA A O   
2714 C CB  . ALA A 348 ? 0.290 0.366 0.284 0.003  0.036  0.010  348 ALA A CB  
2715 N N   . GLY A 349 ? 0.272 0.356 0.254 0.021  0.045  0.001  349 GLY A N   
2716 C CA  . GLY A 349 ? 0.286 0.380 0.263 0.020  0.047  0.002  349 GLY A CA  
2717 C C   . GLY A 349 ? 0.307 0.385 0.274 0.018  0.046  -0.004 349 GLY A C   
2718 O O   . GLY A 349 ? 0.362 0.448 0.324 0.016  0.047  -0.003 349 GLY A O   
2719 N N   . SER A 350 ? 0.278 0.336 0.241 0.016  0.043  -0.008 350 SER A N   
2720 C CA  . SER A 350 ? 0.290 0.340 0.244 0.009  0.040  -0.010 350 SER A CA  
2721 C C   . SER A 350 ? 0.311 0.339 0.244 0.009  0.039  -0.018 350 SER A C   
2722 O O   . SER A 350 ? 0.327 0.342 0.254 0.018  0.042  -0.022 350 SER A O   
2723 C CB  . SER A 350 ? 0.293 0.345 0.257 0.005  0.036  -0.004 350 SER A CB  
2724 O OG  . SER A 350 ? 0.288 0.329 0.252 0.005  0.034  -0.007 350 SER A OG  
2725 N N   . LEU A 351 ? 0.341 0.362 0.259 -0.003 0.035  -0.018 351 LEU A N   
2726 C CA  . LEU A 351 ? 0.382 0.373 0.272 -0.009 0.031  -0.025 351 LEU A CA  
2727 C C   . LEU A 351 ? 0.369 0.352 0.265 -0.010 0.028  -0.025 351 LEU A C   
2728 O O   . LEU A 351 ? 0.408 0.359 0.277 -0.014 0.026  -0.030 351 LEU A O   
2729 C CB  . LEU A 351 ? 0.409 0.405 0.285 -0.029 0.024  -0.020 351 LEU A CB  
2730 C CG  . LEU A 351 ? 0.469 0.464 0.329 -0.031 0.026  -0.022 351 LEU A CG  
2731 C CD1 . LEU A 351 ? 0.491 0.508 0.349 -0.051 0.018  -0.013 351 LEU A CD1 
2732 C CD2 . LEU A 351 ? 0.531 0.481 0.347 -0.026 0.029  -0.033 351 LEU A CD2 
2733 N N   . LEU A 352 ? 0.315 0.321 0.241 -0.007 0.029  -0.018 352 LEU A N   
2734 C CA  . LEU A 352 ? 0.308 0.310 0.241 -0.007 0.026  -0.018 352 LEU A CA  
2735 C C   . LEU A 352 ? 0.311 0.307 0.254 0.006  0.031  -0.021 352 LEU A C   
2736 O O   . LEU A 352 ? 0.309 0.305 0.261 0.007  0.029  -0.020 352 LEU A O   
2737 C CB  . LEU A 352 ? 0.285 0.312 0.237 -0.009 0.024  -0.007 352 LEU A CB  
2738 C CG  . LEU A 352 ? 0.297 0.341 0.243 -0.023 0.018  0.001  352 LEU A CG  
2739 C CD1 . LEU A 352 ? 0.312 0.363 0.248 -0.031 0.017  0.003  352 LEU A CD1 
2740 C CD2 . LEU A 352 ? 0.283 0.356 0.247 -0.018 0.018  0.013  352 LEU A CD2 
2741 N N   . GLU A 353 ? 0.298 0.296 0.239 0.016  0.037  -0.023 353 GLU A N   
2742 C CA  . GLU A 353 ? 0.301 0.303 0.251 0.027  0.041  -0.023 353 GLU A CA  
2743 C C   . GLU A 353 ? 0.321 0.300 0.258 0.032  0.040  -0.027 353 GLU A C   
2744 O O   . GLU A 353 ? 0.353 0.304 0.261 0.033  0.040  -0.033 353 GLU A O   
2745 C CB  . GLU A 353 ? 0.327 0.343 0.275 0.038  0.047  -0.021 353 GLU A CB  
2746 C CG  . GLU A 353 ? 0.336 0.372 0.296 0.048  0.051  -0.016 353 GLU A CG  
2747 C CD  . GLU A 353 ? 0.373 0.438 0.335 0.057  0.057  -0.009 353 GLU A CD  
2748 O OE1 . GLU A 353 ? 0.363 0.443 0.331 0.049  0.055  -0.006 353 GLU A OE1 
2749 O OE2 . GLU A 353 ? 0.462 0.538 0.419 0.075  0.063  -0.006 353 GLU A OE2 
2750 N N   A VAL A 354 ? 0.320 0.369 0.234 0.039  0.060  -0.018 354 VAL A N   
2751 N N   B VAL A 354 ? 0.325 0.373 0.239 0.039  0.060  -0.018 354 VAL A N   
2752 C CA  A VAL A 354 ? 0.321 0.362 0.245 0.037  0.055  -0.028 354 VAL A CA  
2753 C CA  B VAL A 354 ? 0.329 0.369 0.254 0.037  0.055  -0.027 354 VAL A CA  
2754 C C   A VAL A 354 ? 0.342 0.384 0.275 0.040  0.062  -0.032 354 VAL A C   
2755 C C   B VAL A 354 ? 0.346 0.387 0.280 0.039  0.062  -0.032 354 VAL A C   
2756 O O   A VAL A 354 ? 0.364 0.413 0.302 0.040  0.069  -0.026 354 VAL A O   
2757 O O   B VAL A 354 ? 0.364 0.411 0.305 0.039  0.068  -0.025 354 VAL A O   
2758 C CB  A VAL A 354 ? 0.302 0.334 0.237 0.035  0.049  -0.023 354 VAL A CB  
2759 C CB  B VAL A 354 ? 0.317 0.349 0.253 0.035  0.049  -0.023 354 VAL A CB  
2760 C CG1 A VAL A 354 ? 0.307 0.343 0.234 0.036  0.044  -0.018 354 VAL A CG1 
2761 C CG1 B VAL A 354 ? 0.317 0.340 0.262 0.034  0.045  -0.030 354 VAL A CG1 
2762 C CG2 A VAL A 354 ? 0.295 0.324 0.242 0.034  0.054  -0.016 354 VAL A CG2 
2763 C CG2 B VAL A 354 ? 0.324 0.359 0.251 0.035  0.044  -0.017 354 VAL A CG2 
2764 N N   . PRO A 355 ? 0.354 0.388 0.288 0.042  0.061  -0.042 355 PRO A N   
2765 C CA  . PRO A 355 ? 0.353 0.391 0.298 0.048  0.068  -0.045 355 PRO A CA  
2766 C C   . PRO A 355 ? 0.333 0.376 0.297 0.047  0.067  -0.038 355 PRO A C   
2767 O O   . PRO A 355 ? 0.330 0.366 0.301 0.043  0.060  -0.035 355 PRO A O   
2768 C CB  . PRO A 355 ? 0.387 0.408 0.326 0.051  0.066  -0.055 355 PRO A CB  
2769 C CG  . PRO A 355 ? 0.407 0.422 0.331 0.044  0.060  -0.060 355 PRO A CG  
2770 C CD  . PRO A 355 ? 0.386 0.409 0.313 0.039  0.055  -0.050 355 PRO A CD  
2771 N N   . SER A 356 ? 0.330 0.388 0.304 0.049  0.074  -0.036 356 SER A N   
2772 C CA  . SER A 356 ? 0.323 0.393 0.316 0.045  0.074  -0.031 356 SER A CA  
2773 C C   . SER A 356 ? 0.324 0.394 0.329 0.051  0.070  -0.034 356 SER A C   
2774 O O   . SER A 356 ? 0.306 0.386 0.326 0.047  0.067  -0.031 356 SER A O   
2775 C CB  . SER A 356 ? 0.350 0.441 0.350 0.043  0.084  -0.028 356 SER A CB  
2776 O OG  . SER A 356 ? 0.381 0.483 0.382 0.055  0.089  -0.034 356 SER A OG  
2777 N N   . ASP A 357 ? 0.322 0.380 0.318 0.060  0.069  -0.041 357 ASP A N   
2778 C CA  . ASP A 357 ? 0.311 0.365 0.316 0.069  0.066  -0.043 357 ASP A CA  
2779 C C   . ASP A 357 ? 0.302 0.334 0.301 0.065  0.057  -0.043 357 ASP A C   
2780 O O   . ASP A 357 ? 0.303 0.325 0.304 0.072  0.055  -0.044 357 ASP A O   
2781 C CB  . ASP A 357 ? 0.331 0.379 0.328 0.083  0.072  -0.050 357 ASP A CB  
2782 C CG  . ASP A 357 ? 0.393 0.417 0.367 0.082  0.074  -0.057 357 ASP A CG  
2783 O OD1 . ASP A 357 ? 0.415 0.432 0.381 0.071  0.070  -0.057 357 ASP A OD1 
2784 O OD2 . ASP A 357 ? 0.416 0.429 0.381 0.093  0.081  -0.064 357 ASP A OD2 
2785 N N   . LEU A 358 ? 0.284 0.309 0.276 0.054  0.053  -0.041 358 LEU A N   
2786 C CA  . LEU A 358 ? 0.291 0.299 0.277 0.050  0.046  -0.042 358 LEU A CA  
2787 C C   . LEU A 358 ? 0.282 0.293 0.279 0.046  0.040  -0.036 358 LEU A C   
2788 O O   . LEU A 358 ? 0.277 0.299 0.280 0.040  0.041  -0.031 358 LEU A O   
2789 C CB  . LEU A 358 ? 0.335 0.338 0.306 0.044  0.045  -0.044 358 LEU A CB  
2790 C CG  . LEU A 358 ? 0.367 0.356 0.332 0.039  0.038  -0.046 358 LEU A CG  
2791 C CD1 . LEU A 358 ? 0.433 0.411 0.381 0.037  0.040  -0.055 358 LEU A CD1 
2792 C CD2 . LEU A 358 ? 0.458 0.454 0.424 0.033  0.034  -0.040 358 LEU A CD2 
2793 N N   . VAL A 359 ? 0.268 0.268 0.265 0.047  0.035  -0.036 359 VAL A N   
2794 C CA  . VAL A 359 ? 0.256 0.256 0.261 0.042  0.029  -0.032 359 VAL A CA  
2795 C C   . VAL A 359 ? 0.264 0.250 0.258 0.037  0.025  -0.033 359 VAL A C   
2796 O O   . VAL A 359 ? 0.270 0.244 0.255 0.038  0.025  -0.038 359 VAL A O   
2797 C CB  . VAL A 359 ? 0.267 0.269 0.280 0.049  0.027  -0.031 359 VAL A CB  
2798 C CG1 . VAL A 359 ? 0.260 0.262 0.278 0.044  0.021  -0.027 359 VAL A CG1 
2799 C CG2 . VAL A 359 ? 0.275 0.299 0.300 0.054  0.031  -0.030 359 VAL A CG2 
2800 N N   . ARG A 360 ? 0.249 0.238 0.245 0.032  0.021  -0.029 360 ARG A N   
2801 C CA  . ARG A 360 ? 0.244 0.225 0.233 0.028  0.017  -0.029 360 ARG A CA  
2802 C C   . ARG A 360 ? 0.256 0.234 0.250 0.027  0.013  -0.026 360 ARG A C   
2803 O O   . ARG A 360 ? 0.250 0.234 0.252 0.026  0.012  -0.023 360 ARG A O   
2804 C CB  . ARG A 360 ? 0.252 0.240 0.236 0.025  0.017  -0.025 360 ARG A CB  
2805 C CG  . ARG A 360 ? 0.253 0.242 0.230 0.022  0.013  -0.026 360 ARG A CG  
2806 C CD  . ARG A 360 ? 0.254 0.252 0.227 0.023  0.013  -0.021 360 ARG A CD  
2807 N NE  . ARG A 360 ? 0.254 0.247 0.232 0.025  0.013  -0.015 360 ARG A NE  
2808 C CZ  . ARG A 360 ? 0.262 0.256 0.235 0.029  0.015  -0.008 360 ARG A CZ  
2809 N NH1 . ARG A 360 ? 0.257 0.261 0.221 0.033  0.016  -0.006 360 ARG A NH1 
2810 N NH2 . ARG A 360 ? 0.269 0.255 0.244 0.030  0.016  -0.005 360 ARG A NH2 
2811 N N   . LEU A 361 ? 0.254 0.224 0.245 0.025  0.010  -0.028 361 LEU A N   
2812 C CA  . LEU A 361 ? 0.260 0.226 0.253 0.024  0.006  -0.025 361 LEU A CA  
2813 C C   . LEU A 361 ? 0.256 0.224 0.244 0.019  0.004  -0.025 361 LEU A C   
2814 O O   . LEU A 361 ? 0.254 0.221 0.235 0.015  0.004  -0.028 361 LEU A O   
2815 C CB  . LEU A 361 ? 0.264 0.218 0.254 0.027  0.006  -0.026 361 LEU A CB  
2816 C CG  . LEU A 361 ? 0.285 0.238 0.279 0.036  0.009  -0.026 361 LEU A CG  
2817 C CD1 . LEU A 361 ? 0.325 0.261 0.312 0.041  0.010  -0.025 361 LEU A CD1 
2818 C CD2 . LEU A 361 ? 0.281 0.252 0.287 0.038  0.007  -0.023 361 LEU A CD2 
2819 N N   . SER A 362 ? 0.243 0.215 0.235 0.019  0.002  -0.021 362 SER A N   
2820 C CA  . SER A 362 ? 0.238 0.213 0.227 0.016  -0.001 -0.020 362 SER A CA  
2821 C C   . SER A 362 ? 0.230 0.198 0.220 0.016  -0.002 -0.019 362 SER A C   
2822 O O   . SER A 362 ? 0.248 0.216 0.242 0.018  -0.004 -0.017 362 SER A O   
2823 C CB  . SER A 362 ? 0.242 0.224 0.232 0.019  -0.000 -0.016 362 SER A CB  
2824 O OG  . SER A 362 ? 0.238 0.227 0.226 0.018  -0.002 -0.014 362 SER A OG  
2825 N N   . VAL A 363 ? 0.254 0.214 0.239 0.012  -0.002 -0.020 363 VAL A N   
2826 C CA  . VAL A 363 ? 0.246 0.197 0.229 0.012  -0.003 -0.018 363 VAL A CA  
2827 C C   . VAL A 363 ? 0.258 0.217 0.241 0.010  -0.004 -0.016 363 VAL A C   
2828 O O   . VAL A 363 ? 0.266 0.232 0.246 0.004  -0.004 -0.017 363 VAL A O   
2829 C CB  . VAL A 363 ? 0.270 0.203 0.244 0.009  0.001  -0.020 363 VAL A CB  
2830 C CG1 . VAL A 363 ? 0.282 0.204 0.252 0.011  0.001  -0.016 363 VAL A CG1 
2831 C CG2 . VAL A 363 ? 0.292 0.217 0.265 0.014  0.004  -0.023 363 VAL A CG2 
2832 N N   . GLY A 364 ? 0.259 0.219 0.245 0.013  -0.006 -0.013 364 GLY A N   
2833 C CA  . GLY A 364 ? 0.249 0.216 0.233 0.012  -0.007 -0.011 364 GLY A CA  
2834 C C   . GLY A 364 ? 0.263 0.225 0.242 0.009  -0.006 -0.008 364 GLY A C   
2835 O O   . GLY A 364 ? 0.275 0.225 0.249 0.005  -0.004 -0.008 364 GLY A O   
2836 N N   . ILE A 365 ? 0.249 0.217 0.226 0.009  -0.007 -0.006 365 ILE A N   
2837 C CA  . ILE A 365 ? 0.259 0.223 0.230 0.005  -0.005 -0.003 365 ILE A CA  
2838 C C   . ILE A 365 ? 0.266 0.224 0.232 0.010  -0.007 0.001  365 ILE A C   
2839 O O   . ILE A 365 ? 0.282 0.239 0.241 0.008  -0.006 0.005  365 ILE A O   
2840 C CB  . ILE A 365 ? 0.242 0.222 0.213 0.001  -0.004 -0.003 365 ILE A CB  
2841 C CG1 . ILE A 365 ? 0.234 0.223 0.206 0.008  -0.005 -0.003 365 ILE A CG1 
2842 C CG2 . ILE A 365 ? 0.248 0.240 0.224 -0.004 -0.003 -0.006 365 ILE A CG2 
2843 C CD1 . ILE A 365 ? 0.245 0.250 0.217 0.007  -0.002 -0.002 365 ILE A CD1 
2844 N N   . GLU A 366 ? 0.264 0.221 0.233 0.017  -0.010 -0.000 366 GLU A N   
2845 C CA  . GLU A 366 ? 0.268 0.225 0.234 0.022  -0.013 0.003  366 GLU A CA  
2846 C C   . GLU A 366 ? 0.288 0.229 0.245 0.024  -0.010 0.009  366 GLU A C   
2847 O O   . GLU A 366 ? 0.291 0.220 0.245 0.019  -0.006 0.009  366 GLU A O   
2848 C CB  . GLU A 366 ? 0.281 0.246 0.254 0.028  -0.016 0.001  366 GLU A CB  
2849 C CG  . GLU A 366 ? 0.262 0.236 0.240 0.025  -0.017 -0.005 366 GLU A CG  
2850 C CD  . GLU A 366 ? 0.255 0.228 0.240 0.023  -0.015 -0.008 366 GLU A CD  
2851 O OE1 . GLU A 366 ? 0.254 0.219 0.238 0.022  -0.013 -0.007 366 GLU A OE1 
2852 O OE2 . GLU A 366 ? 0.257 0.234 0.246 0.021  -0.015 -0.012 366 GLU A OE2 
2853 N N   . THR A 367 ? 0.291 0.232 0.240 0.030  -0.012 0.015  367 THR A N   
2854 C CA  . THR A 367 ? 0.314 0.236 0.252 0.035  -0.008 0.023  367 THR A CA  
2855 C C   . THR A 367 ? 0.321 0.231 0.261 0.041  -0.006 0.022  367 THR A C   
2856 O O   . THR A 367 ? 0.317 0.240 0.265 0.049  -0.010 0.020  367 THR A O   
2857 C CB  . THR A 367 ? 0.337 0.267 0.268 0.045  -0.012 0.029  367 THR A CB  
2858 O OG1 . THR A 367 ? 0.320 0.264 0.250 0.039  -0.014 0.027  367 THR A OG1 
2859 C CG2 . THR A 367 ? 0.373 0.279 0.287 0.050  -0.007 0.040  367 THR A CG2 
2860 N N   . VAL A 368 ? 0.331 0.216 0.261 0.037  0.000  0.023  368 VAL A N   
2861 C CA  . VAL A 368 ? 0.365 0.237 0.297 0.040  0.003  0.020  368 VAL A CA  
2862 C C   . VAL A 368 ? 0.366 0.238 0.297 0.058  0.002  0.025  368 VAL A C   
2863 O O   . VAL A 368 ? 0.355 0.235 0.296 0.063  0.001  0.020  368 VAL A O   
2864 C CB  . VAL A 368 ? 0.427 0.269 0.345 0.030  0.012  0.019  368 VAL A CB  
2865 C CG1 . VAL A 368 ? 0.489 0.304 0.389 0.034  0.018  0.028  368 VAL A CG1 
2866 C CG2 . VAL A 368 ? 0.496 0.328 0.415 0.031  0.015  0.012  368 VAL A CG2 
2867 N N   . ASP A 369 ? 0.388 0.255 0.309 0.068  0.002  0.034  369 ASP A N   
2868 C CA  . ASP A 369 ? 0.410 0.281 0.330 0.088  0.001  0.040  369 ASP A CA  
2869 C C   . ASP A 369 ? 0.355 0.265 0.295 0.090  -0.007 0.035  369 ASP A C   
2870 O O   . ASP A 369 ? 0.367 0.288 0.313 0.103  -0.008 0.035  369 ASP A O   
2871 C CB  . ASP A 369 ? 0.444 0.307 0.349 0.100  0.002  0.053  369 ASP A CB  
2872 C CG  . ASP A 369 ? 0.533 0.352 0.416 0.101  0.012  0.060  369 ASP A CG  
2873 O OD1 . ASP A 369 ? 0.573 0.365 0.451 0.095  0.019  0.055  369 ASP A OD1 
2874 O OD2 . ASP A 369 ? 0.625 0.435 0.493 0.110  0.014  0.071  369 ASP A OD2 
2875 N N   . ASP A 370 ? 0.343 0.275 0.291 0.080  -0.013 0.030  370 ASP A N   
2876 C CA  . ASP A 370 ? 0.313 0.277 0.277 0.079  -0.020 0.025  370 ASP A CA  
2877 C C   . ASP A 370 ? 0.305 0.270 0.279 0.075  -0.017 0.017  370 ASP A C   
2878 O O   . ASP A 370 ? 0.313 0.300 0.299 0.079  -0.020 0.015  370 ASP A O   
2879 C CB  . ASP A 370 ? 0.301 0.280 0.267 0.068  -0.024 0.020  370 ASP A CB  
2880 C CG  . ASP A 370 ? 0.325 0.309 0.280 0.072  -0.027 0.027  370 ASP A CG  
2881 O OD1 . ASP A 370 ? 0.360 0.348 0.309 0.087  -0.028 0.035  370 ASP A OD1 
2882 O OD2 . ASP A 370 ? 0.320 0.306 0.272 0.063  -0.028 0.024  370 ASP A OD2 
2883 N N   . LEU A 371 ? 0.310 0.255 0.281 0.065  -0.013 0.013  371 LEU A N   
2884 C CA  . LEU A 371 ? 0.302 0.247 0.281 0.061  -0.010 0.007  371 LEU A CA  
2885 C C   . LEU A 371 ? 0.321 0.256 0.298 0.073  -0.006 0.008  371 LEU A C   
2886 O O   . LEU A 371 ? 0.308 0.259 0.295 0.075  -0.006 0.005  371 LEU A O   
2887 C CB  . LEU A 371 ? 0.296 0.226 0.270 0.048  -0.007 0.003  371 LEU A CB  
2888 C CG  . LEU A 371 ? 0.286 0.228 0.263 0.039  -0.010 0.001  371 LEU A CG  
2889 C CD1 . LEU A 371 ? 0.288 0.220 0.261 0.029  -0.007 -0.002 371 LEU A CD1 
2890 C CD2 . LEU A 371 ? 0.272 0.233 0.260 0.038  -0.014 -0.003 371 LEU A CD2 
2891 N N   . VAL A 372 ? 0.314 0.250 0.278 0.033  -0.008 -0.004 372 VAL A N   
2892 C CA  . VAL A 372 ? 0.335 0.255 0.298 0.035  0.002  -0.009 372 VAL A CA  
2893 C C   . VAL A 372 ? 0.340 0.262 0.313 0.053  -0.004 0.001  372 VAL A C   
2894 O O   . VAL A 372 ? 0.341 0.271 0.325 0.056  -0.001 -0.003 372 VAL A O   
2895 C CB  . VAL A 372 ? 0.375 0.262 0.327 0.029  0.018  -0.014 372 VAL A CB  
2896 C CG1 . VAL A 372 ? 0.414 0.270 0.371 0.038  0.036  -0.016 372 VAL A CG1 
2897 C CG2 . VAL A 372 ? 0.381 0.278 0.326 0.005  0.025  -0.029 372 VAL A CG2 
2898 N N   . ASN A 373 ? 0.339 0.260 0.308 0.061  -0.012 0.012  373 ASN A N   
2899 C CA  . ASN A 373 ? 0.354 0.293 0.334 0.075  -0.021 0.023  373 ASN A CA  
2900 C C   . ASN A 373 ? 0.324 0.291 0.319 0.069  -0.028 0.016  373 ASN A C   
2901 O O   . ASN A 373 ? 0.322 0.309 0.334 0.077  -0.030 0.019  373 ASN A O   
2902 C CB  . ASN A 373 ? 0.379 0.326 0.346 0.079  -0.030 0.036  373 ASN A CB  
2903 C CG  . ASN A 373 ? 0.418 0.336 0.373 0.089  -0.021 0.053  373 ASN A CG  
2904 O OD1 . ASN A 373 ? 0.474 0.364 0.439 0.099  -0.005 0.056  373 ASN A OD1 
2905 N ND2 . ASN A 373 ? 0.446 0.366 0.379 0.085  -0.025 0.063  373 ASN A ND2 
2906 N N   . ASP A 374 ? 0.307 0.277 0.299 0.057  -0.031 0.009  374 ASP A N   
2907 C CA  . ASP A 374 ? 0.286 0.272 0.291 0.050  -0.033 0.006  374 ASP A CA  
2908 C C   . ASP A 374 ? 0.306 0.298 0.318 0.050  -0.026 0.005  374 ASP A C   
2909 O O   . ASP A 374 ? 0.291 0.300 0.316 0.050  -0.026 0.005  374 ASP A O   
2910 C CB  . ASP A 374 ? 0.289 0.266 0.293 0.043  -0.031 0.004  374 ASP A CB  
2911 C CG  . ASP A 374 ? 0.296 0.277 0.314 0.036  -0.027 0.004  374 ASP A CG  
2912 O OD1 . ASP A 374 ? 0.300 0.295 0.325 0.030  -0.030 -0.002 374 ASP A OD1 
2913 O OD2 . ASP A 374 ? 0.292 0.266 0.318 0.037  -0.021 0.012  374 ASP A OD2 
2914 N N   . LEU A 375 ? 0.311 0.295 0.313 0.047  -0.020 0.003  375 LEU A N   
2915 C CA  . LEU A 375 ? 0.331 0.327 0.333 0.041  -0.012 -0.003 375 LEU A CA  
2916 C C   . LEU A 375 ? 0.334 0.326 0.346 0.051  -0.002 -0.008 375 LEU A C   
2917 O O   . LEU A 375 ? 0.332 0.342 0.354 0.049  0.004  -0.012 375 LEU A O   
2918 C CB  . LEU A 375 ? 0.362 0.357 0.347 0.030  -0.006 -0.010 375 LEU A CB  
2919 C CG  . LEU A 375 ? 0.398 0.414 0.380 0.022  -0.015 0.000  375 LEU A CG  
2920 C CD1 . LEU A 375 ? 0.397 0.427 0.365 0.007  -0.012 -0.009 375 LEU A CD1 
2921 C CD2 . LEU A 375 ? 0.415 0.454 0.399 0.019  -0.016 0.012  375 LEU A CD2 
2922 N N   . LEU A 376 ? 0.354 0.325 0.368 0.063  0.001  -0.007 376 LEU A N   
2923 C CA  . LEU A 376 ? 0.369 0.336 0.403 0.080  0.014  -0.007 376 LEU A CA  
2924 C C   . LEU A 376 ? 0.348 0.353 0.407 0.089  0.004  0.002  376 LEU A C   
2925 O O   . LEU A 376 ? 0.342 0.361 0.423 0.096  0.017  -0.003 376 LEU A O   
2926 C CB  . LEU A 376 ? 0.411 0.346 0.445 0.095  0.022  0.003  376 LEU A CB  
2927 C CG  . LEU A 376 ? 0.439 0.332 0.453 0.082  0.040  -0.011 376 LEU A CG  
2928 C CD1 . LEU A 376 ? 0.466 0.321 0.478 0.096  0.049  0.005  376 LEU A CD1 
2929 C CD2 . LEU A 376 ? 0.462 0.344 0.479 0.073  0.066  -0.035 376 LEU A CD2 
2930 N N   . GLN A 377 ? 0.346 0.370 0.404 0.086  -0.014 0.010  377 GLN A N   
2931 C CA  . GLN A 377 ? 0.316 0.384 0.398 0.086  -0.023 0.013  377 GLN A CA  
2932 C C   . GLN A 377 ? 0.309 0.389 0.396 0.069  -0.016 0.003  377 GLN A C   
2933 O O   . GLN A 377 ? 0.298 0.411 0.409 0.070  -0.012 0.001  377 GLN A O   
2934 C CB  . GLN A 377 ? 0.333 0.422 0.409 0.080  -0.042 0.018  377 GLN A CB  
2935 C CG  . GLN A 377 ? 0.317 0.387 0.373 0.059  -0.044 0.009  377 GLN A CG  
2936 C CD  . GLN A 377 ? 0.323 0.405 0.389 0.041  -0.041 -0.000 377 GLN A CD  
2937 O OE1 . GLN A 377 ? 0.315 0.436 0.405 0.037  -0.041 -0.003 377 GLN A OE1 
2938 N NE2 . GLN A 377 ? 0.303 0.355 0.357 0.031  -0.034 -0.003 377 GLN A NE2 
2939 N N   . ALA A 378 ? 0.300 0.359 0.365 0.055  -0.014 -0.000 378 ALA A N   
2940 C CA  . ALA A 378 ? 0.298 0.367 0.364 0.040  -0.007 -0.001 378 ALA A CA  
2941 C C   . ALA A 378 ? 0.305 0.384 0.373 0.040  0.009  -0.009 378 ALA A C   
2942 O O   . ALA A 378 ? 0.305 0.404 0.379 0.029  0.017  -0.010 378 ALA A O   
2943 C CB  . ALA A 378 ? 0.305 0.353 0.350 0.030  -0.009 0.006  378 ALA A CB  
2944 N N   . LEU A 379 ? 0.311 0.373 0.371 0.049  0.018  -0.017 379 LEU A N   
2945 C CA  . LEU A 379 ? 0.335 0.399 0.392 0.045  0.040  -0.032 379 LEU A CA  
2946 C C   . LEU A 379 ? 0.348 0.429 0.443 0.062  0.053  -0.037 379 LEU A C   
2947 O O   . LEU A 379 ? 0.377 0.467 0.476 0.058  0.076  -0.052 379 LEU A O   
2948 C CB  . LEU A 379 ? 0.358 0.390 0.394 0.042  0.050  -0.044 379 LEU A CB  
2949 C CG  . LEU A 379 ? 0.347 0.381 0.350 0.021  0.041  -0.044 379 LEU A CG  
2950 C CD1 . LEU A 379 ? 0.375 0.381 0.364 0.017  0.050  -0.058 379 LEU A CD1 
2951 C CD2 . LEU A 379 ? 0.375 0.440 0.358 -0.000 0.048  -0.049 379 LEU A CD2 
2952 N N   . GLU A 380 ? 0.358 0.448 0.478 0.082  0.041  -0.023 380 GLU A N   
2953 C CA  . GLU A 380 ? 0.388 0.505 0.554 0.107  0.051  -0.020 380 GLU A CA  
2954 C C   . GLU A 380 ? 0.411 0.576 0.599 0.095  0.054  -0.025 380 GLU A C   
2955 O O   . GLU A 380 ? 0.435 0.620 0.617 0.077  0.038  -0.020 380 GLU A O   
2956 C CB  . GLU A 380 ? 0.402 0.531 0.585 0.128  0.030  0.002  380 GLU A CB  
2957 C CG  . GLU A 380 ? 0.469 0.620 0.700 0.163  0.041  0.015  380 GLU A CG  
2958 C CD  . GLU A 380 ? 0.535 0.631 0.771 0.182  0.074  0.010  380 GLU A CD  
2959 O OE1 . GLU A 380 ? 0.529 0.570 0.725 0.164  0.086  -0.008 380 GLU A OE1 
2960 O OE2 . GLU A 380 ? 0.600 0.709 0.883 0.215  0.089  0.023  380 GLU A OE2 
2961 N N   . PRO A 381 ? 0.445 0.626 0.658 0.100  0.081  -0.038 381 PRO A N   
2962 C CA  . PRO A 381 ? 0.473 0.699 0.701 0.083  0.090  -0.046 381 PRO A CA  
2963 C C   . PRO A 381 ? 0.447 0.737 0.726 0.092  0.078  -0.035 381 PRO A C   
2964 O O   . PRO A 381 ? 0.470 0.767 0.770 0.117  0.063  -0.020 381 PRO A O   
2965 C CB  . PRO A 381 ? 0.498 0.718 0.735 0.087  0.128  -0.068 381 PRO A CB  
2966 C CG  . PRO A 381 ? 0.511 0.694 0.765 0.119  0.139  -0.067 381 PRO A CG  
2967 C CD  . PRO A 381 ? 0.465 0.613 0.686 0.118  0.111  -0.051 381 PRO A CD  
# 
