data_9LPD
# 
_entry.id   9LPD 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9LPD         pdb_00009lpd 10.2210/pdb9lpd/pdb 
WWPDB D_1300055588 ?            ?                   
# 
_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       2025-05-07 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9LPD 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              zhuihao@mail.sysu.edu.cn 
_pdbx_contact_author.name_first         Zhou 
_pdbx_contact_author.name_last          Huihao 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9675-5007 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Peng, X.' 1 ? 
'Chen, B.' 2 ? 
'Xia, K.'  3 ? 
'Zhou, H.' 4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;The lineage-specific tRNA recognition mechanism of bacterial trptophanyl-tRNA synthetase and its implications for inhibitor discover
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Peng, X.'  1 ? 
primary 'Xia, K.'   2 ? 
primary 'Huang, Q.' 3 ? 
primary 'Xiang, M.' 4 ? 
primary 'Han, L.'   5 ? 
primary 'Qiu, H.'   6 ? 
primary 'Gu, Q.'    7 ? 
primary 'Chen, B.'  8 ? 
primary 'Zhou, H.'  9 ? 
# 
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 'Tryptophan--tRNA ligase' 38373.738 2   6.1.1.2 ? ? ? 
2 non-polymer syn Tirabrutinib              454.481   1   ?       ? ? ? 
3 non-polymer syn 'SULFATE ION'             96.063    3   ?       ? ? ? 
4 non-polymer syn CHLORZOXAZONE             169.565   1   ?       ? ? ? 
5 non-polymer syn "TRYPTOPHANYL-5'AMP"      533.431   1   ?       ? ? ? 
6 water       nat water                     18.015    179 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Tryptophanyl-tRNA synthetase,TrpRS' 
# 
_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       
;MTKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIF
VQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDI
AQRFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNK
AGVSNLLDILSAVTGQSIPELEKQFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKASAHASRT
LKAVYEAIGFVAKRHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIF
VQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDI
AQRFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNK
AGVSNLLDILSAVTGQSIPELEKQFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKASAHASRT
LKAVYEAIGFVAKRHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 Tirabrutinib         A1EK0 
3 'SULFATE ION'        SO4   
4 CHLORZOXAZONE        CLW   
5 "TRYPTOPHANYL-5'AMP" TYM   
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   THR n 
1 3   LYS n 
1 4   PRO n 
1 5   ILE n 
1 6   VAL n 
1 7   PHE n 
1 8   SER n 
1 9   GLY n 
1 10  ALA n 
1 11  GLN n 
1 12  PRO n 
1 13  SER n 
1 14  GLY n 
1 15  GLU n 
1 16  LEU n 
1 17  THR n 
1 18  ILE n 
1 19  GLY n 
1 20  ASN n 
1 21  TYR n 
1 22  MET n 
1 23  GLY n 
1 24  ALA n 
1 25  LEU n 
1 26  ARG n 
1 27  GLN n 
1 28  TRP n 
1 29  VAL n 
1 30  ASN n 
1 31  MET n 
1 32  GLN n 
1 33  ASP n 
1 34  ASP n 
1 35  TYR n 
1 36  HIS n 
1 37  CYS n 
1 38  ILE n 
1 39  TYR n 
1 40  CYS n 
1 41  ILE n 
1 42  VAL n 
1 43  ASP n 
1 44  GLN n 
1 45  HIS n 
1 46  ALA n 
1 47  ILE n 
1 48  THR n 
1 49  VAL n 
1 50  ARG n 
1 51  GLN n 
1 52  ASP n 
1 53  ALA n 
1 54  GLN n 
1 55  LYS n 
1 56  LEU n 
1 57  ARG n 
1 58  LYS n 
1 59  ALA n 
1 60  THR n 
1 61  LEU n 
1 62  ASP n 
1 63  THR n 
1 64  LEU n 
1 65  ALA n 
1 66  LEU n 
1 67  TYR n 
1 68  LEU n 
1 69  ALA n 
1 70  CYS n 
1 71  GLY n 
1 72  ILE n 
1 73  ASP n 
1 74  PRO n 
1 75  GLU n 
1 76  LYS n 
1 77  SER n 
1 78  THR n 
1 79  ILE n 
1 80  PHE n 
1 81  VAL n 
1 82  GLN n 
1 83  SER n 
1 84  HIS n 
1 85  VAL n 
1 86  PRO n 
1 87  GLU n 
1 88  HIS n 
1 89  ALA n 
1 90  GLN n 
1 91  LEU n 
1 92  GLY n 
1 93  TRP n 
1 94  ALA n 
1 95  LEU n 
1 96  ASN n 
1 97  CYS n 
1 98  TYR n 
1 99  THR n 
1 100 TYR n 
1 101 PHE n 
1 102 GLY n 
1 103 GLU n 
1 104 LEU n 
1 105 SER n 
1 106 ARG n 
1 107 MET n 
1 108 THR n 
1 109 GLN n 
1 110 PHE n 
1 111 LYS n 
1 112 ASP n 
1 113 LYS n 
1 114 SER n 
1 115 ALA n 
1 116 ARG n 
1 117 TYR n 
1 118 ALA n 
1 119 GLU n 
1 120 ASN n 
1 121 ILE n 
1 122 ASN n 
1 123 ALA n 
1 124 GLY n 
1 125 LEU n 
1 126 PHE n 
1 127 ASP n 
1 128 TYR n 
1 129 PRO n 
1 130 VAL n 
1 131 LEU n 
1 132 MET n 
1 133 ALA n 
1 134 ALA n 
1 135 ASP n 
1 136 ILE n 
1 137 LEU n 
1 138 LEU n 
1 139 TYR n 
1 140 GLN n 
1 141 THR n 
1 142 ASN n 
1 143 LEU n 
1 144 VAL n 
1 145 PRO n 
1 146 VAL n 
1 147 GLY n 
1 148 GLU n 
1 149 ASP n 
1 150 GLN n 
1 151 LYS n 
1 152 GLN n 
1 153 HIS n 
1 154 LEU n 
1 155 GLU n 
1 156 LEU n 
1 157 SER n 
1 158 ARG n 
1 159 ASP n 
1 160 ILE n 
1 161 ALA n 
1 162 GLN n 
1 163 ARG n 
1 164 PHE n 
1 165 ASN n 
1 166 ALA n 
1 167 LEU n 
1 168 TYR n 
1 169 GLY n 
1 170 GLU n 
1 171 ILE n 
1 172 PHE n 
1 173 LYS n 
1 174 VAL n 
1 175 PRO n 
1 176 GLU n 
1 177 PRO n 
1 178 PHE n 
1 179 ILE n 
1 180 PRO n 
1 181 LYS n 
1 182 SER n 
1 183 GLY n 
1 184 ALA n 
1 185 ARG n 
1 186 VAL n 
1 187 MET n 
1 188 SER n 
1 189 LEU n 
1 190 LEU n 
1 191 GLU n 
1 192 PRO n 
1 193 THR n 
1 194 LYS n 
1 195 LYS n 
1 196 MET n 
1 197 SER n 
1 198 LYS n 
1 199 SER n 
1 200 ASP n 
1 201 ASP n 
1 202 ASN n 
1 203 ARG n 
1 204 ASN n 
1 205 ASN n 
1 206 VAL n 
1 207 ILE n 
1 208 GLY n 
1 209 LEU n 
1 210 LEU n 
1 211 GLU n 
1 212 ASP n 
1 213 PRO n 
1 214 LYS n 
1 215 SER n 
1 216 VAL n 
1 217 VAL n 
1 218 LYS n 
1 219 LYS n 
1 220 ILE n 
1 221 LYS n 
1 222 ARG n 
1 223 ALA n 
1 224 VAL n 
1 225 THR n 
1 226 ASP n 
1 227 SER n 
1 228 ASP n 
1 229 GLU n 
1 230 PRO n 
1 231 PRO n 
1 232 VAL n 
1 233 VAL n 
1 234 ARG n 
1 235 TYR n 
1 236 ASP n 
1 237 VAL n 
1 238 GLN n 
1 239 ASN n 
1 240 LYS n 
1 241 ALA n 
1 242 GLY n 
1 243 VAL n 
1 244 SER n 
1 245 ASN n 
1 246 LEU n 
1 247 LEU n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 SER n 
1 252 ALA n 
1 253 VAL n 
1 254 THR n 
1 255 GLY n 
1 256 GLN n 
1 257 SER n 
1 258 ILE n 
1 259 PRO n 
1 260 GLU n 
1 261 LEU n 
1 262 GLU n 
1 263 LYS n 
1 264 GLN n 
1 265 PHE n 
1 266 GLU n 
1 267 GLY n 
1 268 LYS n 
1 269 MET n 
1 270 TYR n 
1 271 GLY n 
1 272 HIS n 
1 273 LEU n 
1 274 LYS n 
1 275 GLY n 
1 276 GLU n 
1 277 VAL n 
1 278 ALA n 
1 279 ASP n 
1 280 ALA n 
1 281 VAL n 
1 282 SER n 
1 283 GLY n 
1 284 MET n 
1 285 LEU n 
1 286 THR n 
1 287 GLU n 
1 288 LEU n 
1 289 GLN n 
1 290 GLU n 
1 291 ARG n 
1 292 TYR n 
1 293 HIS n 
1 294 ARG n 
1 295 PHE n 
1 296 ARG n 
1 297 ASN n 
1 298 ASP n 
1 299 GLU n 
1 300 ALA n 
1 301 PHE n 
1 302 LEU n 
1 303 GLN n 
1 304 GLN n 
1 305 VAL n 
1 306 MET n 
1 307 LYS n 
1 308 ASP n 
1 309 GLY n 
1 310 ALA n 
1 311 GLU n 
1 312 LYS n 
1 313 ALA n 
1 314 SER n 
1 315 ALA n 
1 316 HIS n 
1 317 ALA n 
1 318 SER n 
1 319 ARG n 
1 320 THR n 
1 321 LEU n 
1 322 LYS n 
1 323 ALA n 
1 324 VAL n 
1 325 TYR n 
1 326 GLU n 
1 327 ALA n 
1 328 ILE n 
1 329 GLY n 
1 330 PHE n 
1 331 VAL n 
1 332 ALA n 
1 333 LYS n 
1 334 ARG n 
1 335 HIS n 
1 336 HIS n 
1 337 HIS n 
1 338 HIS n 
1 339 HIS n 
1 340 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                   340 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 
;trpS, ACU57_16550, B6R15_000448, B6R31_002275, BANRA_02015, BCB93_002501, BGM66_002290, BGZ_04191, BK383_21195, BKL28_001915, BMT91_03555, BvCmsNSP007_00090, BXT93_04920, C0P57_000786, C2R31_002885, C3F40_19370, CG704_07870, CIG67_21025, CTR35_001866, D9D43_04205, DD762_12005, DL968_00250, DNQ45_04190, DTL43_13995, DU321_12325, E4K51_10330, E6D34_04225, EIA08_11870, EPS97_04620, F7F11_12075, F7N46_14665, F9413_17445, F9461_03030, F9B07_12605, FGAF848_25410, FKO60_13960, FOI11_018845, FOI11_04335, FPS11_03390, FZU14_04195, G3V95_06005, G4A38_16925, G4A47_18515, G5603_11025, GAI89_06310, GNW61_08470, GOP25_12480, GP944_08250, GQE86_01825, GQN24_10725, HEP34_002452, HI055_002233, HJQ60_002846, HL563_11055, HL601_09110, HLX92_09755, HLZ50_06610, HMV95_07850, HVW04_17215, HVW43_18350, HVY77_01760, I6H00_19775, IH772_08800, J0541_002134, JNP96_25720, NCTC10764_03793, NCTC10974_00460, NCTC9044_01447, NCTC9073_00479, NCTC9077_00527, NCTC9706_02656, P6223_000209, Q2V20_09290, QDW62_01780, QO046_14075, R8G00_13645, SAMEA3472044_01080, SAMEA3472056_01981, SAMEA3752557_02035
;
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1EK0 non-polymer         . Tirabrutinib         'Btk Kinase inhibitor'   'C25 H22 N6 O3'   454.481 
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 
CLW   non-polymer         . CHLORZOXAZONE        5-CHLORO-2-BENZOXAZOLONE 'C7 H4 Cl N O2'   169.565 
CYS   'L-peptide linking' y CYSTEINE             ?                        'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE            ?                        'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'      ?                        'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE              ?                        'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE            ?                        'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                ?                        'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE           ?                        'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE              ?                        'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE               ?                        'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE           ?                        'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE        ?                        'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE              ?                        'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE               ?                        'C3 H7 N O3'      105.093 
SO4   non-polymer         . 'SULFATE ION'        ?                        'O4 S -2'         96.063  
THR   'L-peptide linking' y THREONINE            ?                        'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN           ?                        'C11 H12 N2 O2'   204.225 
TYM   non-polymer         . "TRYPTOPHANYL-5'AMP" ?                        'C21 H24 N7 O8 P' 533.431 
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   THR 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  MET 22  22  22  MET MET A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  ARG 26  26  26  ARG ARG A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  TRP 28  28  28  TRP TRP A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  MET 31  31  31  MET MET A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  TYR 35  35  35  TYR TYR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  CYS 37  37  37  CYS CYS A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  CYS 40  40  40  CYS CYS A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  GLN 44  44  44  GLN GLN A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  ARG 57  57  57  ARG ARG A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  LEU 64  64  64  LEU LEU 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  TYR 67  67  67  TYR TYR A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  CYS 70  70  70  CYS CYS A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  THR 78  78  78  THR THR A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  HIS 84  84  84  HIS HIS A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  GLN 90  90  90  GLN GLN A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  TRP 93  93  93  TRP TRP A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  CYS 97  97  97  CYS CYS A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 PHE 101 101 101 PHE PHE A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 ARG 106 106 106 ARG ARG A . n 
A 1 107 MET 107 107 107 MET MET A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 GLN 109 109 ?   ?   ?   A . n 
A 1 110 PHE 110 110 ?   ?   ?   A . n 
A 1 111 LYS 111 111 ?   ?   ?   A . n 
A 1 112 ASP 112 112 ?   ?   ?   A . n 
A 1 113 LYS 113 113 ?   ?   ?   A . n 
A 1 114 SER 114 114 ?   ?   ?   A . n 
A 1 115 ALA 115 115 ?   ?   ?   A . n 
A 1 116 ARG 116 116 ?   ?   ?   A . n 
A 1 117 TYR 117 117 117 TYR ALA A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 TYR 128 128 128 TYR TYR A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 MET 132 132 132 MET MET A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 GLN 140 140 140 GLN GLN A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 HIS 153 153 153 HIS HIS A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 GLN 162 162 162 GLN GLN A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 PHE 164 164 164 PHE PHE A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLU 170 170 170 GLU GLU A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 PHE 172 172 172 PHE PHE A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLU 176 176 176 GLU GLU A . n 
A 1 177 PRO 177 177 177 PRO PRO A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 LYS 181 181 181 LYS LYS A . n 
A 1 182 SER 182 182 ?   ?   ?   A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 MET 187 187 187 MET MET 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 LEU 190 190 190 LEU LEU A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 MET 196 196 196 MET MET A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 ASP 201 201 ?   ?   ?   A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 ARG 203 203 203 ARG ARG A . n 
A 1 204 ASN 204 204 204 ASN ASN A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 PRO 213 213 213 PRO PRO A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 LYS 219 219 219 LYS LYS A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 SER 227 227 227 SER SER A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 PRO 231 231 231 PRO PRO A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ARG 234 234 234 ARG ARG A . n 
A 1 235 TYR 235 235 235 TYR TYR A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 GLN 238 238 238 GLN GLN A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 PRO 259 259 259 PRO PRO A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 LYS 263 263 263 LYS LYS A . n 
A 1 264 GLN 264 264 264 GLN GLN A . n 
A 1 265 PHE 265 265 265 PHE PHE A . n 
A 1 266 GLU 266 266 266 GLU GLU A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 LYS 268 268 268 LYS LYS A . n 
A 1 269 MET 269 269 269 MET MET A . n 
A 1 270 TYR 270 270 270 TYR TYR A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 HIS 272 272 272 HIS HIS A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 GLY 275 275 275 GLY GLY 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 ALA 278 278 278 ALA ALA A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 MET 284 284 284 MET MET A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 THR 286 286 286 THR THR A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 GLN 289 289 289 GLN GLN A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 ARG 291 291 291 ARG ARG A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 HIS 293 293 293 HIS HIS A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 PHE 295 295 295 PHE PHE A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 ASN 297 297 297 ASN ASN A . n 
A 1 298 ASP 298 298 298 ASP ASP A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 PHE 301 301 301 PHE PHE A . n 
A 1 302 LEU 302 302 302 LEU LEU A . n 
A 1 303 GLN 303 303 303 GLN GLN A . n 
A 1 304 GLN 304 304 304 GLN GLN A . n 
A 1 305 VAL 305 305 305 VAL VAL A . n 
A 1 306 MET 306 306 306 MET MET A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 ASP 308 308 308 ASP ASP A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 SER 314 314 314 SER SER A . n 
A 1 315 ALA 315 315 315 ALA ALA A . n 
A 1 316 HIS 316 316 316 HIS HIS A . n 
A 1 317 ALA 317 317 317 ALA ALA A . n 
A 1 318 SER 318 318 318 SER SER A . n 
A 1 319 ARG 319 319 319 ARG ARG A . n 
A 1 320 THR 320 320 320 THR THR A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 LYS 322 322 322 LYS LYS A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 TYR 325 325 325 TYR TYR A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 ALA 327 327 327 ALA ALA A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 GLY 329 329 329 GLY GLY A . n 
A 1 330 PHE 330 330 330 PHE PHE A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 ALA 332 332 332 ALA ALA A . n 
A 1 333 LYS 333 333 333 LYS LYS A . n 
A 1 334 ARG 334 334 334 ARG ARG A . n 
A 1 335 HIS 335 335 335 HIS HIS A . n 
A 1 336 HIS 336 336 ?   ?   ?   A . n 
A 1 337 HIS 337 337 ?   ?   ?   A . n 
A 1 338 HIS 338 338 ?   ?   ?   A . n 
A 1 339 HIS 339 339 ?   ?   ?   A . n 
A 1 340 HIS 340 340 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   PRO 4   4   4   PRO PRO B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  ALA 10  10  10  ALA ALA B . n 
B 1 11  GLN 11  11  11  GLN GLN B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  SER 13  13  13  SER SER B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  THR 17  17  17  THR THR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  GLY 19  19  19  GLY GLY B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  MET 22  22  22  MET MET B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  ALA 24  24  24  ALA ALA B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  ARG 26  26  26  ARG ARG B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  TRP 28  28  28  TRP TRP B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  ASN 30  30  30  ASN ASN B . n 
B 1 31  MET 31  31  31  MET MET B . n 
B 1 32  GLN 32  32  32  GLN GLN B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  TYR 35  35  35  TYR TYR B . n 
B 1 36  HIS 36  36  36  HIS HIS B . n 
B 1 37  CYS 37  37  37  CYS CYS B . n 
B 1 38  ILE 38  38  38  ILE ILE B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  CYS 40  40  40  CYS CYS B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ASP 43  43  43  ASP ASP B . n 
B 1 44  GLN 44  44  44  GLN GLN B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  ALA 46  46  46  ALA ALA B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  THR 48  48  48  THR THR B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  GLN 51  51  51  GLN GLN B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ALA 53  53  53  ALA ALA B . n 
B 1 54  GLN 54  54  54  GLN GLN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  ARG 57  57  57  ARG ARG B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  LEU 64  64  64  LEU LEU B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  TYR 67  67  67  TYR TYR B . n 
B 1 68  LEU 68  68  68  LEU LEU B . n 
B 1 69  ALA 69  69  69  ALA ALA B . n 
B 1 70  CYS 70  70  70  CYS CYS B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  ASP 73  73  73  ASP ASP B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  SER 77  77  77  SER SER B . n 
B 1 78  THR 78  78  78  THR THR B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  PHE 80  80  80  PHE PHE B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  HIS 84  84  84  HIS HIS B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  PRO 86  86  86  PRO PRO B . n 
B 1 87  GLU 87  87  87  GLU GLU B . n 
B 1 88  HIS 88  88  88  HIS HIS B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  GLN 90  90  90  GLN GLN B . n 
B 1 91  LEU 91  91  91  LEU LEU B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  TRP 93  93  93  TRP TRP B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  CYS 97  97  97  CYS CYS B . n 
B 1 98  TYR 98  98  98  TYR TYR B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 TYR 100 100 100 TYR TYR B . n 
B 1 101 PHE 101 101 101 PHE PHE B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 GLU 103 103 103 GLU GLU B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 ARG 106 106 106 ARG ARG B . n 
B 1 107 MET 107 107 107 MET MET B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 GLN 109 109 109 GLN GLN B . n 
B 1 110 PHE 110 110 110 PHE PHE B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 ASP 112 112 112 ASP ASP B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 SER 114 114 114 SER SER B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 TYR 117 117 117 TYR TYR B . n 
B 1 118 ALA 118 118 118 ALA ALA B . n 
B 1 119 GLU 119 119 119 GLU GLU B . n 
B 1 120 ASN 120 120 120 ASN ASN B . n 
B 1 121 ILE 121 121 121 ILE ILE B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 PHE 126 126 126 PHE PHE B . n 
B 1 127 ASP 127 127 127 ASP ASP B . n 
B 1 128 TYR 128 128 128 TYR TYR B . n 
B 1 129 PRO 129 129 129 PRO PRO B . n 
B 1 130 VAL 130 130 130 VAL VAL B . n 
B 1 131 LEU 131 131 131 LEU LEU B . n 
B 1 132 MET 132 132 132 MET MET B . n 
B 1 133 ALA 133 133 133 ALA ALA B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 TYR 139 139 139 TYR TYR B . n 
B 1 140 GLN 140 140 140 GLN GLN B . n 
B 1 141 THR 141 141 141 THR THR B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 PRO 145 145 145 PRO PRO B . n 
B 1 146 VAL 146 146 146 VAL VAL B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 ASP 149 149 149 ASP ASP B . n 
B 1 150 GLN 150 150 150 GLN GLN B . n 
B 1 151 LYS 151 151 151 LYS LYS B . n 
B 1 152 GLN 152 152 152 GLN GLN B . n 
B 1 153 HIS 153 153 153 HIS HIS B . n 
B 1 154 LEU 154 154 154 LEU LEU B . n 
B 1 155 GLU 155 155 155 GLU GLU B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 ARG 158 158 158 ARG ARG B . n 
B 1 159 ASP 159 159 159 ASP ASP B . n 
B 1 160 ILE 160 160 160 ILE ILE B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 GLN 162 162 162 GLN GLN B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 PHE 164 164 164 PHE PHE B . n 
B 1 165 ASN 165 165 165 ASN ASN B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 TYR 168 168 168 TYR TYR B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLU 170 170 170 GLU GLU B . n 
B 1 171 ILE 171 171 171 ILE ILE B . n 
B 1 172 PHE 172 172 172 PHE PHE B . n 
B 1 173 LYS 173 173 173 LYS LYS B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLU 176 176 176 GLU GLU B . n 
B 1 177 PRO 177 177 177 PRO PRO B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 PRO 180 180 180 PRO PRO B . n 
B 1 181 LYS 181 181 181 LYS LYS B . n 
B 1 182 SER 182 182 182 SER SER B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 ARG 185 185 185 ARG ARG B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 MET 187 187 187 MET MET B . n 
B 1 188 SER 188 188 188 SER SER B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 LEU 190 190 190 LEU LEU B . n 
B 1 191 GLU 191 191 191 GLU GLU B . n 
B 1 192 PRO 192 192 192 PRO PRO B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 LYS 195 195 195 LYS LYS B . n 
B 1 196 MET 196 196 196 MET MET B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 LYS 198 198 198 LYS LYS B . n 
B 1 199 SER 199 199 199 SER SER B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 ASP 201 201 201 ASP ASP B . n 
B 1 202 ASN 202 202 202 ASN ASN B . n 
B 1 203 ARG 203 203 203 ARG ARG B . n 
B 1 204 ASN 204 204 204 ASN ASN B . n 
B 1 205 ASN 205 205 205 ASN ASN B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 ILE 207 207 207 ILE ILE B . n 
B 1 208 GLY 208 208 208 GLY GLY B . n 
B 1 209 LEU 209 209 209 LEU LEU B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 GLU 211 211 211 GLU GLU B . n 
B 1 212 ASP 212 212 212 ASP ASP B . n 
B 1 213 PRO 213 213 213 PRO PRO B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 LYS 219 219 219 LYS LYS B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 SER 227 227 227 SER SER B . n 
B 1 228 ASP 228 228 228 ASP ASP B . n 
B 1 229 GLU 229 229 229 GLU GLU B . n 
B 1 230 PRO 230 230 230 PRO PRO B . n 
B 1 231 PRO 231 231 231 PRO PRO B . n 
B 1 232 VAL 232 232 232 VAL VAL B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ARG 234 234 234 ARG ARG B . n 
B 1 235 TYR 235 235 235 TYR TYR B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 VAL 237 237 237 VAL VAL B . n 
B 1 238 GLN 238 238 238 GLN GLN B . n 
B 1 239 ASN 239 239 239 ASN ASN B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 GLY 242 242 242 GLY GLY B . n 
B 1 243 VAL 243 243 243 VAL VAL B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 LEU 246 246 246 LEU LEU B . n 
B 1 247 LEU 247 247 247 LEU LEU B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 SER 251 251 251 SER SER B . n 
B 1 252 ALA 252 252 252 ALA ALA B . n 
B 1 253 VAL 253 253 253 VAL VAL B . n 
B 1 254 THR 254 254 254 THR THR B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 SER 257 257 257 SER SER B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 PRO 259 259 259 PRO PRO B . n 
B 1 260 GLU 260 260 260 GLU GLU B . n 
B 1 261 LEU 261 261 261 LEU LEU B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 LYS 263 263 263 LYS LYS B . n 
B 1 264 GLN 264 264 264 GLN GLN B . n 
B 1 265 PHE 265 265 265 PHE PHE B . n 
B 1 266 GLU 266 266 266 GLU GLU B . n 
B 1 267 GLY 267 267 267 GLY GLY B . n 
B 1 268 LYS 268 268 268 LYS LYS B . n 
B 1 269 MET 269 269 269 MET MET B . n 
B 1 270 TYR 270 270 270 TYR TYR B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 HIS 272 272 272 HIS HIS B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 LYS 274 274 274 LYS LYS B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 GLU 276 276 276 GLU GLU B . n 
B 1 277 VAL 277 277 277 VAL VAL B . n 
B 1 278 ALA 278 278 278 ALA ALA B . n 
B 1 279 ASP 279 279 279 ASP ASP B . n 
B 1 280 ALA 280 280 280 ALA ALA B . n 
B 1 281 VAL 281 281 281 VAL VAL B . n 
B 1 282 SER 282 282 282 SER SER B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 MET 284 284 284 MET MET B . n 
B 1 285 LEU 285 285 285 LEU LEU B . n 
B 1 286 THR 286 286 286 THR THR B . n 
B 1 287 GLU 287 287 287 GLU GLU B . n 
B 1 288 LEU 288 288 288 LEU LEU B . n 
B 1 289 GLN 289 289 289 GLN GLN B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 ARG 291 291 291 ARG ARG B . n 
B 1 292 TYR 292 292 292 TYR TYR B . n 
B 1 293 HIS 293 293 293 HIS HIS B . n 
B 1 294 ARG 294 294 294 ARG ARG B . n 
B 1 295 PHE 295 295 295 PHE PHE B . n 
B 1 296 ARG 296 296 296 ARG ARG B . n 
B 1 297 ASN 297 297 297 ASN ASN B . n 
B 1 298 ASP 298 298 298 ASP ASP B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 ALA 300 300 300 ALA ALA B . n 
B 1 301 PHE 301 301 301 PHE PHE B . n 
B 1 302 LEU 302 302 302 LEU LEU B . n 
B 1 303 GLN 303 303 303 GLN GLN B . n 
B 1 304 GLN 304 304 304 GLN GLN B . n 
B 1 305 VAL 305 305 305 VAL VAL B . n 
B 1 306 MET 306 306 306 MET MET B . n 
B 1 307 LYS 307 307 307 LYS LYS B . n 
B 1 308 ASP 308 308 308 ASP ASP B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 ALA 310 310 310 ALA ALA B . n 
B 1 311 GLU 311 311 311 GLU GLU B . n 
B 1 312 LYS 312 312 312 LYS LYS B . n 
B 1 313 ALA 313 313 313 ALA ALA B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 ALA 315 315 315 ALA ALA B . n 
B 1 316 HIS 316 316 316 HIS HIS B . n 
B 1 317 ALA 317 317 317 ALA ALA B . n 
B 1 318 SER 318 318 318 SER SER B . n 
B 1 319 ARG 319 319 319 ARG ARG B . n 
B 1 320 THR 320 320 320 THR THR B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 LYS 322 322 322 LYS LYS B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 VAL 324 324 324 VAL VAL B . n 
B 1 325 TYR 325 325 325 TYR TYR B . n 
B 1 326 GLU 326 326 326 GLU GLU B . n 
B 1 327 ALA 327 327 327 ALA ALA B . n 
B 1 328 ILE 328 328 328 ILE ILE B . n 
B 1 329 GLY 329 329 329 GLY GLY B . n 
B 1 330 PHE 330 330 330 PHE PHE B . n 
B 1 331 VAL 331 331 331 VAL VAL B . n 
B 1 332 ALA 332 332 332 ALA ALA B . n 
B 1 333 LYS 333 333 333 LYS LYS B . n 
B 1 334 ARG 334 334 334 ARG ARG B . n 
B 1 335 HIS 335 335 ?   ?   ?   B . n 
B 1 336 HIS 336 336 ?   ?   ?   B . n 
B 1 337 HIS 337 337 ?   ?   ?   B . n 
B 1 338 HIS 338 338 ?   ?   ?   B . n 
B 1 339 HIS 339 339 ?   ?   ?   B . n 
B 1 340 HIS 340 340 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EK0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EK0 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1EK0 1  401 401 A1EK0 TRB A . 
D 3 SO4   1  402 1   SO4   SO4 A . 
E 3 SO4   1  403 2   SO4   SO4 A . 
F 4 CLW   1  401 402 CLW   Chl B . 
G 5 TYM   1  402 403 TYM   LIG B . 
H 3 SO4   1  403 3   SO4   SO4 B . 
I 6 HOH   1  501 36  HOH   HOH A . 
I 6 HOH   2  502 70  HOH   HOH A . 
I 6 HOH   3  503 3   HOH   HOH A . 
I 6 HOH   4  504 41  HOH   HOH A . 
I 6 HOH   5  505 91  HOH   HOH A . 
I 6 HOH   6  506 127 HOH   HOH A . 
I 6 HOH   7  507 89  HOH   HOH A . 
I 6 HOH   8  508 92  HOH   HOH A . 
I 6 HOH   9  509 145 HOH   HOH A . 
I 6 HOH   10 510 166 HOH   HOH A . 
I 6 HOH   11 511 32  HOH   HOH A . 
I 6 HOH   12 512 120 HOH   HOH A . 
I 6 HOH   13 513 79  HOH   HOH A . 
I 6 HOH   14 514 1   HOH   HOH A . 
I 6 HOH   15 515 117 HOH   HOH A . 
I 6 HOH   16 516 93  HOH   HOH A . 
I 6 HOH   17 517 65  HOH   HOH A . 
I 6 HOH   18 518 46  HOH   HOH A . 
I 6 HOH   19 519 22  HOH   HOH A . 
I 6 HOH   20 520 151 HOH   HOH A . 
I 6 HOH   21 521 8   HOH   HOH A . 
I 6 HOH   22 522 194 HOH   HOH A . 
I 6 HOH   23 523 44  HOH   HOH A . 
I 6 HOH   24 524 87  HOH   HOH A . 
I 6 HOH   25 525 196 HOH   HOH A . 
I 6 HOH   26 526 7   HOH   HOH A . 
I 6 HOH   27 527 195 HOH   HOH A . 
I 6 HOH   28 528 26  HOH   HOH A . 
I 6 HOH   29 529 133 HOH   HOH A . 
I 6 HOH   30 530 206 HOH   HOH A . 
I 6 HOH   31 531 28  HOH   HOH A . 
I 6 HOH   32 532 5   HOH   HOH A . 
I 6 HOH   33 533 139 HOH   HOH A . 
I 6 HOH   34 534 9   HOH   HOH A . 
I 6 HOH   35 535 164 HOH   HOH A . 
I 6 HOH   36 536 150 HOH   HOH A . 
I 6 HOH   37 537 66  HOH   HOH A . 
I 6 HOH   38 538 29  HOH   HOH A . 
I 6 HOH   39 539 171 HOH   HOH A . 
I 6 HOH   40 540 45  HOH   HOH A . 
I 6 HOH   41 541 99  HOH   HOH A . 
I 6 HOH   42 542 96  HOH   HOH A . 
I 6 HOH   43 543 86  HOH   HOH A . 
I 6 HOH   44 544 81  HOH   HOH A . 
I 6 HOH   45 545 23  HOH   HOH A . 
I 6 HOH   46 546 115 HOH   HOH A . 
I 6 HOH   47 547 14  HOH   HOH A . 
I 6 HOH   48 548 147 HOH   HOH A . 
I 6 HOH   49 549 37  HOH   HOH A . 
I 6 HOH   50 550 2   HOH   HOH A . 
I 6 HOH   51 551 176 HOH   HOH A . 
I 6 HOH   52 552 57  HOH   HOH A . 
I 6 HOH   53 553 75  HOH   HOH A . 
I 6 HOH   54 554 146 HOH   HOH A . 
I 6 HOH   55 555 42  HOH   HOH A . 
I 6 HOH   56 556 33  HOH   HOH A . 
I 6 HOH   57 557 51  HOH   HOH A . 
I 6 HOH   58 558 11  HOH   HOH A . 
I 6 HOH   59 559 188 HOH   HOH A . 
I 6 HOH   60 560 106 HOH   HOH A . 
I 6 HOH   61 561 76  HOH   HOH A . 
I 6 HOH   62 562 128 HOH   HOH A . 
I 6 HOH   63 563 213 HOH   HOH A . 
I 6 HOH   64 564 43  HOH   HOH A . 
I 6 HOH   65 565 72  HOH   HOH A . 
I 6 HOH   66 566 202 HOH   HOH A . 
I 6 HOH   67 567 209 HOH   HOH A . 
I 6 HOH   68 568 212 HOH   HOH A . 
I 6 HOH   69 569 114 HOH   HOH A . 
I 6 HOH   70 570 105 HOH   HOH A . 
I 6 HOH   71 571 123 HOH   HOH A . 
I 6 HOH   72 572 83  HOH   HOH A . 
I 6 HOH   73 573 100 HOH   HOH A . 
I 6 HOH   74 574 205 HOH   HOH A . 
I 6 HOH   75 575 152 HOH   HOH A . 
I 6 HOH   76 576 102 HOH   HOH A . 
I 6 HOH   77 577 67  HOH   HOH A . 
I 6 HOH   78 578 27  HOH   HOH A . 
I 6 HOH   79 579 129 HOH   HOH A . 
I 6 HOH   80 580 107 HOH   HOH A . 
I 6 HOH   81 581 55  HOH   HOH A . 
I 6 HOH   82 582 54  HOH   HOH A . 
I 6 HOH   83 583 103 HOH   HOH A . 
I 6 HOH   84 584 153 HOH   HOH A . 
I 6 HOH   85 585 192 HOH   HOH A . 
I 6 HOH   86 586 211 HOH   HOH A . 
I 6 HOH   87 587 90  HOH   HOH A . 
I 6 HOH   88 588 58  HOH   HOH A . 
I 6 HOH   89 589 170 HOH   HOH A . 
I 6 HOH   90 590 124 HOH   HOH A . 
I 6 HOH   91 591 183 HOH   HOH A . 
J 6 HOH   1  501 71  HOH   HOH B . 
J 6 HOH   2  502 48  HOH   HOH B . 
J 6 HOH   3  503 17  HOH   HOH B . 
J 6 HOH   4  504 135 HOH   HOH B . 
J 6 HOH   5  505 130 HOH   HOH B . 
J 6 HOH   6  506 111 HOH   HOH B . 
J 6 HOH   7  507 69  HOH   HOH B . 
J 6 HOH   8  508 12  HOH   HOH B . 
J 6 HOH   9  509 98  HOH   HOH B . 
J 6 HOH   10 510 10  HOH   HOH B . 
J 6 HOH   11 511 24  HOH   HOH B . 
J 6 HOH   12 512 112 HOH   HOH B . 
J 6 HOH   13 513 53  HOH   HOH B . 
J 6 HOH   14 514 122 HOH   HOH B . 
J 6 HOH   15 515 61  HOH   HOH B . 
J 6 HOH   16 516 142 HOH   HOH B . 
J 6 HOH   17 517 140 HOH   HOH B . 
J 6 HOH   18 518 62  HOH   HOH B . 
J 6 HOH   19 519 68  HOH   HOH B . 
J 6 HOH   20 520 125 HOH   HOH B . 
J 6 HOH   21 521 21  HOH   HOH B . 
J 6 HOH   22 522 95  HOH   HOH B . 
J 6 HOH   23 523 25  HOH   HOH B . 
J 6 HOH   24 524 94  HOH   HOH B . 
J 6 HOH   25 525 143 HOH   HOH B . 
J 6 HOH   26 526 15  HOH   HOH B . 
J 6 HOH   27 527 165 HOH   HOH B . 
J 6 HOH   28 528 154 HOH   HOH B . 
J 6 HOH   29 529 181 HOH   HOH B . 
J 6 HOH   30 530 18  HOH   HOH B . 
J 6 HOH   31 531 137 HOH   HOH B . 
J 6 HOH   32 532 73  HOH   HOH B . 
J 6 HOH   33 533 30  HOH   HOH B . 
J 6 HOH   34 534 50  HOH   HOH B . 
J 6 HOH   35 535 6   HOH   HOH B . 
J 6 HOH   36 536 201 HOH   HOH B . 
J 6 HOH   37 537 85  HOH   HOH B . 
J 6 HOH   38 538 31  HOH   HOH B . 
J 6 HOH   39 539 119 HOH   HOH B . 
J 6 HOH   40 540 169 HOH   HOH B . 
J 6 HOH   41 541 64  HOH   HOH B . 
J 6 HOH   42 542 20  HOH   HOH B . 
J 6 HOH   43 543 159 HOH   HOH B . 
J 6 HOH   44 544 179 HOH   HOH B . 
J 6 HOH   45 545 39  HOH   HOH B . 
J 6 HOH   46 546 47  HOH   HOH B . 
J 6 HOH   47 547 121 HOH   HOH B . 
J 6 HOH   48 548 63  HOH   HOH B . 
J 6 HOH   49 549 78  HOH   HOH B . 
J 6 HOH   50 550 108 HOH   HOH B . 
J 6 HOH   51 551 59  HOH   HOH B . 
J 6 HOH   52 552 16  HOH   HOH B . 
J 6 HOH   53 553 190 HOH   HOH B . 
J 6 HOH   54 554 203 HOH   HOH B . 
J 6 HOH   55 555 34  HOH   HOH B . 
J 6 HOH   56 556 101 HOH   HOH B . 
J 6 HOH   57 557 168 HOH   HOH B . 
J 6 HOH   58 558 84  HOH   HOH B . 
J 6 HOH   59 559 60  HOH   HOH B . 
J 6 HOH   60 560 158 HOH   HOH B . 
J 6 HOH   61 561 113 HOH   HOH B . 
J 6 HOH   62 562 126 HOH   HOH B . 
J 6 HOH   63 563 173 HOH   HOH B . 
J 6 HOH   64 564 185 HOH   HOH B . 
J 6 HOH   65 565 172 HOH   HOH B . 
J 6 HOH   66 566 97  HOH   HOH B . 
J 6 HOH   67 567 200 HOH   HOH B . 
J 6 HOH   68 568 88  HOH   HOH B . 
J 6 HOH   69 569 19  HOH   HOH B . 
J 6 HOH   70 570 207 HOH   HOH B . 
J 6 HOH   71 571 56  HOH   HOH B . 
J 6 HOH   72 572 216 HOH   HOH B . 
J 6 HOH   73 573 136 HOH   HOH B . 
J 6 HOH   74 574 109 HOH   HOH B . 
J 6 HOH   75 575 144 HOH   HOH B . 
J 6 HOH   76 576 156 HOH   HOH B . 
J 6 HOH   77 577 141 HOH   HOH B . 
J 6 HOH   78 578 180 HOH   HOH B . 
J 6 HOH   79 579 110 HOH   HOH B . 
J 6 HOH   80 580 162 HOH   HOH B . 
J 6 HOH   81 581 184 HOH   HOH B . 
J 6 HOH   82 582 217 HOH   HOH B . 
J 6 HOH   83 583 138 HOH   HOH B . 
J 6 HOH   84 584 74  HOH   HOH B . 
J 6 HOH   85 585 189 HOH   HOH B . 
J 6 HOH   86 586 134 HOH   HOH B . 
J 6 HOH   87 587 193 HOH   HOH B . 
J 6 HOH   88 588 191 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 15  ? CG  ? A GLU 15  CG  
2   1 Y 1 A GLU 15  ? CD  ? A GLU 15  CD  
3   1 Y 1 A GLU 15  ? OE1 ? A GLU 15  OE1 
4   1 Y 1 A GLU 15  ? OE2 ? A GLU 15  OE2 
5   1 Y 1 A GLU 75  ? CG  ? A GLU 75  CG  
6   1 Y 1 A GLU 75  ? CD  ? A GLU 75  CD  
7   1 Y 1 A GLU 75  ? OE1 ? A GLU 75  OE1 
8   1 Y 1 A GLU 75  ? OE2 ? A GLU 75  OE2 
9   1 Y 1 A TYR 117 ? CG  ? A TYR 117 CG  
10  1 Y 1 A TYR 117 ? CD1 ? A TYR 117 CD1 
11  1 Y 1 A TYR 117 ? CD2 ? A TYR 117 CD2 
12  1 Y 1 A TYR 117 ? CE1 ? A TYR 117 CE1 
13  1 Y 1 A TYR 117 ? CE2 ? A TYR 117 CE2 
14  1 Y 1 A TYR 117 ? CZ  ? A TYR 117 CZ  
15  1 Y 1 A TYR 117 ? OH  ? A TYR 117 OH  
16  1 Y 1 A GLU 119 ? CG  ? A GLU 119 CG  
17  1 Y 1 A GLU 119 ? CD  ? A GLU 119 CD  
18  1 Y 1 A GLU 119 ? OE1 ? A GLU 119 OE1 
19  1 Y 1 A GLU 119 ? OE2 ? A GLU 119 OE2 
20  1 Y 1 A ASN 120 ? CG  ? A ASN 120 CG  
21  1 Y 1 A ASN 120 ? OD1 ? A ASN 120 OD1 
22  1 Y 1 A ASN 120 ? ND2 ? A ASN 120 ND2 
23  1 Y 1 A GLU 148 ? CG  ? A GLU 148 CG  
24  1 Y 1 A GLU 148 ? CD  ? A GLU 148 CD  
25  1 Y 1 A GLU 148 ? OE1 ? A GLU 148 OE1 
26  1 Y 1 A GLU 148 ? OE2 ? A GLU 148 OE2 
27  1 Y 1 A LYS 151 ? CE  ? A LYS 151 CE  
28  1 Y 1 A LYS 151 ? NZ  ? A LYS 151 NZ  
29  1 Y 1 A LYS 181 ? CG  ? A LYS 181 CG  
30  1 Y 1 A LYS 181 ? CD  ? A LYS 181 CD  
31  1 Y 1 A LYS 181 ? CE  ? A LYS 181 CE  
32  1 Y 1 A LYS 181 ? NZ  ? A LYS 181 NZ  
33  1 Y 1 A ARG 185 ? CG  ? A ARG 185 CG  
34  1 Y 1 A ARG 185 ? CD  ? A ARG 185 CD  
35  1 Y 1 A ARG 185 ? NE  ? A ARG 185 NE  
36  1 Y 1 A ARG 185 ? CZ  ? A ARG 185 CZ  
37  1 Y 1 A ARG 185 ? NH1 ? A ARG 185 NH1 
38  1 Y 1 A ARG 185 ? NH2 ? A ARG 185 NH2 
39  1 Y 1 A LYS 194 ? CE  ? A LYS 194 CE  
40  1 Y 1 A LYS 194 ? NZ  ? A LYS 194 NZ  
41  1 Y 1 A LYS 195 ? CG  ? A LYS 195 CG  
42  1 Y 1 A LYS 195 ? CD  ? A LYS 195 CD  
43  1 Y 1 A LYS 195 ? CE  ? A LYS 195 CE  
44  1 Y 1 A LYS 195 ? NZ  ? A LYS 195 NZ  
45  1 Y 1 A SER 197 ? OG  ? A SER 197 OG  
46  1 Y 1 A LYS 198 ? CG  ? A LYS 198 CG  
47  1 Y 1 A LYS 198 ? CD  ? A LYS 198 CD  
48  1 Y 1 A LYS 198 ? CE  ? A LYS 198 CE  
49  1 Y 1 A LYS 198 ? NZ  ? A LYS 198 NZ  
50  1 Y 1 A LYS 214 ? CG  ? A LYS 214 CG  
51  1 Y 1 A LYS 214 ? CD  ? A LYS 214 CD  
52  1 Y 1 A LYS 214 ? CE  ? A LYS 214 CE  
53  1 Y 1 A LYS 214 ? NZ  ? A LYS 214 NZ  
54  1 Y 1 A LYS 218 ? CE  ? A LYS 218 CE  
55  1 Y 1 A LYS 218 ? NZ  ? A LYS 218 NZ  
56  1 Y 1 A LYS 221 ? CG  ? A LYS 221 CG  
57  1 Y 1 A LYS 221 ? CD  ? A LYS 221 CD  
58  1 Y 1 A LYS 221 ? CE  ? A LYS 221 CE  
59  1 Y 1 A LYS 221 ? NZ  ? A LYS 221 NZ  
60  1 Y 1 A ARG 222 ? CG  ? A ARG 222 CG  
61  1 Y 1 A ARG 222 ? CD  ? A ARG 222 CD  
62  1 Y 1 A ARG 222 ? NE  ? A ARG 222 NE  
63  1 Y 1 A ARG 222 ? CZ  ? A ARG 222 CZ  
64  1 Y 1 A ARG 222 ? NH1 ? A ARG 222 NH1 
65  1 Y 1 A ARG 222 ? NH2 ? A ARG 222 NH2 
66  1 Y 1 A VAL 232 ? CG1 ? A VAL 232 CG1 
67  1 Y 1 A VAL 232 ? CG2 ? A VAL 232 CG2 
68  1 Y 1 A LYS 263 ? CG  ? A LYS 263 CG  
69  1 Y 1 A LYS 263 ? CD  ? A LYS 263 CD  
70  1 Y 1 A LYS 263 ? CE  ? A LYS 263 CE  
71  1 Y 1 A LYS 263 ? NZ  ? A LYS 263 NZ  
72  1 Y 1 A GLU 266 ? OE1 ? A GLU 266 OE1 
73  1 Y 1 A GLU 266 ? OE2 ? A GLU 266 OE2 
74  1 Y 1 A GLU 287 ? OE1 ? A GLU 287 OE1 
75  1 Y 1 A GLU 287 ? OE2 ? A GLU 287 OE2 
76  1 Y 1 A GLU 299 ? OE2 ? A GLU 299 OE2 
77  1 Y 1 A GLN 303 ? CG  ? A GLN 303 CG  
78  1 Y 1 A GLN 303 ? CD  ? A GLN 303 CD  
79  1 Y 1 A GLN 303 ? OE1 ? A GLN 303 OE1 
80  1 Y 1 A GLN 303 ? NE2 ? A GLN 303 NE2 
81  1 Y 1 B GLU 75  ? CG  ? B GLU 75  CG  
82  1 Y 1 B GLU 75  ? CD  ? B GLU 75  CD  
83  1 Y 1 B GLU 75  ? OE1 ? B GLU 75  OE1 
84  1 Y 1 B GLU 75  ? OE2 ? B GLU 75  OE2 
85  1 Y 1 B LYS 111 ? CG  ? B LYS 111 CG  
86  1 Y 1 B LYS 111 ? CD  ? B LYS 111 CD  
87  1 Y 1 B LYS 111 ? CE  ? B LYS 111 CE  
88  1 Y 1 B LYS 111 ? NZ  ? B LYS 111 NZ  
89  1 Y 1 B ASP 112 ? CG  ? B ASP 112 CG  
90  1 Y 1 B ASP 112 ? OD1 ? B ASP 112 OD1 
91  1 Y 1 B ASP 112 ? OD2 ? B ASP 112 OD2 
92  1 Y 1 B GLU 119 ? CG  ? B GLU 119 CG  
93  1 Y 1 B GLU 119 ? CD  ? B GLU 119 CD  
94  1 Y 1 B GLU 119 ? OE1 ? B GLU 119 OE1 
95  1 Y 1 B GLU 119 ? OE2 ? B GLU 119 OE2 
96  1 Y 1 B GLU 148 ? CG  ? B GLU 148 CG  
97  1 Y 1 B GLU 148 ? CD  ? B GLU 148 CD  
98  1 Y 1 B GLU 148 ? OE1 ? B GLU 148 OE1 
99  1 Y 1 B GLU 148 ? OE2 ? B GLU 148 OE2 
100 1 Y 1 B LYS 151 ? CG  ? B LYS 151 CG  
101 1 Y 1 B LYS 151 ? CD  ? B LYS 151 CD  
102 1 Y 1 B LYS 151 ? CE  ? B LYS 151 CE  
103 1 Y 1 B LYS 151 ? NZ  ? B LYS 151 NZ  
104 1 Y 1 B GLN 152 ? CG  ? B GLN 152 CG  
105 1 Y 1 B GLN 152 ? CD  ? B GLN 152 CD  
106 1 Y 1 B GLN 152 ? OE1 ? B GLN 152 OE1 
107 1 Y 1 B GLN 152 ? NE2 ? B GLN 152 NE2 
108 1 Y 1 B GLU 170 ? CG  ? B GLU 170 CG  
109 1 Y 1 B GLU 170 ? CD  ? B GLU 170 CD  
110 1 Y 1 B GLU 170 ? OE1 ? B GLU 170 OE1 
111 1 Y 1 B GLU 170 ? OE2 ? B GLU 170 OE2 
112 1 Y 1 B LYS 181 ? CE  ? B LYS 181 CE  
113 1 Y 1 B LYS 181 ? NZ  ? B LYS 181 NZ  
114 1 Y 1 B GLU 191 ? CG  ? B GLU 191 CG  
115 1 Y 1 B GLU 191 ? CD  ? B GLU 191 CD  
116 1 Y 1 B GLU 191 ? OE1 ? B GLU 191 OE1 
117 1 Y 1 B GLU 191 ? OE2 ? B GLU 191 OE2 
118 1 Y 1 B LYS 194 ? CG  ? B LYS 194 CG  
119 1 Y 1 B LYS 194 ? CD  ? B LYS 194 CD  
120 1 Y 1 B LYS 194 ? CE  ? B LYS 194 CE  
121 1 Y 1 B LYS 194 ? NZ  ? B LYS 194 NZ  
122 1 Y 1 B ARG 203 ? CG  ? B ARG 203 CG  
123 1 Y 1 B ARG 203 ? CD  ? B ARG 203 CD  
124 1 Y 1 B ARG 203 ? NE  ? B ARG 203 NE  
125 1 Y 1 B ARG 203 ? CZ  ? B ARG 203 CZ  
126 1 Y 1 B ARG 203 ? NH1 ? B ARG 203 NH1 
127 1 Y 1 B ARG 203 ? NH2 ? B ARG 203 NH2 
128 1 Y 1 B LYS 214 ? CG  ? B LYS 214 CG  
129 1 Y 1 B LYS 214 ? CD  ? B LYS 214 CD  
130 1 Y 1 B LYS 214 ? CE  ? B LYS 214 CE  
131 1 Y 1 B LYS 214 ? NZ  ? B LYS 214 NZ  
132 1 Y 1 B LYS 218 ? CG  ? B LYS 218 CG  
133 1 Y 1 B LYS 218 ? CD  ? B LYS 218 CD  
134 1 Y 1 B LYS 218 ? CE  ? B LYS 218 CE  
135 1 Y 1 B LYS 218 ? NZ  ? B LYS 218 NZ  
136 1 Y 1 B LYS 221 ? CG  ? B LYS 221 CG  
137 1 Y 1 B LYS 221 ? CD  ? B LYS 221 CD  
138 1 Y 1 B LYS 221 ? CE  ? B LYS 221 CE  
139 1 Y 1 B LYS 221 ? NZ  ? B LYS 221 NZ  
140 1 Y 1 B ARG 222 ? CG  ? B ARG 222 CG  
141 1 Y 1 B ARG 222 ? CD  ? B ARG 222 CD  
142 1 Y 1 B ARG 222 ? NE  ? B ARG 222 NE  
143 1 Y 1 B ARG 222 ? CZ  ? B ARG 222 CZ  
144 1 Y 1 B ARG 222 ? NH1 ? B ARG 222 NH1 
145 1 Y 1 B ARG 222 ? NH2 ? B ARG 222 NH2 
146 1 Y 1 B VAL 232 ? CG1 ? B VAL 232 CG1 
147 1 Y 1 B VAL 232 ? CG2 ? B VAL 232 CG2 
148 1 Y 1 B ARG 234 ? CG  ? B ARG 234 CG  
149 1 Y 1 B ARG 234 ? CD  ? B ARG 234 CD  
150 1 Y 1 B ARG 234 ? NE  ? B ARG 234 NE  
151 1 Y 1 B ARG 234 ? CZ  ? B ARG 234 CZ  
152 1 Y 1 B ARG 234 ? NH1 ? B ARG 234 NH1 
153 1 Y 1 B ARG 234 ? NH2 ? B ARG 234 NH2 
154 1 Y 1 B GLN 238 ? CG  ? B GLN 238 CG  
155 1 Y 1 B GLN 238 ? CD  ? B GLN 238 CD  
156 1 Y 1 B GLN 238 ? OE1 ? B GLN 238 OE1 
157 1 Y 1 B GLN 238 ? NE2 ? B GLN 238 NE2 
158 1 Y 1 B ASP 248 ? CG  ? B ASP 248 CG  
159 1 Y 1 B ASP 248 ? OD1 ? B ASP 248 OD1 
160 1 Y 1 B ASP 248 ? OD2 ? B ASP 248 OD2 
161 1 Y 1 B LEU 250 ? CG  ? B LEU 250 CG  
162 1 Y 1 B LEU 250 ? CD1 ? B LEU 250 CD1 
163 1 Y 1 B LEU 250 ? CD2 ? B LEU 250 CD2 
164 1 Y 1 B ILE 258 ? CG1 ? B ILE 258 CG1 
165 1 Y 1 B ILE 258 ? CG2 ? B ILE 258 CG2 
166 1 Y 1 B ILE 258 ? CD1 ? B ILE 258 CD1 
167 1 Y 1 B GLU 260 ? CG  ? B GLU 260 CG  
168 1 Y 1 B GLU 260 ? CD  ? B GLU 260 CD  
169 1 Y 1 B GLU 260 ? OE1 ? B GLU 260 OE1 
170 1 Y 1 B GLU 260 ? OE2 ? B GLU 260 OE2 
171 1 Y 1 B LYS 263 ? CG  ? B LYS 263 CG  
172 1 Y 1 B LYS 263 ? CD  ? B LYS 263 CD  
173 1 Y 1 B LYS 263 ? CE  ? B LYS 263 CE  
174 1 Y 1 B LYS 263 ? NZ  ? B LYS 263 NZ  
175 1 Y 1 B GLN 264 ? CG  ? B GLN 264 CG  
176 1 Y 1 B GLN 264 ? CD  ? B GLN 264 CD  
177 1 Y 1 B GLN 264 ? OE1 ? B GLN 264 OE1 
178 1 Y 1 B GLN 264 ? NE2 ? B GLN 264 NE2 
179 1 Y 1 B GLU 266 ? CG  ? B GLU 266 CG  
180 1 Y 1 B GLU 266 ? CD  ? B GLU 266 CD  
181 1 Y 1 B GLU 266 ? OE1 ? B GLU 266 OE1 
182 1 Y 1 B GLU 266 ? OE2 ? B GLU 266 OE2 
183 1 Y 1 B GLU 290 ? CG  ? B GLU 290 CG  
184 1 Y 1 B GLU 290 ? CD  ? B GLU 290 CD  
185 1 Y 1 B GLU 290 ? OE1 ? B GLU 290 OE1 
186 1 Y 1 B GLU 290 ? OE2 ? B GLU 290 OE2 
187 1 Y 1 B ARG 319 ? CG  ? B ARG 319 CG  
188 1 Y 1 B ARG 319 ? CD  ? B ARG 319 CD  
189 1 Y 1 B ARG 319 ? NE  ? B ARG 319 NE  
190 1 Y 1 B ARG 319 ? CZ  ? B ARG 319 CZ  
191 1 Y 1 B ARG 319 ? NH1 ? B ARG 319 NH1 
192 1 Y 1 B ARG 319 ? NH2 ? B ARG 319 NH2 
193 1 Y 1 B ARG 334 ? CG  ? B ARG 334 CG  
194 1 Y 1 B ARG 334 ? CD  ? B ARG 334 CD  
195 1 Y 1 B ARG 334 ? NE  ? B ARG 334 NE  
196 1 Y 1 B ARG 334 ? CZ  ? B ARG 334 CZ  
197 1 Y 1 B ARG 334 ? NH1 ? B ARG 334 NH1 
198 1 Y 1 B ARG 334 ? NH2 ? B ARG 334 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.18.2_3874: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   105.71 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LPD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.773 
_cell.length_a_esd                 ? 
_cell.length_b                     79.435 
_cell.length_b_esd                 ? 
_cell.length_c                     79.278 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9LPD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9LPD 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.44 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.58 
_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    '0.15 M ammonium sulfate, 0.1M HEPES pH 7.5, 25% w/v PEG 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            290 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-27 
_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   0.97853 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LPD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.05 
_reflns.d_resolution_low                               76.32 
_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                                     46067 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.093 
_reflns.pdbx_Rpim_I_all                                0.052 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.077 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.05 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6713 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.565 
_reflns_shell.pdbx_Rpim_I_all                               0.306 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.473 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9LPD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.05 
_refine.ls_d_res_low                             30.65 
_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                     45967 
_refine.ls_number_reflns_R_free                  2291 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.38 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2330 
_refine.ls_R_factor_R_free                       0.2499 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2320 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      8I1Y 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.05 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.05 
_refine_hist.d_res_low                        30.65 
_refine_hist.number_atoms_solvent             180 
_refine_hist.number_atoms_total               5254 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4977 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         97 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  ? 5178 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.253  ? 7040 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 21.127 ? 1847 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.075  ? 791  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 930  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.05 2.09  . . 132 2774 99.00 . . . . 0.3698 . . . . . . . . . . . 0.3586 
'X-RAY DIFFRACTION' 2.09 2.14  . . 121 2729 98.00 . . . . 0.3505 . . . . . . . . . . . 0.3877 
'X-RAY DIFFRACTION' 2.14 2.19  . . 138 2736 99.00 . . . . 0.3301 . . . . . . . . . . . 0.3126 
'X-RAY DIFFRACTION' 2.19 2.25  . . 134 2695 99.00 . . . . 0.3147 . . . . . . . . . . . 0.3664 
'X-RAY DIFFRACTION' 2.25 2.32  . . 153 2730 99.00 . . . . 0.2977 . . . . . . . . . . . 0.2747 
'X-RAY DIFFRACTION' 2.32 2.39  . . 156 2742 99.00 . . . . 0.2875 . . . . . . . . . . . 0.3205 
'X-RAY DIFFRACTION' 2.39 2.48  . . 134 2722 98.00 . . . . 0.2735 . . . . . . . . . . . 0.3377 
'X-RAY DIFFRACTION' 2.48 2.58  . . 149 2739 99.00 . . . . 0.2652 . . . . . . . . . . . 0.3176 
'X-RAY DIFFRACTION' 2.58 2.69  . . 123 2686 97.00 . . . . 0.2535 . . . . . . . . . . . 0.2411 
'X-RAY DIFFRACTION' 2.69 2.84  . . 141 2747 98.00 . . . . 0.2524 . . . . . . . . . . . 0.2692 
'X-RAY DIFFRACTION' 2.84 3.01  . . 146 2694 98.00 . . . . 0.2588 . . . . . . . . . . . 0.2762 
'X-RAY DIFFRACTION' 3.01 3.25  . . 156 2742 99.00 . . . . 0.2362 . . . . . . . . . . . 0.2743 
'X-RAY DIFFRACTION' 3.25 3.57  . . 145 2740 99.00 . . . . 0.2269 . . . . . . . . . . . 0.2465 
'X-RAY DIFFRACTION' 3.57 4.09  . . 163 2689 98.00 . . . . 0.1902 . . . . . . . . . . . 0.2057 
'X-RAY DIFFRACTION' 4.09 5.15  . . 148 2753 98.00 . . . . 0.1777 . . . . . . . . . . . 0.1869 
'X-RAY DIFFRACTION' 5.15 30.65 . . 152 2758 97.00 . . . . 0.1962 . . . . . . . . . . . 0.2242 
# 
_struct.entry_id                     9LPD 
_struct.title                        
'Crystal structure of Escherichia coli trptophanyl-tRNA synthetase in complex with tirabrutinib' 
_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        9LPD 
_struct_keywords.text            'trptophayl-tRNA synthetase, Tirabrutinib, complex, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 3 ? 
I N N 6 ? 
J N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    E2QFN4_ECOLX 
_struct_ref.pdbx_db_accession          E2QFN4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIF
VQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDI
AQRFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNK
AGVSNLLDILSAVTGQSIPELEKQFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKASAHASRT
LKAVYEAIGFVAK
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9LPD A 1 ? 333 ? E2QFN4 1 ? 333 ? 1 333 
2 1 9LPD B 1 ? 333 ? E2QFN4 1 ? 333 ? 1 333 
# 
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 9LPD ARG A 334 ? UNP E2QFN4 ? ? 'expression tag' 334 1  
1 9LPD HIS A 335 ? UNP E2QFN4 ? ? 'expression tag' 335 2  
1 9LPD HIS A 336 ? UNP E2QFN4 ? ? 'expression tag' 336 3  
1 9LPD HIS A 337 ? UNP E2QFN4 ? ? 'expression tag' 337 4  
1 9LPD HIS A 338 ? UNP E2QFN4 ? ? 'expression tag' 338 5  
1 9LPD HIS A 339 ? UNP E2QFN4 ? ? 'expression tag' 339 6  
1 9LPD HIS A 340 ? UNP E2QFN4 ? ? 'expression tag' 340 7  
2 9LPD ARG B 334 ? UNP E2QFN4 ? ? 'expression tag' 334 8  
2 9LPD HIS B 335 ? UNP E2QFN4 ? ? 'expression tag' 335 9  
2 9LPD HIS B 336 ? UNP E2QFN4 ? ? 'expression tag' 336 10 
2 9LPD HIS B 337 ? UNP E2QFN4 ? ? 'expression tag' 337 11 
2 9LPD HIS B 338 ? UNP E2QFN4 ? ? 'expression tag' 338 12 
2 9LPD HIS B 339 ? UNP E2QFN4 ? ? 'expression tag' 339 13 
2 9LPD HIS B 340 ? UNP E2QFN4 ? ? 'expression tag' 340 14 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 6690  ? 
1 MORE         -73   ? 
1 'SSA (A^2)'  26380 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 17  ? MET A 22  ? THR A 17  MET A 22  1 ? 6  
HELX_P HELX_P2  AA2 ALA A 24  ? ASN A 30  ? ALA A 24  ASN A 30  1 ? 7  
HELX_P HELX_P3  AA3 VAL A 42  ? ILE A 47  ? VAL A 42  ILE A 47  1 ? 6  
HELX_P HELX_P4  AA4 ASP A 52  ? CYS A 70  ? ASP A 52  CYS A 70  1 ? 19 
HELX_P HELX_P5  AA5 SER A 83  ? VAL A 85  ? SER A 83  VAL A 85  5 ? 3  
HELX_P HELX_P6  AA6 PRO A 86  ? CYS A 97  ? PRO A 86  CYS A 97  1 ? 12 
HELX_P HELX_P7  AA7 TYR A 100 ? ARG A 106 ? TYR A 100 ARG A 106 1 ? 7  
HELX_P HELX_P8  AA8 ASN A 122 ? LEU A 138 ? ASN A 122 LEU A 138 1 ? 17 
HELX_P HELX_P9  AA9 GLY A 147 ? ASP A 149 ? GLY A 147 ASP A 149 5 ? 3  
HELX_P HELX_P10 AB1 GLN A 150 ? GLY A 169 ? GLN A 150 GLY A 169 1 ? 20 
HELX_P HELX_P11 AB2 ASN A 202 ? VAL A 206 ? ASN A 202 VAL A 206 5 ? 5  
HELX_P HELX_P12 AB3 ASP A 212 ? ALA A 223 ? ASP A 212 ALA A 223 1 ? 12 
HELX_P HELX_P13 AB4 LYS A 240 ? GLY A 255 ? LYS A 240 GLY A 255 1 ? 16 
HELX_P HELX_P14 AB5 SER A 257 ? PHE A 265 ? SER A 257 PHE A 265 1 ? 9  
HELX_P HELX_P15 AB6 MET A 269 ? ASN A 297 ? MET A 269 ASN A 297 1 ? 29 
HELX_P HELX_P16 AB7 ASP A 298 ? GLY A 329 ? ASP A 298 GLY A 329 1 ? 32 
HELX_P HELX_P17 AB8 THR B 17  ? ALA B 24  ? THR B 17  ALA B 24  1 ? 8  
HELX_P HELX_P18 AB9 ALA B 24  ? MET B 31  ? ALA B 24  MET B 31  1 ? 8  
HELX_P HELX_P19 AC1 VAL B 42  ? ILE B 47  ? VAL B 42  ILE B 47  1 ? 6  
HELX_P HELX_P20 AC2 ASP B 52  ? GLY B 71  ? ASP B 52  GLY B 71  1 ? 20 
HELX_P HELX_P21 AC3 SER B 83  ? VAL B 85  ? SER B 83  VAL B 85  5 ? 3  
HELX_P HELX_P22 AC4 PRO B 86  ? CYS B 97  ? PRO B 86  CYS B 97  1 ? 12 
HELX_P HELX_P23 AC5 TYR B 100 ? ARG B 106 ? TYR B 100 ARG B 106 1 ? 7  
HELX_P HELX_P24 AC6 MET B 107 ? TYR B 117 ? MET B 107 TYR B 117 1 ? 11 
HELX_P HELX_P25 AC7 ALA B 118 ? ILE B 121 ? ALA B 118 ILE B 121 5 ? 4  
HELX_P HELX_P26 AC8 ASN B 122 ? LEU B 138 ? ASN B 122 LEU B 138 1 ? 17 
HELX_P HELX_P27 AC9 GLY B 147 ? ASP B 149 ? GLY B 147 ASP B 149 5 ? 3  
HELX_P HELX_P28 AD1 GLN B 150 ? GLY B 169 ? GLN B 150 GLY B 169 1 ? 20 
HELX_P HELX_P29 AD2 ASN B 202 ? VAL B 206 ? ASN B 202 VAL B 206 5 ? 5  
HELX_P HELX_P30 AD3 ASP B 212 ? ARG B 222 ? ASP B 212 ARG B 222 1 ? 11 
HELX_P HELX_P31 AD4 LYS B 240 ? GLY B 255 ? LYS B 240 GLY B 255 1 ? 16 
HELX_P HELX_P32 AD5 SER B 257 ? PHE B 265 ? SER B 257 PHE B 265 1 ? 9  
HELX_P HELX_P33 AD6 MET B 269 ? ASN B 297 ? MET B 269 ASN B 297 1 ? 29 
HELX_P HELX_P34 AD7 ASP B 298 ? GLY B 329 ? ASP B 298 GLY B 329 1 ? 32 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 GLU 229 A . ? GLU 229 A PRO 230 A ? PRO 230 A 1 -6.30 
2 GLU 229 B . ? GLU 229 B PRO 230 B ? PRO 230 B 1 1.08  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA2 1 2 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA4 1 2 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 5   ? ALA A 10  ? ILE A 5   ALA A 10  
AA1 2 HIS A 36  ? ILE A 41  ? HIS A 36  ILE A 41  
AA1 3 THR A 78  ? VAL A 81  ? THR A 78  VAL A 81  
AA2 1 LEU A 143 ? VAL A 144 ? LEU A 143 VAL A 144 
AA2 2 GLU A 176 ? PRO A 177 ? GLU A 176 PRO A 177 
AA3 1 ILE B 5   ? ALA B 10  ? ILE B 5   ALA B 10  
AA3 2 HIS B 36  ? ILE B 41  ? HIS B 36  ILE B 41  
AA3 3 THR B 78  ? VAL B 81  ? THR B 78  VAL B 81  
AA4 1 LEU B 143 ? PRO B 145 ? LEU B 143 PRO B 145 
AA4 2 GLU B 176 ? PHE B 178 ? GLU B 176 PHE B 178 
# 
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 SER A 8   ? N SER A 8   O CYS A 40  ? O CYS A 40  
AA1 2 3 N TYR A 39  ? N TYR A 39  O THR A 78  ? O THR A 78  
AA2 1 2 N VAL A 144 ? N VAL A 144 O GLU A 176 ? O GLU A 176 
AA3 1 2 N VAL B 6   ? N VAL B 6   O HIS B 36  ? O HIS B 36  
AA3 2 3 N TYR B 39  ? N TYR B 39  O THR B 78  ? O THR B 78  
AA4 1 2 N VAL B 144 ? N VAL B 144 O GLU B 176 ? O GLU B 176 
# 
_pdbx_entry_details.entry_id                   9LPD 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 ALA A 24  ? ? -141.12 -58.88  
2  1 GLU A 191 ? ? -150.15 74.08   
3  1 THR A 225 ? ? -121.07 -133.31 
4  1 ASP A 236 ? ? -169.49 98.49   
5  1 LYS A 240 ? ? -141.03 56.23   
6  1 ALA B 24  ? ? -138.09 -77.80  
7  1 TYR B 117 ? ? -111.95 73.49   
8  1 ASN B 120 ? ? -155.65 62.22   
9  1 ARG B 185 ? ? -152.36 77.66   
10 1 PRO B 192 ? ? -68.07  0.21    
11 1 THR B 225 ? ? -129.53 -123.21 
12 1 LYS B 240 ? ? -144.98 48.04   
13 1 MET B 269 ? ? -118.89 -164.13 
# 
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 30.2956  -4.4796  -4.2004  0.2101 ? -0.0325 ? 0.0035  ? 0.3319 ? -0.0287 ? 0.2087  ? 0.0099  ? 
-0.0215 ? -0.0424 ? -0.0272 ? -0.0173 ? 0.0034  ? -0.1107 ? 0.1856  ? -0.1300 ? 0.0343  ? 0.0803  ? -0.0371 ? -0.0833 ? -0.0642 ? 
-0.0000 ? 
2  'X-RAY DIFFRACTION' ? refined 23.4880  -8.5571  -3.8432  0.2038 ? -0.0423 ? 0.0084  ? 0.3020 ? -0.0235 ? 0.1529  ? 0.1126  ? 
0.0739  ? -0.0415 ? 0.2149  ? -0.1302 ? 0.1775  ? -0.0756 ? 0.1575  ? 0.0178  ? -0.0332 ? 0.1319  ? 0.0257  ? 0.0134  ? 0.0668  ? 
-0.0000 ? 
3  'X-RAY DIFFRACTION' ? refined 20.0003  3.3675   11.5250  0.1881 ? -0.0234 ? -0.0362 ? 0.1811 ? -0.0418 ? 0.2732  ? 0.1448  ? 
-0.0169 ? 0.0466  ? 0.0774  ? -0.2470 ? 0.0559  ? -0.0661 ? -0.0394 ? 0.1652  ? 0.0429  ? -0.0253 ? 0.0262  ? 0.0326  ? 0.0464  ? 
0.0000  ? 
4  'X-RAY DIFFRACTION' ? refined 33.9030  -0.3419  5.9715   0.2148 ? -0.0191 ? -0.0135 ? 0.3105 ? 0.0018  ? 0.2826  ? -0.0004 ? 
0.0419  ? -0.0043 ? 0.0193  ? 0.0956  ? 0.0268  ? 0.0004  ? 0.0111  ? -0.0260 ? 0.1015  ? -0.0875 ? -0.1111 ? -0.1670 ? 0.0306  ? 
-0.0000 ? 
5  'X-RAY DIFFRACTION' ? refined 32.0108  6.4245   -16.8863 0.3530 ? 0.0277  ? 0.0602  ? 0.5798 ? -0.0597 ? 0.4953  ? -0.0055 ? 
0.0030  ? 0.0208  ? -0.0061 ? -0.0175 ? 0.0206  ? 0.0196  ? 0.0482  ? 0.4649  ? 0.2830  ? 0.1798  ? -0.0102 ? -0.0138 ? -0.3473 ? 
-0.0000 ? 
6  'X-RAY DIFFRACTION' ? refined 48.4276  6.2725   -20.2965 0.3439 ? -0.0079 ? 0.0020  ? 0.4199 ? 0.0346  ? 0.2960  ? 0.0548  ? 
-0.0076 ? -0.1716 ? 0.0963  ? -0.0012 ? 0.1299  ? 0.0347  ? -0.1041 ? 0.0121  ? -0.0035 ? -0.2035 ? -0.1118 ? -0.0121 ? -0.1417 ? 
0.0000  ? 
7  'X-RAY DIFFRACTION' ? refined 34.9565  -7.7348  -20.8473 0.4081 ? -0.0792 ? 0.1469  ? 0.4198 ? -0.4846 ? -0.2792 ? 0.0168  ? 
0.0719  ? 0.0862  ? -0.0334 ? 0.0377  ? 0.0331  ? -0.2669 ? 0.6806  ? 0.2614  ? -0.3225 ? -0.6349 ? -1.1721 ? 0.0293  ? -0.0328 ? 
-0.0000 ? 
8  'X-RAY DIFFRACTION' ? refined 14.9298  -15.3299 9.8869   0.2189 ? -0.0087 ? -0.0133 ? 0.1981 ? -0.0804 ? 0.2811  ? 0.0803  ? 
0.1268  ? -0.0564 ? -0.1133 ? -0.0238 ? 0.0367  ? -0.0918 ? -0.2265 ? -0.3359 ? 0.0808  ? 0.1286  ? 0.1031  ? 0.1969  ? 0.2304  ? 
0.0000  ? 
9  'X-RAY DIFFRACTION' ? refined -4.1511  0.7160   14.6989  0.1644 ? 0.0055  ? 0.0002  ? 0.1558 ? -0.0112 ? 0.2601  ? 0.4763  ? 
-0.0013 ? -0.2436 ? -0.0264 ? -0.3698 ? -0.0098 ? 0.0218  ? 0.0242  ? 0.2138  ? 0.0992  ? 0.0511  ? 0.0481  ? 0.0281  ? -0.0767 ? 
-0.0000 ? 
10 'X-RAY DIFFRACTION' ? refined -18.3370 9.0980   34.8368  0.4339 ? 0.0019  ? 0.0650  ? 0.2542 ? -0.0043 ? 0.2489  ? 0.0439  ? 
-0.0829 ? 0.3099  ? 0.1515  ? 0.5741  ? -0.0349 ? -0.0704 ? -0.2732 ? -0.0319 ? -0.3623 ? 0.1491  ? 0.0786  ? -0.1214 ? 0.0762  ? 
-0.0000 ? 
11 'X-RAY DIFFRACTION' ? refined 0.3592   -13.4412 8.4025   0.2492 ? -0.0293 ? -0.0166 ? 0.3046 ? -0.0077 ? 0.2643  ? 0.0855  ? 
0.0446  ? -0.0481 ? 0.0642  ? 0.1208  ? 0.0179  ? -0.0261 ? 0.1469  ? -0.0816 ? -0.0300 ? 0.0920  ? 0.0939  ? 0.1553  ? -0.0680 ? 
0.0000  ? 
# 
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  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 24 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 25 through 86 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 87 through 168 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 169 through 189 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 190 through 212 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 213 through 269 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 270 through 298 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 299 through 335 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 183 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 184 through 298 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 299 through 334 )
;
# 
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 THR 2   ? A THR 2   
3  1 Y 1 A GLN 109 ? A GLN 109 
4  1 Y 1 A PHE 110 ? A PHE 110 
5  1 Y 1 A LYS 111 ? A LYS 111 
6  1 Y 1 A ASP 112 ? A ASP 112 
7  1 Y 1 A LYS 113 ? A LYS 113 
8  1 Y 1 A SER 114 ? A SER 114 
9  1 Y 1 A ALA 115 ? A ALA 115 
10 1 Y 1 A ARG 116 ? A ARG 116 
11 1 Y 1 A SER 182 ? A SER 182 
12 1 Y 1 A ASP 201 ? A ASP 201 
13 1 Y 1 A HIS 336 ? A HIS 336 
14 1 Y 1 A HIS 337 ? A HIS 337 
15 1 Y 1 A HIS 338 ? A HIS 338 
16 1 Y 1 A HIS 339 ? A HIS 339 
17 1 Y 1 A HIS 340 ? A HIS 340 
18 1 Y 1 B MET 1   ? B MET 1   
19 1 Y 1 B HIS 335 ? B HIS 335 
20 1 Y 1 B HIS 336 ? B HIS 336 
21 1 Y 1 B HIS 337 ? B HIS 337 
22 1 Y 1 B HIS 338 ? B HIS 338 
23 1 Y 1 B HIS 339 ? B HIS 339 
24 1 Y 1 B HIS 340 ? B HIS 340 
# 
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 
A1EK0 N1     N  Y N 1   
A1EK0 C2     C  Y N 2   
A1EK0 N3     N  Y N 3   
A1EK0 C4     C  Y N 4   
A1EK0 C7     C  N N 5   
A1EK0 C8     C  N N 6   
A1EK0 C10    C  N N 7   
A1EK0 C12    C  N N 8   
A1EK0 C13    C  N N 9   
A1EK0 C14    C  N N 10  
A1EK0 C15    C  N N 11  
A1EK0 C16    C  N N 12  
A1EK0 C19    C  Y N 13  
A1EK0 C20    C  Y N 14  
A1EK0 C21    C  Y N 15  
A1EK0 C22    C  Y N 16  
A1EK0 C24    C  Y N 17  
A1EK0 C25    C  Y N 18  
A1EK0 C26    C  Y N 19  
A1EK0 C27    C  Y N 20  
A1EK0 C28    C  Y N 21  
A1EK0 C29    C  Y N 22  
A1EK0 C30    C  Y N 23  
A1EK0 C31    C  Y N 24  
A1EK0 C32    C  Y N 25  
A1EK0 C33    C  Y N 26  
A1EK0 C6     C  N R 27  
A1EK0 N18    N  N N 28  
A1EK0 N34    N  N N 29  
A1EK0 N5     N  N N 30  
A1EK0 N9     N  N N 31  
A1EK0 O11    O  N N 32  
A1EK0 O17    O  N N 33  
A1EK0 O23    O  N N 34  
A1EK0 H1     H  N N 35  
A1EK0 H2     H  N N 36  
A1EK0 H3     H  N N 37  
A1EK0 H4     H  N N 38  
A1EK0 H5     H  N N 39  
A1EK0 H6     H  N N 40  
A1EK0 H7     H  N N 41  
A1EK0 H8     H  N N 42  
A1EK0 H9     H  N N 43  
A1EK0 H10    H  N N 44  
A1EK0 H11    H  N N 45  
A1EK0 H12    H  N N 46  
A1EK0 H13    H  N N 47  
A1EK0 H14    H  N N 48  
A1EK0 H15    H  N N 49  
A1EK0 H16    H  N N 50  
A1EK0 H17    H  N N 51  
A1EK0 H18    H  N N 52  
A1EK0 H19    H  N N 53  
A1EK0 H20    H  N N 54  
A1EK0 H21    H  N N 55  
A1EK0 H22    H  N N 56  
ALA   N      N  N N 57  
ALA   CA     C  N S 58  
ALA   C      C  N N 59  
ALA   O      O  N N 60  
ALA   CB     C  N N 61  
ALA   OXT    O  N N 62  
ALA   H      H  N N 63  
ALA   H2     H  N N 64  
ALA   HA     H  N N 65  
ALA   HB1    H  N N 66  
ALA   HB2    H  N N 67  
ALA   HB3    H  N N 68  
ALA   HXT    H  N N 69  
ARG   N      N  N N 70  
ARG   CA     C  N S 71  
ARG   C      C  N N 72  
ARG   O      O  N N 73  
ARG   CB     C  N N 74  
ARG   CG     C  N N 75  
ARG   CD     C  N N 76  
ARG   NE     N  N N 77  
ARG   CZ     C  N N 78  
ARG   NH1    N  N N 79  
ARG   NH2    N  N N 80  
ARG   OXT    O  N N 81  
ARG   H      H  N N 82  
ARG   H2     H  N N 83  
ARG   HA     H  N N 84  
ARG   HB2    H  N N 85  
ARG   HB3    H  N N 86  
ARG   HG2    H  N N 87  
ARG   HG3    H  N N 88  
ARG   HD2    H  N N 89  
ARG   HD3    H  N N 90  
ARG   HE     H  N N 91  
ARG   HH11   H  N N 92  
ARG   HH12   H  N N 93  
ARG   HH21   H  N N 94  
ARG   HH22   H  N N 95  
ARG   HXT    H  N N 96  
ASN   N      N  N N 97  
ASN   CA     C  N S 98  
ASN   C      C  N N 99  
ASN   O      O  N N 100 
ASN   CB     C  N N 101 
ASN   CG     C  N N 102 
ASN   OD1    O  N N 103 
ASN   ND2    N  N N 104 
ASN   OXT    O  N N 105 
ASN   H      H  N N 106 
ASN   H2     H  N N 107 
ASN   HA     H  N N 108 
ASN   HB2    H  N N 109 
ASN   HB3    H  N N 110 
ASN   HD21   H  N N 111 
ASN   HD22   H  N N 112 
ASN   HXT    H  N N 113 
ASP   N      N  N N 114 
ASP   CA     C  N S 115 
ASP   C      C  N N 116 
ASP   O      O  N N 117 
ASP   CB     C  N N 118 
ASP   CG     C  N N 119 
ASP   OD1    O  N N 120 
ASP   OD2    O  N N 121 
ASP   OXT    O  N N 122 
ASP   H      H  N N 123 
ASP   H2     H  N N 124 
ASP   HA     H  N N 125 
ASP   HB2    H  N N 126 
ASP   HB3    H  N N 127 
ASP   HD2    H  N N 128 
ASP   HXT    H  N N 129 
CLW   C1     C  Y N 130 
CLW   C2     C  Y N 131 
CLW   C3     C  Y N 132 
CLW   C4     C  Y N 133 
CLW   C5     C  Y N 134 
CLW   C6     C  Y N 135 
CLW   CL1    CL N N 136 
CLW   O1     O  Y N 137 
CLW   C7     C  Y N 138 
CLW   N1     N  Y N 139 
CLW   O2     O  N N 140 
CLW   H11    H  N N 141 
CLW   H21    H  N N 142 
CLW   H51    H  N N 143 
CLW   HN11   H  N N 144 
CYS   N      N  N N 145 
CYS   CA     C  N R 146 
CYS   C      C  N N 147 
CYS   O      O  N N 148 
CYS   CB     C  N N 149 
CYS   SG     S  N N 150 
CYS   OXT    O  N N 151 
CYS   H      H  N N 152 
CYS   H2     H  N N 153 
CYS   HA     H  N N 154 
CYS   HB2    H  N N 155 
CYS   HB3    H  N N 156 
CYS   HG     H  N N 157 
CYS   HXT    H  N N 158 
GLN   N      N  N N 159 
GLN   CA     C  N S 160 
GLN   C      C  N N 161 
GLN   O      O  N N 162 
GLN   CB     C  N N 163 
GLN   CG     C  N N 164 
GLN   CD     C  N N 165 
GLN   OE1    O  N N 166 
GLN   NE2    N  N N 167 
GLN   OXT    O  N N 168 
GLN   H      H  N N 169 
GLN   H2     H  N N 170 
GLN   HA     H  N N 171 
GLN   HB2    H  N N 172 
GLN   HB3    H  N N 173 
GLN   HG2    H  N N 174 
GLN   HG3    H  N N 175 
GLN   HE21   H  N N 176 
GLN   HE22   H  N N 177 
GLN   HXT    H  N N 178 
GLU   N      N  N N 179 
GLU   CA     C  N S 180 
GLU   C      C  N N 181 
GLU   O      O  N N 182 
GLU   CB     C  N N 183 
GLU   CG     C  N N 184 
GLU   CD     C  N N 185 
GLU   OE1    O  N N 186 
GLU   OE2    O  N N 187 
GLU   OXT    O  N N 188 
GLU   H      H  N N 189 
GLU   H2     H  N N 190 
GLU   HA     H  N N 191 
GLU   HB2    H  N N 192 
GLU   HB3    H  N N 193 
GLU   HG2    H  N N 194 
GLU   HG3    H  N N 195 
GLU   HE2    H  N N 196 
GLU   HXT    H  N N 197 
GLY   N      N  N N 198 
GLY   CA     C  N N 199 
GLY   C      C  N N 200 
GLY   O      O  N N 201 
GLY   OXT    O  N N 202 
GLY   H      H  N N 203 
GLY   H2     H  N N 204 
GLY   HA2    H  N N 205 
GLY   HA3    H  N N 206 
GLY   HXT    H  N N 207 
HIS   N      N  N N 208 
HIS   CA     C  N S 209 
HIS   C      C  N N 210 
HIS   O      O  N N 211 
HIS   CB     C  N N 212 
HIS   CG     C  Y N 213 
HIS   ND1    N  Y N 214 
HIS   CD2    C  Y N 215 
HIS   CE1    C  Y N 216 
HIS   NE2    N  Y N 217 
HIS   OXT    O  N N 218 
HIS   H      H  N N 219 
HIS   H2     H  N N 220 
HIS   HA     H  N N 221 
HIS   HB2    H  N N 222 
HIS   HB3    H  N N 223 
HIS   HD1    H  N N 224 
HIS   HD2    H  N N 225 
HIS   HE1    H  N N 226 
HIS   HE2    H  N N 227 
HIS   HXT    H  N N 228 
HOH   O      O  N N 229 
HOH   H1     H  N N 230 
HOH   H2     H  N N 231 
ILE   N      N  N N 232 
ILE   CA     C  N S 233 
ILE   C      C  N N 234 
ILE   O      O  N N 235 
ILE   CB     C  N S 236 
ILE   CG1    C  N N 237 
ILE   CG2    C  N N 238 
ILE   CD1    C  N N 239 
ILE   OXT    O  N N 240 
ILE   H      H  N N 241 
ILE   H2     H  N N 242 
ILE   HA     H  N N 243 
ILE   HB     H  N N 244 
ILE   HG12   H  N N 245 
ILE   HG13   H  N N 246 
ILE   HG21   H  N N 247 
ILE   HG22   H  N N 248 
ILE   HG23   H  N N 249 
ILE   HD11   H  N N 250 
ILE   HD12   H  N N 251 
ILE   HD13   H  N N 252 
ILE   HXT    H  N N 253 
LEU   N      N  N N 254 
LEU   CA     C  N S 255 
LEU   C      C  N N 256 
LEU   O      O  N N 257 
LEU   CB     C  N N 258 
LEU   CG     C  N N 259 
LEU   CD1    C  N N 260 
LEU   CD2    C  N N 261 
LEU   OXT    O  N N 262 
LEU   H      H  N N 263 
LEU   H2     H  N N 264 
LEU   HA     H  N N 265 
LEU   HB2    H  N N 266 
LEU   HB3    H  N N 267 
LEU   HG     H  N N 268 
LEU   HD11   H  N N 269 
LEU   HD12   H  N N 270 
LEU   HD13   H  N N 271 
LEU   HD21   H  N N 272 
LEU   HD22   H  N N 273 
LEU   HD23   H  N N 274 
LEU   HXT    H  N N 275 
LYS   N      N  N N 276 
LYS   CA     C  N S 277 
LYS   C      C  N N 278 
LYS   O      O  N N 279 
LYS   CB     C  N N 280 
LYS   CG     C  N N 281 
LYS   CD     C  N N 282 
LYS   CE     C  N N 283 
LYS   NZ     N  N N 284 
LYS   OXT    O  N N 285 
LYS   H      H  N N 286 
LYS   H2     H  N N 287 
LYS   HA     H  N N 288 
LYS   HB2    H  N N 289 
LYS   HB3    H  N N 290 
LYS   HG2    H  N N 291 
LYS   HG3    H  N N 292 
LYS   HD2    H  N N 293 
LYS   HD3    H  N N 294 
LYS   HE2    H  N N 295 
LYS   HE3    H  N N 296 
LYS   HZ1    H  N N 297 
LYS   HZ2    H  N N 298 
LYS   HZ3    H  N N 299 
LYS   HXT    H  N N 300 
MET   N      N  N N 301 
MET   CA     C  N S 302 
MET   C      C  N N 303 
MET   O      O  N N 304 
MET   CB     C  N N 305 
MET   CG     C  N N 306 
MET   SD     S  N N 307 
MET   CE     C  N N 308 
MET   OXT    O  N N 309 
MET   H      H  N N 310 
MET   H2     H  N N 311 
MET   HA     H  N N 312 
MET   HB2    H  N N 313 
MET   HB3    H  N N 314 
MET   HG2    H  N N 315 
MET   HG3    H  N N 316 
MET   HE1    H  N N 317 
MET   HE2    H  N N 318 
MET   HE3    H  N N 319 
MET   HXT    H  N N 320 
PHE   N      N  N N 321 
PHE   CA     C  N S 322 
PHE   C      C  N N 323 
PHE   O      O  N N 324 
PHE   CB     C  N N 325 
PHE   CG     C  Y N 326 
PHE   CD1    C  Y N 327 
PHE   CD2    C  Y N 328 
PHE   CE1    C  Y N 329 
PHE   CE2    C  Y N 330 
PHE   CZ     C  Y N 331 
PHE   OXT    O  N N 332 
PHE   H      H  N N 333 
PHE   H2     H  N N 334 
PHE   HA     H  N N 335 
PHE   HB2    H  N N 336 
PHE   HB3    H  N N 337 
PHE   HD1    H  N N 338 
PHE   HD2    H  N N 339 
PHE   HE1    H  N N 340 
PHE   HE2    H  N N 341 
PHE   HZ     H  N N 342 
PHE   HXT    H  N N 343 
PRO   N      N  N N 344 
PRO   CA     C  N S 345 
PRO   C      C  N N 346 
PRO   O      O  N N 347 
PRO   CB     C  N N 348 
PRO   CG     C  N N 349 
PRO   CD     C  N N 350 
PRO   OXT    O  N N 351 
PRO   H      H  N N 352 
PRO   HA     H  N N 353 
PRO   HB2    H  N N 354 
PRO   HB3    H  N N 355 
PRO   HG2    H  N N 356 
PRO   HG3    H  N N 357 
PRO   HD2    H  N N 358 
PRO   HD3    H  N N 359 
PRO   HXT    H  N N 360 
SER   N      N  N N 361 
SER   CA     C  N S 362 
SER   C      C  N N 363 
SER   O      O  N N 364 
SER   CB     C  N N 365 
SER   OG     O  N N 366 
SER   OXT    O  N N 367 
SER   H      H  N N 368 
SER   H2     H  N N 369 
SER   HA     H  N N 370 
SER   HB2    H  N N 371 
SER   HB3    H  N N 372 
SER   HG     H  N N 373 
SER   HXT    H  N N 374 
SO4   S      S  N N 375 
SO4   O1     O  N N 376 
SO4   O2     O  N N 377 
SO4   O3     O  N N 378 
SO4   O4     O  N N 379 
THR   N      N  N N 380 
THR   CA     C  N S 381 
THR   C      C  N N 382 
THR   O      O  N N 383 
THR   CB     C  N R 384 
THR   OG1    O  N N 385 
THR   CG2    C  N N 386 
THR   OXT    O  N N 387 
THR   H      H  N N 388 
THR   H2     H  N N 389 
THR   HA     H  N N 390 
THR   HB     H  N N 391 
THR   HG1    H  N N 392 
THR   HG21   H  N N 393 
THR   HG22   H  N N 394 
THR   HG23   H  N N 395 
THR   HXT    H  N N 396 
TRP   N      N  N N 397 
TRP   CA     C  N S 398 
TRP   C      C  N N 399 
TRP   O      O  N N 400 
TRP   CB     C  N N 401 
TRP   CG     C  Y N 402 
TRP   CD1    C  Y N 403 
TRP   CD2    C  Y N 404 
TRP   NE1    N  Y N 405 
TRP   CE2    C  Y N 406 
TRP   CE3    C  Y N 407 
TRP   CZ2    C  Y N 408 
TRP   CZ3    C  Y N 409 
TRP   CH2    C  Y N 410 
TRP   OXT    O  N N 411 
TRP   H      H  N N 412 
TRP   H2     H  N N 413 
TRP   HA     H  N N 414 
TRP   HB2    H  N N 415 
TRP   HB3    H  N N 416 
TRP   HD1    H  N N 417 
TRP   HE1    H  N N 418 
TRP   HE3    H  N N 419 
TRP   HZ2    H  N N 420 
TRP   HZ3    H  N N 421 
TRP   HH2    H  N N 422 
TRP   HXT    H  N N 423 
TYM   P      P  N R 424 
TYM   O1P    O  N N 425 
TYM   O2P    O  N N 426 
TYM   "O5'"  O  N N 427 
TYM   "C5'"  C  N N 428 
TYM   "C4'"  C  N R 429 
TYM   "O4'"  O  N N 430 
TYM   "C1'"  C  N R 431 
TYM   N9     N  Y N 432 
TYM   C4     C  Y N 433 
TYM   N3     N  Y N 434 
TYM   C2     C  Y N 435 
TYM   N1     N  Y N 436 
TYM   C6     C  Y N 437 
TYM   N6     N  N N 438 
TYM   C5     C  Y N 439 
TYM   N7     N  Y N 440 
TYM   C8     C  Y N 441 
TYM   "C2'"  C  N R 442 
TYM   "O2'"  O  N N 443 
TYM   "C3'"  C  N S 444 
TYM   "O3'"  O  N N 445 
TYM   NH3    N  N N 446 
TYM   CA     C  N S 447 
TYM   CB     C  N N 448 
TYM   CG     C  Y N 449 
TYM   CD2    C  Y N 450 
TYM   CE2    C  Y N 451 
TYM   CE3    C  Y N 452 
TYM   CD1    C  Y N 453 
TYM   NE1    N  Y N 454 
TYM   CZ2    C  Y N 455 
TYM   CZ3    C  Y N 456 
TYM   CH2    C  Y N 457 
TYM   C      C  N N 458 
TYM   O      O  N N 459 
TYM   OPP    O  N N 460 
TYM   H1PO   H  N N 461 
TYM   "H5'1" H  N N 462 
TYM   "H5'2" H  N N 463 
TYM   "H4'C" H  N N 464 
TYM   "H1'C" H  N N 465 
TYM   HC2    H  N N 466 
TYM   HN61   H  N N 467 
TYM   HN62   H  N N 468 
TYM   HC8    H  N N 469 
TYM   "H2'C" H  N N 470 
TYM   "H2'O" H  N N 471 
TYM   "H3'C" H  N N 472 
TYM   "H3'O" H  N N 473 
TYM   HH31   H  N N 474 
TYM   HH32   H  N N 475 
TYM   HCA    H  N N 476 
TYM   HCB1   H  N N 477 
TYM   HCB2   H  N N 478 
TYM   HE3C   H  N N 479 
TYM   HD1C   H  N N 480 
TYM   HE1N   H  N N 481 
TYM   HZ2C   H  N N 482 
TYM   HZ3C   H  N N 483 
TYM   HH2C   H  N N 484 
TYR   N      N  N N 485 
TYR   CA     C  N S 486 
TYR   C      C  N N 487 
TYR   O      O  N N 488 
TYR   CB     C  N N 489 
TYR   CG     C  Y N 490 
TYR   CD1    C  Y N 491 
TYR   CD2    C  Y N 492 
TYR   CE1    C  Y N 493 
TYR   CE2    C  Y N 494 
TYR   CZ     C  Y N 495 
TYR   OH     O  N N 496 
TYR   OXT    O  N N 497 
TYR   H      H  N N 498 
TYR   H2     H  N N 499 
TYR   HA     H  N N 500 
TYR   HB2    H  N N 501 
TYR   HB3    H  N N 502 
TYR   HD1    H  N N 503 
TYR   HD2    H  N N 504 
TYR   HE1    H  N N 505 
TYR   HE2    H  N N 506 
TYR   HH     H  N N 507 
TYR   HXT    H  N N 508 
VAL   N      N  N N 509 
VAL   CA     C  N S 510 
VAL   C      C  N N 511 
VAL   O      O  N N 512 
VAL   CB     C  N N 513 
VAL   CG1    C  N N 514 
VAL   CG2    C  N N 515 
VAL   OXT    O  N N 516 
VAL   H      H  N N 517 
VAL   H2     H  N N 518 
VAL   HA     H  N N 519 
VAL   HB     H  N N 520 
VAL   HG11   H  N N 521 
VAL   HG12   H  N N 522 
VAL   HG13   H  N N 523 
VAL   HG21   H  N N 524 
VAL   HG22   H  N N 525 
VAL   HG23   H  N N 526 
VAL   HXT    H  N N 527 
# 
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 
A1EK0 C7    C8     sing N N 1   
A1EK0 C7    C6     sing N N 2   
A1EK0 C8    N9     sing N N 3   
A1EK0 C2    N3     doub Y N 4   
A1EK0 C2    N1     sing Y N 5   
A1EK0 N3    C4     sing Y N 6   
A1EK0 N1    C33    doub Y N 7   
A1EK0 C6    N5     sing N N 8   
A1EK0 C6    C15    sing N N 9   
A1EK0 C4    N5     sing N N 10  
A1EK0 C4    C32    doub Y N 11  
A1EK0 C31   C30    doub Y N 12  
A1EK0 C31   C19    sing Y N 13  
A1EK0 C33   C32    sing Y N 14  
A1EK0 C33   N34    sing N N 15  
A1EK0 N5    C16    sing N N 16  
A1EK0 N9    C10    sing N N 17  
A1EK0 N9    C15    sing N N 18  
A1EK0 O11   C10    doub N N 19  
A1EK0 C32   N18    sing N N 20  
A1EK0 C30   C22    sing Y N 21  
A1EK0 C16   N18    sing N N 22  
A1EK0 C16   O17    doub N N 23  
A1EK0 N18   C19    sing N N 24  
A1EK0 C10   C12    sing N N 25  
A1EK0 C19   C20    doub Y N 26  
A1EK0 C22   O23    sing N N 27  
A1EK0 C22   C21    doub Y N 28  
A1EK0 O23   C24    sing N N 29  
A1EK0 C12   C13    trip N N 30  
A1EK0 C20   C21    sing Y N 31  
A1EK0 C25   C24    doub Y N 32  
A1EK0 C25   C26    sing Y N 33  
A1EK0 C24   C29    sing Y N 34  
A1EK0 C13   C14    sing N N 35  
A1EK0 C26   C27    doub Y N 36  
A1EK0 C29   C28    doub Y N 37  
A1EK0 C27   C28    sing Y N 38  
A1EK0 C2    H1     sing N N 39  
A1EK0 C7    H2     sing N N 40  
A1EK0 C7    H3     sing N N 41  
A1EK0 C8    H4     sing N N 42  
A1EK0 C8    H5     sing N N 43  
A1EK0 C14   H6     sing N N 44  
A1EK0 C14   H7     sing N N 45  
A1EK0 C14   H8     sing N N 46  
A1EK0 C15   H9     sing N N 47  
A1EK0 C15   H10    sing N N 48  
A1EK0 C20   H11    sing N N 49  
A1EK0 C21   H12    sing N N 50  
A1EK0 C25   H13    sing N N 51  
A1EK0 C26   H14    sing N N 52  
A1EK0 C27   H15    sing N N 53  
A1EK0 C28   H16    sing N N 54  
A1EK0 C29   H17    sing N N 55  
A1EK0 C30   H18    sing N N 56  
A1EK0 C31   H19    sing N N 57  
A1EK0 C6    H20    sing N N 58  
A1EK0 N34   H21    sing N N 59  
A1EK0 N34   H22    sing N N 60  
ALA   N     CA     sing N N 61  
ALA   N     H      sing N N 62  
ALA   N     H2     sing N N 63  
ALA   CA    C      sing N N 64  
ALA   CA    CB     sing N N 65  
ALA   CA    HA     sing N N 66  
ALA   C     O      doub N N 67  
ALA   C     OXT    sing N N 68  
ALA   CB    HB1    sing N N 69  
ALA   CB    HB2    sing N N 70  
ALA   CB    HB3    sing N N 71  
ALA   OXT   HXT    sing N N 72  
ARG   N     CA     sing N N 73  
ARG   N     H      sing N N 74  
ARG   N     H2     sing N N 75  
ARG   CA    C      sing N N 76  
ARG   CA    CB     sing N N 77  
ARG   CA    HA     sing N N 78  
ARG   C     O      doub N N 79  
ARG   C     OXT    sing N N 80  
ARG   CB    CG     sing N N 81  
ARG   CB    HB2    sing N N 82  
ARG   CB    HB3    sing N N 83  
ARG   CG    CD     sing N N 84  
ARG   CG    HG2    sing N N 85  
ARG   CG    HG3    sing N N 86  
ARG   CD    NE     sing N N 87  
ARG   CD    HD2    sing N N 88  
ARG   CD    HD3    sing N N 89  
ARG   NE    CZ     sing N N 90  
ARG   NE    HE     sing N N 91  
ARG   CZ    NH1    sing N N 92  
ARG   CZ    NH2    doub N N 93  
ARG   NH1   HH11   sing N N 94  
ARG   NH1   HH12   sing N N 95  
ARG   NH2   HH21   sing N N 96  
ARG   NH2   HH22   sing N N 97  
ARG   OXT   HXT    sing N N 98  
ASN   N     CA     sing N N 99  
ASN   N     H      sing N N 100 
ASN   N     H2     sing N N 101 
ASN   CA    C      sing N N 102 
ASN   CA    CB     sing N N 103 
ASN   CA    HA     sing N N 104 
ASN   C     O      doub N N 105 
ASN   C     OXT    sing N N 106 
ASN   CB    CG     sing N N 107 
ASN   CB    HB2    sing N N 108 
ASN   CB    HB3    sing N N 109 
ASN   CG    OD1    doub N N 110 
ASN   CG    ND2    sing N N 111 
ASN   ND2   HD21   sing N N 112 
ASN   ND2   HD22   sing N N 113 
ASN   OXT   HXT    sing N N 114 
ASP   N     CA     sing N N 115 
ASP   N     H      sing N N 116 
ASP   N     H2     sing N N 117 
ASP   CA    C      sing N N 118 
ASP   CA    CB     sing N N 119 
ASP   CA    HA     sing N N 120 
ASP   C     O      doub N N 121 
ASP   C     OXT    sing N N 122 
ASP   CB    CG     sing N N 123 
ASP   CB    HB2    sing N N 124 
ASP   CB    HB3    sing N N 125 
ASP   CG    OD1    doub N N 126 
ASP   CG    OD2    sing N N 127 
ASP   OD2   HD2    sing N N 128 
ASP   OXT   HXT    sing N N 129 
CLW   C1    C2     doub Y N 130 
CLW   C1    C6     sing Y N 131 
CLW   C1    H11    sing N N 132 
CLW   C2    C3     sing Y N 133 
CLW   C2    H21    sing N N 134 
CLW   C3    C4     doub Y N 135 
CLW   C3    O1     sing Y N 136 
CLW   C4    C5     sing Y N 137 
CLW   C4    N1     sing Y N 138 
CLW   C5    C6     doub Y N 139 
CLW   C5    H51    sing N N 140 
CLW   C6    CL1    sing N N 141 
CLW   O1    C7     sing Y N 142 
CLW   C7    N1     sing Y N 143 
CLW   C7    O2     doub N N 144 
CLW   N1    HN11   sing N N 145 
CYS   N     CA     sing N N 146 
CYS   N     H      sing N N 147 
CYS   N     H2     sing N N 148 
CYS   CA    C      sing N N 149 
CYS   CA    CB     sing N N 150 
CYS   CA    HA     sing N N 151 
CYS   C     O      doub N N 152 
CYS   C     OXT    sing N N 153 
CYS   CB    SG     sing N N 154 
CYS   CB    HB2    sing N N 155 
CYS   CB    HB3    sing N N 156 
CYS   SG    HG     sing N N 157 
CYS   OXT   HXT    sing N N 158 
GLN   N     CA     sing N N 159 
GLN   N     H      sing N N 160 
GLN   N     H2     sing N N 161 
GLN   CA    C      sing N N 162 
GLN   CA    CB     sing N N 163 
GLN   CA    HA     sing N N 164 
GLN   C     O      doub N N 165 
GLN   C     OXT    sing N N 166 
GLN   CB    CG     sing N N 167 
GLN   CB    HB2    sing N N 168 
GLN   CB    HB3    sing N N 169 
GLN   CG    CD     sing N N 170 
GLN   CG    HG2    sing N N 171 
GLN   CG    HG3    sing N N 172 
GLN   CD    OE1    doub N N 173 
GLN   CD    NE2    sing N N 174 
GLN   NE2   HE21   sing N N 175 
GLN   NE2   HE22   sing N N 176 
GLN   OXT   HXT    sing N N 177 
GLU   N     CA     sing N N 178 
GLU   N     H      sing N N 179 
GLU   N     H2     sing N N 180 
GLU   CA    C      sing N N 181 
GLU   CA    CB     sing N N 182 
GLU   CA    HA     sing N N 183 
GLU   C     O      doub N N 184 
GLU   C     OXT    sing N N 185 
GLU   CB    CG     sing N N 186 
GLU   CB    HB2    sing N N 187 
GLU   CB    HB3    sing N N 188 
GLU   CG    CD     sing N N 189 
GLU   CG    HG2    sing N N 190 
GLU   CG    HG3    sing N N 191 
GLU   CD    OE1    doub N N 192 
GLU   CD    OE2    sing N N 193 
GLU   OE2   HE2    sing N N 194 
GLU   OXT   HXT    sing N N 195 
GLY   N     CA     sing N N 196 
GLY   N     H      sing N N 197 
GLY   N     H2     sing N N 198 
GLY   CA    C      sing N N 199 
GLY   CA    HA2    sing N N 200 
GLY   CA    HA3    sing N N 201 
GLY   C     O      doub N N 202 
GLY   C     OXT    sing N N 203 
GLY   OXT   HXT    sing N N 204 
HIS   N     CA     sing N N 205 
HIS   N     H      sing N N 206 
HIS   N     H2     sing N N 207 
HIS   CA    C      sing N N 208 
HIS   CA    CB     sing N N 209 
HIS   CA    HA     sing N N 210 
HIS   C     O      doub N N 211 
HIS   C     OXT    sing N N 212 
HIS   CB    CG     sing N N 213 
HIS   CB    HB2    sing N N 214 
HIS   CB    HB3    sing N N 215 
HIS   CG    ND1    sing Y N 216 
HIS   CG    CD2    doub Y N 217 
HIS   ND1   CE1    doub Y N 218 
HIS   ND1   HD1    sing N N 219 
HIS   CD2   NE2    sing Y N 220 
HIS   CD2   HD2    sing N N 221 
HIS   CE1   NE2    sing Y N 222 
HIS   CE1   HE1    sing N N 223 
HIS   NE2   HE2    sing N N 224 
HIS   OXT   HXT    sing N N 225 
HOH   O     H1     sing N N 226 
HOH   O     H2     sing N N 227 
ILE   N     CA     sing N N 228 
ILE   N     H      sing N N 229 
ILE   N     H2     sing N N 230 
ILE   CA    C      sing N N 231 
ILE   CA    CB     sing N N 232 
ILE   CA    HA     sing N N 233 
ILE   C     O      doub N N 234 
ILE   C     OXT    sing N N 235 
ILE   CB    CG1    sing N N 236 
ILE   CB    CG2    sing N N 237 
ILE   CB    HB     sing N N 238 
ILE   CG1   CD1    sing N N 239 
ILE   CG1   HG12   sing N N 240 
ILE   CG1   HG13   sing N N 241 
ILE   CG2   HG21   sing N N 242 
ILE   CG2   HG22   sing N N 243 
ILE   CG2   HG23   sing N N 244 
ILE   CD1   HD11   sing N N 245 
ILE   CD1   HD12   sing N N 246 
ILE   CD1   HD13   sing N N 247 
ILE   OXT   HXT    sing N N 248 
LEU   N     CA     sing N N 249 
LEU   N     H      sing N N 250 
LEU   N     H2     sing N N 251 
LEU   CA    C      sing N N 252 
LEU   CA    CB     sing N N 253 
LEU   CA    HA     sing N N 254 
LEU   C     O      doub N N 255 
LEU   C     OXT    sing N N 256 
LEU   CB    CG     sing N N 257 
LEU   CB    HB2    sing N N 258 
LEU   CB    HB3    sing N N 259 
LEU   CG    CD1    sing N N 260 
LEU   CG    CD2    sing N N 261 
LEU   CG    HG     sing N N 262 
LEU   CD1   HD11   sing N N 263 
LEU   CD1   HD12   sing N N 264 
LEU   CD1   HD13   sing N N 265 
LEU   CD2   HD21   sing N N 266 
LEU   CD2   HD22   sing N N 267 
LEU   CD2   HD23   sing N N 268 
LEU   OXT   HXT    sing N N 269 
LYS   N     CA     sing N N 270 
LYS   N     H      sing N N 271 
LYS   N     H2     sing N N 272 
LYS   CA    C      sing N N 273 
LYS   CA    CB     sing N N 274 
LYS   CA    HA     sing N N 275 
LYS   C     O      doub N N 276 
LYS   C     OXT    sing N N 277 
LYS   CB    CG     sing N N 278 
LYS   CB    HB2    sing N N 279 
LYS   CB    HB3    sing N N 280 
LYS   CG    CD     sing N N 281 
LYS   CG    HG2    sing N N 282 
LYS   CG    HG3    sing N N 283 
LYS   CD    CE     sing N N 284 
LYS   CD    HD2    sing N N 285 
LYS   CD    HD3    sing N N 286 
LYS   CE    NZ     sing N N 287 
LYS   CE    HE2    sing N N 288 
LYS   CE    HE3    sing N N 289 
LYS   NZ    HZ1    sing N N 290 
LYS   NZ    HZ2    sing N N 291 
LYS   NZ    HZ3    sing N N 292 
LYS   OXT   HXT    sing N N 293 
MET   N     CA     sing N N 294 
MET   N     H      sing N N 295 
MET   N     H2     sing N N 296 
MET   CA    C      sing N N 297 
MET   CA    CB     sing N N 298 
MET   CA    HA     sing N N 299 
MET   C     O      doub N N 300 
MET   C     OXT    sing N N 301 
MET   CB    CG     sing N N 302 
MET   CB    HB2    sing N N 303 
MET   CB    HB3    sing N N 304 
MET   CG    SD     sing N N 305 
MET   CG    HG2    sing N N 306 
MET   CG    HG3    sing N N 307 
MET   SD    CE     sing N N 308 
MET   CE    HE1    sing N N 309 
MET   CE    HE2    sing N N 310 
MET   CE    HE3    sing N N 311 
MET   OXT   HXT    sing N N 312 
PHE   N     CA     sing N N 313 
PHE   N     H      sing N N 314 
PHE   N     H2     sing N N 315 
PHE   CA    C      sing N N 316 
PHE   CA    CB     sing N N 317 
PHE   CA    HA     sing N N 318 
PHE   C     O      doub N N 319 
PHE   C     OXT    sing N N 320 
PHE   CB    CG     sing N N 321 
PHE   CB    HB2    sing N N 322 
PHE   CB    HB3    sing N N 323 
PHE   CG    CD1    doub Y N 324 
PHE   CG    CD2    sing Y N 325 
PHE   CD1   CE1    sing Y N 326 
PHE   CD1   HD1    sing N N 327 
PHE   CD2   CE2    doub Y N 328 
PHE   CD2   HD2    sing N N 329 
PHE   CE1   CZ     doub Y N 330 
PHE   CE1   HE1    sing N N 331 
PHE   CE2   CZ     sing Y N 332 
PHE   CE2   HE2    sing N N 333 
PHE   CZ    HZ     sing N N 334 
PHE   OXT   HXT    sing N N 335 
PRO   N     CA     sing N N 336 
PRO   N     CD     sing N N 337 
PRO   N     H      sing N N 338 
PRO   CA    C      sing N N 339 
PRO   CA    CB     sing N N 340 
PRO   CA    HA     sing N N 341 
PRO   C     O      doub N N 342 
PRO   C     OXT    sing N N 343 
PRO   CB    CG     sing N N 344 
PRO   CB    HB2    sing N N 345 
PRO   CB    HB3    sing N N 346 
PRO   CG    CD     sing N N 347 
PRO   CG    HG2    sing N N 348 
PRO   CG    HG3    sing N N 349 
PRO   CD    HD2    sing N N 350 
PRO   CD    HD3    sing N N 351 
PRO   OXT   HXT    sing N N 352 
SER   N     CA     sing N N 353 
SER   N     H      sing N N 354 
SER   N     H2     sing N N 355 
SER   CA    C      sing N N 356 
SER   CA    CB     sing N N 357 
SER   CA    HA     sing N N 358 
SER   C     O      doub N N 359 
SER   C     OXT    sing N N 360 
SER   CB    OG     sing N N 361 
SER   CB    HB2    sing N N 362 
SER   CB    HB3    sing N N 363 
SER   OG    HG     sing N N 364 
SER   OXT   HXT    sing N N 365 
SO4   S     O1     doub N N 366 
SO4   S     O2     doub N N 367 
SO4   S     O3     sing N N 368 
SO4   S     O4     sing N N 369 
THR   N     CA     sing N N 370 
THR   N     H      sing N N 371 
THR   N     H2     sing N N 372 
THR   CA    C      sing N N 373 
THR   CA    CB     sing N N 374 
THR   CA    HA     sing N N 375 
THR   C     O      doub N N 376 
THR   C     OXT    sing N N 377 
THR   CB    OG1    sing N N 378 
THR   CB    CG2    sing N N 379 
THR   CB    HB     sing N N 380 
THR   OG1   HG1    sing N N 381 
THR   CG2   HG21   sing N N 382 
THR   CG2   HG22   sing N N 383 
THR   CG2   HG23   sing N N 384 
THR   OXT   HXT    sing N N 385 
TRP   N     CA     sing N N 386 
TRP   N     H      sing N N 387 
TRP   N     H2     sing N N 388 
TRP   CA    C      sing N N 389 
TRP   CA    CB     sing N N 390 
TRP   CA    HA     sing N N 391 
TRP   C     O      doub N N 392 
TRP   C     OXT    sing N N 393 
TRP   CB    CG     sing N N 394 
TRP   CB    HB2    sing N N 395 
TRP   CB    HB3    sing N N 396 
TRP   CG    CD1    doub Y N 397 
TRP   CG    CD2    sing Y N 398 
TRP   CD1   NE1    sing Y N 399 
TRP   CD1   HD1    sing N N 400 
TRP   CD2   CE2    doub Y N 401 
TRP   CD2   CE3    sing Y N 402 
TRP   NE1   CE2    sing Y N 403 
TRP   NE1   HE1    sing N N 404 
TRP   CE2   CZ2    sing Y N 405 
TRP   CE3   CZ3    doub Y N 406 
TRP   CE3   HE3    sing N N 407 
TRP   CZ2   CH2    doub Y N 408 
TRP   CZ2   HZ2    sing N N 409 
TRP   CZ3   CH2    sing Y N 410 
TRP   CZ3   HZ3    sing N N 411 
TRP   CH2   HH2    sing N N 412 
TRP   OXT   HXT    sing N N 413 
TYM   P     O1P    sing N N 414 
TYM   P     O2P    doub N N 415 
TYM   P     "O5'"  sing N N 416 
TYM   P     OPP    sing N N 417 
TYM   O1P   H1PO   sing N N 418 
TYM   "O5'" "C5'"  sing N N 419 
TYM   "C5'" "C4'"  sing N N 420 
TYM   "C5'" "H5'1" sing N N 421 
TYM   "C5'" "H5'2" sing N N 422 
TYM   "C4'" "O4'"  sing N N 423 
TYM   "C4'" "C3'"  sing N N 424 
TYM   "C4'" "H4'C" sing N N 425 
TYM   "O4'" "C1'"  sing N N 426 
TYM   "C1'" N9     sing N N 427 
TYM   "C1'" "C2'"  sing N N 428 
TYM   "C1'" "H1'C" sing N N 429 
TYM   N9    C4     sing Y N 430 
TYM   N9    C8     sing Y N 431 
TYM   C4    N3     doub Y N 432 
TYM   C4    C5     sing Y N 433 
TYM   N3    C2     sing Y N 434 
TYM   C2    N1     doub Y N 435 
TYM   C2    HC2    sing N N 436 
TYM   N1    C6     sing Y N 437 
TYM   C6    N6     sing N N 438 
TYM   C6    C5     doub Y N 439 
TYM   N6    HN61   sing N N 440 
TYM   N6    HN62   sing N N 441 
TYM   C5    N7     sing Y N 442 
TYM   N7    C8     doub Y N 443 
TYM   C8    HC8    sing N N 444 
TYM   "C2'" "O2'"  sing N N 445 
TYM   "C2'" "C3'"  sing N N 446 
TYM   "C2'" "H2'C" sing N N 447 
TYM   "O2'" "H2'O" sing N N 448 
TYM   "C3'" "O3'"  sing N N 449 
TYM   "C3'" "H3'C" sing N N 450 
TYM   "O3'" "H3'O" sing N N 451 
TYM   NH3   CA     sing N N 452 
TYM   NH3   HH31   sing N N 453 
TYM   NH3   HH32   sing N N 454 
TYM   CA    CB     sing N N 455 
TYM   CA    C      sing N N 456 
TYM   CA    HCA    sing N N 457 
TYM   CB    CG     sing N N 458 
TYM   CB    HCB1   sing N N 459 
TYM   CB    HCB2   sing N N 460 
TYM   CG    CD2    sing Y N 461 
TYM   CG    CD1    doub Y N 462 
TYM   CD2   CE2    doub Y N 463 
TYM   CD2   CE3    sing Y N 464 
TYM   CE2   NE1    sing Y N 465 
TYM   CE2   CZ2    sing Y N 466 
TYM   CE3   CZ3    doub Y N 467 
TYM   CE3   HE3C   sing N N 468 
TYM   CD1   NE1    sing Y N 469 
TYM   CD1   HD1C   sing N N 470 
TYM   NE1   HE1N   sing N N 471 
TYM   CZ2   CH2    doub Y N 472 
TYM   CZ2   HZ2C   sing N N 473 
TYM   CZ3   CH2    sing Y N 474 
TYM   CZ3   HZ3C   sing N N 475 
TYM   CH2   HH2C   sing N N 476 
TYM   C     O      doub N N 477 
TYM   C     OPP    sing N N 478 
TYR   N     CA     sing N N 479 
TYR   N     H      sing N N 480 
TYR   N     H2     sing N N 481 
TYR   CA    C      sing N N 482 
TYR   CA    CB     sing N N 483 
TYR   CA    HA     sing N N 484 
TYR   C     O      doub N N 485 
TYR   C     OXT    sing N N 486 
TYR   CB    CG     sing N N 487 
TYR   CB    HB2    sing N N 488 
TYR   CB    HB3    sing N N 489 
TYR   CG    CD1    doub Y N 490 
TYR   CG    CD2    sing Y N 491 
TYR   CD1   CE1    sing Y N 492 
TYR   CD1   HD1    sing N N 493 
TYR   CD2   CE2    doub Y N 494 
TYR   CD2   HD2    sing N N 495 
TYR   CE1   CZ     doub Y N 496 
TYR   CE1   HE1    sing N N 497 
TYR   CE2   CZ     sing Y N 498 
TYR   CE2   HE2    sing N N 499 
TYR   CZ    OH     sing N N 500 
TYR   OH    HH     sing N N 501 
TYR   OXT   HXT    sing N N 502 
VAL   N     CA     sing N N 503 
VAL   N     H      sing N N 504 
VAL   N     H2     sing N N 505 
VAL   CA    C      sing N N 506 
VAL   CA    CB     sing N N 507 
VAL   CA    HA     sing N N 508 
VAL   C     O      doub N N 509 
VAL   C     OXT    sing N N 510 
VAL   CB    CG1    sing N N 511 
VAL   CB    CG2    sing N N 512 
VAL   CB    HB     sing N N 513 
VAL   CG1   HG11   sing N N 514 
VAL   CG1   HG12   sing N N 515 
VAL   CG1   HG13   sing N N 516 
VAL   CG2   HG21   sing N N 517 
VAL   CG2   HG22   sing N N 518 
VAL   CG2   HG23   sing N N 519 
VAL   OXT   HXT    sing N N 520 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           22177140 
_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   8I1Y 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9LPD 
_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]   0.016188 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004554 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012589 
_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]   0.013104 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . LYS   A 1 3   ? 35.806  -15.682 13.018  1.00 53.00  ?  3   LYS   A N     1 
ATOM   2    C  CA    . LYS   A 1 3   ? 35.797  -15.076 11.646  1.00 47.36  ?  3   LYS   A CA    1 
ATOM   3    C  C     . LYS   A 1 3   ? 34.858  -13.868 11.582  1.00 41.17  ?  3   LYS   A C     1 
ATOM   4    O  O     . LYS   A 1 3   ? 33.669  -14.008 11.803  1.00 40.14  ?  3   LYS   A O     1 
ATOM   5    C  CB    . LYS   A 1 3   ? 35.371  -16.114 10.603  1.00 51.52  ?  3   LYS   A CB    1 
ATOM   6    C  CG    . LYS   A 1 3   ? 35.410  -15.604 9.175   1.00 50.53  ?  3   LYS   A CG    1 
ATOM   7    C  CD    . LYS   A 1 3   ? 35.028  -16.671 8.168   1.00 53.52  ?  3   LYS   A CD    1 
ATOM   8    C  CE    . LYS   A 1 3   ? 36.119  -17.706 7.988   1.00 56.45  ?  3   LYS   A CE    1 
ATOM   9    N  NZ    . LYS   A 1 3   ? 35.820  -18.551 6.801   1.00 59.49  ?  3   LYS   A NZ    1 
ATOM   10   N  N     . PRO   A 1 4   ? 35.386  -12.680 11.268  1.00 35.78  ?  4   PRO   A N     1 
ATOM   11   C  CA    . PRO   A 1 4   ? 34.533  -11.507 11.246  1.00 33.00  ?  4   PRO   A CA    1 
ATOM   12   C  C     . PRO   A 1 4   ? 33.444  -11.537 10.170  1.00 31.87  ?  4   PRO   A C     1 
ATOM   13   O  O     . PRO   A 1 4   ? 33.703  -11.966 9.031   1.00 31.24  ?  4   PRO   A O     1 
ATOM   14   C  CB    . PRO   A 1 4   ? 35.508  -10.353 10.981  1.00 36.26  ?  4   PRO   A CB    1 
ATOM   15   C  CG    . PRO   A 1 4   ? 36.843  -10.862 11.414  1.00 36.72  ?  4   PRO   A CG    1 
ATOM   16   C  CD    . PRO   A 1 4   ? 36.810  -12.328 11.107  1.00 37.58  ?  4   PRO   A CD    1 
ATOM   17   N  N     . ILE   A 1 5   ? 32.246  -11.091 10.547  1.00 26.49  ?  5   ILE   A N     1 
ATOM   18   C  CA    . ILE   A 1 5   ? 31.086  -10.986 9.647   1.00 25.79  ?  5   ILE   A CA    1 
ATOM   19   C  C     . ILE   A 1 5   ? 31.145  -9.646  8.923   1.00 25.08  ?  5   ILE   A C     1 
ATOM   20   O  O     . ILE   A 1 5   ? 31.206  -8.582  9.575   1.00 23.23  ?  5   ILE   A O     1 
ATOM   21   C  CB    . ILE   A 1 5   ? 29.763  -11.161 10.418  1.00 26.31  ?  5   ILE   A CB    1 
ATOM   22   C  CG1   . ILE   A 1 5   ? 29.666  -12.617 10.961  1.00 26.74  ?  5   ILE   A CG1   1 
ATOM   23   C  CG2   . ILE   A 1 5   ? 28.562  -10.834 9.545   1.00 25.88  ?  5   ILE   A CG2   1 
ATOM   24   C  CD1   . ILE   A 1 5   ? 28.650  -12.799 12.036  1.00 26.54  ?  5   ILE   A CD1   1 
ATOM   25   N  N     . VAL   A 1 6   ? 31.170  -9.694  7.579   1.00 24.58  ?  6   VAL   A N     1 
ATOM   26   C  CA    . VAL   A 1 6   ? 31.187  -8.477  6.751   1.00 29.02  ?  6   VAL   A CA    1 
ATOM   27   C  C     . VAL   A 1 6   ? 29.818  -8.350  6.093   1.00 28.88  ?  6   VAL   A C     1 
ATOM   28   O  O     . VAL   A 1 6   ? 29.310  -9.323  5.564   1.00 31.28  ?  6   VAL   A O     1 
ATOM   29   C  CB    . VAL   A 1 6   ? 32.315  -8.546  5.694   1.00 33.31  ?  6   VAL   A CB    1 
ATOM   30   C  CG1   . VAL   A 1 6   ? 32.389  -7.281  4.859   1.00 35.53  ?  6   VAL   A CG1   1 
ATOM   31   C  CG2   . VAL   A 1 6   ? 33.665  -8.749  6.372   1.00 33.40  ?  6   VAL   A CG2   1 
ATOM   32   N  N     . PHE   A 1 7   ? 29.220  -7.169  6.153   1.00 27.33  ?  7   PHE   A N     1 
ATOM   33   C  CA    . PHE   A 1 7   ? 27.935  -6.890  5.489   1.00 28.71  ?  7   PHE   A CA    1 
ATOM   34   C  C     . PHE   A 1 7   ? 28.068  -5.803  4.423   1.00 28.42  ?  7   PHE   A C     1 
ATOM   35   O  O     . PHE   A 1 7   ? 28.592  -4.701  4.695   1.00 28.07  ?  7   PHE   A O     1 
ATOM   36   C  CB    . PHE   A 1 7   ? 26.881  -6.480  6.534   1.00 28.77  ?  7   PHE   A CB    1 
ATOM   37   C  CG    . PHE   A 1 7   ? 25.497  -6.406  5.985   1.00 28.94  ?  7   PHE   A CG    1 
ATOM   38   C  CD1   . PHE   A 1 7   ? 25.045  -5.247  5.330   1.00 29.29  ?  7   PHE   A CD1   1 
ATOM   39   C  CD2   . PHE   A 1 7   ? 24.640  -7.489  6.104   1.00 26.49  ?  7   PHE   A CD2   1 
ATOM   40   C  CE1   . PHE   A 1 7   ? 23.758  -5.193  4.818   1.00 29.27  ?  7   PHE   A CE1   1 
ATOM   41   C  CE2   . PHE   A 1 7   ? 23.352  -7.422  5.590   1.00 26.50  ?  7   PHE   A CE2   1 
ATOM   42   C  CZ    . PHE   A 1 7   ? 22.911  -6.296  4.948   1.00 25.44  ?  7   PHE   A CZ    1 
ATOM   43   N  N     . SER   A 1 8   ? 27.568  -6.105  3.233   1.00 30.91  ?  8   SER   A N     1 
ATOM   44   C  CA    . SER   A 1 8   ? 27.529  -5.178  2.079   1.00 31.85  ?  8   SER   A CA    1 
ATOM   45   C  C     . SER   A 1 8   ? 26.114  -5.133  1.503   1.00 30.83  ?  8   SER   A C     1 
ATOM   46   O  O     . SER   A 1 8   ? 25.490  -6.176  1.300   1.00 30.35  ?  8   SER   A O     1 
ATOM   47   C  CB    . SER   A 1 8   ? 28.479  -5.663  0.968   1.00 32.75  ?  8   SER   A CB    1 
ATOM   48   O  OG    . SER   A 1 8   ? 29.783  -5.887  1.461   1.00 37.48  ?  8   SER   A OG    1 
ATOM   49   N  N     . GLY   A 1 9   ? 25.636  -3.914  1.230   1.00 33.20  ?  9   GLY   A N     1 
ATOM   50   C  CA    . GLY   A 1 9   ? 24.385  -3.673  0.511   1.00 33.60  ?  9   GLY   A CA    1 
ATOM   51   C  C     . GLY   A 1 9   ? 24.654  -3.336  -0.955  1.00 37.72  ?  9   GLY   A C     1 
ATOM   52   O  O     . GLY   A 1 9   ? 25.322  -2.340  -1.270  1.00 43.09  ?  9   GLY   A O     1 
ATOM   53   N  N     . ALA   A 1 10  ? 24.117  -4.149  -1.855  1.00 37.48  ?  10  ALA   A N     1 
ATOM   54   C  CA    . ALA   A 1 10  ? 24.226  -3.931  -3.294  1.00 37.33  ?  10  ALA   A CA    1 
ATOM   55   C  C     . ALA   A 1 10  ? 22.884  -3.492  -3.872  1.00 41.12  ?  10  ALA   A C     1 
ATOM   56   O  O     . ALA   A 1 10  ? 21.973  -4.300  -4.006  1.00 37.11  ?  10  ALA   A O     1 
ATOM   57   C  CB    . ALA   A 1 10  ? 24.705  -5.204  -3.965  1.00 36.18  ?  10  ALA   A CB    1 
ATOM   58   N  N     . GLN   A 1 11  ? 22.790  -2.232  -4.274  1.00 40.74  ?  11  GLN   A N     1 
ATOM   59   C  CA    . GLN   A 1 11  ? 21.536  -1.645  -4.706  1.00 44.91  ?  11  GLN   A CA    1 
ATOM   60   C  C     . GLN   A 1 11  ? 21.136  -2.217  -6.074  1.00 50.35  ?  11  GLN   A C     1 
ATOM   61   O  O     . GLN   A 1 11  ? 21.922  -2.084  -7.001  1.00 44.60  ?  11  GLN   A O     1 
ATOM   62   C  CB    . GLN   A 1 11  ? 21.725  -0.127  -4.760  1.00 46.27  ?  11  GLN   A CB    1 
ATOM   63   C  CG    . GLN   A 1 11  ? 22.107  0.430   -3.388  1.00 45.63  ?  11  GLN   A CG    1 
ATOM   64   C  CD    . GLN   A 1 11  ? 22.379  1.918   -3.345  1.00 52.24  ?  11  GLN   A CD    1 
ATOM   65   O  OE1   . GLN   A 1 11  ? 23.339  2.360   -2.707  1.00 52.62  ?  11  GLN   A OE1   1 
ATOM   66   N  NE2   . GLN   A 1 11  ? 21.524  2.706   -3.989  1.00 54.45  ?  11  GLN   A NE2   1 
ATOM   67   N  N     . PRO   A 1 12  ? 19.937  -2.859  -6.200  1.00 51.74  ?  12  PRO   A N     1 
ATOM   68   C  CA    . PRO   A 1 12  ? 19.610  -3.600  -7.428  1.00 58.75  ?  12  PRO   A CA    1 
ATOM   69   C  C     . PRO   A 1 12  ? 19.723  -2.746  -8.688  1.00 64.03  ?  12  PRO   A C     1 
ATOM   70   O  O     . PRO   A 1 12  ? 19.937  -3.281  -9.773  1.00 77.85  ?  12  PRO   A O     1 
ATOM   71   C  CB    . PRO   A 1 12  ? 18.163  -4.073  -7.206  1.00 54.32  ?  12  PRO   A CB    1 
ATOM   72   C  CG    . PRO   A 1 12  ? 17.635  -3.186  -6.151  1.00 53.00  ?  12  PRO   A CG    1 
ATOM   73   C  CD    . PRO   A 1 12  ? 18.808  -2.902  -5.260  1.00 53.96  ?  12  PRO   A CD    1 
ATOM   74   N  N     . SER   A 1 13  ? 19.621  -1.430  -8.539  1.00 65.81  ?  13  SER   A N     1 
ATOM   75   C  CA    . SER   A 1 13  ? 19.803  -0.499  -9.658  1.00 71.23  ?  13  SER   A CA    1 
ATOM   76   C  C     . SER   A 1 13  ? 21.258  -0.039  -9.854  1.00 76.42  ?  13  SER   A C     1 
ATOM   77   O  O     . SER   A 1 13  ? 22.115  -0.286  -9.018  1.00 90.24  ?  13  SER   A O     1 
ATOM   78   C  CB    . SER   A 1 13  ? 18.902  0.707   -9.420  1.00 74.59  ?  13  SER   A CB    1 
ATOM   79   O  OG    . SER   A 1 13  ? 18.894  1.576   -10.533 1.00 80.63  ?  13  SER   A OG    1 
ATOM   80   N  N     . GLY   A 1 14  ? 21.524  0.644   -10.962 1.00 76.84  ?  14  GLY   A N     1 
ATOM   81   C  CA    . GLY   A 1 14  ? 22.876  1.122   -11.288 1.00 79.23  ?  14  GLY   A CA    1 
ATOM   82   C  C     . GLY   A 1 14  ? 23.699  0.065   -12.011 1.00 79.52  ?  14  GLY   A C     1 
ATOM   83   O  O     . GLY   A 1 14  ? 23.764  -1.087  -11.557 1.00 81.91  ?  14  GLY   A O     1 
ATOM   84   N  N     . GLU   A 1 15  ? 24.311  0.444   -13.139 1.00 71.90  ?  15  GLU   A N     1 
ATOM   85   C  CA    . GLU   A 1 15  ? 25.186  -0.460  -13.892 1.00 68.13  ?  15  GLU   A CA    1 
ATOM   86   C  C     . GLU   A 1 15  ? 26.602  -0.352  -13.310 1.00 64.87  ?  15  GLU   A C     1 
ATOM   87   O  O     . GLU   A 1 15  ? 27.181  0.744   -13.268 1.00 66.00  ?  15  GLU   A O     1 
ATOM   88   C  CB    . GLU   A 1 15  ? 25.169  -0.119  -15.387 1.00 67.48  ?  15  GLU   A CB    1 
ATOM   89   N  N     . LEU   A 1 16  ? 27.124  -1.475  -12.810 1.00 58.93  ?  16  LEU   A N     1 
ATOM   90   C  CA    . LEU   A 1 16  ? 28.480  -1.540  -12.238 1.00 54.14  ?  16  LEU   A CA    1 
ATOM   91   C  C     . LEU   A 1 16  ? 29.536  -1.187  -13.296 1.00 52.52  ?  16  LEU   A C     1 
ATOM   92   O  O     . LEU   A 1 16  ? 29.413  -1.607  -14.446 1.00 55.73  ?  16  LEU   A O     1 
ATOM   93   C  CB    . LEU   A 1 16  ? 28.767  -2.938  -11.666 1.00 52.08  ?  16  LEU   A CB    1 
ATOM   94   C  CG    . LEU   A 1 16  ? 28.002  -3.373  -10.411 1.00 53.43  ?  16  LEU   A CG    1 
ATOM   95   C  CD1   . LEU   A 1 16  ? 28.380  -4.797  -10.023 1.00 50.78  ?  16  LEU   A CD1   1 
ATOM   96   C  CD2   . LEU   A 1 16  ? 28.249  -2.427  -9.238  1.00 52.79  ?  16  LEU   A CD2   1 
ATOM   97   N  N     . THR   A 1 17  ? 30.551  -0.421  -12.890 1.00 48.48  ?  17  THR   A N     1 
ATOM   98   C  CA    . THR   A 1 17  ? 31.679  -0.037  -13.743 1.00 47.85  ?  17  THR   A CA    1 
ATOM   99   C  C     . THR   A 1 17  ? 32.926  -0.874  -13.429 1.00 43.84  ?  17  THR   A C     1 
ATOM   100  O  O     . THR   A 1 17  ? 32.988  -1.550  -12.414 1.00 43.52  ?  17  THR   A O     1 
ATOM   101  C  CB    . THR   A 1 17  ? 32.032  1.462   -13.581 1.00 48.43  ?  17  THR   A CB    1 
ATOM   102  O  OG1   . THR   A 1 17  ? 32.807  1.668   -12.391 1.00 49.13  ?  17  THR   A OG1   1 
ATOM   103  C  CG2   . THR   A 1 17  ? 30.772  2.339   -13.528 1.00 48.53  ?  17  THR   A CG2   1 
ATOM   104  N  N     . ILE   A 1 18  ? 33.917  -0.792  -14.313 1.00 41.80  ?  18  ILE   A N     1 
ATOM   105  C  CA    . ILE   A 1 18  ? 35.256  -1.400  -14.116 1.00 39.84  ?  18  ILE   A CA    1 
ATOM   106  C  C     . ILE   A 1 18  ? 35.942  -0.881  -12.838 1.00 34.29  ?  18  ILE   A C     1 
ATOM   107  O  O     . ILE   A 1 18  ? 36.672  -1.596  -12.203 1.00 36.66  ?  18  ILE   A O     1 
ATOM   108  C  CB    . ILE   A 1 18  ? 36.176  -1.200  -15.353 1.00 37.41  ?  18  ILE   A CB    1 
ATOM   109  C  CG1   . ILE   A 1 18  ? 36.468  0.282   -15.617 1.00 40.14  ?  18  ILE   A CG1   1 
ATOM   110  C  CG2   . ILE   A 1 18  ? 35.562  -1.869  -16.571 1.00 39.22  ?  18  ILE   A CG2   1 
ATOM   111  C  CD1   . ILE   A 1 18  ? 37.387  0.538   -16.795 1.00 43.03  ?  18  ILE   A CD1   1 
ATOM   112  N  N     . GLY   A 1 19  ? 35.681  0.368   -12.482 1.00 37.15  ?  19  GLY   A N     1 
ATOM   113  C  CA    . GLY   A 1 19  ? 36.105  0.935   -11.176 1.00 41.53  ?  19  GLY   A CA    1 
ATOM   114  C  C     . GLY   A 1 19  ? 35.533  0.206   -9.958  1.00 43.34  ?  19  GLY   A C     1 
ATOM   115  O  O     . GLY   A 1 19  ? 36.209  0.040   -8.939  1.00 41.45  ?  19  GLY   A O     1 
ATOM   116  N  N     . ASN   A 1 20  ? 34.282  -0.239  -10.073 1.00 46.38  ?  20  ASN   A N     1 
ATOM   117  C  CA    . ASN   A 1 20  ? 33.663  -1.085  -9.061  1.00 47.93  ?  20  ASN   A CA    1 
ATOM   118  C  C     . ASN   A 1 20  ? 34.291  -2.471  -9.028  1.00 46.56  ?  20  ASN   A C     1 
ATOM   119  O  O     . ASN   A 1 20  ? 34.577  -2.975  -7.951  1.00 45.98  ?  20  ASN   A O     1 
ATOM   120  C  CB    . ASN   A 1 20  ? 32.132  -1.223  -9.264  1.00 50.33  ?  20  ASN   A CB    1 
ATOM   121  C  CG    . ASN   A 1 20  ? 31.395  0.117   -9.281  1.00 51.68  ?  20  ASN   A CG    1 
ATOM   122  O  OD1   . ASN   A 1 20  ? 30.556  0.358   -10.145 1.00 50.20  ?  20  ASN   A OD1   1 
ATOM   123  N  ND2   . ASN   A 1 20  ? 31.676  0.981   -8.313  1.00 51.66  ?  20  ASN   A ND2   1 
ATOM   124  N  N     . TYR   A 1 21  ? 34.518  -3.071  -10.202 1.00 48.06  ?  21  TYR   A N     1 
ATOM   125  C  CA    . TYR   A 1 21  ? 34.951  -4.491  -10.269 1.00 51.38  ?  21  TYR   A CA    1 
ATOM   126  C  C     . TYR   A 1 21  ? 36.412  -4.687  -9.852  1.00 53.29  ?  21  TYR   A C     1 
ATOM   127  O  O     . TYR   A 1 21  ? 36.701  -5.468  -8.956  1.00 56.50  ?  21  TYR   A O     1 
ATOM   128  C  CB    . TYR   A 1 21  ? 34.735  -5.104  -11.656 1.00 52.80  ?  21  TYR   A CB    1 
ATOM   129  C  CG    . TYR   A 1 21  ? 35.400  -6.457  -11.786 1.00 51.49  ?  21  TYR   A CG    1 
ATOM   130  C  CD1   . TYR   A 1 21  ? 34.945  -7.541  -11.059 1.00 49.31  ?  21  TYR   A CD1   1 
ATOM   131  C  CD2   . TYR   A 1 21  ? 36.516  -6.634  -12.595 1.00 54.47  ?  21  TYR   A CD2   1 
ATOM   132  C  CE1   . TYR   A 1 21  ? 35.558  -8.778  -11.151 1.00 54.31  ?  21  TYR   A CE1   1 
ATOM   133  C  CE2   . TYR   A 1 21  ? 37.142  -7.867  -12.690 1.00 56.25  ?  21  TYR   A CE2   1 
ATOM   134  C  CZ    . TYR   A 1 21  ? 36.651  -8.935  -11.966 1.00 54.60  ?  21  TYR   A CZ    1 
ATOM   135  O  OH    . TYR   A 1 21  ? 37.248  -10.163 -12.045 1.00 60.67  ?  21  TYR   A OH    1 
ATOM   136  N  N     . MET   A 1 22  ? 37.318  -3.979  -10.515 1.00 50.35  ?  22  MET   A N     1 
ATOM   137  C  CA    . MET   A 1 22  ? 38.770  -4.126  -10.253 1.00 53.30  ?  22  MET   A CA    1 
ATOM   138  C  C     . MET   A 1 22  ? 39.167  -3.314  -9.025  1.00 54.43  ?  22  MET   A C     1 
ATOM   139  O  O     . MET   A 1 22  ? 40.218  -3.542  -8.423  1.00 53.67  ?  22  MET   A O     1 
ATOM   140  C  CB    . MET   A 1 22  ? 39.649  -3.632  -11.414 1.00 47.76  ?  22  MET   A CB    1 
ATOM   141  C  CG    . MET   A 1 22  ? 39.097  -3.768  -12.820 1.00 51.39  ?  22  MET   A CG    1 
ATOM   142  S  SD    . MET   A 1 22  ? 40.242  -2.966  -13.971 1.00 49.55  ?  22  MET   A SD    1 
ATOM   143  C  CE    . MET   A 1 22  ? 39.700  -1.256  -13.800 1.00 54.73  ?  22  MET   A CE    1 
ATOM   144  N  N     . GLY   A 1 23  ? 38.343  -2.335  -8.680  1.00 58.26  ?  23  GLY   A N     1 
ATOM   145  C  CA    . GLY   A 1 23  ? 38.633  -1.463  -7.566  1.00 59.56  ?  23  GLY   A CA    1 
ATOM   146  C  C     . GLY   A 1 23  ? 38.125  -1.935  -6.212  1.00 62.39  ?  23  GLY   A C     1 
ATOM   147  O  O     . GLY   A 1 23  ? 38.695  -1.547  -5.191  1.00 70.52  ?  23  GLY   A O     1 
ATOM   148  N  N     . ALA   A 1 24  ? 37.073  -2.755  -6.179  1.00 60.50  ?  24  ALA   A N     1 
ATOM   149  C  CA    . ALA   A 1 24  ? 36.419  -3.155  -4.916  1.00 54.55  ?  24  ALA   A CA    1 
ATOM   150  C  C     . ALA   A 1 24  ? 35.969  -4.613  -4.871  1.00 56.61  ?  24  ALA   A C     1 
ATOM   151  O  O     . ALA   A 1 24  ? 36.382  -5.353  -3.985  1.00 52.97  ?  24  ALA   A O     1 
ATOM   152  C  CB    . ALA   A 1 24  ? 35.229  -2.265  -4.644  1.00 55.40  ?  24  ALA   A CB    1 
ATOM   153  N  N     . LEU   A 1 25  ? 35.101  -5.008  -5.808  1.00 53.04  ?  25  LEU   A N     1 
ATOM   154  C  CA    . LEU   A 1 25  ? 34.545  -6.341  -5.821  1.00 48.11  ?  25  LEU   A CA    1 
ATOM   155  C  C     . LEU   A 1 25  ? 35.633  -7.366  -5.964  1.00 48.67  ?  25  LEU   A C     1 
ATOM   156  O  O     . LEU   A 1 25  ? 35.618  -8.363  -5.270  1.00 49.45  ?  25  LEU   A O     1 
ATOM   157  C  CB    . LEU   A 1 25  ? 33.505  -6.490  -6.938  1.00 48.43  ?  25  LEU   A CB    1 
ATOM   158  C  CG    . LEU   A 1 25  ? 32.397  -7.529  -6.745  1.00 49.25  ?  25  LEU   A CG    1 
ATOM   159  C  CD1   . LEU   A 1 25  ? 31.987  -7.711  -5.282  1.00 50.97  ?  25  LEU   A CD1   1 
ATOM   160  C  CD2   . LEU   A 1 25  ? 31.199  -7.125  -7.583  1.00 49.72  ?  25  LEU   A CD2   1 
ATOM   161  N  N     . ARG   A 1 26  ? 36.605  -7.095  -6.835  1.00 52.59  ?  26  ARG   A N     1 
ATOM   162  C  CA    . ARG   A 1 26  ? 37.682  -8.059  -7.119  1.00 53.23  ?  26  ARG   A CA    1 
ATOM   163  C  C     . ARG   A 1 26  ? 38.490  -8.351  -5.857  1.00 47.73  ?  26  ARG   A C     1 
ATOM   164  O  O     . ARG   A 1 26  ? 38.825  -9.499  -5.590  1.00 45.80  ?  26  ARG   A O     1 
ATOM   165  C  CB    . ARG   A 1 26  ? 38.595  -7.571  -8.254  1.00 50.22  ?  26  ARG   A CB    1 
ATOM   166  C  CG    . ARG   A 1 26  ? 39.484  -8.649  -8.845  1.00 54.61  ?  26  ARG   A CG    1 
ATOM   167  C  CD    . ARG   A 1 26  ? 40.192  -8.176  -10.109 1.00 52.41  ?  26  ARG   A CD    1 
ATOM   168  N  NE    . ARG   A 1 26  ? 41.095  -7.057  -9.822  1.00 53.64  ?  26  ARG   A NE    1 
ATOM   169  C  CZ    . ARG   A 1 26  ? 41.724  -6.316  -10.735 1.00 54.03  ?  26  ARG   A CZ    1 
ATOM   170  N  NH1   . ARG   A 1 26  ? 42.511  -5.313  -10.342 1.00 54.65  ?  26  ARG   A NH1   1 
ATOM   171  N  NH2   . ARG   A 1 26  ? 41.563  -6.548  -12.037 1.00 54.30  ?  26  ARG   A NH2   1 
ATOM   172  N  N     . GLN   A 1 27  ? 38.779  -7.295  -5.107  1.00 48.19  ?  27  GLN   A N     1 
ATOM   173  C  CA    . GLN   A 1 27  ? 39.321  -7.372  -3.738  1.00 54.07  ?  27  GLN   A CA    1 
ATOM   174  C  C     . GLN   A 1 27  ? 38.553  -8.400  -2.863  1.00 48.07  ?  27  GLN   A C     1 
ATOM   175  O  O     . GLN   A 1 27  ? 39.132  -9.351  -2.348  1.00 50.10  ?  27  GLN   A O     1 
ATOM   176  C  CB    . GLN   A 1 27  ? 39.260  -5.967  -3.096  1.00 58.72  ?  27  GLN   A CB    1 
ATOM   177  C  CG    . GLN   A 1 27  ? 39.825  -5.842  -1.688  1.00 64.71  ?  27  GLN   A CG    1 
ATOM   178  C  CD    . GLN   A 1 27  ? 39.547  -4.499  -1.001  1.00 64.82  ?  27  GLN   A CD    1 
ATOM   179  O  OE1   . GLN   A 1 27  ? 38.926  -3.598  -1.570  1.00 65.23  ?  27  GLN   A OE1   1 
ATOM   180  N  NE2   . GLN   A 1 27  ? 40.003  -4.372  0.246   1.00 63.86  ?  27  GLN   A NE2   1 
ATOM   181  N  N     . TRP   A 1 28  ? 37.243  -8.204  -2.740  1.00 42.13  ?  28  TRP   A N     1 
ATOM   182  C  CA    . TRP   A 1 28  ? 36.405  -8.980  -1.811  1.00 39.91  ?  28  TRP   A CA    1 
ATOM   183  C  C     . TRP   A 1 28  ? 36.128  -10.407 -2.246  1.00 39.39  ?  28  TRP   A C     1 
ATOM   184  O  O     . TRP   A 1 28  ? 36.038  -11.293 -1.400  1.00 38.67  ?  28  TRP   A O     1 
ATOM   185  C  CB    . TRP   A 1 28  ? 35.103  -8.231  -1.525  1.00 39.92  ?  28  TRP   A CB    1 
ATOM   186  C  CG    . TRP   A 1 28  ? 35.329  -7.112  -0.554  1.00 35.34  ?  28  TRP   A CG    1 
ATOM   187  C  CD1   . TRP   A 1 28  ? 35.435  -5.787  -0.828  1.00 37.26  ?  28  TRP   A CD1   1 
ATOM   188  C  CD2   . TRP   A 1 28  ? 35.494  -7.245  0.848   1.00 34.00  ?  28  TRP   A CD2   1 
ATOM   189  N  NE1   . TRP   A 1 28  ? 35.656  -5.082  0.323   1.00 36.42  ?  28  TRP   A NE1   1 
ATOM   190  C  CE2   . TRP   A 1 28  ? 35.689  -5.958  1.371   1.00 36.65  ?  28  TRP   A CE2   1 
ATOM   191  C  CE3   . TRP   A 1 28  ? 35.455  -8.323  1.721   1.00 31.91  ?  28  TRP   A CE3   1 
ATOM   192  C  CZ2   . TRP   A 1 28  ? 35.859  -5.727  2.734   1.00 36.10  ?  28  TRP   A CZ2   1 
ATOM   193  C  CZ3   . TRP   A 1 28  ? 35.632  -8.090  3.063   1.00 32.84  ?  28  TRP   A CZ3   1 
ATOM   194  C  CH2   . TRP   A 1 28  ? 35.834  -6.802  3.556   1.00 34.08  ?  28  TRP   A CH2   1 
ATOM   195  N  N     . VAL   A 1 29  ? 36.060  -10.651 -3.551  1.00 41.53  ?  29  VAL   A N     1 
ATOM   196  C  CA    . VAL   A 1 29  ? 35.984  -12.014 -4.096  1.00 45.54  ?  29  VAL   A CA    1 
ATOM   197  C  C     . VAL   A 1 29  ? 37.138  -12.866 -3.541  1.00 46.01  ?  29  VAL   A C     1 
ATOM   198  O  O     . VAL   A 1 29  ? 36.980  -14.078 -3.277  1.00 45.58  ?  29  VAL   A O     1 
ATOM   199  C  CB    . VAL   A 1 29  ? 36.008  -11.989 -5.659  1.00 46.51  ?  29  VAL   A CB    1 
ATOM   200  C  CG1   . VAL   A 1 29  ? 36.133  -13.388 -6.246  1.00 46.38  ?  29  VAL   A CG1   1 
ATOM   201  C  CG2   . VAL   A 1 29  ? 34.760  -11.306 -6.210  1.00 43.26  ?  29  VAL   A CG2   1 
ATOM   202  N  N     . ASN   A 1 30  ? 38.293  -12.215 -3.349  1.00 48.48  ?  30  ASN   A N     1 
ATOM   203  C  CA    . ASN   A 1 30  ? 39.519  -12.877 -2.881  1.00 52.62  ?  30  ASN   A CA    1 
ATOM   204  C  C     . ASN   A 1 30  ? 39.706  -12.889 -1.361  1.00 53.07  ?  30  ASN   A C     1 
ATOM   205  O  O     . ASN   A 1 30  ? 40.786  -13.244 -0.881  1.00 56.59  ?  30  ASN   A O     1 
ATOM   206  C  CB    . ASN   A 1 30  ? 40.754  -12.245 -3.551  1.00 58.41  ?  30  ASN   A CB    1 
ATOM   207  C  CG    . ASN   A 1 30  ? 40.739  -12.378 -5.076  1.00 61.04  ?  30  ASN   A CG    1 
ATOM   208  O  OD1   . ASN   A 1 30  ? 41.000  -11.404 -5.783  1.00 63.22  ?  30  ASN   A OD1   1 
ATOM   209  N  ND2   . ASN   A 1 30  ? 40.441  -13.584 -5.588  1.00 59.32  ?  30  ASN   A ND2   1 
ATOM   210  N  N     . MET   A 1 31  ? 38.653  -12.533 -0.615  1.00 46.90  ?  31  MET   A N     1 
ATOM   211  C  CA    . MET   A 1 31  ? 38.640  -12.603 0.850   1.00 46.64  ?  31  MET   A CA    1 
ATOM   212  C  C     . MET   A 1 31  ? 37.440  -13.395 1.414   1.00 44.43  ?  31  MET   A C     1 
ATOM   213  O  O     . MET   A 1 31  ? 37.150  -13.319 2.619   1.00 42.13  ?  31  MET   A O     1 
ATOM   214  C  CB    . MET   A 1 31  ? 38.690  -11.174 1.439   1.00 47.76  ?  31  MET   A CB    1 
ATOM   215  C  CG    . MET   A 1 31  ? 39.914  -10.361 1.005   1.00 47.42  ?  31  MET   A CG    1 
ATOM   216  S  SD    . MET   A 1 31  ? 40.238  -8.854  1.977   1.00 50.36  ?  31  MET   A SD    1 
ATOM   217  C  CE    . MET   A 1 31  ? 39.055  -7.781  1.187   1.00 48.69  ?  31  MET   A CE    1 
ATOM   218  N  N     . GLN   A 1 32  ? 36.810  -14.216 0.570   1.00 41.20  ?  32  GLN   A N     1 
ATOM   219  C  CA    . GLN   A 1 32  ? 35.599  -14.958 0.951   1.00 44.79  ?  32  GLN   A CA    1 
ATOM   220  C  C     . GLN   A 1 32  ? 35.873  -16.110 1.927   1.00 43.66  ?  32  GLN   A C     1 
ATOM   221  O  O     . GLN   A 1 32  ? 34.954  -16.620 2.561   1.00 40.48  ?  32  GLN   A O     1 
ATOM   222  C  CB    . GLN   A 1 32  ? 34.862  -15.491 -0.292  1.00 42.75  ?  32  GLN   A CB    1 
ATOM   223  C  CG    . GLN   A 1 32  ? 34.369  -14.377 -1.211  1.00 42.36  ?  32  GLN   A CG    1 
ATOM   224  C  CD    . GLN   A 1 32  ? 33.511  -14.898 -2.343  1.00 44.20  ?  32  GLN   A CD    1 
ATOM   225  O  OE1   . GLN   A 1 32  ? 32.340  -15.248 -2.133  1.00 41.47  ?  32  GLN   A OE1   1 
ATOM   226  N  NE2   . GLN   A 1 32  ? 34.075  -14.945 -3.560  1.00 41.96  ?  32  GLN   A NE2   1 
ATOM   227  N  N     . ASP   A 1 33  ? 37.128  -16.532 2.024   1.00 48.00  ?  33  ASP   A N     1 
ATOM   228  C  CA    . ASP   A 1 33  ? 37.556  -17.523 3.027   1.00 46.45  ?  33  ASP   A CA    1 
ATOM   229  C  C     . ASP   A 1 33  ? 38.096  -16.863 4.295   1.00 42.77  ?  33  ASP   A C     1 
ATOM   230  O  O     . ASP   A 1 33  ? 38.149  -17.488 5.336   1.00 43.26  ?  33  ASP   A O     1 
ATOM   231  C  CB    . ASP   A 1 33  ? 38.602  -18.463 2.417   1.00 50.29  ?  33  ASP   A CB    1 
ATOM   232  C  CG    . ASP   A 1 33  ? 38.000  -19.418 1.376   1.00 54.82  ?  33  ASP   A CG    1 
ATOM   233  O  OD1   . ASP   A 1 33  ? 38.457  -19.377 0.218   1.00 58.13  ?  33  ASP   A OD1   1 
ATOM   234  O  OD2   . ASP   A 1 33  ? 37.071  -20.195 1.709   1.00 55.03  ?  33  ASP   A OD2   1 
ATOM   235  N  N     . ASP   A 1 34  ? 38.479  -15.590 4.199   1.00 40.62  ?  34  ASP   A N     1 
ATOM   236  C  CA    . ASP   A 1 34  ? 38.994  -14.815 5.340   1.00 37.15  ?  34  ASP   A CA    1 
ATOM   237  C  C     . ASP   A 1 34  ? 37.873  -14.319 6.268   1.00 36.52  ?  34  ASP   A C     1 
ATOM   238  O  O     . ASP   A 1 34  ? 38.056  -14.260 7.499   1.00 31.37  ?  34  ASP   A O     1 
ATOM   239  C  CB    . ASP   A 1 34  ? 39.807  -13.613 4.829   1.00 39.76  ?  34  ASP   A CB    1 
ATOM   240  C  CG    . ASP   A 1 34  ? 41.022  -14.030 4.023   1.00 42.17  ?  34  ASP   A CG    1 
ATOM   241  O  OD1   . ASP   A 1 34  ? 41.807  -14.849 4.549   1.00 43.40  ?  34  ASP   A OD1   1 
ATOM   242  O  OD2   . ASP   A 1 34  ? 41.184  -13.542 2.885   1.00 39.93  ?  34  ASP   A OD2   1 
ATOM   243  N  N     . TYR   A 1 35  ? 36.739  -13.935 5.663   1.00 34.85  ?  35  TYR   A N     1 
ATOM   244  C  CA    . TYR   A 1 35  ? 35.563  -13.396 6.362   1.00 32.60  ?  35  TYR   A CA    1 
ATOM   245  C  C     . TYR   A 1 35  ? 34.265  -14.129 5.971   1.00 31.83  ?  35  TYR   A C     1 
ATOM   246  O  O     . TYR   A 1 35  ? 34.156  -14.682 4.877   1.00 33.08  ?  35  TYR   A O     1 
ATOM   247  C  CB    . TYR   A 1 35  ? 35.387  -11.925 6.019   1.00 34.01  ?  35  TYR   A CB    1 
ATOM   248  C  CG    . TYR   A 1 35  ? 36.582  -11.058 6.266   1.00 33.58  ?  35  TYR   A CG    1 
ATOM   249  C  CD1   . TYR   A 1 35  ? 37.519  -10.820 5.268   1.00 35.41  ?  35  TYR   A CD1   1 
ATOM   250  C  CD2   . TYR   A 1 35  ? 36.744  -10.412 7.472   1.00 36.53  ?  35  TYR   A CD2   1 
ATOM   251  C  CE1   . TYR   A 1 35  ? 38.618  -9.994  5.492   1.00 36.81  ?  35  TYR   A CE1   1 
ATOM   252  C  CE2   . TYR   A 1 35  ? 37.848  -9.579  7.711   1.00 40.83  ?  35  TYR   A CE2   1 
ATOM   253  C  CZ    . TYR   A 1 35  ? 38.789  -9.387  6.715   1.00 38.35  ?  35  TYR   A CZ    1 
ATOM   254  O  OH    . TYR   A 1 35  ? 39.884  -8.566  6.948   1.00 44.11  ?  35  TYR   A OH    1 
ATOM   255  N  N     . HIS   A 1 36  ? 33.287  -14.118 6.871   1.00 34.15  ?  36  HIS   A N     1 
ATOM   256  C  CA    . HIS   A 1 36  ? 31.909  -14.509 6.578   1.00 31.38  ?  36  HIS   A CA    1 
ATOM   257  C  C     . HIS   A 1 36  ? 31.246  -13.291 5.918   1.00 27.82  ?  36  HIS   A C     1 
ATOM   258  O  O     . HIS   A 1 36  ? 30.791  -12.396 6.611   1.00 25.50  ?  36  HIS   A O     1 
ATOM   259  C  CB    . HIS   A 1 36  ? 31.189  -14.899 7.878   1.00 32.74  ?  36  HIS   A CB    1 
ATOM   260  C  CG    . HIS   A 1 36  ? 29.720  -15.184 7.700   1.00 40.52  ?  36  HIS   A CG    1 
ATOM   261  N  ND1   . HIS   A 1 36  ? 29.223  -16.458 7.508   1.00 41.76  ?  36  HIS   A ND1   1 
ATOM   262  C  CD2   . HIS   A 1 36  ? 28.644  -14.363 7.703   1.00 39.04  ?  36  HIS   A CD2   1 
ATOM   263  C  CE1   . HIS   A 1 36  ? 27.908  -16.405 7.398   1.00 42.04  ?  36  HIS   A CE1   1 
ATOM   264  N  NE2   . HIS   A 1 36  ? 27.531  -15.148 7.515   1.00 42.35  ?  36  HIS   A NE2   1 
ATOM   265  N  N     . CYS   A 1 37  ? 31.200  -13.280 4.577   1.00 24.47  ?  37  CYS   A N     1 
ATOM   266  C  CA    . CYS   A 1 37  ? 30.752  -12.149 3.796   1.00 24.99  ?  37  CYS   A CA    1 
ATOM   267  C  C     . CYS   A 1 37  ? 29.269  -12.342 3.490   1.00 25.55  ?  37  CYS   A C     1 
ATOM   268  O  O     . CYS   A 1 37  ? 28.858  -13.406 3.047   1.00 27.77  ?  37  CYS   A O     1 
ATOM   269  C  CB    . CYS   A 1 37  ? 31.563  -12.032 2.492   1.00 28.06  ?  37  CYS   A CB    1 
ATOM   270  S  SG    . CYS   A 1 37  ? 33.343  -11.768 2.726   1.00 34.56  ?  37  CYS   A SG    1 
ATOM   271  N  N     . ILE   A 1 38  ? 28.502  -11.284 3.696   1.00 24.19  ?  38  ILE   A N     1 
ATOM   272  C  CA    . ILE   A 1 38  ? 27.068  -11.220 3.409   1.00 24.33  ?  38  ILE   A CA    1 
ATOM   273  C  C     . ILE   A 1 38  ? 26.850  -10.124 2.377   1.00 26.30  ?  38  ILE   A C     1 
ATOM   274  O  O     . ILE   A 1 38  ? 27.191  -8.933  2.636   1.00 28.91  ?  38  ILE   A O     1 
ATOM   275  C  CB    . ILE   A 1 38  ? 26.236  -10.899 4.680   1.00 21.54  ?  38  ILE   A CB    1 
ATOM   276  C  CG1   . ILE   A 1 38  ? 26.458  -11.946 5.751   1.00 22.56  ?  38  ILE   A CG1   1 
ATOM   277  C  CG2   . ILE   A 1 38  ? 24.719  -10.802 4.346   1.00 21.37  ?  38  ILE   A CG2   1 
ATOM   278  C  CD1   . ILE   A 1 38  ? 26.052  -11.520 7.134   1.00 23.00  ?  38  ILE   A CD1   1 
ATOM   279  N  N     . TYR   A 1 39  ? 26.252  -10.496 1.245   1.00 30.16  ?  39  TYR   A N     1 
ATOM   280  C  CA    . TYR   A 1 39  ? 25.829  -9.553  0.161   1.00 28.55  ?  39  TYR   A CA    1 
ATOM   281  C  C     . TYR   A 1 39  ? 24.288  -9.551  0.064   1.00 29.93  ?  39  TYR   A C     1 
ATOM   282  O  O     . TYR   A 1 39  ? 23.669  -10.568 -0.330  1.00 28.33  ?  39  TYR   A O     1 
ATOM   283  C  CB    . TYR   A 1 39  ? 26.462  -9.968  -1.165  1.00 27.53  ?  39  TYR   A CB    1 
ATOM   284  C  CG    . TYR   A 1 39  ? 27.958  -9.797  -1.179  1.00 30.02  ?  39  TYR   A CG    1 
ATOM   285  C  CD1   . TYR   A 1 39  ? 28.797  -10.847 -0.834  1.00 30.70  ?  39  TYR   A CD1   1 
ATOM   286  C  CD2   . TYR   A 1 39  ? 28.545  -8.578  -1.510  1.00 28.69  ?  39  TYR   A CD2   1 
ATOM   287  C  CE1   . TYR   A 1 39  ? 30.169  -10.695 -0.841  1.00 32.15  ?  39  TYR   A CE1   1 
ATOM   288  C  CE2   . TYR   A 1 39  ? 29.926  -8.431  -1.519  1.00 30.64  ?  39  TYR   A CE2   1 
ATOM   289  C  CZ    . TYR   A 1 39  ? 30.721  -9.492  -1.160  1.00 32.18  ?  39  TYR   A CZ    1 
ATOM   290  O  OH    . TYR   A 1 39  ? 32.081  -9.374  -1.145  1.00 37.75  ?  39  TYR   A OH    1 
ATOM   291  N  N     . CYS   A 1 40  ? 23.698  -8.413  0.440   1.00 28.92  ?  40  CYS   A N     1 
ATOM   292  C  CA    . CYS   A 1 40  ? 22.261  -8.193  0.477   1.00 30.98  ?  40  CYS   A CA    1 
ATOM   293  C  C     . CYS   A 1 40  ? 21.843  -7.240  -0.638  1.00 31.39  ?  40  CYS   A C     1 
ATOM   294  O  O     . CYS   A 1 40  ? 22.258  -6.053  -0.625  1.00 27.51  ?  40  CYS   A O     1 
ATOM   295  C  CB    . CYS   A 1 40  ? 21.847  -7.593  1.830   1.00 29.05  ?  40  CYS   A CB    1 
ATOM   296  S  SG    . CYS   A 1 40  ? 20.096  -7.178  2.001   1.00 28.11  ?  40  CYS   A SG    1 
ATOM   297  N  N     . ILE   A 1 41  ? 21.054  -7.743  -1.599  1.00 31.23  ?  41  ILE   A N     1 
ATOM   298  C  CA    . ILE   A 1 41  ? 20.488  -6.873  -2.651  1.00 32.90  ?  41  ILE   A CA    1 
ATOM   299  C  C     . ILE   A 1 41  ? 19.328  -6.092  -2.067  1.00 29.04  ?  41  ILE   A C     1 
ATOM   300  O  O     . ILE   A 1 41  ? 18.274  -6.635  -1.785  1.00 31.54  ?  41  ILE   A O     1 
ATOM   301  C  CB    . ILE   A 1 41  ? 20.048  -7.626  -3.928  1.00 35.90  ?  41  ILE   A CB    1 
ATOM   302  C  CG1   . ILE   A 1 41  ? 21.224  -8.394  -4.544  1.00 37.03  ?  41  ILE   A CG1   1 
ATOM   303  C  CG2   . ILE   A 1 41  ? 19.475  -6.636  -4.934  1.00 38.16  ?  41  ILE   A CG2   1 
ATOM   304  C  CD1   . ILE   A 1 41  ? 21.091  -9.893  -4.448  1.00 38.62  ?  41  ILE   A CD1   1 
ATOM   305  N  N     . VAL   A 1 42  ? 19.507  -4.789  -1.952  1.00 31.28  ?  42  VAL   A N     1 
ATOM   306  C  CA    . VAL   A 1 42  ? 18.678  -3.954  -1.101  1.00 32.09  ?  42  VAL   A CA    1 
ATOM   307  C  C     . VAL   A 1 42  ? 17.499  -3.291  -1.859  1.00 35.49  ?  42  VAL   A C     1 
ATOM   308  O  O     . VAL   A 1 42  ? 17.446  -2.061  -2.063  1.00 33.23  ?  42  VAL   A O     1 
ATOM   309  C  CB    . VAL   A 1 42  ? 19.538  -2.934  -0.324  1.00 31.65  ?  42  VAL   A CB    1 
ATOM   310  C  CG1   . VAL   A 1 42  ? 20.321  -3.658  0.770   1.00 30.96  ?  42  VAL   A CG1   1 
ATOM   311  C  CG2   . VAL   A 1 42  ? 20.488  -2.152  -1.231  1.00 33.42  ?  42  VAL   A CG2   1 
ATOM   312  N  N     . ASP   A 1 43  ? 16.544  -4.128  -2.250  1.00 34.76  ?  43  ASP   A N     1 
ATOM   313  C  CA    . ASP   A 1 43  ? 15.363  -3.668  -3.003  1.00 34.55  ?  43  ASP   A CA    1 
ATOM   314  C  C     . ASP   A 1 43  ? 14.446  -2.780  -2.176  1.00 34.93  ?  43  ASP   A C     1 
ATOM   315  O  O     . ASP   A 1 43  ? 13.777  -1.896  -2.733  1.00 36.41  ?  43  ASP   A O     1 
ATOM   316  C  CB    . ASP   A 1 43  ? 14.600  -4.845  -3.665  1.00 36.40  ?  43  ASP   A CB    1 
ATOM   317  C  CG    . ASP   A 1 43  ? 14.188  -5.927  -2.684  1.00 37.15  ?  43  ASP   A CG    1 
ATOM   318  O  OD1   . ASP   A 1 43  ? 14.655  -5.881  -1.509  1.00 34.34  ?  43  ASP   A OD1   1 
ATOM   319  O  OD2   . ASP   A 1 43  ? 13.386  -6.809  -3.079  1.00 34.44  ?  43  ASP   A OD2   1 
ATOM   320  N  N     . GLN   A 1 44  ? 14.431  -2.985  -0.844  1.00 30.85  ?  44  GLN   A N     1 
ATOM   321  C  CA    . GLN   A 1 44  ? 13.663  -2.117  0.063   1.00 29.96  ?  44  GLN   A CA    1 
ATOM   322  C  C     . GLN   A 1 44  ? 14.235  -0.704  0.143   1.00 29.96  ?  44  GLN   A C     1 
ATOM   323  O  O     . GLN   A 1 44  ? 13.466  0.259   0.294   1.00 31.28  ?  44  GLN   A O     1 
ATOM   324  C  CB    . GLN   A 1 44  ? 13.480  -2.744  1.465   1.00 29.87  ?  44  GLN   A CB    1 
ATOM   325  C  CG    . GLN   A 1 44  ? 12.793  -4.117  1.424   1.00 32.68  ?  44  GLN   A CG    1 
ATOM   326  C  CD    . GLN   A 1 44  ? 12.566  -4.707  2.785   1.00 32.00  ?  44  GLN   A CD    1 
ATOM   327  O  OE1   . GLN   A 1 44  ? 13.282  -5.601  3.219   1.00 33.03  ?  44  GLN   A OE1   1 
ATOM   328  N  NE2   . GLN   A 1 44  ? 11.558  -4.202  3.477   1.00 32.92  ?  44  GLN   A NE2   1 
ATOM   329  N  N     . HIS   A 1 45  ? 15.562  -0.571  0.022   1.00 28.71  ?  45  HIS   A N     1 
ATOM   330  C  CA    . HIS   A 1 45  ? 16.216  0.761   -0.093  1.00 30.70  ?  45  HIS   A CA    1 
ATOM   331  C  C     . HIS   A 1 45  ? 15.899  1.458   -1.408  1.00 32.72  ?  45  HIS   A C     1 
ATOM   332  O  O     . HIS   A 1 45  ? 15.689  2.692   -1.430  1.00 31.32  ?  45  HIS   A O     1 
ATOM   333  C  CB    . HIS   A 1 45  ? 17.746  0.660   0.089   1.00 30.21  ?  45  HIS   A CB    1 
ATOM   334  C  CG    . HIS   A 1 45  ? 18.171  0.583   1.530   1.00 26.16  ?  45  HIS   A CG    1 
ATOM   335  N  ND1   . HIS   A 1 45  ? 18.181  1.685   2.351   1.00 25.65  ?  45  HIS   A ND1   1 
ATOM   336  C  CD2   . HIS   A 1 45  ? 18.550  -0.463  2.299   1.00 24.84  ?  45  HIS   A CD2   1 
ATOM   337  C  CE1   . HIS   A 1 45  ? 18.558  1.325   3.562   1.00 26.60  ?  45  HIS   A CE1   1 
ATOM   338  N  NE2   . HIS   A 1 45  ? 18.773  0.022   3.565   1.00 24.21  ?  45  HIS   A NE2   1 
ATOM   339  N  N     . ALA   A 1 46  ? 15.850  0.658   -2.485  1.00 33.42  ?  46  ALA   A N     1 
ATOM   340  C  CA    . ALA   A 1 46  ? 15.589  1.155   -3.859  1.00 35.59  ?  46  ALA   A CA    1 
ATOM   341  C  C     . ALA   A 1 46  ? 14.283  1.946   -3.998  1.00 38.50  ?  46  ALA   A C     1 
ATOM   342  O  O     . ALA   A 1 46  ? 14.233  2.941   -4.727  1.00 40.08  ?  46  ALA   A O     1 
ATOM   343  C  CB    . ALA   A 1 46  ? 15.602  -0.011  -4.828  1.00 32.17  ?  46  ALA   A CB    1 
ATOM   344  N  N     . ILE   A 1 47  ? 13.234  1.521   -3.283  1.00 38.43  ?  47  ILE   A N     1 
ATOM   345  C  CA    . ILE   A 1 47  ? 11.886  2.120   -3.464  1.00 37.92  ?  47  ILE   A CA    1 
ATOM   346  C  C     . ILE   A 1 47  ? 11.720  3.484   -2.798  1.00 38.27  ?  47  ILE   A C     1 
ATOM   347  O  O     . ILE   A 1 47  ? 10.635  4.067   -2.838  1.00 43.58  ?  47  ILE   A O     1 
ATOM   348  C  CB    . ILE   A 1 47  ? 10.734  1.160   -3.073  1.00 38.51  ?  47  ILE   A CB    1 
ATOM   349  C  CG1   . ILE   A 1 47  ? 10.811  0.747   -1.585  1.00 36.11  ?  47  ILE   A CG1   1 
ATOM   350  C  CG2   . ILE   A 1 47  ? 10.732  -0.058  -3.997  1.00 39.74  ?  47  ILE   A CG2   1 
ATOM   351  C  CD1   . ILE   A 1 47  ? 9.506   0.232   -1.037  1.00 35.82  ?  47  ILE   A CD1   1 
ATOM   352  N  N     . THR   A 1 48  ? 12.782  3.993   -2.176  1.00 39.44  ?  48  THR   A N     1 
ATOM   353  C  CA    . THR   A 1 48  ? 12.824  5.381   -1.704  1.00 40.41  ?  48  THR   A CA    1 
ATOM   354  C  C     . THR   A 1 48  ? 12.746  6.387   -2.878  1.00 42.28  ?  48  THR   A C     1 
ATOM   355  O  O     . THR   A 1 48  ? 12.340  7.520   -2.686  1.00 45.86  ?  48  THR   A O     1 
ATOM   356  C  CB    . THR   A 1 48  ? 14.113  5.657   -0.926  1.00 40.42  ?  48  THR   A CB    1 
ATOM   357  O  OG1   . THR   A 1 48  ? 15.221  5.266   -1.729  1.00 41.84  ?  48  THR   A OG1   1 
ATOM   358  C  CG2   . THR   A 1 48  ? 14.142  4.907   0.398   1.00 42.02  ?  48  THR   A CG2   1 
ATOM   359  N  N     . VAL   A 1 49  ? 13.182  5.960   -4.064  1.00 43.27  ?  49  VAL   A N     1 
ATOM   360  C  CA    . VAL   A 1 49  ? 13.002  6.672   -5.328  1.00 48.47  ?  49  VAL   A CA    1 
ATOM   361  C  C     . VAL   A 1 49  ? 11.984  5.910   -6.195  1.00 48.68  ?  49  VAL   A C     1 
ATOM   362  O  O     . VAL   A 1 49  ? 12.155  4.726   -6.441  1.00 46.39  ?  49  VAL   A O     1 
ATOM   363  C  CB    . VAL   A 1 49  ? 14.351  6.741   -6.087  1.00 50.71  ?  49  VAL   A CB    1 
ATOM   364  C  CG1   . VAL   A 1 49  ? 14.183  7.258   -7.520  1.00 54.90  ?  49  VAL   A CG1   1 
ATOM   365  C  CG2   . VAL   A 1 49  ? 15.353  7.611   -5.336  1.00 49.86  ?  49  VAL   A CG2   1 
ATOM   366  N  N     . ARG   A 1 50  ? 10.967  6.605   -6.704  1.00 53.42  ?  50  ARG   A N     1 
ATOM   367  C  CA    . ARG   A 1 50  ? 9.975   5.982   -7.580  1.00 57.04  ?  50  ARG   A CA    1 
ATOM   368  C  C     . ARG   A 1 50  ? 10.625  5.475   -8.862  1.00 58.05  ?  50  ARG   A C     1 
ATOM   369  O  O     . ARG   A 1 50  ? 11.400  6.197   -9.485  1.00 58.78  ?  50  ARG   A O     1 
ATOM   370  C  CB    . ARG   A 1 50  ? 8.845   6.968   -7.923  1.00 63.08  ?  50  ARG   A CB    1 
ATOM   371  C  CG    . ARG   A 1 50  ? 7.571   6.326   -8.487  1.00 67.39  ?  50  ARG   A CG    1 
ATOM   372  C  CD    . ARG   A 1 50  ? 6.982   5.268   -7.570  1.00 67.96  ?  50  ARG   A CD    1 
ATOM   373  N  NE    . ARG   A 1 50  ? 7.075   5.677   -6.167  1.00 73.37  ?  50  ARG   A NE    1 
ATOM   374  C  CZ    . ARG   A 1 50  ? 6.219   6.480   -5.540  1.00 72.03  ?  50  ARG   A CZ    1 
ATOM   375  N  NH1   . ARG   A 1 50  ? 5.148   6.959   -6.169  1.00 69.41  ?  50  ARG   A NH1   1 
ATOM   376  N  NH2   . ARG   A 1 50  ? 6.427   6.783   -4.257  1.00 73.68  ?  50  ARG   A NH2   1 
ATOM   377  N  N     . GLN   A 1 51  ? 10.321  4.228   -9.227  1.00 58.08  ?  51  GLN   A N     1 
ATOM   378  C  CA    . GLN   A 1 51  ? 10.824  3.619   -10.459 1.00 55.90  ?  51  GLN   A CA    1 
ATOM   379  C  C     . GLN   A 1 51  ? 9.832   2.600   -10.988 1.00 52.58  ?  51  GLN   A C     1 
ATOM   380  O  O     . GLN   A 1 51  ? 8.913   2.190   -10.289 1.00 52.93  ?  51  GLN   A O     1 
ATOM   381  C  CB    . GLN   A 1 51  ? 12.201  2.974   -10.233 1.00 59.93  ?  51  GLN   A CB    1 
ATOM   382  C  CG    . GLN   A 1 51  ? 12.284  2.040   -9.029  1.00 58.14  ?  51  GLN   A CG    1 
ATOM   383  C  CD    . GLN   A 1 51  ? 13.674  2.041   -8.430  1.00 56.74  ?  51  GLN   A CD    1 
ATOM   384  O  OE1   . GLN   A 1 51  ? 14.027  2.951   -7.671  1.00 53.23  ?  51  GLN   A OE1   1 
ATOM   385  N  NE2   . GLN   A 1 51  ? 14.470  1.020   -8.758  1.00 57.44  ?  51  GLN   A NE2   1 
ATOM   386  N  N     . ASP   A 1 52  ? 10.025  2.234   -12.249 1.00 54.21  ?  52  ASP   A N     1 
ATOM   387  C  CA    . ASP   A 1 52  ? 9.222   1.244   -12.937 1.00 55.04  ?  52  ASP   A CA    1 
ATOM   388  C  C     . ASP   A 1 52  ? 9.429   -0.121  -12.286 1.00 50.11  ?  52  ASP   A C     1 
ATOM   389  O  O     . ASP   A 1 52  ? 10.563  -0.560  -12.133 1.00 51.01  ?  52  ASP   A O     1 
ATOM   390  C  CB    . ASP   A 1 52  ? 9.621   1.195   -14.414 1.00 55.47  ?  52  ASP   A CB    1 
ATOM   391  C  CG    . ASP   A 1 52  ? 8.654   0.407   -15.245 1.00 60.39  ?  52  ASP   A CG    1 
ATOM   392  O  OD1   . ASP   A 1 52  ? 9.043   -0.702  -15.704 1.00 67.30  ?  52  ASP   A OD1   1 
ATOM   393  O  OD2   . ASP   A 1 52  ? 7.508   0.895   -15.425 1.00 65.41  ?  52  ASP   A OD2   1 
ATOM   394  N  N     . ALA   A 1 53  ? 8.325   -0.767  -11.917 1.00 49.22  ?  53  ALA   A N     1 
ATOM   395  C  CA    . ALA   A 1 53  ? 8.331   -1.992  -11.121 1.00 48.38  ?  53  ALA   A CA    1 
ATOM   396  C  C     . ALA   A 1 53  ? 9.029   -3.130  -11.843 1.00 49.11  ?  53  ALA   A C     1 
ATOM   397  O  O     . ALA   A 1 53  ? 9.765   -3.897  -11.231 1.00 46.39  ?  53  ALA   A O     1 
ATOM   398  C  CB    . ALA   A 1 53  ? 6.897   -2.389  -10.774 1.00 49.61  ?  53  ALA   A CB    1 
ATOM   399  N  N     . GLN   A 1 54  ? 8.790   -3.237  -13.146 1.00 49.49  ?  54  GLN   A N     1 
ATOM   400  C  CA    . GLN   A 1 54  ? 9.335   -4.330  -13.941 1.00 52.33  ?  54  GLN   A CA    1 
ATOM   401  C  C     . GLN   A 1 54  ? 10.843  -4.172  -14.123 1.00 48.95  ?  54  GLN   A C     1 
ATOM   402  O  O     . GLN   A 1 54  ? 11.568  -5.174  -14.144 1.00 48.05  ?  54  GLN   A O     1 
ATOM   403  C  CB    . GLN   A 1 54  ? 8.601   -4.439  -15.287 1.00 57.10  ?  54  GLN   A CB    1 
ATOM   404  C  CG    . GLN   A 1 54  ? 7.089   -4.651  -15.129 1.00 62.00  ?  54  GLN   A CG    1 
ATOM   405  C  CD    . GLN   A 1 54  ? 6.354   -4.826  -16.448 1.00 66.54  ?  54  GLN   A CD    1 
ATOM   406  O  OE1   . GLN   A 1 54  ? 6.922   -4.641  -17.525 1.00 74.62  ?  54  GLN   A OE1   1 
ATOM   407  N  NE2   . GLN   A 1 54  ? 5.082   -5.180  -16.368 1.00 69.78  ?  54  GLN   A NE2   1 
ATOM   408  N  N     . LYS   A 1 55  ? 11.303  -2.916  -14.213 1.00 47.01  ?  55  LYS   A N     1 
ATOM   409  C  CA    . LYS   A 1 55  ? 12.744  -2.593  -14.256 1.00 45.41  ?  55  LYS   A CA    1 
ATOM   410  C  C     . LYS   A 1 55  ? 13.449  -2.924  -12.933 1.00 41.61  ?  55  LYS   A C     1 
ATOM   411  O  O     . LYS   A 1 55  ? 14.555  -3.488  -12.953 1.00 39.66  ?  55  LYS   A O     1 
ATOM   412  C  CB    . LYS   A 1 55  ? 12.979  -1.111  -14.609 1.00 50.48  ?  55  LYS   A CB    1 
ATOM   413  C  CG    . LYS   A 1 55  ? 12.936  -0.821  -16.107 1.00 53.57  ?  55  LYS   A CG    1 
ATOM   414  C  CD    . LYS   A 1 55  ? 13.141  0.658   -16.416 1.00 58.03  ?  55  LYS   A CD    1 
ATOM   415  C  CE    . LYS   A 1 55  ? 12.855  0.969   -17.883 1.00 61.46  ?  55  LYS   A CE    1 
ATOM   416  N  NZ    . LYS   A 1 55  ? 13.675  2.111   -18.367 1.00 63.99  ?  55  LYS   A NZ    1 
ATOM   417  N  N     . LEU   A 1 56  ? 12.797  -2.599  -11.800 1.00 38.79  ?  56  LEU   A N     1 
ATOM   418  C  CA    . LEU   A 1 56  ? 13.295  -2.976  -10.469 1.00 38.05  ?  56  LEU   A CA    1 
ATOM   419  C  C     . LEU   A 1 56  ? 13.422  -4.499  -10.309 1.00 37.92  ?  56  LEU   A C     1 
ATOM   420  O  O     . LEU   A 1 56  ? 14.463  -5.000  -9.889  1.00 38.90  ?  56  LEU   A O     1 
ATOM   421  C  CB    . LEU   A 1 56  ? 12.394  -2.393  -9.373  1.00 41.22  ?  56  LEU   A CB    1 
ATOM   422  C  CG    . LEU   A 1 56  ? 12.784  -2.629  -7.902  1.00 40.73  ?  56  LEU   A CG    1 
ATOM   423  C  CD1   . LEU   A 1 56  ? 14.269  -2.419  -7.647  1.00 39.37  ?  56  LEU   A CD1   1 
ATOM   424  C  CD2   . LEU   A 1 56  ? 11.987  -1.695  -6.994  1.00 40.35  ?  56  LEU   A CD2   1 
ATOM   425  N  N     . ARG   A 1 57  ? 12.384  -5.228  -10.690 1.00 37.23  ?  57  ARG   A N     1 
ATOM   426  C  CA    . ARG   A 1 57  ? 12.421  -6.699  -10.653 1.00 40.18  ?  57  ARG   A CA    1 
ATOM   427  C  C     . ARG   A 1 57  ? 13.564  -7.235  -11.508 1.00 41.24  ?  57  ARG   A C     1 
ATOM   428  O  O     . ARG   A 1 57  ? 14.343  -8.066  -11.043 1.00 44.56  ?  57  ARG   A O     1 
ATOM   429  C  CB    . ARG   A 1 57  ? 11.078  -7.304  -11.101 1.00 39.46  ?  57  ARG   A CB    1 
ATOM   430  C  CG    . ARG   A 1 57  ? 11.056  -8.844  -11.097 1.00 38.80  ?  57  ARG   A CG    1 
ATOM   431  C  CD    . ARG   A 1 57  ? 9.652   -9.442  -11.189 1.00 40.76  ?  57  ARG   A CD    1 
ATOM   432  N  NE    . ARG   A 1 57  ? 8.786   -8.987  -10.099 1.00 43.60  ?  57  ARG   A NE    1 
ATOM   433  C  CZ    . ARG   A 1 57  ? 7.822   -8.071  -10.191 1.00 41.33  ?  57  ARG   A CZ    1 
ATOM   434  N  NH1   . ARG   A 1 57  ? 7.521   -7.497  -11.346 1.00 40.02  ?  57  ARG   A NH1   1 
ATOM   435  N  NH2   . ARG   A 1 57  ? 7.147   -7.725  -9.095  1.00 41.69  ?  57  ARG   A NH2   1 
ATOM   436  N  N     . LYS   A 1 58  ? 13.669  -6.736  -12.749 1.00 43.36  ?  58  LYS   A N     1 
ATOM   437  C  CA    . LYS   A 1 58  ? 14.752  -7.134  -13.670 1.00 40.98  ?  58  LYS   A CA    1 
ATOM   438  C  C     . LYS   A 1 58  ? 16.155  -6.815  -13.122 1.00 37.77  ?  58  LYS   A C     1 
ATOM   439  O  O     . LYS   A 1 58  ? 17.032  -7.664  -13.193 1.00 36.78  ?  58  LYS   A O     1 
ATOM   440  C  CB    . LYS   A 1 58  ? 14.604  -6.481  -15.065 1.00 42.13  ?  58  LYS   A CB    1 
ATOM   441  C  CG    . LYS   A 1 58  ? 15.723  -6.908  -16.031 1.00 45.26  ?  58  LYS   A CG    1 
ATOM   442  C  CD    . LYS   A 1 58  ? 15.604  -6.416  -17.475 1.00 52.52  ?  58  LYS   A CD    1 
ATOM   443  C  CE    . LYS   A 1 58  ? 15.838  -4.919  -17.627 1.00 57.56  ?  58  LYS   A CE    1 
ATOM   444  N  NZ    . LYS   A 1 58  ? 17.114  -4.417  -17.028 1.00 63.49  ?  58  LYS   A NZ    1 
ATOM   445  N  N     . ALA   A 1 59  ? 16.326  -5.594  -12.603 1.00 34.01  ?  59  ALA   A N     1 
ATOM   446  C  CA    . ALA   A 1 59  ? 17.591  -5.087  -12.093 1.00 35.98  ?  59  ALA   A CA    1 
ATOM   447  C  C     . ALA   A 1 59  ? 18.053  -5.789  -10.806 1.00 34.85  ?  59  ALA   A C     1 
ATOM   448  O  O     . ALA   A 1 59  ? 19.252  -5.850  -10.538 1.00 34.00  ?  59  ALA   A O     1 
ATOM   449  C  CB    . ALA   A 1 59  ? 17.512  -3.566  -11.879 1.00 36.11  ?  59  ALA   A CB    1 
ATOM   450  N  N     . THR   A 1 60  ? 17.108  -6.307  -10.030 1.00 34.19  ?  60  THR   A N     1 
ATOM   451  C  CA    . THR   A 1 60  ? 17.410  -7.160  -8.874  1.00 36.95  ?  60  THR   A CA    1 
ATOM   452  C  C     . THR   A 1 60  ? 18.115  -8.433  -9.344  1.00 36.56  ?  60  THR   A C     1 
ATOM   453  O  O     . THR   A 1 60  ? 19.168  -8.800  -8.818  1.00 38.68  ?  60  THR   A O     1 
ATOM   454  C  CB    . THR   A 1 60  ? 16.117  -7.519  -8.072  1.00 36.77  ?  60  THR   A CB    1 
ATOM   455  O  OG1   . THR   A 1 60  ? 15.520  -6.326  -7.544  1.00 34.38  ?  60  THR   A OG1   1 
ATOM   456  C  CG2   . THR   A 1 60  ? 16.394  -8.481  -6.912  1.00 35.82  ?  60  THR   A CG2   1 
ATOM   457  N  N     . LEU   A 1 61  ? 17.540  -9.083  -10.353 1.00 37.40  ?  61  LEU   A N     1 
ATOM   458  C  CA    . LEU   A 1 61  ? 18.116  -10.300 -10.947 1.00 37.92  ?  61  LEU   A CA    1 
ATOM   459  C  C     . LEU   A 1 61  ? 19.381  -9.980  -11.760 1.00 36.41  ?  61  LEU   A C     1 
ATOM   460  O  O     . LEU   A 1 61  ? 20.310  -10.778 -11.773 1.00 37.07  ?  61  LEU   A O     1 
ATOM   461  C  CB    . LEU   A 1 61  ? 17.106  -11.016 -11.830 1.00 40.02  ?  61  LEU   A CB    1 
ATOM   462  C  CG    . LEU   A 1 61  ? 15.778  -11.385 -11.181 1.00 39.34  ?  61  LEU   A CG    1 
ATOM   463  C  CD1   . LEU   A 1 61  ? 14.717  -11.594 -12.256 1.00 41.89  ?  61  LEU   A CD1   1 
ATOM   464  C  CD2   . LEU   A 1 61  ? 15.936  -12.602 -10.281 1.00 38.30  ?  61  LEU   A CD2   1 
ATOM   465  N  N     . ASP   A 1 62  ? 19.408  -8.831  -12.423 1.00 37.52  ?  62  ASP   A N     1 
ATOM   466  C  CA    . ASP   A 1 62  ? 20.658  -8.334  -13.097 1.00 42.29  ?  62  ASP   A CA    1 
ATOM   467  C  C     . ASP   A 1 62  ? 21.818  -8.209  -12.081 1.00 40.77  ?  62  ASP   A C     1 
ATOM   468  O  O     . ASP   A 1 62  ? 22.927  -8.690  -12.321 1.00 43.60  ?  62  ASP   A O     1 
ATOM   469  C  CB    . ASP   A 1 62  ? 20.448  -6.965  -13.780 1.00 40.31  ?  62  ASP   A CB    1 
ATOM   470  C  CG    . ASP   A 1 62  ? 19.512  -7.021  -15.009 1.00 43.91  ?  62  ASP   A CG    1 
ATOM   471  O  OD1   . ASP   A 1 62  ? 19.025  -8.132  -15.373 1.00 39.06  ?  62  ASP   A OD1   1 
ATOM   472  O  OD2   . ASP   A 1 62  ? 19.250  -5.925  -15.583 1.00 41.37  ?  62  ASP   A OD2   1 
ATOM   473  N  N     . THR   A 1 63  ? 21.534  -7.578  -10.937 1.00 39.68  ?  63  THR   A N     1 
ATOM   474  C  CA    . THR   A 1 63  ? 22.524  -7.386  -9.870  1.00 36.08  ?  63  THR   A CA    1 
ATOM   475  C  C     . THR   A 1 63  ? 23.029  -8.738  -9.336  1.00 36.98  ?  63  THR   A C     1 
ATOM   476  O  O     . THR   A 1 63  ? 24.243  -8.955  -9.184  1.00 35.66  ?  63  THR   A O     1 
ATOM   477  C  CB    . THR   A 1 63  ? 21.963  -6.493  -8.762  1.00 36.19  ?  63  THR   A CB    1 
ATOM   478  O  OG1   . THR   A 1 63  ? 21.720  -5.183  -9.302  1.00 36.74  ?  63  THR   A OG1   1 
ATOM   479  C  CG2   . THR   A 1 63  ? 22.917  -6.369  -7.597  1.00 36.87  ?  63  THR   A CG2   1 
ATOM   480  N  N     . LEU   A 1 64  ? 22.110  -9.660  -9.098  1.00 35.65  ?  64  LEU   A N     1 
ATOM   481  C  CA    . LEU   A 1 64  ? 22.467  -10.962 -8.546  1.00 35.27  ?  64  LEU   A CA    1 
ATOM   482  C  C     . LEU   A 1 64  ? 23.399  -11.696 -9.506  1.00 39.96  ?  64  LEU   A C     1 
ATOM   483  O  O     . LEU   A 1 64  ? 24.432  -12.209 -9.089  1.00 43.93  ?  64  LEU   A O     1 
ATOM   484  C  CB    . LEU   A 1 64  ? 21.216  -11.796 -8.244  1.00 34.81  ?  64  LEU   A CB    1 
ATOM   485  C  CG    . LEU   A 1 64  ? 21.409  -13.275 -7.880  1.00 34.44  ?  64  LEU   A CG    1 
ATOM   486  C  CD1   . LEU   A 1 64  ? 22.241  -13.433 -6.628  1.00 36.79  ?  64  LEU   A CD1   1 
ATOM   487  C  CD2   . LEU   A 1 64  ? 20.079  -13.978 -7.712  1.00 35.68  ?  64  LEU   A CD2   1 
ATOM   488  N  N     . ALA   A 1 65  ? 23.020  -11.765 -10.783 1.00 38.04  ?  65  ALA   A N     1 
ATOM   489  C  CA    . ALA   A 1 65  ? 23.814  -12.460 -11.801 1.00 39.32  ?  65  ALA   A CA    1 
ATOM   490  C  C     . ALA   A 1 65  ? 25.232  -11.892 -11.938 1.00 37.86  ?  65  ALA   A C     1 
ATOM   491  O  O     . ALA   A 1 65  ? 26.178  -12.632 -11.999 1.00 41.96  ?  65  ALA   A O     1 
ATOM   492  C  CB    . ALA   A 1 65  ? 23.084  -12.422 -13.147 1.00 42.76  ?  65  ALA   A CB    1 
ATOM   493  N  N     . LEU   A 1 66  ? 25.355  -10.560 -11.958 1.00 38.92  ?  66  LEU   A N     1 
ATOM   494  C  CA    . LEU   A 1 66  ? 26.639  -9.883  -12.084 1.00 39.14  ?  66  LEU   A CA    1 
ATOM   495  C  C     . LEU   A 1 66  ? 27.582  -10.125 -10.895 1.00 37.82  ?  66  LEU   A C     1 
ATOM   496  O  O     . LEU   A 1 66  ? 28.782  -10.355 -11.101 1.00 37.90  ?  66  LEU   A O     1 
ATOM   497  C  CB    . LEU   A 1 66  ? 26.416  -8.376  -12.308 1.00 44.58  ?  66  LEU   A CB    1 
ATOM   498  C  CG    . LEU   A 1 66  ? 27.558  -7.592  -12.961 1.00 46.37  ?  66  LEU   A CG    1 
ATOM   499  C  CD1   . LEU   A 1 66  ? 28.088  -8.264  -14.219 1.00 48.42  ?  66  LEU   A CD1   1 
ATOM   500  C  CD2   . LEU   A 1 66  ? 27.112  -6.179  -13.279 1.00 46.27  ?  66  LEU   A CD2   1 
ATOM   501  N  N     . TYR   A 1 67  ? 27.032  -10.105 -9.669  1.00 35.07  ?  67  TYR   A N     1 
ATOM   502  C  CA    . TYR   A 1 67  ? 27.802  -10.426 -8.460  1.00 38.05  ?  67  TYR   A CA    1 
ATOM   503  C  C     . TYR   A 1 67  ? 28.325  -11.864 -8.469  1.00 37.43  ?  67  TYR   A C     1 
ATOM   504  O  O     . TYR   A 1 67  ? 29.482  -12.118 -8.132  1.00 35.58  ?  67  TYR   A O     1 
ATOM   505  C  CB    . TYR   A 1 67  ? 26.981  -10.128 -7.176  1.00 38.58  ?  67  TYR   A CB    1 
ATOM   506  C  CG    . TYR   A 1 67  ? 27.151  -8.720  -6.659  1.00 36.60  ?  67  TYR   A CG    1 
ATOM   507  C  CD1   . TYR   A 1 67  ? 26.567  -7.653  -7.295  1.00 39.59  ?  67  TYR   A CD1   1 
ATOM   508  C  CD2   . TYR   A 1 67  ? 27.925  -8.459  -5.530  1.00 40.97  ?  67  TYR   A CD2   1 
ATOM   509  C  CE1   . TYR   A 1 67  ? 26.724  -6.358  -6.833  1.00 40.68  ?  67  TYR   A CE1   1 
ATOM   510  C  CE2   . TYR   A 1 67  ? 28.096  -7.170  -5.064  1.00 37.95  ?  67  TYR   A CE2   1 
ATOM   511  C  CZ    . TYR   A 1 67  ? 27.492  -6.129  -5.723  1.00 39.37  ?  67  TYR   A CZ    1 
ATOM   512  O  OH    . TYR   A 1 67  ? 27.636  -4.850  -5.278  1.00 38.43  ?  67  TYR   A OH    1 
ATOM   513  N  N     . LEU   A 1 68  ? 27.475  -12.789 -8.908  1.00 41.97  ?  68  LEU   A N     1 
ATOM   514  C  CA    . LEU   A 1 68  ? 27.882  -14.187 -9.142  1.00 43.54  ?  68  LEU   A CA    1 
ATOM   515  C  C     . LEU   A 1 68  ? 28.948  -14.309 -10.245 1.00 44.43  ?  68  LEU   A C     1 
ATOM   516  O  O     . LEU   A 1 68  ? 29.872  -15.095 -10.118 1.00 46.52  ?  68  LEU   A O     1 
ATOM   517  C  CB    . LEU   A 1 68  ? 26.665  -15.041 -9.501  1.00 43.99  ?  68  LEU   A CB    1 
ATOM   518  C  CG    . LEU   A 1 68  ? 25.620  -15.190 -8.396  1.00 44.95  ?  68  LEU   A CG    1 
ATOM   519  C  CD1   . LEU   A 1 68  ? 24.263  -15.615 -8.928  1.00 44.05  ?  68  LEU   A CD1   1 
ATOM   520  C  CD2   . LEU   A 1 68  ? 26.115  -16.145 -7.317  1.00 43.94  ?  68  LEU   A CD2   1 
ATOM   521  N  N     . ALA   A 1 69  ? 28.809  -13.511 -11.307 1.00 46.25  ?  69  ALA   A N     1 
ATOM   522  C  CA    . ALA   A 1 69  ? 29.759  -13.507 -12.435 1.00 46.99  ?  69  ALA   A CA    1 
ATOM   523  C  C     . ALA   A 1 69  ? 31.098  -12.864 -12.047 1.00 49.62  ?  69  ALA   A C     1 
ATOM   524  O  O     . ALA   A 1 69  ? 32.158  -13.311 -12.496 1.00 47.47  ?  69  ALA   A O     1 
ATOM   525  C  CB    . ALA   A 1 69  ? 29.164  -12.785 -13.641 1.00 44.98  ?  69  ALA   A CB    1 
ATOM   526  N  N     . CYS   A 1 70  ? 31.044  -11.819 -11.212 1.00 48.62  ?  70  CYS   A N     1 
ATOM   527  C  CA    . CYS   A 1 70  ? 32.257  -11.208 -10.632 1.00 43.87  ?  70  CYS   A CA    1 
ATOM   528  C  C     . CYS   A 1 70  ? 33.030  -12.134 -9.677  1.00 42.64  ?  70  CYS   A C     1 
ATOM   529  O  O     . CYS   A 1 70  ? 34.178  -11.821 -9.327  1.00 45.09  ?  70  CYS   A O     1 
ATOM   530  C  CB    . CYS   A 1 70  ? 31.928  -9.904  -9.937  1.00 39.88  ?  70  CYS   A CB    1 
ATOM   531  S  SG    . CYS   A 1 70  ? 31.454  -8.613  -11.066 1.00 46.57  ?  70  CYS   A SG    1 
ATOM   532  N  N     . GLY   A 1 71  ? 32.409  -13.246 -9.263  1.00 40.20  ?  71  GLY   A N     1 
ATOM   533  C  CA    . GLY   A 1 71  ? 33.066  -14.314 -8.509  1.00 39.51  ?  71  GLY   A CA    1 
ATOM   534  C  C     . GLY   A 1 71  ? 32.560  -14.543 -7.070  1.00 42.57  ?  71  GLY   A C     1 
ATOM   535  O  O     . GLY   A 1 71  ? 33.114  -15.396 -6.337  1.00 38.83  ?  71  GLY   A O     1 
ATOM   536  N  N     . ILE   A 1 72  ? 31.515  -13.828 -6.649  1.00 42.40  ?  72  ILE   A N     1 
ATOM   537  C  CA    . ILE   A 1 72  ? 30.889  -14.100 -5.322  1.00 42.27  ?  72  ILE   A CA    1 
ATOM   538  C  C     . ILE   A 1 72  ? 30.282  -15.508 -5.336  1.00 42.15  ?  72  ILE   A C     1 
ATOM   539  O  O     . ILE   A 1 72  ? 29.380  -15.795 -6.126  1.00 42.55  ?  72  ILE   A O     1 
ATOM   540  C  CB    . ILE   A 1 72  ? 29.827  -13.043 -4.905  1.00 39.33  ?  72  ILE   A CB    1 
ATOM   541  C  CG1   . ILE   A 1 72  ? 30.466  -11.647 -4.726  1.00 41.89  ?  72  ILE   A CG1   1 
ATOM   542  C  CG2   . ILE   A 1 72  ? 29.100  -13.440 -3.615  1.00 41.22  ?  72  ILE   A CG2   1 
ATOM   543  C  CD1   . ILE   A 1 72  ? 31.686  -11.620 -3.821  1.00 40.76  ?  72  ILE   A CD1   1 
ATOM   544  N  N     . ASP   A 1 73  ? 30.796  -16.354 -4.449  1.00 43.26  ?  73  ASP   A N     1 
ATOM   545  C  CA    . ASP   A 1 73  ? 30.464  -17.762 -4.371  1.00 45.30  ?  73  ASP   A CA    1 
ATOM   546  C  C     . ASP   A 1 73  ? 29.318  -17.916 -3.365  1.00 49.39  ?  73  ASP   A C     1 
ATOM   547  O  O     . ASP   A 1 73  ? 29.507  -17.615 -2.179  1.00 48.76  ?  73  ASP   A O     1 
ATOM   548  C  CB    . ASP   A 1 73  ? 31.709  -18.537 -3.920  1.00 47.48  ?  73  ASP   A CB    1 
ATOM   549  C  CG    . ASP   A 1 73  ? 31.469  -20.030 -3.749  1.00 53.24  ?  73  ASP   A CG    1 
ATOM   550  O  OD1   . ASP   A 1 73  ? 32.475  -20.761 -3.684  1.00 57.65  ?  73  ASP   A OD1   1 
ATOM   551  O  OD2   . ASP   A 1 73  ? 30.300  -20.481 -3.653  1.00 57.22  ?  73  ASP   A OD2   1 
ATOM   552  N  N     . PRO   A 1 74  ? 28.138  -18.402 -3.821  1.00 47.64  ?  74  PRO   A N     1 
ATOM   553  C  CA    . PRO   A 1 74  ? 27.001  -18.583 -2.921  1.00 47.98  ?  74  PRO   A CA    1 
ATOM   554  C  C     . PRO   A 1 74  ? 27.167  -19.722 -1.898  1.00 46.55  ?  74  PRO   A C     1 
ATOM   555  O  O     . PRO   A 1 74  ? 26.334  -19.869 -1.005  1.00 43.92  ?  74  PRO   A O     1 
ATOM   556  C  CB    . PRO   A 1 74  ? 25.837  -18.876 -3.879  1.00 47.94  ?  74  PRO   A CB    1 
ATOM   557  C  CG    . PRO   A 1 74  ? 26.471  -19.459 -5.078  1.00 49.30  ?  74  PRO   A CG    1 
ATOM   558  C  CD    . PRO   A 1 74  ? 27.796  -18.770 -5.210  1.00 48.26  ?  74  PRO   A CD    1 
ATOM   559  N  N     . GLU   A 1 75  ? 28.219  -20.518 -2.041  1.00 46.61  ?  75  GLU   A N     1 
ATOM   560  C  CA    . GLU   A 1 75  ? 28.539  -21.588 -1.086  1.00 48.83  ?  75  GLU   A CA    1 
ATOM   561  C  C     . GLU   A 1 75  ? 29.449  -21.103 0.046   1.00 46.66  ?  75  GLU   A C     1 
ATOM   562  O  O     . GLU   A 1 75  ? 29.415  -21.662 1.132   1.00 52.20  ?  75  GLU   A O     1 
ATOM   563  C  CB    . GLU   A 1 75  ? 29.174  -22.785 -1.823  1.00 48.00  ?  75  GLU   A CB    1 
ATOM   564  N  N     . LYS   A 1 76  ? 30.253  -20.070 -0.216  1.00 49.28  ?  76  LYS   A N     1 
ATOM   565  C  CA    . LYS   A 1 76  ? 31.150  -19.459 0.786   1.00 49.79  ?  76  LYS   A CA    1 
ATOM   566  C  C     . LYS   A 1 76  ? 30.537  -18.191 1.417   1.00 44.46  ?  76  LYS   A C     1 
ATOM   567  O  O     . LYS   A 1 76  ? 30.560  -18.028 2.617   1.00 45.77  ?  76  LYS   A O     1 
ATOM   568  C  CB    . LYS   A 1 76  ? 32.512  -19.132 0.160   1.00 53.22  ?  76  LYS   A CB    1 
ATOM   569  C  CG    . LYS   A 1 76  ? 33.295  -20.328 -0.381  1.00 60.96  ?  76  LYS   A CG    1 
ATOM   570  C  CD    . LYS   A 1 76  ? 33.744  -21.315 0.693   1.00 64.95  ?  76  LYS   A CD    1 
ATOM   571  C  CE    . LYS   A 1 76  ? 32.797  -22.499 0.845   1.00 67.02  ?  76  LYS   A CE    1 
ATOM   572  N  NZ    . LYS   A 1 76  ? 33.286  -23.445 1.885   1.00 70.22  ?  76  LYS   A NZ    1 
ATOM   573  N  N     . SER   A 1 77  ? 29.990  -17.311 0.590   1.00 41.03  ?  77  SER   A N     1 
ATOM   574  C  CA    . SER   A 1 77  ? 29.311  -16.103 1.027   1.00 36.96  ?  77  SER   A CA    1 
ATOM   575  C  C     . SER   A 1 77  ? 27.781  -16.293 1.057   1.00 37.10  ?  77  SER   A C     1 
ATOM   576  O  O     . SER   A 1 77  ? 27.261  -17.167 0.392   1.00 36.38  ?  77  SER   A O     1 
ATOM   577  C  CB    . SER   A 1 77  ? 29.686  -14.952 0.089   1.00 35.59  ?  77  SER   A CB    1 
ATOM   578  O  OG    . SER   A 1 77  ? 31.078  -14.696 0.155   1.00 32.21  ?  77  SER   A OG    1 
ATOM   579  N  N     . THR   A 1 78  ? 27.092  -15.447 1.834   1.00 34.40  ?  78  THR   A N     1 
ATOM   580  C  CA    . THR   A 1 78  ? 25.633  -15.367 1.884   1.00 31.30  ?  78  THR   A CA    1 
ATOM   581  C  C     . THR   A 1 78  ? 25.198  -14.234 0.968   1.00 33.56  ?  78  THR   A C     1 
ATOM   582  O  O     . THR   A 1 78  ? 25.514  -13.037 1.213   1.00 32.79  ?  78  THR   A O     1 
ATOM   583  C  CB    . THR   A 1 78  ? 25.129  -15.110 3.319   1.00 31.01  ?  78  THR   A CB    1 
ATOM   584  O  OG1   . THR   A 1 78  ? 25.532  -16.189 4.170   1.00 32.21  ?  78  THR   A OG1   1 
ATOM   585  C  CG2   . THR   A 1 78  ? 23.614  -14.996 3.385   1.00 31.40  ?  78  THR   A CG2   1 
ATOM   586  N  N     . ILE   A 1 79  ? 24.504  -14.600 -0.107  1.00 33.17  ?  79  ILE   A N     1 
ATOM   587  C  CA    . ILE   A 1 79  ? 23.954  -13.632 -1.069  1.00 33.16  ?  79  ILE   A CA    1 
ATOM   588  C  C     . ILE   A 1 79  ? 22.429  -13.865 -1.155  1.00 30.44  ?  79  ILE   A C     1 
ATOM   589  O  O     . ILE   A 1 79  ? 21.986  -15.015 -1.306  1.00 31.45  ?  79  ILE   A O     1 
ATOM   590  C  CB    . ILE   A 1 79  ? 24.697  -13.707 -2.447  1.00 32.10  ?  79  ILE   A CB    1 
ATOM   591  C  CG1   . ILE   A 1 79  ? 24.204  -12.622 -3.397  1.00 34.68  ?  79  ILE   A CG1   1 
ATOM   592  C  CG2   . ILE   A 1 79  ? 24.556  -15.055 -3.077  1.00 33.77  ?  79  ILE   A CG2   1 
ATOM   593  C  CD1   . ILE   A 1 79  ? 25.135  -12.333 -4.553  1.00 36.49  ?  79  ILE   A CD1   1 
ATOM   594  N  N     . PHE   A 1 80  ? 21.647  -12.797 -1.031  1.00 27.27  ?  80  PHE   A N     1 
ATOM   595  C  CA    . PHE   A 1 80  ? 20.170  -12.872 -0.925  1.00 28.14  ?  80  PHE   A CA    1 
ATOM   596  C  C     . PHE   A 1 80  ? 19.533  -11.524 -1.192  1.00 26.42  ?  80  PHE   A C     1 
ATOM   597  O  O     . PHE   A 1 80  ? 20.226  -10.494 -1.167  1.00 31.23  ?  80  PHE   A O     1 
ATOM   598  C  CB    . PHE   A 1 80  ? 19.734  -13.385 0.487   1.00 30.24  ?  80  PHE   A CB    1 
ATOM   599  C  CG    . PHE   A 1 80  ? 19.934  -12.369 1.618   1.00 27.07  ?  80  PHE   A CG    1 
ATOM   600  C  CD1   . PHE   A 1 80  ? 21.201  -12.083 2.098   1.00 26.10  ?  80  PHE   A CD1   1 
ATOM   601  C  CD2   . PHE   A 1 80  ? 18.851  -11.706 2.173   1.00 25.48  ?  80  PHE   A CD2   1 
ATOM   602  C  CE1   . PHE   A 1 80  ? 21.387  -11.171 3.109   1.00 26.83  ?  80  PHE   A CE1   1 
ATOM   603  C  CE2   . PHE   A 1 80  ? 19.019  -10.792 3.195   1.00 27.70  ?  80  PHE   A CE2   1 
ATOM   604  C  CZ    . PHE   A 1 80  ? 20.298  -10.537 3.692   1.00 29.36  ?  80  PHE   A CZ    1 
ATOM   605  N  N     . VAL   A 1 81  ? 18.221  -11.528 -1.417  1.00 27.84  ?  81  VAL   A N     1 
ATOM   606  C  CA    . VAL   A 1 81  ? 17.427  -10.296 -1.662  1.00 29.37  ?  81  VAL   A CA    1 
ATOM   607  C  C     . VAL   A 1 81  ? 16.831  -9.834  -0.324  1.00 30.56  ?  81  VAL   A C     1 
ATOM   608  O  O     . VAL   A 1 81  ? 16.222  -10.633 0.372   1.00 29.03  ?  81  VAL   A O     1 
ATOM   609  C  CB    . VAL   A 1 81  ? 16.308  -10.542 -2.720  1.00 30.37  ?  81  VAL   A CB    1 
ATOM   610  C  CG1   . VAL   A 1 81  ? 15.433  -9.311  -2.934  1.00 29.79  ?  81  VAL   A CG1   1 
ATOM   611  C  CG2   . VAL   A 1 81  ? 16.933  -10.983 -4.048  1.00 31.89  ?  81  VAL   A CG2   1 
ATOM   612  N  N     . GLN   A 1 82  ? 16.971  -8.536  -0.019  1.00 27.29  ?  82  GLN   A N     1 
ATOM   613  C  CA    . GLN   A 1 82  ? 16.571  -7.929  1.249   1.00 26.55  ?  82  GLN   A CA    1 
ATOM   614  C  C     . GLN   A 1 82  ? 15.118  -8.219  1.608   1.00 25.87  ?  82  GLN   A C     1 
ATOM   615  O  O     . GLN   A 1 82  ? 14.805  -8.559  2.739   1.00 24.29  ?  82  GLN   A O     1 
ATOM   616  C  CB    . GLN   A 1 82  ? 16.780  -6.379  1.185   1.00 25.05  ?  82  GLN   A CB    1 
ATOM   617  C  CG    . GLN   A 1 82  ? 16.778  -5.683  2.522   1.00 23.64  ?  82  GLN   A CG    1 
ATOM   618  C  CD    . GLN   A 1 82  ? 16.776  -4.160  2.410   1.00 26.70  ?  82  GLN   A CD    1 
ATOM   619  O  OE1   . GLN   A 1 82  ? 16.652  -3.594  1.329   1.00 29.88  ?  82  GLN   A OE1   1 
ATOM   620  N  NE2   . GLN   A 1 82  ? 16.922  -3.498  3.519   1.00 25.18  ?  82  GLN   A NE2   1 
ATOM   621  N  N     . SER   A 1 83  ? 14.228  -8.073  0.630   1.00 26.00  ?  83  SER   A N     1 
ATOM   622  C  CA    . SER   A 1 83  ? 12.788  -8.236  0.856   1.00 26.61  ?  83  SER   A CA    1 
ATOM   623  C  C     . SER   A 1 83  ? 12.344  -9.669  1.187   1.00 25.51  ?  83  SER   A C     1 
ATOM   624  O  O     . SER   A 1 83  ? 11.225  -9.857  1.649   1.00 28.12  ?  83  SER   A O     1 
ATOM   625  C  CB    . SER   A 1 83  ? 11.995  -7.717  -0.351  1.00 26.66  ?  83  SER   A CB    1 
ATOM   626  O  OG    . SER   A 1 83  ? 12.134  -8.587  -1.462  1.00 25.96  ?  83  SER   A OG    1 
ATOM   627  N  N     . HIS   A 1 84  ? 13.214  -10.645 0.983   1.00 25.67  ?  84  HIS   A N     1 
ATOM   628  C  CA    . HIS   A 1 84  ? 12.947  -12.062 1.278   1.00 26.59  ?  84  HIS   A CA    1 
ATOM   629  C  C     . HIS   A 1 84  ? 13.178  -12.423 2.752   1.00 27.81  ?  84  HIS   A C     1 
ATOM   630  O  O     . HIS   A 1 84  ? 12.870  -13.543 3.181   1.00 28.16  ?  84  HIS   A O     1 
ATOM   631  C  CB    . HIS   A 1 84  ? 13.800  -12.966 0.404   1.00 28.20  ?  84  HIS   A CB    1 
ATOM   632  C  CG    . HIS   A 1 84  ? 13.561  -12.815 -1.078  1.00 31.01  ?  84  HIS   A CG    1 
ATOM   633  N  ND1   . HIS   A 1 84  ? 14.074  -13.704 -2.002  1.00 30.41  ?  84  HIS   A ND1   1 
ATOM   634  C  CD2   . HIS   A 1 84  ? 12.868  -11.891 -1.790  1.00 30.69  ?  84  HIS   A CD2   1 
ATOM   635  C  CE1   . HIS   A 1 84  ? 13.706  -13.340 -3.213  1.00 30.87  ?  84  HIS   A CE1   1 
ATOM   636  N  NE2   . HIS   A 1 84  ? 12.972  -12.244 -3.116  1.00 34.35  ?  84  HIS   A NE2   1 
ATOM   637  N  N     . VAL   A 1 85  ? 13.692  -11.472 3.539   1.00 24.76  ?  85  VAL   A N     1 
ATOM   638  C  CA    . VAL   A 1 85  ? 13.961  -11.682 4.974   1.00 23.84  ?  85  VAL   A CA    1 
ATOM   639  C  C     . VAL   A 1 85  ? 13.202  -10.619 5.789   1.00 23.36  ?  85  VAL   A C     1 
ATOM   640  O  O     . VAL   A 1 85  ? 13.699  -9.500  5.941   1.00 26.79  ?  85  VAL   A O     1 
ATOM   641  C  CB    . VAL   A 1 85  ? 15.475  -11.583 5.244   1.00 24.05  ?  85  VAL   A CB    1 
ATOM   642  C  CG1   . VAL   A 1 85  ? 15.802  -11.864 6.733   1.00 24.42  ?  85  VAL   A CG1   1 
ATOM   643  C  CG2   . VAL   A 1 85  ? 16.222  -12.506 4.336   1.00 24.14  ?  85  VAL   A CG2   1 
ATOM   644  N  N     . PRO   A 1 86  ? 11.973  -10.939 6.270   1.00 26.66  ?  86  PRO   A N     1 
ATOM   645  C  CA    . PRO   A 1 86  ? 11.139  -9.953  6.966   1.00 24.98  ?  86  PRO   A CA    1 
ATOM   646  C  C     . PRO   A 1 86  ? 11.795  -9.302  8.193   1.00 24.94  ?  86  PRO   A C     1 
ATOM   647  O  O     . PRO   A 1 86  ? 11.373  -8.244  8.609   1.00 24.77  ?  86  PRO   A O     1 
ATOM   648  C  CB    . PRO   A 1 86  ? 9.931   -10.779 7.421   1.00 26.31  ?  86  PRO   A CB    1 
ATOM   649  C  CG    . PRO   A 1 86  ? 9.869   -11.922 6.455   1.00 26.92  ?  86  PRO   A CG    1 
ATOM   650  C  CD    . PRO   A 1 86  ? 11.302  -12.252 6.180   1.00 25.19  ?  86  PRO   A CD    1 
ATOM   651  N  N     . GLU   A 1 87  ? 12.832  -9.943  8.740   1.00 23.11  ?  87  GLU   A N     1 
ATOM   652  C  CA    . GLU   A 1 87  ? 13.527  -9.420  9.912   1.00 24.42  ?  87  GLU   A CA    1 
ATOM   653  C  C     . GLU   A 1 87  ? 14.076  -8.008  9.711   1.00 23.27  ?  87  GLU   A C     1 
ATOM   654  O  O     . GLU   A 1 87  ? 14.208  -7.293  10.685  1.00 24.71  ?  87  GLU   A O     1 
ATOM   655  C  CB    . GLU   A 1 87  ? 14.618  -10.390 10.356  1.00 26.96  ?  87  GLU   A CB    1 
ATOM   656  C  CG    . GLU   A 1 87  ? 14.076  -11.686 11.018  1.00 27.25  ?  87  GLU   A CG    1 
ATOM   657  C  CD    . GLU   A 1 87  ? 13.715  -12.778 10.035  1.00 29.33  ?  87  GLU   A CD    1 
ATOM   658  O  OE1   . GLU   A 1 87  ? 13.467  -12.498 8.841   1.00 27.26  ?  87  GLU   A OE1   1 
ATOM   659  O  OE2   . GLU   A 1 87  ? 13.652  -13.951 10.451  1.00 37.09  ?  87  GLU   A OE2   1 
ATOM   660  N  N     . HIS   A 1 88  ? 14.421  -7.641  8.456   1.00 22.38  ?  88  HIS   A N     1 
ATOM   661  C  CA    . HIS   A 1 88  ? 14.952  -6.322  8.097   1.00 22.12  ?  88  HIS   A CA    1 
ATOM   662  C  C     . HIS   A 1 88  ? 13.983  -5.214  8.403   1.00 24.43  ?  88  HIS   A C     1 
ATOM   663  O  O     . HIS   A 1 88  ? 14.326  -4.256  9.104   1.00 27.60  ?  88  HIS   A O     1 
ATOM   664  C  CB    . HIS   A 1 88  ? 15.414  -6.297  6.631   1.00 21.47  ?  88  HIS   A CB    1 
ATOM   665  C  CG    . HIS   A 1 88  ? 16.633  -7.118  6.377   1.00 21.70  ?  88  HIS   A CG    1 
ATOM   666  N  ND1   . HIS   A 1 88  ? 17.867  -6.568  6.131   1.00 22.56  ?  88  HIS   A ND1   1 
ATOM   667  C  CD2   . HIS   A 1 88  ? 16.814  -8.464  6.373   1.00 22.19  ?  88  HIS   A CD2   1 
ATOM   668  C  CE1   . HIS   A 1 88  ? 18.741  -7.536  5.935   1.00 24.63  ?  88  HIS   A CE1   1 
ATOM   669  N  NE2   . HIS   A 1 88  ? 18.127  -8.693  6.084   1.00 21.85  ?  88  HIS   A NE2   1 
ATOM   670  N  N     . ALA   A 1 89  ? 12.745  -5.357  7.925   1.00 24.18  ?  89  ALA   A N     1 
ATOM   671  C  CA    . ALA   A 1 89  ? 11.674  -4.401  8.226   1.00 22.70  ?  89  ALA   A CA    1 
ATOM   672  C  C     . ALA   A 1 89  ? 11.264  -4.440  9.732   1.00 23.85  ?  89  ALA   A C     1 
ATOM   673  O  O     . ALA   A 1 89  ? 11.024  -3.412  10.334  1.00 22.20  ?  89  ALA   A O     1 
ATOM   674  C  CB    . ALA   A 1 89  ? 10.477  -4.734  7.376   1.00 22.51  ?  89  ALA   A CB    1 
ATOM   675  N  N     . GLN   A 1 90  ? 11.203  -5.638  10.288  1.00 21.19  ?  90  GLN   A N     1 
ATOM   676  C  CA    . GLN   A 1 90  ? 10.905  -5.850  11.721  1.00 22.90  ?  90  GLN   A CA    1 
ATOM   677  C  C     . GLN   A 1 90  ? 11.884  -5.141  12.658  1.00 24.42  ?  90  GLN   A C     1 
ATOM   678  O  O     . GLN   A 1 90  ? 11.471  -4.414  13.570  1.00 28.70  ?  90  GLN   A O     1 
ATOM   679  C  CB    . GLN   A 1 90  ? 10.878  -7.359  12.009  1.00 22.80  ?  90  GLN   A CB    1 
ATOM   680  C  CG    . GLN   A 1 90  ? 9.640   -8.087  11.477  1.00 22.16  ?  90  GLN   A CG    1 
ATOM   681  C  CD    . GLN   A 1 90  ? 9.672   -9.578  11.798  1.00 24.80  ?  90  GLN   A CD    1 
ATOM   682  O  OE1   . GLN   A 1 90  ? 10.302  -10.340 11.082  1.00 26.54  ?  90  GLN   A OE1   1 
ATOM   683  N  NE2   . GLN   A 1 90  ? 9.044   -9.987  12.905  1.00 25.22  ?  90  GLN   A NE2   1 
ATOM   684  N  N     . LEU   A 1 91  ? 13.186  -5.336  12.429  1.00 21.36  ?  91  LEU   A N     1 
ATOM   685  C  CA    . LEU   A 1 91  ? 14.174  -4.670  13.209  1.00 21.42  ?  91  LEU   A CA    1 
ATOM   686  C  C     . LEU   A 1 91  ? 14.228  -3.177  12.921  1.00 21.46  ?  91  LEU   A C     1 
ATOM   687  O  O     . LEU   A 1 91  ? 14.472  -2.414  13.843  1.00 25.03  ?  91  LEU   A O     1 
ATOM   688  C  CB    . LEU   A 1 91  ? 15.580  -5.294  13.063  1.00 22.68  ?  91  LEU   A CB    1 
ATOM   689  C  CG    . LEU   A 1 91  ? 16.639  -4.746  14.034  1.00 23.65  ?  91  LEU   A CG    1 
ATOM   690  C  CD1   . LEU   A 1 91  ? 16.167  -4.911  15.478  1.00 23.30  ?  91  LEU   A CD1   1 
ATOM   691  C  CD2   . LEU   A 1 91  ? 17.981  -5.448  13.874  1.00 24.99  ?  91  LEU   A CD2   1 
ATOM   692  N  N     . GLY   A 1 92  ? 14.056  -2.809  11.657  1.00 22.25  ?  92  GLY   A N     1 
ATOM   693  C  CA    . GLY   A 1 92  ? 13.868  -1.437  11.204  1.00 24.91  ?  92  GLY   A CA    1 
ATOM   694  C  C     . GLY   A 1 92  ? 12.867  -0.661  12.072  1.00 27.71  ?  92  GLY   A C     1 
ATOM   695  O  O     . GLY   A 1 92  ? 13.185  0.413   12.575  1.00 30.10  ?  92  GLY   A O     1 
ATOM   696  N  N     . TRP   A 1 93  ? 11.653  -1.176  12.220  1.00 26.82  ?  93  TRP   A N     1 
ATOM   697  C  CA    . TRP   A 1 93  ? 10.630  -0.496  13.028  1.00 28.09  ?  93  TRP   A CA    1 
ATOM   698  C  C     . TRP   A 1 93  ? 11.083  -0.355  14.491  1.00 29.51  ?  93  TRP   A C     1 
ATOM   699  O  O     . TRP   A 1 93  ? 11.024  0.745   15.037  1.00 27.15  ?  93  TRP   A O     1 
ATOM   700  C  CB    . TRP   A 1 93  ? 9.259   -1.196  13.037  1.00 26.56  ?  93  TRP   A CB    1 
ATOM   701  C  CG    . TRP   A 1 93  ? 8.402   -0.505  14.007  1.00 25.99  ?  93  TRP   A CG    1 
ATOM   702  C  CD1   . TRP   A 1 93  ? 8.080   -0.920  15.273  1.00 27.35  ?  93  TRP   A CD1   1 
ATOM   703  C  CD2   . TRP   A 1 93  ? 7.863   0.806   13.865  1.00 27.79  ?  93  TRP   A CD2   1 
ATOM   704  N  NE1   . TRP   A 1 93  ? 7.351   0.053   15.906  1.00 28.06  ?  93  TRP   A NE1   1 
ATOM   705  C  CE2   . TRP   A 1 93  ? 7.196   1.117   15.060  1.00 28.12  ?  93  TRP   A CE2   1 
ATOM   706  C  CE3   . TRP   A 1 93  ? 7.853   1.745   12.816  1.00 30.08  ?  93  TRP   A CE3   1 
ATOM   707  C  CZ2   . TRP   A 1 93  ? 6.522   2.324   15.246  1.00 30.13  ?  93  TRP   A CZ2   1 
ATOM   708  C  CZ3   . TRP   A 1 93  ? 7.191   2.959   13.011  1.00 29.53  ?  93  TRP   A CZ3   1 
ATOM   709  C  CH2   . TRP   A 1 93  ? 6.536   3.231   14.211  1.00 29.03  ?  93  TRP   A CH2   1 
ATOM   710  N  N     . ALA   A 1 94  ? 11.545  -1.449  15.095  1.00 26.91  ?  94  ALA   A N     1 
ATOM   711  C  CA    . ALA   A 1 94  ? 11.993  -1.423  16.490  1.00 31.68  ?  94  ALA   A CA    1 
ATOM   712  C  C     . ALA   A 1 94  ? 13.099  -0.380  16.712  1.00 31.59  ?  94  ALA   A C     1 
ATOM   713  O  O     . ALA   A 1 94  ? 13.071  0.323   17.722  1.00 33.97  ?  94  ALA   A O     1 
ATOM   714  C  CB    . ALA   A 1 94  ? 12.453  -2.799  16.961  1.00 29.86  ?  94  ALA   A CB    1 
ATOM   715  N  N     . LEU   A 1 95  ? 14.019  -0.263  15.753  1.00 28.66  ?  95  LEU   A N     1 
ATOM   716  C  CA    . LEU   A 1 95  ? 15.145  0.666   15.850  1.00 31.33  ?  95  LEU   A CA    1 
ATOM   717  C  C     . LEU   A 1 95  ? 14.710  2.103   15.591  1.00 32.07  ?  95  LEU   A C     1 
ATOM   718  O  O     . LEU   A 1 95  ? 15.401  3.017   16.043  1.00 33.19  ?  95  LEU   A O     1 
ATOM   719  C  CB    . LEU   A 1 95  ? 16.314  0.272   14.928  1.00 29.89  ?  95  LEU   A CB    1 
ATOM   720  C  CG    . LEU   A 1 95  ? 17.108  -1.004  15.245  1.00 28.60  ?  95  LEU   A CG    1 
ATOM   721  C  CD1   . LEU   A 1 95  ? 18.331  -1.079  14.356  1.00 27.86  ?  95  LEU   A CD1   1 
ATOM   722  C  CD2   . LEU   A 1 95  ? 17.537  -1.156  16.693  1.00 29.48  ?  95  LEU   A CD2   1 
ATOM   723  N  N     . ASN   A 1 96  ? 13.578  2.297   14.896  1.00 29.87  ?  96  ASN   A N     1 
ATOM   724  C  CA    . ASN   A 1 96  ? 12.952  3.643   14.768  1.00 31.13  ?  96  ASN   A CA    1 
ATOM   725  C  C     . ASN   A 1 96  ? 12.668  4.252   16.146  1.00 32.08  ?  96  ASN   A C     1 
ATOM   726  O  O     . ASN   A 1 96  ? 12.864  5.459   16.372  1.00 34.40  ?  96  ASN   A O     1 
ATOM   727  C  CB    . ASN   A 1 96  ? 11.637  3.592   13.967  1.00 30.96  ?  96  ASN   A CB    1 
ATOM   728  C  CG    . ASN   A 1 96  ? 11.779  4.084   12.539  1.00 33.03  ?  96  ASN   A CG    1 
ATOM   729  O  OD1   . ASN   A 1 96  ? 12.736  4.759   12.184  1.00 37.50  ?  96  ASN   A OD1   1 
ATOM   730  N  ND2   . ASN   A 1 96  ? 10.787  3.786   11.721  1.00 37.79  ?  96  ASN   A ND2   1 
ATOM   731  N  N     . CYS   A 1 97  ? 12.237  3.392   17.056  1.00 32.57  ?  97  CYS   A N     1 
ATOM   732  C  CA    . CYS   A 1 97  ? 11.894  3.749   18.418  1.00 36.74  ?  97  CYS   A CA    1 
ATOM   733  C  C     . CYS   A 1 97  ? 13.078  4.042   19.351  1.00 37.24  ?  97  CYS   A C     1 
ATOM   734  O  O     . CYS   A 1 97  ? 12.851  4.492   20.491  1.00 42.68  ?  97  CYS   A O     1 
ATOM   735  C  CB    . CYS   A 1 97  ? 10.996  2.648   19.012  1.00 37.64  ?  97  CYS   A CB    1 
ATOM   736  S  SG    . CYS   A 1 97  ? 9.443   2.423   18.081  1.00 36.26  ?  97  CYS   A SG    1 
ATOM   737  N  N     . TYR   A 1 98  ? 14.310  3.803   18.875  1.00 36.80  ?  98  TYR   A N     1 
ATOM   738  C  CA    . TYR   A 1 98  ? 15.551  4.141   19.589  1.00 37.16  ?  98  TYR   A CA    1 
ATOM   739  C  C     . TYR   A 1 98  ? 16.452  5.091   18.812  1.00 36.97  ?  98  TYR   A C     1 
ATOM   740  O  O     . TYR   A 1 98  ? 17.601  5.242   19.148  1.00 41.36  ?  98  TYR   A O     1 
ATOM   741  C  CB    . TYR   A 1 98  ? 16.299  2.851   19.942  1.00 37.84  ?  98  TYR   A CB    1 
ATOM   742  C  CG    . TYR   A 1 98  ? 15.504  1.978   20.863  1.00 39.64  ?  98  TYR   A CG    1 
ATOM   743  C  CD1   . TYR   A 1 98  ? 15.675  2.043   22.234  1.00 40.40  ?  98  TYR   A CD1   1 
ATOM   744  C  CD2   . TYR   A 1 98  ? 14.545  1.117   20.364  1.00 34.47  ?  98  TYR   A CD2   1 
ATOM   745  C  CE1   . TYR   A 1 98  ? 14.916  1.251   23.081  1.00 42.88  ?  98  TYR   A CE1   1 
ATOM   746  C  CE2   . TYR   A 1 98  ? 13.795  0.329   21.194  1.00 39.03  ?  98  TYR   A CE2   1 
ATOM   747  C  CZ    . TYR   A 1 98  ? 13.968  0.396   22.552  1.00 38.40  ?  98  TYR   A CZ    1 
ATOM   748  O  OH    . TYR   A 1 98  ? 13.223  -0.400  23.383  1.00 34.58  ?  98  TYR   A OH    1 
ATOM   749  N  N     . THR   A 1 99  ? 15.920  5.706   17.760  1.00 38.54  ?  99  THR   A N     1 
ATOM   750  C  CA    . THR   A 1 99  ? 16.630  6.643   16.896  1.00 40.45  ?  99  THR   A CA    1 
ATOM   751  C  C     . THR   A 1 99  ? 15.951  8.001   17.056  1.00 42.58  ?  99  THR   A C     1 
ATOM   752  O  O     . THR   A 1 99  ? 14.744  8.103   16.863  1.00 43.60  ?  99  THR   A O     1 
ATOM   753  C  CB    . THR   A 1 99  ? 16.528  6.221   15.414  1.00 37.38  ?  99  THR   A CB    1 
ATOM   754  O  OG1   . THR   A 1 99  ? 17.097  4.929   15.274  1.00 35.04  ?  99  THR   A OG1   1 
ATOM   755  C  CG2   . THR   A 1 99  ? 17.258  7.191   14.465  1.00 37.50  ?  99  THR   A CG2   1 
ATOM   756  N  N     . TYR   A 1 100 ? 16.720  9.023   17.423  1.00 48.80  ?  100 TYR   A N     1 
ATOM   757  C  CA    . TYR   A 1 100 ? 16.191  10.395  17.557  1.00 50.81  ?  100 TYR   A CA    1 
ATOM   758  C  C     . TYR   A 1 100 ? 15.826  10.914  16.181  1.00 49.17  ?  100 TYR   A C     1 
ATOM   759  O  O     . TYR   A 1 100 ? 16.543  10.663  15.224  1.00 47.77  ?  100 TYR   A O     1 
ATOM   760  C  CB    . TYR   A 1 100 ? 17.222  11.318  18.209  1.00 52.36  ?  100 TYR   A CB    1 
ATOM   761  C  CG    . TYR   A 1 100 ? 17.415  11.076  19.694  1.00 55.78  ?  100 TYR   A CG    1 
ATOM   762  C  CD1   . TYR   A 1 100 ? 16.470  11.522  20.622  1.00 56.67  ?  100 TYR   A CD1   1 
ATOM   763  C  CD2   . TYR   A 1 100 ? 18.540  10.413  20.176  1.00 56.23  ?  100 TYR   A CD2   1 
ATOM   764  C  CE1   . TYR   A 1 100 ? 16.640  11.303  21.981  1.00 57.38  ?  100 TYR   A CE1   1 
ATOM   765  C  CE2   . TYR   A 1 100 ? 18.717  10.193  21.538  1.00 57.67  ?  100 TYR   A CE2   1 
ATOM   766  C  CZ    . TYR   A 1 100 ? 17.773  10.638  22.431  1.00 58.83  ?  100 TYR   A CZ    1 
ATOM   767  O  OH    . TYR   A 1 100 ? 17.977  10.405  23.766  1.00 62.73  ?  100 TYR   A OH    1 
ATOM   768  N  N     . PHE   A 1 101 ? 14.696  11.613  16.090  1.00 56.04  ?  101 PHE   A N     1 
ATOM   769  C  CA    . PHE   A 1 101 ? 14.305  12.356  14.871  1.00 57.81  ?  101 PHE   A CA    1 
ATOM   770  C  C     . PHE   A 1 101 ? 15.429  13.307  14.416  1.00 56.19  ?  101 PHE   A C     1 
ATOM   771  O  O     . PHE   A 1 101 ? 15.708  13.426  13.223  1.00 54.51  ?  101 PHE   A O     1 
ATOM   772  C  CB    . PHE   A 1 101 ? 13.002  13.145  15.138  1.00 59.91  ?  101 PHE   A CB    1 
ATOM   773  C  CG    . PHE   A 1 101 ? 12.498  13.943  13.947  1.00 62.43  ?  101 PHE   A CG    1 
ATOM   774  C  CD1   . PHE   A 1 101 ? 11.505  13.436  13.122  1.00 60.35  ?  101 PHE   A CD1   1 
ATOM   775  C  CD2   . PHE   A 1 101 ? 13.008  15.211  13.667  1.00 62.37  ?  101 PHE   A CD2   1 
ATOM   776  C  CE1   . PHE   A 1 101 ? 11.043  14.166  12.043  1.00 59.54  ?  101 PHE   A CE1   1 
ATOM   777  C  CE2   . PHE   A 1 101 ? 12.554  15.936  12.582  1.00 62.19  ?  101 PHE   A CE2   1 
ATOM   778  C  CZ    . PHE   A 1 101 ? 11.572  15.411  11.777  1.00 60.67  ?  101 PHE   A CZ    1 
ATOM   779  N  N     . GLY   A 1 102 ? 16.068  13.971  15.384  1.00 59.14  ?  102 GLY   A N     1 
ATOM   780  C  CA    . GLY   A 1 102 ? 17.196  14.880  15.121  1.00 58.93  ?  102 GLY   A CA    1 
ATOM   781  C  C     . GLY   A 1 102 ? 18.331  14.273  14.310  1.00 57.56  ?  102 GLY   A C     1 
ATOM   782  O  O     . GLY   A 1 102 ? 18.904  14.926  13.441  1.00 57.05  ?  102 GLY   A O     1 
ATOM   783  N  N     . GLU   A 1 103 ? 18.643  13.007  14.588  1.00 54.69  ?  103 GLU   A N     1 
ATOM   784  C  CA    . GLU   A 1 103 ? 19.730  12.289  13.911  1.00 54.17  ?  103 GLU   A CA    1 
ATOM   785  C  C     . GLU   A 1 103 ? 19.427  12.034  12.437  1.00 52.87  ?  103 GLU   A C     1 
ATOM   786  O  O     . GLU   A 1 103 ? 20.341  12.035  11.617  1.00 56.99  ?  103 GLU   A O     1 
ATOM   787  C  CB    . GLU   A 1 103 ? 20.025  10.951  14.608  1.00 55.59  ?  103 GLU   A CB    1 
ATOM   788  C  CG    . GLU   A 1 103 ? 20.534  11.090  16.036  1.00 55.18  ?  103 GLU   A CG    1 
ATOM   789  C  CD    . GLU   A 1 103 ? 20.570  9.785   16.801  1.00 58.65  ?  103 GLU   A CD    1 
ATOM   790  O  OE1   . GLU   A 1 103 ? 21.452  9.633   17.675  1.00 61.17  ?  103 GLU   A OE1   1 
ATOM   791  O  OE2   . GLU   A 1 103 ? 19.711  8.905   16.571  1.00 58.12  ?  103 GLU   A OE2   1 
ATOM   792  N  N     . LEU   A 1 104 ? 18.151  11.803  12.113  1.00 51.57  ?  104 LEU   A N     1 
ATOM   793  C  CA    . LEU   A 1 104 ? 17.691  11.643  10.721  1.00 49.13  ?  104 LEU   A CA    1 
ATOM   794  C  C     . LEU   A 1 104 ? 17.634  12.976  9.960   1.00 53.59  ?  104 LEU   A C     1 
ATOM   795  O  O     . LEU   A 1 104 ? 17.942  13.025  8.771   1.00 53.23  ?  104 LEU   A O     1 
ATOM   796  C  CB    . LEU   A 1 104 ? 16.310  10.957  10.676  1.00 46.16  ?  104 LEU   A CB    1 
ATOM   797  C  CG    . LEU   A 1 104 ? 16.297  9.469   10.976  1.00 44.86  ?  104 LEU   A CG    1 
ATOM   798  C  CD1   . LEU   A 1 104 ? 14.887  8.914   10.823  1.00 45.16  ?  104 LEU   A CD1   1 
ATOM   799  C  CD2   . LEU   A 1 104 ? 17.266  8.723   10.070  1.00 41.99  ?  104 LEU   A CD2   1 
ATOM   800  N  N     . SER   A 1 105 ? 17.240  14.049  10.643  1.00 58.16  ?  105 SER   A N     1 
ATOM   801  C  CA    . SER   A 1 105 ? 17.239  15.387  10.041  1.00 59.63  ?  105 SER   A CA    1 
ATOM   802  C  C     . SER   A 1 105 ? 18.653  15.949  9.890   1.00 61.53  ?  105 SER   A C     1 
ATOM   803  O  O     . SER   A 1 105 ? 18.887  16.756  9.000   1.00 64.62  ?  105 SER   A O     1 
ATOM   804  C  CB    . SER   A 1 105 ? 16.352  16.341  10.843  1.00 59.43  ?  105 SER   A CB    1 
ATOM   805  O  OG    . SER   A 1 105 ? 16.773  16.425  12.182  1.00 67.28  ?  105 SER   A OG    1 
ATOM   806  N  N     . ARG   A 1 106 ? 19.596  15.483  10.718  1.00 68.63  ?  106 ARG   A N     1 
ATOM   807  C  CA    . ARG   A 1 106 ? 21.015  15.933  10.667  1.00 73.09  ?  106 ARG   A CA    1 
ATOM   808  C  C     . ARG   A 1 106 ? 21.798  15.414  9.460   1.00 72.74  ?  106 ARG   A C     1 
ATOM   809  O  O     . ARG   A 1 106 ? 22.925  15.842  9.236   1.00 78.98  ?  106 ARG   A O     1 
ATOM   810  C  CB    . ARG   A 1 106 ? 21.781  15.574  11.969  1.00 74.53  ?  106 ARG   A CB    1 
ATOM   811  C  CG    . ARG   A 1 106 ? 21.900  16.735  12.944  1.00 74.27  ?  106 ARG   A CG    1 
ATOM   812  C  CD    . ARG   A 1 106 ? 22.640  16.394  14.239  1.00 71.54  ?  106 ARG   A CD    1 
ATOM   813  N  NE    . ARG   A 1 106 ? 21.791  15.816  15.290  1.00 73.24  ?  106 ARG   A NE    1 
ATOM   814  C  CZ    . ARG   A 1 106 ? 20.790  16.444  15.925  1.00 74.72  ?  106 ARG   A CZ    1 
ATOM   815  N  NH1   . ARG   A 1 106 ? 20.441  17.697  15.613  1.00 74.80  ?  106 ARG   A NH1   1 
ATOM   816  N  NH2   . ARG   A 1 106 ? 20.104  15.805  16.877  1.00 72.46  ?  106 ARG   A NH2   1 
ATOM   817  N  N     . MET   A 1 107 ? 21.222  14.472  8.716   1.00 76.16  ?  107 MET   A N     1 
ATOM   818  C  CA    . MET   A 1 107 ? 21.814  13.954  7.490   1.00 77.16  ?  107 MET   A CA    1 
ATOM   819  C  C     . MET   A 1 107 ? 21.223  14.700  6.304   1.00 86.74  ?  107 MET   A C     1 
ATOM   820  O  O     . MET   A 1 107 ? 19.999  14.728  6.157   1.00 93.96  ?  107 MET   A O     1 
ATOM   821  C  CB    . MET   A 1 107 ? 21.524  12.460  7.372   1.00 72.49  ?  107 MET   A CB    1 
ATOM   822  C  CG    . MET   A 1 107 ? 22.077  11.664  8.537   1.00 71.64  ?  107 MET   A CG    1 
ATOM   823  S  SD    . MET   A 1 107 ? 22.527  9.991   8.107   1.00 65.32  ?  107 MET   A SD    1 
ATOM   824  C  CE    . MET   A 1 107 ? 22.989  9.396   9.722   1.00 66.89  ?  107 MET   A CE    1 
ATOM   825  N  N     . THR   A 1 108 ? 22.103  15.296  5.483   1.00 86.18  ?  108 THR   A N     1 
ATOM   826  C  CA    . THR   A 1 108 ? 21.766  16.179  4.339   1.00 86.73  ?  108 THR   A CA    1 
ATOM   827  C  C     . THR   A 1 108 ? 20.277  16.589  4.193   1.00 81.20  ?  108 THR   A C     1 
ATOM   828  O  O     . THR   A 1 108 ? 19.495  15.966  3.467   1.00 73.64  ?  108 THR   A O     1 
ATOM   829  C  CB    . THR   A 1 108 ? 22.333  15.591  3.017   1.00 92.31  ?  108 THR   A CB    1 
ATOM   830  O  OG1   . THR   A 1 108 ? 23.730  15.298  3.191   1.00 90.88  ?  108 THR   A OG1   1 
ATOM   831  C  CG2   . THR   A 1 108 ? 22.172  16.566  1.830   1.00 97.41  ?  108 THR   A CG2   1 
ATOM   832  N  N     . TYR   A 1 117 ? 9.059   21.988  0.223   1.00 77.03  ?  117 TYR   A N     1 
ATOM   833  C  CA    . TYR   A 1 117 ? 10.484  21.727  0.067   1.00 79.00  ?  117 TYR   A CA    1 
ATOM   834  C  C     . TYR   A 1 117 ? 10.850  20.290  0.501   1.00 80.90  ?  117 TYR   A C     1 
ATOM   835  O  O     . TYR   A 1 117 ? 11.047  19.408  -0.346  1.00 76.74  ?  117 TYR   A O     1 
ATOM   836  C  CB    . TYR   A 1 117 ? 11.287  22.770  0.842   1.00 77.55  ?  117 TYR   A CB    1 
ATOM   837  N  N     . ALA   A 1 118 ? 10.927  20.079  1.818   1.00 81.06  ?  118 ALA   A N     1 
ATOM   838  C  CA    . ALA   A 1 118 ? 11.143  18.766  2.432   1.00 74.84  ?  118 ALA   A CA    1 
ATOM   839  C  C     . ALA   A 1 118 ? 9.818   18.053  2.707   1.00 72.60  ?  118 ALA   A C     1 
ATOM   840  O  O     . ALA   A 1 118 ? 9.790   16.841  2.878   1.00 74.07  ?  118 ALA   A O     1 
ATOM   841  C  CB    . ALA   A 1 118 ? 11.923  18.918  3.728   1.00 73.50  ?  118 ALA   A CB    1 
ATOM   842  N  N     . GLU   A 1 119 ? 8.721   18.810  2.746   1.00 70.76  ?  119 GLU   A N     1 
ATOM   843  C  CA    . GLU   A 1 119 ? 7.380   18.249  2.916   1.00 72.32  ?  119 GLU   A CA    1 
ATOM   844  C  C     . GLU   A 1 119 ? 6.997   17.292  1.771   1.00 70.78  ?  119 GLU   A C     1 
ATOM   845  O  O     . GLU   A 1 119 ? 6.145   16.423  1.956   1.00 73.92  ?  119 GLU   A O     1 
ATOM   846  C  CB    . GLU   A 1 119 ? 6.345   19.378  3.033   1.00 68.78  ?  119 GLU   A CB    1 
ATOM   847  N  N     . ASN   A 1 120 ? 7.641   17.454  0.611   1.00 70.58  ?  120 ASN   A N     1 
ATOM   848  C  CA    . ASN   A 1 120 ? 7.353   16.679  -0.599  1.00 70.49  ?  120 ASN   A CA    1 
ATOM   849  C  C     . ASN   A 1 120 ? 8.271   15.454  -0.832  1.00 67.50  ?  120 ASN   A C     1 
ATOM   850  O  O     . ASN   A 1 120 ? 8.125   14.763  -1.848  1.00 63.37  ?  120 ASN   A O     1 
ATOM   851  C  CB    . ASN   A 1 120 ? 7.398   17.597  -1.824  1.00 69.89  ?  120 ASN   A CB    1 
ATOM   852  N  N     . ILE   A 1 121 ? 9.217   15.204  0.082   1.00 62.76  ?  121 ILE   A N     1 
ATOM   853  C  CA    . ILE   A 1 121 ? 10.011  13.960  0.062   1.00 57.01  ?  121 ILE   A CA    1 
ATOM   854  C  C     . ILE   A 1 121 ? 9.223   12.836  0.742   1.00 52.06  ?  121 ILE   A C     1 
ATOM   855  O  O     . ILE   A 1 121 ? 8.559   13.059  1.764   1.00 57.20  ?  121 ILE   A O     1 
ATOM   856  C  CB    . ILE   A 1 121 ? 11.428  14.118  0.700   1.00 59.17  ?  121 ILE   A CB    1 
ATOM   857  C  CG1   . ILE   A 1 121 ? 11.394  14.373  2.222   1.00 62.02  ?  121 ILE   A CG1   1 
ATOM   858  C  CG2   . ILE   A 1 121 ? 12.201  15.234  0.002   1.00 58.23  ?  121 ILE   A CG2   1 
ATOM   859  C  CD1   . ILE   A 1 121 ? 12.616  13.872  2.959   1.00 61.55  ?  121 ILE   A CD1   1 
ATOM   860  N  N     . ASN   A 1 122 ? 9.294   11.625  0.194   1.00 47.73  ?  122 ASN   A N     1 
ATOM   861  C  CA    . ASN   A 1 122 ? 8.641   10.494  0.835   1.00 45.44  ?  122 ASN   A CA    1 
ATOM   862  C  C     . ASN   A 1 122 ? 9.356   10.132  2.149   1.00 42.90  ?  122 ASN   A C     1 
ATOM   863  O  O     . ASN   A 1 122 ? 10.544  10.364  2.285   1.00 45.38  ?  122 ASN   A O     1 
ATOM   864  C  CB    . ASN   A 1 122 ? 8.469   9.308   -0.131  1.00 45.11  ?  122 ASN   A CB    1 
ATOM   865  C  CG    . ASN   A 1 122 ? 9.759   8.619   -0.463  1.00 43.21  ?  122 ASN   A CG    1 
ATOM   866  O  OD1   . ASN   A 1 122 ? 10.363  8.010   0.402   1.00 45.00  ?  122 ASN   A OD1   1 
ATOM   867  N  ND2   . ASN   A 1 122 ? 10.166  8.668   -1.732  1.00 44.57  ?  122 ASN   A ND2   1 
ATOM   868  N  N     . ALA   A 1 123 ? 8.609   9.596   3.114   1.00 44.38  ?  123 ALA   A N     1 
ATOM   869  C  CA    . ALA   A 1 123 ? 9.125   9.223   4.437   1.00 43.44  ?  123 ALA   A CA    1 
ATOM   870  C  C     . ALA   A 1 123 ? 10.225  8.166   4.374   1.00 45.22  ?  123 ALA   A C     1 
ATOM   871  O  O     . ALA   A 1 123 ? 10.994  8.054   5.321   1.00 46.42  ?  123 ALA   A O     1 
ATOM   872  C  CB    . ALA   A 1 123 ? 8.001   8.736   5.348   1.00 46.26  ?  123 ALA   A CB    1 
ATOM   873  N  N     . GLY   A 1 124 ? 10.265  7.398   3.279   1.00 42.61  ?  124 GLY   A N     1 
ATOM   874  C  CA    . GLY   A 1 124 ? 11.342  6.456   2.978   1.00 43.67  ?  124 GLY   A CA    1 
ATOM   875  C  C     . GLY   A 1 124 ? 12.708  7.116   2.860   1.00 44.02  ?  124 GLY   A C     1 
ATOM   876  O  O     . GLY   A 1 124 ? 13.664  6.665   3.482   1.00 38.15  ?  124 GLY   A O     1 
ATOM   877  N  N     . LEU   A 1 125 ? 12.764  8.202   2.091   1.00 46.36  ?  125 LEU   A N     1 
ATOM   878  C  CA    . LEU   A 1 125 ? 13.977  8.987   1.882   1.00 49.29  ?  125 LEU   A CA    1 
ATOM   879  C  C     . LEU   A 1 125 ? 14.510  9.608   3.166   1.00 50.17  ?  125 LEU   A C     1 
ATOM   880  O  O     . LEU   A 1 125 ? 15.678  9.930   3.248   1.00 59.52  ?  125 LEU   A O     1 
ATOM   881  C  CB    . LEU   A 1 125 ? 13.726  10.100  0.855   1.00 54.93  ?  125 LEU   A CB    1 
ATOM   882  C  CG    . LEU   A 1 125 ? 14.961  10.673  0.147   1.00 58.71  ?  125 LEU   A CG    1 
ATOM   883  C  CD1   . LEU   A 1 125 ? 15.525  9.662   -0.830  1.00 60.69  ?  125 LEU   A CD1   1 
ATOM   884  C  CD2   . LEU   A 1 125 ? 14.622  11.952  -0.588  1.00 58.80  ?  125 LEU   A CD2   1 
ATOM   885  N  N     . PHE   A 1 126 ? 13.641  9.774   4.154   1.00 50.12  ?  126 PHE   A N     1 
ATOM   886  C  CA    . PHE   A 1 126 ? 13.975  10.320  5.456   1.00 47.91  ?  126 PHE   A CA    1 
ATOM   887  C  C     . PHE   A 1 126 ? 14.390  9.246   6.458   1.00 48.01  ?  126 PHE   A C     1 
ATOM   888  O  O     . PHE   A 1 126 ? 15.232  9.507   7.311   1.00 46.41  ?  126 PHE   A O     1 
ATOM   889  C  CB    . PHE   A 1 126 ? 12.766  11.096  5.991   1.00 49.37  ?  126 PHE   A CB    1 
ATOM   890  C  CG    . PHE   A 1 126 ? 12.969  11.695  7.363   1.00 51.41  ?  126 PHE   A CG    1 
ATOM   891  C  CD1   . PHE   A 1 126 ? 12.407  11.103  8.481   1.00 51.83  ?  126 PHE   A CD1   1 
ATOM   892  C  CD2   . PHE   A 1 126 ? 13.709  12.863  7.531   1.00 55.31  ?  126 PHE   A CD2   1 
ATOM   893  C  CE1   . PHE   A 1 126 ? 12.582  11.647  9.744   1.00 54.37  ?  126 PHE   A CE1   1 
ATOM   894  C  CE2   . PHE   A 1 126 ? 13.899  13.409  8.792   1.00 55.03  ?  126 PHE   A CE2   1 
ATOM   895  C  CZ    . PHE   A 1 126 ? 13.331  12.801  9.900   1.00 57.31  ?  126 PHE   A CZ    1 
ATOM   896  N  N     . ASP   A 1 127 ? 13.785  8.061   6.364   1.00 42.61  ?  127 ASP   A N     1 
ATOM   897  C  CA    . ASP   A 1 127 ? 13.891  7.029   7.389   1.00 40.61  ?  127 ASP   A CA    1 
ATOM   898  C  C     . ASP   A 1 127 ? 14.835  5.896   7.030   1.00 36.88  ?  127 ASP   A C     1 
ATOM   899  O  O     . ASP   A 1 127 ? 15.115  5.072   7.886   1.00 34.03  ?  127 ASP   A O     1 
ATOM   900  C  CB    . ASP   A 1 127 ? 12.494  6.424   7.647   1.00 41.97  ?  127 ASP   A CB    1 
ATOM   901  C  CG    . ASP   A 1 127 ? 12.336  5.875   9.038   1.00 41.16  ?  127 ASP   A CG    1 
ATOM   902  O  OD1   . ASP   A 1 127 ? 13.090  6.268   9.943   1.00 43.40  ?  127 ASP   A OD1   1 
ATOM   903  O  OD2   . ASP   A 1 127 ? 11.435  5.040   9.232   1.00 44.54  ?  127 ASP   A OD2   1 
ATOM   904  N  N     . TYR   A 1 128 ? 15.325  5.851   5.780   1.00 33.90  ?  128 TYR   A N     1 
ATOM   905  C  CA    . TYR   A 1 128 ? 16.116  4.704   5.283   1.00 34.70  ?  128 TYR   A CA    1 
ATOM   906  C  C     . TYR   A 1 128 ? 17.412  4.450   6.085   1.00 33.80  ?  128 TYR   A C     1 
ATOM   907  O  O     . TYR   A 1 128 ? 17.896  3.309   6.099   1.00 36.07  ?  128 TYR   A O     1 
ATOM   908  C  CB    . TYR   A 1 128 ? 16.440  4.823   3.775   1.00 33.49  ?  128 TYR   A CB    1 
ATOM   909  C  CG    . TYR   A 1 128 ? 17.539  5.819   3.461   1.00 39.91  ?  128 TYR   A CG    1 
ATOM   910  C  CD1   . TYR   A 1 128 ? 17.239  7.138   3.119   1.00 40.33  ?  128 TYR   A CD1   1 
ATOM   911  C  CD2   . TYR   A 1 128 ? 18.891  5.453   3.540   1.00 39.97  ?  128 TYR   A CD2   1 
ATOM   912  C  CE1   . TYR   A 1 128 ? 18.249  8.052   2.847   1.00 40.76  ?  128 TYR   A CE1   1 
ATOM   913  C  CE2   . TYR   A 1 128 ? 19.896  6.369   3.277   1.00 38.88  ?  128 TYR   A CE2   1 
ATOM   914  C  CZ    . TYR   A 1 128 ? 19.564  7.663   2.938   1.00 38.66  ?  128 TYR   A CZ    1 
ATOM   915  O  OH    . TYR   A 1 128 ? 20.546  8.574   2.701   1.00 40.04  ?  128 TYR   A OH    1 
ATOM   916  N  N     . PRO   A 1 129 ? 18.004  5.487   6.719   1.00 34.12  ?  129 PRO   A N     1 
ATOM   917  C  CA    . PRO   A 1 129 ? 19.217  5.182   7.486   1.00 36.74  ?  129 PRO   A CA    1 
ATOM   918  C  C     . PRO   A 1 129 ? 18.963  4.237   8.669   1.00 34.53  ?  129 PRO   A C     1 
ATOM   919  O  O     . PRO   A 1 129 ? 19.878  3.544   9.100   1.00 35.32  ?  129 PRO   A O     1 
ATOM   920  C  CB    . PRO   A 1 129 ? 19.690  6.571   7.950   1.00 35.87  ?  129 PRO   A CB    1 
ATOM   921  C  CG    . PRO   A 1 129 ? 19.171  7.491   6.912   1.00 35.42  ?  129 PRO   A CG    1 
ATOM   922  C  CD    . PRO   A 1 129 ? 17.803  6.949   6.636   1.00 35.05  ?  129 PRO   A CD    1 
ATOM   923  N  N     . VAL   A 1 130 ? 17.727  4.183   9.150   1.00 31.86  ?  130 VAL   A N     1 
ATOM   924  C  CA    . VAL   A 1 130 ? 17.328  3.295   10.237  1.00 33.11  ?  130 VAL   A CA    1 
ATOM   925  C  C     . VAL   A 1 130 ? 17.223  1.872   9.699   1.00 31.63  ?  130 VAL   A C     1 
ATOM   926  O  O     . VAL   A 1 130 ? 17.603  0.952   10.371  1.00 30.92  ?  130 VAL   A O     1 
ATOM   927  C  CB    . VAL   A 1 130 ? 15.995  3.755   10.901  1.00 34.85  ?  130 VAL   A CB    1 
ATOM   928  C  CG1   . VAL   A 1 130 ? 15.566  2.811   12.027  1.00 35.76  ?  130 VAL   A CG1   1 
ATOM   929  C  CG2   . VAL   A 1 130 ? 16.138  5.144   11.485  1.00 35.60  ?  130 VAL   A CG2   1 
ATOM   930  N  N     . LEU   A 1 131 ? 16.719  1.719   8.472   1.00 34.10  ?  131 LEU   A N     1 
ATOM   931  C  CA    . LEU   A 1 131 ? 16.698  0.429   7.786   1.00 31.72  ?  131 LEU   A CA    1 
ATOM   932  C  C     . LEU   A 1 131 ? 18.136  -0.075  7.575   1.00 30.53  ?  131 LEU   A C     1 
ATOM   933  O  O     . LEU   A 1 131 ? 18.438  -1.227  7.832   1.00 28.99  ?  131 LEU   A O     1 
ATOM   934  C  CB    . LEU   A 1 131 ? 15.951  0.530   6.448   1.00 31.11  ?  131 LEU   A CB    1 
ATOM   935  C  CG    . LEU   A 1 131 ? 15.753  -0.775  5.655   1.00 31.73  ?  131 LEU   A CG    1 
ATOM   936  C  CD1   . LEU   A 1 131 ? 14.978  -1.799  6.473   1.00 29.56  ?  131 LEU   A CD1   1 
ATOM   937  C  CD2   . LEU   A 1 131 ? 15.020  -0.508  4.354   1.00 35.18  ?  131 LEU   A CD2   1 
ATOM   938  N  N     . MET   A 1 132 ? 19.019  0.824   7.136   1.00 30.80  ?  132 MET   A N     1 
ATOM   939  C  CA    . MET   A 1 132 ? 20.450  0.509   6.980   1.00 28.66  ?  132 MET   A CA    1 
ATOM   940  C  C     . MET   A 1 132 ? 21.040  0.000   8.299   1.00 25.10  ?  132 MET   A C     1 
ATOM   941  O  O     . MET   A 1 132 ? 21.731  -1.024  8.310   1.00 29.72  ?  132 MET   A O     1 
ATOM   942  C  CB    . MET   A 1 132 ? 21.249  1.713   6.429   1.00 31.14  ?  132 MET   A CB    1 
ATOM   943  C  CG    . MET   A 1 132 ? 22.773  1.501   6.471   1.00 33.17  ?  132 MET   A CG    1 
ATOM   944  S  SD    . MET   A 1 132 ? 23.717  2.630   5.480   1.00 39.89  ?  132 MET   A SD    1 
ATOM   945  C  CE    . MET   A 1 132 ? 25.391  2.102   5.862   1.00 38.83  ?  132 MET   A CE    1 
ATOM   946  N  N     . ALA   A 1 133 ? 20.762  0.696   9.402   1.00 23.84  ?  133 ALA   A N     1 
ATOM   947  C  CA    . ALA   A 1 133 ? 21.153  0.235   10.743  1.00 23.63  ?  133 ALA   A CA    1 
ATOM   948  C  C     . ALA   A 1 133 ? 20.659  -1.177  11.046  1.00 26.62  ?  133 ALA   A C     1 
ATOM   949  O  O     . ALA   A 1 133 ? 21.457  -2.043  11.440  1.00 25.11  ?  133 ALA   A O     1 
ATOM   950  C  CB    . ALA   A 1 133 ? 20.695  1.204   11.824  1.00 28.05  ?  133 ALA   A CB    1 
ATOM   951  N  N     . ALA   A 1 134 ? 19.364  -1.427  10.825  1.00 26.45  ?  134 ALA   A N     1 
ATOM   952  C  CA    . ALA   A 1 134 ? 18.798  -2.769  10.983  1.00 25.21  ?  134 ALA   A CA    1 
ATOM   953  C  C     . ALA   A 1 134 ? 19.456  -3.819  10.097  1.00 23.93  ?  134 ALA   A C     1 
ATOM   954  O  O     . ALA   A 1 134 ? 19.801  -4.882  10.560  1.00 28.80  ?  134 ALA   A O     1 
ATOM   955  C  CB    . ALA   A 1 134 ? 17.290  -2.724  10.742  1.00 25.25  ?  134 ALA   A CB    1 
ATOM   956  N  N     . ASP   A 1 135 ? 19.582  -3.534  8.797   1.00 25.19  ?  135 ASP   A N     1 
ATOM   957  C  CA    . ASP   A 1 135 ? 20.260  -4.424  7.860   1.00 24.53  ?  135 ASP   A CA    1 
ATOM   958  C  C     . ASP   A 1 135 ? 21.607  -4.948  8.412   1.00 27.47  ?  135 ASP   A C     1 
ATOM   959  O  O     . ASP   A 1 135 ? 21.887  -6.162  8.333   1.00 26.01  ?  135 ASP   A O     1 
ATOM   960  C  CB    . ASP   A 1 135 ? 20.553  -3.726  6.513   1.00 25.30  ?  135 ASP   A CB    1 
ATOM   961  C  CG    . ASP   A 1 135 ? 19.312  -3.299  5.746   1.00 27.70  ?  135 ASP   A CG    1 
ATOM   962  O  OD1   . ASP   A 1 135 ? 18.226  -3.953  5.840   1.00 26.88  ?  135 ASP   A OD1   1 
ATOM   963  O  OD2   . ASP   A 1 135 ? 19.416  -2.264  5.045   1.00 26.44  ?  135 ASP   A OD2   1 
ATOM   964  N  N     . ILE   A 1 136 ? 22.420  -4.027  8.955   1.00 24.89  ?  136 ILE   A N     1 
ATOM   965  C  CA    . ILE   A 1 136 ? 23.758  -4.313  9.498   1.00 25.02  ?  136 ILE   A CA    1 
ATOM   966  C  C     . ILE   A 1 136 ? 23.681  -5.070  10.836  1.00 25.54  ?  136 ILE   A C     1 
ATOM   967  O  O     . ILE   A 1 136 ? 24.323  -6.122  10.998  1.00 25.52  ?  136 ILE   A O     1 
ATOM   968  C  CB    . ILE   A 1 136 ? 24.579  -3.006  9.669   1.00 28.12  ?  136 ILE   A CB    1 
ATOM   969  C  CG1   . ILE   A 1 136 ? 24.930  -2.393  8.293   1.00 29.00  ?  136 ILE   A CG1   1 
ATOM   970  C  CG2   . ILE   A 1 136 ? 25.874  -3.248  10.472  1.00 28.34  ?  136 ILE   A CG2   1 
ATOM   971  C  CD1   . ILE   A 1 136 ? 25.293  -0.913  8.346   1.00 30.19  ?  136 ILE   A CD1   1 
ATOM   972  N  N     . LEU   A 1 137 ? 22.871  -4.568  11.772  1.00 24.19  ?  137 LEU   A N     1 
ATOM   973  C  CA    . LEU   A 1 137 ? 22.846  -5.091  13.138  1.00 22.37  ?  137 LEU   A CA    1 
ATOM   974  C  C     . LEU   A 1 137 ? 22.242  -6.477  13.289  1.00 24.66  ?  137 LEU   A C     1 
ATOM   975  O  O     . LEU   A 1 137 ? 22.554  -7.153  14.278  1.00 23.14  ?  137 LEU   A O     1 
ATOM   976  C  CB    . LEU   A 1 137 ? 22.202  -4.075  14.073  1.00 26.05  ?  137 LEU   A CB    1 
ATOM   977  C  CG    . LEU   A 1 137 ? 22.826  -2.650  14.105  1.00 26.68  ?  137 LEU   A CG    1 
ATOM   978  C  CD1   . LEU   A 1 137 ? 22.129  -1.769  15.120  1.00 29.10  ?  137 LEU   A CD1   1 
ATOM   979  C  CD2   . LEU   A 1 137 ? 24.321  -2.687  14.346  1.00 27.93  ?  137 LEU   A CD2   1 
ATOM   980  N  N     . LEU   A 1 138 ? 21.405  -6.900  12.322  1.00 27.10  ?  138 LEU   A N     1 
ATOM   981  C  CA    . LEU   A 1 138 ? 20.743  -8.197  12.346  1.00 26.04  ?  138 LEU   A CA    1 
ATOM   982  C  C     . LEU   A 1 138 ? 21.713  -9.363  12.324  1.00 26.00  ?  138 LEU   A C     1 
ATOM   983  O  O     . LEU   A 1 138 ? 21.453  -10.372 12.971  1.00 27.30  ?  138 LEU   A O     1 
ATOM   984  C  CB    . LEU   A 1 138 ? 19.817  -8.382  11.124  1.00 27.16  ?  138 LEU   A CB    1 
ATOM   985  C  CG    . LEU   A 1 138 ? 18.375  -7.950  11.212  1.00 26.81  ?  138 LEU   A CG    1 
ATOM   986  C  CD1   . LEU   A 1 138 ? 17.732  -8.043  9.813   1.00 29.10  ?  138 LEU   A CD1   1 
ATOM   987  C  CD2   . LEU   A 1 138 ? 17.613  -8.820  12.200  1.00 26.12  ?  138 LEU   A CD2   1 
ATOM   988  N  N     . TYR   A 1 139 ? 22.816  -9.204  11.589  1.00 27.05  ?  139 TYR   A N     1 
ATOM   989  C  CA    . TYR   A 1 139 ? 23.817  -10.237 11.379  1.00 29.43  ?  139 TYR   A CA    1 
ATOM   990  C  C     . TYR   A 1 139 ? 25.052  -10.144 12.271  1.00 30.71  ?  139 TYR   A C     1 
ATOM   991  O  O     . TYR   A 1 139 ? 26.079  -10.754 11.952  1.00 29.68  ?  139 TYR   A O     1 
ATOM   992  C  CB    . TYR   A 1 139 ? 24.212  -10.262 9.893   1.00 28.99  ?  139 TYR   A CB    1 
ATOM   993  C  CG    . TYR   A 1 139 ? 22.967  -10.425 9.055   1.00 29.52  ?  139 TYR   A CG    1 
ATOM   994  C  CD1   . TYR   A 1 139 ? 22.369  -11.676 8.888   1.00 28.83  ?  139 TYR   A CD1   1 
ATOM   995  C  CD2   . TYR   A 1 139 ? 22.322  -9.324  8.524   1.00 28.37  ?  139 TYR   A CD2   1 
ATOM   996  C  CE1   . TYR   A 1 139 ? 21.193  -11.809 8.164   1.00 28.02  ?  139 TYR   A CE1   1 
ATOM   997  C  CE2   . TYR   A 1 139 ? 21.145  -9.464  7.778   1.00 28.52  ?  139 TYR   A CE2   1 
ATOM   998  C  CZ    . TYR   A 1 139 ? 20.589  -10.690 7.632   1.00 27.07  ?  139 TYR   A CZ    1 
ATOM   999  O  OH    . TYR   A 1 139 ? 19.443  -10.809 6.912   1.00 28.44  ?  139 TYR   A OH    1 
ATOM   1000 N  N     . GLN   A 1 140 ? 24.950  -9.433  13.399  1.00 29.88  ?  140 GLN   A N     1 
ATOM   1001 C  CA    . GLN   A 1 140 ? 26.056  -9.298  14.351  1.00 29.53  ?  140 GLN   A CA    1 
ATOM   1002 C  C     . GLN   A 1 140 ? 27.339  -8.906  13.593  1.00 30.89  ?  140 GLN   A C     1 
ATOM   1003 O  O     . GLN   A 1 140 ? 28.431  -9.426  13.870  1.00 31.46  ?  140 GLN   A O     1 
ATOM   1004 C  CB    . GLN   A 1 140 ? 26.237  -10.594 15.154  1.00 29.26  ?  140 GLN   A CB    1 
ATOM   1005 C  CG    . GLN   A 1 140 ? 25.002  -11.019 15.982  1.00 32.57  ?  140 GLN   A CG    1 
ATOM   1006 C  CD    . GLN   A 1 140 ? 24.723  -10.077 17.176  1.00 33.08  ?  140 GLN   A CD    1 
ATOM   1007 O  OE1   . GLN   A 1 140 ? 25.653  -9.609  17.857  1.00 29.57  ?  140 GLN   A OE1   1 
ATOM   1008 N  NE2   . GLN   A 1 140 ? 23.456  -9.761  17.404  1.00 27.91  ?  140 GLN   A NE2   1 
ATOM   1009 N  N     . THR   A 1 141 ? 27.169  -7.998  12.624  1.00 28.61  ?  141 THR   A N     1 
ATOM   1010 C  CA    . THR   A 1 141 ? 28.213  -7.622  11.687  1.00 28.99  ?  141 THR   A CA    1 
ATOM   1011 C  C     . THR   A 1 141 ? 29.402  -6.965  12.426  1.00 28.68  ?  141 THR   A C     1 
ATOM   1012 O  O     . THR   A 1 141 ? 29.200  -6.146  13.322  1.00 31.29  ?  141 THR   A O     1 
ATOM   1013 C  CB    . THR   A 1 141 ? 27.646  -6.643  10.631  1.00 27.61  ?  141 THR   A CB    1 
ATOM   1014 O  OG1   . THR   A 1 141 ? 26.607  -7.323  9.910   1.00 26.04  ?  141 THR   A OG1   1 
ATOM   1015 C  CG2   . THR   A 1 141 ? 28.708  -6.186  9.634   1.00 24.95  ?  141 THR   A CG2   1 
ATOM   1016 N  N     . ASN   A 1 142 ? 30.614  -7.350  12.047  1.00 25.56  ?  142 ASN   A N     1 
ATOM   1017 C  CA    . ASN   A 1 142 ? 31.859  -6.738  12.570  1.00 27.15  ?  142 ASN   A CA    1 
ATOM   1018 C  C     . ASN   A 1 142 ? 32.312  -5.570  11.688  1.00 28.83  ?  142 ASN   A C     1 
ATOM   1019 O  O     . ASN   A 1 142 ? 32.611  -4.489  12.190  1.00 29.84  ?  142 ASN   A O     1 
ATOM   1020 C  CB    . ASN   A 1 142 ? 32.956  -7.784  12.717  1.00 26.85  ?  142 ASN   A CB    1 
ATOM   1021 C  CG    . ASN   A 1 142 ? 32.550  -8.932  13.614  1.00 28.02  ?  142 ASN   A CG    1 
ATOM   1022 O  OD1   . ASN   A 1 142 ? 32.293  -10.026 13.149  1.00 27.65  ?  142 ASN   A OD1   1 
ATOM   1023 N  ND2   . ASN   A 1 142 ? 32.414  -8.661  14.904  1.00 31.22  ?  142 ASN   A ND2   1 
ATOM   1024 N  N     . LEU   A 1 143 ? 32.308  -5.786  10.367  1.00 30.83  ?  143 LEU   A N     1 
ATOM   1025 C  CA    . LEU   A 1 143 ? 32.891  -4.855  9.375   1.00 30.70  ?  143 LEU   A CA    1 
ATOM   1026 C  C     . LEU   A 1 143 ? 31.890  -4.475  8.294   1.00 30.93  ?  143 LEU   A C     1 
ATOM   1027 O  O     . LEU   A 1 143 ? 31.183  -5.333  7.790   1.00 26.19  ?  143 LEU   A O     1 
ATOM   1028 C  CB    . LEU   A 1 143 ? 34.114  -5.507  8.726   1.00 32.28  ?  143 LEU   A CB    1 
ATOM   1029 C  CG    . LEU   A 1 143 ? 35.274  -5.798  9.699   1.00 33.31  ?  143 LEU   A CG    1 
ATOM   1030 C  CD1   . LEU   A 1 143 ? 36.285  -6.784  9.136   1.00 33.04  ?  143 LEU   A CD1   1 
ATOM   1031 C  CD2   . LEU   A 1 143 ? 35.965  -4.508  10.152  1.00 36.24  ?  143 LEU   A CD2   1 
ATOM   1032 N  N     . VAL   A 1 144 ? 31.774  -3.183  7.991   1.00 31.78  ?  144 VAL   A N     1 
ATOM   1033 C  CA    . VAL   A 1 144 ? 30.940  -2.704  6.879   1.00 32.81  ?  144 VAL   A CA    1 
ATOM   1034 C  C     . VAL   A 1 144 ? 31.820  -1.871  5.940   1.00 35.28  ?  144 VAL   A C     1 
ATOM   1035 O  O     . VAL   A 1 144 ? 32.281  -0.787  6.335   1.00 37.20  ?  144 VAL   A O     1 
ATOM   1036 C  CB    . VAL   A 1 144 ? 29.741  -1.868  7.369   1.00 32.70  ?  144 VAL   A CB    1 
ATOM   1037 C  CG1   . VAL   A 1 144 ? 28.801  -1.561  6.235   1.00 32.27  ?  144 VAL   A CG1   1 
ATOM   1038 C  CG2   . VAL   A 1 144 ? 28.980  -2.617  8.450   1.00 34.06  ?  144 VAL   A CG2   1 
ATOM   1039 N  N     . PRO   A 1 145 ? 32.089  -2.381  4.720   1.00 34.96  ?  145 PRO   A N     1 
ATOM   1040 C  CA    . PRO   A 1 145 ? 32.801  -1.595  3.709   1.00 39.08  ?  145 PRO   A CA    1 
ATOM   1041 C  C     . PRO   A 1 145 ? 31.911  -0.475  3.208   1.00 43.83  ?  145 PRO   A C     1 
ATOM   1042 O  O     . PRO   A 1 145 ? 30.897  -0.738  2.585   1.00 49.75  ?  145 PRO   A O     1 
ATOM   1043 C  CB    . PRO   A 1 145 ? 33.067  -2.603  2.575   1.00 38.98  ?  145 PRO   A CB    1 
ATOM   1044 C  CG    . PRO   A 1 145 ? 32.751  -3.946  3.126   1.00 40.02  ?  145 PRO   A CG    1 
ATOM   1045 C  CD    . PRO   A 1 145 ? 31.743  -3.721  4.209   1.00 36.95  ?  145 PRO   A CD    1 
ATOM   1046 N  N     . VAL   A 1 146 ? 32.269  0.764   3.488   1.00 47.93  ?  146 VAL   A N     1 
ATOM   1047 C  CA    . VAL   A 1 146 ? 31.440  1.907   3.103   1.00 51.84  ?  146 VAL   A CA    1 
ATOM   1048 C  C     . VAL   A 1 146 ? 32.281  2.951   2.375   1.00 53.76  ?  146 VAL   A C     1 
ATOM   1049 O  O     . VAL   A 1 146 ? 33.465  3.114   2.670   1.00 52.83  ?  146 VAL   A O     1 
ATOM   1050 C  CB    . VAL   A 1 146 ? 30.752  2.572   4.319   1.00 54.78  ?  146 VAL   A CB    1 
ATOM   1051 C  CG1   . VAL   A 1 146 ? 29.660  1.674   4.874   1.00 57.28  ?  146 VAL   A CG1   1 
ATOM   1052 C  CG2   . VAL   A 1 146 ? 31.754  2.935   5.413   1.00 54.53  ?  146 VAL   A CG2   1 
ATOM   1053 N  N     . GLY   A 1 147 ? 31.660  3.653   1.427   1.00 54.59  ?  147 GLY   A N     1 
ATOM   1054 C  CA    . GLY   A 1 147 ? 32.249  4.868   0.812   1.00 56.83  ?  147 GLY   A CA    1 
ATOM   1055 C  C     . GLY   A 1 147 ? 31.969  6.085   1.670   1.00 54.32  ?  147 GLY   A C     1 
ATOM   1056 O  O     . GLY   A 1 147 ? 31.278  5.970   2.683   1.00 60.08  ?  147 GLY   A O     1 
ATOM   1057 N  N     . GLU   A 1 148 ? 32.487  7.249   1.280   1.00 57.57  ?  148 GLU   A N     1 
ATOM   1058 C  CA    . GLU   A 1 148 ? 32.354  8.472   2.092   1.00 59.24  ?  148 GLU   A CA    1 
ATOM   1059 C  C     . GLU   A 1 148 ? 30.920  9.001   2.176   1.00 62.76  ?  148 GLU   A C     1 
ATOM   1060 O  O     . GLU   A 1 148 ? 30.532  9.584   3.190   1.00 66.37  ?  148 GLU   A O     1 
ATOM   1061 C  CB    . GLU   A 1 148 ? 33.272  9.580   1.568   1.00 61.95  ?  148 GLU   A CB    1 
ATOM   1062 N  N     . ASP   A 1 149 ? 30.149  8.805   1.107   1.00 69.43  ?  149 ASP   A N     1 
ATOM   1063 C  CA    . ASP   A 1 149 ? 28.714  9.129   1.097   1.00 67.86  ?  149 ASP   A CA    1 
ATOM   1064 C  C     . ASP   A 1 149 ? 27.908  8.437   2.221   1.00 62.36  ?  149 ASP   A C     1 
ATOM   1065 O  O     . ASP   A 1 149 ? 26.889  8.976   2.656   1.00 58.47  ?  149 ASP   A O     1 
ATOM   1066 C  CB    . ASP   A 1 149 ? 28.083  8.845   -0.287  1.00 73.38  ?  149 ASP   A CB    1 
ATOM   1067 C  CG    . ASP   A 1 149 ? 28.339  7.429   -0.786  1.00 80.10  ?  149 ASP   A CG    1 
ATOM   1068 O  OD1   . ASP   A 1 149 ? 27.387  6.783   -1.269  1.00 85.30  ?  149 ASP   A OD1   1 
ATOM   1069 O  OD2   . ASP   A 1 149 ? 29.498  6.969   -0.710  1.00 89.35  ?  149 ASP   A OD2   1 
ATOM   1070 N  N     . GLN   A 1 150 ? 28.396  7.284   2.703   1.00 56.92  ?  150 GLN   A N     1 
ATOM   1071 C  CA    . GLN   A 1 150 ? 27.704  6.463   3.701   1.00 54.68  ?  150 GLN   A CA    1 
ATOM   1072 C  C     . GLN   A 1 150 ? 28.420  6.324   5.055   1.00 53.88  ?  150 GLN   A C     1 
ATOM   1073 O  O     . GLN   A 1 150 ? 28.072  5.450   5.854   1.00 48.22  ?  150 GLN   A O     1 
ATOM   1074 C  CB    . GLN   A 1 150 ? 27.402  5.083   3.109   1.00 52.70  ?  150 GLN   A CB    1 
ATOM   1075 C  CG    . GLN   A 1 150 ? 26.101  5.038   2.331   1.00 50.32  ?  150 GLN   A CG    1 
ATOM   1076 C  CD    . GLN   A 1 150 ? 25.990  3.823   1.453   1.00 48.74  ?  150 GLN   A CD    1 
ATOM   1077 O  OE1   . GLN   A 1 150 ? 26.940  3.066   1.298   1.00 49.33  ?  150 GLN   A OE1   1 
ATOM   1078 N  NE2   . GLN   A 1 150 ? 24.821  3.630   0.864   1.00 50.47  ?  150 GLN   A NE2   1 
ATOM   1079 N  N     . LYS   A 1 151 ? 29.396  7.194   5.317   1.00 54.41  ?  151 LYS   A N     1 
ATOM   1080 C  CA    . LYS   A 1 151 ? 30.145  7.179   6.576   1.00 52.19  ?  151 LYS   A CA    1 
ATOM   1081 C  C     . LYS   A 1 151 ? 29.292  7.675   7.744   1.00 50.28  ?  151 LYS   A C     1 
ATOM   1082 O  O     . LYS   A 1 151 ? 29.354  7.129   8.844   1.00 53.54  ?  151 LYS   A O     1 
ATOM   1083 C  CB    . LYS   A 1 151 ? 31.413  8.036   6.465   1.00 56.81  ?  151 LYS   A CB    1 
ATOM   1084 C  CG    . LYS   A 1 151 ? 32.569  7.404   5.693   1.00 59.11  ?  151 LYS   A CG    1 
ATOM   1085 C  CD    . LYS   A 1 151 ? 33.542  6.650   6.583   1.00 60.05  ?  151 LYS   A CD    1 
ATOM   1086 N  N     . GLN   A 1 152 ? 28.513  8.720   7.502   1.00 46.32  ?  152 GLN   A N     1 
ATOM   1087 C  CA    . GLN   A 1 152 ? 27.570  9.254   8.483   1.00 50.01  ?  152 GLN   A CA    1 
ATOM   1088 C  C     . GLN   A 1 152 ? 26.514  8.202   8.909   1.00 48.48  ?  152 GLN   A C     1 
ATOM   1089 O  O     . GLN   A 1 152 ? 26.155  8.102   10.104  1.00 42.49  ?  152 GLN   A O     1 
ATOM   1090 C  CB    . GLN   A 1 152 ? 26.886  10.498  7.900   1.00 56.04  ?  152 GLN   A CB    1 
ATOM   1091 C  CG    . GLN   A 1 152 ? 26.165  11.354  8.922   1.00 59.61  ?  152 GLN   A CG    1 
ATOM   1092 C  CD    . GLN   A 1 152 ? 25.641  12.657  8.345   1.00 57.74  ?  152 GLN   A CD    1 
ATOM   1093 O  OE1   . GLN   A 1 152 ? 25.382  12.766  7.144   1.00 59.78  ?  152 GLN   A OE1   1 
ATOM   1094 N  NE2   . GLN   A 1 152 ? 25.464  13.646  9.205   1.00 59.76  ?  152 GLN   A NE2   1 
ATOM   1095 N  N     . HIS   A 1 153 ? 26.086  7.385   7.939   1.00 41.47  ?  153 HIS   A N     1 
ATOM   1096 C  CA    . HIS   A 1 153 ? 25.079  6.327   8.146   1.00 40.37  ?  153 HIS   A CA    1 
ATOM   1097 C  C     . HIS   A 1 153 ? 25.602  5.214   9.056   1.00 36.73  ?  153 HIS   A C     1 
ATOM   1098 O  O     . HIS   A 1 153 ? 24.875  4.753   9.931   1.00 33.99  ?  153 HIS   A O     1 
ATOM   1099 C  CB    . HIS   A 1 153 ? 24.650  5.712   6.817   1.00 40.45  ?  153 HIS   A CB    1 
ATOM   1100 C  CG    . HIS   A 1 153 ? 24.063  6.698   5.851   1.00 45.17  ?  153 HIS   A CG    1 
ATOM   1101 N  ND1   . HIS   A 1 153 ? 24.836  7.552   5.097   1.00 45.13  ?  153 HIS   A ND1   1 
ATOM   1102 C  CD2   . HIS   A 1 153 ? 22.779  6.955   5.503   1.00 42.64  ?  153 HIS   A CD2   1 
ATOM   1103 C  CE1   . HIS   A 1 153 ? 24.058  8.295   4.332   1.00 45.29  ?  153 HIS   A CE1   1 
ATOM   1104 N  NE2   . HIS   A 1 153 ? 22.807  7.948   4.558   1.00 44.40  ?  153 HIS   A NE2   1 
ATOM   1105 N  N     . LEU   A 1 154 ? 26.851  4.789   8.842   1.00 39.36  ?  154 LEU   A N     1 
ATOM   1106 C  CA    . LEU   A 1 154 ? 27.500  3.777   9.691   1.00 40.04  ?  154 LEU   A CA    1 
ATOM   1107 C  C     . LEU   A 1 154 ? 27.638  4.275   11.130  1.00 40.00  ?  154 LEU   A C     1 
ATOM   1108 O  O     . LEU   A 1 154 ? 27.401  3.537   12.057  1.00 39.56  ?  154 LEU   A O     1 
ATOM   1109 C  CB    . LEU   A 1 154 ? 28.875  3.371   9.129   1.00 40.51  ?  154 LEU   A CB    1 
ATOM   1110 C  CG    . LEU   A 1 154 ? 29.594  2.248   9.895   1.00 43.96  ?  154 LEU   A CG    1 
ATOM   1111 C  CD1   . LEU   A 1 154 ? 28.777  0.949   9.928   1.00 41.88  ?  154 LEU   A CD1   1 
ATOM   1112 C  CD2   . LEU   A 1 154 ? 30.968  1.962   9.317   1.00 42.69  ?  154 LEU   A CD2   1 
ATOM   1113 N  N     . GLU   A 1 155 ? 28.002  5.543   11.304  1.00 44.10  ?  155 GLU   A N     1 
ATOM   1114 C  CA    . GLU   A 1 155 ? 28.120  6.114   12.646  1.00 46.91  ?  155 GLU   A CA    1 
ATOM   1115 C  C     . GLU   A 1 155 ? 26.783  6.121   13.375  1.00 43.21  ?  155 GLU   A C     1 
ATOM   1116 O  O     . GLU   A 1 155 ? 26.736  5.803   14.569  1.00 47.25  ?  155 GLU   A O     1 
ATOM   1117 C  CB    . GLU   A 1 155 ? 28.740  7.527   12.615  1.00 50.93  ?  155 GLU   A CB    1 
ATOM   1118 C  CG    . GLU   A 1 155 ? 29.381  7.947   13.943  1.00 57.68  ?  155 GLU   A CG    1 
ATOM   1119 C  CD    . GLU   A 1 155 ? 30.533  7.039   14.387  1.00 61.31  ?  155 GLU   A CD    1 
ATOM   1120 O  OE1   . GLU   A 1 155 ? 31.309  6.567   13.516  1.00 61.65  ?  155 GLU   A OE1   1 
ATOM   1121 O  OE2   . GLU   A 1 155 ? 30.651  6.779   15.610  1.00 61.10  ?  155 GLU   A OE2   1 
ATOM   1122 N  N     . LEU   A 1 156 ? 25.699  6.448   12.665  1.00 39.26  ?  156 LEU   A N     1 
ATOM   1123 C  CA    . LEU   A 1 156 ? 24.348  6.333   13.240  1.00 39.95  ?  156 LEU   A CA    1 
ATOM   1124 C  C     . LEU   A 1 156 ? 24.045  4.884   13.681  1.00 38.79  ?  156 LEU   A C     1 
ATOM   1125 O  O     . LEU   A 1 156 ? 23.505  4.645   14.778  1.00 41.26  ?  156 LEU   A O     1 
ATOM   1126 C  CB    . LEU   A 1 156 ? 23.283  6.821   12.248  1.00 40.46  ?  156 LEU   A CB    1 
ATOM   1127 C  CG    . LEU   A 1 156 ? 21.853  6.903   12.779  1.00 39.71  ?  156 LEU   A CG    1 
ATOM   1128 C  CD1   . LEU   A 1 156 ? 21.796  7.792   14.003  1.00 42.31  ?  156 LEU   A CD1   1 
ATOM   1129 C  CD2   . LEU   A 1 156 ? 20.874  7.430   11.751  1.00 42.44  ?  156 LEU   A CD2   1 
ATOM   1130 N  N     . SER   A 1 157 ? 24.406  3.929   12.826  1.00 35.47  ?  157 SER   A N     1 
ATOM   1131 C  CA    . SER   A 1 157 ? 24.271  2.483   13.142  1.00 34.44  ?  157 SER   A CA    1 
ATOM   1132 C  C     . SER   A 1 157 ? 25.061  2.132   14.406  1.00 34.33  ?  157 SER   A C     1 
ATOM   1133 O  O     . SER   A 1 157 ? 24.591  1.395   15.264  1.00 32.18  ?  157 SER   A O     1 
ATOM   1134 C  CB    . SER   A 1 157 ? 24.744  1.636   11.960  1.00 33.43  ?  157 SER   A CB    1 
ATOM   1135 O  OG    . SER   A 1 157 ? 24.148  2.093   10.742  1.00 38.86  ?  157 SER   A OG    1 
ATOM   1136 N  N     . ARG   A 1 158 ? 26.266  2.690   14.529  1.00 33.36  ?  158 ARG   A N     1 
ATOM   1137 C  CA    . ARG   A 1 158 ? 27.096  2.453   15.701  1.00 33.81  ?  158 ARG   A CA    1 
ATOM   1138 C  C     . ARG   A 1 158 ? 26.484  3.054   16.959  1.00 32.53  ?  158 ARG   A C     1 
ATOM   1139 O  O     . ARG   A 1 158 ? 26.432  2.373   17.983  1.00 30.53  ?  158 ARG   A O     1 
ATOM   1140 C  CB    . ARG   A 1 158 ? 28.521  2.997   15.475  1.00 33.38  ?  158 ARG   A CB    1 
ATOM   1141 C  CG    . ARG   A 1 158 ? 29.255  2.294   14.347  1.00 38.43  ?  158 ARG   A CG    1 
ATOM   1142 C  CD    . ARG   A 1 158 ? 30.503  3.038   13.910  1.00 43.81  ?  158 ARG   A CD    1 
ATOM   1143 N  NE    . ARG   A 1 158 ? 31.221  3.592   15.058  1.00 47.61  ?  158 ARG   A NE    1 
ATOM   1144 C  CZ    . ARG   A 1 158 ? 31.930  2.885   15.927  1.00 43.77  ?  158 ARG   A CZ    1 
ATOM   1145 N  NH1   . ARG   A 1 158 ? 32.068  1.583   15.791  1.00 44.74  ?  158 ARG   A NH1   1 
ATOM   1146 N  NH2   . ARG   A 1 158 ? 32.522  3.495   16.937  1.00 46.73  ?  158 ARG   A NH2   1 
ATOM   1147 N  N     . ASP   A 1 159 ? 26.044  4.327   16.878  1.00 33.80  ?  159 ASP   A N     1 
ATOM   1148 C  CA    . ASP   A 1 159 ? 25.365  5.000   18.007  1.00 39.60  ?  159 ASP   A CA    1 
ATOM   1149 C  C     . ASP   A 1 159 ? 24.099  4.238   18.424  1.00 39.10  ?  159 ASP   A C     1 
ATOM   1150 O  O     . ASP   A 1 159 ? 23.845  4.053   19.624  1.00 38.06  ?  159 ASP   A O     1 
ATOM   1151 C  CB    . ASP   A 1 159 ? 24.989  6.480   17.688  1.00 40.37  ?  159 ASP   A CB    1 
ATOM   1152 C  CG    . ASP   A 1 159 ? 26.214  7.381   17.392  1.00 42.60  ?  159 ASP   A CG    1 
ATOM   1153 O  OD1   . ASP   A 1 159 ? 27.339  7.056   17.796  1.00 43.33  ?  159 ASP   A OD1   1 
ATOM   1154 O  OD2   . ASP   A 1 159 ? 26.052  8.425   16.732  1.00 45.62  ?  159 ASP   A OD2   1 
ATOM   1155 N  N     . ILE   A 1 160 ? 23.287  3.829   17.442  1.00 38.15  ?  160 ILE   A N     1 
ATOM   1156 C  CA    . ILE   A 1 160 ? 22.046  3.078   17.745  1.00 40.29  ?  160 ILE   A CA    1 
ATOM   1157 C  C     . ILE   A 1 160 ? 22.338  1.769   18.486  1.00 35.42  ?  160 ILE   A C     1 
ATOM   1158 O  O     . ILE   A 1 160 ? 21.667  1.442   19.463  1.00 39.06  ?  160 ILE   A O     1 
ATOM   1159 C  CB    . ILE   A 1 160 ? 21.188  2.818   16.473  1.00 39.78  ?  160 ILE   A CB    1 
ATOM   1160 C  CG1   . ILE   A 1 160 ? 20.483  4.095   16.036  1.00 43.26  ?  160 ILE   A CG1   1 
ATOM   1161 C  CG2   . ILE   A 1 160 ? 20.132  1.732   16.722  1.00 41.52  ?  160 ILE   A CG2   1 
ATOM   1162 C  CD1   . ILE   A 1 160 ? 20.073  4.102   14.583  1.00 42.13  ?  160 ILE   A CD1   1 
ATOM   1163 N  N     . ALA   A 1 161 ? 23.349  1.041   18.025  1.00 36.48  ?  161 ALA   A N     1 
ATOM   1164 C  CA    . ALA   A 1 161 ? 23.754  -0.236  18.663  1.00 38.66  ?  161 ALA   A CA    1 
ATOM   1165 C  C     . ALA   A 1 161 ? 24.184  -0.068  20.108  1.00 38.50  ?  161 ALA   A C     1 
ATOM   1166 O  O     . ALA   A 1 161 ? 23.793  -0.863  20.948  1.00 36.93  ?  161 ALA   A O     1 
ATOM   1167 C  CB    . ALA   A 1 161 ? 24.875  -0.896  17.874  1.00 39.99  ?  161 ALA   A CB    1 
ATOM   1168 N  N     . GLN   A 1 162 ? 24.979  0.976   20.367  1.00 39.28  ?  162 GLN   A N     1 
ATOM   1169 C  CA    . GLN   A 1 162 ? 25.507  1.289   21.702  1.00 40.25  ?  162 GLN   A CA    1 
ATOM   1170 C  C     . GLN   A 1 162 ? 24.425  1.736   22.676  1.00 39.62  ?  162 GLN   A C     1 
ATOM   1171 O  O     . GLN   A 1 162 ? 24.391  1.292   23.815  1.00 42.50  ?  162 GLN   A O     1 
ATOM   1172 C  CB    . GLN   A 1 162 ? 26.586  2.389   21.599  1.00 45.09  ?  162 GLN   A CB    1 
ATOM   1173 C  CG    . GLN   A 1 162 ? 27.854  1.950   20.883  1.00 46.25  ?  162 GLN   A CG    1 
ATOM   1174 C  CD    . GLN   A 1 162 ? 28.914  3.054   20.828  1.00 48.99  ?  162 GLN   A CD    1 
ATOM   1175 O  OE1   . GLN   A 1 162 ? 30.025  2.871   21.304  1.00 49.40  ?  162 GLN   A OE1   1 
ATOM   1176 N  NE2   . GLN   A 1 162 ? 28.571  4.190   20.236  1.00 49.05  ?  162 GLN   A NE2   1 
ATOM   1177 N  N     . ARG   A 1 163 ? 23.553  2.618   22.204  1.00 39.10  ?  163 ARG   A N     1 
ATOM   1178 C  CA    . ARG   A 1 163 ? 22.382  3.067   22.946  1.00 41.74  ?  163 ARG   A CA    1 
ATOM   1179 C  C     . ARG   A 1 163 ? 21.500  1.871   23.371  1.00 40.75  ?  163 ARG   A C     1 
ATOM   1180 O  O     . ARG   A 1 163 ? 21.177  1.717   24.564  1.00 39.76  ?  163 ARG   A O     1 
ATOM   1181 C  CB    . ARG   A 1 163 ? 21.597  4.062   22.086  1.00 42.14  ?  163 ARG   A CB    1 
ATOM   1182 C  CG    . ARG   A 1 163 ? 20.362  4.646   22.722  1.00 44.75  ?  163 ARG   A CG    1 
ATOM   1183 C  CD    . ARG   A 1 163 ? 19.709  5.589   21.736  1.00 47.58  ?  163 ARG   A CD    1 
ATOM   1184 N  NE    . ARG   A 1 163 ? 20.662  6.582   21.262  1.00 46.26  ?  163 ARG   A NE    1 
ATOM   1185 C  CZ    . ARG   A 1 163 ? 20.718  7.091   20.036  1.00 47.24  ?  163 ARG   A CZ    1 
ATOM   1186 N  NH1   . ARG   A 1 163 ? 19.873  6.721   19.083  1.00 45.27  ?  163 ARG   A NH1   1 
ATOM   1187 N  NH2   . ARG   A 1 163 ? 21.653  7.990   19.753  1.00 50.50  ?  163 ARG   A NH2   1 
ATOM   1188 N  N     . PHE   A 1 164 ? 21.140  1.030   22.400  1.00 36.29  ?  164 PHE   A N     1 
ATOM   1189 C  CA    . PHE   A 1 164 ? 20.336  -0.188  22.673  1.00 35.93  ?  164 PHE   A CA    1 
ATOM   1190 C  C     . PHE   A 1 164 ? 21.064  -1.102  23.634  1.00 32.82  ?  164 PHE   A C     1 
ATOM   1191 O  O     . PHE   A 1 164 ? 20.472  -1.576  24.599  1.00 39.04  ?  164 PHE   A O     1 
ATOM   1192 C  CB    . PHE   A 1 164 ? 19.974  -0.944  21.381  1.00 33.07  ?  164 PHE   A CB    1 
ATOM   1193 C  CG    . PHE   A 1 164 ? 18.895  -1.974  21.556  1.00 30.16  ?  164 PHE   A CG    1 
ATOM   1194 C  CD1   . PHE   A 1 164 ? 19.211  -3.285  21.858  1.00 30.26  ?  164 PHE   A CD1   1 
ATOM   1195 C  CD2   . PHE   A 1 164 ? 17.568  -1.638  21.393  1.00 30.26  ?  164 PHE   A CD2   1 
ATOM   1196 C  CE1   . PHE   A 1 164 ? 18.223  -4.236  22.030  1.00 32.85  ?  164 PHE   A CE1   1 
ATOM   1197 C  CE2   . PHE   A 1 164 ? 16.567  -2.574  21.554  1.00 29.50  ?  164 PHE   A CE2   1 
ATOM   1198 C  CZ    . PHE   A 1 164 ? 16.885  -3.882  21.876  1.00 31.70  ?  164 PHE   A CZ    1 
ATOM   1199 N  N     . ASN   A 1 165 ? 22.352  -1.330  23.384  1.00 34.88  ?  165 ASN   A N     1 
ATOM   1200 C  CA    . ASN   A 1 165 ? 23.161  -2.199  24.257  1.00 35.91  ?  165 ASN   A CA    1 
ATOM   1201 C  C     . ASN   A 1 165 ? 23.218  -1.690  25.736  1.00 36.10  ?  165 ASN   A C     1 
ATOM   1202 O  O     . ASN   A 1 165 ? 23.159  -2.486  26.678  1.00 33.66  ?  165 ASN   A O     1 
ATOM   1203 C  CB    . ASN   A 1 165 ? 24.583  -2.386  23.697  1.00 36.52  ?  165 ASN   A CB    1 
ATOM   1204 C  CG    . ASN   A 1 165 ? 24.650  -3.363  22.524  1.00 35.25  ?  165 ASN   A CG    1 
ATOM   1205 O  OD1   . ASN   A 1 165 ? 23.669  -4.033  22.172  1.00 30.01  ?  165 ASN   A OD1   1 
ATOM   1206 N  ND2   . ASN   A 1 165 ? 25.820  -3.451  21.913  1.00 32.99  ?  165 ASN   A ND2   1 
ATOM   1207 N  N     . ALA   A 1 166 ? 23.317  -0.370  25.914  1.00 34.66  ?  166 ALA   A N     1 
ATOM   1208 C  CA    . ALA   A 1 166 ? 23.503  0.226   27.254  1.00 37.21  ?  166 ALA   A CA    1 
ATOM   1209 C  C     . ALA   A 1 166 ? 22.236  0.065   28.076  1.00 36.45  ?  166 ALA   A C     1 
ATOM   1210 O  O     . ALA   A 1 166 ? 22.307  -0.049  29.267  1.00 36.74  ?  166 ALA   A O     1 
ATOM   1211 C  CB    . ALA   A 1 166 ? 23.896  1.705   27.144  1.00 36.15  ?  166 ALA   A CB    1 
ATOM   1212 N  N     . LEU   A 1 167 ? 21.079  0.041   27.406  1.00 40.76  ?  167 LEU   A N     1 
ATOM   1213 C  CA    . LEU   A 1 167 ? 19.780  -0.194  28.044  1.00 40.14  ?  167 LEU   A CA    1 
ATOM   1214 C  C     . LEU   A 1 167 ? 19.508  -1.676  28.301  1.00 38.20  ?  167 LEU   A C     1 
ATOM   1215 O  O     . LEU   A 1 167 ? 19.006  -2.033  29.362  1.00 39.55  ?  167 LEU   A O     1 
ATOM   1216 C  CB    . LEU   A 1 167 ? 18.667  0.399   27.178  1.00 41.12  ?  167 LEU   A CB    1 
ATOM   1217 C  CG    . LEU   A 1 167 ? 18.768  1.924   27.017  1.00 44.31  ?  167 LEU   A CG    1 
ATOM   1218 C  CD1   . LEU   A 1 167 ? 17.986  2.413   25.809  1.00 46.71  ?  167 LEU   A CD1   1 
ATOM   1219 C  CD2   . LEU   A 1 167 ? 18.297  2.614   28.294  1.00 45.69  ?  167 LEU   A CD2   1 
ATOM   1220 N  N     . TYR   A 1 168 ? 19.870  -2.534  27.352  1.00 35.75  ?  168 TYR   A N     1 
ATOM   1221 C  CA    . TYR   A 1 168 ? 19.410  -3.954  27.374  1.00 37.61  ?  168 TYR   A CA    1 
ATOM   1222 C  C     . TYR   A 1 168 ? 20.505  -5.015  27.536  1.00 37.28  ?  168 TYR   A C     1 
ATOM   1223 O  O     . TYR   A 1 168 ? 20.193  -6.213  27.667  1.00 38.34  ?  168 TYR   A O     1 
ATOM   1224 C  CB    . TYR   A 1 168 ? 18.568  -4.228  26.122  1.00 35.85  ?  168 TYR   A CB    1 
ATOM   1225 C  CG    . TYR   A 1 168 ? 17.347  -3.315  26.023  1.00 35.23  ?  168 TYR   A CG    1 
ATOM   1226 C  CD1   . TYR   A 1 168 ? 17.245  -2.360  25.018  1.00 35.17  ?  168 TYR   A CD1   1 
ATOM   1227 C  CD2   . TYR   A 1 168 ? 16.307  -3.394  26.958  1.00 37.26  ?  168 TYR   A CD2   1 
ATOM   1228 C  CE1   . TYR   A 1 168 ? 16.145  -1.513  24.930  1.00 36.64  ?  168 TYR   A CE1   1 
ATOM   1229 C  CE2   . TYR   A 1 168 ? 15.202  -2.552  26.880  1.00 36.96  ?  168 TYR   A CE2   1 
ATOM   1230 C  CZ    . TYR   A 1 168 ? 15.120  -1.616  25.865  1.00 35.96  ?  168 TYR   A CZ    1 
ATOM   1231 O  OH    . TYR   A 1 168 ? 14.028  -0.786  25.786  1.00 34.77  ?  168 TYR   A OH    1 
ATOM   1232 N  N     . GLY   A 1 169 ? 21.769  -4.581  27.556  1.00 36.98  ?  169 GLY   A N     1 
ATOM   1233 C  CA    . GLY   A 1 169 ? 22.921  -5.496  27.536  1.00 38.36  ?  169 GLY   A CA    1 
ATOM   1234 C  C     . GLY   A 1 169 ? 23.461  -5.655  26.110  1.00 38.70  ?  169 GLY   A C     1 
ATOM   1235 O  O     . GLY   A 1 169 ? 23.044  -4.941  25.205  1.00 39.96  ?  169 GLY   A O     1 
ATOM   1236 N  N     . GLU   A 1 170 ? 24.387  -6.591  25.921  1.00 39.87  ?  170 GLU   A N     1 
ATOM   1237 C  CA    . GLU   A 1 170 ? 25.141  -6.702  24.667  1.00 40.75  ?  170 GLU   A CA    1 
ATOM   1238 C  C     . GLU   A 1 170 ? 24.394  -7.570  23.637  1.00 36.63  ?  170 GLU   A C     1 
ATOM   1239 O  O     . GLU   A 1 170 ? 24.777  -8.702  23.344  1.00 39.70  ?  170 GLU   A O     1 
ATOM   1240 C  CB    . GLU   A 1 170 ? 26.577  -7.205  24.940  1.00 45.33  ?  170 GLU   A CB    1 
ATOM   1241 C  CG    . GLU   A 1 170 ? 27.358  -6.370  25.978  1.00 48.28  ?  170 GLU   A CG    1 
ATOM   1242 C  CD    . GLU   A 1 170 ? 27.247  -4.844  25.749  1.00 52.32  ?  170 GLU   A CD    1 
ATOM   1243 O  OE1   . GLU   A 1 170 ? 27.715  -4.329  24.695  1.00 51.68  ?  170 GLU   A OE1   1 
ATOM   1244 O  OE2   . GLU   A 1 170 ? 26.664  -4.151  26.628  1.00 53.64  ?  170 GLU   A OE2   1 
ATOM   1245 N  N     . ILE   A 1 171 ? 23.337  -6.992  23.084  1.00 30.67  ?  171 ILE   A N     1 
ATOM   1246 C  CA    . ILE   A 1 171 ? 22.466  -7.630  22.106  1.00 29.75  ?  171 ILE   A CA    1 
ATOM   1247 C  C     . ILE   A 1 171 ? 23.093  -7.519  20.697  1.00 29.57  ?  171 ILE   A C     1 
ATOM   1248 O  O     . ILE   A 1 171 ? 23.080  -8.495  19.938  1.00 29.03  ?  171 ILE   A O     1 
ATOM   1249 C  CB    . ILE   A 1 171 ? 21.064  -6.949  22.083  1.00 30.49  ?  171 ILE   A CB    1 
ATOM   1250 C  CG1   . ILE   A 1 171 ? 20.405  -6.949  23.488  1.00 34.43  ?  171 ILE   A CG1   1 
ATOM   1251 C  CG2   . ILE   A 1 171 ? 20.161  -7.565  21.035  1.00 28.07  ?  171 ILE   A CG2   1 
ATOM   1252 C  CD1   . ILE   A 1 171 ? 20.055  -8.302  24.031  1.00 35.26  ?  171 ILE   A CD1   1 
ATOM   1253 N  N     . PHE   A 1 172 ? 23.613  -6.334  20.355  1.00 25.76  ?  172 PHE   A N     1 
ATOM   1254 C  CA    . PHE   A 1 172 ? 24.260  -6.066  19.071  1.00 27.04  ?  172 PHE   A CA    1 
ATOM   1255 C  C     . PHE   A 1 172 ? 25.808  -6.073  19.175  1.00 30.91  ?  172 PHE   A C     1 
ATOM   1256 O  O     . PHE   A 1 172 ? 26.381  -5.763  20.228  1.00 34.35  ?  172 PHE   A O     1 
ATOM   1257 C  CB    . PHE   A 1 172 ? 23.844  -4.678  18.565  1.00 28.74  ?  172 PHE   A CB    1 
ATOM   1258 C  CG    . PHE   A 1 172 ? 22.356  -4.524  18.298  1.00 30.55  ?  172 PHE   A CG    1 
ATOM   1259 C  CD1   . PHE   A 1 172 ? 21.647  -3.467  18.848  1.00 27.49  ?  172 PHE   A CD1   1 
ATOM   1260 C  CD2   . PHE   A 1 172 ? 21.680  -5.424  17.466  1.00 26.15  ?  172 PHE   A CD2   1 
ATOM   1261 C  CE1   . PHE   A 1 172 ? 20.282  -3.335  18.595  1.00 30.55  ?  172 PHE   A CE1   1 
ATOM   1262 C  CE2   . PHE   A 1 172 ? 20.330  -5.290  17.205  1.00 26.52  ?  172 PHE   A CE2   1 
ATOM   1263 C  CZ    . PHE   A 1 172 ? 19.632  -4.240  17.753  1.00 28.02  ?  172 PHE   A CZ    1 
ATOM   1264 N  N     . LYS   A 1 173 ? 26.483  -6.412  18.085  1.00 30.25  ?  173 LYS   A N     1 
ATOM   1265 C  CA    . LYS   A 1 173 ? 27.879  -6.029  17.878  1.00 30.19  ?  173 LYS   A CA    1 
ATOM   1266 C  C     . LYS   A 1 173 ? 27.871  -4.597  17.387  1.00 31.73  ?  173 LYS   A C     1 
ATOM   1267 O  O     . LYS   A 1 173 ? 26.980  -4.230  16.617  1.00 30.58  ?  173 LYS   A O     1 
ATOM   1268 C  CB    . LYS   A 1 173 ? 28.563  -6.888  16.804  1.00 33.28  ?  173 LYS   A CB    1 
ATOM   1269 C  CG    . LYS   A 1 173 ? 28.676  -8.367  17.127  1.00 36.50  ?  173 LYS   A CG    1 
ATOM   1270 C  CD    . LYS   A 1 173 ? 29.606  -8.649  18.309  1.00 41.91  ?  173 LYS   A CD    1 
ATOM   1271 C  CE    . LYS   A 1 173 ? 29.751  -10.159 18.542  1.00 44.89  ?  173 LYS   A CE    1 
ATOM   1272 N  NZ    . LYS   A 1 173 ? 30.546  -10.436 19.767  1.00 48.99  ?  173 LYS   A NZ    1 
ATOM   1273 N  N     . VAL   A 1 174 ? 28.835  -3.794  17.846  1.00 28.50  ?  174 VAL   A N     1 
ATOM   1274 C  CA    . VAL   A 1 174 ? 29.059  -2.437  17.338  1.00 30.25  ?  174 VAL   A CA    1 
ATOM   1275 C  C     . VAL   A 1 174 ? 29.867  -2.577  16.050  1.00 29.35  ?  174 VAL   A C     1 
ATOM   1276 O  O     . VAL   A 1 174 ? 31.016  -2.959  16.103  1.00 31.14  ?  174 VAL   A O     1 
ATOM   1277 C  CB    . VAL   A 1 174 ? 29.792  -1.542  18.377  1.00 32.07  ?  174 VAL   A CB    1 
ATOM   1278 C  CG1   . VAL   A 1 174 ? 30.008  -0.126  17.856  1.00 32.94  ?  174 VAL   A CG1   1 
ATOM   1279 C  CG2   . VAL   A 1 174 ? 29.003  -1.480  19.674  1.00 35.13  ?  174 VAL   A CG2   1 
ATOM   1280 N  N     . PRO   A 1 175 ? 29.273  -2.279  14.883  1.00 30.40  ?  175 PRO   A N     1 
ATOM   1281 C  CA    . PRO   A 1 175 ? 29.995  -2.447  13.599  1.00 31.51  ?  175 PRO   A CA    1 
ATOM   1282 C  C     . PRO   A 1 175 ? 31.179  -1.468  13.437  1.00 33.95  ?  175 PRO   A C     1 
ATOM   1283 O  O     . PRO   A 1 175 ? 31.148  -0.346  13.984  1.00 35.22  ?  175 PRO   A O     1 
ATOM   1284 C  CB    . PRO   A 1 175 ? 28.909  -2.163  12.553  1.00 30.83  ?  175 PRO   A CB    1 
ATOM   1285 C  CG    . PRO   A 1 175 ? 28.028  -1.188  13.226  1.00 31.51  ?  175 PRO   A CG    1 
ATOM   1286 C  CD    . PRO   A 1 175 ? 27.976  -1.621  14.675  1.00 32.24  ?  175 PRO   A CD    1 
ATOM   1287 N  N     . GLU   A 1 176 ? 32.209  -1.898  12.713  1.00 33.23  ?  176 GLU   A N     1 
ATOM   1288 C  CA    . GLU   A 1 176 ? 33.361  -1.042  12.384  1.00 36.09  ?  176 GLU   A CA    1 
ATOM   1289 C  C     . GLU   A 1 176 ? 33.445  -0.871  10.862  1.00 34.09  ?  176 GLU   A C     1 
ATOM   1290 O  O     . GLU   A 1 176 ? 33.070  -1.759  10.141  1.00 32.45  ?  176 GLU   A O     1 
ATOM   1291 C  CB    . GLU   A 1 176 ? 34.675  -1.635  12.923  1.00 38.25  ?  176 GLU   A CB    1 
ATOM   1292 C  CG    . GLU   A 1 176 ? 34.797  -1.625  14.447  1.00 41.08  ?  176 GLU   A CG    1 
ATOM   1293 C  CD    . GLU   A 1 176 ? 34.831  -0.229  15.046  1.00 42.17  ?  176 GLU   A CD    1 
ATOM   1294 O  OE1   . GLU   A 1 176 ? 35.343  0.701   14.402  1.00 44.85  ?  176 GLU   A OE1   1 
ATOM   1295 O  OE2   . GLU   A 1 176 ? 34.347  -0.070  16.182  1.00 45.63  ?  176 GLU   A OE2   1 
ATOM   1296 N  N     . PRO   A 1 177 ? 33.901  0.301   10.383  1.00 36.18  ?  177 PRO   A N     1 
ATOM   1297 C  CA    . PRO   A 1 177 ? 34.190  0.472   8.969   1.00 36.59  ?  177 PRO   A CA    1 
ATOM   1298 C  C     . PRO   A 1 177 ? 35.378  -0.391  8.547   1.00 37.64  ?  177 PRO   A C     1 
ATOM   1299 O  O     . PRO   A 1 177 ? 36.218  -0.715  9.388   1.00 36.49  ?  177 PRO   A O     1 
ATOM   1300 C  CB    . PRO   A 1 177 ? 34.540  1.945   8.871   1.00 38.25  ?  177 PRO   A CB    1 
ATOM   1301 C  CG    . PRO   A 1 177 ? 35.114  2.270   10.204  1.00 38.44  ?  177 PRO   A CG    1 
ATOM   1302 C  CD    . PRO   A 1 177 ? 34.267  1.506   11.159  1.00 37.09  ?  177 PRO   A CD    1 
ATOM   1303 N  N     . PHE   A 1 178 ? 35.414  -0.797  7.283   1.00 38.27  ?  178 PHE   A N     1 
ATOM   1304 C  CA    . PHE   A 1 178 ? 36.555  -1.518  6.712   1.00 42.67  ?  178 PHE   A CA    1 
ATOM   1305 C  C     . PHE   A 1 178 ? 37.514  -0.478  6.130   1.00 44.20  ?  178 PHE   A C     1 
ATOM   1306 O  O     . PHE   A 1 178 ? 37.292  0.042   5.043   1.00 47.96  ?  178 PHE   A O     1 
ATOM   1307 C  CB    . PHE   A 1 178 ? 36.107  -2.530  5.651   1.00 41.82  ?  178 PHE   A CB    1 
ATOM   1308 C  CG    . PHE   A 1 178 ? 37.178  -3.500  5.244   1.00 42.51  ?  178 PHE   A CG    1 
ATOM   1309 C  CD1   . PHE   A 1 178 ? 37.974  -3.251  4.139   1.00 44.03  ?  178 PHE   A CD1   1 
ATOM   1310 C  CD2   . PHE   A 1 178 ? 37.378  -4.678  5.961   1.00 43.18  ?  178 PHE   A CD2   1 
ATOM   1311 C  CE1   . PHE   A 1 178 ? 38.966  -4.144  3.764   1.00 47.07  ?  178 PHE   A CE1   1 
ATOM   1312 C  CE2   . PHE   A 1 178 ? 38.370  -5.583  5.595   1.00 45.83  ?  178 PHE   A CE2   1 
ATOM   1313 C  CZ    . PHE   A 1 178 ? 39.167  -5.312  4.491   1.00 46.83  ?  178 PHE   A CZ    1 
ATOM   1314 N  N     . ILE   A 1 179 ? 38.581  -0.183  6.874   1.00 46.33  ?  179 ILE   A N     1 
ATOM   1315 C  CA    . ILE   A 1 179 ? 39.478  0.944   6.576   1.00 47.26  ?  179 ILE   A CA    1 
ATOM   1316 C  C     . ILE   A 1 179 ? 40.254  0.755   5.263   1.00 46.31  ?  179 ILE   A C     1 
ATOM   1317 O  O     . ILE   A 1 179 ? 40.233  1.660   4.433   1.00 47.20  ?  179 ILE   A O     1 
ATOM   1318 C  CB    . ILE   A 1 179 ? 40.441  1.247   7.758   1.00 49.70  ?  179 ILE   A CB    1 
ATOM   1319 C  CG1   . ILE   A 1 179 ? 39.674  1.476   9.076   1.00 50.64  ?  179 ILE   A CG1   1 
ATOM   1320 C  CG2   . ILE   A 1 179 ? 41.328  2.447   7.454   1.00 49.77  ?  179 ILE   A CG2   1 
ATOM   1321 C  CD1   . ILE   A 1 179 ? 38.561  2.499   9.006   1.00 51.76  ?  179 ILE   A CD1   1 
ATOM   1322 N  N     . PRO   A 1 180 ? 40.924  -0.404  5.064   1.00 43.83  ?  180 PRO   A N     1 
ATOM   1323 C  CA    . PRO   A 1 180 ? 41.792  -0.574  3.879   1.00 46.82  ?  180 PRO   A CA    1 
ATOM   1324 C  C     . PRO   A 1 180 ? 41.064  -0.440  2.526   1.00 50.30  ?  180 PRO   A C     1 
ATOM   1325 O  O     . PRO   A 1 180 ? 40.056  -1.110  2.306   1.00 52.21  ?  180 PRO   A O     1 
ATOM   1326 C  CB    . PRO   A 1 180 ? 42.344  -2.001  4.050   1.00 47.65  ?  180 PRO   A CB    1 
ATOM   1327 C  CG    . PRO   A 1 180 ? 42.260  -2.247  5.524   1.00 47.53  ?  180 PRO   A CG    1 
ATOM   1328 C  CD    . PRO   A 1 180 ? 40.980  -1.588  5.937   1.00 43.71  ?  180 PRO   A CD    1 
ATOM   1329 N  N     . LYS   A 1 181 ? 41.593  0.414   1.647   1.00 56.23  ?  181 LYS   A N     1 
ATOM   1330 C  CA    . LYS   A 1 181 ? 41.018  0.682   0.306   1.00 61.57  ?  181 LYS   A CA    1 
ATOM   1331 C  C     . LYS   A 1 181 ? 41.540  -0.251  -0.797  1.00 63.21  ?  181 LYS   A C     1 
ATOM   1332 O  O     . LYS   A 1 181 ? 42.611  -0.870  -0.672  1.00 73.45  ?  181 LYS   A O     1 
ATOM   1333 C  CB    . LYS   A 1 181 ? 41.298  2.129   -0.107  1.00 59.92  ?  181 LYS   A CB    1 
ATOM   1334 N  N     . GLY   A 1 183 ? 42.186  -1.199  -4.100  1.00 76.75  ?  183 GLY   A N     1 
ATOM   1335 C  CA    . GLY   A 1 183 ? 43.494  -0.563  -4.349  1.00 78.68  ?  183 GLY   A CA    1 
ATOM   1336 C  C     . GLY   A 1 183 ? 43.724  0.176   -5.669  1.00 78.06  ?  183 GLY   A C     1 
ATOM   1337 O  O     . GLY   A 1 183 ? 44.721  0.896   -5.804  1.00 78.26  ?  183 GLY   A O     1 
ATOM   1338 N  N     . ALA   A 1 184 ? 42.805  0.021   -6.626  1.00 75.04  ?  184 ALA   A N     1 
ATOM   1339 C  CA    . ALA   A 1 184 ? 42.947  0.570   -7.969  1.00 71.77  ?  184 ALA   A CA    1 
ATOM   1340 C  C     . ALA   A 1 184 ? 42.191  1.889   -8.107  1.00 71.14  ?  184 ALA   A C     1 
ATOM   1341 O  O     . ALA   A 1 184 ? 41.039  1.993   -7.687  1.00 71.18  ?  184 ALA   A O     1 
ATOM   1342 C  CB    . ALA   A 1 184 ? 42.420  -0.427  -8.981  1.00 70.64  ?  184 ALA   A CB    1 
ATOM   1343 N  N     . ARG   A 1 185 ? 42.840  2.877   -8.722  1.00 68.70  ?  185 ARG   A N     1 
ATOM   1344 C  CA    . ARG   A 1 185 ? 42.255  4.199   -8.954  1.00 67.44  ?  185 ARG   A CA    1 
ATOM   1345 C  C     . ARG   A 1 185 ? 41.709  4.281   -10.376 1.00 61.79  ?  185 ARG   A C     1 
ATOM   1346 O  O     . ARG   A 1 185 ? 42.481  4.393   -11.335 1.00 65.57  ?  185 ARG   A O     1 
ATOM   1347 C  CB    . ARG   A 1 185 ? 43.309  5.292   -8.739  1.00 66.51  ?  185 ARG   A CB    1 
ATOM   1348 N  N     . VAL   A 1 186 ? 40.388  4.208   -10.513 1.00 56.36  ?  186 VAL   A N     1 
ATOM   1349 C  CA    . VAL   A 1 186 ? 39.754  4.302   -11.825 1.00 52.63  ?  186 VAL   A CA    1 
ATOM   1350 C  C     . VAL   A 1 186 ? 38.991  5.616   -11.842 1.00 51.91  ?  186 VAL   A C     1 
ATOM   1351 O  O     . VAL   A 1 186 ? 38.037  5.797   -11.091 1.00 50.58  ?  186 VAL   A O     1 
ATOM   1352 C  CB    . VAL   A 1 186 ? 38.871  3.085   -12.141 1.00 47.87  ?  186 VAL   A CB    1 
ATOM   1353 C  CG1   . VAL   A 1 186 ? 38.235  3.222   -13.529 1.00 49.24  ?  186 VAL   A CG1   1 
ATOM   1354 C  CG2   . VAL   A 1 186 ? 39.707  1.825   -12.081 1.00 45.42  ?  186 VAL   A CG2   1 
ATOM   1355 N  N     . MET   A 1 187 ? 39.442  6.523   -12.704 1.00 52.30  ?  187 MET   A N     1 
ATOM   1356 C  CA    . MET   A 1 187 ? 38.913  7.880   -12.795 1.00 53.80  ?  187 MET   A CA    1 
ATOM   1357 C  C     . MET   A 1 187 ? 38.085  8.047   -14.053 1.00 54.66  ?  187 MET   A C     1 
ATOM   1358 O  O     . MET   A 1 187 ? 38.123  7.198   -14.947 1.00 55.23  ?  187 MET   A O     1 
ATOM   1359 C  CB    . MET   A 1 187 ? 40.044  8.912   -12.786 1.00 53.27  ?  187 MET   A CB    1 
ATOM   1360 C  CG    . MET   A 1 187 ? 41.070  8.697   -11.676 1.00 56.07  ?  187 MET   A CG    1 
ATOM   1361 S  SD    . MET   A 1 187 ? 40.389  8.923   -10.018 1.00 56.00  ?  187 MET   A SD    1 
ATOM   1362 C  CE    . MET   A 1 187 ? 39.960  10.656  -10.091 1.00 57.00  ?  187 MET   A CE    1 
ATOM   1363 N  N     . SER   A 1 188 ? 37.349  9.157   -14.104 1.00 57.36  ?  188 SER   A N     1 
ATOM   1364 C  CA    . SER   A 1 188 ? 36.435  9.454   -15.197 1.00 56.94  ?  188 SER   A CA    1 
ATOM   1365 C  C     . SER   A 1 188 ? 37.201  9.760   -16.484 1.00 54.33  ?  188 SER   A C     1 
ATOM   1366 O  O     . SER   A 1 188 ? 38.193  10.488  -16.464 1.00 54.45  ?  188 SER   A O     1 
ATOM   1367 C  CB    . SER   A 1 188 ? 35.527  10.626  -14.806 1.00 60.67  ?  188 SER   A CB    1 
ATOM   1368 O  OG    . SER   A 1 188 ? 34.771  10.315  -13.640 1.00 59.83  ?  188 SER   A OG    1 
ATOM   1369 N  N     . LEU   A 1 189 ? 36.714  9.222   -17.597 1.00 52.89  ?  189 LEU   A N     1 
ATOM   1370 C  CA    . LEU   A 1 189 ? 37.406  9.316   -18.880 1.00 51.09  ?  189 LEU   A CA    1 
ATOM   1371 C  C     . LEU   A 1 189 ? 37.485  10.736  -19.424 1.00 53.40  ?  189 LEU   A C     1 
ATOM   1372 O  O     . LEU   A 1 189 ? 38.476  11.097  -20.044 1.00 58.97  ?  189 LEU   A O     1 
ATOM   1373 C  CB    . LEU   A 1 189 ? 36.751  8.387   -19.900 1.00 49.95  ?  189 LEU   A CB    1 
ATOM   1374 C  CG    . LEU   A 1 189 ? 36.696  6.898   -19.521 1.00 47.26  ?  189 LEU   A CG    1 
ATOM   1375 C  CD1   . LEU   A 1 189 ? 36.043  6.122   -20.636 1.00 47.12  ?  189 LEU   A CD1   1 
ATOM   1376 C  CD2   . LEU   A 1 189 ? 38.069  6.327   -19.235 1.00 49.20  ?  189 LEU   A CD2   1 
ATOM   1377 N  N     . LEU   A 1 190 ? 36.454  11.538  -19.186 1.00 58.79  ?  190 LEU   A N     1 
ATOM   1378 C  CA    . LEU   A 1 190 ? 36.412  12.936  -19.665 1.00 56.72  ?  190 LEU   A CA    1 
ATOM   1379 C  C     . LEU   A 1 190 ? 36.604  13.987  -18.558 1.00 55.69  ?  190 LEU   A C     1 
ATOM   1380 O  O     . LEU   A 1 190 ? 36.564  15.175  -18.825 1.00 61.68  ?  190 LEU   A O     1 
ATOM   1381 C  CB    . LEU   A 1 190 ? 35.101  13.176  -20.410 1.00 59.96  ?  190 LEU   A CB    1 
ATOM   1382 C  CG    . LEU   A 1 190 ? 34.747  12.135  -21.477 1.00 61.62  ?  190 LEU   A CG    1 
ATOM   1383 C  CD1   . LEU   A 1 190 ? 33.460  12.527  -22.189 1.00 63.58  ?  190 LEU   A CD1   1 
ATOM   1384 C  CD2   . LEU   A 1 190 ? 35.865  11.952  -22.493 1.00 59.80  ?  190 LEU   A CD2   1 
ATOM   1385 N  N     . GLU   A 1 191 ? 36.835  13.528  -17.332 1.00 56.41  ?  191 GLU   A N     1 
ATOM   1386 C  CA    . GLU   A 1 191 ? 37.078  14.371  -16.166 1.00 51.84  ?  191 GLU   A CA    1 
ATOM   1387 C  C     . GLU   A 1 191 ? 37.996  13.552  -15.238 1.00 57.27  ?  191 GLU   A C     1 
ATOM   1388 O  O     . GLU   A 1 191 ? 37.561  13.037  -14.195 1.00 56.98  ?  191 GLU   A O     1 
ATOM   1389 C  CB    . GLU   A 1 191 ? 35.753  14.691  -15.489 1.00 48.29  ?  191 GLU   A CB    1 
ATOM   1390 C  CG    . GLU   A 1 191 ? 35.716  16.002  -14.716 1.00 47.95  ?  191 GLU   A CG    1 
ATOM   1391 C  CD    . GLU   A 1 191 ? 34.336  16.258  -14.169 1.00 48.71  ?  191 GLU   A CD    1 
ATOM   1392 O  OE1   . GLU   A 1 191 ? 33.400  16.489  -15.003 1.00 48.07  ?  191 GLU   A OE1   1 
ATOM   1393 O  OE2   . GLU   A 1 191 ? 34.152  16.179  -12.913 1.00 49.44  ?  191 GLU   A OE2   1 
ATOM   1394 N  N     . PRO   A 1 192 ? 39.285  13.433  -15.610 1.00 59.91  ?  192 PRO   A N     1 
ATOM   1395 C  CA    . PRO   A 1 192 ? 40.237  12.556  -14.921 1.00 61.26  ?  192 PRO   A CA    1 
ATOM   1396 C  C     . PRO   A 1 192 ? 40.509  12.882  -13.441 1.00 62.49  ?  192 PRO   A C     1 
ATOM   1397 O  O     . PRO   A 1 192 ? 41.214  12.120  -12.786 1.00 63.23  ?  192 PRO   A O     1 
ATOM   1398 C  CB    . PRO   A 1 192 ? 41.506  12.690  -15.773 1.00 59.87  ?  192 PRO   A CB    1 
ATOM   1399 C  CG    . PRO   A 1 192 ? 41.394  14.026  -16.423 1.00 60.90  ?  192 PRO   A CG    1 
ATOM   1400 C  CD    . PRO   A 1 192 ? 39.929  14.176  -16.707 1.00 59.61  ?  192 PRO   A CD    1 
ATOM   1401 N  N     . THR   A 1 193 ? 39.953  13.984  -12.931 1.00 65.40  ?  193 THR   A N     1 
ATOM   1402 C  CA    . THR   A 1 193 ? 40.038  14.349  -11.510 1.00 68.16  ?  193 THR   A CA    1 
ATOM   1403 C  C     . THR   A 1 193 ? 38.916  13.709  -10.653 1.00 68.67  ?  193 THR   A C     1 
ATOM   1404 O  O     . THR   A 1 193 ? 39.089  13.532  -9.445  1.00 72.70  ?  193 THR   A O     1 
ATOM   1405 C  CB    . THR   A 1 193 ? 39.996  15.884  -11.349 1.00 70.48  ?  193 THR   A CB    1 
ATOM   1406 O  OG1   . THR   A 1 193 ? 38.793  16.386  -11.946 1.00 77.37  ?  193 THR   A OG1   1 
ATOM   1407 C  CG2   . THR   A 1 193 ? 41.194  16.540  -12.029 1.00 68.37  ?  193 THR   A CG2   1 
ATOM   1408 N  N     . LYS   A 1 194 ? 37.784  13.370  -11.280 1.00 69.64  ?  194 LYS   A N     1 
ATOM   1409 C  CA    . LYS   A 1 194 ? 36.620  12.765  -10.605 1.00 67.02  ?  194 LYS   A CA    1 
ATOM   1410 C  C     . LYS   A 1 194 ? 36.652  11.247  -10.784 1.00 67.86  ?  194 LYS   A C     1 
ATOM   1411 O  O     . LYS   A 1 194 ? 36.888  10.761  -11.895 1.00 69.71  ?  194 LYS   A O     1 
ATOM   1412 C  CB    . LYS   A 1 194 ? 35.314  13.335  -11.186 1.00 67.28  ?  194 LYS   A CB    1 
ATOM   1413 C  CG    . LYS   A 1 194 ? 34.019  12.686  -10.691 1.00 68.01  ?  194 LYS   A CG    1 
ATOM   1414 C  CD    . LYS   A 1 194 ? 32.799  13.323  -11.346 1.00 68.39  ?  194 LYS   A CD    1 
ATOM   1415 N  N     . LYS   A 1 195 ? 36.407  10.508  -9.698  1.00 62.91  ?  195 LYS   A N     1 
ATOM   1416 C  CA    . LYS   A 1 195 ? 36.415  9.036   -9.719  1.00 61.37  ?  195 LYS   A CA    1 
ATOM   1417 C  C     . LYS   A 1 195 ? 35.237  8.504   -10.547 1.00 61.79  ?  195 LYS   A C     1 
ATOM   1418 O  O     . LYS   A 1 195 ? 34.147  9.065   -10.502 1.00 61.26  ?  195 LYS   A O     1 
ATOM   1419 C  CB    . LYS   A 1 195 ? 36.359  8.482   -8.296  1.00 57.38  ?  195 LYS   A CB    1 
ATOM   1420 N  N     . MET   A 1 196 ? 35.469  7.441   -11.316 1.00 63.92  ?  196 MET   A N     1 
ATOM   1421 C  CA    . MET   A 1 196 ? 34.432  6.844   -12.166 1.00 65.53  ?  196 MET   A CA    1 
ATOM   1422 C  C     . MET   A 1 196 ? 33.360  6.242   -11.263 1.00 67.28  ?  196 MET   A C     1 
ATOM   1423 O  O     . MET   A 1 196 ? 33.669  5.379   -10.456 1.00 66.99  ?  196 MET   A O     1 
ATOM   1424 C  CB    . MET   A 1 196 ? 35.040  5.772   -13.087 1.00 62.17  ?  196 MET   A CB    1 
ATOM   1425 C  CG    . MET   A 1 196 ? 34.045  4.953   -13.907 1.00 60.02  ?  196 MET   A CG    1 
ATOM   1426 S  SD    . MET   A 1 196 ? 34.808  3.595   -14.832 1.00 58.78  ?  196 MET   A SD    1 
ATOM   1427 C  CE    . MET   A 1 196 ? 35.817  4.498   -16.008 1.00 60.06  ?  196 MET   A CE    1 
ATOM   1428 N  N     . SER   A 1 197 ? 32.119  6.716   -11.405 1.00 70.60  ?  197 SER   A N     1 
ATOM   1429 C  CA    . SER   A 1 197 ? 30.990  6.292   -10.568 1.00 74.80  ?  197 SER   A CA    1 
ATOM   1430 C  C     . SER   A 1 197 ? 29.756  6.015   -11.418 1.00 76.83  ?  197 SER   A C     1 
ATOM   1431 O  O     . SER   A 1 197 ? 29.426  6.813   -12.298 1.00 78.89  ?  197 SER   A O     1 
ATOM   1432 C  CB    . SER   A 1 197 ? 30.658  7.372   -9.531  1.00 78.15  ?  197 SER   A CB    1 
ATOM   1433 N  N     . LYS   A 1 198 ? 29.072  4.899   -11.135 1.00 79.62  ?  198 LYS   A N     1 
ATOM   1434 C  CA    . LYS   A 1 198 ? 27.818  4.507   -11.823 1.00 82.08  ?  198 LYS   A CA    1 
ATOM   1435 C  C     . LYS   A 1 198 ? 26.771  5.622   -11.835 1.00 83.78  ?  198 LYS   A C     1 
ATOM   1436 O  O     . LYS   A 1 198 ? 26.043  5.790   -12.810 1.00 83.11  ?  198 LYS   A O     1 
ATOM   1437 C  CB    . LYS   A 1 198 ? 27.221  3.257   -11.163 1.00 77.33  ?  198 LYS   A CB    1 
ATOM   1438 N  N     . SER   A 1 199 ? 26.749  6.404   -10.755 1.00 93.44  ?  199 SER   A N     1 
ATOM   1439 C  CA    . SER   A 1 199 ? 25.856  7.555   -10.587 1.00 97.98  ?  199 SER   A CA    1 
ATOM   1440 C  C     . SER   A 1 199 ? 26.038  8.699   -11.610 1.00 101.99 ?  199 SER   A C     1 
ATOM   1441 O  O     . SER   A 1 199 ? 25.220  9.619   -11.642 1.00 109.59 ?  199 SER   A O     1 
ATOM   1442 C  CB    . SER   A 1 199 ? 26.026  8.107   -9.166  1.00 98.66  ?  199 SER   A CB    1 
ATOM   1443 O  OG    . SER   A 1 199 ? 27.399  8.323   -8.869  1.00 101.75 ?  199 SER   A OG    1 
ATOM   1444 N  N     . ASP   A 1 200 ? 27.093  8.645   -12.430 1.00 97.81  ?  200 ASP   A N     1 
ATOM   1445 C  CA    . ASP   A 1 200 ? 27.367  9.669   -13.451 1.00 94.19  ?  200 ASP   A CA    1 
ATOM   1446 C  C     . ASP   A 1 200 ? 26.327  9.621   -14.577 1.00 86.99  ?  200 ASP   A C     1 
ATOM   1447 O  O     . ASP   A 1 200 ? 26.035  8.553   -15.127 1.00 79.10  ?  200 ASP   A O     1 
ATOM   1448 C  CB    . ASP   A 1 200 ? 28.791  9.489   -14.020 1.00 90.85  ?  200 ASP   A CB    1 
ATOM   1449 C  CG    . ASP   A 1 200 ? 29.311  10.739  -14.718 1.00 88.89  ?  200 ASP   A CG    1 
ATOM   1450 O  OD1   . ASP   A 1 200 ? 28.631  11.258  -15.630 1.00 89.56  ?  200 ASP   A OD1   1 
ATOM   1451 O  OD2   . ASP   A 1 200 ? 30.411  11.206  -14.354 1.00 86.89  ?  200 ASP   A OD2   1 
ATOM   1452 N  N     . ASN   A 1 202 ? 26.875  11.588  -17.610 1.00 84.37  ?  202 ASN   A N     1 
ATOM   1453 C  CA    . ASN   A 1 202 ? 27.685  11.376  -18.803 1.00 82.18  ?  202 ASN   A CA    1 
ATOM   1454 C  C     . ASN   A 1 202 ? 28.262  9.969   -18.752 1.00 84.42  ?  202 ASN   A C     1 
ATOM   1455 O  O     . ASN   A 1 202 ? 29.280  9.731   -18.095 1.00 86.14  ?  202 ASN   A O     1 
ATOM   1456 C  CB    . ASN   A 1 202 ? 28.807  12.430  -18.891 1.00 83.04  ?  202 ASN   A CB    1 
ATOM   1457 C  CG    . ASN   A 1 202 ? 29.262  12.705  -20.318 1.00 87.94  ?  202 ASN   A CG    1 
ATOM   1458 O  OD1   . ASN   A 1 202 ? 28.809  12.073  -21.276 1.00 84.36  ?  202 ASN   A OD1   1 
ATOM   1459 N  ND2   . ASN   A 1 202 ? 30.165  13.673  -20.463 1.00 93.81  ?  202 ASN   A ND2   1 
ATOM   1460 N  N     . ARG   A 1 203 ? 27.598  9.034   -19.435 1.00 80.27  ?  203 ARG   A N     1 
ATOM   1461 C  CA    . ARG   A 1 203 ? 28.077  7.651   -19.526 1.00 79.23  ?  203 ARG   A CA    1 
ATOM   1462 C  C     . ARG   A 1 203 ? 29.383  7.551   -20.323 1.00 74.27  ?  203 ARG   A C     1 
ATOM   1463 O  O     . ARG   A 1 203 ? 30.050  6.522   -20.281 1.00 66.95  ?  203 ARG   A O     1 
ATOM   1464 C  CB    . ARG   A 1 203 ? 27.012  6.726   -20.137 1.00 80.93  ?  203 ARG   A CB    1 
ATOM   1465 C  CG    . ARG   A 1 203 ? 25.636  6.785   -19.469 1.00 85.11  ?  203 ARG   A CG    1 
ATOM   1466 C  CD    . ARG   A 1 203 ? 25.697  6.698   -17.938 1.00 85.06  ?  203 ARG   A CD    1 
ATOM   1467 N  NE    . ARG   A 1 203 ? 26.474  5.544   -17.464 1.00 81.93  ?  203 ARG   A NE    1 
ATOM   1468 C  CZ    . ARG   A 1 203 ? 25.994  4.326   -17.185 1.00 80.84  ?  203 ARG   A CZ    1 
ATOM   1469 N  NH1   . ARG   A 1 203 ? 24.701  4.044   -17.308 1.00 85.89  ?  203 ARG   A NH1   1 
ATOM   1470 N  NH2   . ARG   A 1 203 ? 26.817  3.362   -16.769 1.00 75.37  ?  203 ARG   A NH2   1 
ATOM   1471 N  N     . ASN   A 1 204 ? 29.734  8.621   -21.045 1.00 70.77  ?  204 ASN   A N     1 
ATOM   1472 C  CA    . ASN   A 1 204 ? 31.047  8.755   -21.682 1.00 71.38  ?  204 ASN   A CA    1 
ATOM   1473 C  C     . ASN   A 1 204 ? 32.226  8.890   -20.703 1.00 69.29  ?  204 ASN   A C     1 
ATOM   1474 O  O     . ASN   A 1 204 ? 33.371  8.723   -21.117 1.00 75.05  ?  204 ASN   A O     1 
ATOM   1475 C  CB    . ASN   A 1 204 ? 31.041  9.923   -22.679 1.00 69.99  ?  204 ASN   A CB    1 
ATOM   1476 C  CG    . ASN   A 1 204 ? 30.149  9.663   -23.878 1.00 69.17  ?  204 ASN   A CG    1 
ATOM   1477 O  OD1   . ASN   A 1 204 ? 29.777  8.525   -24.154 1.00 69.13  ?  204 ASN   A OD1   1 
ATOM   1478 N  ND2   . ASN   A 1 204 ? 29.814  10.718  -24.607 1.00 70.05  ?  204 ASN   A ND2   1 
ATOM   1479 N  N     . ASN   A 1 205 ? 31.945  9.175   -19.426 1.00 65.87  ?  205 ASN   A N     1 
ATOM   1480 C  CA    . ASN   A 1 205 ? 32.964  9.163   -18.358 1.00 63.75  ?  205 ASN   A CA    1 
ATOM   1481 C  C     . ASN   A 1 205 ? 33.255  7.772   -17.771 1.00 58.32  ?  205 ASN   A C     1 
ATOM   1482 O  O     . ASN   A 1 205 ? 34.275  7.579   -17.114 1.00 58.64  ?  205 ASN   A O     1 
ATOM   1483 C  CB    . ASN   A 1 205 ? 32.555  10.106  -17.218 1.00 66.12  ?  205 ASN   A CB    1 
ATOM   1484 C  CG    . ASN   A 1 205 ? 32.980  11.540  -17.463 1.00 71.25  ?  205 ASN   A CG    1 
ATOM   1485 O  OD1   . ASN   A 1 205 ? 34.141  11.800  -17.764 1.00 72.06  ?  205 ASN   A OD1   1 
ATOM   1486 N  ND2   . ASN   A 1 205 ? 32.056  12.484  -17.289 1.00 78.13  ?  205 ASN   A ND2   1 
ATOM   1487 N  N     . VAL   A 1 206 ? 32.377  6.803   -18.021 1.00 55.54  ?  206 VAL   A N     1 
ATOM   1488 C  CA    . VAL   A 1 206 ? 32.464  5.484   -17.385 1.00 52.64  ?  206 VAL   A CA    1 
ATOM   1489 C  C     . VAL   A 1 206 ? 32.495  4.377   -18.416 1.00 48.33  ?  206 VAL   A C     1 
ATOM   1490 O  O     . VAL   A 1 206 ? 32.158  4.600   -19.563 1.00 51.99  ?  206 VAL   A O     1 
ATOM   1491 C  CB    . VAL   A 1 206 ? 31.285  5.242   -16.408 1.00 57.28  ?  206 VAL   A CB    1 
ATOM   1492 C  CG1   . VAL   A 1 206 ? 31.060  6.454   -15.493 1.00 61.53  ?  206 VAL   A CG1   1 
ATOM   1493 C  CG2   . VAL   A 1 206 ? 29.996  4.934   -17.153 1.00 58.48  ?  206 VAL   A CG2   1 
ATOM   1494 N  N     . ILE   A 1 207 ? 32.910  3.185   -17.987 1.00 51.91  ?  207 ILE   A N     1 
ATOM   1495 C  CA    . ILE   A 1 207 ? 32.798  1.940   -18.774 1.00 49.16  ?  207 ILE   A CA    1 
ATOM   1496 C  C     . ILE   A 1 207 ? 32.067  0.915   -17.904 1.00 47.32  ?  207 ILE   A C     1 
ATOM   1497 O  O     . ILE   A 1 207 ? 32.562  0.544   -16.833 1.00 44.98  ?  207 ILE   A O     1 
ATOM   1498 C  CB    . ILE   A 1 207 ? 34.181  1.417   -19.243 1.00 47.77  ?  207 ILE   A CB    1 
ATOM   1499 C  CG1   . ILE   A 1 207 ? 34.606  2.188   -20.497 1.00 53.44  ?  207 ILE   A CG1   1 
ATOM   1500 C  CG2   . ILE   A 1 207 ? 34.160  -0.087  -19.530 1.00 43.21  ?  207 ILE   A CG2   1 
ATOM   1501 C  CD1   . ILE   A 1 207 ? 36.003  1.874   -20.999 1.00 57.00  ?  207 ILE   A CD1   1 
ATOM   1502 N  N     . GLY   A 1 208 ? 30.888  0.483   -18.366 1.00 47.09  ?  208 GLY   A N     1 
ATOM   1503 C  CA    . GLY   A 1 208 ? 30.073  -0.525  -17.671 1.00 42.62  ?  208 GLY   A CA    1 
ATOM   1504 C  C     . GLY   A 1 208 ? 30.604  -1.904  -17.951 1.00 40.34  ?  208 GLY   A C     1 
ATOM   1505 O  O     . GLY   A 1 208 ? 31.176  -2.121  -19.005 1.00 41.14  ?  208 GLY   A O     1 
ATOM   1506 N  N     . LEU   A 1 209 ? 30.390  -2.837  -17.022 1.00 39.26  ?  209 LEU   A N     1 
ATOM   1507 C  CA    . LEU   A 1 209 ? 30.920  -4.202  -17.130 1.00 39.69  ?  209 LEU   A CA    1 
ATOM   1508 C  C     . LEU   A 1 209 ? 30.328  -5.007  -18.291 1.00 43.38  ?  209 LEU   A C     1 
ATOM   1509 O  O     . LEU   A 1 209 ? 30.891  -6.042  -18.670 1.00 44.81  ?  209 LEU   A O     1 
ATOM   1510 C  CB    . LEU   A 1 209 ? 30.692  -4.964  -15.816 1.00 40.84  ?  209 LEU   A CB    1 
ATOM   1511 C  CG    . LEU   A 1 209 ? 31.392  -4.421  -14.561 1.00 40.79  ?  209 LEU   A CG    1 
ATOM   1512 C  CD1   . LEU   A 1 209 ? 31.238  -5.409  -13.422 1.00 40.85  ?  209 LEU   A CD1   1 
ATOM   1513 C  CD2   . LEU   A 1 209 ? 32.877  -4.139  -14.817 1.00 41.58  ?  209 LEU   A CD2   1 
ATOM   1514 N  N     . LEU   A 1 210 ? 29.189  -4.547  -18.815 1.00 46.55  ?  210 LEU   A N     1 
ATOM   1515 C  CA    . LEU   A 1 210 ? 28.472  -5.188  -19.908 1.00 53.99  ?  210 LEU   A CA    1 
ATOM   1516 C  C     . LEU   A 1 210 ? 28.658  -4.489  -21.267 1.00 54.60  ?  210 LEU   A C     1 
ATOM   1517 O  O     . LEU   A 1 210 ? 28.019  -4.879  -22.251 1.00 56.36  ?  210 LEU   A O     1 
ATOM   1518 C  CB    . LEU   A 1 210 ? 26.988  -5.275  -19.547 1.00 54.44  ?  210 LEU   A CB    1 
ATOM   1519 C  CG    . LEU   A 1 210 ? 26.638  -6.114  -18.303 1.00 54.41  ?  210 LEU   A CG    1 
ATOM   1520 C  CD1   . LEU   A 1 210 ? 25.128  -6.082  -18.067 1.00 52.79  ?  210 LEU   A CD1   1 
ATOM   1521 C  CD2   . LEU   A 1 210 ? 27.127  -7.558  -18.411 1.00 51.40  ?  210 LEU   A CD2   1 
ATOM   1522 N  N     . GLU   A 1 211 ? 29.546  -3.490  -21.319 1.00 54.83  ?  211 GLU   A N     1 
ATOM   1523 C  CA    . GLU   A 1 211 ? 29.833  -2.749  -22.553 1.00 53.98  ?  211 GLU   A CA    1 
ATOM   1524 C  C     . GLU   A 1 211 ? 30.583  -3.611  -23.557 1.00 51.59  ?  211 GLU   A C     1 
ATOM   1525 O  O     . GLU   A 1 211 ? 31.420  -4.424  -23.171 1.00 54.47  ?  211 GLU   A O     1 
ATOM   1526 C  CB    . GLU   A 1 211 ? 30.614  -1.452  -22.273 1.00 52.34  ?  211 GLU   A CB    1 
ATOM   1527 C  CG    . GLU   A 1 211 ? 29.715  -0.318  -21.837 1.00 57.36  ?  211 GLU   A CG    1 
ATOM   1528 C  CD    . GLU   A 1 211 ? 30.334  1.061   -21.986 1.00 60.54  ?  211 GLU   A CD    1 
ATOM   1529 O  OE1   . GLU   A 1 211 ? 30.891  1.391   -23.058 1.00 60.49  ?  211 GLU   A OE1   1 
ATOM   1530 O  OE2   . GLU   A 1 211 ? 30.220  1.842   -21.023 1.00 61.45  ?  211 GLU   A OE2   1 
ATOM   1531 N  N     . ASP   A 1 212 ? 30.274  -3.425  -24.842 1.00 52.03  ?  212 ASP   A N     1 
ATOM   1532 C  CA    . ASP   A 1 212 ? 30.871  -4.241  -25.911 1.00 55.81  ?  212 ASP   A CA    1 
ATOM   1533 C  C     . ASP   A 1 212 ? 32.263  -3.705  -26.279 1.00 52.04  ?  212 ASP   A C     1 
ATOM   1534 O  O     . ASP   A 1 212 ? 32.566  -2.539  -26.012 1.00 50.78  ?  212 ASP   A O     1 
ATOM   1535 C  CB    . ASP   A 1 212 ? 29.932  -4.352  -27.157 1.00 59.56  ?  212 ASP   A CB    1 
ATOM   1536 C  CG    . ASP   A 1 212 ? 29.647  -3.017  -27.841 1.00 64.28  ?  212 ASP   A CG    1 
ATOM   1537 O  OD1   . ASP   A 1 212 ? 30.345  -2.030  -27.574 1.00 75.78  ?  212 ASP   A OD1   1 
ATOM   1538 O  OD2   . ASP   A 1 212 ? 28.710  -2.960  -28.663 1.00 67.62  ?  212 ASP   A OD2   1 
ATOM   1539 N  N     . PRO   A 1 213 ? 33.108  -4.541  -26.911 1.00 56.29  ?  213 PRO   A N     1 
ATOM   1540 C  CA    . PRO   A 1 213 ? 34.419  -4.071  -27.395 1.00 57.45  ?  213 PRO   A CA    1 
ATOM   1541 C  C     . PRO   A 1 213 ? 34.400  -2.762  -28.203 1.00 57.26  ?  213 PRO   A C     1 
ATOM   1542 O  O     . PRO   A 1 213 ? 35.297  -1.934  -28.019 1.00 61.29  ?  213 PRO   A O     1 
ATOM   1543 C  CB    . PRO   A 1 213 ? 34.908  -5.243  -28.248 1.00 55.17  ?  213 PRO   A CB    1 
ATOM   1544 C  CG    . PRO   A 1 213 ? 34.307  -6.434  -27.583 1.00 54.10  ?  213 PRO   A CG    1 
ATOM   1545 C  CD    . PRO   A 1 213 ? 32.939  -5.987  -27.148 1.00 53.65  ?  213 PRO   A CD    1 
ATOM   1546 N  N     . LYS   A 1 214 ? 33.374  -2.571  -29.043 1.00 51.35  ?  214 LYS   A N     1 
ATOM   1547 C  CA    . LYS   A 1 214 ? 33.251  -1.382  -29.893 1.00 49.38  ?  214 LYS   A CA    1 
ATOM   1548 C  C     . LYS   A 1 214 ? 32.944  -0.120  -29.107 1.00 50.24  ?  214 LYS   A C     1 
ATOM   1549 O  O     . LYS   A 1 214 ? 33.470  0.946   -29.414 1.00 50.96  ?  214 LYS   A O     1 
ATOM   1550 C  CB    . LYS   A 1 214 ? 32.167  -1.581  -30.956 1.00 49.94  ?  214 LYS   A CB    1 
ATOM   1551 N  N     . SER   A 1 215 ? 32.081  -0.238  -28.100 1.00 53.00  ?  215 SER   A N     1 
ATOM   1552 C  CA    . SER   A 1 215 ? 31.751  0.883   -27.203 1.00 53.21  ?  215 SER   A CA    1 
ATOM   1553 C  C     . SER   A 1 215 ? 32.969  1.278   -26.363 1.00 49.19  ?  215 SER   A C     1 
ATOM   1554 O  O     . SER   A 1 215 ? 33.258  2.464   -26.206 1.00 46.99  ?  215 SER   A O     1 
ATOM   1555 C  CB    . SER   A 1 215 ? 30.565  0.555   -26.290 1.00 52.37  ?  215 SER   A CB    1 
ATOM   1556 O  OG    . SER   A 1 215 ? 30.194  1.687   -25.540 1.00 51.42  ?  215 SER   A OG    1 
ATOM   1557 N  N     . VAL   A 1 216 ? 33.679  0.276   -25.850 1.00 47.80  ?  216 VAL   A N     1 
ATOM   1558 C  CA    . VAL   A 1 216 ? 34.894  0.496   -25.048 1.00 49.80  ?  216 VAL   A CA    1 
ATOM   1559 C  C     . VAL   A 1 216 ? 35.906  1.352   -25.845 1.00 52.82  ?  216 VAL   A C     1 
ATOM   1560 O  O     . VAL   A 1 216 ? 36.395  2.390   -25.341 1.00 51.40  ?  216 VAL   A O     1 
ATOM   1561 C  CB    . VAL   A 1 216 ? 35.510  -0.855  -24.584 1.00 51.28  ?  216 VAL   A CB    1 
ATOM   1562 C  CG1   . VAL   A 1 216 ? 36.912  -0.675  -23.987 1.00 51.66  ?  216 VAL   A CG1   1 
ATOM   1563 C  CG2   . VAL   A 1 216 ? 34.605  -1.538  -23.566 1.00 49.83  ?  216 VAL   A CG2   1 
ATOM   1564 N  N     . VAL   A 1 217 ? 36.160  0.959   -27.099 1.00 49.33  ?  217 VAL   A N     1 
ATOM   1565 C  CA    . VAL   A 1 217 ? 37.069  1.699   -27.981 1.00 49.75  ?  217 VAL   A CA    1 
ATOM   1566 C  C     . VAL   A 1 217 ? 36.643  3.166   -28.138 1.00 49.78  ?  217 VAL   A C     1 
ATOM   1567 O  O     . VAL   A 1 217 ? 37.488  4.056   -28.043 1.00 48.87  ?  217 VAL   A O     1 
ATOM   1568 C  CB    . VAL   A 1 217 ? 37.238  1.002   -29.373 1.00 51.53  ?  217 VAL   A CB    1 
ATOM   1569 C  CG1   . VAL   A 1 217 ? 37.925  1.914   -30.395 1.00 49.75  ?  217 VAL   A CG1   1 
ATOM   1570 C  CG2   . VAL   A 1 217 ? 38.046  -0.287  -29.224 1.00 52.92  ?  217 VAL   A CG2   1 
ATOM   1571 N  N     . LYS   A 1 218 ? 35.356  3.403   -28.396 1.00 49.32  ?  218 LYS   A N     1 
ATOM   1572 C  CA    . LYS   A 1 218 ? 34.831  4.766   -28.609 1.00 50.75  ?  218 LYS   A CA    1 
ATOM   1573 C  C     . LYS   A 1 218 ? 35.000  5.661   -27.369 1.00 47.68  ?  218 LYS   A C     1 
ATOM   1574 O  O     . LYS   A 1 218 ? 35.355  6.836   -27.476 1.00 53.11  ?  218 LYS   A O     1 
ATOM   1575 C  CB    . LYS   A 1 218 ? 33.352  4.712   -29.065 1.00 52.38  ?  218 LYS   A CB    1 
ATOM   1576 C  CG    . LYS   A 1 218 ? 32.631  6.058   -29.085 1.00 55.43  ?  218 LYS   A CG    1 
ATOM   1577 C  CD    . LYS   A 1 218 ? 31.587  6.129   -30.196 1.00 57.16  ?  218 LYS   A CD    1 
ATOM   1578 N  N     . LYS   A 1 219 ? 34.753  5.093   -26.195 1.00 46.38  ?  219 LYS   A N     1 
ATOM   1579 C  CA    . LYS   A 1 219 ? 34.908  5.818   -24.924 1.00 46.01  ?  219 LYS   A CA    1 
ATOM   1580 C  C     . LYS   A 1 219 ? 36.375  6.116   -24.577 1.00 45.27  ?  219 LYS   A C     1 
ATOM   1581 O  O     . LYS   A 1 219 ? 36.691  7.251   -24.163 1.00 43.45  ?  219 LYS   A O     1 
ATOM   1582 C  CB    . LYS   A 1 219 ? 34.236  5.056   -23.797 1.00 50.41  ?  219 LYS   A CB    1 
ATOM   1583 C  CG    . LYS   A 1 219 ? 32.736  4.872   -24.018 1.00 53.48  ?  219 LYS   A CG    1 
ATOM   1584 C  CD    . LYS   A 1 219 ? 31.982  4.619   -22.736 1.00 55.27  ?  219 LYS   A CD    1 
ATOM   1585 C  CE    . LYS   A 1 219 ? 30.476  4.651   -22.962 1.00 53.39  ?  219 LYS   A CE    1 
ATOM   1586 N  NZ    . LYS   A 1 219 ? 29.797  4.450   -21.651 1.00 52.57  ?  219 LYS   A NZ    1 
ATOM   1587 N  N     . ILE   A 1 220 ? 37.251  5.126   -24.778 1.00 42.93  ?  220 ILE   A N     1 
ATOM   1588 C  CA    . ILE   A 1 220 ? 38.709  5.292   -24.543 1.00 45.99  ?  220 ILE   A CA    1 
ATOM   1589 C  C     . ILE   A 1 220 ? 39.327  6.273   -25.556 1.00 43.18  ?  220 ILE   A C     1 
ATOM   1590 O  O     . ILE   A 1 220 ? 40.165  7.103   -25.192 1.00 40.30  ?  220 ILE   A O     1 
ATOM   1591 C  CB    . ILE   A 1 220 ? 39.487  3.938   -24.570 1.00 44.47  ?  220 ILE   A CB    1 
ATOM   1592 C  CG1   . ILE   A 1 220 ? 38.915  2.916   -23.580 1.00 44.72  ?  220 ILE   A CG1   1 
ATOM   1593 C  CG2   . ILE   A 1 220 ? 40.967  4.145   -24.251 1.00 43.32  ?  220 ILE   A CG2   1 
ATOM   1594 C  CD1   . ILE   A 1 220 ? 39.015  3.292   -22.111 1.00 45.54  ?  220 ILE   A CD1   1 
ATOM   1595 N  N     . LYS   A 1 221 ? 38.887  6.203   -26.816 1.00 45.28  ?  221 LYS   A N     1 
ATOM   1596 C  CA    . LYS   A 1 221 ? 39.341  7.125   -27.875 1.00 42.27  ?  221 LYS   A CA    1 
ATOM   1597 C  C     . LYS   A 1 221 ? 39.031  8.591   -27.554 1.00 46.26  ?  221 LYS   A C     1 
ATOM   1598 O  O     . LYS   A 1 221 ? 39.816  9.486   -27.885 1.00 51.92  ?  221 LYS   A O     1 
ATOM   1599 C  CB    . LYS   A 1 221 ? 38.732  6.753   -29.230 1.00 42.52  ?  221 LYS   A CB    1 
ATOM   1600 N  N     . ARG   A 1 222 ? 37.910  8.825   -26.880 1.00 48.39  ?  222 ARG   A N     1 
ATOM   1601 C  CA    . ARG   A 1 222 ? 37.498  10.174  -26.446 1.00 52.81  ?  222 ARG   A CA    1 
ATOM   1602 C  C     . ARG   A 1 222 ? 38.170  10.644  -25.146 1.00 50.99  ?  222 ARG   A C     1 
ATOM   1603 O  O     . ARG   A 1 222 ? 38.140  11.844  -24.836 1.00 50.37  ?  222 ARG   A O     1 
ATOM   1604 C  CB    . ARG   A 1 222 ? 35.968  10.226  -26.260 1.00 54.04  ?  222 ARG   A CB    1 
ATOM   1605 N  N     . ALA   A 1 223 ? 38.764  9.708   -24.395 1.00 48.99  ?  223 ALA   A N     1 
ATOM   1606 C  CA    . ALA   A 1 223 ? 39.357  9.994   -23.080 1.00 47.50  ?  223 ALA   A CA    1 
ATOM   1607 C  C     . ALA   A 1 223 ? 40.361  11.115  -23.167 1.00 45.23  ?  223 ALA   A C     1 
ATOM   1608 O  O     . ALA   A 1 223 ? 41.204  11.120  -24.055 1.00 46.68  ?  223 ALA   A O     1 
ATOM   1609 C  CB    . ALA   A 1 223 ? 40.005  8.748   -22.495 1.00 48.47  ?  223 ALA   A CB    1 
ATOM   1610 N  N     . VAL   A 1 224 ? 40.255  12.069  -22.257 1.00 48.72  ?  224 VAL   A N     1 
ATOM   1611 C  CA    . VAL   A 1 224 ? 41.085  13.277  -22.314 1.00 52.35  ?  224 VAL   A CA    1 
ATOM   1612 C  C     . VAL   A 1 224 ? 42.550  12.917  -22.082 1.00 49.50  ?  224 VAL   A C     1 
ATOM   1613 O  O     . VAL   A 1 224 ? 42.841  12.038  -21.285 1.00 50.39  ?  224 VAL   A O     1 
ATOM   1614 C  CB    . VAL   A 1 224 ? 40.626  14.362  -21.311 1.00 53.91  ?  224 VAL   A CB    1 
ATOM   1615 C  CG1   . VAL   A 1 224 ? 39.251  14.888  -21.694 1.00 55.08  ?  224 VAL   A CG1   1 
ATOM   1616 C  CG2   . VAL   A 1 224 ? 40.622  13.851  -19.880 1.00 56.82  ?  224 VAL   A CG2   1 
ATOM   1617 N  N     . THR   A 1 225 ? 43.449  13.572  -22.808 1.00 49.55  ?  225 THR   A N     1 
ATOM   1618 C  CA    . THR   A 1 225 ? 44.890  13.362  -22.626 1.00 50.45  ?  225 THR   A CA    1 
ATOM   1619 C  C     . THR   A 1 225 ? 45.522  14.710  -22.255 1.00 48.48  ?  225 THR   A C     1 
ATOM   1620 O  O     . THR   A 1 225 ? 45.010  15.373  -21.367 1.00 52.38  ?  225 THR   A O     1 
ATOM   1621 C  CB    . THR   A 1 225 ? 45.510  12.652  -23.849 1.00 48.50  ?  225 THR   A CB    1 
ATOM   1622 O  OG1   . THR   A 1 225 ? 45.206  13.380  -25.037 1.00 50.05  ?  225 THR   A OG1   1 
ATOM   1623 C  CG2   . THR   A 1 225 ? 44.975  11.241  -23.958 1.00 46.33  ?  225 THR   A CG2   1 
ATOM   1624 N  N     . ASP   A 1 226 ? 46.632  15.097  -22.876 1.00 50.40  ?  226 ASP   A N     1 
ATOM   1625 C  CA    . ASP   A 1 226 ? 47.246  16.421  -22.662 1.00 47.07  ?  226 ASP   A CA    1 
ATOM   1626 C  C     . ASP   A 1 226 ? 47.789  16.931  -23.982 1.00 45.20  ?  226 ASP   A C     1 
ATOM   1627 O  O     . ASP   A 1 226 ? 47.749  16.214  -24.977 1.00 45.03  ?  226 ASP   A O     1 
ATOM   1628 C  CB    . ASP   A 1 226 ? 48.353  16.362  -21.597 1.00 46.67  ?  226 ASP   A CB    1 
ATOM   1629 C  CG    . ASP   A 1 226 ? 49.419  15.317  -21.902 1.00 48.11  ?  226 ASP   A CG    1 
ATOM   1630 O  OD1   . ASP   A 1 226 ? 50.083  15.429  -22.949 1.00 43.74  ?  226 ASP   A OD1   1 
ATOM   1631 O  OD2   . ASP   A 1 226 ? 49.586  14.376  -21.079 1.00 51.39  ?  226 ASP   A OD2   1 
ATOM   1632 N  N     . SER   A 1 227 ? 48.304  18.161  -23.961 1.00 44.85  ?  227 SER   A N     1 
ATOM   1633 C  CA    . SER   A 1 227 ? 48.904  18.829  -25.115 1.00 44.27  ?  227 SER   A CA    1 
ATOM   1634 C  C     . SER   A 1 227 ? 50.440  18.820  -25.082 1.00 43.59  ?  227 SER   A C     1 
ATOM   1635 O  O     . SER   A 1 227 ? 51.071  19.676  -25.693 1.00 44.39  ?  227 SER   A O     1 
ATOM   1636 C  CB    . SER   A 1 227 ? 48.420  20.287  -25.147 1.00 46.28  ?  227 SER   A CB    1 
ATOM   1637 O  OG    . SER   A 1 227 ? 48.729  20.948  -23.932 1.00 48.85  ?  227 SER   A OG    1 
ATOM   1638 N  N     . ASP   A 1 228 ? 51.047  17.876  -24.364 1.00 43.56  ?  228 ASP   A N     1 
ATOM   1639 C  CA    . ASP   A 1 228 ? 52.511  17.760  -24.320 1.00 41.01  ?  228 ASP   A CA    1 
ATOM   1640 C  C     . ASP   A 1 228 ? 53.026  17.518  -25.735 1.00 39.85  ?  228 ASP   A C     1 
ATOM   1641 O  O     . ASP   A 1 228 ? 52.440  16.730  -26.480 1.00 35.66  ?  228 ASP   A O     1 
ATOM   1642 C  CB    . ASP   A 1 228 ? 52.969  16.614  -23.398 1.00 43.02  ?  228 ASP   A CB    1 
ATOM   1643 C  CG    . ASP   A 1 228 ? 52.715  16.904  -21.904 1.00 44.97  ?  228 ASP   A CG    1 
ATOM   1644 O  OD1   . ASP   A 1 228 ? 52.216  18.006  -21.571 1.00 44.21  ?  228 ASP   A OD1   1 
ATOM   1645 O  OD2   . ASP   A 1 228 ? 53.036  16.023  -21.075 1.00 40.45  ?  228 ASP   A OD2   1 
ATOM   1646 N  N     . GLU   A 1 229 ? 54.103  18.220  -26.085 1.00 40.59  ?  229 GLU   A N     1 
ATOM   1647 C  CA    . GLU   A 1 229 ? 54.778  18.088  -27.378 1.00 41.65  ?  229 GLU   A CA    1 
ATOM   1648 C  C     . GLU   A 1 229 ? 56.279  17.859  -27.128 1.00 40.01  ?  229 GLU   A C     1 
ATOM   1649 O  O     . GLU   A 1 229 ? 56.916  18.707  -26.513 1.00 39.75  ?  229 GLU   A O     1 
ATOM   1650 C  CB    . GLU   A 1 229 ? 54.563  19.349  -28.227 1.00 44.68  ?  229 GLU   A CB    1 
ATOM   1651 C  CG    . GLU   A 1 229 ? 55.323  19.381  -29.553 1.00 46.87  ?  229 GLU   A CG    1 
ATOM   1652 C  CD    . GLU   A 1 229 ? 55.107  18.139  -30.422 1.00 47.51  ?  229 GLU   A CD    1 
ATOM   1653 O  OE1   . GLU   A 1 229 ? 53.979  17.576  -30.443 1.00 45.57  ?  229 GLU   A OE1   1 
ATOM   1654 O  OE2   . GLU   A 1 229 ? 56.074  17.727  -31.092 1.00 46.15  ?  229 GLU   A OE2   1 
ATOM   1655 N  N     . PRO   A 1 230 ? 56.832  16.698  -27.552 1.00 38.41  ?  230 PRO   A N     1 
ATOM   1656 C  CA    . PRO   A 1 230 ? 56.084  15.563  -28.125 1.00 40.18  ?  230 PRO   A CA    1 
ATOM   1657 C  C     . PRO   A 1 230 ? 55.163  14.909  -27.088 1.00 43.75  ?  230 PRO   A C     1 
ATOM   1658 O  O     . PRO   A 1 230 ? 55.356  15.090  -25.875 1.00 39.73  ?  230 PRO   A O     1 
ATOM   1659 C  CB    . PRO   A 1 230 ? 57.183  14.591  -28.575 1.00 39.25  ?  230 PRO   A CB    1 
ATOM   1660 C  CG    . PRO   A 1 230 ? 58.432  15.412  -28.636 1.00 41.16  ?  230 PRO   A CG    1 
ATOM   1661 C  CD    . PRO   A 1 230 ? 58.281  16.429  -27.546 1.00 39.14  ?  230 PRO   A CD    1 
ATOM   1662 N  N     . PRO   A 1 231 ? 54.141  14.180  -27.545 1.00 45.99  ?  231 PRO   A N     1 
ATOM   1663 C  CA    . PRO   A 1 231 ? 53.361  13.386  -26.595 1.00 48.12  ?  231 PRO   A CA    1 
ATOM   1664 C  C     . PRO   A 1 231 ? 54.265  12.398  -25.858 1.00 46.70  ?  231 PRO   A C     1 
ATOM   1665 O  O     . PRO   A 1 231 ? 55.114  11.786  -26.491 1.00 46.13  ?  231 PRO   A O     1 
ATOM   1666 C  CB    . PRO   A 1 231 ? 52.352  12.659  -27.491 1.00 48.81  ?  231 PRO   A CB    1 
ATOM   1667 C  CG    . PRO   A 1 231 ? 52.210  13.558  -28.671 1.00 47.69  ?  231 PRO   A CG    1 
ATOM   1668 C  CD    . PRO   A 1 231 ? 53.571  14.136  -28.900 1.00 46.31  ?  231 PRO   A CD    1 
ATOM   1669 N  N     . VAL   A 1 232 ? 54.103  12.298  -24.535 1.00 42.58  ?  232 VAL   A N     1 
ATOM   1670 C  CA    . VAL   A 1 232 ? 54.950  11.463  -23.675 1.00 44.80  ?  232 VAL   A CA    1 
ATOM   1671 C  C     . VAL   A 1 232 ? 54.053  10.676  -22.705 1.00 42.67  ?  232 VAL   A C     1 
ATOM   1672 O  O     . VAL   A 1 232 ? 53.260  11.272  -21.984 1.00 41.76  ?  232 VAL   A O     1 
ATOM   1673 C  CB    . VAL   A 1 232 ? 55.965  12.313  -22.868 1.00 45.69  ?  232 VAL   A CB    1 
ATOM   1674 N  N     . VAL   A 1 233 ? 54.168  9.345   -22.720 1.00 39.29  ?  233 VAL   A N     1 
ATOM   1675 C  CA    . VAL   A 1 233 ? 53.374  8.450   -21.859 1.00 41.28  ?  233 VAL   A CA    1 
ATOM   1676 C  C     . VAL   A 1 233 ? 54.147  8.192   -20.548 1.00 43.93  ?  233 VAL   A C     1 
ATOM   1677 O  O     . VAL   A 1 233 ? 54.928  7.225   -20.434 1.00 41.20  ?  233 VAL   A O     1 
ATOM   1678 C  CB    . VAL   A 1 233 ? 53.037  7.131   -22.593 1.00 40.19  ?  233 VAL   A CB    1 
ATOM   1679 C  CG1   . VAL   A 1 233 ? 52.391  6.101   -21.670 1.00 40.37  ?  233 VAL   A CG1   1 
ATOM   1680 C  CG2   . VAL   A 1 233 ? 52.099  7.410   -23.748 1.00 41.56  ?  233 VAL   A CG2   1 
ATOM   1681 N  N     . ARG   A 1 234 ? 53.927  9.087   -19.584 1.00 47.80  ?  234 ARG   A N     1 
ATOM   1682 C  CA    . ARG   A 1 234 ? 54.555  9.062   -18.266 1.00 50.83  ?  234 ARG   A CA    1 
ATOM   1683 C  C     . ARG   A 1 234 ? 53.494  9.339   -17.205 1.00 46.57  ?  234 ARG   A C     1 
ATOM   1684 O  O     . ARG   A 1 234 ? 52.551  10.079  -17.457 1.00 47.22  ?  234 ARG   A O     1 
ATOM   1685 C  CB    . ARG   A 1 234 ? 55.678  10.118  -18.184 1.00 53.73  ?  234 ARG   A CB    1 
ATOM   1686 C  CG    . ARG   A 1 234 ? 56.896  9.820   -19.066 1.00 58.73  ?  234 ARG   A CG    1 
ATOM   1687 C  CD    . ARG   A 1 234 ? 57.671  8.575   -18.646 1.00 58.14  ?  234 ARG   A CD    1 
ATOM   1688 N  NE    . ARG   A 1 234 ? 57.958  8.556   -17.203 1.00 63.30  ?  234 ARG   A NE    1 
ATOM   1689 C  CZ    . ARG   A 1 234 ? 59.066  9.007   -16.609 1.00 63.46  ?  234 ARG   A CZ    1 
ATOM   1690 N  NH1   . ARG   A 1 234 ? 60.066  9.539   -17.309 1.00 69.22  ?  234 ARG   A NH1   1 
ATOM   1691 N  NH2   . ARG   A 1 234 ? 59.176  8.922   -15.288 1.00 62.88  ?  234 ARG   A NH2   1 
ATOM   1692 N  N     . TYR   A 1 235 ? 53.655  8.741   -16.025 1.00 48.05  ?  235 TYR   A N     1 
ATOM   1693 C  CA    . TYR   A 1 235 ? 52.717  8.917   -14.907 1.00 45.62  ?  235 TYR   A CA    1 
ATOM   1694 C  C     . TYR   A 1 235 ? 52.965  10.260  -14.218 1.00 46.52  ?  235 TYR   A C     1 
ATOM   1695 O  O     . TYR   A 1 235 ? 54.087  10.561  -13.836 1.00 47.86  ?  235 TYR   A O     1 
ATOM   1696 C  CB    . TYR   A 1 235 ? 52.861  7.776   -13.905 1.00 48.64  ?  235 TYR   A CB    1 
ATOM   1697 C  CG    . TYR   A 1 235 ? 51.663  7.608   -12.978 1.00 49.98  ?  235 TYR   A CG    1 
ATOM   1698 C  CD1   . TYR   A 1 235 ? 50.514  6.936   -13.409 1.00 47.99  ?  235 TYR   A CD1   1 
ATOM   1699 C  CD2   . TYR   A 1 235 ? 51.684  8.105   -11.678 1.00 49.40  ?  235 TYR   A CD2   1 
ATOM   1700 C  CE1   . TYR   A 1 235 ? 49.422  6.768   -12.585 1.00 47.22  ?  235 TYR   A CE1   1 
ATOM   1701 C  CE2   . TYR   A 1 235 ? 50.588  7.956   -10.834 1.00 53.45  ?  235 TYR   A CE2   1 
ATOM   1702 C  CZ    . TYR   A 1 235 ? 49.460  7.270   -11.286 1.00 54.64  ?  235 TYR   A CZ    1 
ATOM   1703 O  OH    . TYR   A 1 235 ? 48.370  7.120   -10.448 1.00 50.29  ?  235 TYR   A OH    1 
ATOM   1704 N  N     . ASP   A 1 236 ? 51.915  11.061  -14.088 1.00 45.06  ?  236 ASP   A N     1 
ATOM   1705 C  CA    . ASP   A 1 236 ? 51.964  12.362  -13.419 1.00 44.39  ?  236 ASP   A CA    1 
ATOM   1706 C  C     . ASP   A 1 236 ? 50.516  12.796  -13.271 1.00 43.55  ?  236 ASP   A C     1 
ATOM   1707 O  O     . ASP   A 1 236 ? 49.948  13.298  -14.224 1.00 45.56  ?  236 ASP   A O     1 
ATOM   1708 C  CB    . ASP   A 1 236 ? 52.789  13.375  -14.244 1.00 47.24  ?  236 ASP   A CB    1 
ATOM   1709 C  CG    . ASP   A 1 236 ? 52.970  14.732  -13.549 1.00 47.15  ?  236 ASP   A CG    1 
ATOM   1710 O  OD1   . ASP   A 1 236 ? 52.130  15.135  -12.715 1.00 46.74  ?  236 ASP   A OD1   1 
ATOM   1711 O  OD2   . ASP   A 1 236 ? 53.960  15.426  -13.878 1.00 50.93  ?  236 ASP   A OD2   1 
ATOM   1712 N  N     . VAL   A 1 237 ? 49.931  12.583  -12.086 1.00 43.51  ?  237 VAL   A N     1 
ATOM   1713 C  CA    . VAL   A 1 237 ? 48.496  12.843  -11.838 1.00 46.00  ?  237 VAL   A CA    1 
ATOM   1714 C  C     . VAL   A 1 237 ? 48.182  14.345  -11.884 1.00 47.93  ?  237 VAL   A C     1 
ATOM   1715 O  O     . VAL   A 1 237 ? 47.125  14.755  -12.387 1.00 47.57  ?  237 VAL   A O     1 
ATOM   1716 C  CB    . VAL   A 1 237 ? 48.005  12.238  -10.487 1.00 43.66  ?  237 VAL   A CB    1 
ATOM   1717 C  CG1   . VAL   A 1 237 ? 46.507  12.490  -10.274 1.00 42.70  ?  237 VAL   A CG1   1 
ATOM   1718 C  CG2   . VAL   A 1 237 ? 48.280  10.740  -10.420 1.00 44.63  ?  237 VAL   A CG2   1 
ATOM   1719 N  N     . GLN   A 1 238 ? 49.105  15.153  -11.366 1.00 52.11  ?  238 GLN   A N     1 
ATOM   1720 C  CA    . GLN   A 1 238 ? 48.926  16.617  -11.318 1.00 55.65  ?  238 GLN   A CA    1 
ATOM   1721 C  C     . GLN   A 1 238 ? 48.898  17.248  -12.724 1.00 56.23  ?  238 GLN   A C     1 
ATOM   1722 O  O     . GLN   A 1 238 ? 47.945  17.946  -13.076 1.00 58.64  ?  238 GLN   A O     1 
ATOM   1723 C  CB    . GLN   A 1 238 ? 50.030  17.248  -10.460 1.00 60.24  ?  238 GLN   A CB    1 
ATOM   1724 C  CG    . GLN   A 1 238 ? 50.071  18.773  -10.472 1.00 63.84  ?  238 GLN   A CG    1 
ATOM   1725 C  CD    . GLN   A 1 238 ? 51.077  19.343  -9.482  1.00 66.02  ?  238 GLN   A CD    1 
ATOM   1726 O  OE1   . GLN   A 1 238 ? 52.069  19.960  -9.869  1.00 67.99  ?  238 GLN   A OE1   1 
ATOM   1727 N  NE2   . GLN   A 1 238 ? 50.831  19.127  -8.201  1.00 66.37  ?  238 GLN   A NE2   1 
ATOM   1728 N  N     . ASN   A 1 239 ? 49.926  16.964  -13.523 1.00 54.33  ?  239 ASN   A N     1 
ATOM   1729 C  CA    . ASN   A 1 239 ? 50.111  17.581  -14.845 1.00 53.76  ?  239 ASN   A CA    1 
ATOM   1730 C  C     . ASN   A 1 239 ? 49.559  16.780  -16.031 1.00 51.24  ?  239 ASN   A C     1 
ATOM   1731 O  O     . ASN   A 1 239 ? 49.420  17.341  -17.129 1.00 49.69  ?  239 ASN   A O     1 
ATOM   1732 C  CB    . ASN   A 1 239 ? 51.600  17.853  -15.103 1.00 55.05  ?  239 ASN   A CB    1 
ATOM   1733 C  CG    . ASN   A 1 239 ? 52.221  18.744  -14.050 1.00 56.14  ?  239 ASN   A CG    1 
ATOM   1734 O  OD1   . ASN   A 1 239 ? 51.760  19.868  -13.833 1.00 62.14  ?  239 ASN   A OD1   1 
ATOM   1735 N  ND2   . ASN   A 1 239 ? 53.271  18.256  -13.389 1.00 55.32  ?  239 ASN   A ND2   1 
ATOM   1736 N  N     . LYS   A 1 240 ? 49.290  15.485  -15.828 1.00 47.92  ?  240 LYS   A N     1 
ATOM   1737 C  CA    . LYS   A 1 240 ? 48.878  14.563  -16.904 1.00 44.60  ?  240 LYS   A CA    1 
ATOM   1738 C  C     . LYS   A 1 240 ? 47.798  13.587  -16.422 1.00 44.61  ?  240 LYS   A C     1 
ATOM   1739 O  O     . LYS   A 1 240 ? 47.964  12.364  -16.516 1.00 44.68  ?  240 LYS   A O     1 
ATOM   1740 C  CB    . LYS   A 1 240 ? 50.086  13.773  -17.426 1.00 41.95  ?  240 LYS   A CB    1 
ATOM   1741 C  CG    . LYS   A 1 240 ? 51.275  14.619  -17.891 1.00 41.53  ?  240 LYS   A CG    1 
ATOM   1742 C  CD    . LYS   A 1 240 ? 52.489  13.769  -18.232 1.00 40.29  ?  240 LYS   A CD    1 
ATOM   1743 C  CE    . LYS   A 1 240 ? 52.288  12.774  -19.367 1.00 40.18  ?  240 LYS   A CE    1 
ATOM   1744 N  NZ    . LYS   A 1 240 ? 52.138  13.462  -20.677 1.00 38.66  ?  240 LYS   A NZ    1 
ATOM   1745 N  N     . ALA   A 1 241 ? 46.697  14.139  -15.916 1.00 48.20  ?  241 ALA   A N     1 
ATOM   1746 C  CA    . ALA   A 1 241 ? 45.612  13.361  -15.290 1.00 49.27  ?  241 ALA   A CA    1 
ATOM   1747 C  C     . ALA   A 1 241 ? 45.064  12.251  -16.206 1.00 47.09  ?  241 ALA   A C     1 
ATOM   1748 O  O     . ALA   A 1 241 ? 45.004  11.076  -15.818 1.00 47.06  ?  241 ALA   A O     1 
ATOM   1749 C  CB    . ALA   A 1 241 ? 44.490  14.296  -14.839 1.00 50.29  ?  241 ALA   A CB    1 
ATOM   1750 N  N     . GLY   A 1 242 ? 44.723  12.624  -17.433 1.00 43.55  ?  242 GLY   A N     1 
ATOM   1751 C  CA    . GLY   A 1 242 ? 44.141  11.695  -18.406 1.00 43.51  ?  242 GLY   A CA    1 
ATOM   1752 C  C     . GLY   A 1 242 ? 44.988  10.478  -18.718 1.00 39.91  ?  242 GLY   A C     1 
ATOM   1753 O  O     . GLY   A 1 242 ? 44.514  9.333   -18.628 1.00 36.19  ?  242 GLY   A O     1 
ATOM   1754 N  N     . VAL   A 1 243 ? 46.245  10.741  -19.072 1.00 41.65  ?  243 VAL   A N     1 
ATOM   1755 C  CA    . VAL   A 1 243 ? 47.242  9.699   -19.395 1.00 40.56  ?  243 VAL   A CA    1 
ATOM   1756 C  C     . VAL   A 1 243 ? 47.553  8.815   -18.175 1.00 38.10  ?  243 VAL   A C     1 
ATOM   1757 O  O     . VAL   A 1 243 ? 47.727  7.596   -18.303 1.00 34.18  ?  243 VAL   A O     1 
ATOM   1758 C  CB    . VAL   A 1 243 ? 48.541  10.337  -19.946 1.00 40.64  ?  243 VAL   A CB    1 
ATOM   1759 C  CG1   . VAL   A 1 243 ? 49.653  9.294   -20.127 1.00 42.99  ?  243 VAL   A CG1   1 
ATOM   1760 C  CG2   . VAL   A 1 243 ? 48.264  11.043  -21.283 1.00 42.50  ?  243 VAL   A CG2   1 
ATOM   1761 N  N     . SER   A 1 244 ? 47.642  9.448   -17.005 1.00 35.87  ?  244 SER   A N     1 
ATOM   1762 C  CA    . SER   A 1 244 ? 47.883  8.732   -15.751 1.00 38.10  ?  244 SER   A CA    1 
ATOM   1763 C  C     . SER   A 1 244 ? 46.750  7.751   -15.436 1.00 37.50  ?  244 SER   A C     1 
ATOM   1764 O  O     . SER   A 1 244 ? 46.999  6.619   -15.022 1.00 40.50  ?  244 SER   A O     1 
ATOM   1765 C  CB    . SER   A 1 244 ? 48.105  9.722   -14.604 1.00 40.02  ?  244 SER   A CB    1 
ATOM   1766 O  OG    . SER   A 1 244 ? 49.293  10.486  -14.824 1.00 40.76  ?  244 SER   A OG    1 
ATOM   1767 N  N     . ASN   A 1 245 ? 45.510  8.182   -15.656 1.00 38.10  ?  245 ASN   A N     1 
ATOM   1768 C  CA    . ASN   A 1 245 ? 44.344  7.326   -15.493 1.00 40.26  ?  245 ASN   A CA    1 
ATOM   1769 C  C     . ASN   A 1 245 ? 44.404  6.127   -16.427 1.00 38.85  ?  245 ASN   A C     1 
ATOM   1770 O  O     . ASN   A 1 245 ? 44.197  4.996   -15.990 1.00 40.01  ?  245 ASN   A O     1 
ATOM   1771 C  CB    . ASN   A 1 245 ? 43.044  8.117   -15.729 1.00 43.21  ?  245 ASN   A CB    1 
ATOM   1772 C  CG    . ASN   A 1 245 ? 41.791  7.344   -15.318 1.00 46.86  ?  245 ASN   A CG    1 
ATOM   1773 O  OD1   . ASN   A 1 245 ? 41.780  6.644   -14.311 1.00 47.81  ?  245 ASN   A OD1   1 
ATOM   1774 N  ND2   . ASN   A 1 245 ? 40.713  7.504   -16.082 1.00 49.27  ?  245 ASN   A ND2   1 
ATOM   1775 N  N     . LEU   A 1 246 ? 44.715  6.379   -17.709 1.00 38.24  ?  246 LEU   A N     1 
ATOM   1776 C  CA    . LEU   A 1 246 ? 44.855  5.309   -18.705 1.00 37.14  ?  246 LEU   A CA    1 
ATOM   1777 C  C     . LEU   A 1 246 ? 45.879  4.263   -18.282 1.00 37.07  ?  246 LEU   A C     1 
ATOM   1778 O  O     . LEU   A 1 246 ? 45.661  3.061   -18.458 1.00 34.44  ?  246 LEU   A O     1 
ATOM   1779 C  CB    . LEU   A 1 246 ? 45.197  5.884   -20.091 1.00 36.95  ?  246 LEU   A CB    1 
ATOM   1780 C  CG    . LEU   A 1 246 ? 44.114  6.781   -20.711 1.00 38.68  ?  246 LEU   A CG    1 
ATOM   1781 C  CD1   . LEU   A 1 246 ? 44.639  7.434   -21.974 1.00 41.44  ?  246 LEU   A CD1   1 
ATOM   1782 C  CD2   . LEU   A 1 246 ? 42.814  6.039   -21.017 1.00 38.03  ?  246 LEU   A CD2   1 
ATOM   1783 N  N     . LEU   A 1 247 ? 46.984  4.731   -17.688 1.00 37.83  ?  247 LEU   A N     1 
ATOM   1784 C  CA    . LEU   A 1 247 ? 48.030  3.849   -17.182 1.00 37.59  ?  247 LEU   A CA    1 
ATOM   1785 C  C     . LEU   A 1 247 ? 47.585  3.032   -15.969 1.00 36.43  ?  247 LEU   A C     1 
ATOM   1786 O  O     . LEU   A 1 247 ? 47.879  1.828   -15.895 1.00 34.75  ?  247 LEU   A O     1 
ATOM   1787 C  CB    . LEU   A 1 247 ? 49.302  4.654   -16.840 1.00 37.27  ?  247 LEU   A CB    1 
ATOM   1788 C  CG    . LEU   A 1 247 ? 50.119  5.136   -18.041 1.00 35.86  ?  247 LEU   A CG    1 
ATOM   1789 C  CD1   . LEU   A 1 247 ? 51.185  6.117   -17.590 1.00 37.58  ?  247 LEU   A CD1   1 
ATOM   1790 C  CD2   . LEU   A 1 247 ? 50.746  3.955   -18.760 1.00 34.14  ?  247 LEU   A CD2   1 
ATOM   1791 N  N     . ASP   A 1 248 ? 46.891  3.685   -15.040 1.00 37.66  ?  248 ASP   A N     1 
ATOM   1792 C  CA    . ASP   A 1 248 ? 46.363  3.012   -13.837 1.00 40.88  ?  248 ASP   A CA    1 
ATOM   1793 C  C     . ASP   A 1 248 ? 45.367  1.926   -14.209 1.00 39.77  ?  248 ASP   A C     1 
ATOM   1794 O  O     . ASP   A 1 248 ? 45.439  0.828   -13.693 1.00 38.71  ?  248 ASP   A O     1 
ATOM   1795 C  CB    . ASP   A 1 248 ? 45.696  4.015   -12.882 1.00 43.96  ?  248 ASP   A CB    1 
ATOM   1796 C  CG    . ASP   A 1 248 ? 46.684  4.705   -11.970 1.00 45.90  ?  248 ASP   A CG    1 
ATOM   1797 O  OD1   . ASP   A 1 248 ? 46.397  5.848   -11.576 1.00 46.37  ?  248 ASP   A OD1   1 
ATOM   1798 O  OD2   . ASP   A 1 248 ? 47.740  4.112   -11.661 1.00 44.28  ?  248 ASP   A OD2   1 
ATOM   1799 N  N     . ILE   A 1 249 ? 44.465  2.249   -15.137 1.00 41.97  ?  249 ILE   A N     1 
ATOM   1800 C  CA    . ILE   A 1 249 ? 43.460  1.292   -15.637 1.00 40.60  ?  249 ILE   A CA    1 
ATOM   1801 C  C     . ILE   A 1 249 ? 44.158  0.082   -16.248 1.00 37.48  ?  249 ILE   A C     1 
ATOM   1802 O  O     . ILE   A 1 249 ? 43.749  -1.036  -15.997 1.00 35.01  ?  249 ILE   A O     1 
ATOM   1803 C  CB    . ILE   A 1 249 ? 42.480  1.936   -16.654 1.00 41.47  ?  249 ILE   A CB    1 
ATOM   1804 C  CG1   . ILE   A 1 249 ? 41.656  3.045   -15.981 1.00 41.83  ?  249 ILE   A CG1   1 
ATOM   1805 C  CG2   . ILE   A 1 249 ? 41.538  0.871   -17.246 1.00 42.52  ?  249 ILE   A CG2   1 
ATOM   1806 C  CD1   . ILE   A 1 249 ? 40.746  3.836   -16.896 1.00 40.51  ?  249 ILE   A CD1   1 
ATOM   1807 N  N     . LEU   A 1 250 ? 45.217  0.324   -17.029 1.00 40.35  ?  250 LEU   A N     1 
ATOM   1808 C  CA    . LEU   A 1 250 ? 45.928  -0.747  -17.733 1.00 40.54  ?  250 LEU   A CA    1 
ATOM   1809 C  C     . LEU   A 1 250 ? 46.671  -1.656  -16.744 1.00 40.65  ?  250 LEU   A C     1 
ATOM   1810 O  O     . LEU   A 1 250 ? 46.627  -2.894  -16.847 1.00 33.45  ?  250 LEU   A O     1 
ATOM   1811 C  CB    . LEU   A 1 250 ? 46.882  -0.164  -18.774 1.00 38.47  ?  250 LEU   A CB    1 
ATOM   1812 C  CG    . LEU   A 1 250 ? 47.667  -1.176  -19.613 1.00 41.27  ?  250 LEU   A CG    1 
ATOM   1813 C  CD1   . LEU   A 1 250 ? 46.770  -2.192  -20.301 1.00 40.31  ?  250 LEU   A CD1   1 
ATOM   1814 C  CD2   . LEU   A 1 250 ? 48.523  -0.432  -20.644 1.00 41.73  ?  250 LEU   A CD2   1 
ATOM   1815 N  N     . SER   A 1 251 ? 47.333  -1.020  -15.779 1.00 40.77  ?  251 SER   A N     1 
ATOM   1816 C  CA    . SER   A 1 251 ? 48.009  -1.733  -14.694 1.00 46.03  ?  251 SER   A CA    1 
ATOM   1817 C  C     . SER   A 1 251 ? 47.069  -2.627  -13.870 1.00 44.45  ?  251 SER   A C     1 
ATOM   1818 O  O     . SER   A 1 251 ? 47.416  -3.747  -13.534 1.00 43.99  ?  251 SER   A O     1 
ATOM   1819 C  CB    . SER   A 1 251 ? 48.694  -0.729  -13.766 1.00 43.84  ?  251 SER   A CB    1 
ATOM   1820 O  OG    . SER   A 1 251 ? 49.388  -1.399  -12.743 1.00 46.13  ?  251 SER   A OG    1 
ATOM   1821 N  N     . ALA   A 1 252 ? 45.888  -2.106  -13.551 1.00 44.42  ?  252 ALA   A N     1 
ATOM   1822 C  CA    . ALA   A 1 252 ? 44.871  -2.828  -12.767 1.00 46.34  ?  252 ALA   A CA    1 
ATOM   1823 C  C     . ALA   A 1 252 ? 44.399  -4.080  -13.470 1.00 44.57  ?  252 ALA   A C     1 
ATOM   1824 O  O     . ALA   A 1 252 ? 44.208  -5.098  -12.821 1.00 45.51  ?  252 ALA   A O     1 
ATOM   1825 C  CB    . ALA   A 1 252 ? 43.684  -1.915  -12.472 1.00 45.50  ?  252 ALA   A CB    1 
ATOM   1826 N  N     . VAL   A 1 253 ? 44.238  -4.000  -14.797 1.00 47.02  ?  253 VAL   A N     1 
ATOM   1827 C  CA    . VAL   A 1 253 ? 43.804  -5.138  -15.627 1.00 47.92  ?  253 VAL   A CA    1 
ATOM   1828 C  C     . VAL   A 1 253 ? 44.912  -6.172  -15.789 1.00 48.37  ?  253 VAL   A C     1 
ATOM   1829 O  O     . VAL   A 1 253 ? 44.686  -7.358  -15.569 1.00 49.30  ?  253 VAL   A O     1 
ATOM   1830 C  CB    . VAL   A 1 253 ? 43.307  -4.690  -17.024 1.00 47.06  ?  253 VAL   A CB    1 
ATOM   1831 C  CG1   . VAL   A 1 253 ? 42.855  -5.881  -17.853 1.00 47.01  ?  253 VAL   A CG1   1 
ATOM   1832 C  CG2   . VAL   A 1 253 ? 42.150  -3.713  -16.904 1.00 46.82  ?  253 VAL   A CG2   1 
ATOM   1833 N  N     . THR   A 1 254 ? 46.103  -5.710  -16.171 1.00 51.33  ?  254 THR   A N     1 
ATOM   1834 C  CA    . THR   A 1 254 ? 47.223  -6.592  -16.556 1.00 50.53  ?  254 THR   A CA    1 
ATOM   1835 C  C     . THR   A 1 254 ? 48.126  -7.003  -15.393 1.00 49.11  ?  254 THR   A C     1 
ATOM   1836 O  O     . THR   A 1 254 ? 48.813  -8.020  -15.458 1.00 52.37  ?  254 THR   A O     1 
ATOM   1837 C  CB    . THR   A 1 254 ? 48.084  -5.916  -17.650 1.00 50.63  ?  254 THR   A CB    1 
ATOM   1838 O  OG1   . THR   A 1 254 ? 48.704  -4.722  -17.141 1.00 49.75  ?  254 THR   A OG1   1 
ATOM   1839 C  CG2   . THR   A 1 254 ? 47.224  -5.537  -18.862 1.00 46.80  ?  254 THR   A CG2   1 
ATOM   1840 N  N     . GLY   A 1 255 ? 48.127  -6.204  -14.330 1.00 50.22  ?  255 GLY   A N     1 
ATOM   1841 C  CA    . GLY   A 1 255 ? 49.030  -6.408  -13.194 1.00 50.15  ?  255 GLY   A CA    1 
ATOM   1842 C  C     . GLY   A 1 255 ? 50.464  -5.972  -13.462 1.00 51.10  ?  255 GLY   A C     1 
ATOM   1843 O  O     . GLY   A 1 255 ? 51.327  -6.180  -12.613 1.00 51.03  ?  255 GLY   A O     1 
ATOM   1844 N  N     . GLN   A 1 256 ? 50.715  -5.358  -14.626 1.00 47.97  ?  256 GLN   A N     1 
ATOM   1845 C  CA    . GLN   A 1 256 ? 52.023  -4.802  -14.966 1.00 46.41  ?  256 GLN   A CA    1 
ATOM   1846 C  C     . GLN   A 1 256 ? 52.191  -3.515  -14.191 1.00 41.94  ?  256 GLN   A C     1 
ATOM   1847 O  O     . GLN   A 1 256 ? 51.242  -2.746  -14.071 1.00 42.00  ?  256 GLN   A O     1 
ATOM   1848 C  CB    . GLN   A 1 256 ? 52.120  -4.473  -16.463 1.00 47.76  ?  256 GLN   A CB    1 
ATOM   1849 C  CG    . GLN   A 1 256 ? 51.870  -5.627  -17.408 1.00 50.46  ?  256 GLN   A CG    1 
ATOM   1850 C  CD    . GLN   A 1 256 ? 51.925  -5.172  -18.848 1.00 53.38  ?  256 GLN   A CD    1 
ATOM   1851 O  OE1   . GLN   A 1 256 ? 50.895  -5.014  -19.510 1.00 56.95  ?  256 GLN   A OE1   1 
ATOM   1852 N  NE2   . GLN   A 1 256 ? 53.131  -4.919  -19.331 1.00 53.35  ?  256 GLN   A NE2   1 
ATOM   1853 N  N     . SER   A 1 257 ? 53.394  -3.266  -13.683 1.00 41.41  ?  257 SER   A N     1 
ATOM   1854 C  CA    . SER   A 1 257 ? 53.678  -2.035  -12.915 1.00 39.64  ?  257 SER   A CA    1 
ATOM   1855 C  C     . SER   A 1 257 ? 53.681  -0.802  -13.816 1.00 38.93  ?  257 SER   A C     1 
ATOM   1856 O  O     . SER   A 1 257 ? 53.881  -0.913  -15.023 1.00 38.29  ?  257 SER   A O     1 
ATOM   1857 C  CB    . SER   A 1 257 ? 55.015  -2.144  -12.171 1.00 40.78  ?  257 SER   A CB    1 
ATOM   1858 O  OG    . SER   A 1 257 ? 56.121  -2.005  -13.042 1.00 42.81  ?  257 SER   A OG    1 
ATOM   1859 N  N     . ILE   A 1 258 ? 53.486  0.367   -13.214 1.00 39.12  ?  258 ILE   A N     1 
ATOM   1860 C  CA    . ILE   A 1 258 ? 53.557  1.639   -13.936 1.00 41.22  ?  258 ILE   A CA    1 
ATOM   1861 C  C     . ILE   A 1 258 ? 54.925  1.843   -14.596 1.00 43.36  ?  258 ILE   A C     1 
ATOM   1862 O  O     . ILE   A 1 258 ? 54.968  2.158   -15.783 1.00 43.79  ?  258 ILE   A O     1 
ATOM   1863 C  CB    . ILE   A 1 258 ? 53.147  2.838   -13.026 1.00 39.02  ?  258 ILE   A CB    1 
ATOM   1864 C  CG1   . ILE   A 1 258 ? 51.661  2.787   -12.687 1.00 41.05  ?  258 ILE   A CG1   1 
ATOM   1865 C  CG2   . ILE   A 1 258 ? 53.479  4.186   -13.660 1.00 44.38  ?  258 ILE   A CG2   1 
ATOM   1866 C  CD1   . ILE   A 1 258 ? 50.713  2.619   -13.856 1.00 41.61  ?  258 ILE   A CD1   1 
ATOM   1867 N  N     . PRO   A 1 259 ? 56.039  1.671   -13.847 1.00 44.94  ?  259 PRO   A N     1 
ATOM   1868 C  CA    . PRO   A 1 259 ? 57.371  1.818   -14.459 1.00 47.85  ?  259 PRO   A CA    1 
ATOM   1869 C  C     . PRO   A 1 259 ? 57.598  0.904   -15.667 1.00 50.15  ?  259 PRO   A C     1 
ATOM   1870 O  O     . PRO   A 1 259 ? 58.194  1.334   -16.672 1.00 48.09  ?  259 PRO   A O     1 
ATOM   1871 C  CB    . PRO   A 1 259 ? 58.325  1.458   -13.313 1.00 49.13  ?  259 PRO   A CB    1 
ATOM   1872 C  CG    . PRO   A 1 259 ? 57.570  1.829   -12.090 1.00 48.93  ?  259 PRO   A CG    1 
ATOM   1873 C  CD    . PRO   A 1 259 ? 56.146  1.491   -12.387 1.00 49.64  ?  259 PRO   A CD    1 
ATOM   1874 N  N     . GLU   A 1 260 ? 57.118  -0.339  -15.574 1.00 50.16  ?  260 GLU   A N     1 
ATOM   1875 C  CA    . GLU   A 1 260 ? 57.203  -1.282  -16.687 1.00 49.23  ?  260 GLU   A CA    1 
ATOM   1876 C  C     . GLU   A 1 260 ? 56.424  -0.763  -17.912 1.00 48.13  ?  260 GLU   A C     1 
ATOM   1877 O  O     . GLU   A 1 260 ? 56.872  -0.923  -19.042 1.00 53.68  ?  260 GLU   A O     1 
ATOM   1878 C  CB    . GLU   A 1 260 ? 56.683  -2.662  -16.269 1.00 50.75  ?  260 GLU   A CB    1 
ATOM   1879 C  CG    . GLU   A 1 260 ? 56.964  -3.778  -17.285 1.00 55.46  ?  260 GLU   A CG    1 
ATOM   1880 C  CD    . GLU   A 1 260 ? 56.185  -5.076  -17.036 1.00 57.90  ?  260 GLU   A CD    1 
ATOM   1881 O  OE1   . GLU   A 1 260 ? 55.720  -5.695  -18.031 1.00 55.98  ?  260 GLU   A OE1   1 
ATOM   1882 O  OE2   . GLU   A 1 260 ? 56.045  -5.487  -15.858 1.00 59.56  ?  260 GLU   A OE2   1 
ATOM   1883 N  N     . LEU   A 1 261 ? 55.260  -0.149  -17.687 1.00 41.64  ?  261 LEU   A N     1 
ATOM   1884 C  CA    . LEU   A 1 261 ? 54.427  0.359   -18.783 1.00 39.59  ?  261 LEU   A CA    1 
ATOM   1885 C  C     . LEU   A 1 261 ? 55.016  1.629   -19.397 1.00 40.28  ?  261 LEU   A C     1 
ATOM   1886 O  O     . LEU   A 1 261 ? 55.036  1.770   -20.615 1.00 39.60  ?  261 LEU   A O     1 
ATOM   1887 C  CB    . LEU   A 1 261 ? 52.996  0.614   -18.310 1.00 38.08  ?  261 LEU   A CB    1 
ATOM   1888 C  CG    . LEU   A 1 261 ? 52.194  -0.635  -17.955 1.00 39.90  ?  261 LEU   A CG    1 
ATOM   1889 C  CD1   . LEU   A 1 261 ? 50.935  -0.219  -17.224 1.00 41.30  ?  261 LEU   A CD1   1 
ATOM   1890 C  CD2   . LEU   A 1 261 ? 51.843  -1.477  -19.170 1.00 41.24  ?  261 LEU   A CD2   1 
ATOM   1891 N  N     . GLU   A 1 262 ? 55.503  2.540   -18.555 1.00 40.53  ?  262 GLU   A N     1 
ATOM   1892 C  CA    . GLU   A 1 262 ? 56.228  3.722   -19.016 1.00 44.65  ?  262 GLU   A CA    1 
ATOM   1893 C  C     . GLU   A 1 262 ? 57.357  3.359   -20.005 1.00 47.92  ?  262 GLU   A C     1 
ATOM   1894 O  O     . GLU   A 1 262 ? 57.577  4.066   -20.985 1.00 50.28  ?  262 GLU   A O     1 
ATOM   1895 C  CB    . GLU   A 1 262 ? 56.788  4.511   -17.828 1.00 47.01  ?  262 GLU   A CB    1 
ATOM   1896 C  CG    . GLU   A 1 262 ? 55.745  5.359   -17.119 1.00 48.44  ?  262 GLU   A CG    1 
ATOM   1897 C  CD    . GLU   A 1 262 ? 56.238  5.974   -15.821 1.00 49.80  ?  262 GLU   A CD    1 
ATOM   1898 O  OE1   . GLU   A 1 262 ? 56.957  5.298   -15.059 1.00 55.92  ?  262 GLU   A OE1   1 
ATOM   1899 O  OE2   . GLU   A 1 262 ? 55.886  7.134   -15.539 1.00 48.14  ?  262 GLU   A OE2   1 
ATOM   1900 N  N     . LYS   A 1 263 ? 58.044  2.244   -19.756 1.00 49.34  ?  263 LYS   A N     1 
ATOM   1901 C  CA    . LYS   A 1 263 ? 59.074  1.738   -20.673 1.00 52.45  ?  263 LYS   A CA    1 
ATOM   1902 C  C     . LYS   A 1 263 ? 58.450  1.128   -21.929 1.00 51.47  ?  263 LYS   A C     1 
ATOM   1903 O  O     . LYS   A 1 263 ? 58.899  1.412   -23.034 1.00 52.31  ?  263 LYS   A O     1 
ATOM   1904 C  CB    . LYS   A 1 263 ? 59.981  0.714   -19.976 1.00 51.79  ?  263 LYS   A CB    1 
ATOM   1905 N  N     . GLN   A 1 264 ? 57.401  0.318   -21.742 1.00 53.39  ?  264 GLN   A N     1 
ATOM   1906 C  CA    . GLN   A 1 264 ? 56.663  -0.334  -22.834 1.00 55.06  ?  264 GLN   A CA    1 
ATOM   1907 C  C     . GLN   A 1 264 ? 56.152  0.645   -23.911 1.00 54.22  ?  264 GLN   A C     1 
ATOM   1908 O  O     . GLN   A 1 264 ? 56.071  0.272   -25.083 1.00 51.17  ?  264 GLN   A O     1 
ATOM   1909 C  CB    . GLN   A 1 264 ? 55.505  -1.172  -22.260 1.00 55.90  ?  264 GLN   A CB    1 
ATOM   1910 C  CG    . GLN   A 1 264 ? 54.670  -1.923  -23.294 1.00 59.88  ?  264 GLN   A CG    1 
ATOM   1911 C  CD    . GLN   A 1 264 ? 53.759  -2.973  -22.667 1.00 61.60  ?  264 GLN   A CD    1 
ATOM   1912 O  OE1   . GLN   A 1 264 ? 54.197  -3.771  -21.839 1.00 64.11  ?  264 GLN   A OE1   1 
ATOM   1913 N  NE2   . GLN   A 1 264 ? 52.488  -2.981  -23.063 1.00 62.30  ?  264 GLN   A NE2   1 
ATOM   1914 N  N     . PHE   A 1 265 ? 55.826  1.877   -23.494 1.00 51.62  ?  265 PHE   A N     1 
ATOM   1915 C  CA    . PHE   A 1 265 ? 55.303  2.931   -24.371 1.00 51.51  ?  265 PHE   A CA    1 
ATOM   1916 C  C     . PHE   A 1 265 ? 56.308  4.083   -24.595 1.00 53.13  ?  265 PHE   A C     1 
ATOM   1917 O  O     . PHE   A 1 265 ? 55.905  5.223   -24.924 1.00 48.66  ?  265 PHE   A O     1 
ATOM   1918 C  CB    . PHE   A 1 265 ? 53.984  3.486   -23.779 1.00 49.21  ?  265 PHE   A CB    1 
ATOM   1919 C  CG    . PHE   A 1 265 ? 52.860  2.485   -23.749 1.00 48.89  ?  265 PHE   A CG    1 
ATOM   1920 C  CD1   . PHE   A 1 265 ? 52.554  1.794   -22.587 1.00 49.05  ?  265 PHE   A CD1   1 
ATOM   1921 C  CD2   . PHE   A 1 265 ? 52.103  2.226   -24.889 1.00 48.17  ?  265 PHE   A CD2   1 
ATOM   1922 C  CE1   . PHE   A 1 265 ? 51.532  0.847   -22.562 1.00 49.79  ?  265 PHE   A CE1   1 
ATOM   1923 C  CE2   . PHE   A 1 265 ? 51.080  1.282   -24.870 1.00 47.00  ?  265 PHE   A CE2   1 
ATOM   1924 C  CZ    . PHE   A 1 265 ? 50.790  0.595   -23.703 1.00 48.52  ?  265 PHE   A CZ    1 
ATOM   1925 N  N     . GLU   A 1 266 ? 57.608  3.810   -24.437 1.00 50.65  ?  266 GLU   A N     1 
ATOM   1926 C  CA    . GLU   A 1 266 ? 58.624  4.859   -24.677 1.00 53.52  ?  266 GLU   A CA    1 
ATOM   1927 C  C     . GLU   A 1 266 ? 58.688  5.203   -26.185 1.00 49.03  ?  266 GLU   A C     1 
ATOM   1928 O  O     . GLU   A 1 266 ? 58.718  4.312   -27.029 1.00 47.36  ?  266 GLU   A O     1 
ATOM   1929 C  CB    . GLU   A 1 266 ? 60.010  4.451   -24.146 1.00 54.85  ?  266 GLU   A CB    1 
ATOM   1930 C  CG    . GLU   A 1 266 ? 60.910  5.648   -23.828 1.00 57.61  ?  266 GLU   A CG    1 
ATOM   1931 C  CD    . GLU   A 1 266 ? 62.372  5.263   -23.615 1.00 55.95  ?  266 GLU   A CD    1 
ATOM   1932 N  N     . GLY   A 1 267 ? 58.661  6.494   -26.500 1.00 48.39  ?  267 GLY   A N     1 
ATOM   1933 C  CA    . GLY   A 1 267 ? 58.608  6.970   -27.893 1.00 51.79  ?  267 GLY   A CA    1 
ATOM   1934 C  C     . GLY   A 1 267 ? 57.283  6.731   -28.606 1.00 55.14  ?  267 GLY   A C     1 
ATOM   1935 O  O     . GLY   A 1 267 ? 57.207  6.820   -29.850 1.00 50.36  ?  267 GLY   A O     1 
ATOM   1936 N  N     . LYS   A 1 268 ? 56.238  6.446   -27.821 1.00 57.36  ?  268 LYS   A N     1 
ATOM   1937 C  CA    . LYS   A 1 268 ? 54.910  6.142   -28.351 1.00 56.51  ?  268 LYS   A CA    1 
ATOM   1938 C  C     . LYS   A 1 268 ? 53.927  7.260   -27.992 1.00 52.75  ?  268 LYS   A C     1 
ATOM   1939 O  O     . LYS   A 1 268 ? 54.136  8.029   -27.064 1.00 51.53  ?  268 LYS   A O     1 
ATOM   1940 C  CB    . LYS   A 1 268 ? 54.424  4.787   -27.854 1.00 57.46  ?  268 LYS   A CB    1 
ATOM   1941 C  CG    . LYS   A 1 268 ? 55.409  3.653   -28.102 1.00 62.30  ?  268 LYS   A CG    1 
ATOM   1942 C  CD    . LYS   A 1 268 ? 55.607  3.338   -29.581 1.00 66.61  ?  268 LYS   A CD    1 
ATOM   1943 C  CE    . LYS   A 1 268 ? 54.606  2.320   -30.094 1.00 71.28  ?  268 LYS   A CE    1 
ATOM   1944 N  NZ    . LYS   A 1 268 ? 54.880  0.953   -29.560 1.00 74.94  ?  268 LYS   A NZ    1 
ATOM   1945 N  N     . MET   A 1 269 ? 52.899  7.363   -28.813 1.00 49.97  ?  269 MET   A N     1 
ATOM   1946 C  CA    . MET   A 1 269 ? 51.832  8.348   -28.729 1.00 48.78  ?  269 MET   A CA    1 
ATOM   1947 C  C     . MET   A 1 269 ? 50.621  7.779   -28.001 1.00 46.72  ?  269 MET   A C     1 
ATOM   1948 O  O     . MET   A 1 269 ? 50.498  6.563   -27.792 1.00 46.23  ?  269 MET   A O     1 
ATOM   1949 C  CB    . MET   A 1 269 ? 51.434  8.779   -30.144 1.00 48.85  ?  269 MET   A CB    1 
ATOM   1950 C  CG    . MET   A 1 269 ? 52.615  9.106   -31.057 1.00 48.94  ?  269 MET   A CG    1 
ATOM   1951 S  SD    . MET   A 1 269 ? 53.567  10.542  -30.504 1.00 51.41  ?  269 MET   A SD    1 
ATOM   1952 C  CE    . MET   A 1 269 ? 55.224  9.864   -30.556 1.00 55.43  ?  269 MET   A CE    1 
ATOM   1953 N  N     . TYR   A 1 270 ? 49.710  8.674   -27.642 1.00 57.18  ?  270 TYR   A N     1 
ATOM   1954 C  CA    . TYR   A 1 270 ? 48.543  8.313   -26.814 1.00 53.92  ?  270 TYR   A CA    1 
ATOM   1955 C  C     . TYR   A 1 270 ? 47.556  7.377   -27.507 1.00 50.19  ?  270 TYR   A C     1 
ATOM   1956 O  O     . TYR   A 1 270 ? 46.833  6.664   -26.848 1.00 53.05  ?  270 TYR   A O     1 
ATOM   1957 C  CB    . TYR   A 1 270 ? 47.841  9.578   -26.316 1.00 49.80  ?  270 TYR   A CB    1 
ATOM   1958 C  CG    . TYR   A 1 270 ? 48.741  10.562  -25.589 1.00 46.02  ?  270 TYR   A CG    1 
ATOM   1959 C  CD1   . TYR   A 1 270 ? 49.924  10.160  -24.980 1.00 46.20  ?  270 TYR   A CD1   1 
ATOM   1960 C  CD2   . TYR   A 1 270 ? 48.388  11.898  -25.496 1.00 46.35  ?  270 TYR   A CD2   1 
ATOM   1961 C  CE1   . TYR   A 1 270 ? 50.744  11.061  -24.321 1.00 48.20  ?  270 TYR   A CE1   1 
ATOM   1962 C  CE2   . TYR   A 1 270 ? 49.195  12.810  -24.829 1.00 48.15  ?  270 TYR   A CE2   1 
ATOM   1963 C  CZ    . TYR   A 1 270 ? 50.375  12.392  -24.241 1.00 48.68  ?  270 TYR   A CZ    1 
ATOM   1964 O  OH    . TYR   A 1 270 ? 51.170  13.302  -23.583 1.00 49.90  ?  270 TYR   A OH    1 
ATOM   1965 N  N     . GLY   A 1 271 ? 47.554  7.350   -28.834 1.00 53.30  ?  271 GLY   A N     1 
ATOM   1966 C  CA    . GLY   A 1 271 ? 46.743  6.389   -29.582 1.00 53.64  ?  271 GLY   A CA    1 
ATOM   1967 C  C     . GLY   A 1 271 ? 47.134  4.947   -29.323 1.00 52.64  ?  271 GLY   A C     1 
ATOM   1968 O  O     . GLY   A 1 271 ? 46.253  4.104   -29.150 1.00 49.02  ?  271 GLY   A O     1 
ATOM   1969 N  N     . HIS   A 1 272 ? 48.449  4.674   -29.267 1.00 50.64  ?  272 HIS   A N     1 
ATOM   1970 C  CA    . HIS   A 1 272 ? 48.939  3.332   -28.924 1.00 50.86  ?  272 HIS   A CA    1 
ATOM   1971 C  C     . HIS   A 1 272 ? 48.450  2.932   -27.542 1.00 51.33  ?  272 HIS   A C     1 
ATOM   1972 O  O     . HIS   A 1 272 ? 47.961  1.817   -27.354 1.00 50.00  ?  272 HIS   A O     1 
ATOM   1973 C  CB    . HIS   A 1 272 ? 50.477  3.230   -28.882 1.00 50.80  ?  272 HIS   A CB    1 
ATOM   1974 C  CG    . HIS   A 1 272 ? 51.162  3.870   -30.046 1.00 54.00  ?  272 HIS   A CG    1 
ATOM   1975 N  ND1   . HIS   A 1 272 ? 51.182  3.320   -31.311 1.00 56.28  ?  272 HIS   A ND1   1 
ATOM   1976 C  CD2   . HIS   A 1 272 ? 51.836  5.040   -30.135 1.00 54.86  ?  272 HIS   A CD2   1 
ATOM   1977 C  CE1   . HIS   A 1 272 ? 51.858  4.119   -32.128 1.00 57.50  ?  272 HIS   A CE1   1 
ATOM   1978 N  NE2   . HIS   A 1 272 ? 52.257  5.180   -31.442 1.00 56.52  ?  272 HIS   A NE2   1 
ATOM   1979 N  N     . LEU   A 1 273 ? 48.622  3.838   -26.576 1.00 48.99  ?  273 LEU   A N     1 
ATOM   1980 C  CA    . LEU   A 1 273 ? 48.179  3.570   -25.209 1.00 49.56  ?  273 LEU   A CA    1 
ATOM   1981 C  C     . LEU   A 1 273 ? 46.682  3.254   -25.196 1.00 47.84  ?  273 LEU   A C     1 
ATOM   1982 O  O     . LEU   A 1 273 ? 46.264  2.205   -24.680 1.00 41.99  ?  273 LEU   A O     1 
ATOM   1983 C  CB    . LEU   A 1 273 ? 48.457  4.776   -24.311 1.00 47.22  ?  273 LEU   A CB    1 
ATOM   1984 C  CG    . LEU   A 1 273 ? 47.928  4.687   -22.869 1.00 44.84  ?  273 LEU   A CG    1 
ATOM   1985 C  CD1   . LEU   A 1 273 ? 48.392  3.406   -22.187 1.00 42.01  ?  273 LEU   A CD1   1 
ATOM   1986 C  CD2   . LEU   A 1 273 ? 48.361  5.918   -22.106 1.00 42.69  ?  273 LEU   A CD2   1 
ATOM   1987 N  N     . LYS   A 1 274 ? 45.907  4.171   -25.793 1.00 45.39  ?  274 LYS   A N     1 
ATOM   1988 C  CA    . LYS   A 1 274 ? 44.438  4.062   -25.844 1.00 46.76  ?  274 LYS   A CA    1 
ATOM   1989 C  C     . LYS   A 1 274 ? 43.992  2.730   -26.447 1.00 47.28  ?  274 LYS   A C     1 
ATOM   1990 O  O     . LYS   A 1 274 ? 43.071  2.106   -25.941 1.00 46.21  ?  274 LYS   A O     1 
ATOM   1991 C  CB    . LYS   A 1 274 ? 43.830  5.226   -26.640 1.00 46.52  ?  274 LYS   A CB    1 
ATOM   1992 C  CG    . LYS   A 1 274 ? 43.753  6.527   -25.854 1.00 45.86  ?  274 LYS   A CG    1 
ATOM   1993 C  CD    . LYS   A 1 274 ? 43.294  7.686   -26.721 1.00 45.36  ?  274 LYS   A CD    1 
ATOM   1994 C  CE    . LYS   A 1 274 ? 42.944  8.902   -25.876 1.00 45.59  ?  274 LYS   A CE    1 
ATOM   1995 N  NZ    . LYS   A 1 274 ? 42.698  10.103  -26.726 1.00 46.04  ?  274 LYS   A NZ    1 
ATOM   1996 N  N     . GLY   A 1 275 ? 44.670  2.310   -27.517 1.00 53.96  ?  275 GLY   A N     1 
ATOM   1997 C  CA    . GLY   A 1 275 ? 44.381  1.056   -28.210 1.00 53.08  ?  275 GLY   A CA    1 
ATOM   1998 C  C     . GLY   A 1 275 ? 44.612  -0.159  -27.348 1.00 55.13  ?  275 GLY   A C     1 
ATOM   1999 O  O     . GLY   A 1 275 ? 43.835  -1.106  -27.389 1.00 57.62  ?  275 GLY   A O     1 
ATOM   2000 N  N     . GLU   A 1 276 ? 45.677  -0.113  -26.555 1.00 55.09  ?  276 GLU   A N     1 
ATOM   2001 C  CA    . GLU   A 1 276 ? 46.060  -1.206  -25.674 1.00 57.97  ?  276 GLU   A CA    1 
ATOM   2002 C  C     . GLU   A 1 276 ? 45.154  -1.301  -24.443 1.00 51.09  ?  276 GLU   A C     1 
ATOM   2003 O  O     . GLU   A 1 276 ? 44.882  -2.383  -23.935 1.00 51.02  ?  276 GLU   A O     1 
ATOM   2004 C  CB    . GLU   A 1 276 ? 47.504  -0.995  -25.202 1.00 59.66  ?  276 GLU   A CB    1 
ATOM   2005 C  CG    . GLU   A 1 276 ? 48.087  -2.194  -24.491 1.00 65.71  ?  276 GLU   A CG    1 
ATOM   2006 C  CD    . GLU   A 1 276 ? 47.905  -3.446  -25.313 1.00 69.48  ?  276 GLU   A CD    1 
ATOM   2007 O  OE1   . GLU   A 1 276 ? 48.444  -3.482  -26.454 1.00 75.73  ?  276 GLU   A OE1   1 
ATOM   2008 O  OE2   . GLU   A 1 276 ? 47.184  -4.356  -24.837 1.00 70.81  ?  276 GLU   A OE2   1 
ATOM   2009 N  N     . VAL   A 1 277 ? 44.754  -0.143  -23.938 1.00 46.90  ?  277 VAL   A N     1 
ATOM   2010 C  CA    . VAL   A 1 277 ? 43.850  -0.060  -22.799 1.00 42.54  ?  277 VAL   A CA    1 
ATOM   2011 C  C     . VAL   A 1 277 ? 42.513  -0.702  -23.176 1.00 39.63  ?  277 VAL   A C     1 
ATOM   2012 O  O     . VAL   A 1 277 ? 42.008  -1.502  -22.429 1.00 41.13  ?  277 VAL   A O     1 
ATOM   2013 C  CB    . VAL   A 1 277 ? 43.650  1.400   -22.342 1.00 39.96  ?  277 VAL   A CB    1 
ATOM   2014 C  CG1   . VAL   A 1 277 ? 42.488  1.528   -21.342 1.00 39.56  ?  277 VAL   A CG1   1 
ATOM   2015 C  CG2   . VAL   A 1 277 ? 44.919  1.936   -21.702 1.00 39.92  ?  277 VAL   A CG2   1 
ATOM   2016 N  N     . ALA   A 1 278 ? 41.961  -0.334  -24.334 1.00 41.31  ?  278 ALA   A N     1 
ATOM   2017 C  CA    . ALA   A 1 278 ? 40.669  -0.863  -24.817 1.00 45.53  ?  278 ALA   A CA    1 
ATOM   2018 C  C     . ALA   A 1 278 ? 40.699  -2.382  -25.020 1.00 47.11  ?  278 ALA   A C     1 
ATOM   2019 O  O     . ALA   A 1 278 ? 39.735  -3.063  -24.683 1.00 49.11  ?  278 ALA   A O     1 
ATOM   2020 C  CB    . ALA   A 1 278 ? 40.258  -0.161  -26.104 1.00 46.11  ?  278 ALA   A CB    1 
ATOM   2021 N  N     . ASP   A 1 279 ? 41.821  -2.894  -25.534 1.00 49.48  ?  279 ASP   A N     1 
ATOM   2022 C  CA    . ASP   A 1 279 ? 42.045  -4.344  -25.697 1.00 54.61  ?  279 ASP   A CA    1 
ATOM   2023 C  C     . ASP   A 1 279 ? 42.087  -5.063  -24.344 1.00 53.22  ?  279 ASP   A C     1 
ATOM   2024 O  O     . ASP   A 1 279 ? 41.471  -6.109  -24.167 1.00 52.12  ?  279 ASP   A O     1 
ATOM   2025 C  CB    . ASP   A 1 279 ? 43.374  -4.629  -26.430 1.00 57.13  ?  279 ASP   A CB    1 
ATOM   2026 C  CG    . ASP   A 1 279 ? 43.372  -4.199  -27.906 1.00 63.10  ?  279 ASP   A CG    1 
ATOM   2027 O  OD1   . ASP   A 1 279 ? 42.297  -3.941  -28.496 1.00 62.32  ?  279 ASP   A OD1   1 
ATOM   2028 O  OD2   . ASP   A 1 279 ? 44.484  -4.128  -28.476 1.00 62.75  ?  279 ASP   A OD2   1 
ATOM   2029 N  N     . ALA   A 1 280 ? 42.858  -4.513  -23.407 1.00 47.85  ?  280 ALA   A N     1 
ATOM   2030 C  CA    . ALA   A 1 280 ? 42.988  -5.087  -22.069 1.00 48.19  ?  280 ALA   A CA    1 
ATOM   2031 C  C     . ALA   A 1 280 ? 41.633  -5.152  -21.342 1.00 43.99  ?  280 ALA   A C     1 
ATOM   2032 O  O     . ALA   A 1 280 ? 41.240  -6.217  -20.873 1.00 42.22  ?  280 ALA   A O     1 
ATOM   2033 C  CB    . ALA   A 1 280 ? 43.992  -4.293  -21.258 1.00 49.00  ?  280 ALA   A CB    1 
ATOM   2034 N  N     . VAL   A 1 281 ? 40.922  -4.023  -21.302 1.00 43.90  ?  281 VAL   A N     1 
ATOM   2035 C  CA    . VAL   A 1 281 ? 39.614  -3.914  -20.619 1.00 44.52  ?  281 VAL   A CA    1 
ATOM   2036 C  C     . VAL   A 1 281 ? 38.598  -4.884  -21.231 1.00 48.53  ?  281 VAL   A C     1 
ATOM   2037 O  O     . VAL   A 1 281 ? 38.051  -5.723  -20.525 1.00 50.00  ?  281 VAL   A O     1 
ATOM   2038 C  CB    . VAL   A 1 281 ? 39.072  -2.461  -20.643 1.00 45.17  ?  281 VAL   A CB    1 
ATOM   2039 C  CG1   . VAL   A 1 281 ? 37.603  -2.374  -20.205 1.00 44.65  ?  281 VAL   A CG1   1 
ATOM   2040 C  CG2   . VAL   A 1 281 ? 39.918  -1.555  -19.754 1.00 43.01  ?  281 VAL   A CG2   1 
ATOM   2041 N  N     . SER   A 1 282 ? 38.393  -4.785  -22.548 1.00 52.50  ?  282 SER   A N     1 
ATOM   2042 C  CA    . SER   A 1 282 ? 37.469  -5.667  -23.292 1.00 52.28  ?  282 SER   A CA    1 
ATOM   2043 C  C     . SER   A 1 282 ? 37.855  -7.132  -23.162 1.00 49.81  ?  282 SER   A C     1 
ATOM   2044 O  O     . SER   A 1 282 ? 36.988  -7.989  -23.147 1.00 56.88  ?  282 SER   A O     1 
ATOM   2045 C  CB    . SER   A 1 282 ? 37.383  -5.264  -24.767 1.00 54.44  ?  282 SER   A CB    1 
ATOM   2046 O  OG    . SER   A 1 282 ? 36.916  -3.930  -24.921 1.00 54.45  ?  282 SER   A OG    1 
ATOM   2047 N  N     . GLY   A 1 283 ? 39.151  -7.400  -23.031 1.00 51.38  ?  283 GLY   A N     1 
ATOM   2048 C  CA    . GLY   A 1 283 ? 39.660  -8.737  -22.691 1.00 51.99  ?  283 GLY   A CA    1 
ATOM   2049 C  C     . GLY   A 1 283 ? 39.203  -9.243  -21.320 1.00 56.53  ?  283 GLY   A C     1 
ATOM   2050 O  O     . GLY   A 1 283 ? 38.960  -10.445 -21.135 1.00 55.97  ?  283 GLY   A O     1 
ATOM   2051 N  N     . MET   A 1 284 ? 39.106  -8.326  -20.353 1.00 55.11  ?  284 MET   A N     1 
ATOM   2052 C  CA    . MET   A 1 284 ? 38.687  -8.646  -18.975 1.00 51.04  ?  284 MET   A CA    1 
ATOM   2053 C  C     . MET   A 1 284 ? 37.170  -8.816  -18.888 1.00 48.65  ?  284 MET   A C     1 
ATOM   2054 O  O     . MET   A 1 284 ? 36.679  -9.788  -18.323 1.00 48.97  ?  284 MET   A O     1 
ATOM   2055 C  CB    . MET   A 1 284 ? 39.152  -7.548  -18.008 1.00 48.00  ?  284 MET   A CB    1 
ATOM   2056 C  CG    . MET   A 1 284 ? 38.805  -7.793  -16.541 1.00 45.22  ?  284 MET   A CG    1 
ATOM   2057 S  SD    . MET   A 1 284 ? 39.391  -6.459  -15.495 1.00 40.53  ?  284 MET   A SD    1 
ATOM   2058 C  CE    . MET   A 1 284 ? 38.406  -5.096  -16.105 1.00 35.79  ?  284 MET   A CE    1 
ATOM   2059 N  N     . LEU   A 1 285 ? 36.442  -7.879  -19.486 1.00 50.09  ?  285 LEU   A N     1 
ATOM   2060 C  CA    . LEU   A 1 285 ? 34.979  -7.894  -19.477 1.00 51.21  ?  285 LEU   A CA    1 
ATOM   2061 C  C     . LEU   A 1 285 ? 34.375  -9.141  -20.145 1.00 59.52  ?  285 LEU   A C     1 
ATOM   2062 O  O     . LEU   A 1 285 ? 33.245  -9.539  -19.832 1.00 65.67  ?  285 LEU   A O     1 
ATOM   2063 C  CB    . LEU   A 1 285 ? 34.437  -6.633  -20.162 1.00 46.77  ?  285 LEU   A CB    1 
ATOM   2064 C  CG    . LEU   A 1 285 ? 34.849  -5.296  -19.555 1.00 45.17  ?  285 LEU   A CG    1 
ATOM   2065 C  CD1   . LEU   A 1 285 ? 34.304  -4.152  -20.394 1.00 47.21  ?  285 LEU   A CD1   1 
ATOM   2066 C  CD2   . LEU   A 1 285 ? 34.392  -5.159  -18.109 1.00 46.64  ?  285 LEU   A CD2   1 
ATOM   2067 N  N     . THR   A 1 286 ? 35.128  -9.767  -21.050 1.00 67.61  ?  286 THR   A N     1 
ATOM   2068 C  CA    . THR   A 1 286 ? 34.625  -10.899 -21.841 1.00 68.84  ?  286 THR   A CA    1 
ATOM   2069 C  C     . THR   A 1 286 ? 34.305  -12.154 -21.019 1.00 63.34  ?  286 THR   A C     1 
ATOM   2070 O  O     . THR   A 1 286 ? 33.246  -12.740 -21.210 1.00 62.90  ?  286 THR   A O     1 
ATOM   2071 C  CB    . THR   A 1 286 ? 35.592  -11.228 -22.996 1.00 69.19  ?  286 THR   A CB    1 
ATOM   2072 O  OG1   . THR   A 1 286 ? 35.581  -10.131 -23.924 1.00 64.76  ?  286 THR   A OG1   1 
ATOM   2073 C  CG2   . THR   A 1 286 ? 35.182  -12.514 -23.746 1.00 69.73  ?  286 THR   A CG2   1 
ATOM   2074 N  N     . GLU   A 1 287 ? 35.209  -12.581 -20.143 1.00 59.50  ?  287 GLU   A N     1 
ATOM   2075 C  CA    . GLU   A 1 287 ? 34.928  -13.761 -19.296 1.00 63.08  ?  287 GLU   A CA    1 
ATOM   2076 C  C     . GLU   A 1 287 ? 33.876  -13.444 -18.217 1.00 59.85  ?  287 GLU   A C     1 
ATOM   2077 O  O     . GLU   A 1 287 ? 33.112  -14.317 -17.809 1.00 61.52  ?  287 GLU   A O     1 
ATOM   2078 C  CB    . GLU   A 1 287 ? 36.200  -14.320 -18.651 1.00 61.82  ?  287 GLU   A CB    1 
ATOM   2079 C  CG    . GLU   A 1 287 ? 36.015  -15.640 -17.892 1.00 62.03  ?  287 GLU   A CG    1 
ATOM   2080 C  CD    . GLU   A 1 287 ? 35.178  -16.666 -18.643 1.00 62.34  ?  287 GLU   A CD    1 
ATOM   2081 N  N     . LEU   A 1 288 ? 33.850  -12.189 -17.768 1.00 57.65  ?  288 LEU   A N     1 
ATOM   2082 C  CA    . LEU   A 1 288 ? 32.796  -11.677 -16.882 1.00 53.22  ?  288 LEU   A CA    1 
ATOM   2083 C  C     . LEU   A 1 288 ? 31.431  -11.746 -17.577 1.00 54.09  ?  288 LEU   A C     1 
ATOM   2084 O  O     . LEU   A 1 288 ? 30.495  -12.339 -17.036 1.00 53.93  ?  288 LEU   A O     1 
ATOM   2085 C  CB    . LEU   A 1 288 ? 33.088  -10.230 -16.446 1.00 48.73  ?  288 LEU   A CB    1 
ATOM   2086 C  CG    . LEU   A 1 288 ? 34.064  -10.101 -15.273 1.00 49.07  ?  288 LEU   A CG    1 
ATOM   2087 C  CD1   . LEU   A 1 288 ? 34.666  -8.712  -15.208 1.00 50.47  ?  288 LEU   A CD1   1 
ATOM   2088 C  CD2   . LEU   A 1 288 ? 33.365  -10.405 -13.966 1.00 50.65  ?  288 LEU   A CD2   1 
ATOM   2089 N  N     . GLN   A 1 289 ? 31.351  -11.139 -18.763 1.00 51.16  ?  289 GLN   A N     1 
ATOM   2090 C  CA    . GLN   A 1 289 ? 30.130  -11.105 -19.577 1.00 55.85  ?  289 GLN   A CA    1 
ATOM   2091 C  C     . GLN   A 1 289 ? 29.658  -12.524 -19.928 1.00 60.33  ?  289 GLN   A C     1 
ATOM   2092 O  O     . GLN   A 1 289 ? 28.464  -12.811 -19.883 1.00 60.24  ?  289 GLN   A O     1 
ATOM   2093 C  CB    . GLN   A 1 289 ? 30.326  -10.263 -20.849 1.00 55.62  ?  289 GLN   A CB    1 
ATOM   2094 C  CG    . GLN   A 1 289 ? 30.180  -8.755  -20.613 1.00 56.75  ?  289 GLN   A CG    1 
ATOM   2095 C  CD    . GLN   A 1 289 ? 30.776  -7.888  -21.727 1.00 54.90  ?  289 GLN   A CD    1 
ATOM   2096 O  OE1   . GLN   A 1 289 ? 31.021  -8.355  -22.834 1.00 57.42  ?  289 GLN   A OE1   1 
ATOM   2097 N  NE2   . GLN   A 1 289 ? 31.006  -6.611  -21.431 1.00 51.72  ?  289 GLN   A NE2   1 
ATOM   2098 N  N     . GLU   A 1 290 ? 30.601  -13.417 -20.221 1.00 62.15  ?  290 GLU   A N     1 
ATOM   2099 C  CA    . GLU   A 1 290 ? 30.289  -14.820 -20.505 1.00 65.97  ?  290 GLU   A CA    1 
ATOM   2100 C  C     . GLU   A 1 290 ? 29.545  -15.456 -19.337 1.00 65.88  ?  290 GLU   A C     1 
ATOM   2101 O  O     . GLU   A 1 290 ? 28.461  -15.996 -19.521 1.00 72.03  ?  290 GLU   A O     1 
ATOM   2102 C  CB    . GLU   A 1 290 ? 31.564  -15.614 -20.806 1.00 72.11  ?  290 GLU   A CB    1 
ATOM   2103 C  CG    . GLU   A 1 290 ? 31.326  -16.997 -21.419 1.00 75.79  ?  290 GLU   A CG    1 
ATOM   2104 C  CD    . GLU   A 1 290 ? 31.107  -18.094 -20.393 1.00 77.29  ?  290 GLU   A CD    1 
ATOM   2105 O  OE1   . GLU   A 1 290 ? 31.887  -18.176 -19.424 1.00 78.57  ?  290 GLU   A OE1   1 
ATOM   2106 O  OE2   . GLU   A 1 290 ? 30.150  -18.889 -20.532 1.00 83.08  ?  290 GLU   A OE2   1 
ATOM   2107 N  N     . ARG   A 1 291 ? 30.129  -15.382 -18.140 1.00 60.35  ?  291 ARG   A N     1 
ATOM   2108 C  CA    . ARG   A 1 291 ? 29.491  -15.918 -16.924 1.00 57.63  ?  291 ARG   A CA    1 
ATOM   2109 C  C     . ARG   A 1 291 ? 28.158  -15.224 -16.597 1.00 49.17  ?  291 ARG   A C     1 
ATOM   2110 O  O     . ARG   A 1 291 ? 27.193  -15.896 -16.234 1.00 49.39  ?  291 ARG   A O     1 
ATOM   2111 C  CB    . ARG   A 1 291 ? 30.449  -15.832 -15.735 1.00 58.76  ?  291 ARG   A CB    1 
ATOM   2112 C  CG    . ARG   A 1 291 ? 31.583  -16.849 -15.786 1.00 59.02  ?  291 ARG   A CG    1 
ATOM   2113 C  CD    . ARG   A 1 291 ? 32.817  -16.359 -15.053 1.00 54.59  ?  291 ARG   A CD    1 
ATOM   2114 N  NE    . ARG   A 1 291 ? 32.496  -15.869 -13.718 1.00 52.84  ?  291 ARG   A NE    1 
ATOM   2115 C  CZ    . ARG   A 1 291 ? 32.192  -16.636 -12.667 1.00 52.14  ?  291 ARG   A CZ    1 
ATOM   2116 N  NH1   . ARG   A 1 291 ? 32.133  -17.968 -12.762 1.00 52.82  ?  291 ARG   A NH1   1 
ATOM   2117 N  NH2   . ARG   A 1 291 ? 31.939  -16.070 -11.502 1.00 47.82  ?  291 ARG   A NH2   1 
ATOM   2118 N  N     . TYR   A 1 292 ? 28.114  -13.898 -16.770 1.00 45.79  ?  292 TYR   A N     1 
ATOM   2119 C  CA    . TYR   A 1 292 ? 26.914  -13.095 -16.506 1.00 46.29  ?  292 TYR   A CA    1 
ATOM   2120 C  C     . TYR   A 1 292 ? 25.703  -13.609 -17.280 1.00 48.79  ?  292 TYR   A C     1 
ATOM   2121 O  O     . TYR   A 1 292 ? 24.762  -14.096 -16.661 1.00 52.74  ?  292 TYR   A O     1 
ATOM   2122 C  CB    . TYR   A 1 292 ? 27.142  -11.600 -16.806 1.00 47.22  ?  292 TYR   A CB    1 
ATOM   2123 C  CG    . TYR   A 1 292 ? 25.870  -10.797 -16.731 1.00 46.40  ?  292 TYR   A CG    1 
ATOM   2124 C  CD1   . TYR   A 1 292 ? 25.295  -10.501 -15.497 1.00 48.72  ?  292 TYR   A CD1   1 
ATOM   2125 C  CD2   . TYR   A 1 292 ? 25.208  -10.381 -17.880 1.00 46.22  ?  292 TYR   A CD2   1 
ATOM   2126 C  CE1   . TYR   A 1 292 ? 24.103  -9.793  -15.411 1.00 48.46  ?  292 TYR   A CE1   1 
ATOM   2127 C  CE2   . TYR   A 1 292 ? 24.016  -9.670  -17.803 1.00 48.74  ?  292 TYR   A CE2   1 
ATOM   2128 C  CZ    . TYR   A 1 292 ? 23.459  -9.388  -16.560 1.00 47.29  ?  292 TYR   A CZ    1 
ATOM   2129 O  OH    . TYR   A 1 292 ? 22.276  -8.691  -16.446 1.00 44.55  ?  292 TYR   A OH    1 
ATOM   2130 N  N     . HIS   A 1 293 ? 25.759  -13.532 -18.616 1.00 48.48  ?  293 HIS   A N     1 
ATOM   2131 C  CA    . HIS   A 1 293 ? 24.674  -13.984 -19.513 1.00 51.83  ?  293 HIS   A CA    1 
ATOM   2132 C  C     . HIS   A 1 293 ? 24.292  -15.449 -19.275 1.00 55.44  ?  293 HIS   A C     1 
ATOM   2133 O  O     . HIS   A 1 293 ? 23.119  -15.801 -19.365 1.00 60.82  ?  293 HIS   A O     1 
ATOM   2134 C  CB    . HIS   A 1 293 ? 25.043  -13.796 -20.990 1.00 51.56  ?  293 HIS   A CB    1 
ATOM   2135 C  CG    . HIS   A 1 293 ? 25.172  -12.364 -21.406 1.00 52.21  ?  293 HIS   A CG    1 
ATOM   2136 N  ND1   . HIS   A 1 293 ? 24.123  -11.474 -21.346 1.00 55.82  ?  293 HIS   A ND1   1 
ATOM   2137 C  CD2   . HIS   A 1 293 ? 26.225  -11.668 -21.890 1.00 51.99  ?  293 HIS   A CD2   1 
ATOM   2138 C  CE1   . HIS   A 1 293 ? 24.526  -10.288 -21.764 1.00 55.91  ?  293 HIS   A CE1   1 
ATOM   2139 N  NE2   . HIS   A 1 293 ? 25.799  -10.379 -22.098 1.00 55.13  ?  293 HIS   A NE2   1 
ATOM   2140 N  N     . ARG   A 1 294 ? 25.276  -16.284 -18.952 1.00 53.26  ?  294 ARG   A N     1 
ATOM   2141 C  CA    . ARG   A 1 294 ? 25.038  -17.677 -18.601 1.00 57.05  ?  294 ARG   A CA    1 
ATOM   2142 C  C     . ARG   A 1 294 ? 24.263  -17.811 -17.291 1.00 60.40  ?  294 ARG   A C     1 
ATOM   2143 O  O     . ARG   A 1 294 ? 23.320  -18.612 -17.206 1.00 64.37  ?  294 ARG   A O     1 
ATOM   2144 C  CB    . ARG   A 1 294 ? 26.369  -18.427 -18.506 1.00 60.44  ?  294 ARG   A CB    1 
ATOM   2145 C  CG    . ARG   A 1 294 ? 26.268  -19.867 -18.019 1.00 65.11  ?  294 ARG   A CG    1 
ATOM   2146 C  CD    . ARG   A 1 294 ? 27.414  -20.709 -18.558 1.00 70.84  ?  294 ARG   A CD    1 
ATOM   2147 N  NE    . ARG   A 1 294 ? 28.713  -20.030 -18.455 1.00 71.48  ?  294 ARG   A NE    1 
ATOM   2148 C  CZ    . ARG   A 1 294 ? 29.569  -20.142 -17.437 1.00 73.07  ?  294 ARG   A CZ    1 
ATOM   2149 N  NH1   . ARG   A 1 294 ? 29.305  -20.919 -16.388 1.00 76.18  ?  294 ARG   A NH1   1 
ATOM   2150 N  NH2   . ARG   A 1 294 ? 30.715  -19.471 -17.462 1.00 72.38  ?  294 ARG   A NH2   1 
ATOM   2151 N  N     . PHE   A 1 295 ? 24.667  -17.051 -16.268 1.00 53.78  ?  295 PHE   A N     1 
ATOM   2152 C  CA    . PHE   A 1 295 ? 23.945  -17.053 -14.985 1.00 50.18  ?  295 PHE   A CA    1 
ATOM   2153 C  C     . PHE   A 1 295 ? 22.588  -16.344 -15.095 1.00 45.12  ?  295 PHE   A C     1 
ATOM   2154 O  O     . PHE   A 1 295 ? 21.593  -16.814 -14.564 1.00 41.80  ?  295 PHE   A O     1 
ATOM   2155 C  CB    . PHE   A 1 295 ? 24.772  -16.384 -13.874 1.00 49.48  ?  295 PHE   A CB    1 
ATOM   2156 C  CG    . PHE   A 1 295 ? 25.986  -17.168 -13.415 1.00 48.51  ?  295 PHE   A CG    1 
ATOM   2157 C  CD1   . PHE   A 1 295 ? 25.986  -18.564 -13.352 1.00 53.42  ?  295 PHE   A CD1   1 
ATOM   2158 C  CD2   . PHE   A 1 295 ? 27.129  -16.489 -12.986 1.00 44.18  ?  295 PHE   A CD2   1 
ATOM   2159 C  CE1   . PHE   A 1 295 ? 27.110  -19.254 -12.910 1.00 51.61  ?  295 PHE   A CE1   1 
ATOM   2160 C  CE2   . PHE   A 1 295 ? 28.242  -17.170 -12.546 1.00 42.99  ?  295 PHE   A CE2   1 
ATOM   2161 C  CZ    . PHE   A 1 295 ? 28.240  -18.555 -12.507 1.00 47.07  ?  295 PHE   A CZ    1 
ATOM   2162 N  N     . ARG   A 1 296 ? 22.574  -15.201 -15.775 1.00 46.41  ?  296 ARG   A N     1 
ATOM   2163 C  CA    . ARG   A 1 296 ? 21.391  -14.361 -15.884 1.00 46.57  ?  296 ARG   A CA    1 
ATOM   2164 C  C     . ARG   A 1 296 ? 20.227  -15.048 -16.577 1.00 53.18  ?  296 ARG   A C     1 
ATOM   2165 O  O     . ARG   A 1 296 ? 19.082  -14.826 -16.206 1.00 49.45  ?  296 ARG   A O     1 
ATOM   2166 C  CB    . ARG   A 1 296 ? 21.709  -13.068 -16.634 1.00 45.87  ?  296 ARG   A CB    1 
ATOM   2167 C  CG    . ARG   A 1 296 ? 20.561  -12.047 -16.670 1.00 44.75  ?  296 ARG   A CG    1 
ATOM   2168 C  CD    . ARG   A 1 296 ? 20.072  -11.667 -15.257 1.00 42.89  ?  296 ARG   A CD    1 
ATOM   2169 N  NE    . ARG   A 1 296 ? 18.951  -10.735 -15.310 1.00 42.81  ?  296 ARG   A NE    1 
ATOM   2170 C  CZ    . ARG   A 1 296 ? 17.666  -11.079 -15.424 1.00 41.54  ?  296 ARG   A CZ    1 
ATOM   2171 N  NH1   . ARG   A 1 296 ? 17.293  -12.359 -15.494 1.00 43.21  ?  296 ARG   A NH1   1 
ATOM   2172 N  NH2   . ARG   A 1 296 ? 16.748  -10.130 -15.472 1.00 37.54  ?  296 ARG   A NH2   1 
ATOM   2173 N  N     . ASN   A 1 297 ? 20.542  -15.867 -17.584 1.00 61.23  ?  297 ASN   A N     1 
ATOM   2174 C  CA    . ASN   A 1 297 ? 19.536  -16.566 -18.404 1.00 68.35  ?  297 ASN   A CA    1 
ATOM   2175 C  C     . ASN   A 1 297 ? 19.248  -17.987 -17.893 1.00 65.27  ?  297 ASN   A C     1 
ATOM   2176 O  O     . ASN   A 1 297 ? 18.832  -18.846 -18.658 1.00 74.41  ?  297 ASN   A O     1 
ATOM   2177 C  CB    . ASN   A 1 297 ? 19.976  -16.593 -19.886 1.00 69.01  ?  297 ASN   A CB    1 
ATOM   2178 C  CG    . ASN   A 1 297 ? 20.229  -15.196 -20.456 1.00 71.31  ?  297 ASN   A CG    1 
ATOM   2179 O  OD1   . ASN   A 1 297 ? 19.691  -14.196 -19.980 1.00 74.06  ?  297 ASN   A OD1   1 
ATOM   2180 N  ND2   . ASN   A 1 297 ? 21.054  -15.129 -21.482 1.00 76.92  ?  297 ASN   A ND2   1 
ATOM   2181 N  N     . ASP   A 1 298 ? 19.467  -18.214 -16.598 1.00 60.46  ?  298 ASP   A N     1 
ATOM   2182 C  CA    . ASP   A 1 298 ? 19.174  -19.478 -15.932 1.00 57.88  ?  298 ASP   A CA    1 
ATOM   2183 C  C     . ASP   A 1 298 ? 18.359  -19.167 -14.669 1.00 59.20  ?  298 ASP   A C     1 
ATOM   2184 O  O     . ASP   A 1 298 ? 18.929  -18.972 -13.578 1.00 54.53  ?  298 ASP   A O     1 
ATOM   2185 C  CB    . ASP   A 1 298 ? 20.487  -20.201 -15.607 1.00 56.50  ?  298 ASP   A CB    1 
ATOM   2186 C  CG    . ASP   A 1 298 ? 20.283  -21.584 -15.000 1.00 57.07  ?  298 ASP   A CG    1 
ATOM   2187 O  OD1   . ASP   A 1 298 ? 19.127  -21.964 -14.735 1.00 58.55  ?  298 ASP   A OD1   1 
ATOM   2188 O  OD2   . ASP   A 1 298 ? 21.295  -22.279 -14.758 1.00 52.97  ?  298 ASP   A OD2   1 
ATOM   2189 N  N     . GLU   A 1 299 ? 17.033  -19.129 -14.832 1.00 51.95  ?  299 GLU   A N     1 
ATOM   2190 C  CA    . GLU   A 1 299 ? 16.110  -18.768 -13.747 1.00 55.72  ?  299 GLU   A CA    1 
ATOM   2191 C  C     . GLU   A 1 299 ? 16.228  -19.670 -12.510 1.00 55.77  ?  299 GLU   A C     1 
ATOM   2192 O  O     . GLU   A 1 299 ? 16.274  -19.176 -11.378 1.00 57.39  ?  299 GLU   A O     1 
ATOM   2193 C  CB    . GLU   A 1 299 ? 14.654  -18.729 -14.242 1.00 56.77  ?  299 GLU   A CB    1 
ATOM   2194 C  CG    . GLU   A 1 299 ? 13.589  -19.052 -13.190 1.00 60.17  ?  299 GLU   A CG    1 
ATOM   2195 C  CD    . GLU   A 1 299 ? 12.195  -19.174 -13.787 1.00 61.32  ?  299 GLU   A CD    1 
ATOM   2196 O  OE1   . GLU   A 1 299 ? 11.379  -19.925 -13.208 1.00 68.05  ?  299 GLU   A OE1   1 
ATOM   2197 N  N     . ALA   A 1 300 ? 16.256  -20.981 -12.735 1.00 53.07  ?  300 ALA   A N     1 
ATOM   2198 C  CA    . ALA   A 1 300 ? 16.238  -21.949 -11.653 1.00 51.12  ?  300 ALA   A CA    1 
ATOM   2199 C  C     . ALA   A 1 300 ? 17.490  -21.860 -10.781 1.00 48.35  ?  300 ALA   A C     1 
ATOM   2200 O  O     . ALA   A 1 300 ? 17.397  -21.958 -9.558  1.00 51.96  ?  300 ALA   A O     1 
ATOM   2201 C  CB    . ALA   A 1 300 ? 16.066  -23.352 -12.199 1.00 52.79  ?  300 ALA   A CB    1 
ATOM   2202 N  N     . PHE   A 1 301 ? 18.651  -21.671 -11.410 1.00 43.39  ?  301 PHE   A N     1 
ATOM   2203 C  CA    . PHE   A 1 301 ? 19.893  -21.363 -10.675 1.00 43.33  ?  301 PHE   A CA    1 
ATOM   2204 C  C     . PHE   A 1 301 ? 19.740  -20.092 -9.797  1.00 41.89  ?  301 PHE   A C     1 
ATOM   2205 O  O     . PHE   A 1 301 ? 19.966  -20.139 -8.588  1.00 44.73  ?  301 PHE   A O     1 
ATOM   2206 C  CB    . PHE   A 1 301 ? 21.067  -21.222 -11.637 1.00 45.37  ?  301 PHE   A CB    1 
ATOM   2207 C  CG    . PHE   A 1 301 ? 22.342  -20.720 -10.992 1.00 43.96  ?  301 PHE   A CG    1 
ATOM   2208 C  CD1   . PHE   A 1 301 ? 23.057  -21.513 -10.102 1.00 43.29  ?  301 PHE   A CD1   1 
ATOM   2209 C  CD2   . PHE   A 1 301 ? 22.827  -19.447 -11.289 1.00 44.99  ?  301 PHE   A CD2   1 
ATOM   2210 C  CE1   . PHE   A 1 301 ? 24.234  -21.044 -9.516  1.00 42.30  ?  301 PHE   A CE1   1 
ATOM   2211 C  CE2   . PHE   A 1 301 ? 24.000  -18.979 -10.716 1.00 44.48  ?  301 PHE   A CE2   1 
ATOM   2212 C  CZ    . PHE   A 1 301 ? 24.704  -19.781 -9.832  1.00 45.89  ?  301 PHE   A CZ    1 
ATOM   2213 N  N     . LEU   A 1 302 ? 19.305  -18.990 -10.406 1.00 41.18  ?  302 LEU   A N     1 
ATOM   2214 C  CA    . LEU   A 1 302 ? 19.091  -17.742 -9.701  1.00 38.01  ?  302 LEU   A CA    1 
ATOM   2215 C  C     . LEU   A 1 302 ? 18.096  -17.889 -8.552  1.00 41.98  ?  302 LEU   A C     1 
ATOM   2216 O  O     . LEU   A 1 302 ? 18.380  -17.423 -7.437  1.00 32.78  ?  302 LEU   A O     1 
ATOM   2217 C  CB    . LEU   A 1 302 ? 18.627  -16.662 -10.660 1.00 37.85  ?  302 LEU   A CB    1 
ATOM   2218 C  CG    . LEU   A 1 302 ? 19.633  -16.199 -11.707 1.00 35.72  ?  302 LEU   A CG    1 
ATOM   2219 C  CD1   . LEU   A 1 302 ? 19.098  -14.992 -12.458 1.00 34.99  ?  302 LEU   A CD1   1 
ATOM   2220 C  CD2   . LEU   A 1 302 ? 20.988  -15.882 -11.087 1.00 36.82  ?  302 LEU   A CD2   1 
ATOM   2221 N  N     . GLN   A 1 303 ? 16.969  -18.572 -8.818  1.00 42.58  ?  303 GLN   A N     1 
ATOM   2222 C  CA    . GLN   A 1 303 ? 15.953  -18.872 -7.816  1.00 40.01  ?  303 GLN   A CA    1 
ATOM   2223 C  C     . GLN   A 1 303 ? 16.499  -19.740 -6.678  1.00 40.87  ?  303 GLN   A C     1 
ATOM   2224 O  O     . GLN   A 1 303 ? 16.156  -19.518 -5.512  1.00 38.10  ?  303 GLN   A O     1 
ATOM   2225 C  CB    . GLN   A 1 303 ? 14.726  -19.535 -8.463  1.00 42.47  ?  303 GLN   A CB    1 
ATOM   2226 N  N     . GLN   A 1 304 ? 17.371  -20.690 -7.007  1.00 40.20  ?  304 GLN   A N     1 
ATOM   2227 C  CA    . GLN   A 1 304 ? 18.016  -21.538 -5.997  1.00 45.07  ?  304 GLN   A CA    1 
ATOM   2228 C  C     . GLN   A 1 304 ? 19.020  -20.786 -5.097  1.00 42.78  ?  304 GLN   A C     1 
ATOM   2229 O  O     . GLN   A 1 304 ? 19.050  -21.001 -3.880  1.00 40.99  ?  304 GLN   A O     1 
ATOM   2230 C  CB    . GLN   A 1 304 ? 18.716  -22.748 -6.643  1.00 45.95  ?  304 GLN   A CB    1 
ATOM   2231 C  CG    . GLN   A 1 304 ? 19.166  -23.823 -5.654  1.00 50.32  ?  304 GLN   A CG    1 
ATOM   2232 C  CD    . GLN   A 1 304 ? 18.025  -24.388 -4.806  1.00 57.83  ?  304 GLN   A CD    1 
ATOM   2233 O  OE1   . GLN   A 1 304 ? 16.897  -24.531 -5.281  1.00 57.35  ?  304 GLN   A OE1   1 
ATOM   2234 N  NE2   . GLN   A 1 304 ? 18.317  -24.708 -3.536  1.00 65.05  ?  304 GLN   A NE2   1 
ATOM   2235 N  N     . VAL   A 1 305 ? 19.837  -19.930 -5.702  1.00 44.35  ?  305 VAL   A N     1 
ATOM   2236 C  CA    . VAL   A 1 305 ? 20.776  -19.048 -4.957  1.00 41.13  ?  305 VAL   A CA    1 
ATOM   2237 C  C     . VAL   A 1 305 ? 19.978  -18.171 -3.984  1.00 39.68  ?  305 VAL   A C     1 
ATOM   2238 O  O     . VAL   A 1 305 ? 20.339  -18.069 -2.807  1.00 35.98  ?  305 VAL   A O     1 
ATOM   2239 C  CB    . VAL   A 1 305 ? 21.643  -18.159 -5.894  1.00 39.97  ?  305 VAL   A CB    1 
ATOM   2240 C  CG1   . VAL   A 1 305 ? 22.551  -17.195 -5.107  1.00 34.27  ?  305 VAL   A CG1   1 
ATOM   2241 C  CG2   . VAL   A 1 305 ? 22.512  -19.026 -6.814  1.00 40.69  ?  305 VAL   A CG2   1 
ATOM   2242 N  N     . MET   A 1 306 ? 18.878  -17.585 -4.473  1.00 41.87  ?  306 MET   A N     1 
ATOM   2243 C  CA    . MET   A 1 306 ? 18.035  -16.701 -3.677  1.00 38.49  ?  306 MET   A CA    1 
ATOM   2244 C  C     . MET   A 1 306 ? 17.374  -17.406 -2.499  1.00 40.18  ?  306 MET   A C     1 
ATOM   2245 O  O     . MET   A 1 306 ? 17.324  -16.850 -1.386  1.00 42.80  ?  306 MET   A O     1 
ATOM   2246 C  CB    . MET   A 1 306 ? 16.984  -16.036 -4.555  1.00 40.99  ?  306 MET   A CB    1 
ATOM   2247 C  CG    . MET   A 1 306 ? 17.540  -14.938 -5.454  1.00 39.99  ?  306 MET   A CG    1 
ATOM   2248 S  SD    . MET   A 1 306 ? 16.274  -13.948 -6.279  1.00 40.66  ?  306 MET   A SD    1 
ATOM   2249 C  CE    . MET   A 1 306 ? 15.438  -15.240 -7.219  1.00 46.10  ?  306 MET   A CE    1 
ATOM   2250 N  N     . LYS   A 1 307 ? 16.885  -18.618 -2.740  1.00 36.20  ?  307 LYS   A N     1 
ATOM   2251 C  CA    . LYS   A 1 307 ? 16.258  -19.444 -1.722  1.00 41.89  ?  307 LYS   A CA    1 
ATOM   2252 C  C     . LYS   A 1 307 ? 17.262  -19.811 -0.633  1.00 42.41  ?  307 LYS   A C     1 
ATOM   2253 O  O     . LYS   A 1 307 ? 16.956  -19.688 0.554   1.00 42.08  ?  307 LYS   A O     1 
ATOM   2254 C  CB    . LYS   A 1 307 ? 15.613  -20.716 -2.352  1.00 44.05  ?  307 LYS   A CB    1 
ATOM   2255 C  CG    . LYS   A 1 307 ? 15.285  -21.844 -1.370  1.00 48.83  ?  307 LYS   A CG    1 
ATOM   2256 C  CD    . LYS   A 1 307 ? 14.137  -22.736 -1.847  1.00 54.34  ?  307 LYS   A CD    1 
ATOM   2257 C  CE    . LYS   A 1 307 ? 13.868  -23.897 -0.896  1.00 59.04  ?  307 LYS   A CE    1 
ATOM   2258 N  NZ    . LYS   A 1 307 ? 14.832  -25.024 -1.103  1.00 63.31  ?  307 LYS   A NZ    1 
ATOM   2259 N  N     . ASP   A 1 308 ? 18.434  -20.293 -1.049  1.00 48.85  ?  308 ASP   A N     1 
ATOM   2260 C  CA    . ASP   A 1 308 ? 19.502  -20.714 -0.135  1.00 49.56  ?  308 ASP   A CA    1 
ATOM   2261 C  C     . ASP   A 1 308 ? 20.033  -19.557 0.699   1.00 42.53  ?  308 ASP   A C     1 
ATOM   2262 O  O     . ASP   A 1 308 ? 20.185  -19.672 1.907   1.00 47.78  ?  308 ASP   A O     1 
ATOM   2263 C  CB    . ASP   A 1 308 ? 20.662  -21.369 -0.896  1.00 55.80  ?  308 ASP   A CB    1 
ATOM   2264 C  CG    . ASP   A 1 308 ? 20.311  -22.757 -1.451  1.00 64.91  ?  308 ASP   A CG    1 
ATOM   2265 O  OD1   . ASP   A 1 308 ? 21.183  -23.360 -2.120  1.00 73.81  ?  308 ASP   A OD1   1 
ATOM   2266 O  OD2   . ASP   A 1 308 ? 19.177  -23.249 -1.244  1.00 66.01  ?  308 ASP   A OD2   1 
ATOM   2267 N  N     . GLY   A 1 309 ? 20.307  -18.445 0.038   1.00 41.61  ?  309 GLY   A N     1 
ATOM   2268 C  CA    . GLY   A 1 309 ? 20.768  -17.223 0.691   1.00 36.65  ?  309 GLY   A CA    1 
ATOM   2269 C  C     . GLY   A 1 309 ? 19.854  -16.745 1.803   1.00 35.26  ?  309 GLY   A C     1 
ATOM   2270 O  O     . GLY   A 1 309 ? 20.317  -16.470 2.903   1.00 32.48  ?  309 GLY   A O     1 
ATOM   2271 N  N     . ALA   A 1 310 ? 18.554  -16.666 1.500   1.00 36.05  ?  310 ALA   A N     1 
ATOM   2272 C  CA    . ALA   A 1 310 ? 17.577  -16.092 2.404   1.00 35.42  ?  310 ALA   A CA    1 
ATOM   2273 C  C     . ALA   A 1 310 ? 17.350  -16.987 3.610   1.00 38.73  ?  310 ALA   A C     1 
ATOM   2274 O  O     . ALA   A 1 310 ? 17.119  -16.494 4.701   1.00 38.04  ?  310 ALA   A O     1 
ATOM   2275 C  CB    . ALA   A 1 310 ? 16.266  -15.799 1.685   1.00 34.55  ?  310 ALA   A CB    1 
ATOM   2276 N  N     . GLU   A 1 311 ? 17.403  -18.301 3.395   1.00 42.13  ?  311 GLU   A N     1 
ATOM   2277 C  CA    . GLU   A 1 311 ? 17.332  -19.269 4.469   1.00 44.81  ?  311 GLU   A CA    1 
ATOM   2278 C  C     . GLU   A 1 311 ? 18.516  -19.109 5.411   1.00 44.09  ?  311 GLU   A C     1 
ATOM   2279 O  O     . GLU   A 1 311 ? 18.336  -19.157 6.616   1.00 48.21  ?  311 GLU   A O     1 
ATOM   2280 C  CB    . GLU   A 1 311 ? 17.280  -20.700 3.894   1.00 51.64  ?  311 GLU   A CB    1 
ATOM   2281 C  CG    . GLU   A 1 311 ? 17.304  -21.827 4.931   1.00 57.56  ?  311 GLU   A CG    1 
ATOM   2282 C  CD    . GLU   A 1 311 ? 17.660  -23.189 4.335   1.00 66.46  ?  311 GLU   A CD    1 
ATOM   2283 O  OE1   . GLU   A 1 311 ? 18.137  -24.063 5.095   1.00 72.43  ?  311 GLU   A OE1   1 
ATOM   2284 O  OE2   . GLU   A 1 311 ? 17.467  -23.397 3.116   1.00 67.14  ?  311 GLU   A OE2   1 
ATOM   2285 N  N     . LYS   A 1 312 ? 19.724  -18.965 4.856   1.00 45.38  ?  312 LYS   A N     1 
ATOM   2286 C  CA    . LYS   A 1 312 ? 20.950  -18.723 5.656   1.00 44.63  ?  312 LYS   A CA    1 
ATOM   2287 C  C     . LYS   A 1 312 ? 20.873  -17.398 6.430   1.00 40.65  ?  312 LYS   A C     1 
ATOM   2288 O  O     . LYS   A 1 312 ? 21.166  -17.353 7.626   1.00 39.73  ?  312 LYS   A O     1 
ATOM   2289 C  CB    . LYS   A 1 312 ? 22.207  -18.757 4.777   1.00 44.84  ?  312 LYS   A CB    1 
ATOM   2290 C  CG    . LYS   A 1 312 ? 22.582  -20.165 4.325   1.00 50.08  ?  312 LYS   A CG    1 
ATOM   2291 C  CD    . LYS   A 1 312 ? 23.988  -20.260 3.755   1.00 52.00  ?  312 LYS   A CD    1 
ATOM   2292 C  CE    . LYS   A 1 312 ? 24.052  -19.888 2.282   1.00 53.71  ?  312 LYS   A CE    1 
ATOM   2293 N  NZ    . LYS   A 1 312 ? 25.430  -20.053 1.742   1.00 54.41  ?  312 LYS   A NZ    1 
ATOM   2294 N  N     . ALA   A 1 313 ? 20.445  -16.341 5.740   1.00 37.24  ?  313 ALA   A N     1 
ATOM   2295 C  CA    . ALA   A 1 313 ? 20.256  -15.024 6.342   1.00 35.88  ?  313 ALA   A CA    1 
ATOM   2296 C  C     . ALA   A 1 313 ? 19.196  -15.040 7.479   1.00 35.88  ?  313 ALA   A C     1 
ATOM   2297 O  O     . ALA   A 1 313 ? 19.467  -14.532 8.573   1.00 32.97  ?  313 ALA   A O     1 
ATOM   2298 C  CB    . ALA   A 1 313 ? 19.890  -13.999 5.276   1.00 32.76  ?  313 ALA   A CB    1 
ATOM   2299 N  N     . SER   A 1 314 ? 18.037  -15.649 7.217   1.00 36.69  ?  314 SER   A N     1 
ATOM   2300 C  CA    . SER   A 1 314 ? 16.942  -15.715 8.170   1.00 40.08  ?  314 SER   A CA    1 
ATOM   2301 C  C     . SER   A 1 314 ? 17.306  -16.493 9.437   1.00 43.44  ?  314 SER   A C     1 
ATOM   2302 O  O     . SER   A 1 314 ? 16.846  -16.146 10.507  1.00 38.65  ?  314 SER   A O     1 
ATOM   2303 C  CB    . SER   A 1 314 ? 15.683  -16.317 7.544   1.00 44.95  ?  314 SER   A CB    1 
ATOM   2304 O  OG    . SER   A 1 314 ? 14.965  -15.351 6.791   1.00 54.79  ?  314 SER   A OG    1 
ATOM   2305 N  N     . ALA   A 1 315 ? 18.098  -17.552 9.300   1.00 44.58  ?  315 ALA   A N     1 
ATOM   2306 C  CA    . ALA   A 1 315 ? 18.548  -18.340 10.446  1.00 47.92  ?  315 ALA   A CA    1 
ATOM   2307 C  C     . ALA   A 1 315 ? 19.320  -17.479 11.452  1.00 47.02  ?  315 ALA   A C     1 
ATOM   2308 O  O     . ALA   A 1 315 ? 19.157  -17.620 12.658  1.00 50.28  ?  315 ALA   A O     1 
ATOM   2309 C  CB    . ALA   A 1 315 ? 19.413  -19.491 9.974   1.00 48.42  ?  315 ALA   A CB    1 
ATOM   2310 N  N     . HIS   A 1 316 ? 20.163  -16.589 10.943  1.00 44.46  ?  316 HIS   A N     1 
ATOM   2311 C  CA    . HIS   A 1 316 ? 20.974  -15.707 11.770  1.00 43.55  ?  316 HIS   A CA    1 
ATOM   2312 C  C     . HIS   A 1 316 ? 20.201  -14.432 12.164  1.00 38.73  ?  316 HIS   A C     1 
ATOM   2313 O  O     . HIS   A 1 316 ? 20.257  -14.000 13.303  1.00 36.95  ?  316 HIS   A O     1 
ATOM   2314 C  CB    . HIS   A 1 316 ? 22.277  -15.374 11.034  1.00 46.72  ?  316 HIS   A CB    1 
ATOM   2315 C  CG    . HIS   A 1 316 ? 23.296  -14.686 11.885  1.00 51.76  ?  316 HIS   A CG    1 
ATOM   2316 N  ND1   . HIS   A 1 316 ? 24.395  -14.045 11.352  1.00 53.47  ?  316 HIS   A ND1   1 
ATOM   2317 C  CD2   . HIS   A 1 316 ? 23.373  -14.508 13.230  1.00 54.03  ?  316 HIS   A CD2   1 
ATOM   2318 C  CE1   . HIS   A 1 316 ? 25.108  -13.513 12.331  1.00 50.06  ?  316 HIS   A CE1   1 
ATOM   2319 N  NE2   . HIS   A 1 316 ? 24.515  -13.780 13.479  1.00 51.89  ?  316 HIS   A NE2   1 
ATOM   2320 N  N     . ALA   A 1 317 ? 19.461  -13.859 11.218  1.00 34.24  ?  317 ALA   A N     1 
ATOM   2321 C  CA    . ALA   A 1 317 ? 18.620  -12.686 11.487  1.00 32.23  ?  317 ALA   A CA    1 
ATOM   2322 C  C     . ALA   A 1 317 ? 17.578  -12.965 12.568  1.00 32.26  ?  317 ALA   A C     1 
ATOM   2323 O  O     . ALA   A 1 317 ? 17.343  -12.101 13.410  1.00 24.93  ?  317 ALA   A O     1 
ATOM   2324 C  CB    . ALA   A 1 317 ? 17.941  -12.206 10.231  1.00 31.47  ?  317 ALA   A CB    1 
ATOM   2325 N  N     . SER   A 1 318 ? 17.002  -14.179 12.550  1.00 30.84  ?  318 SER   A N     1 
ATOM   2326 C  CA    . SER   A 1 318 ? 15.936  -14.557 13.454  1.00 32.77  ?  318 SER   A CA    1 
ATOM   2327 C  C     . SER   A 1 318 ? 16.430  -14.625 14.883  1.00 33.26  ?  318 SER   A C     1 
ATOM   2328 O  O     . SER   A 1 318 ? 15.681  -14.327 15.797  1.00 35.46  ?  318 SER   A O     1 
ATOM   2329 C  CB    . SER   A 1 318 ? 15.280  -15.892 13.068  1.00 33.47  ?  318 SER   A CB    1 
ATOM   2330 O  OG    . SER   A 1 318 ? 16.177  -16.952 13.221  1.00 39.88  ?  318 SER   A OG    1 
ATOM   2331 N  N     . ARG   A 1 319 ? 17.678  -15.037 15.091  1.00 38.98  ?  319 ARG   A N     1 
ATOM   2332 C  CA    . ARG   A 1 319 ? 18.211  -15.160 16.468  1.00 40.92  ?  319 ARG   A CA    1 
ATOM   2333 C  C     . ARG   A 1 319 ? 18.486  -13.777 17.080  1.00 34.95  ?  319 ARG   A C     1 
ATOM   2334 O  O     . ARG   A 1 319 ? 18.318  -13.592 18.264  1.00 35.21  ?  319 ARG   A O     1 
ATOM   2335 C  CB    . ARG   A 1 319 ? 19.485  -15.989 16.527  1.00 45.95  ?  319 ARG   A CB    1 
ATOM   2336 C  CG    . ARG   A 1 319 ? 19.353  -17.413 15.997  1.00 55.61  ?  319 ARG   A CG    1 
ATOM   2337 C  CD    . ARG   A 1 319 ? 20.622  -18.249 16.236  1.00 60.59  ?  319 ARG   A CD    1 
ATOM   2338 N  NE    . ARG   A 1 319 ? 21.834  -17.406 16.320  1.00 66.38  ?  319 ARG   A NE    1 
ATOM   2339 C  CZ    . ARG   A 1 319 ? 22.861  -17.398 15.464  1.00 68.81  ?  319 ARG   A CZ    1 
ATOM   2340 N  NH1   . ARG   A 1 319 ? 23.873  -16.551 15.676  1.00 69.18  ?  319 ARG   A NH1   1 
ATOM   2341 N  NH2   . ARG   A 1 319 ? 22.916  -18.227 14.418  1.00 68.09  ?  319 ARG   A NH2   1 
ATOM   2342 N  N     . THR   A 1 320 ? 18.925  -12.836 16.262  1.00 33.71  ?  320 THR   A N     1 
ATOM   2343 C  CA    . THR   A 1 320 ? 19.107  -11.444 16.708  1.00 32.35  ?  320 THR   A CA    1 
ATOM   2344 C  C     . THR   A 1 320 ? 17.760  -10.800 17.033  1.00 31.83  ?  320 THR   A C     1 
ATOM   2345 O  O     . THR   A 1 320 ? 17.602  -10.211 18.104  1.00 34.02  ?  320 THR   A O     1 
ATOM   2346 C  CB    . THR   A 1 320 ? 19.917  -10.624 15.696  1.00 30.81  ?  320 THR   A CB    1 
ATOM   2347 O  OG1   . THR   A 1 320 ? 21.194  -11.252 15.487  1.00 29.98  ?  320 THR   A OG1   1 
ATOM   2348 C  CG2   . THR   A 1 320 ? 20.170  -9.151  16.196  1.00 27.98  ?  320 THR   A CG2   1 
ATOM   2349 N  N     . LEU   A 1 321 ? 16.788  -10.915 16.133  1.00 29.86  ?  321 LEU   A N     1 
ATOM   2350 C  CA    . LEU   A 1 321 ? 15.459  -10.292 16.337  1.00 27.32  ?  321 LEU   A CA    1 
ATOM   2351 C  C     . LEU   A 1 321 ? 14.760  -10.830 17.559  1.00 27.36  ?  321 LEU   A C     1 
ATOM   2352 O  O     . LEU   A 1 321 ? 14.129  -10.079 18.248  1.00 28.17  ?  321 LEU   A O     1 
ATOM   2353 C  CB    . LEU   A 1 321 ? 14.549  -10.475 15.127  1.00 24.42  ?  321 LEU   A CB    1 
ATOM   2354 C  CG    . LEU   A 1 321 ? 13.271  -9.628  15.143  1.00 22.68  ?  321 LEU   A CG    1 
ATOM   2355 C  CD1   . LEU   A 1 321 ? 13.607  -8.161  14.992  1.00 22.78  ?  321 LEU   A CD1   1 
ATOM   2356 C  CD2   . LEU   A 1 321 ? 12.280  -10.029 14.074  1.00 21.96  ?  321 LEU   A CD2   1 
ATOM   2357 N  N     . LYS   A 1 322 ? 14.890  -12.140 17.807  1.00 31.44  ?  322 LYS   A N     1 
ATOM   2358 C  CA    . LYS   A 1 322 ? 14.331  -12.793 18.990  1.00 37.41  ?  322 LYS   A CA    1 
ATOM   2359 C  C     . LYS   A 1 322 ? 14.920  -12.263 20.288  1.00 35.12  ?  322 LYS   A C     1 
ATOM   2360 O  O     . LYS   A 1 322 ? 14.187  -12.085 21.282  1.00 37.73  ?  322 LYS   A O     1 
ATOM   2361 C  CB    . LYS   A 1 322 ? 14.517  -14.324 18.917  1.00 42.07  ?  322 LYS   A CB    1 
ATOM   2362 C  CG    . LYS   A 1 322 ? 13.722  -15.120 19.925  1.00 47.96  ?  322 LYS   A CG    1 
ATOM   2363 C  CD    . LYS   A 1 322 ? 13.690  -16.609 19.565  1.00 55.77  ?  322 LYS   A CD    1 
ATOM   2364 C  CE    . LYS   A 1 322 ? 13.159  -17.490 20.695  1.00 57.44  ?  322 LYS   A CE    1 
ATOM   2365 N  NZ    . LYS   A 1 322 ? 11.689  -17.360 20.860  1.00 59.04  ?  322 LYS   A NZ    1 
ATOM   2366 N  N     . ALA   A 1 323 ? 16.230  -12.022 20.300  1.00 34.86  ?  323 ALA   A N     1 
ATOM   2367 C  CA    . ALA   A 1 323 ? 16.884  -11.394 21.469  1.00 35.75  ?  323 ALA   A CA    1 
ATOM   2368 C  C     . ALA   A 1 323 ? 16.460  -9.889  21.616  1.00 33.70  ?  323 ALA   A C     1 
ATOM   2369 O  O     . ALA   A 1 323 ? 16.196  -9.388  22.702  1.00 36.49  ?  323 ALA   A O     1 
ATOM   2370 C  CB    . ALA   A 1 323 ? 18.390  -11.546 21.364  1.00 35.98  ?  323 ALA   A CB    1 
ATOM   2371 N  N     . VAL   A 1 324 ? 16.336  -9.193  20.507  1.00 29.69  ?  324 VAL   A N     1 
ATOM   2372 C  CA    . VAL   A 1 324 ? 15.864  -7.789  20.520  1.00 29.47  ?  324 VAL   A CA    1 
ATOM   2373 C  C     . VAL   A 1 324 ? 14.443  -7.709  21.089  1.00 32.57  ?  324 VAL   A C     1 
ATOM   2374 O  O     . VAL   A 1 324 ? 14.154  -6.858  21.922  1.00 33.33  ?  324 VAL   A O     1 
ATOM   2375 C  CB    . VAL   A 1 324 ? 15.950  -7.142  19.116  1.00 29.92  ?  324 VAL   A CB    1 
ATOM   2376 C  CG1   . VAL   A 1 324 ? 15.177  -5.814  19.024  1.00 27.71  ?  324 VAL   A CG1   1 
ATOM   2377 C  CG2   . VAL   A 1 324 ? 17.403  -6.914  18.733  1.00 29.92  ?  324 VAL   A CG2   1 
ATOM   2378 N  N     . TYR   A 1 325 ? 13.580  -8.637  20.652  1.00 31.12  ?  325 TYR   A N     1 
ATOM   2379 C  CA    . TYR   A 1 325 ? 12.176  -8.669  21.045  1.00 32.87  ?  325 TYR   A CA    1 
ATOM   2380 C  C     . TYR   A 1 325 ? 12.021  -9.035  22.537  1.00 33.26  ?  325 TYR   A C     1 
ATOM   2381 O  O     . TYR   A 1 325 ? 11.217  -8.442  23.212  1.00 31.31  ?  325 TYR   A O     1 
ATOM   2382 C  CB    . TYR   A 1 325 ? 11.387  -9.606  20.107  1.00 32.44  ?  325 TYR   A CB    1 
ATOM   2383 C  CG    . TYR   A 1 325 ? 10.845  -8.932  18.847  1.00 33.51  ?  325 TYR   A CG    1 
ATOM   2384 C  CD1   . TYR   A 1 325 ? 11.404  -7.737  18.348  1.00 30.05  ?  325 TYR   A CD1   1 
ATOM   2385 C  CD2   . TYR   A 1 325 ? 9.761   -9.486  18.148  1.00 34.00  ?  325 TYR   A CD2   1 
ATOM   2386 C  CE1   . TYR   A 1 325 ? 10.904  -7.109  17.225  1.00 29.70  ?  325 TYR   A CE1   1 
ATOM   2387 C  CE2   . TYR   A 1 325 ? 9.258   -8.862  16.988  1.00 32.35  ?  325 TYR   A CE2   1 
ATOM   2388 C  CZ    . TYR   A 1 325 ? 9.822   -7.679  16.546  1.00 31.23  ?  325 TYR   A CZ    1 
ATOM   2389 O  OH    . TYR   A 1 325 ? 9.341   -7.034  15.405  1.00 30.18  ?  325 TYR   A OH    1 
ATOM   2390 N  N     . GLU   A 1 326 ? 12.817  -9.987  23.016  1.00 35.35  ?  326 GLU   A N     1 
ATOM   2391 C  CA    . GLU   A 1 326 ? 12.852  -10.375 24.426  1.00 38.59  ?  326 GLU   A CA    1 
ATOM   2392 C  C     . GLU   A 1 326 ? 13.319  -9.221  25.328  1.00 37.62  ?  326 GLU   A C     1 
ATOM   2393 O  O     . GLU   A 1 326 ? 12.716  -8.973  26.361  1.00 38.65  ?  326 GLU   A O     1 
ATOM   2394 C  CB    . GLU   A 1 326 ? 13.732  -11.618 24.629  1.00 46.96  ?  326 GLU   A CB    1 
ATOM   2395 C  CG    . GLU   A 1 326 ? 13.923  -12.083 26.079  1.00 54.56  ?  326 GLU   A CG    1 
ATOM   2396 C  CD    . GLU   A 1 326 ? 12.697  -12.781 26.648  1.00 61.48  ?  326 GLU   A CD    1 
ATOM   2397 O  OE1   . GLU   A 1 326 ? 12.509  -12.736 27.896  1.00 63.82  ?  326 GLU   A OE1   1 
ATOM   2398 O  OE2   . GLU   A 1 326 ? 11.915  -13.358 25.847  1.00 62.01  ?  326 GLU   A OE2   1 
ATOM   2399 N  N     . ALA   A 1 327 ? 14.376  -8.525  24.908  1.00 35.02  ?  327 ALA   A N     1 
ATOM   2400 C  CA    . ALA   A 1 327 ? 14.927  -7.352  25.608  1.00 37.42  ?  327 ALA   A CA    1 
ATOM   2401 C  C     . ALA   A 1 327 ? 13.908  -6.250  25.739  1.00 33.74  ?  327 ALA   A C     1 
ATOM   2402 O  O     . ALA   A 1 327 ? 13.685  -5.741  26.822  1.00 33.49  ?  327 ALA   A O     1 
ATOM   2403 C  CB    . ALA   A 1 327 ? 16.159  -6.826  24.884  1.00 35.86  ?  327 ALA   A CB    1 
ATOM   2404 N  N     . ILE   A 1 328 ? 13.267  -5.908  24.630  1.00 35.93  ?  328 ILE   A N     1 
ATOM   2405 C  CA    . ILE   A 1 328 ? 12.220  -4.865  24.613  1.00 35.38  ?  328 ILE   A CA    1 
ATOM   2406 C  C     . ILE   A 1 328 ? 11.019  -5.270  25.495  1.00 34.58  ?  328 ILE   A C     1 
ATOM   2407 O  O     . ILE   A 1 328 ? 10.356  -4.413  26.080  1.00 30.46  ?  328 ILE   A O     1 
ATOM   2408 C  CB    . ILE   A 1 328 ? 11.737  -4.566  23.180  1.00 35.36  ?  328 ILE   A CB    1 
ATOM   2409 C  CG1   . ILE   A 1 328 ? 12.860  -3.987  22.336  1.00 32.70  ?  328 ILE   A CG1   1 
ATOM   2410 C  CG2   . ILE   A 1 328 ? 10.550  -3.590  23.168  1.00 36.32  ?  328 ILE   A CG2   1 
ATOM   2411 C  CD1   . ILE   A 1 328 ? 12.572  -4.039  20.827  1.00 30.65  ?  328 ILE   A CD1   1 
ATOM   2412 N  N     . GLY   A 1 329 ? 10.752  -6.579  25.551  1.00 34.73  ?  329 GLY   A N     1 
ATOM   2413 C  CA    . GLY   A 1 329 ? 9.734   -7.159  26.421  1.00 36.17  ?  329 GLY   A CA    1 
ATOM   2414 C  C     . GLY   A 1 329 ? 8.430   -7.557  25.723  1.00 34.97  ?  329 GLY   A C     1 
ATOM   2415 O  O     . GLY   A 1 329 ? 7.428   -7.709  26.385  1.00 36.07  ?  329 GLY   A O     1 
ATOM   2416 N  N     . PHE   A 1 330 ? 8.443   -7.717  24.398  1.00 30.10  ?  330 PHE   A N     1 
ATOM   2417 C  CA    . PHE   A 1 330 ? 7.277   -8.155  23.656  1.00 27.62  ?  330 PHE   A CA    1 
ATOM   2418 C  C     . PHE   A 1 330 ? 6.975   -9.608  24.032  1.00 31.38  ?  330 PHE   A C     1 
ATOM   2419 O  O     . PHE   A 1 330 ? 7.893   -10.416 24.270  1.00 30.54  ?  330 PHE   A O     1 
ATOM   2420 C  CB    . PHE   A 1 330 ? 7.535   -8.115  22.128  1.00 29.85  ?  330 PHE   A CB    1 
ATOM   2421 C  CG    . PHE   A 1 330 ? 7.553   -6.741  21.492  1.00 28.44  ?  330 PHE   A CG    1 
ATOM   2422 C  CD1   . PHE   A 1 330 ? 6.890   -5.673  22.034  1.00 29.90  ?  330 PHE   A CD1   1 
ATOM   2423 C  CD2   . PHE   A 1 330 ? 8.169   -6.565  20.258  1.00 30.26  ?  330 PHE   A CD2   1 
ATOM   2424 C  CE1   . PHE   A 1 330 ? 6.913   -4.442  21.416  1.00 29.27  ?  330 PHE   A CE1   1 
ATOM   2425 C  CE2   . PHE   A 1 330 ? 8.161   -5.342  19.617  1.00 29.29  ?  330 PHE   A CE2   1 
ATOM   2426 C  CZ    . PHE   A 1 330 ? 7.528   -4.274  20.199  1.00 26.43  ?  330 PHE   A CZ    1 
ATOM   2427 N  N     . VAL   A 1 331 ? 5.693   -9.956  24.091  1.00 30.46  ?  331 VAL   A N     1 
ATOM   2428 C  CA    . VAL   A 1 331 ? 5.294   -11.367 24.270  1.00 30.40  ?  331 VAL   A CA    1 
ATOM   2429 C  C     . VAL   A 1 331 ? 5.773   -12.166 23.054  1.00 31.34  ?  331 VAL   A C     1 
ATOM   2430 O  O     . VAL   A 1 331 ? 5.568   -11.756 21.921  1.00 31.27  ?  331 VAL   A O     1 
ATOM   2431 C  CB    . VAL   A 1 331 ? 3.753   -11.500 24.445  1.00 30.59  ?  331 VAL   A CB    1 
ATOM   2432 C  CG1   . VAL   A 1 331 ? 3.333   -12.978 24.460  1.00 30.95  ?  331 VAL   A CG1   1 
ATOM   2433 C  CG2   . VAL   A 1 331 ? 3.309   -10.821 25.743  1.00 30.88  ?  331 VAL   A CG2   1 
ATOM   2434 N  N     . ALA   A 1 332 ? 6.410   -13.312 23.276  1.00 35.13  ?  332 ALA   A N     1 
ATOM   2435 C  CA    . ALA   A 1 332 ? 6.959   -14.095 22.193  1.00 36.12  ?  332 ALA   A CA    1 
ATOM   2436 C  C     . ALA   A 1 332 ? 5.854   -14.736 21.339  1.00 35.63  ?  332 ALA   A C     1 
ATOM   2437 O  O     . ALA   A 1 332 ? 4.790   -15.080 21.845  1.00 35.74  ?  332 ALA   A O     1 
ATOM   2438 C  CB    . ALA   A 1 332 ? 7.890   -15.158 22.749  1.00 40.82  ?  332 ALA   A CB    1 
ATOM   2439 N  N     . LYS   A 1 333 ? 6.130   -14.897 20.050  1.00 35.99  ?  333 LYS   A N     1 
ATOM   2440 C  CA    . LYS   A 1 333 ? 5.176   -15.476 19.120  1.00 39.23  ?  333 LYS   A CA    1 
ATOM   2441 C  C     . LYS   A 1 333 ? 4.932   -16.933 19.488  1.00 38.44  ?  333 LYS   A C     1 
ATOM   2442 O  O     . LYS   A 1 333 ? 5.848   -17.636 19.851  1.00 36.46  ?  333 LYS   A O     1 
ATOM   2443 C  CB    . LYS   A 1 333 ? 5.704   -15.396 17.676  1.00 43.51  ?  333 LYS   A CB    1 
ATOM   2444 C  CG    . LYS   A 1 333 ? 4.788   -16.074 16.684  1.00 47.79  ?  333 LYS   A CG    1 
ATOM   2445 C  CD    . LYS   A 1 333 ? 4.987   -15.631 15.240  1.00 49.78  ?  333 LYS   A CD    1 
ATOM   2446 C  CE    . LYS   A 1 333 ? 3.953   -16.267 14.292  1.00 50.51  ?  333 LYS   A CE    1 
ATOM   2447 N  NZ    . LYS   A 1 333 ? 2.708   -16.781 14.963  1.00 48.91  ?  333 LYS   A NZ    1 
ATOM   2448 N  N     . ARG   A 1 334 ? 3.692   -17.367 19.345  1.00 39.78  ?  334 ARG   A N     1 
ATOM   2449 C  CA    . ARG   A 1 334 ? 3.280   -18.685 19.776  1.00 42.61  ?  334 ARG   A CA    1 
ATOM   2450 C  C     . ARG   A 1 334 ? 3.484   -19.643 18.621  1.00 45.50  ?  334 ARG   A C     1 
ATOM   2451 O  O     . ARG   A 1 334 ? 4.288   -20.551 18.721  1.00 59.55  ?  334 ARG   A O     1 
ATOM   2452 C  CB    . ARG   A 1 334 ? 1.839   -18.668 20.288  1.00 37.85  ?  334 ARG   A CB    1 
ATOM   2453 C  CG    . ARG   A 1 334 ? 1.519   -17.502 21.253  1.00 38.18  ?  334 ARG   A CG    1 
ATOM   2454 C  CD    . ARG   A 1 334 ? 2.037   -17.697 22.656  1.00 38.76  ?  334 ARG   A CD    1 
ATOM   2455 N  NE    . ARG   A 1 334 ? 1.992   -19.102 23.104  1.00 39.83  ?  334 ARG   A NE    1 
ATOM   2456 C  CZ    . ARG   A 1 334 ? 2.754   -19.610 24.078  1.00 38.47  ?  334 ARG   A CZ    1 
ATOM   2457 N  NH1   . ARG   A 1 334 ? 3.634   -18.853 24.749  1.00 36.17  ?  334 ARG   A NH1   1 
ATOM   2458 N  NH2   . ARG   A 1 334 ? 2.648   -20.888 24.380  1.00 39.10  ?  334 ARG   A NH2   1 
ATOM   2459 N  N     . HIS   A 1 335 ? 2.831   -19.430 17.498  1.00 41.85  ?  335 HIS   A N     1 
ATOM   2460 C  CA    . HIS   A 1 335 ? 2.919   -20.436 16.409  1.00 44.48  ?  335 HIS   A CA    1 
ATOM   2461 C  C     . HIS   A 1 335 ? 3.143   -21.823 17.068  1.00 45.62  ?  335 HIS   A C     1 
ATOM   2462 O  O     . HIS   A 1 335 ? 2.788   -22.850 16.470  1.00 47.11  ?  335 HIS   A O     1 
ATOM   2463 C  CB    . HIS   A 1 335 ? 4.002   -20.134 15.336  1.00 42.78  ?  335 HIS   A CB    1 
ATOM   2464 C  CG    . HIS   A 1 335 ? 5.408   -20.092 15.864  1.00 43.28  ?  335 HIS   A CG    1 
ATOM   2465 N  ND1   . HIS   A 1 335 ? 5.932   -21.082 16.679  1.00 43.06  ?  335 HIS   A ND1   1 
ATOM   2466 C  CD2   . HIS   A 1 335 ? 6.393   -19.167 15.706  1.00 40.53  ?  335 HIS   A CD2   1 
ATOM   2467 C  CE1   . HIS   A 1 335 ? 7.164   -20.745 17.029  1.00 44.17  ?  335 HIS   A CE1   1 
ATOM   2468 N  NE2   . HIS   A 1 335 ? 7.465   -19.587 16.452  1.00 41.60  ?  335 HIS   A NE2   1 
ATOM   2469 N  N     . THR   B 1 2   ? -18.579 -12.931 1.324   1.00 54.67  ?  2   THR   B N     1 
ATOM   2470 C  CA    . THR   B 1 2   ? -17.748 -12.680 2.543   1.00 53.57  ?  2   THR   B CA    1 
ATOM   2471 C  C     . THR   B 1 2   ? -18.187 -11.346 3.145   1.00 48.38  ?  2   THR   B C     1 
ATOM   2472 O  O     . THR   B 1 2   ? -18.597 -10.431 2.417   1.00 48.58  ?  2   THR   B O     1 
ATOM   2473 C  CB    . THR   B 1 2   ? -16.219 -12.682 2.251   1.00 57.24  ?  2   THR   B CB    1 
ATOM   2474 O  OG1   . THR   B 1 2   ? -15.841 -11.472 1.582   1.00 63.31  ?  2   THR   B OG1   1 
ATOM   2475 C  CG2   . THR   B 1 2   ? -15.810 -13.891 1.389   1.00 58.85  ?  2   THR   B CG2   1 
ATOM   2476 N  N     . LYS   B 1 3   ? -18.131 -11.252 4.469   1.00 42.18  ?  3   LYS   B N     1 
ATOM   2477 C  CA    . LYS   B 1 3   ? -18.548 -10.026 5.152   1.00 39.93  ?  3   LYS   B CA    1 
ATOM   2478 C  C     . LYS   B 1 3   ? -17.506 -8.911  4.972   1.00 39.39  ?  3   LYS   B C     1 
ATOM   2479 O  O     . LYS   B 1 3   ? -16.319 -9.195  4.783   1.00 34.66  ?  3   LYS   B O     1 
ATOM   2480 C  CB    . LYS   B 1 3   ? -18.784 -10.272 6.654   1.00 39.55  ?  3   LYS   B CB    1 
ATOM   2481 C  CG    . LYS   B 1 3   ? -19.767 -11.400 6.966   1.00 38.62  ?  3   LYS   B CG    1 
ATOM   2482 C  CD    . LYS   B 1 3   ? -20.106 -11.457 8.457   1.00 40.73  ?  3   LYS   B CD    1 
ATOM   2483 C  CE    . LYS   B 1 3   ? -20.577 -12.845 8.874   1.00 40.81  ?  3   LYS   B CE    1 
ATOM   2484 N  NZ    . LYS   B 1 3   ? -20.982 -12.873 10.305  1.00 41.92  ?  3   LYS   B NZ    1 
ATOM   2485 N  N     . PRO   B 1 4   ? -17.940 -7.642  5.069   1.00 37.38  ?  4   PRO   B N     1 
ATOM   2486 C  CA    . PRO   B 1 4   ? -16.983 -6.549  5.222   1.00 35.38  ?  4   PRO   B CA    1 
ATOM   2487 C  C     . PRO   B 1 4   ? -16.113 -6.724  6.481   1.00 35.23  ?  4   PRO   B C     1 
ATOM   2488 O  O     . PRO   B 1 4   ? -16.575 -7.309  7.485   1.00 35.16  ?  4   PRO   B O     1 
ATOM   2489 C  CB    . PRO   B 1 4   ? -17.875 -5.290  5.367   1.00 35.17  ?  4   PRO   B CB    1 
ATOM   2490 C  CG    . PRO   B 1 4   ? -19.212 -5.694  4.834   1.00 37.83  ?  4   PRO   B CG    1 
ATOM   2491 C  CD    . PRO   B 1 4   ? -19.334 -7.166  5.107   1.00 38.39  ?  4   PRO   B CD    1 
ATOM   2492 N  N     . ILE   B 1 5   ? -14.883 -6.208  6.421   1.00 31.89  ?  5   ILE   B N     1 
ATOM   2493 C  CA    . ILE   B 1 5   ? -13.867 -6.405  7.453   1.00 30.80  ?  5   ILE   B CA    1 
ATOM   2494 C  C     . ILE   B 1 5   ? -13.779 -5.186  8.370   1.00 31.10  ?  5   ILE   B C     1 
ATOM   2495 O  O     . ILE   B 1 5   ? -13.712 -4.060  7.891   1.00 31.68  ?  5   ILE   B O     1 
ATOM   2496 C  CB    . ILE   B 1 5   ? -12.487 -6.762  6.805   1.00 31.79  ?  5   ILE   B CB    1 
ATOM   2497 C  CG1   . ILE   B 1 5   ? -12.541 -8.190  6.236   1.00 32.61  ?  5   ILE   B CG1   1 
ATOM   2498 C  CG2   . ILE   B 1 5   ? -11.349 -6.677  7.814   1.00 29.41  ?  5   ILE   B CG2   1 
ATOM   2499 C  CD1   . ILE   B 1 5   ? -11.543 -8.463  5.152   1.00 34.64  ?  5   ILE   B CD1   1 
ATOM   2500 N  N     . VAL   B 1 6   ? -13.842 -5.437  9.685   1.00 31.25  ?  6   VAL   B N     1 
ATOM   2501 C  CA    . VAL   B 1 6   ? -13.574 -4.447  10.741  1.00 30.33  ?  6   VAL   B CA    1 
ATOM   2502 C  C     . VAL   B 1 6   ? -12.164 -4.718  11.307  1.00 28.23  ?  6   VAL   B C     1 
ATOM   2503 O  O     . VAL   B 1 6   ? -11.807 -5.862  11.591  1.00 26.09  ?  6   VAL   B O     1 
ATOM   2504 C  CB    . VAL   B 1 6   ? -14.635 -4.544  11.851  1.00 32.21  ?  6   VAL   B CB    1 
ATOM   2505 C  CG1   . VAL   B 1 6   ? -14.271 -3.699  13.085  1.00 32.89  ?  6   VAL   B CG1   1 
ATOM   2506 C  CG2   . VAL   B 1 6   ? -16.003 -4.128  11.313  1.00 34.64  ?  6   VAL   B CG2   1 
ATOM   2507 N  N     . PHE   B 1 7   ? -11.376 -3.667  11.436  1.00 26.62  ?  7   PHE   B N     1 
ATOM   2508 C  CA    . PHE   B 1 7   ? -10.062 -3.704  12.090  1.00 29.06  ?  7   PHE   B CA    1 
ATOM   2509 C  C     . PHE   B 1 7   ? -9.908  -2.557  13.088  1.00 30.35  ?  7   PHE   B C     1 
ATOM   2510 O  O     . PHE   B 1 7   ? -10.169 -1.411  12.754  1.00 29.80  ?  7   PHE   B O     1 
ATOM   2511 C  CB    . PHE   B 1 7   ? -8.904  -3.683  11.062  1.00 27.73  ?  7   PHE   B CB    1 
ATOM   2512 C  CG    . PHE   B 1 7   ? -7.534  -3.881  11.680  1.00 28.08  ?  7   PHE   B CG    1 
ATOM   2513 C  CD1   . PHE   B 1 7   ? -6.791  -2.787  12.096  1.00 28.28  ?  7   PHE   B CD1   1 
ATOM   2514 C  CD2   . PHE   B 1 7   ? -7.009  -5.154  11.873  1.00 27.43  ?  7   PHE   B CD2   1 
ATOM   2515 C  CE1   . PHE   B 1 7   ? -5.542  -2.939  12.686  1.00 29.37  ?  7   PHE   B CE1   1 
ATOM   2516 C  CE2   . PHE   B 1 7   ? -5.751  -5.323  12.466  1.00 30.29  ?  7   PHE   B CE2   1 
ATOM   2517 C  CZ    . PHE   B 1 7   ? -5.024  -4.212  12.891  1.00 27.87  ?  7   PHE   B CZ    1 
ATOM   2518 N  N     . SER   B 1 8   ? -9.511  -2.871  14.324  1.00 32.51  ?  8   SER   B N     1 
ATOM   2519 C  CA    . SER   B 1 8   ? -9.025  -1.830  15.248  1.00 34.34  ?  8   SER   B CA    1 
ATOM   2520 C  C     . SER   B 1 8   ? -7.898  -2.351  16.142  1.00 34.19  ?  8   SER   B C     1 
ATOM   2521 O  O     . SER   B 1 8   ? -7.671  -3.561  16.223  1.00 28.38  ?  8   SER   B O     1 
ATOM   2522 C  CB    . SER   B 1 8   ? -10.152 -1.276  16.082  1.00 36.30  ?  8   SER   B CB    1 
ATOM   2523 O  OG    . SER   B 1 8   ? -9.827  0.036   16.548  1.00 34.10  ?  8   SER   B OG    1 
ATOM   2524 N  N     . GLY   B 1 9   ? -7.214  -1.417  16.815  1.00 34.76  ?  9   GLY   B N     1 
ATOM   2525 C  CA    . GLY   B 1 9   ? -6.117  -1.729  17.757  1.00 35.38  ?  9   GLY   B CA    1 
ATOM   2526 C  C     . GLY   B 1 9   ? -6.170  -0.908  19.037  1.00 35.14  ?  9   GLY   B C     1 
ATOM   2527 O  O     . GLY   B 1 9   ? -6.744  0.176   19.059  1.00 33.74  ?  9   GLY   B O     1 
ATOM   2528 N  N     . ALA   B 1 10  ? -5.586  -1.439  20.105  1.00 35.15  ?  10  ALA   B N     1 
ATOM   2529 C  CA    . ALA   B 1 10  ? -5.326  -0.681  21.326  1.00 35.39  ?  10  ALA   B CA    1 
ATOM   2530 C  C     . ALA   B 1 10  ? -3.909  -0.982  21.783  1.00 38.63  ?  10  ALA   B C     1 
ATOM   2531 O  O     . ALA   B 1 10  ? -3.463  -2.138  21.728  1.00 32.96  ?  10  ALA   B O     1 
ATOM   2532 C  CB    . ALA   B 1 10  ? -6.313  -1.035  22.419  1.00 35.07  ?  10  ALA   B CB    1 
ATOM   2533 N  N     . GLN   B 1 11  ? -3.216  0.053   22.263  1.00 39.26  ?  11  GLN   B N     1 
ATOM   2534 C  CA    . GLN   B 1 11  ? -1.848  -0.064  22.747  1.00 42.29  ?  11  GLN   B CA    1 
ATOM   2535 C  C     . GLN   B 1 11  ? -1.791  -0.747  24.102  1.00 41.56  ?  11  GLN   B C     1 
ATOM   2536 O  O     . GLN   B 1 11  ? -2.573  -0.407  24.965  1.00 40.79  ?  11  GLN   B O     1 
ATOM   2537 C  CB    . GLN   B 1 11  ? -1.244  1.328   22.914  1.00 45.78  ?  11  GLN   B CB    1 
ATOM   2538 C  CG    . GLN   B 1 11  ? -0.837  1.998   21.622  1.00 46.80  ?  11  GLN   B CG    1 
ATOM   2539 C  CD    . GLN   B 1 11  ? -0.096  3.292   21.876  1.00 46.14  ?  11  GLN   B CD    1 
ATOM   2540 O  OE1   . GLN   B 1 11  ? 0.336   3.568   22.988  1.00 46.01  ?  11  GLN   B OE1   1 
ATOM   2541 N  NE2   . GLN   B 1 11  ? 0.057   4.079   20.843  1.00 45.37  ?  11  GLN   B NE2   1 
ATOM   2542 N  N     . PRO   B 1 12  ? -0.848  -1.689  24.303  1.00 40.90  ?  12  PRO   B N     1 
ATOM   2543 C  CA    . PRO   B 1 12  ? -0.638  -2.302  25.609  1.00 43.34  ?  12  PRO   B CA    1 
ATOM   2544 C  C     . PRO   B 1 12  ? 0.274   -1.426  26.468  1.00 46.22  ?  12  PRO   B C     1 
ATOM   2545 O  O     . PRO   B 1 12  ? 1.342   -1.869  26.899  1.00 49.77  ?  12  PRO   B O     1 
ATOM   2546 C  CB    . PRO   B 1 12  ? 0.043   -3.621  25.252  1.00 42.64  ?  12  PRO   B CB    1 
ATOM   2547 C  CG    . PRO   B 1 12  ? 0.877   -3.256  24.085  1.00 41.72  ?  12  PRO   B CG    1 
ATOM   2548 C  CD    . PRO   B 1 12  ? 0.029   -2.294  23.292  1.00 40.81  ?  12  PRO   B CD    1 
ATOM   2549 N  N     . SER   B 1 13  ? -0.144  -0.178  26.685  1.00 46.28  ?  13  SER   B N     1 
ATOM   2550 C  CA    . SER   B 1 13  ? 0.596   0.796   27.494  1.00 50.11  ?  13  SER   B CA    1 
ATOM   2551 C  C     . SER   B 1 13  ? -0.387  1.480   28.442  1.00 55.84  ?  13  SER   B C     1 
ATOM   2552 O  O     . SER   B 1 13  ? -1.544  1.742   28.075  1.00 56.16  ?  13  SER   B O     1 
ATOM   2553 C  CB    . SER   B 1 13  ? 1.305   1.824   26.614  1.00 48.68  ?  13  SER   B CB    1 
ATOM   2554 O  OG    . SER   B 1 13  ? 0.402   2.475   25.744  1.00 51.20  ?  13  SER   B OG    1 
ATOM   2555 N  N     . GLY   B 1 14  ? 0.062   1.759   29.660  1.00 59.74  ?  14  GLY   B N     1 
ATOM   2556 C  CA    . GLY   B 1 14  ? -0.798  2.380   30.679  1.00 61.60  ?  14  GLY   B CA    1 
ATOM   2557 C  C     . GLY   B 1 14  ? -1.954  1.491   31.112  1.00 58.00  ?  14  GLY   B C     1 
ATOM   2558 O  O     . GLY   B 1 14  ? -1.810  0.263   31.185  1.00 58.72  ?  14  GLY   B O     1 
ATOM   2559 N  N     . GLU   B 1 15  ? -3.094  2.120   31.407  1.00 59.82  ?  15  GLU   B N     1 
ATOM   2560 C  CA    . GLU   B 1 15  ? -4.279  1.439   31.966  1.00 58.27  ?  15  GLU   B CA    1 
ATOM   2561 C  C     . GLU   B 1 15  ? -5.547  1.918   31.243  1.00 55.08  ?  15  GLU   B C     1 
ATOM   2562 O  O     . GLU   B 1 15  ? -5.936  3.080   31.366  1.00 54.47  ?  15  GLU   B O     1 
ATOM   2563 C  CB    . GLU   B 1 15  ? -4.391  1.725   33.463  1.00 60.69  ?  15  GLU   B CB    1 
ATOM   2564 C  CG    . GLU   B 1 15  ? -3.172  1.310   34.285  1.00 67.02  ?  15  GLU   B CG    1 
ATOM   2565 C  CD    . GLU   B 1 15  ? -3.204  1.801   35.735  1.00 69.63  ?  15  GLU   B CD    1 
ATOM   2566 O  OE1   . GLU   B 1 15  ? -4.122  2.550   36.124  1.00 75.94  ?  15  GLU   B OE1   1 
ATOM   2567 O  OE2   . GLU   B 1 15  ? -2.289  1.448   36.499  1.00 70.95  ?  15  GLU   B OE2   1 
ATOM   2568 N  N     . LEU   B 1 16  ? -6.181  1.025   30.488  1.00 49.80  ?  16  LEU   B N     1 
ATOM   2569 C  CA    . LEU   B 1 16  ? -7.355  1.366   29.699  1.00 50.17  ?  16  LEU   B CA    1 
ATOM   2570 C  C     . LEU   B 1 16  ? -8.470  1.935   30.580  1.00 50.71  ?  16  LEU   B C     1 
ATOM   2571 O  O     . LEU   B 1 16  ? -8.721  1.443   31.680  1.00 49.32  ?  16  LEU   B O     1 
ATOM   2572 C  CB    . LEU   B 1 16  ? -7.844  0.142   28.891  1.00 52.65  ?  16  LEU   B CB    1 
ATOM   2573 C  CG    . LEU   B 1 16  ? -6.900  -0.393  27.794  1.00 54.34  ?  16  LEU   B CG    1 
ATOM   2574 C  CD1   . LEU   B 1 16  ? -7.472  -1.620  27.100  1.00 56.22  ?  16  LEU   B CD1   1 
ATOM   2575 C  CD2   . LEU   B 1 16  ? -6.623  0.667   26.750  1.00 54.79  ?  16  LEU   B CD2   1 
ATOM   2576 N  N     . THR   B 1 17  ? -9.139  2.966   30.067  1.00 48.24  ?  17  THR   B N     1 
ATOM   2577 C  CA    . THR   B 1 17  ? -10.096 3.760   30.825  1.00 48.48  ?  17  THR   B CA    1 
ATOM   2578 C  C     . THR   B 1 17  ? -11.519 3.574   30.267  1.00 50.36  ?  17  THR   B C     1 
ATOM   2579 O  O     . THR   B 1 17  ? -11.706 2.938   29.216  1.00 48.11  ?  17  THR   B O     1 
ATOM   2580 C  CB    . THR   B 1 17  ? -9.722  5.262   30.771  1.00 49.29  ?  17  THR   B CB    1 
ATOM   2581 O  OG1   . THR   B 1 17  ? -10.298 5.871   29.615  1.00 52.16  ?  17  THR   B OG1   1 
ATOM   2582 C  CG2   . THR   B 1 17  ? -8.202  5.478   30.773  1.00 49.74  ?  17  THR   B CG2   1 
ATOM   2583 N  N     . ILE   B 1 18  ? -12.508 4.150   30.956  1.00 51.04  ?  18  ILE   B N     1 
ATOM   2584 C  CA    . ILE   B 1 18  ? -13.902 4.180   30.482  1.00 53.75  ?  18  ILE   B CA    1 
ATOM   2585 C  C     . ILE   B 1 18  ? -13.984 4.883   29.120  1.00 53.83  ?  18  ILE   B C     1 
ATOM   2586 O  O     . ILE   B 1 18  ? -14.897 4.619   28.349  1.00 52.83  ?  18  ILE   B O     1 
ATOM   2587 C  CB    . ILE   B 1 18  ? -14.854 4.870   31.516  1.00 55.74  ?  18  ILE   B CB    1 
ATOM   2588 C  CG1   . ILE   B 1 18  ? -16.305 4.419   31.354  1.00 56.42  ?  18  ILE   B CG1   1 
ATOM   2589 C  CG2   . ILE   B 1 18  ? -14.767 6.390   31.454  1.00 55.79  ?  18  ILE   B CG2   1 
ATOM   2590 C  CD1   . ILE   B 1 18  ? -16.563 3.032   31.901  1.00 57.92  ?  18  ILE   B CD1   1 
ATOM   2591 N  N     . GLY   B 1 19  ? -13.054 5.813   28.870  1.00 56.92  ?  19  GLY   B N     1 
ATOM   2592 C  CA    . GLY   B 1 19  ? -12.917 6.492   27.574  1.00 57.13  ?  19  GLY   B CA    1 
ATOM   2593 C  C     . GLY   B 1 19  ? -12.577 5.527   26.456  1.00 52.09  ?  19  GLY   B C     1 
ATOM   2594 O  O     . GLY   B 1 19  ? -13.304 5.446   25.475  1.00 54.20  ?  19  GLY   B O     1 
ATOM   2595 N  N     . ASN   B 1 20  ? -11.483 4.780   26.633  1.00 55.00  ?  20  ASN   B N     1 
ATOM   2596 C  CA    . ASN   B 1 20  ? -11.093 3.689   25.709  1.00 54.14  ?  20  ASN   B CA    1 
ATOM   2597 C  C     . ASN   B 1 20  ? -12.247 2.692   25.453  1.00 49.04  ?  20  ASN   B C     1 
ATOM   2598 O  O     . ASN   B 1 20  ? -12.450 2.251   24.323  1.00 48.10  ?  20  ASN   B O     1 
ATOM   2599 C  CB    . ASN   B 1 20  ? -9.865  2.912   26.232  1.00 56.18  ?  20  ASN   B CB    1 
ATOM   2600 C  CG    . ASN   B 1 20  ? -8.631  3.790   26.412  1.00 56.74  ?  20  ASN   B CG    1 
ATOM   2601 O  OD1   . ASN   B 1 20  ? -8.169  4.012   27.534  1.00 55.33  ?  20  ASN   B OD1   1 
ATOM   2602 N  ND2   . ASN   B 1 20  ? -8.102  4.301   25.316  1.00 53.68  ?  20  ASN   B ND2   1 
ATOM   2603 N  N     . TYR   B 1 21  ? -13.020 2.386   26.496  1.00 46.05  ?  21  TYR   B N     1 
ATOM   2604 C  CA    . TYR   B 1 21  ? -14.175 1.473   26.395  1.00 45.46  ?  21  TYR   B CA    1 
ATOM   2605 C  C     . TYR   B 1 21  ? -15.330 2.035   25.568  1.00 46.25  ?  21  TYR   B C     1 
ATOM   2606 O  O     . TYR   B 1 21  ? -15.782 1.418   24.603  1.00 48.12  ?  21  TYR   B O     1 
ATOM   2607 C  CB    . TYR   B 1 21  ? -14.712 1.103   27.782  1.00 45.31  ?  21  TYR   B CB    1 
ATOM   2608 C  CG    . TYR   B 1 21  ? -15.838 0.099   27.720  1.00 46.14  ?  21  TYR   B CG    1 
ATOM   2609 C  CD1   . TYR   B 1 21  ? -15.578 -1.245  27.472  1.00 48.72  ?  21  TYR   B CD1   1 
ATOM   2610 C  CD2   . TYR   B 1 21  ? -17.162 0.486   27.878  1.00 49.65  ?  21  TYR   B CD2   1 
ATOM   2611 C  CE1   . TYR   B 1 21  ? -16.600 -2.171  27.405  1.00 49.29  ?  21  TYR   B CE1   1 
ATOM   2612 C  CE2   . TYR   B 1 21  ? -18.190 -0.440  27.818  1.00 49.12  ?  21  TYR   B CE2   1 
ATOM   2613 C  CZ    . TYR   B 1 21  ? -17.896 -1.767  27.583  1.00 48.33  ?  21  TYR   B CZ    1 
ATOM   2614 O  OH    . TYR   B 1 21  ? -18.887 -2.712  27.522  1.00 51.90  ?  21  TYR   B OH    1 
ATOM   2615 N  N     . MET   B 1 22  ? -15.824 3.192   25.983  1.00 49.24  ?  22  MET   B N     1 
ATOM   2616 C  CA    . MET   B 1 22  ? -16.963 3.848   25.324  1.00 54.81  ?  22  MET   B CA    1 
ATOM   2617 C  C     . MET   B 1 22  ? -16.689 4.329   23.885  1.00 55.28  ?  22  MET   B C     1 
ATOM   2618 O  O     . MET   B 1 22  ? -17.590 4.348   23.051  1.00 55.20  ?  22  MET   B O     1 
ATOM   2619 C  CB    . MET   B 1 22  ? -17.433 5.037   26.176  1.00 56.32  ?  22  MET   B CB    1 
ATOM   2620 C  CG    . MET   B 1 22  ? -18.005 4.634   27.520  1.00 61.51  ?  22  MET   B CG    1 
ATOM   2621 S  SD    . MET   B 1 22  ? -19.306 3.381   27.353  1.00 72.53  ?  22  MET   B SD    1 
ATOM   2622 C  CE    . MET   B 1 22  ? -19.736 3.226   29.073  1.00 75.59  ?  22  MET   B CE    1 
ATOM   2623 N  N     . GLY   B 1 23  ? -15.446 4.702   23.599  1.00 54.36  ?  23  GLY   B N     1 
ATOM   2624 C  CA    . GLY   B 1 23  ? -15.068 5.172   22.264  1.00 55.12  ?  23  GLY   B CA    1 
ATOM   2625 C  C     . GLY   B 1 23  ? -14.629 4.113   21.264  1.00 54.01  ?  23  GLY   B C     1 
ATOM   2626 O  O     . GLY   B 1 23  ? -14.591 4.387   20.044  1.00 56.59  ?  23  GLY   B O     1 
ATOM   2627 N  N     . ALA   B 1 24  ? -14.278 2.924   21.771  1.00 48.59  ?  24  ALA   B N     1 
ATOM   2628 C  CA    . ALA   B 1 24  ? -13.722 1.861   20.949  1.00 46.73  ?  24  ALA   B CA    1 
ATOM   2629 C  C     . ALA   B 1 24  ? -14.310 0.511   21.320  1.00 45.45  ?  24  ALA   B C     1 
ATOM   2630 O  O     . ALA   B 1 24  ? -15.237 0.050   20.641  1.00 45.16  ?  24  ALA   B O     1 
ATOM   2631 C  CB    . ALA   B 1 24  ? -12.208 1.863   21.084  1.00 45.18  ?  24  ALA   B CB    1 
ATOM   2632 N  N     . LEU   B 1 25  ? -13.834 -0.073  22.423  1.00 46.03  ?  25  LEU   B N     1 
ATOM   2633 C  CA    . LEU   B 1 25  ? -14.151 -1.470  22.788  1.00 47.19  ?  25  LEU   B CA    1 
ATOM   2634 C  C     . LEU   B 1 25  ? -15.642 -1.797  22.729  1.00 43.94  ?  25  LEU   B C     1 
ATOM   2635 O  O     . LEU   B 1 25  ? -16.030 -2.814  22.173  1.00 44.99  ?  25  LEU   B O     1 
ATOM   2636 C  CB    . LEU   B 1 25  ? -13.596 -1.810  24.171  1.00 45.23  ?  25  LEU   B CB    1 
ATOM   2637 C  CG    . LEU   B 1 25  ? -12.155 -1.347  24.451  1.00 50.03  ?  25  LEU   B CG    1 
ATOM   2638 C  CD1   . LEU   B 1 25  ? -11.670 -1.789  25.842  1.00 50.27  ?  25  LEU   B CD1   1 
ATOM   2639 C  CD2   . LEU   B 1 25  ? -11.186 -1.824  23.371  1.00 49.09  ?  25  LEU   B CD2   1 
ATOM   2640 N  N     . ARG   B 1 26  ? -16.477 -0.935  23.292  1.00 45.20  ?  26  ARG   B N     1 
ATOM   2641 C  CA    . ARG   B 1 26  ? -17.918 -1.190  23.294  1.00 48.62  ?  26  ARG   B CA    1 
ATOM   2642 C  C     . ARG   B 1 26  ? -18.424 -1.471  21.882  1.00 45.91  ?  26  ARG   B C     1 
ATOM   2643 O  O     . ARG   B 1 26  ? -19.225 -2.380  21.691  1.00 48.43  ?  26  ARG   B O     1 
ATOM   2644 C  CB    . ARG   B 1 26  ? -18.683 -0.021  23.899  1.00 54.39  ?  26  ARG   B CB    1 
ATOM   2645 C  CG    . ARG   B 1 26  ? -20.205 -0.142  23.750  1.00 58.44  ?  26  ARG   B CG    1 
ATOM   2646 C  CD    . ARG   B 1 26  ? -20.956 1.085   24.214  1.00 63.45  ?  26  ARG   B CD    1 
ATOM   2647 N  NE    . ARG   B 1 26  ? -20.373 2.329   23.698  1.00 67.86  ?  26  ARG   B NE    1 
ATOM   2648 C  CZ    . ARG   B 1 26  ? -20.955 3.524   23.757  1.00 69.47  ?  26  ARG   B CZ    1 
ATOM   2649 N  NH1   . ARG   B 1 26  ? -20.319 4.586   23.267  1.00 61.33  ?  26  ARG   B NH1   1 
ATOM   2650 N  NH2   . ARG   B 1 26  ? -22.173 3.659   24.292  1.00 70.67  ?  26  ARG   B NH2   1 
ATOM   2651 N  N     . GLN   B 1 27  ? -17.951 -0.691  20.907  1.00 46.88  ?  27  GLN   B N     1 
ATOM   2652 C  CA    . GLN   B 1 27  ? -18.339 -0.884  19.489  1.00 47.89  ?  27  GLN   B CA    1 
ATOM   2653 C  C     . GLN   B 1 27  ? -17.760 -2.204  18.967  1.00 46.49  ?  27  GLN   B C     1 
ATOM   2654 O  O     . GLN   B 1 27  ? -18.459 -2.976  18.322  1.00 44.83  ?  27  GLN   B O     1 
ATOM   2655 C  CB    . GLN   B 1 27  ? -17.896 0.276   18.588  1.00 49.92  ?  27  GLN   B CB    1 
ATOM   2656 C  CG    . GLN   B 1 27  ? -18.714 1.554   18.748  1.00 50.74  ?  27  GLN   B CG    1 
ATOM   2657 C  CD    . GLN   B 1 27  ? -18.610 2.132   20.139  1.00 53.01  ?  27  GLN   B CD    1 
ATOM   2658 O  OE1   . GLN   B 1 27  ? -19.576 2.090   20.898  1.00 56.37  ?  27  GLN   B OE1   1 
ATOM   2659 N  NE2   . GLN   B 1 27  ? -17.419 2.623   20.505  1.00 55.43  ?  27  GLN   B NE2   1 
ATOM   2660 N  N     . TRP   B 1 28  ? -16.491 -2.462  19.302  1.00 42.43  ?  28  TRP   B N     1 
ATOM   2661 C  CA    . TRP   B 1 28  ? -15.808 -3.693  18.913  1.00 43.65  ?  28  TRP   B CA    1 
ATOM   2662 C  C     . TRP   B 1 28  ? -16.674 -4.910  19.218  1.00 41.38  ?  28  TRP   B C     1 
ATOM   2663 O  O     . TRP   B 1 28  ? -16.875 -5.756  18.349  1.00 46.89  ?  28  TRP   B O     1 
ATOM   2664 C  CB    . TRP   B 1 28  ? -14.452 -3.873  19.614  1.00 41.46  ?  28  TRP   B CB    1 
ATOM   2665 C  CG    . TRP   B 1 28  ? -13.401 -2.856  19.296  1.00 41.93  ?  28  TRP   B CG    1 
ATOM   2666 C  CD1   . TRP   B 1 28  ? -13.554 -1.668  18.620  1.00 41.42  ?  28  TRP   B CD1   1 
ATOM   2667 C  CD2   . TRP   B 1 28  ? -12.043 -2.901  19.716  1.00 40.52  ?  28  TRP   B CD2   1 
ATOM   2668 N  NE1   . TRP   B 1 28  ? -12.374 -0.988  18.596  1.00 41.44  ?  28  TRP   B NE1   1 
ATOM   2669 C  CE2   . TRP   B 1 28  ? -11.423 -1.714  19.254  1.00 38.70  ?  28  TRP   B CE2   1 
ATOM   2670 C  CE3   . TRP   B 1 28  ? -11.287 -3.825  20.453  1.00 37.66  ?  28  TRP   B CE3   1 
ATOM   2671 C  CZ2   . TRP   B 1 28  ? -10.064 -1.431  19.489  1.00 39.33  ?  28  TRP   B CZ2   1 
ATOM   2672 C  CZ3   . TRP   B 1 28  ? -9.945  -3.555  20.682  1.00 41.23  ?  28  TRP   B CZ3   1 
ATOM   2673 C  CH2   . TRP   B 1 28  ? -9.344  -2.357  20.200  1.00 39.84  ?  28  TRP   B CH2   1 
ATOM   2674 N  N     . VAL   B 1 29  ? -17.188 -4.961  20.449  1.00 38.49  ?  29  VAL   B N     1 
ATOM   2675 C  CA    . VAL   B 1 29  ? -17.982 -6.105  20.972  1.00 41.83  ?  29  VAL   B CA    1 
ATOM   2676 C  C     . VAL   B 1 29  ? -19.294 -6.286  20.190  1.00 37.76  ?  29  VAL   B C     1 
ATOM   2677 O  O     . VAL   B 1 29  ? -19.673 -7.414  19.853  1.00 38.72  ?  29  VAL   B O     1 
ATOM   2678 C  CB    . VAL   B 1 29  ? -18.269 -5.936  22.488  1.00 40.36  ?  29  VAL   B CB    1 
ATOM   2679 C  CG1   . VAL   B 1 29  ? -19.048 -7.118  23.048  1.00 40.39  ?  29  VAL   B CG1   1 
ATOM   2680 C  CG2   . VAL   B 1 29  ? -16.969 -5.778  23.266  1.00 40.24  ?  29  VAL   B CG2   1 
ATOM   2681 N  N     . ASN   B 1 30  ? -19.927 -5.164  19.862  1.00 39.35  ?  30  ASN   B N     1 
ATOM   2682 C  CA    . ASN   B 1 30  ? -21.244 -5.135  19.189  1.00 43.49  ?  30  ASN   B CA    1 
ATOM   2683 C  C     . ASN   B 1 30  ? -21.194 -5.460  17.691  1.00 42.19  ?  30  ASN   B C     1 
ATOM   2684 O  O     . ASN   B 1 30  ? -22.200 -5.880  17.125  1.00 40.50  ?  30  ASN   B O     1 
ATOM   2685 C  CB    . ASN   B 1 30  ? -21.906 -3.748  19.349  1.00 45.91  ?  30  ASN   B CB    1 
ATOM   2686 C  CG    . ASN   B 1 30  ? -22.233 -3.401  20.803  1.00 49.96  ?  30  ASN   B CG    1 
ATOM   2687 O  OD1   . ASN   B 1 30  ? -22.517 -4.279  21.636  1.00 50.26  ?  30  ASN   B OD1   1 
ATOM   2688 N  ND2   . ASN   B 1 30  ? -22.214 -2.106  21.108  1.00 50.92  ?  30  ASN   B ND2   1 
ATOM   2689 N  N     . MET   B 1 31  ? -20.026 -5.274  17.060  1.00 39.54  ?  31  MET   B N     1 
ATOM   2690 C  CA    . MET   B 1 31  ? -19.874 -5.454  15.596  1.00 38.53  ?  31  MET   B CA    1 
ATOM   2691 C  C     . MET   B 1 31  ? -19.540 -6.883  15.164  1.00 37.99  ?  31  MET   B C     1 
ATOM   2692 O  O     . MET   B 1 31  ? -19.480 -7.147  13.947  1.00 37.86  ?  31  MET   B O     1 
ATOM   2693 C  CB    . MET   B 1 31  ? -18.803 -4.487  15.061  1.00 40.34  ?  31  MET   B CB    1 
ATOM   2694 C  CG    . MET   B 1 31  ? -19.139 -3.009  15.245  1.00 42.12  ?  31  MET   B CG    1 
ATOM   2695 S  SD    . MET   B 1 31  ? -17.752 -1.929  14.840  1.00 44.44  ?  31  MET   B SD    1 
ATOM   2696 C  CE    . MET   B 1 31  ? -18.019 -1.678  13.082  1.00 41.59  ?  31  MET   B CE    1 
ATOM   2697 N  N     . GLN   B 1 32  ? -19.358 -7.789  16.136  1.00 35.62  ?  32  GLN   B N     1 
ATOM   2698 C  CA    . GLN   B 1 32  ? -18.675 -9.071  15.909  1.00 38.52  ?  32  GLN   B CA    1 
ATOM   2699 C  C     . GLN   B 1 32  ? -19.433 -10.031 15.014  1.00 40.20  ?  32  GLN   B C     1 
ATOM   2700 O  O     . GLN   B 1 32  ? -18.809 -10.851 14.352  1.00 43.83  ?  32  GLN   B O     1 
ATOM   2701 C  CB    . GLN   B 1 32  ? -18.340 -9.782  17.229  1.00 38.88  ?  32  GLN   B CB    1 
ATOM   2702 C  CG    . GLN   B 1 32  ? -17.206 -9.141  18.011  1.00 39.76  ?  32  GLN   B CG    1 
ATOM   2703 C  CD    . GLN   B 1 32  ? -16.843 -9.948  19.240  1.00 40.20  ?  32  GLN   B CD    1 
ATOM   2704 O  OE1   . GLN   B 1 32  ? -15.872 -10.708 19.227  1.00 42.61  ?  32  GLN   B OE1   1 
ATOM   2705 N  NE2   . GLN   B 1 32  ? -17.644 -9.811  20.306  1.00 38.74  ?  32  GLN   B NE2   1 
ATOM   2706 N  N     . ASP   B 1 33  ? -20.764 -9.981  15.030  1.00 43.06  ?  33  ASP   B N     1 
ATOM   2707 C  CA    . ASP   B 1 33  ? -21.585 -10.842 14.131  1.00 43.19  ?  33  ASP   B CA    1 
ATOM   2708 C  C     . ASP   B 1 33  ? -21.892 -10.129 12.805  1.00 38.41  ?  33  ASP   B C     1 
ATOM   2709 O  O     . ASP   B 1 33  ? -21.834 -10.745 11.740  1.00 38.37  ?  33  ASP   B O     1 
ATOM   2710 C  CB    . ASP   B 1 33  ? -22.881 -11.289 14.823  1.00 45.49  ?  33  ASP   B CB    1 
ATOM   2711 C  CG    . ASP   B 1 33  ? -22.632 -12.232 15.985  1.00 47.30  ?  33  ASP   B CG    1 
ATOM   2712 O  OD1   . ASP   B 1 33  ? -23.041 -11.893 17.113  1.00 53.86  ?  33  ASP   B OD1   1 
ATOM   2713 O  OD2   . ASP   B 1 33  ? -22.045 -13.314 15.783  1.00 47.47  ?  33  ASP   B OD2   1 
ATOM   2714 N  N     . ASP   B 1 34  ? -22.201 -8.830  12.879  1.00 36.07  ?  34  ASP   B N     1 
ATOM   2715 C  CA    . ASP   B 1 34  ? -22.518 -8.025  11.697  1.00 37.76  ?  34  ASP   B CA    1 
ATOM   2716 C  C     . ASP   B 1 34  ? -21.393 -7.993  10.659  1.00 37.99  ?  34  ASP   B C     1 
ATOM   2717 O  O     . ASP   B 1 34  ? -21.654 -7.993  9.455   1.00 37.12  ?  34  ASP   B O     1 
ATOM   2718 C  CB    . ASP   B 1 34  ? -22.892 -6.590  12.098  1.00 38.57  ?  34  ASP   B CB    1 
ATOM   2719 C  CG    . ASP   B 1 34  ? -24.226 -6.502  12.805  1.00 41.29  ?  34  ASP   B CG    1 
ATOM   2720 O  OD1   . ASP   B 1 34  ? -24.936 -7.554  12.891  1.00 37.17  ?  34  ASP   B OD1   1 
ATOM   2721 O  OD2   . ASP   B 1 34  ? -24.531 -5.370  13.275  1.00 40.07  ?  34  ASP   B OD2   1 
ATOM   2722 N  N     . TYR   B 1 35  ? -20.149 -7.941  11.140  1.00 37.41  ?  35  TYR   B N     1 
ATOM   2723 C  CA    . TYR   B 1 35  ? -18.966 -7.864  10.292  1.00 37.78  ?  35  TYR   B CA    1 
ATOM   2724 C  C     . TYR   B 1 35  ? -17.880 -8.870  10.731  1.00 37.45  ?  35  TYR   B C     1 
ATOM   2725 O  O     . TYR   B 1 35  ? -17.913 -9.412  11.844  1.00 38.68  ?  35  TYR   B O     1 
ATOM   2726 C  CB    . TYR   B 1 35  ? -18.391 -6.441  10.326  1.00 38.70  ?  35  TYR   B CB    1 
ATOM   2727 C  CG    . TYR   B 1 35  ? -19.378 -5.346  10.034  1.00 38.80  ?  35  TYR   B CG    1 
ATOM   2728 C  CD1   . TYR   B 1 35  ? -19.905 -4.561  11.059  1.00 42.24  ?  35  TYR   B CD1   1 
ATOM   2729 C  CD2   . TYR   B 1 35  ? -19.777 -5.068  8.734   1.00 43.09  ?  35  TYR   B CD2   1 
ATOM   2730 C  CE1   . TYR   B 1 35  ? -20.805 -3.525  10.793  1.00 40.51  ?  35  TYR   B CE1   1 
ATOM   2731 C  CE2   . TYR   B 1 35  ? -20.684 -4.043  8.458   1.00 41.88  ?  35  TYR   B CE2   1 
ATOM   2732 C  CZ    . TYR   B 1 35  ? -21.200 -3.280  9.492   1.00 41.42  ?  35  TYR   B CZ    1 
ATOM   2733 O  OH    . TYR   B 1 35  ? -22.107 -2.282  9.248   1.00 39.97  ?  35  TYR   B OH    1 
ATOM   2734 N  N     . HIS   B 1 36  ? -16.924 -9.109  9.842   1.00 35.64  ?  36  HIS   B N     1 
ATOM   2735 C  CA    . HIS   B 1 36  ? -15.705 -9.889  10.134  1.00 32.80  ?  36  HIS   B CA    1 
ATOM   2736 C  C     . HIS   B 1 36  ? -14.712 -8.988  10.845  1.00 30.10  ?  36  HIS   B C     1 
ATOM   2737 O  O     . HIS   B 1 36  ? -14.104 -8.114  10.215  1.00 29.58  ?  36  HIS   B O     1 
ATOM   2738 C  CB    . HIS   B 1 36  ? -15.093 -10.423 8.836   1.00 31.94  ?  36  HIS   B CB    1 
ATOM   2739 C  CG    . HIS   B 1 36  ? -13.870 -11.256 9.042   1.00 31.63  ?  36  HIS   B CG    1 
ATOM   2740 N  ND1   . HIS   B 1 36  ? -13.918 -12.625 9.188   1.00 31.84  ?  36  HIS   B ND1   1 
ATOM   2741 C  CD2   . HIS   B 1 36  ? -12.571 -10.909 9.141   1.00 29.30  ?  36  HIS   B CD2   1 
ATOM   2742 C  CE1   . HIS   B 1 36  ? -12.696 -13.086 9.378   1.00 32.16  ?  36  HIS   B CE1   1 
ATOM   2743 N  NE2   . HIS   B 1 36  ? -11.862 -12.065 9.341   1.00 31.52  ?  36  HIS   B NE2   1 
ATOM   2744 N  N     . CYS   B 1 37  ? -14.557 -9.203  12.158  1.00 28.80  ?  37  CYS   B N     1 
ATOM   2745 C  CA    . CYS   B 1 37  ? -13.832 -8.276  13.044  1.00 29.91  ?  37  CYS   B CA    1 
ATOM   2746 C  C     . CYS   B 1 37  ? -12.449 -8.808  13.411  1.00 28.06  ?  37  CYS   B C     1 
ATOM   2747 O  O     . CYS   B 1 37  ? -12.287 -9.992  13.746  1.00 27.57  ?  37  CYS   B O     1 
ATOM   2748 C  CB    . CYS   B 1 37  ? -14.649 -8.029  14.312  1.00 34.18  ?  37  CYS   B CB    1 
ATOM   2749 S  SG    . CYS   B 1 37  ? -16.201 -7.171  14.009  1.00 34.94  ?  37  CYS   B SG    1 
ATOM   2750 N  N     . ILE   B 1 38  ? -11.453 -7.938  13.320  1.00 27.62  ?  38  ILE   B N     1 
ATOM   2751 C  CA    . ILE   B 1 38  ? -10.045 -8.288  13.619  1.00 25.55  ?  38  ILE   B CA    1 
ATOM   2752 C  C     . ILE   B 1 38  ? -9.553  -7.235  14.611  1.00 27.77  ?  38  ILE   B C     1 
ATOM   2753 O  O     . ILE   B 1 38  ? -9.557  -6.000  14.294  1.00 30.95  ?  38  ILE   B O     1 
ATOM   2754 C  CB    . ILE   B 1 38  ? -9.177  -8.303  12.337  1.00 23.73  ?  38  ILE   B CB    1 
ATOM   2755 C  CG1   . ILE   B 1 38  ? -9.693  -9.304  11.310  1.00 23.25  ?  38  ILE   B CG1   1 
ATOM   2756 C  CG2   . ILE   B 1 38  ? -7.687  -8.599  12.653  1.00 22.12  ?  38  ILE   B CG2   1 
ATOM   2757 C  CD1   . ILE   B 1 38  ? -9.302  -8.990  9.884   1.00 24.86  ?  38  ILE   B CD1   1 
ATOM   2758 N  N     . TYR   B 1 39  ? -9.176  -7.688  15.810  1.00 27.51  ?  39  TYR   B N     1 
ATOM   2759 C  CA    . TYR   B 1 39  ? -8.717  -6.810  16.897  1.00 27.05  ?  39  TYR   B CA    1 
ATOM   2760 C  C     . TYR   B 1 39  ? -7.253  -7.138  17.231  1.00 28.90  ?  39  TYR   B C     1 
ATOM   2761 O  O     . TYR   B 1 39  ? -6.879  -8.322  17.361  1.00 27.48  ?  39  TYR   B O     1 
ATOM   2762 C  CB    . TYR   B 1 39  ? -9.638  -6.942  18.117  1.00 28.47  ?  39  TYR   B CB    1 
ATOM   2763 C  CG    . TYR   B 1 39  ? -11.067 -6.558  17.760  1.00 29.22  ?  39  TYR   B CG    1 
ATOM   2764 C  CD1   . TYR   B 1 39  ? -11.369 -5.267  17.319  1.00 31.28  ?  39  TYR   B CD1   1 
ATOM   2765 C  CD2   . TYR   B 1 39  ? -12.081 -7.479  17.812  1.00 29.95  ?  39  TYR   B CD2   1 
ATOM   2766 C  CE1   . TYR   B 1 39  ? -12.666 -4.915  16.964  1.00 33.11  ?  39  TYR   B CE1   1 
ATOM   2767 C  CE2   . TYR   B 1 39  ? -13.391 -7.140  17.487  1.00 31.93  ?  39  TYR   B CE2   1 
ATOM   2768 C  CZ    . TYR   B 1 39  ? -13.677 -5.862  17.051  1.00 32.14  ?  39  TYR   B CZ    1 
ATOM   2769 O  OH    . TYR   B 1 39  ? -14.962 -5.536  16.686  1.00 35.83  ?  39  TYR   B OH    1 
ATOM   2770 N  N     . CYS   B 1 40  ? -6.446  -6.094  17.346  1.00 28.08  ?  40  CYS   B N     1 
ATOM   2771 C  CA    . CYS   B 1 40  ? -4.997  -6.191  17.440  1.00 33.90  ?  40  CYS   B CA    1 
ATOM   2772 C  C     . CYS   B 1 40  ? -4.478  -5.461  18.679  1.00 34.10  ?  40  CYS   B C     1 
ATOM   2773 O  O     . CYS   B 1 40  ? -4.857  -4.308  18.917  1.00 33.69  ?  40  CYS   B O     1 
ATOM   2774 C  CB    . CYS   B 1 40  ? -4.334  -5.608  16.184  1.00 32.81  ?  40  CYS   B CB    1 
ATOM   2775 S  SG    . CYS   B 1 40  ? -2.547  -5.834  16.130  1.00 36.99  ?  40  CYS   B SG    1 
ATOM   2776 N  N     . ILE   B 1 41  ? -3.595  -6.126  19.434  1.00 34.81  ?  41  ILE   B N     1 
ATOM   2777 C  CA    . ILE   B 1 41  ? -2.834  -5.484  20.524  1.00 37.32  ?  41  ILE   B CA    1 
ATOM   2778 C  C     . ILE   B 1 41  ? -1.541  -4.944  19.910  1.00 36.37  ?  41  ILE   B C     1 
ATOM   2779 O  O     . ILE   B 1 41  ? -0.653  -5.718  19.608  1.00 37.90  ?  41  ILE   B O     1 
ATOM   2780 C  CB    . ILE   B 1 41  ? -2.564  -6.474  21.680  1.00 36.98  ?  41  ILE   B CB    1 
ATOM   2781 C  CG1   . ILE   B 1 41  ? -3.914  -6.976  22.240  1.00 38.91  ?  41  ILE   B CG1   1 
ATOM   2782 C  CG2   . ILE   B 1 41  ? -1.741  -5.815  22.776  1.00 37.72  ?  41  ILE   B CG2   1 
ATOM   2783 C  CD1   . ILE   B 1 41  ? -3.811  -8.186  23.124  1.00 41.51  ?  41  ILE   B CD1   1 
ATOM   2784 N  N     . VAL   B 1 42  ? -1.451  -3.609  19.771  1.00 33.25  ?  42  VAL   B N     1 
ATOM   2785 C  CA    . VAL   B 1 42  ? -0.403  -2.964  18.984  1.00 33.36  ?  42  VAL   B CA    1 
ATOM   2786 C  C     . VAL   B 1 42  ? 0.849   -2.649  19.824  1.00 33.31  ?  42  VAL   B C     1 
ATOM   2787 O  O     . VAL   B 1 42  ? 1.148   -1.475  20.102  1.00 27.72  ?  42  VAL   B O     1 
ATOM   2788 C  CB    . VAL   B 1 42  ? -0.905  -1.707  18.219  1.00 33.35  ?  42  VAL   B CB    1 
ATOM   2789 C  CG1   . VAL   B 1 42  ? -1.824  -2.124  17.095  1.00 39.02  ?  42  VAL   B CG1   1 
ATOM   2790 C  CG2   . VAL   B 1 42  ? -1.615  -0.720  19.108  1.00 34.72  ?  42  VAL   B CG2   1 
ATOM   2791 N  N     . ASP   B 1 43  ? 1.564   -3.710  20.209  1.00 30.77  ?  43  ASP   B N     1 
ATOM   2792 C  CA    . ASP   B 1 43  ? 2.795   -3.595  21.024  1.00 32.43  ?  43  ASP   B CA    1 
ATOM   2793 C  C     . ASP   B 1 43  ? 3.951   -2.851  20.309  1.00 32.51  ?  43  ASP   B C     1 
ATOM   2794 O  O     . ASP   B 1 43  ? 4.743   -2.109  20.939  1.00 35.10  ?  43  ASP   B O     1 
ATOM   2795 C  CB    . ASP   B 1 43  ? 3.244   -4.974  21.551  1.00 30.38  ?  43  ASP   B CB    1 
ATOM   2796 C  CG    . ASP   B 1 43  ? 3.450   -6.009  20.443  1.00 31.01  ?  43  ASP   B CG    1 
ATOM   2797 O  OD1   . ASP   B 1 43  ? 3.045   -5.760  19.281  1.00 27.74  ?  43  ASP   B OD1   1 
ATOM   2798 O  OD2   . ASP   B 1 43  ? 4.042   -7.067  20.759  1.00 31.36  ?  43  ASP   B OD2   1 
ATOM   2799 N  N     . GLN   B 1 44  ? 4.016   -3.006  18.990  1.00 29.08  ?  44  GLN   B N     1 
ATOM   2800 C  CA    . GLN   B 1 44  ? 4.932   -2.213  18.162  1.00 27.72  ?  44  GLN   B CA    1 
ATOM   2801 C  C     . GLN   B 1 44  ? 4.668   -0.690  18.196  1.00 27.08  ?  44  GLN   B C     1 
ATOM   2802 O  O     . GLN   B 1 44  ? 5.630   0.088   18.238  1.00 26.28  ?  44  GLN   B O     1 
ATOM   2803 C  CB    . GLN   B 1 44  ? 4.982   -2.720  16.723  1.00 25.19  ?  44  GLN   B CB    1 
ATOM   2804 C  CG    . GLN   B 1 44  ? 5.754   -4.032  16.590  1.00 25.85  ?  44  GLN   B CG    1 
ATOM   2805 C  CD    . GLN   B 1 44  ? 5.687   -4.582  15.181  1.00 23.41  ?  44  GLN   B CD    1 
ATOM   2806 O  OE1   . GLN   B 1 44  ? 4.625   -4.897  14.697  1.00 24.22  ?  44  GLN   B OE1   1 
ATOM   2807 N  NE2   . GLN   B 1 44  ? 6.801   -4.671  14.527  1.00 23.70  ?  44  GLN   B NE2   1 
ATOM   2808 N  N     . HIS   B 1 45  ? 3.389   -0.292  18.233  1.00 25.89  ?  45  HIS   B N     1 
ATOM   2809 C  CA    . HIS   B 1 45  ? 3.020   1.138   18.412  1.00 27.79  ?  45  HIS   B CA    1 
ATOM   2810 C  C     . HIS   B 1 45  ? 3.344   1.666   19.832  1.00 29.03  ?  45  HIS   B C     1 
ATOM   2811 O  O     . HIS   B 1 45  ? 3.717   2.838   19.983  1.00 30.14  ?  45  HIS   B O     1 
ATOM   2812 C  CB    . HIS   B 1 45  ? 1.535   1.387   18.077  1.00 29.51  ?  45  HIS   B CB    1 
ATOM   2813 C  CG    . HIS   B 1 45  ? 1.285   1.661   16.629  1.00 29.88  ?  45  HIS   B CG    1 
ATOM   2814 N  ND1   . HIS   B 1 45  ? 0.731   0.735   15.767  1.00 27.13  ?  45  HIS   B ND1   1 
ATOM   2815 C  CD2   . HIS   B 1 45  ? 1.554   2.758   15.885  1.00 32.08  ?  45  HIS   B CD2   1 
ATOM   2816 C  CE1   . HIS   B 1 45  ? 0.658   1.265   14.559  1.00 29.31  ?  45  HIS   B CE1   1 
ATOM   2817 N  NE2   . HIS   B 1 45  ? 1.148   2.494   14.604  1.00 29.12  ?  45  HIS   B NE2   1 
ATOM   2818 N  N     . ALA   B 1 46  ? 3.225   0.796   20.839  1.00 27.17  ?  46  ALA   B N     1 
ATOM   2819 C  CA    . ALA   B 1 46  ? 3.406   1.144   22.246  1.00 29.94  ?  46  ALA   B CA    1 
ATOM   2820 C  C     . ALA   B 1 46  ? 4.814   1.589   22.595  1.00 33.39  ?  46  ALA   B C     1 
ATOM   2821 O  O     . ALA   B 1 46  ? 4.985   2.399   23.497  1.00 36.29  ?  46  ALA   B O     1 
ATOM   2822 C  CB    . ALA   B 1 46  ? 3.016   -0.036  23.123  1.00 31.18  ?  46  ALA   B CB    1 
ATOM   2823 N  N     . ILE   B 1 47  ? 5.810   1.049   21.889  1.00 34.82  ?  47  ILE   B N     1 
ATOM   2824 C  CA    . ILE   B 1 47  ? 7.229   1.324   22.144  1.00 34.81  ?  47  ILE   B CA    1 
ATOM   2825 C  C     . ILE   B 1 47  ? 7.709   2.632   21.527  1.00 34.57  ?  47  ILE   B C     1 
ATOM   2826 O  O     . ILE   B 1 47  ? 8.891   2.938   21.576  1.00 37.57  ?  47  ILE   B O     1 
ATOM   2827 C  CB    . ILE   B 1 47  ? 8.155   0.166   21.698  1.00 33.47  ?  47  ILE   B CB    1 
ATOM   2828 C  CG1   . ILE   B 1 47  ? 8.044   -0.094  20.185  1.00 33.19  ?  47  ILE   B CG1   1 
ATOM   2829 C  CG2   . ILE   B 1 47  ? 7.806   -1.087  22.486  1.00 35.33  ?  47  ILE   B CG2   1 
ATOM   2830 C  CD1   . ILE   B 1 47  ? 9.297   -0.683  19.557  1.00 36.09  ?  47  ILE   B CD1   1 
ATOM   2831 N  N     . THR   B 1 48  ? 6.804   3.400   20.924  1.00 34.71  ?  48  THR   B N     1 
ATOM   2832 C  CA    . THR   B 1 48  ? 7.089   4.808   20.569  1.00 34.54  ?  48  THR   B CA    1 
ATOM   2833 C  C     . THR   B 1 48  ? 7.222   5.729   21.799  1.00 37.95  ?  48  THR   B C     1 
ATOM   2834 O  O     . THR   B 1 48  ? 7.713   6.856   21.678  1.00 35.17  ?  48  THR   B O     1 
ATOM   2835 C  CB    . THR   B 1 48  ? 6.006   5.378   19.650  1.00 35.89  ?  48  THR   B CB    1 
ATOM   2836 O  OG1   . THR   B 1 48  ? 4.724   5.191   20.254  1.00 34.99  ?  48  THR   B OG1   1 
ATOM   2837 C  CG2   . THR   B 1 48  ? 6.051   4.696   18.263  1.00 38.24  ?  48  THR   B CG2   1 
ATOM   2838 N  N     . VAL   B 1 49  ? 6.712   5.268   22.953  1.00 43.11  ?  49  VAL   B N     1 
ATOM   2839 C  CA    . VAL   B 1 49  ? 6.999   5.844   24.267  1.00 42.92  ?  49  VAL   B CA    1 
ATOM   2840 C  C     . VAL   B 1 49  ? 7.745   4.764   25.046  1.00 45.12  ?  49  VAL   B C     1 
ATOM   2841 O  O     . VAL   B 1 49  ? 7.334   3.605   25.028  1.00 41.79  ?  49  VAL   B O     1 
ATOM   2842 C  CB    . VAL   B 1 49  ? 5.690   6.239   24.998  1.00 46.62  ?  49  VAL   B CB    1 
ATOM   2843 C  CG1   . VAL   B 1 49  ? 5.940   6.649   26.448  1.00 48.50  ?  49  VAL   B CG1   1 
ATOM   2844 C  CG2   . VAL   B 1 49  ? 4.989   7.366   24.245  1.00 46.92  ?  49  VAL   B CG2   1 
ATOM   2845 N  N     . ARG   B 1 50  ? 8.818   5.155   25.741  1.00 44.19  ?  50  ARG   B N     1 
ATOM   2846 C  CA    . ARG   B 1 50  ? 9.733   4.209   26.369  1.00 46.65  ?  50  ARG   B CA    1 
ATOM   2847 C  C     . ARG   B 1 50  ? 9.022   3.419   27.480  1.00 44.05  ?  50  ARG   B C     1 
ATOM   2848 O  O     . ARG   B 1 50  ? 8.386   3.999   28.336  1.00 43.16  ?  50  ARG   B O     1 
ATOM   2849 C  CB    . ARG   B 1 50  ? 10.970  4.937   26.916  1.00 48.72  ?  50  ARG   B CB    1 
ATOM   2850 C  CG    . ARG   B 1 50  ? 12.135  4.028   27.306  1.00 52.29  ?  50  ARG   B CG    1 
ATOM   2851 C  CD    . ARG   B 1 50  ? 12.543  3.059   26.201  1.00 50.83  ?  50  ARG   B CD    1 
ATOM   2852 N  NE    . ARG   B 1 50  ? 12.786  3.729   24.918  1.00 51.03  ?  50  ARG   B NE    1 
ATOM   2853 C  CZ    . ARG   B 1 50  ? 13.891  4.409   24.597  1.00 50.50  ?  50  ARG   B CZ    1 
ATOM   2854 N  NH1   . ARG   B 1 50  ? 13.991  4.972   23.391  1.00 50.36  ?  50  ARG   B NH1   1 
ATOM   2855 N  NH2   . ARG   B 1 50  ? 14.896  4.536   25.465  1.00 51.08  ?  50  ARG   B NH2   1 
ATOM   2856 N  N     . GLN   B 1 51  ? 9.124   2.092   27.430  1.00 44.13  ?  51  GLN   B N     1 
ATOM   2857 C  CA    . GLN   B 1 51  ? 8.444   1.186   28.356  1.00 43.19  ?  51  GLN   B CA    1 
ATOM   2858 C  C     . GLN   B 1 51  ? 9.465   0.348   29.121  1.00 40.40  ?  51  GLN   B C     1 
ATOM   2859 O  O     . GLN   B 1 51  ? 10.482  -0.023  28.571  1.00 39.56  ?  51  GLN   B O     1 
ATOM   2860 C  CB    . GLN   B 1 51  ? 7.539   0.205   27.584  1.00 43.21  ?  51  GLN   B CB    1 
ATOM   2861 C  CG    . GLN   B 1 51  ? 6.526   0.822   26.647  1.00 45.22  ?  51  GLN   B CG    1 
ATOM   2862 C  CD    . GLN   B 1 51  ? 5.380   1.488   27.383  1.00 47.98  ?  51  GLN   B CD    1 
ATOM   2863 O  OE1   . GLN   B 1 51  ? 4.780   0.896   28.273  1.00 47.33  ?  51  GLN   B OE1   1 
ATOM   2864 N  NE2   . GLN   B 1 51  ? 5.079   2.739   27.018  1.00 49.43  ?  51  GLN   B NE2   1 
ATOM   2865 N  N     . ASP   B 1 52  ? 9.184   0.067   30.388  1.00 37.88  ?  52  ASP   B N     1 
ATOM   2866 C  CA    . ASP   B 1 52  ? 9.866   -0.974  31.135  1.00 40.62  ?  52  ASP   B CA    1 
ATOM   2867 C  C     . ASP   B 1 52  ? 9.510   -2.357  30.491  1.00 40.53  ?  52  ASP   B C     1 
ATOM   2868 O  O     . ASP   B 1 52  ? 8.338   -2.658  30.250  1.00 38.19  ?  52  ASP   B O     1 
ATOM   2869 C  CB    . ASP   B 1 52  ? 9.425   -0.919  32.607  1.00 41.40  ?  52  ASP   B CB    1 
ATOM   2870 C  CG    . ASP   B 1 52  ? 10.019  -2.014  33.430  1.00 42.97  ?  52  ASP   B CG    1 
ATOM   2871 O  OD1   . ASP   B 1 52  ? 11.124  -1.821  33.981  1.00 49.14  ?  52  ASP   B OD1   1 
ATOM   2872 O  OD2   . ASP   B 1 52  ? 9.372   -3.082  33.538  1.00 48.40  ?  52  ASP   B OD2   1 
ATOM   2873 N  N     . ALA   B 1 53  ? 10.517  -3.178  30.218  1.00 35.25  ?  53  ALA   B N     1 
ATOM   2874 C  CA    . ALA   B 1 53  ? 10.325  -4.416  29.471  1.00 37.37  ?  53  ALA   B CA    1 
ATOM   2875 C  C     . ALA   B 1 53  ? 9.296   -5.351  30.131  1.00 38.79  ?  53  ALA   B C     1 
ATOM   2876 O  O     . ALA   B 1 53  ? 8.455   -5.932  29.438  1.00 35.21  ?  53  ALA   B O     1 
ATOM   2877 C  CB    . ALA   B 1 53  ? 11.649  -5.132  29.289  1.00 39.60  ?  53  ALA   B CB    1 
ATOM   2878 N  N     . GLN   B 1 54  ? 9.351   -5.467  31.462  1.00 37.38  ?  54  GLN   B N     1 
ATOM   2879 C  CA    . GLN   B 1 54  ? 8.406   -6.298  32.208  1.00 38.66  ?  54  GLN   B CA    1 
ATOM   2880 C  C     . GLN   B 1 54  ? 6.987   -5.720  32.171  1.00 38.99  ?  54  GLN   B C     1 
ATOM   2881 O  O     . GLN   B 1 54  ? 6.024   -6.474  32.012  1.00 37.91  ?  54  GLN   B O     1 
ATOM   2882 C  CB    . GLN   B 1 54  ? 8.872   -6.519  33.656  1.00 44.37  ?  54  GLN   B CB    1 
ATOM   2883 C  CG    . GLN   B 1 54  ? 9.851   -7.674  33.829  1.00 46.51  ?  54  GLN   B CG    1 
ATOM   2884 C  CD    . GLN   B 1 54  ? 11.175  -7.424  33.131  1.00 47.73  ?  54  GLN   B CD    1 
ATOM   2885 O  OE1   . GLN   B 1 54  ? 11.865  -6.444  33.408  1.00 53.71  ?  54  GLN   B OE1   1 
ATOM   2886 N  NE2   . GLN   B 1 54  ? 11.538  -8.307  32.206  1.00 54.38  ?  54  GLN   B NE2   1 
ATOM   2887 N  N     . LYS   B 1 55  ? 6.869   -4.389  32.291  1.00 37.17  ?  55  LYS   B N     1 
ATOM   2888 C  CA    . LYS   B 1 55  ? 5.578   -3.694  32.195  1.00 38.70  ?  55  LYS   B CA    1 
ATOM   2889 C  C     . LYS   B 1 55  ? 4.881   -3.934  30.868  1.00 35.43  ?  55  LYS   B C     1 
ATOM   2890 O  O     . LYS   B 1 55  ? 3.673   -4.150  30.856  1.00 35.81  ?  55  LYS   B O     1 
ATOM   2891 C  CB    . LYS   B 1 55  ? 5.708   -2.175  32.442  1.00 42.70  ?  55  LYS   B CB    1 
ATOM   2892 C  CG    . LYS   B 1 55  ? 5.810   -1.811  33.923  1.00 50.32  ?  55  LYS   B CG    1 
ATOM   2893 C  CD    . LYS   B 1 55  ? 5.881   -0.297  34.160  1.00 57.14  ?  55  LYS   B CD    1 
ATOM   2894 C  CE    . LYS   B 1 55  ? 4.511   0.381   34.151  1.00 62.08  ?  55  LYS   B CE    1 
ATOM   2895 N  NZ    . LYS   B 1 55  ? 4.441   1.503   35.138  1.00 68.69  ?  55  LYS   B NZ    1 
ATOM   2896 N  N     . LEU   B 1 56  ? 5.643   -3.893  29.775  1.00 34.41  ?  56  LEU   B N     1 
ATOM   2897 C  CA    . LEU   B 1 56  ? 5.110   -4.109  28.411  1.00 33.38  ?  56  LEU   B CA    1 
ATOM   2898 C  C     . LEU   B 1 56  ? 4.548   -5.524  28.206  1.00 31.41  ?  56  LEU   B C     1 
ATOM   2899 O  O     . LEU   B 1 56  ? 3.430   -5.704  27.718  1.00 31.58  ?  56  LEU   B O     1 
ATOM   2900 C  CB    . LEU   B 1 56  ? 6.203   -3.831  27.387  1.00 33.44  ?  56  LEU   B CB    1 
ATOM   2901 C  CG    . LEU   B 1 56  ? 5.832   -3.822  25.889  1.00 33.99  ?  56  LEU   B CG    1 
ATOM   2902 C  CD1   . LEU   B 1 56  ? 4.692   -2.863  25.596  1.00 32.79  ?  56  LEU   B CD1   1 
ATOM   2903 C  CD2   . LEU   B 1 56  ? 7.048   -3.435  25.050  1.00 34.11  ?  56  LEU   B CD2   1 
ATOM   2904 N  N     . ARG   B 1 57  ? 5.330   -6.520  28.598  1.00 33.12  ?  57  ARG   B N     1 
ATOM   2905 C  CA    . ARG   B 1 57  ? 4.904   -7.918  28.511  1.00 32.86  ?  57  ARG   B CA    1 
ATOM   2906 C  C     . ARG   B 1 57  ? 3.606   -8.127  29.286  1.00 36.23  ?  57  ARG   B C     1 
ATOM   2907 O  O     . ARG   B 1 57  ? 2.624   -8.662  28.739  1.00 31.82  ?  57  ARG   B O     1 
ATOM   2908 C  CB    . ARG   B 1 57  ? 5.988   -8.871  29.033  1.00 34.58  ?  57  ARG   B CB    1 
ATOM   2909 C  CG    . ARG   B 1 57  ? 5.733   -10.333 28.667  1.00 33.97  ?  57  ARG   B CG    1 
ATOM   2910 C  CD    . ARG   B 1 57  ? 7.021   -11.129 28.588  1.00 36.47  ?  57  ARG   B CD    1 
ATOM   2911 N  NE    . ARG   B 1 57  ? 7.866   -10.681 27.491  1.00 37.08  ?  57  ARG   B NE    1 
ATOM   2912 C  CZ    . ARG   B 1 57  ? 9.139   -11.014 27.335  1.00 40.57  ?  57  ARG   B CZ    1 
ATOM   2913 N  NH1   . ARG   B 1 57  ? 9.745   -11.823 28.207  1.00 47.62  ?  57  ARG   B NH1   1 
ATOM   2914 N  NH2   . ARG   B 1 57  ? 9.833   -10.534 26.308  1.00 39.02  ?  57  ARG   B NH2   1 
ATOM   2915 N  N     . LYS   B 1 58  ? 3.608   -7.696  30.551  1.00 35.24  ?  58  LYS   B N     1 
ATOM   2916 C  CA    . LYS   B 1 58  ? 2.437   -7.794  31.413  1.00 35.40  ?  58  LYS   B CA    1 
ATOM   2917 C  C     . LYS   B 1 58  ? 1.237   -7.031  30.864  1.00 33.08  ?  58  LYS   B C     1 
ATOM   2918 O  O     . LYS   B 1 58  ? 0.138   -7.575  30.831  1.00 32.90  ?  58  LYS   B O     1 
ATOM   2919 C  CB    . LYS   B 1 58  ? 2.762   -7.297  32.831  1.00 37.11  ?  58  LYS   B CB    1 
ATOM   2920 C  CG    . LYS   B 1 58  ? 1.640   -7.509  33.845  1.00 39.79  ?  58  LYS   B CG    1 
ATOM   2921 C  CD    . LYS   B 1 58  ? 2.173   -7.478  35.297  1.00 43.37  ?  58  LYS   B CD    1 
ATOM   2922 C  CE    . LYS   B 1 58  ? 1.076   -7.639  36.340  1.00 45.04  ?  58  LYS   B CE    1 
ATOM   2923 N  NZ    . LYS   B 1 58  ? -0.142  -6.839  36.038  1.00 48.78  ?  58  LYS   B NZ    1 
ATOM   2924 N  N     . ALA   B 1 59  ? 1.466   -5.798  30.412  1.00 30.36  ?  59  ALA   B N     1 
ATOM   2925 C  CA    . ALA   B 1 59  ? 0.419   -4.954  29.837  1.00 31.88  ?  59  ALA   B CA    1 
ATOM   2926 C  C     . ALA   B 1 59  ? -0.173  -5.491  28.538  1.00 32.47  ?  59  ALA   B C     1 
ATOM   2927 O  O     . ALA   B 1 59  ? -1.331  -5.204  28.242  1.00 29.97  ?  59  ALA   B O     1 
ATOM   2928 C  CB    . ALA   B 1 59  ? 0.931   -3.542  29.609  1.00 30.43  ?  59  ALA   B CB    1 
ATOM   2929 N  N     . THR   B 1 60  ? 0.621   -6.248  27.771  1.00 34.05  ?  60  THR   B N     1 
ATOM   2930 C  CA    . THR   B 1 60  ? 0.161   -6.895  26.531  1.00 34.44  ?  60  THR   B CA    1 
ATOM   2931 C  C     . THR   B 1 60  ? -0.847  -7.979  26.880  1.00 33.76  ?  60  THR   B C     1 
ATOM   2932 O  O     . THR   B 1 60  ? -1.910  -8.057  26.281  1.00 35.52  ?  60  THR   B O     1 
ATOM   2933 C  CB    . THR   B 1 60  ? 1.355   -7.458  25.692  1.00 34.35  ?  60  THR   B CB    1 
ATOM   2934 O  OG1   . THR   B 1 60  ? 2.268   -6.391  25.394  1.00 29.39  ?  60  THR   B OG1   1 
ATOM   2935 C  CG2   . THR   B 1 60  ? 0.906   -8.075  24.387  1.00 33.89  ?  60  THR   B CG2   1 
ATOM   2936 N  N     . LEU   B 1 61  ? -0.531  -8.785  27.883  1.00 38.19  ?  61  LEU   B N     1 
ATOM   2937 C  CA    . LEU   B 1 61  ? -1.434  -9.856  28.342  1.00 36.57  ?  61  LEU   B CA    1 
ATOM   2938 C  C     . LEU   B 1 61  ? -2.646  -9.298  29.134  1.00 35.69  ?  61  LEU   B C     1 
ATOM   2939 O  O     . LEU   B 1 61  ? -3.754  -9.827  29.050  1.00 35.88  ?  61  LEU   B O     1 
ATOM   2940 C  CB    . LEU   B 1 61  ? -0.637  -10.876 29.169  1.00 36.63  ?  61  LEU   B CB    1 
ATOM   2941 C  CG    . LEU   B 1 61  ? 0.541   -11.536 28.467  1.00 36.25  ?  61  LEU   B CG    1 
ATOM   2942 C  CD1   . LEU   B 1 61  ? 1.392   -12.347 29.438  1.00 39.54  ?  61  LEU   B CD1   1 
ATOM   2943 C  CD2   . LEU   B 1 61  ? 0.082   -12.423 27.319  1.00 35.54  ?  61  LEU   B CD2   1 
ATOM   2944 N  N     . ASP   B 1 62  ? -2.444  -8.199  29.861  1.00 37.39  ?  62  ASP   B N     1 
ATOM   2945 C  CA    . ASP   B 1 62  ? -3.569  -7.447  30.488  1.00 39.04  ?  62  ASP   B CA    1 
ATOM   2946 C  C     . ASP   B 1 62  ? -4.591  -6.982  29.429  1.00 37.80  ?  62  ASP   B C     1 
ATOM   2947 O  O     . ASP   B 1 62  ? -5.798  -7.141  29.593  1.00 37.60  ?  62  ASP   B O     1 
ATOM   2948 C  CB    . ASP   B 1 62  ? -3.068  -6.220  31.267  1.00 38.10  ?  62  ASP   B CB    1 
ATOM   2949 C  CG    . ASP   B 1 62  ? -2.269  -6.579  32.508  1.00 38.44  ?  62  ASP   B CG    1 
ATOM   2950 O  OD1   . ASP   B 1 62  ? -1.584  -5.680  33.020  1.00 40.50  ?  62  ASP   B OD1   1 
ATOM   2951 O  OD2   . ASP   B 1 62  ? -2.313  -7.740  32.972  1.00 38.20  ?  62  ASP   B OD2   1 
ATOM   2952 N  N     . THR   B 1 63  ? -4.082  -6.399  28.344  1.00 40.99  ?  63  THR   B N     1 
ATOM   2953 C  CA    . THR   B 1 63  ? -4.922  -5.881  27.258  1.00 39.61  ?  63  THR   B CA    1 
ATOM   2954 C  C     . THR   B 1 63  ? -5.717  -7.010  26.586  1.00 37.59  ?  63  THR   B C     1 
ATOM   2955 O  O     . THR   B 1 63  ? -6.904  -6.854  26.331  1.00 36.50  ?  63  THR   B O     1 
ATOM   2956 C  CB    . THR   B 1 63  ? -4.083  -5.113  26.243  1.00 37.81  ?  63  THR   B CB    1 
ATOM   2957 O  OG1   . THR   B 1 63  ? -3.358  -4.084  26.943  1.00 36.33  ?  63  THR   B OG1   1 
ATOM   2958 C  CG2   . THR   B 1 63  ? -4.941  -4.483  25.159  1.00 38.34  ?  63  THR   B CG2   1 
ATOM   2959 N  N     . LEU   B 1 64  ? -5.064  -8.149  26.357  1.00 36.50  ?  64  LEU   B N     1 
ATOM   2960 C  CA    . LEU   B 1 64  ? -5.715  -9.325  25.797  1.00 36.52  ?  64  LEU   B CA    1 
ATOM   2961 C  C     . LEU   B 1 64  ? -6.873  -9.787  26.677  1.00 34.02  ?  64  LEU   B C     1 
ATOM   2962 O  O     . LEU   B 1 64  ? -7.978  -9.959  26.181  1.00 33.70  ?  64  LEU   B O     1 
ATOM   2963 C  CB    . LEU   B 1 64  ? -4.702  -10.460 25.594  1.00 38.91  ?  64  LEU   B CB    1 
ATOM   2964 C  CG    . LEU   B 1 64  ? -5.265  -11.793 25.106  1.00 39.63  ?  64  LEU   B CG    1 
ATOM   2965 C  CD1   . LEU   B 1 64  ? -5.877  -11.657 23.724  1.00 40.40  ?  64  LEU   B CD1   1 
ATOM   2966 C  CD2   . LEU   B 1 64  ? -4.177  -12.850 25.119  1.00 41.30  ?  64  LEU   B CD2   1 
ATOM   2967 N  N     . ALA   B 1 65  ? -6.601  -9.978  27.977  1.00 30.71  ?  65  ALA   B N     1 
ATOM   2968 C  CA    . ALA   B 1 65  ? -7.603  -10.421 28.939  1.00 30.27  ?  65  ALA   B CA    1 
ATOM   2969 C  C     . ALA   B 1 65  ? -8.744  -9.412  29.078  1.00 30.27  ?  65  ALA   B C     1 
ATOM   2970 O  O     . ALA   B 1 65  ? -9.892  -9.794  29.254  1.00 29.67  ?  65  ALA   B O     1 
ATOM   2971 C  CB    . ALA   B 1 65  ? -6.967  -10.709 30.299  1.00 30.66  ?  65  ALA   B CB    1 
ATOM   2972 N  N     . LEU   B 1 66  ? -8.421  -8.123  28.970  1.00 32.52  ?  66  LEU   B N     1 
ATOM   2973 C  CA    . LEU   B 1 66  ? -9.432  -7.073  29.017  1.00 32.22  ?  66  LEU   B CA    1 
ATOM   2974 C  C     . LEU   B 1 66  ? -10.391 -7.111  27.809  1.00 32.50  ?  66  LEU   B C     1 
ATOM   2975 O  O     . LEU   B 1 66  ? -11.611 -6.959  27.971  1.00 31.88  ?  66  LEU   B O     1 
ATOM   2976 C  CB    . LEU   B 1 66  ? -8.772  -5.698  29.169  1.00 35.43  ?  66  LEU   B CB    1 
ATOM   2977 C  CG    . LEU   B 1 66  ? -9.677  -4.540  29.581  1.00 41.32  ?  66  LEU   B CG    1 
ATOM   2978 C  CD1   . LEU   B 1 66  ? -10.643 -4.924  30.695  1.00 44.63  ?  66  LEU   B CD1   1 
ATOM   2979 C  CD2   . LEU   B 1 66  ? -8.835  -3.360  30.058  1.00 45.11  ?  66  LEU   B CD2   1 
ATOM   2980 N  N     . TYR   B 1 67  ? -9.841  -7.343  26.618  1.00 33.39  ?  67  TYR   B N     1 
ATOM   2981 C  CA    . TYR   B 1 67  ? -10.642 -7.569  25.404  1.00 33.49  ?  67  TYR   B CA    1 
ATOM   2982 C  C     . TYR   B 1 67  ? -11.624 -8.713  25.581  1.00 32.66  ?  67  TYR   B C     1 
ATOM   2983 O  O     . TYR   B 1 67  ? -12.818 -8.562  25.296  1.00 32.78  ?  67  TYR   B O     1 
ATOM   2984 C  CB    . TYR   B 1 67  ? -9.758  -7.933  24.212  1.00 34.13  ?  67  TYR   B CB    1 
ATOM   2985 C  CG    . TYR   B 1 67  ? -8.897  -6.867  23.606  1.00 35.93  ?  67  TYR   B CG    1 
ATOM   2986 C  CD1   . TYR   B 1 67  ? -8.777  -5.582  24.157  1.00 38.69  ?  67  TYR   B CD1   1 
ATOM   2987 C  CD2   . TYR   B 1 67  ? -8.156  -7.161  22.454  1.00 38.14  ?  67  TYR   B CD2   1 
ATOM   2988 C  CE1   . TYR   B 1 67  ? -7.945  -4.621  23.567  1.00 39.22  ?  67  TYR   B CE1   1 
ATOM   2989 C  CE2   . TYR   B 1 67  ? -7.342  -6.218  21.864  1.00 38.97  ?  67  TYR   B CE2   1 
ATOM   2990 C  CZ    . TYR   B 1 67  ? -7.219  -4.959  22.413  1.00 39.18  ?  67  TYR   B CZ    1 
ATOM   2991 O  OH    . TYR   B 1 67  ? -6.380  -4.076  21.757  1.00 37.29  ?  67  TYR   B OH    1 
ATOM   2992 N  N     . LEU   B 1 68  ? -11.118 -9.850  26.058  1.00 30.81  ?  68  LEU   B N     1 
ATOM   2993 C  CA    . LEU   B 1 68  ? -11.939 -11.034 26.291  1.00 32.06  ?  68  LEU   B CA    1 
ATOM   2994 C  C     . LEU   B 1 68  ? -13.029 -10.772 27.337  1.00 35.61  ?  68  LEU   B C     1 
ATOM   2995 O  O     . LEU   B 1 68  ? -14.188 -11.123 27.105  1.00 37.49  ?  68  LEU   B O     1 
ATOM   2996 C  CB    . LEU   B 1 68  ? -11.061 -12.219 26.687  1.00 33.33  ?  68  LEU   B CB    1 
ATOM   2997 C  CG    . LEU   B 1 68  ? -10.134 -12.726 25.568  1.00 35.53  ?  68  LEU   B CG    1 
ATOM   2998 C  CD1   . LEU   B 1 68  ? -8.994  -13.571 26.105  1.00 36.88  ?  68  LEU   B CD1   1 
ATOM   2999 C  CD2   . LEU   B 1 68  ? -10.910 -13.539 24.556  1.00 34.62  ?  68  LEU   B CD2   1 
ATOM   3000 N  N     . ALA   B 1 69  ? -12.665 -10.093 28.433  1.00 35.77  ?  69  ALA   B N     1 
ATOM   3001 C  CA    . ALA   B 1 69  ? -13.591 -9.721  29.502  1.00 36.28  ?  69  ALA   B CA    1 
ATOM   3002 C  C     . ALA   B 1 69  ? -14.660 -8.726  29.032  1.00 37.53  ?  69  ALA   B C     1 
ATOM   3003 O  O     . ALA   B 1 69  ? -15.774 -8.760  29.497  1.00 36.78  ?  69  ALA   B O     1 
ATOM   3004 C  CB    . ALA   B 1 69  ? -12.823 -9.142  30.681  1.00 37.27  ?  69  ALA   B CB    1 
ATOM   3005 N  N     . CYS   B 1 70  ? -14.312 -7.853  28.091  1.00 42.55  ?  70  CYS   B N     1 
ATOM   3006 C  CA    . CYS   B 1 70  ? -15.270 -6.901  27.477  1.00 39.46  ?  70  CYS   B CA    1 
ATOM   3007 C  C     . CYS   B 1 70  ? -16.334 -7.581  26.614  1.00 38.40  ?  70  CYS   B C     1 
ATOM   3008 O  O     . CYS   B 1 70  ? -17.364 -6.989  26.336  1.00 38.40  ?  70  CYS   B O     1 
ATOM   3009 C  CB    . CYS   B 1 70  ? -14.538 -5.848  26.661  1.00 41.13  ?  70  CYS   B CB    1 
ATOM   3010 S  SG    . CYS   B 1 70  ? -13.833 -4.518  27.637  1.00 47.01  ?  70  CYS   B SG    1 
ATOM   3011 N  N     . GLY   B 1 71  ? -16.090 -8.831  26.219  1.00 36.50  ?  71  GLY   B N     1 
ATOM   3012 C  CA    . GLY   B 1 71  ? -16.989 -9.606  25.376  1.00 33.79  ?  71  GLY   B CA    1 
ATOM   3013 C  C     . GLY   B 1 71  ? -16.469 -9.890  23.965  1.00 34.63  ?  71  GLY   B C     1 
ATOM   3014 O  O     . GLY   B 1 71  ? -17.215 -10.413 23.139  1.00 32.79  ?  71  GLY   B O     1 
ATOM   3015 N  N     . ILE   B 1 72  ? -15.205 -9.579  23.681  1.00 31.92  ?  72  ILE   B N     1 
ATOM   3016 C  CA    . ILE   B 1 72  ? -14.584 -9.992  22.416  1.00 32.08  ?  72  ILE   B CA    1 
ATOM   3017 C  C     . ILE   B 1 72  ? -14.445 -11.525 22.446  1.00 34.50  ?  72  ILE   B C     1 
ATOM   3018 O  O     . ILE   B 1 72  ? -13.874 -12.079 23.387  1.00 33.90  ?  72  ILE   B O     1 
ATOM   3019 C  CB    . ILE   B 1 72  ? -13.191 -9.352  22.176  1.00 33.38  ?  72  ILE   B CB    1 
ATOM   3020 C  CG1   . ILE   B 1 72  ? -13.235 -7.811  22.234  1.00 33.97  ?  72  ILE   B CG1   1 
ATOM   3021 C  CG2   . ILE   B 1 72  ? -12.621 -9.785  20.827  1.00 32.60  ?  72  ILE   B CG2   1 
ATOM   3022 C  CD1   . ILE   B 1 72  ? -14.144 -7.170  21.208  1.00 36.98  ?  72  ILE   B CD1   1 
ATOM   3023 N  N     . ASP   B 1 73  ? -14.951 -12.172 21.399  1.00 35.29  ?  73  ASP   B N     1 
ATOM   3024 C  CA    . ASP   B 1 73  ? -15.105 -13.622 21.334  1.00 36.84  ?  73  ASP   B CA    1 
ATOM   3025 C  C     . ASP   B 1 73  ? -14.057 -14.153 20.351  1.00 37.37  ?  73  ASP   B C     1 
ATOM   3026 O  O     . ASP   B 1 73  ? -14.152 -13.909 19.133  1.00 34.12  ?  73  ASP   B O     1 
ATOM   3027 C  CB    . ASP   B 1 73  ? -16.542 -13.989 20.904  1.00 39.96  ?  73  ASP   B CB    1 
ATOM   3028 C  CG    . ASP   B 1 73  ? -16.868 -15.501 21.049  1.00 44.24  ?  73  ASP   B CG    1 
ATOM   3029 O  OD1   . ASP   B 1 73  ? -15.980 -16.327 21.366  1.00 47.80  ?  73  ASP   B OD1   1 
ATOM   3030 O  OD2   . ASP   B 1 73  ? -18.041 -15.862 20.834  1.00 45.47  ?  73  ASP   B OD2   1 
ATOM   3031 N  N     . PRO   B 1 74  ? -13.063 -14.910 20.858  1.00 36.45  ?  74  PRO   B N     1 
ATOM   3032 C  CA    . PRO   B 1 74  ? -12.090 -15.526 19.958  1.00 40.09  ?  74  PRO   B CA    1 
ATOM   3033 C  C     . PRO   B 1 74  ? -12.697 -16.531 18.938  1.00 39.47  ?  74  PRO   B C     1 
ATOM   3034 O  O     . PRO   B 1 74  ? -12.045 -16.861 17.972  1.00 37.42  ?  74  PRO   B O     1 
ATOM   3035 C  CB    . PRO   B 1 74  ? -11.125 -16.240 20.917  1.00 40.15  ?  74  PRO   B CB    1 
ATOM   3036 C  CG    . PRO   B 1 74  ? -11.936 -16.527 22.119  1.00 40.56  ?  74  PRO   B CG    1 
ATOM   3037 C  CD    . PRO   B 1 74  ? -12.891 -15.374 22.241  1.00 38.97  ?  74  PRO   B CD    1 
ATOM   3038 N  N     . GLU   B 1 75  ? -13.921 -17.007 19.164  1.00 43.85  ?  75  GLU   B N     1 
ATOM   3039 C  CA    . GLU   B 1 75  ? -14.629 -17.879 18.208  1.00 43.53  ?  75  GLU   B CA    1 
ATOM   3040 C  C     . GLU   B 1 75  ? -15.288 -17.093 17.059  1.00 44.21  ?  75  GLU   B C     1 
ATOM   3041 O  O     . GLU   B 1 75  ? -15.608 -17.668 16.030  1.00 49.73  ?  75  GLU   B O     1 
ATOM   3042 C  CB    . GLU   B 1 75  ? -15.677 -18.720 18.949  1.00 45.05  ?  75  GLU   B CB    1 
ATOM   3043 N  N     . LYS   B 1 76  ? -15.493 -15.786 17.245  1.00 41.73  ?  76  LYS   B N     1 
ATOM   3044 C  CA    . LYS   B 1 76  ? -16.104 -14.896 16.242  1.00 40.19  ?  76  LYS   B CA    1 
ATOM   3045 C  C     . LYS   B 1 76  ? -15.085 -13.951 15.565  1.00 39.91  ?  76  LYS   B C     1 
ATOM   3046 O  O     . LYS   B 1 76  ? -15.127 -13.757 14.354  1.00 39.08  ?  76  LYS   B O     1 
ATOM   3047 C  CB    . LYS   B 1 76  ? -17.220 -14.068 16.898  1.00 41.89  ?  76  LYS   B CB    1 
ATOM   3048 C  CG    . LYS   B 1 76  ? -18.455 -14.877 17.307  1.00 42.41  ?  76  LYS   B CG    1 
ATOM   3049 C  CD    . LYS   B 1 76  ? -19.529 -14.000 17.940  1.00 44.76  ?  76  LYS   B CD    1 
ATOM   3050 C  CE    . LYS   B 1 76  ? -20.719 -14.822 18.427  1.00 46.69  ?  76  LYS   B CE    1 
ATOM   3051 N  NZ    . LYS   B 1 76  ? -21.674 -13.962 19.173  1.00 46.99  ?  76  LYS   B NZ    1 
ATOM   3052 N  N     . SER   B 1 77  ? -14.175 -13.388 16.362  1.00 35.72  ?  77  SER   B N     1 
ATOM   3053 C  CA    . SER   B 1 77  ? -13.183 -12.422 15.911  1.00 36.34  ?  77  SER   B CA    1 
ATOM   3054 C  C     . SER   B 1 77  ? -11.762 -12.985 15.971  1.00 30.60  ?  77  SER   B C     1 
ATOM   3055 O  O     . SER   B 1 77  ? -11.487 -13.916 16.719  1.00 27.08  ?  77  SER   B O     1 
ATOM   3056 C  CB    . SER   B 1 77  ? -13.278 -11.159 16.772  1.00 36.78  ?  77  SER   B CB    1 
ATOM   3057 O  OG    . SER   B 1 77  ? -14.618 -10.702 16.818  1.00 34.86  ?  77  SER   B OG    1 
ATOM   3058 N  N     . THR   B 1 78  ? -10.882 -12.398 15.170  1.00 32.61  ?  78  THR   B N     1 
ATOM   3059 C  CA    . THR   B 1 78  ? -9.434  -12.629 15.234  1.00 33.26  ?  78  THR   B CA    1 
ATOM   3060 C  C     . THR   B 1 78  ? -8.832  -11.621 16.232  1.00 33.84  ?  78  THR   B C     1 
ATOM   3061 O  O     . THR   B 1 78  ? -9.002  -10.393 16.075  1.00 32.24  ?  78  THR   B O     1 
ATOM   3062 C  CB    . THR   B 1 78  ? -8.785  -12.468 13.840  1.00 32.11  ?  78  THR   B CB    1 
ATOM   3063 O  OG1   . THR   B 1 78  ? -9.378  -13.397 12.923  1.00 33.77  ?  78  THR   B OG1   1 
ATOM   3064 C  CG2   . THR   B 1 78  ? -7.295  -12.761 13.886  1.00 32.32  ?  78  THR   B CG2   1 
ATOM   3065 N  N     . ILE   B 1 79  ? -8.170  -12.152 17.260  1.00 31.71  ?  79  ILE   B N     1 
ATOM   3066 C  CA    . ILE   B 1 79  ? -7.505  -11.366 18.292  1.00 31.21  ?  79  ILE   B CA    1 
ATOM   3067 C  C     . ILE   B 1 79  ? -6.049  -11.800 18.228  1.00 29.82  ?  79  ILE   B C     1 
ATOM   3068 O  O     . ILE   B 1 79  ? -5.755  -13.019 18.351  1.00 26.69  ?  79  ILE   B O     1 
ATOM   3069 C  CB    . ILE   B 1 79  ? -8.069  -11.647 19.708  1.00 32.90  ?  79  ILE   B CB    1 
ATOM   3070 C  CG1   . ILE   B 1 79  ? -9.594  -11.797 19.687  1.00 36.16  ?  79  ILE   B CG1   1 
ATOM   3071 C  CG2   . ILE   B 1 79  ? -7.649  -10.545 20.664  1.00 33.37  ?  79  ILE   B CG2   1 
ATOM   3072 C  CD1   . ILE   B 1 79  ? -10.197 -12.283 20.990  1.00 39.31  ?  79  ILE   B CD1   1 
ATOM   3073 N  N     . PHE   B 1 80  ? -5.147  -10.824 18.037  1.00 28.27  ?  80  PHE   B N     1 
ATOM   3074 C  CA    . PHE   B 1 80  ? -3.688  -11.096 17.884  1.00 27.19  ?  80  PHE   B CA    1 
ATOM   3075 C  C     . PHE   B 1 80  ? -2.850  -9.918  18.341  1.00 27.46  ?  80  PHE   B C     1 
ATOM   3076 O  O     . PHE   B 1 80  ? -3.356  -8.786  18.476  1.00 26.01  ?  80  PHE   B O     1 
ATOM   3077 C  CB    . PHE   B 1 80  ? -3.319  -11.487 16.422  1.00 27.66  ?  80  PHE   B CB    1 
ATOM   3078 C  CG    . PHE   B 1 80  ? -3.305  -10.322 15.463  1.00 27.46  ?  80  PHE   B CG    1 
ATOM   3079 C  CD1   . PHE   B 1 80  ? -4.504  -9.764  15.009  1.00 25.43  ?  80  PHE   B CD1   1 
ATOM   3080 C  CD2   . PHE   B 1 80  ? -2.105  -9.791  15.004  1.00 24.36  ?  80  PHE   B CD2   1 
ATOM   3081 C  CE1   . PHE   B 1 80  ? -4.497  -8.689  14.143  1.00 26.59  ?  80  PHE   B CE1   1 
ATOM   3082 C  CE2   . PHE   B 1 80  ? -2.097  -8.701  14.143  1.00 26.49  ?  80  PHE   B CE2   1 
ATOM   3083 C  CZ    . PHE   B 1 80  ? -3.302  -8.165  13.695  1.00 28.97  ?  80  PHE   B CZ    1 
ATOM   3084 N  N     . VAL   B 1 81  ? -1.584  -10.225 18.633  1.00 28.27  ?  81  VAL   B N     1 
ATOM   3085 C  CA    . VAL   B 1 81  ? -0.568  -9.242  19.029  1.00 27.65  ?  81  VAL   B CA    1 
ATOM   3086 C  C     . VAL   B 1 81  ? 0.205   -8.843  17.763  1.00 26.31  ?  81  VAL   B C     1 
ATOM   3087 O  O     . VAL   B 1 81  ? 0.692   -9.705  17.026  1.00 25.26  ?  81  VAL   B O     1 
ATOM   3088 C  CB    . VAL   B 1 81  ? 0.330   -9.845  20.137  1.00 24.16  ?  81  VAL   B CB    1 
ATOM   3089 C  CG1   . VAL   B 1 81  ? 1.477   -8.937  20.505  1.00 24.42  ?  81  VAL   B CG1   1 
ATOM   3090 C  CG2   . VAL   B 1 81  ? -0.527  -10.132 21.378  1.00 22.16  ?  81  VAL   B CG2   1 
ATOM   3091 N  N     . GLN   B 1 82  ? 0.332   -7.528  17.537  1.00 22.86  ?  82  GLN   B N     1 
ATOM   3092 C  CA    . GLN   B 1 82  ? 0.841   -6.961  16.305  1.00 23.10  ?  82  GLN   B CA    1 
ATOM   3093 C  C     . GLN   B 1 82  ? 2.212   -7.504  15.897  1.00 21.85  ?  82  GLN   B C     1 
ATOM   3094 O  O     . GLN   B 1 82  ? 2.475   -7.724  14.704  1.00 22.93  ?  82  GLN   B O     1 
ATOM   3095 C  CB    . GLN   B 1 82  ? 0.952   -5.416  16.491  1.00 22.88  ?  82  GLN   B CB    1 
ATOM   3096 C  CG    . GLN   B 1 82  ? 1.185   -4.618  15.245  1.00 23.53  ?  82  GLN   B CG    1 
ATOM   3097 C  CD    . GLN   B 1 82  ? 1.434   -3.143  15.551  1.00 27.04  ?  82  GLN   B CD    1 
ATOM   3098 O  OE1   . GLN   B 1 82  ? 1.727   -2.761  16.703  1.00 28.44  ?  82  GLN   B OE1   1 
ATOM   3099 N  NE2   . GLN   B 1 82  ? 1.353   -2.315  14.520  1.00 27.74  ?  82  GLN   B NE2   1 
ATOM   3100 N  N     . SER   B 1 83  ? 3.101   -7.675  16.872  1.00 20.24  ?  83  SER   B N     1 
ATOM   3101 C  CA    . SER   B 1 83  ? 4.503   -8.082  16.621  1.00 19.67  ?  83  SER   B CA    1 
ATOM   3102 C  C     . SER   B 1 83  ? 4.635   -9.557  16.241  1.00 20.83  ?  83  SER   B C     1 
ATOM   3103 O  O     . SER   B 1 83  ? 5.685   -9.957  15.824  1.00 21.01  ?  83  SER   B O     1 
ATOM   3104 C  CB    . SER   B 1 83  ? 5.408   -7.771  17.825  1.00 23.00  ?  83  SER   B CB    1 
ATOM   3105 O  OG    . SER   B 1 83  ? 5.138   -8.597  18.970  1.00 22.78  ?  83  SER   B OG    1 
ATOM   3106 N  N     . HIS   B 1 84  ? 3.553   -10.329 16.348  1.00 22.01  ?  84  HIS   B N     1 
ATOM   3107 C  CA    . HIS   B 1 84  ? 3.539   -11.767 15.991  1.00 23.06  ?  84  HIS   B CA    1 
ATOM   3108 C  C     . HIS   B 1 84  ? 3.322   -11.972 14.486  1.00 23.57  ?  84  HIS   B C     1 
ATOM   3109 O  O     . HIS   B 1 84  ? 3.365   -13.098 14.011  1.00 25.02  ?  84  HIS   B O     1 
ATOM   3110 C  CB    . HIS   B 1 84  ? 2.457   -12.520 16.773  1.00 24.18  ?  84  HIS   B CB    1 
ATOM   3111 C  CG    . HIS   B 1 84  ? 2.678   -12.558 18.253  1.00 23.89  ?  84  HIS   B CG    1 
ATOM   3112 N  ND1   . HIS   B 1 84  ? 1.858   -13.260 19.101  1.00 23.23  ?  84  HIS   B ND1   1 
ATOM   3113 C  CD2   . HIS   B 1 84  ? 3.614   -11.971 19.039  1.00 25.70  ?  84  HIS   B CD2   1 
ATOM   3114 C  CE1   . HIS   B 1 84  ? 2.278   -13.121 20.345  1.00 24.01  ?  84  HIS   B CE1   1 
ATOM   3115 N  NE2   . HIS   B 1 84  ? 3.331   -12.328 20.341  1.00 21.99  ?  84  HIS   B NE2   1 
ATOM   3116 N  N     . VAL   B 1 85  ? 3.081   -10.882 13.759  1.00 23.92  ?  85  VAL   B N     1 
ATOM   3117 C  CA    . VAL   B 1 85  ? 2.792   -10.875 12.323  1.00 23.56  ?  85  VAL   B CA    1 
ATOM   3118 C  C     . VAL   B 1 85  ? 3.749   -9.915  11.625  1.00 21.96  ?  85  VAL   B C     1 
ATOM   3119 O  O     . VAL   B 1 85  ? 3.493   -8.689  11.582  1.00 23.61  ?  85  VAL   B O     1 
ATOM   3120 C  CB    . VAL   B 1 85  ? 1.312   -10.453 12.089  1.00 24.06  ?  85  VAL   B CB    1 
ATOM   3121 C  CG1   . VAL   B 1 85  ? 0.969   -10.378 10.598  1.00 23.97  ?  85  VAL   B CG1   1 
ATOM   3122 C  CG2   . VAL   B 1 85  ? 0.369   -11.406 12.818  1.00 23.18  ?  85  VAL   B CG2   1 
ATOM   3123 N  N     . PRO   B 1 86  ? 4.862   -10.434 11.076  1.00 22.65  ?  86  PRO   B N     1 
ATOM   3124 C  CA    . PRO   B 1 86  ? 5.860   -9.575  10.465  1.00 21.80  ?  86  PRO   B CA    1 
ATOM   3125 C  C     . PRO   B 1 86  ? 5.366   -8.672  9.342   1.00 21.24  ?  86  PRO   B C     1 
ATOM   3126 O  O     . PRO   B 1 86  ? 6.023   -7.671  9.053   1.00 17.95  ?  86  PRO   B O     1 
ATOM   3127 C  CB    . PRO   B 1 86  ? 6.892   -10.575 9.923   1.00 22.96  ?  86  PRO   B CB    1 
ATOM   3128 C  CG    . PRO   B 1 86  ? 6.739   -11.770 10.792  1.00 21.94  ?  86  PRO   B CG    1 
ATOM   3129 C  CD    . PRO   B 1 86  ? 5.284   -11.853 11.032  1.00 22.93  ?  86  PRO   B CD    1 
ATOM   3130 N  N     . GLU   B 1 87  ? 4.216   -9.000  8.756   1.00 20.18  ?  87  GLU   B N     1 
ATOM   3131 C  CA    . GLU   B 1 87  ? 3.679   -8.274  7.608   1.00 22.24  ?  87  GLU   B CA    1 
ATOM   3132 C  C     . GLU   B 1 87  ? 3.409   -6.811  7.894   1.00 19.08  ?  87  GLU   B C     1 
ATOM   3133 O  O     . GLU   B 1 87  ? 3.503   -6.022  6.990   1.00 20.41  ?  87  GLU   B O     1 
ATOM   3134 C  CB    . GLU   B 1 87  ? 2.418   -8.964  7.041   1.00 22.98  ?  87  GLU   B CB    1 
ATOM   3135 C  CG    . GLU   B 1 87  ? 2.707   -10.232 6.248   1.00 24.73  ?  87  GLU   B CG    1 
ATOM   3136 C  CD    . GLU   B 1 87  ? 2.849   -11.480 7.083   1.00 26.18  ?  87  GLU   B CD    1 
ATOM   3137 O  OE1   . GLU   B 1 87  ? 2.922   -11.432 8.333   1.00 27.25  ?  87  GLU   B OE1   1 
ATOM   3138 O  OE2   . GLU   B 1 87  ? 2.837   -12.557 6.474   1.00 35.24  ?  87  GLU   B OE2   1 
ATOM   3139 N  N     . HIS   B 1 88  ? 3.094   -6.487  9.162   1.00 21.74  ?  88  HIS   B N     1 
ATOM   3140 C  CA    . HIS   B 1 88  ? 2.882   -5.125  9.634   1.00 20.41  ?  88  HIS   B CA    1 
ATOM   3141 C  C     . HIS   B 1 88  ? 4.075   -4.221  9.449   1.00 23.26  ?  88  HIS   B C     1 
ATOM   3142 O  O     . HIS   B 1 88  ? 3.946   -3.096  8.888   1.00 26.33  ?  88  HIS   B O     1 
ATOM   3143 C  CB    . HIS   B 1 88  ? 2.395   -5.136  11.122  1.00 24.06  ?  88  HIS   B CB    1 
ATOM   3144 C  CG    . HIS   B 1 88  ? 1.029   -5.716  11.304  1.00 24.36  ?  88  HIS   B CG    1 
ATOM   3145 N  ND1   . HIS   B 1 88  ? -0.067  -4.950  11.622  1.00 26.58  ?  88  HIS   B ND1   1 
ATOM   3146 C  CD2   . HIS   B 1 88  ? 0.580   -6.989  11.199  1.00 24.99  ?  88  HIS   B CD2   1 
ATOM   3147 C  CE1   . HIS   B 1 88  ? -1.134  -5.724  11.702  1.00 26.93  ?  88  HIS   B CE1   1 
ATOM   3148 N  NE2   . HIS   B 1 88  ? -0.772  -6.967  11.435  1.00 26.16  ?  88  HIS   B NE2   1 
ATOM   3149 N  N     . ALA   B 1 89  ? 5.248   -4.679  9.902   1.00 25.84  ?  89  ALA   B N     1 
ATOM   3150 C  CA    . ALA   B 1 89  ? 6.502   -3.920  9.742   1.00 22.24  ?  89  ALA   B CA    1 
ATOM   3151 C  C     . ALA   B 1 89  ? 6.927   -3.894  8.232   1.00 24.19  ?  89  ALA   B C     1 
ATOM   3152 O  O     . ALA   B 1 89  ? 7.416   -2.874  7.722   1.00 21.06  ?  89  ALA   B O     1 
ATOM   3153 C  CB    . ALA   B 1 89  ? 7.588   -4.525  10.591  1.00 23.60  ?  89  ALA   B CB    1 
ATOM   3154 N  N     . GLN   B 1 90  ? 6.692   -4.993  7.531   1.00 20.75  ?  90  GLN   B N     1 
ATOM   3155 C  CA    . GLN   B 1 90  ? 7.060   -5.115  6.109   1.00 23.22  ?  90  GLN   B CA    1 
ATOM   3156 C  C     . GLN   B 1 90  ? 6.262   -4.130  5.240   1.00 24.29  ?  90  GLN   B C     1 
ATOM   3157 O  O     . GLN   B 1 90  ? 6.840   -3.358  4.487   1.00 28.03  ?  90  GLN   B O     1 
ATOM   3158 C  CB    . GLN   B 1 90  ? 6.787   -6.526  5.618   1.00 24.98  ?  90  GLN   B CB    1 
ATOM   3159 C  CG    . GLN   B 1 90  ? 7.718   -7.578  6.171   1.00 23.78  ?  90  GLN   B CG    1 
ATOM   3160 C  CD    . GLN   B 1 90  ? 7.351   -8.966  5.696   1.00 22.99  ?  90  GLN   B CD    1 
ATOM   3161 O  OE1   . GLN   B 1 90  ? 6.450   -9.590  6.253   1.00 27.84  ?  90  GLN   B OE1   1 
ATOM   3162 N  NE2   . GLN   B 1 90  ? 8.037   -9.452  4.683   1.00 22.69  ?  90  GLN   B NE2   1 
ATOM   3163 N  N     . LEU   B 1 91  ? 4.940   -4.110  5.414   1.00 25.30  ?  91  LEU   B N     1 
ATOM   3164 C  CA    . LEU   B 1 91  ? 4.100   -3.199  4.665   1.00 26.34  ?  91  LEU   B CA    1 
ATOM   3165 C  C     . LEU   B 1 91  ? 4.378   -1.770  5.074   1.00 24.11  ?  91  LEU   B C     1 
ATOM   3166 O  O     . LEU   B 1 91  ? 4.379   -0.871  4.219   1.00 23.78  ?  91  LEU   B O     1 
ATOM   3167 C  CB    . LEU   B 1 91  ? 2.602   -3.525  4.829   1.00 27.85  ?  91  LEU   B CB    1 
ATOM   3168 C  CG    . LEU   B 1 91  ? 1.643   -2.622  4.026   1.00 28.82  ?  91  LEU   B CG    1 
ATOM   3169 C  CD1   . LEU   B 1 91  ? 2.020   -2.560  2.552   1.00 29.94  ?  91  LEU   B CD1   1 
ATOM   3170 C  CD2   . LEU   B 1 91  ? 0.205   -3.102  4.183   1.00 30.98  ?  91  LEU   B CD2   1 
ATOM   3171 N  N     . GLY   B 1 92  ? 4.611   -1.577  6.375   1.00 22.29  ?  92  GLY   B N     1 
ATOM   3172 C  CA    . GLY   B 1 92  ? 4.935   -0.265  6.938   1.00 25.31  ?  92  GLY   B CA    1 
ATOM   3173 C  C     . GLY   B 1 92  ? 6.129   0.400   6.263   1.00 27.16  ?  92  GLY   B C     1 
ATOM   3174 O  O     . GLY   B 1 92  ? 6.093   1.594   5.994   1.00 31.04  ?  92  GLY   B O     1 
ATOM   3175 N  N     . TRP   B 1 93  ? 7.215   -0.334  6.055   1.00 27.51  ?  93  TRP   B N     1 
ATOM   3176 C  CA    . TRP   B 1 93  ? 8.368   0.206   5.325   1.00 30.04  ?  93  TRP   B CA    1 
ATOM   3177 C  C     . TRP   B 1 93  ? 7.997   0.618   3.894   1.00 31.55  ?  93  TRP   B C     1 
ATOM   3178 O  O     . TRP   B 1 93  ? 8.276   1.749   3.467   1.00 30.15  ?  93  TRP   B O     1 
ATOM   3179 C  CB    . TRP   B 1 93  ? 9.576   -0.758  5.231   1.00 28.89  ?  93  TRP   B CB    1 
ATOM   3180 C  CG    . TRP   B 1 93  ? 10.508  -0.220  4.234   1.00 29.12  ?  93  TRP   B CG    1 
ATOM   3181 C  CD1   . TRP   B 1 93  ? 10.655  -0.640  2.951   1.00 28.50  ?  93  TRP   B CD1   1 
ATOM   3182 C  CD2   . TRP   B 1 93  ? 11.283  0.982   4.355   1.00 28.68  ?  93  TRP   B CD2   1 
ATOM   3183 N  NE1   . TRP   B 1 93  ? 11.513  0.187   2.277   1.00 27.92  ?  93  TRP   B NE1   1 
ATOM   3184 C  CE2   . TRP   B 1 93  ? 11.918  1.191   3.117   1.00 30.55  ?  93  TRP   B CE2   1 
ATOM   3185 C  CE3   . TRP   B 1 93  ? 11.525  1.884   5.403   1.00 32.71  ?  93  TRP   B CE3   1 
ATOM   3186 C  CZ2   . TRP   B 1 93  ? 12.797  2.257   2.893   1.00 32.45  ?  93  TRP   B CZ2   1 
ATOM   3187 C  CZ3   . TRP   B 1 93  ? 12.402  2.970   5.173   1.00 31.41  ?  93  TRP   B CZ3   1 
ATOM   3188 C  CH2   . TRP   B 1 93  ? 13.017  3.135   3.932   1.00 33.67  ?  93  TRP   B CH2   1 
ATOM   3189 N  N     . ALA   B 1 94  ? 7.407   -0.322  3.154   1.00 31.82  ?  94  ALA   B N     1 
ATOM   3190 C  CA    . ALA   B 1 94  ? 6.955   -0.044  1.783   1.00 34.04  ?  94  ALA   B CA    1 
ATOM   3191 C  C     . ALA   B 1 94  ? 6.034   1.189   1.722   1.00 33.08  ?  94  ALA   B C     1 
ATOM   3192 O  O     . ALA   B 1 94  ? 6.156   1.987   0.814   1.00 37.65  ?  94  ALA   B O     1 
ATOM   3193 C  CB    . ALA   B 1 94  ? 6.270   -1.256  1.178   1.00 36.45  ?  94  ALA   B CB    1 
ATOM   3194 N  N     . LEU   B 1 95  ? 5.161   1.343   2.712   1.00 34.98  ?  95  LEU   B N     1 
ATOM   3195 C  CA    . LEU   B 1 95  ? 4.207   2.454   2.768   1.00 35.68  ?  95  LEU   B CA    1 
ATOM   3196 C  C     . LEU   B 1 95  ? 4.849   3.800   3.204   1.00 35.40  ?  95  LEU   B C     1 
ATOM   3197 O  O     . LEU   B 1 95  ? 4.310   4.862   2.904   1.00 38.04  ?  95  LEU   B O     1 
ATOM   3198 C  CB    . LEU   B 1 95  ? 3.028   2.089   3.667   1.00 36.72  ?  95  LEU   B CB    1 
ATOM   3199 C  CG    . LEU   B 1 95  ? 2.023   1.026   3.182   1.00 37.98  ?  95  LEU   B CG    1 
ATOM   3200 C  CD1   . LEU   B 1 95  ? 0.776   1.081   4.059   1.00 39.01  ?  95  LEU   B CD1   1 
ATOM   3201 C  CD2   . LEU   B 1 95  ? 1.634   1.191   1.728   1.00 36.75  ?  95  LEU   B CD2   1 
ATOM   3202 N  N     . ASN   B 1 96  ? 6.002   3.754   3.871   1.00 34.02  ?  96  ASN   B N     1 
ATOM   3203 C  CA    . ASN   B 1 96  ? 6.839   4.957   4.064   1.00 36.79  ?  96  ASN   B CA    1 
ATOM   3204 C  C     . ASN   B 1 96  ? 7.187   5.665   2.744   1.00 36.14  ?  96  ASN   B C     1 
ATOM   3205 O  O     . ASN   B 1 96  ? 7.232   6.895   2.675   1.00 38.00  ?  96  ASN   B O     1 
ATOM   3206 C  CB    . ASN   B 1 96  ? 8.157   4.632   4.798   1.00 37.80  ?  96  ASN   B CB    1 
ATOM   3207 C  CG    . ASN   B 1 96  ? 8.130   4.980   6.261   1.00 40.39  ?  96  ASN   B CG    1 
ATOM   3208 O  OD1   . ASN   B 1 96  ? 7.294   5.729   6.718   1.00 40.29  ?  96  ASN   B OD1   1 
ATOM   3209 N  ND2   . ASN   B 1 96  ? 9.096   4.451   7.011   1.00 44.86  ?  96  ASN   B ND2   1 
ATOM   3210 N  N     . CYS   B 1 97  ? 7.424   4.879   1.706   1.00 36.28  ?  97  CYS   B N     1 
ATOM   3211 C  CA    . CYS   B 1 97  ? 7.849   5.396   0.403   1.00 38.06  ?  97  CYS   B CA    1 
ATOM   3212 C  C     . CYS   B 1 97  ? 6.710   5.999   -0.444  1.00 41.58  ?  97  CYS   B C     1 
ATOM   3213 O  O     . CYS   B 1 97  ? 6.979   6.521   -1.522  1.00 42.99  ?  97  CYS   B O     1 
ATOM   3214 C  CB    . CYS   B 1 97  ? 8.541   4.268   -0.380  1.00 39.19  ?  97  CYS   B CB    1 
ATOM   3215 S  SG    . CYS   B 1 97  ? 9.958   3.503   0.494   1.00 35.05  ?  97  CYS   B SG    1 
ATOM   3216 N  N     . TYR   B 1 98  ? 5.462   5.879   0.036   1.00 40.99  ?  98  TYR   B N     1 
ATOM   3217 C  CA    . TYR   B 1 98  ? 4.271   6.496   -0.553  1.00 42.03  ?  98  TYR   B CA    1 
ATOM   3218 C  C     . TYR   B 1 98  ? 3.588   7.451   0.435   1.00 42.84  ?  98  TYR   B C     1 
ATOM   3219 O  O     . TYR   B 1 98  ? 2.426   7.786   0.274   1.00 44.90  ?  98  TYR   B O     1 
ATOM   3220 C  CB    . TYR   B 1 98  ? 3.305   5.390   -1.024  1.00 40.70  ?  98  TYR   B CB    1 
ATOM   3221 C  CG    . TYR   B 1 98  ? 3.947   4.477   -2.027  1.00 38.90  ?  98  TYR   B CG    1 
ATOM   3222 C  CD1   . TYR   B 1 98  ? 3.937   4.785   -3.388  1.00 39.28  ?  98  TYR   B CD1   1 
ATOM   3223 C  CD2   . TYR   B 1 98  ? 4.599   3.330   -1.624  1.00 37.94  ?  98  TYR   B CD2   1 
ATOM   3224 C  CE1   . TYR   B 1 98  ? 4.544   3.957   -4.309  1.00 39.39  ?  98  TYR   B CE1   1 
ATOM   3225 C  CE2   . TYR   B 1 98  ? 5.214   2.491   -2.546  1.00 39.69  ?  98  TYR   B CE2   1 
ATOM   3226 C  CZ    . TYR   B 1 98  ? 5.189   2.818   -3.881  1.00 38.95  ?  98  TYR   B CZ    1 
ATOM   3227 O  OH    . TYR   B 1 98  ? 5.787   2.003   -4.793  1.00 44.14  ?  98  TYR   B OH    1 
ATOM   3228 N  N     . THR   B 1 99  ? 4.327   7.878   1.456   1.00 45.51  ?  99  THR   B N     1 
ATOM   3229 C  CA    . THR   B 1 99  ? 3.860   8.821   2.478   1.00 47.49  ?  99  THR   B CA    1 
ATOM   3230 C  C     . THR   B 1 99  ? 4.827   9.988   2.486   1.00 52.37  ?  99  THR   B C     1 
ATOM   3231 O  O     . THR   B 1 99  ? 6.034   9.769   2.538   1.00 55.08  ?  99  THR   B O     1 
ATOM   3232 C  CB    . THR   B 1 99  ? 3.865   8.182   3.876   1.00 46.23  ?  99  THR   B CB    1 
ATOM   3233 O  OG1   . THR   B 1 99  ? 3.030   7.010   3.864   1.00 48.20  ?  99  THR   B OG1   1 
ATOM   3234 C  CG2   . THR   B 1 99  ? 3.382   9.165   4.955   1.00 46.12  ?  99  THR   B CG2   1 
ATOM   3235 N  N     . TYR   B 1 100 ? 4.309   11.213  2.458   1.00 53.96  ?  100 TYR   B N     1 
ATOM   3236 C  CA    . TYR   B 1 100 ? 5.152   12.412  2.451   1.00 57.09  ?  100 TYR   B CA    1 
ATOM   3237 C  C     . TYR   B 1 100 ? 5.473   12.861  3.872   1.00 56.10  ?  100 TYR   B C     1 
ATOM   3238 O  O     . TYR   B 1 100 ? 4.687   12.650  4.782   1.00 52.98  ?  100 TYR   B O     1 
ATOM   3239 C  CB    . TYR   B 1 100 ? 4.452   13.562  1.733   1.00 61.37  ?  100 TYR   B CB    1 
ATOM   3240 C  CG    . TYR   B 1 100 ? 4.241   13.393  0.249   1.00 63.90  ?  100 TYR   B CG    1 
ATOM   3241 C  CD1   . TYR   B 1 100 ? 5.134   13.936  -0.657  1.00 68.79  ?  100 TYR   B CD1   1 
ATOM   3242 C  CD2   . TYR   B 1 100 ? 3.128   12.728  -0.251  1.00 66.75  ?  100 TYR   B CD2   1 
ATOM   3243 C  CE1   . TYR   B 1 100 ? 4.948   13.810  -2.024  1.00 69.81  ?  100 TYR   B CE1   1 
ATOM   3244 C  CE2   . TYR   B 1 100 ? 2.930   12.590  -1.616  1.00 68.72  ?  100 TYR   B CE2   1 
ATOM   3245 C  CZ    . TYR   B 1 100 ? 3.846   13.135  -2.498  1.00 70.54  ?  100 TYR   B CZ    1 
ATOM   3246 O  OH    . TYR   B 1 100 ? 3.669   13.013  -3.852  1.00 70.18  ?  100 TYR   B OH    1 
ATOM   3247 N  N     . PHE   B 1 101 ? 6.628   13.500  4.035   1.00 61.14  ?  101 PHE   B N     1 
ATOM   3248 C  CA    . PHE   B 1 101 ? 7.084   14.042  5.323   1.00 59.76  ?  101 PHE   B CA    1 
ATOM   3249 C  C     . PHE   B 1 101 ? 6.071   15.040  5.895   1.00 55.44  ?  101 PHE   B C     1 
ATOM   3250 O  O     . PHE   B 1 101 ? 5.799   15.030  7.101   1.00 57.14  ?  101 PHE   B O     1 
ATOM   3251 C  CB    . PHE   B 1 101 ? 8.474   14.678  5.120   1.00 61.49  ?  101 PHE   B CB    1 
ATOM   3252 C  CG    . PHE   B 1 101 ? 9.116   15.228  6.373   1.00 66.32  ?  101 PHE   B CG    1 
ATOM   3253 C  CD1   . PHE   B 1 101 ? 10.219  14.592  6.945   1.00 66.85  ?  101 PHE   B CD1   1 
ATOM   3254 C  CD2   . PHE   B 1 101 ? 8.658   16.416  6.951   1.00 68.52  ?  101 PHE   B CD2   1 
ATOM   3255 C  CE1   . PHE   B 1 101 ? 10.822  15.115  8.082   1.00 70.96  ?  101 PHE   B CE1   1 
ATOM   3256 C  CE2   . PHE   B 1 101 ? 9.252   16.933  8.088   1.00 70.58  ?  101 PHE   B CE2   1 
ATOM   3257 C  CZ    . PHE   B 1 101 ? 10.336  16.288  8.650   1.00 72.09  ?  101 PHE   B CZ    1 
ATOM   3258 N  N     . GLY   B 1 102 ? 5.512   15.885  5.030   1.00 54.76  ?  102 GLY   B N     1 
ATOM   3259 C  CA    . GLY   B 1 102 ? 4.542   16.910  5.445   1.00 52.71  ?  102 GLY   B CA    1 
ATOM   3260 C  C     . GLY   B 1 102 ? 3.329   16.312  6.131   1.00 54.45  ?  102 GLY   B C     1 
ATOM   3261 O  O     . GLY   B 1 102 ? 2.898   16.778  7.191   1.00 53.01  ?  102 GLY   B O     1 
ATOM   3262 N  N     . GLU   B 1 103 ? 2.813   15.229  5.552   1.00 55.93  ?  103 GLU   B N     1 
ATOM   3263 C  CA    . GLU   B 1 103 ? 1.679   14.503  6.131   1.00 54.50  ?  103 GLU   B CA    1 
ATOM   3264 C  C     . GLU   B 1 103 ? 1.959   14.021  7.563   1.00 56.34  ?  103 GLU   B C     1 
ATOM   3265 O  O     . GLU   B 1 103 ? 1.055   13.995  8.400   1.00 62.87  ?  103 GLU   B O     1 
ATOM   3266 C  CB    . GLU   B 1 103 ? 1.300   13.320  5.247   1.00 57.59  ?  103 GLU   B CB    1 
ATOM   3267 C  CG    . GLU   B 1 103 ? 0.723   13.725  3.902   1.00 58.71  ?  103 GLU   B CG    1 
ATOM   3268 C  CD    . GLU   B 1 103 ? 0.567   12.569  2.930   1.00 59.18  ?  103 GLU   B CD    1 
ATOM   3269 O  OE1   . GLU   B 1 103 ? 1.290   11.552  3.071   1.00 58.43  ?  103 GLU   B OE1   1 
ATOM   3270 O  OE2   . GLU   B 1 103 ? -0.264  12.689  1.999   1.00 54.81  ?  103 GLU   B OE2   1 
ATOM   3271 N  N     . LEU   B 1 104 ? 3.214   13.673  7.853   1.00 52.15  ?  104 LEU   B N     1 
ATOM   3272 C  CA    . LEU   B 1 104 ? 3.624   13.212  9.189   1.00 49.18  ?  104 LEU   B CA    1 
ATOM   3273 C  C     . LEU   B 1 104 ? 3.945   14.328  10.189  1.00 51.28  ?  104 LEU   B C     1 
ATOM   3274 O  O     . LEU   B 1 104 ? 3.599   14.219  11.374  1.00 52.09  ?  104 LEU   B O     1 
ATOM   3275 C  CB    . LEU   B 1 104 ? 4.802   12.239  9.048   1.00 46.33  ?  104 LEU   B CB    1 
ATOM   3276 C  CG    . LEU   B 1 104 ? 4.492   11.003  8.198   1.00 44.81  ?  104 LEU   B CG    1 
ATOM   3277 C  CD1   . LEU   B 1 104 ? 5.697   10.077  8.082   1.00 44.82  ?  104 LEU   B CD1   1 
ATOM   3278 C  CD2   . LEU   B 1 104 ? 3.289   10.248  8.752   1.00 44.58  ?  104 LEU   B CD2   1 
ATOM   3279 N  N     . SER   B 1 105 ? 4.568   15.408  9.713   1.00 56.95  ?  105 SER   B N     1 
ATOM   3280 C  CA    . SER   B 1 105 ? 4.928   16.561  10.579  1.00 61.04  ?  105 SER   B CA    1 
ATOM   3281 C  C     . SER   B 1 105 ? 3.730   17.238  11.271  1.00 63.20  ?  105 SER   B C     1 
ATOM   3282 O  O     . SER   B 1 105 ? 3.829   17.630  12.441  1.00 61.75  ?  105 SER   B O     1 
ATOM   3283 C  CB    . SER   B 1 105 ? 5.724   17.591  9.778   1.00 58.83  ?  105 SER   B CB    1 
ATOM   3284 O  OG    . SER   B 1 105 ? 4.971   18.093  8.706   1.00 62.52  ?  105 SER   B OG    1 
ATOM   3285 N  N     . ARG   B 1 106 ? 2.598   17.292  10.565  1.00 65.00  ?  106 ARG   B N     1 
ATOM   3286 C  CA    . ARG   B 1 106 ? 1.380   17.975  11.033  1.00 72.18  ?  106 ARG   B CA    1 
ATOM   3287 C  C     . ARG   B 1 106 ? 0.538   17.224  12.078  1.00 71.23  ?  106 ARG   B C     1 
ATOM   3288 O  O     . ARG   B 1 106 ? -0.470  17.760  12.552  1.00 69.69  ?  106 ARG   B O     1 
ATOM   3289 C  CB    . ARG   B 1 106 ? 0.479   18.308  9.834   1.00 76.63  ?  106 ARG   B CB    1 
ATOM   3290 C  CG    . ARG   B 1 106 ? -0.077  17.092  9.102   1.00 81.33  ?  106 ARG   B CG    1 
ATOM   3291 C  CD    . ARG   B 1 106 ? -1.151  17.447  8.090   1.00 84.50  ?  106 ARG   B CD    1 
ATOM   3292 N  NE    . ARG   B 1 106 ? -0.594  18.121  6.912   1.00 85.00  ?  106 ARG   B NE    1 
ATOM   3293 C  CZ    . ARG   B 1 106 ? -0.974  17.926  5.647   1.00 80.97  ?  106 ARG   B CZ    1 
ATOM   3294 N  NH1   . ARG   B 1 106 ? -1.929  17.053  5.329   1.00 80.37  ?  106 ARG   B NH1   1 
ATOM   3295 N  NH2   . ARG   B 1 106 ? -0.375  18.610  4.677   1.00 81.95  ?  106 ARG   B NH2   1 
ATOM   3296 N  N     . MET   B 1 107 ? 0.933   15.998  12.424  1.00 69.88  ?  107 MET   B N     1 
ATOM   3297 C  CA    . MET   B 1 107 ? 0.106   15.128  13.252  1.00 68.59  ?  107 MET   B CA    1 
ATOM   3298 C  C     . MET   B 1 107 ? 0.057   15.597  14.710  1.00 74.90  ?  107 MET   B C     1 
ATOM   3299 O  O     . MET   B 1 107 ? 1.098   15.769  15.361  1.00 81.29  ?  107 MET   B O     1 
ATOM   3300 C  CB    . MET   B 1 107 ? 0.601   13.680  13.169  1.00 66.76  ?  107 MET   B CB    1 
ATOM   3301 C  CG    . MET   B 1 107 ? 0.380   13.034  11.803  1.00 63.24  ?  107 MET   B CG    1 
ATOM   3302 S  SD    . MET   B 1 107 ? -1.358  12.722  11.430  1.00 58.52  ?  107 MET   B SD    1 
ATOM   3303 C  CE    . MET   B 1 107 ? -1.283  12.445  9.676   1.00 54.68  ?  107 MET   B CE    1 
ATOM   3304 N  N     . THR   B 1 108 ? -1.164  15.798  15.203  1.00 73.09  ?  108 THR   B N     1 
ATOM   3305 C  CA    . THR   B 1 108 ? -1.424  16.269  16.563  1.00 74.50  ?  108 THR   B CA    1 
ATOM   3306 C  C     . THR   B 1 108 ? -0.865  15.377  17.657  1.00 76.11  ?  108 THR   B C     1 
ATOM   3307 O  O     . THR   B 1 108 ? -0.293  15.890  18.628  1.00 80.32  ?  108 THR   B O     1 
ATOM   3308 C  CB    . THR   B 1 108 ? -2.939  16.421  16.797  1.00 74.64  ?  108 THR   B CB    1 
ATOM   3309 O  OG1   . THR   B 1 108 ? -3.407  17.560  16.064  1.00 77.52  ?  108 THR   B OG1   1 
ATOM   3310 C  CG2   . THR   B 1 108 ? -3.290  16.565  18.312  1.00 74.37  ?  108 THR   B CG2   1 
ATOM   3311 N  N     . GLN   B 1 109 ? -1.070  14.061  17.535  1.00 73.32  ?  109 GLN   B N     1 
ATOM   3312 C  CA    . GLN   B 1 109 ? -0.541  13.124  18.535  1.00 72.00  ?  109 GLN   B CA    1 
ATOM   3313 C  C     . GLN   B 1 109 ? 0.987   13.275  18.618  1.00 65.81  ?  109 GLN   B C     1 
ATOM   3314 O  O     . GLN   B 1 109 ? 1.517   13.380  19.710  1.00 63.79  ?  109 GLN   B O     1 
ATOM   3315 C  CB    . GLN   B 1 109 ? -0.951  11.660  18.262  1.00 72.43  ?  109 GLN   B CB    1 
ATOM   3316 C  CG    . GLN   B 1 109 ? -0.265  10.653  19.195  1.00 72.12  ?  109 GLN   B CG    1 
ATOM   3317 C  CD    . GLN   B 1 109 ? -0.461  9.197   18.795  1.00 71.96  ?  109 GLN   B CD    1 
ATOM   3318 O  OE1   . GLN   B 1 109 ? -1.598  8.729   18.616  1.00 72.92  ?  109 GLN   B OE1   1 
ATOM   3319 N  NE2   . GLN   B 1 109 ? 0.652   8.453   18.681  1.00 65.61  ?  109 GLN   B NE2   1 
ATOM   3320 N  N     . PHE   B 1 110 ? 1.675   13.330  17.476  1.00 61.33  ?  110 PHE   B N     1 
ATOM   3321 C  CA    . PHE   B 1 110 ? 3.130   13.549  17.481  1.00 65.54  ?  110 PHE   B CA    1 
ATOM   3322 C  C     . PHE   B 1 110 ? 3.512   14.805  18.278  1.00 66.91  ?  110 PHE   B C     1 
ATOM   3323 O  O     . PHE   B 1 110 ? 4.381   14.742  19.157  1.00 60.05  ?  110 PHE   B O     1 
ATOM   3324 C  CB    . PHE   B 1 110 ? 3.717   13.643  16.074  1.00 63.66  ?  110 PHE   B CB    1 
ATOM   3325 C  CG    . PHE   B 1 110 ? 5.196   13.919  16.072  1.00 66.87  ?  110 PHE   B CG    1 
ATOM   3326 C  CD1   . PHE   B 1 110 ? 6.095   12.962  16.562  1.00 64.72  ?  110 PHE   B CD1   1 
ATOM   3327 C  CD2   . PHE   B 1 110 ? 5.700   15.148  15.632  1.00 65.76  ?  110 PHE   B CD2   1 
ATOM   3328 C  CE1   . PHE   B 1 110 ? 7.459   13.213  16.581  1.00 61.17  ?  110 PHE   B CE1   1 
ATOM   3329 C  CE2   . PHE   B 1 110 ? 7.067   15.393  15.638  1.00 63.95  ?  110 PHE   B CE2   1 
ATOM   3330 C  CZ    . PHE   B 1 110 ? 7.946   14.426  16.114  1.00 62.85  ?  110 PHE   B CZ    1 
ATOM   3331 N  N     . LYS   B 1 111 ? 2.844   15.923  17.971  1.00 67.79  ?  111 LYS   B N     1 
ATOM   3332 C  CA    . LYS   B 1 111 ? 3.048   17.196  18.681  1.00 68.96  ?  111 LYS   B CA    1 
ATOM   3333 C  C     . LYS   B 1 111 ? 2.853   17.069  20.198  1.00 71.00  ?  111 LYS   B C     1 
ATOM   3334 O  O     . LYS   B 1 111 ? 3.754   17.397  20.975  1.00 70.58  ?  111 LYS   B O     1 
ATOM   3335 C  CB    . LYS   B 1 111 ? 2.120   18.278  18.129  1.00 66.50  ?  111 LYS   B CB    1 
ATOM   3336 N  N     . ASP   B 1 112 ? 1.682   16.563  20.596  1.00 72.78  ?  112 ASP   B N     1 
ATOM   3337 C  CA    . ASP   B 1 112 ? 1.312   16.387  22.017  1.00 75.65  ?  112 ASP   B CA    1 
ATOM   3338 C  C     . ASP   B 1 112 ? 2.220   15.400  22.764  1.00 74.33  ?  112 ASP   B C     1 
ATOM   3339 O  O     . ASP   B 1 112 ? 2.591   15.648  23.912  1.00 71.04  ?  112 ASP   B O     1 
ATOM   3340 C  CB    . ASP   B 1 112 ? -0.153  15.939  22.144  1.00 76.52  ?  112 ASP   B CB    1 
ATOM   3341 N  N     . LYS   B 1 113 ? 2.550   14.284  22.103  1.00 74.04  ?  113 LYS   B N     1 
ATOM   3342 C  CA    . LYS   B 1 113 ? 3.522   13.288  22.598  1.00 72.10  ?  113 LYS   B CA    1 
ATOM   3343 C  C     . LYS   B 1 113 ? 4.930   13.871  22.783  1.00 70.07  ?  113 LYS   B C     1 
ATOM   3344 O  O     . LYS   B 1 113 ? 5.554   13.674  23.832  1.00 66.96  ?  113 LYS   B O     1 
ATOM   3345 C  CB    . LYS   B 1 113 ? 3.621   12.100  21.630  1.00 70.74  ?  113 LYS   B CB    1 
ATOM   3346 C  CG    . LYS   B 1 113 ? 2.382   11.221  21.513  1.00 73.04  ?  113 LYS   B CG    1 
ATOM   3347 C  CD    . LYS   B 1 113 ? 2.137   10.432  22.779  1.00 73.68  ?  113 LYS   B CD    1 
ATOM   3348 C  CE    . LYS   B 1 113 ? 0.915   9.542   22.642  1.00 75.73  ?  113 LYS   B CE    1 
ATOM   3349 N  NZ    . LYS   B 1 113 ? 0.637   8.830   23.923  1.00 73.20  ?  113 LYS   B NZ    1 
ATOM   3350 N  N     . SER   B 1 114 ? 5.414   14.557  21.744  1.00 70.31  ?  114 SER   B N     1 
ATOM   3351 C  CA    . SER   B 1 114 ? 6.754   15.171  21.721  1.00 71.99  ?  114 SER   B CA    1 
ATOM   3352 C  C     . SER   B 1 114 ? 6.966   16.148  22.877  1.00 71.65  ?  114 SER   B C     1 
ATOM   3353 O  O     . SER   B 1 114 ? 8.014   16.140  23.513  1.00 70.82  ?  114 SER   B O     1 
ATOM   3354 C  CB    . SER   B 1 114 ? 7.000   15.915  20.393  1.00 71.34  ?  114 SER   B CB    1 
ATOM   3355 O  OG    . SER   B 1 114 ? 6.999   15.043  19.281  1.00 73.35  ?  114 SER   B OG    1 
ATOM   3356 N  N     . ALA   B 1 115 ? 5.963   16.987  23.130  1.00 73.88  ?  115 ALA   B N     1 
ATOM   3357 C  CA    . ALA   B 1 115 ? 6.015   17.994  24.196  1.00 73.40  ?  115 ALA   B CA    1 
ATOM   3358 C  C     . ALA   B 1 115 ? 6.083   17.341  25.581  1.00 71.84  ?  115 ALA   B C     1 
ATOM   3359 O  O     . ALA   B 1 115 ? 6.780   17.821  26.469  1.00 72.51  ?  115 ALA   B O     1 
ATOM   3360 C  CB    . ALA   B 1 115 ? 4.808   18.914  24.102  1.00 73.30  ?  115 ALA   B CB    1 
ATOM   3361 N  N     . ARG   B 1 116 ? 5.377   16.228  25.733  1.00 71.89  ?  116 ARG   B N     1 
ATOM   3362 C  CA    . ARG   B 1 116 ? 5.285   15.500  26.998  1.00 75.66  ?  116 ARG   B CA    1 
ATOM   3363 C  C     . ARG   B 1 116 ? 6.524   14.647  27.263  1.00 74.99  ?  116 ARG   B C     1 
ATOM   3364 O  O     . ARG   B 1 116 ? 6.994   14.579  28.401  1.00 75.71  ?  116 ARG   B O     1 
ATOM   3365 C  CB    . ARG   B 1 116 ? 4.038   14.621  26.971  1.00 78.74  ?  116 ARG   B CB    1 
ATOM   3366 C  CG    . ARG   B 1 116 ? 3.939   13.607  28.090  1.00 79.78  ?  116 ARG   B CG    1 
ATOM   3367 C  CD    . ARG   B 1 116 ? 2.509   13.142  28.251  1.00 79.55  ?  116 ARG   B CD    1 
ATOM   3368 N  NE    . ARG   B 1 116 ? 2.279   12.733  29.633  1.00 82.53  ?  116 ARG   B NE    1 
ATOM   3369 C  CZ    . ARG   B 1 116 ? 1.714   11.598  30.029  1.00 80.43  ?  116 ARG   B CZ    1 
ATOM   3370 N  NH1   . ARG   B 1 116 ? 1.258   10.705  29.151  1.00 79.61  ?  116 ARG   B NH1   1 
ATOM   3371 N  NH2   . ARG   B 1 116 ? 1.583   11.365  31.332  1.00 82.08  ?  116 ARG   B NH2   1 
ATOM   3372 N  N     . TYR   B 1 117 ? 7.009   13.971  26.217  1.00 74.35  ?  117 TYR   B N     1 
ATOM   3373 C  CA    . TYR   B 1 117 ? 8.279   13.217  26.255  1.00 71.35  ?  117 TYR   B CA    1 
ATOM   3374 C  C     . TYR   B 1 117 ? 9.304   13.921  25.343  1.00 68.89  ?  117 TYR   B C     1 
ATOM   3375 O  O     . TYR   B 1 117 ? 9.606   13.474  24.225  1.00 68.53  ?  117 TYR   B O     1 
ATOM   3376 C  CB    . TYR   B 1 117 ? 8.061   11.740  25.868  1.00 69.56  ?  117 TYR   B CB    1 
ATOM   3377 C  CG    . TYR   B 1 117 ? 6.918   11.080  26.613  1.00 68.44  ?  117 TYR   B CG    1 
ATOM   3378 C  CD1   . TYR   B 1 117 ? 7.054   10.713  27.949  1.00 68.04  ?  117 TYR   B CD1   1 
ATOM   3379 C  CD2   . TYR   B 1 117 ? 5.692   10.840  25.983  1.00 67.01  ?  117 TYR   B CD2   1 
ATOM   3380 C  CE1   . TYR   B 1 117 ? 6.008   10.127  28.640  1.00 69.08  ?  117 TYR   B CE1   1 
ATOM   3381 C  CE2   . TYR   B 1 117 ? 4.639   10.247  26.665  1.00 67.03  ?  117 TYR   B CE2   1 
ATOM   3382 C  CZ    . TYR   B 1 117 ? 4.802   9.898   27.999  1.00 67.79  ?  117 TYR   B CZ    1 
ATOM   3383 O  OH    . TYR   B 1 117 ? 3.780   9.311   28.708  1.00 67.28  ?  117 TYR   B OH    1 
ATOM   3384 N  N     . ALA   B 1 118 ? 9.797   15.060  25.831  1.00 65.18  ?  118 ALA   B N     1 
ATOM   3385 C  CA    . ALA   B 1 118 ? 10.800  15.880  25.132  1.00 64.91  ?  118 ALA   B CA    1 
ATOM   3386 C  C     . ALA   B 1 118 ? 12.171  15.196  25.080  1.00 60.96  ?  118 ALA   B C     1 
ATOM   3387 O  O     . ALA   B 1 118 ? 12.909  15.366  24.110  1.00 59.38  ?  118 ALA   B O     1 
ATOM   3388 C  CB    . ALA   B 1 118 ? 10.914  17.255  25.792  1.00 62.82  ?  118 ALA   B CB    1 
ATOM   3389 N  N     . GLU   B 1 119 ? 12.465  14.386  26.100  1.00 58.48  ?  119 GLU   B N     1 
ATOM   3390 C  CA    . GLU   B 1 119 ? 13.689  13.578  26.172  1.00 62.87  ?  119 GLU   B CA    1 
ATOM   3391 C  C     . GLU   B 1 119 ? 13.637  12.249  25.366  1.00 62.83  ?  119 GLU   B C     1 
ATOM   3392 O  O     . GLU   B 1 119 ? 14.545  11.408  25.493  1.00 61.35  ?  119 GLU   B O     1 
ATOM   3393 C  CB    . GLU   B 1 119 ? 14.001  13.256  27.646  1.00 61.65  ?  119 GLU   B CB    1 
ATOM   3394 N  N     . ASN   B 1 120 ? 12.578  12.043  24.576  1.00 58.26  ?  120 ASN   B N     1 
ATOM   3395 C  CA    . ASN   B 1 120 ? 12.436  10.847  23.741  1.00 57.69  ?  120 ASN   B CA    1 
ATOM   3396 C  C     . ASN   B 1 120 ? 11.510  11.121  22.543  1.00 56.72  ?  120 ASN   B C     1 
ATOM   3397 O  O     . ASN   B 1 120 ? 10.445  10.513  22.405  1.00 52.72  ?  120 ASN   B O     1 
ATOM   3398 C  CB    . ASN   B 1 120 ? 11.947  9.661   24.600  1.00 56.96  ?  120 ASN   B CB    1 
ATOM   3399 C  CG    . ASN   B 1 120 ? 11.854  8.358   23.821  1.00 56.94  ?  120 ASN   B CG    1 
ATOM   3400 O  OD1   . ASN   B 1 120 ? 12.515  8.175   22.793  1.00 57.30  ?  120 ASN   B OD1   1 
ATOM   3401 N  ND2   . ASN   B 1 120 ? 11.013  7.446   24.301  1.00 53.84  ?  120 ASN   B ND2   1 
ATOM   3402 N  N     . ILE   B 1 121 ? 11.935  12.057  21.692  1.00 58.16  ?  121 ILE   B N     1 
ATOM   3403 C  CA    . ILE   B 1 121 ? 11.242  12.366  20.421  1.00 62.14  ?  121 ILE   B CA    1 
ATOM   3404 C  C     . ILE   B 1 121 ? 11.887  11.509  19.320  1.00 55.07  ?  121 ILE   B C     1 
ATOM   3405 O  O     . ILE   B 1 121 ? 12.681  11.986  18.503  1.00 54.53  ?  121 ILE   B O     1 
ATOM   3406 C  CB    . ILE   B 1 121 ? 11.267  13.888  20.063  1.00 63.83  ?  121 ILE   B CB    1 
ATOM   3407 C  CG1   . ILE   B 1 121 ? 10.814  14.737  21.269  1.00 66.80  ?  121 ILE   B CG1   1 
ATOM   3408 C  CG2   . ILE   B 1 121 ? 10.394  14.164  18.833  1.00 61.22  ?  121 ILE   B CG2   1 
ATOM   3409 C  CD1   . ILE   B 1 121 ? 10.853  16.243  21.064  1.00 68.29  ?  121 ILE   B CD1   1 
ATOM   3410 N  N     . ASN   B 1 122 ? 11.526  10.227  19.322  1.00 50.09  ?  122 ASN   B N     1 
ATOM   3411 C  CA    . ASN   B 1 122 ? 12.127  9.234   18.408  1.00 44.26  ?  122 ASN   B CA    1 
ATOM   3412 C  C     . ASN   B 1 122 ? 11.405  9.192   17.064  1.00 41.17  ?  122 ASN   B C     1 
ATOM   3413 O  O     . ASN   B 1 122 ? 10.281  9.680   16.948  1.00 44.03  ?  122 ASN   B O     1 
ATOM   3414 C  CB    . ASN   B 1 122 ? 12.178  7.851   19.071  1.00 42.05  ?  122 ASN   B CB    1 
ATOM   3415 C  CG    . ASN   B 1 122 ? 10.812  7.299   19.382  1.00 39.09  ?  122 ASN   B CG    1 
ATOM   3416 O  OD1   . ASN   B 1 122 ? 10.107  6.857   18.487  1.00 37.47  ?  122 ASN   B OD1   1 
ATOM   3417 N  ND2   . ASN   B 1 122 ? 10.437  7.323   20.646  1.00 35.73  ?  122 ASN   B ND2   1 
ATOM   3418 N  N     . ALA   B 1 123 ? 12.056  8.582   16.072  1.00 37.11  ?  123 ALA   B N     1 
ATOM   3419 C  CA    . ALA   B 1 123 ? 11.567  8.512   14.694  1.00 34.88  ?  123 ALA   B CA    1 
ATOM   3420 C  C     . ALA   B 1 123 ? 10.330  7.625   14.540  1.00 37.16  ?  123 ALA   B C     1 
ATOM   3421 O  O     . ALA   B 1 123 ? 9.597   7.788   13.580  1.00 35.96  ?  123 ALA   B O     1 
ATOM   3422 C  CB    . ALA   B 1 123 ? 12.668  8.013   13.782  1.00 33.00  ?  123 ALA   B CB    1 
ATOM   3423 N  N     . GLY   B 1 124 ? 10.143  6.664   15.457  1.00 39.25  ?  124 GLY   B N     1 
ATOM   3424 C  CA    . GLY   B 1 124 ? 8.931   5.847   15.520  1.00 41.53  ?  124 GLY   B CA    1 
ATOM   3425 C  C     . GLY   B 1 124 ? 7.682   6.665   15.826  1.00 43.62  ?  124 GLY   B C     1 
ATOM   3426 O  O     . GLY   B 1 124 ? 6.612   6.393   15.292  1.00 40.95  ?  124 GLY   B O     1 
ATOM   3427 N  N     . LEU   B 1 125 ? 7.836   7.670   16.687  1.00 49.32  ?  125 LEU   B N     1 
ATOM   3428 C  CA    . LEU   B 1 125 ? 6.749   8.559   17.094  1.00 50.37  ?  125 LEU   B CA    1 
ATOM   3429 C  C     . LEU   B 1 125 ? 6.310   9.415   15.922  1.00 50.06  ?  125 LEU   B C     1 
ATOM   3430 O  O     . LEU   B 1 125 ? 5.111   9.646   15.722  1.00 56.77  ?  125 LEU   B O     1 
ATOM   3431 C  CB    . LEU   B 1 125 ? 7.183   9.439   18.269  1.00 53.38  ?  125 LEU   B CB    1 
ATOM   3432 C  CG    . LEU   B 1 125 ? 6.082   10.062  19.113  1.00 56.25  ?  125 LEU   B CG    1 
ATOM   3433 C  CD1   . LEU   B 1 125 ? 5.289   9.008   19.868  1.00 58.12  ?  125 LEU   B CD1   1 
ATOM   3434 C  CD2   . LEU   B 1 125 ? 6.703   11.054  20.082  1.00 60.90  ?  125 LEU   B CD2   1 
ATOM   3435 N  N     . PHE   B 1 126 ? 7.287   9.862   15.147  1.00 45.68  ?  126 PHE   B N     1 
ATOM   3436 C  CA    . PHE   B 1 126 ? 7.049   10.591  13.900  1.00 47.94  ?  126 PHE   B CA    1 
ATOM   3437 C  C     . PHE   B 1 126 ? 6.344   9.739   12.848  1.00 44.33  ?  126 PHE   B C     1 
ATOM   3438 O  O     . PHE   B 1 126 ? 5.456   10.206  12.145  1.00 48.78  ?  126 PHE   B O     1 
ATOM   3439 C  CB    . PHE   B 1 126 ? 8.371   11.089  13.327  1.00 45.87  ?  126 PHE   B CB    1 
ATOM   3440 C  CG    . PHE   B 1 126 ? 8.222   11.929  12.086  1.00 47.13  ?  126 PHE   B CG    1 
ATOM   3441 C  CD1   . PHE   B 1 126 ? 7.717   13.220  12.168  1.00 48.89  ?  126 PHE   B CD1   1 
ATOM   3442 C  CD2   . PHE   B 1 126 ? 8.613   11.447  10.843  1.00 46.87  ?  126 PHE   B CD2   1 
ATOM   3443 C  CE1   . PHE   B 1 126 ? 7.585   14.000  11.035  1.00 48.14  ?  126 PHE   B CE1   1 
ATOM   3444 C  CE2   . PHE   B 1 126 ? 8.493   12.238  9.700   1.00 49.96  ?  126 PHE   B CE2   1 
ATOM   3445 C  CZ    . PHE   B 1 126 ? 7.972   13.512  9.802   1.00 47.58  ?  126 PHE   B CZ    1 
ATOM   3446 N  N     . ASP   B 1 127 ? 6.780   8.495   12.738  1.00 46.12  ?  127 ASP   B N     1 
ATOM   3447 C  CA    . ASP   B 1 127 ? 6.391   7.577   11.665  1.00 45.20  ?  127 ASP   B CA    1 
ATOM   3448 C  C     . ASP   B 1 127 ? 5.274   6.609   12.114  1.00 43.77  ?  127 ASP   B C     1 
ATOM   3449 O  O     . ASP   B 1 127 ? 4.864   5.745   11.335  1.00 38.46  ?  127 ASP   B O     1 
ATOM   3450 C  CB    . ASP   B 1 127 ? 7.651   6.802   11.247  1.00 45.71  ?  127 ASP   B CB    1 
ATOM   3451 C  CG    . ASP   B 1 127 ? 7.598   6.285   9.861   1.00 45.11  ?  127 ASP   B CG    1 
ATOM   3452 O  OD1   . ASP   B 1 127 ? 8.071   5.146   9.669   1.00 46.92  ?  127 ASP   B OD1   1 
ATOM   3453 O  OD2   . ASP   B 1 127 ? 7.120   7.012   8.961   1.00 46.18  ?  127 ASP   B OD2   1 
ATOM   3454 N  N     . TYR   B 1 128 ? 4.806   6.789   13.362  1.00 41.17  ?  128 TYR   B N     1 
ATOM   3455 C  CA    . TYR   B 1 128 ? 3.642   6.138   13.954  1.00 41.75  ?  128 TYR   B CA    1 
ATOM   3456 C  C     . TYR   B 1 128 ? 2.472   5.945   12.970  1.00 42.93  ?  128 TYR   B C     1 
ATOM   3457 O  O     . TYR   B 1 128 ? 1.906   4.842   12.917  1.00 42.67  ?  128 TYR   B O     1 
ATOM   3458 C  CB    . TYR   B 1 128 ? 3.194   6.940   15.200  1.00 42.70  ?  128 TYR   B CB    1 
ATOM   3459 C  CG    . TYR   B 1 128 ? 2.125   6.298   16.083  1.00 47.27  ?  128 TYR   B CG    1 
ATOM   3460 C  CD1   . TYR   B 1 128 ? 2.436   5.834   17.372  1.00 44.80  ?  128 TYR   B CD1   1 
ATOM   3461 C  CD2   . TYR   B 1 128 ? 0.785   6.206   15.657  1.00 49.83  ?  128 TYR   B CD2   1 
ATOM   3462 C  CE1   . TYR   B 1 128 ? 1.469   5.259   18.181  1.00 45.67  ?  128 TYR   B CE1   1 
ATOM   3463 C  CE2   . TYR   B 1 128 ? -0.199  5.627   16.467  1.00 49.33  ?  128 TYR   B CE2   1 
ATOM   3464 C  CZ    . TYR   B 1 128 ? 0.141   5.164   17.726  1.00 49.01  ?  128 TYR   B CZ    1 
ATOM   3465 O  OH    . TYR   B 1 128 ? -0.822  4.582   18.502  1.00 41.77  ?  128 TYR   B OH    1 
ATOM   3466 N  N     . PRO   B 1 129 ? 2.094   7.001   12.209  1.00 42.43  ?  129 PRO   B N     1 
ATOM   3467 C  CA    . PRO   B 1 129 ? 0.929   6.872   11.332  1.00 44.59  ?  129 PRO   B CA    1 
ATOM   3468 C  C     . PRO   B 1 129 ? 1.069   5.885   10.173  1.00 40.42  ?  129 PRO   B C     1 
ATOM   3469 O  O     . PRO   B 1 129 ? 0.054   5.370   9.707   1.00 35.39  ?  129 PRO   B O     1 
ATOM   3470 C  CB    . PRO   B 1 129 ? 0.736   8.296   10.786  1.00 45.67  ?  129 PRO   B CB    1 
ATOM   3471 C  CG    . PRO   B 1 129 ? 1.393   9.169   11.779  1.00 45.21  ?  129 PRO   B CG    1 
ATOM   3472 C  CD    . PRO   B 1 129 ? 2.598   8.390   12.187  1.00 44.98  ?  129 PRO   B CD    1 
ATOM   3473 N  N     . VAL   B 1 130 ? 2.301   5.634   9.731   1.00 38.43  ?  130 VAL   B N     1 
ATOM   3474 C  CA    . VAL   B 1 130 ? 2.559   4.799   8.545   1.00 37.79  ?  130 VAL   B CA    1 
ATOM   3475 C  C     . VAL   B 1 130 ? 2.406   3.318   8.913   1.00 38.80  ?  130 VAL   B C     1 
ATOM   3476 O  O     . VAL   B 1 130 ? 1.863   2.528   8.127   1.00 37.82  ?  130 VAL   B O     1 
ATOM   3477 C  CB    . VAL   B 1 130 ? 3.937   5.060   7.902   1.00 36.88  ?  130 VAL   B CB    1 
ATOM   3478 C  CG1   . VAL   B 1 130 ? 4.044   4.335   6.579   1.00 37.24  ?  130 VAL   B CG1   1 
ATOM   3479 C  CG2   . VAL   B 1 130 ? 4.159   6.550   7.658   1.00 38.46  ?  130 VAL   B CG2   1 
ATOM   3480 N  N     . LEU   B 1 131 ? 2.871   2.962   10.112  1.00 35.14  ?  131 LEU   B N     1 
ATOM   3481 C  CA    . LEU   B 1 131 ? 2.617   1.639   10.676  1.00 32.41  ?  131 LEU   B CA    1 
ATOM   3482 C  C     . LEU   B 1 131 ? 1.113   1.401   10.884  1.00 32.69  ?  131 LEU   B C     1 
ATOM   3483 O  O     . LEU   B 1 131 ? 0.606   0.295   10.620  1.00 32.93  ?  131 LEU   B O     1 
ATOM   3484 C  CB    . LEU   B 1 131 ? 3.359   1.463   12.003  1.00 28.06  ?  131 LEU   B CB    1 
ATOM   3485 C  CG    . LEU   B 1 131 ? 3.330   0.047   12.562  1.00 29.88  ?  131 LEU   B CG    1 
ATOM   3486 C  CD1   . LEU   B 1 131 ? 4.009   -0.920  11.598  1.00 29.06  ?  131 LEU   B CD1   1 
ATOM   3487 C  CD2   . LEU   B 1 131 ? 3.964   0.001   13.955  1.00 30.71  ?  131 LEU   B CD2   1 
ATOM   3488 N  N     . MET   B 1 132 ? 0.421   2.410   11.402  1.00 32.91  ?  132 MET   B N     1 
ATOM   3489 C  CA    . MET   B 1 132 ? -1.041  2.337   11.649  1.00 32.77  ?  132 MET   B CA    1 
ATOM   3490 C  C     . MET   B 1 132 ? -1.838  2.169   10.363  1.00 32.67  ?  132 MET   B C     1 
ATOM   3491 O  O     . MET   B 1 132 ? -2.849  1.434   10.348  1.00 38.16  ?  132 MET   B O     1 
ATOM   3492 C  CB    . MET   B 1 132 ? -1.532  3.552   12.421  1.00 34.92  ?  132 MET   B CB    1 
ATOM   3493 C  CG    . MET   B 1 132 ? -3.030  3.530   12.768  1.00 40.51  ?  132 MET   B CG    1 
ATOM   3494 S  SD    . MET   B 1 132 ? -3.592  4.888   13.826  1.00 43.86  ?  132 MET   B SD    1 
ATOM   3495 C  CE    . MET   B 1 132 ? -5.336  4.915   13.406  1.00 47.31  ?  132 MET   B CE    1 
ATOM   3496 N  N     . ALA   B 1 133 ? -1.389  2.810   9.284   1.00 33.24  ?  133 ALA   B N     1 
ATOM   3497 C  CA    . ALA   B 1 133 ? -1.933  2.554   7.948   1.00 29.04  ?  133 ALA   B CA    1 
ATOM   3498 C  C     . ALA   B 1 133 ? -1.720  1.099   7.508   1.00 33.08  ?  133 ALA   B C     1 
ATOM   3499 O  O     . ALA   B 1 133 ? -2.673  0.433   7.056   1.00 30.64  ?  133 ALA   B O     1 
ATOM   3500 C  CB    . ALA   B 1 133 ? -1.348  3.507   6.956   1.00 29.43  ?  133 ALA   B CB    1 
ATOM   3501 N  N     . ALA   B 1 134 ? -0.473  0.618   7.612   1.00 29.07  ?  134 ALA   B N     1 
ATOM   3502 C  CA    . ALA   B 1 134 ? -0.141  -0.760  7.260   1.00 28.43  ?  134 ALA   B CA    1 
ATOM   3503 C  C     . ALA   B 1 134 ? -1.019  -1.752  8.014   1.00 29.52  ?  134 ALA   B C     1 
ATOM   3504 O  O     . ALA   B 1 134 ? -1.521  -2.710  7.409   1.00 32.49  ?  134 ALA   B O     1 
ATOM   3505 C  CB    . ALA   B 1 134 ? 1.340   -1.042  7.532   1.00 29.35  ?  134 ALA   B CB    1 
ATOM   3506 N  N     . ASP   B 1 135 ? -1.136  -1.564  9.339   1.00 28.71  ?  135 ASP   B N     1 
ATOM   3507 C  CA    . ASP   B 1 135 ? -2.014  -2.332  10.184  1.00 30.09  ?  135 ASP   B CA    1 
ATOM   3508 C  C     . ASP   B 1 135 ? -3.412  -2.489  9.556   1.00 31.03  ?  135 ASP   B C     1 
ATOM   3509 O  O     . ASP   B 1 135 ? -3.937  -3.591  9.478   1.00 34.67  ?  135 ASP   B O     1 
ATOM   3510 C  CB    . ASP   B 1 135 ? -2.209  -1.649  11.561  1.00 31.39  ?  135 ASP   B CB    1 
ATOM   3511 C  CG    . ASP   B 1 135 ? -0.980  -1.679  12.443  1.00 34.06  ?  135 ASP   B CG    1 
ATOM   3512 O  OD1   . ASP   B 1 135 ? -1.033  -0.999  13.497  1.00 35.76  ?  135 ASP   B OD1   1 
ATOM   3513 O  OD2   . ASP   B 1 135 ? 0.024   -2.368  12.118  1.00 30.67  ?  135 ASP   B OD2   1 
ATOM   3514 N  N     . ILE   B 1 136 ? -4.002  -1.369  9.152   1.00 26.30  ?  136 ILE   B N     1 
ATOM   3515 C  CA    . ILE   B 1 136 ? -5.345  -1.317  8.583   1.00 29.37  ?  136 ILE   B CA    1 
ATOM   3516 C  C     . ILE   B 1 136 ? -5.383  -1.941  7.174   1.00 30.40  ?  136 ILE   B C     1 
ATOM   3517 O  O     . ILE   B 1 136 ? -6.219  -2.827  6.890   1.00 34.06  ?  136 ILE   B O     1 
ATOM   3518 C  CB    . ILE   B 1 136 ? -5.857  0.158   8.514   1.00 28.49  ?  136 ILE   B CB    1 
ATOM   3519 C  CG1   . ILE   B 1 136 ? -6.038  0.733   9.910   1.00 31.13  ?  136 ILE   B CG1   1 
ATOM   3520 C  CG2   . ILE   B 1 136 ? -7.179  0.244   7.734   1.00 31.50  ?  136 ILE   B CG2   1 
ATOM   3521 C  CD1   . ILE   B 1 136 ? -6.078  2.261   9.957   1.00 31.55  ?  136 ILE   B CD1   1 
ATOM   3522 N  N     . LEU   B 1 137 ? -4.484  -1.506  6.295   1.00 29.82  ?  137 LEU   B N     1 
ATOM   3523 C  CA    . LEU   B 1 137 ? -4.546  -1.905  4.859   1.00 29.53  ?  137 LEU   B CA    1 
ATOM   3524 C  C     . LEU   B 1 137 ? -4.197  -3.371  4.567   1.00 31.32  ?  137 LEU   B C     1 
ATOM   3525 O  O     . LEU   B 1 137 ? -4.559  -3.913  3.515   1.00 26.87  ?  137 LEU   B O     1 
ATOM   3526 C  CB    . LEU   B 1 137 ? -3.644  -0.985  4.030   1.00 33.43  ?  137 LEU   B CB    1 
ATOM   3527 C  CG    . LEU   B 1 137 ? -3.890  0.537   4.077   1.00 32.39  ?  137 LEU   B CG    1 
ATOM   3528 C  CD1   . LEU   B 1 137 ? -3.035  1.223   3.026   1.00 32.65  ?  137 LEU   B CD1   1 
ATOM   3529 C  CD2   . LEU   B 1 137 ? -5.360  0.903   3.894   1.00 32.57  ?  137 LEU   B CD2   1 
ATOM   3530 N  N     . LEU   B 1 138 ? -3.489  -4.006  5.497   1.00 29.46  ?  138 LEU   B N     1 
ATOM   3531 C  CA    . LEU   B 1 138 ? -3.112  -5.416  5.370   1.00 30.93  ?  138 LEU   B CA    1 
ATOM   3532 C  C     . LEU   B 1 138 ? -4.297  -6.358  5.246   1.00 31.94  ?  138 LEU   B C     1 
ATOM   3533 O  O     . LEU   B 1 138 ? -4.196  -7.390  4.554   1.00 37.28  ?  138 LEU   B O     1 
ATOM   3534 C  CB    . LEU   B 1 138 ? -2.258  -5.876  6.559   1.00 29.61  ?  138 LEU   B CB    1 
ATOM   3535 C  CG    . LEU   B 1 138 ? -0.737  -5.733  6.484   1.00 29.10  ?  138 LEU   B CG    1 
ATOM   3536 C  CD1   . LEU   B 1 138 ? -0.110  -6.087  7.830   1.00 28.12  ?  138 LEU   B CD1   1 
ATOM   3537 C  CD2   . LEU   B 1 138 ? -0.126  -6.597  5.403   1.00 26.58  ?  138 LEU   B CD2   1 
ATOM   3538 N  N     . TYR   B 1 139 ? -5.386  -6.036  5.933   1.00 32.61  ?  139 TYR   B N     1 
ATOM   3539 C  CA    . TYR   B 1 139 ? -6.533  -6.942  6.094   1.00 32.56  ?  139 TYR   B CA    1 
ATOM   3540 C  C     . TYR   B 1 139 ? -7.723  -6.582  5.208   1.00 32.62  ?  139 TYR   B C     1 
ATOM   3541 O  O     . TYR   B 1 139 ? -8.818  -7.088  5.429   1.00 34.13  ?  139 TYR   B O     1 
ATOM   3542 C  CB    . TYR   B 1 139 ? -6.933  -7.002  7.591   1.00 32.46  ?  139 TYR   B CB    1 
ATOM   3543 C  CG    . TYR   B 1 139 ? -5.787  -7.514  8.410   1.00 30.54  ?  139 TYR   B CG    1 
ATOM   3544 C  CD1   . TYR   B 1 139 ? -5.550  -8.885  8.535   1.00 31.10  ?  139 TYR   B CD1   1 
ATOM   3545 C  CD2   . TYR   B 1 139 ? -4.879  -6.635  8.971   1.00 32.49  ?  139 TYR   B CD2   1 
ATOM   3546 C  CE1   . TYR   B 1 139 ? -4.449  -9.354  9.245   1.00 32.70  ?  139 TYR   B CE1   1 
ATOM   3547 C  CE2   . TYR   B 1 139 ? -3.764  -7.086  9.673   1.00 30.22  ?  139 TYR   B CE2   1 
ATOM   3548 C  CZ    . TYR   B 1 139 ? -3.553  -8.434  9.808   1.00 31.10  ?  139 TYR   B CZ    1 
ATOM   3549 O  OH    . TYR   B 1 139 ? -2.475  -8.846  10.503  1.00 30.49  ?  139 TYR   B OH    1 
ATOM   3550 N  N     . GLN   B 1 140 ? -7.487  -5.768  4.179   1.00 32.45  ?  140 GLN   B N     1 
ATOM   3551 C  CA    . GLN   B 1 140 ? -8.522  -5.323  3.230   1.00 35.73  ?  140 GLN   B CA    1 
ATOM   3552 C  C     . GLN   B 1 140 ? -9.690  -4.714  4.019   1.00 35.45  ?  140 GLN   B C     1 
ATOM   3553 O  O     . GLN   B 1 140 ? -10.857 -5.025  3.766   1.00 36.29  ?  140 GLN   B O     1 
ATOM   3554 C  CB    . GLN   B 1 140 ? -8.969  -6.498  2.331   1.00 35.62  ?  140 GLN   B CB    1 
ATOM   3555 C  CG    . GLN   B 1 140 ? -7.882  -7.099  1.449   1.00 35.47  ?  140 GLN   B CG    1 
ATOM   3556 C  CD    . GLN   B 1 140 ? -7.312  -6.095  0.463   1.00 37.10  ?  140 GLN   B CD    1 
ATOM   3557 O  OE1   . GLN   B 1 140 ? -8.071  -5.411  -0.211  1.00 36.74  ?  140 GLN   B OE1   1 
ATOM   3558 N  NE2   . GLN   B 1 140 ? -5.970  -5.977  0.390   1.00 33.77  ?  140 GLN   B NE2   1 
ATOM   3559 N  N     . THR   B 1 141 ? -9.350  -3.870  4.992   1.00 35.57  ?  141 THR   B N     1 
ATOM   3560 C  CA    . THR   B 1 141 ? -10.307 -3.370  5.978   1.00 39.53  ?  141 THR   B CA    1 
ATOM   3561 C  C     . THR   B 1 141 ? -11.309 -2.389  5.362   1.00 40.14  ?  141 THR   B C     1 
ATOM   3562 O  O     . THR   B 1 141 ? -10.914 -1.468  4.659   1.00 42.76  ?  141 THR   B O     1 
ATOM   3563 C  CB    . THR   B 1 141 ? -9.571  -2.661  7.135   1.00 38.63  ?  141 THR   B CB    1 
ATOM   3564 O  OG1   . THR   B 1 141 ? -8.713  -3.606  7.787   1.00 33.81  ?  141 THR   B OG1   1 
ATOM   3565 C  CG2   . THR   B 1 141 ? -10.543 -2.079  8.129   1.00 37.63  ?  141 THR   B CG2   1 
ATOM   3566 N  N     . ASN   B 1 142 ? -12.594 -2.584  5.666   1.00 38.94  ?  142 ASN   B N     1 
ATOM   3567 C  CA    . ASN   B 1 142 ? -13.669 -1.667  5.246   1.00 35.14  ?  142 ASN   B CA    1 
ATOM   3568 C  C     . ASN   B 1 142 ? -13.989 -0.641  6.329   1.00 36.52  ?  142 ASN   B C     1 
ATOM   3569 O  O     . ASN   B 1 142 ? -14.086 0.557   6.034   1.00 36.97  ?  142 ASN   B O     1 
ATOM   3570 C  CB    . ASN   B 1 142 ? -14.901 -2.456  4.851   1.00 34.36  ?  142 ASN   B CB    1 
ATOM   3571 C  CG    . ASN   B 1 142 ? -14.623 -3.424  3.742   1.00 33.86  ?  142 ASN   B CG    1 
ATOM   3572 O  OD1   . ASN   B 1 142 ? -14.642 -4.643  3.926   1.00 32.42  ?  142 ASN   B OD1   1 
ATOM   3573 N  ND2   . ASN   B 1 142 ? -14.341 -2.893  2.578   1.00 37.02  ?  142 ASN   B ND2   1 
ATOM   3574 N  N     . LEU   B 1 143 ? -14.113 -1.098  7.582   1.00 37.26  ?  143 LEU   B N     1 
ATOM   3575 C  CA    . LEU   B 1 143 ? -14.429 -0.219  8.742   1.00 38.42  ?  143 LEU   B CA    1 
ATOM   3576 C  C     . LEU   B 1 143 ? -13.340 -0.219  9.828   1.00 36.54  ?  143 LEU   B C     1 
ATOM   3577 O  O     . LEU   B 1 143 ? -12.770 -1.249  10.088  1.00 35.85  ?  143 LEU   B O     1 
ATOM   3578 C  CB    . LEU   B 1 143 ? -15.757 -0.643  9.374   1.00 36.88  ?  143 LEU   B CB    1 
ATOM   3579 C  CG    . LEU   B 1 143 ? -17.007 -0.293  8.567   1.00 39.69  ?  143 LEU   B CG    1 
ATOM   3580 C  CD1   . LEU   B 1 143 ? -18.218 -0.944  9.187   1.00 40.39  ?  143 LEU   B CD1   1 
ATOM   3581 C  CD2   . LEU   B 1 143 ? -17.219 1.210   8.460   1.00 40.41  ?  143 LEU   B CD2   1 
ATOM   3582 N  N     . VAL   B 1 144 ? -13.066 0.946   10.429  1.00 37.91  ?  144 VAL   B N     1 
ATOM   3583 C  CA    . VAL   B 1 144 ? -12.114 1.090   11.550  1.00 39.41  ?  144 VAL   B CA    1 
ATOM   3584 C  C     . VAL   B 1 144 ? -12.783 1.817   12.741  1.00 38.82  ?  144 VAL   B C     1 
ATOM   3585 O  O     . VAL   B 1 144 ? -12.919 3.032   12.735  1.00 41.62  ?  144 VAL   B O     1 
ATOM   3586 C  CB    . VAL   B 1 144 ? -10.800 1.803   11.122  1.00 39.75  ?  144 VAL   B CB    1 
ATOM   3587 C  CG1   . VAL   B 1 144 ? -9.763  1.785   12.234  1.00 40.19  ?  144 VAL   B CG1   1 
ATOM   3588 C  CG2   . VAL   B 1 144 ? -10.205 1.176   9.865   1.00 41.39  ?  144 VAL   B CG2   1 
ATOM   3589 N  N     . PRO   B 1 145 ? -13.199 1.072   13.771  1.00 40.05  ?  145 PRO   B N     1 
ATOM   3590 C  CA    . PRO   B 1 145 ? -13.842 1.677   14.934  1.00 42.57  ?  145 PRO   B CA    1 
ATOM   3591 C  C     . PRO   B 1 145 ? -12.845 2.251   15.945  1.00 44.09  ?  145 PRO   B C     1 
ATOM   3592 O  O     . PRO   B 1 145 ? -12.139 1.505   16.619  1.00 44.88  ?  145 PRO   B O     1 
ATOM   3593 C  CB    . PRO   B 1 145 ? -14.640 0.516   15.536  1.00 40.82  ?  145 PRO   B CB    1 
ATOM   3594 C  CG    . PRO   B 1 145 ? -13.868 -0.693  15.174  1.00 38.78  ?  145 PRO   B CG    1 
ATOM   3595 C  CD    . PRO   B 1 145 ? -13.242 -0.402  13.844  1.00 39.74  ?  145 PRO   B CD    1 
ATOM   3596 N  N     . VAL   B 1 146 ? -12.803 3.571   16.042  1.00 46.32  ?  146 VAL   B N     1 
ATOM   3597 C  CA    . VAL   B 1 146 ? -11.851 4.282   16.895  1.00 53.35  ?  146 VAL   B CA    1 
ATOM   3598 C  C     . VAL   B 1 146 ? -12.549 5.437   17.628  1.00 53.27  ?  146 VAL   B C     1 
ATOM   3599 O  O     . VAL   B 1 146 ? -13.734 5.703   17.406  1.00 51.91  ?  146 VAL   B O     1 
ATOM   3600 C  CB    . VAL   B 1 146 ? -10.650 4.822   16.073  1.00 53.60  ?  146 VAL   B CB    1 
ATOM   3601 C  CG1   . VAL   B 1 146 ? -9.747  3.671   15.642  1.00 55.07  ?  146 VAL   B CG1   1 
ATOM   3602 C  CG2   . VAL   B 1 146 ? -11.110 5.641   14.865  1.00 54.59  ?  146 VAL   B CG2   1 
ATOM   3603 N  N     . GLY   B 1 147 ? -11.808 6.093   18.516  1.00 50.03  ?  147 GLY   B N     1 
ATOM   3604 C  CA    . GLY   B 1 147 ? -12.237 7.352   19.131  1.00 51.85  ?  147 GLY   B CA    1 
ATOM   3605 C  C     . GLY   B 1 147 ? -11.871 8.529   18.244  1.00 52.16  ?  147 GLY   B C     1 
ATOM   3606 O  O     . GLY   B 1 147 ? -11.094 8.371   17.292  1.00 53.06  ?  147 GLY   B O     1 
ATOM   3607 N  N     . GLU   B 1 148 ? -12.408 9.710   18.577  1.00 54.03  ?  148 GLU   B N     1 
ATOM   3608 C  CA    . GLU   B 1 148 ? -12.221 10.934  17.780  1.00 55.78  ?  148 GLU   B CA    1 
ATOM   3609 C  C     . GLU   B 1 148 ? -10.745 11.342  17.651  1.00 56.66  ?  148 GLU   B C     1 
ATOM   3610 O  O     . GLU   B 1 148 ? -10.335 11.902  16.630  1.00 56.54  ?  148 GLU   B O     1 
ATOM   3611 C  CB    . GLU   B 1 148 ? -13.054 12.090  18.357  1.00 56.63  ?  148 GLU   B CB    1 
ATOM   3612 N  N     . ASP   B 1 149 ? -9.945  11.021  18.667  1.00 56.78  ?  149 ASP   B N     1 
ATOM   3613 C  CA    . ASP   B 1 149 ? -8.516  11.368  18.671  1.00 61.28  ?  149 ASP   B CA    1 
ATOM   3614 C  C     . ASP   B 1 149 ? -7.693  10.685  17.575  1.00 59.09  ?  149 ASP   B C     1 
ATOM   3615 O  O     . ASP   B 1 149 ? -6.599  11.152  17.274  1.00 63.60  ?  149 ASP   B O     1 
ATOM   3616 C  CB    . ASP   B 1 149 ? -7.867  11.136  20.058  1.00 61.26  ?  149 ASP   B CB    1 
ATOM   3617 C  CG    . ASP   B 1 149 ? -7.903  9.677   20.512  1.00 65.17  ?  149 ASP   B CG    1 
ATOM   3618 O  OD1   . ASP   B 1 149 ? -9.011  9.138   20.734  1.00 69.52  ?  149 ASP   B OD1   1 
ATOM   3619 O  OD2   . ASP   B 1 149 ? -6.822  9.073   20.686  1.00 64.17  ?  149 ASP   B OD2   1 
ATOM   3620 N  N     . GLN   B 1 150 ? -8.228  9.616   16.972  1.00 58.20  ?  150 GLN   B N     1 
ATOM   3621 C  CA    . GLN   B 1 150 ? -7.556  8.861   15.896  1.00 54.06  ?  150 GLN   B CA    1 
ATOM   3622 C  C     . GLN   B 1 150 ? -8.065  9.166   14.488  1.00 53.56  ?  150 GLN   B C     1 
ATOM   3623 O  O     . GLN   B 1 150 ? -7.637  8.516   13.531  1.00 53.64  ?  150 GLN   B O     1 
ATOM   3624 C  CB    . GLN   B 1 150 ? -7.675  7.344   16.180  1.00 53.34  ?  150 GLN   B CB    1 
ATOM   3625 C  CG    . GLN   B 1 150 ? -6.905  6.875   17.405  1.00 52.37  ?  150 GLN   B CG    1 
ATOM   3626 C  CD    . GLN   B 1 150 ? -5.444  7.263   17.320  1.00 51.49  ?  150 GLN   B CD    1 
ATOM   3627 O  OE1   . GLN   B 1 150 ? -4.723  6.793   16.438  1.00 47.56  ?  150 GLN   B OE1   1 
ATOM   3628 N  NE2   . GLN   B 1 150 ? -5.007  8.163   18.201  1.00 51.97  ?  150 GLN   B NE2   1 
ATOM   3629 N  N     . LYS   B 1 151 ? -8.929  10.178  14.353  1.00 56.26  ?  151 LYS   B N     1 
ATOM   3630 C  CA    . LYS   B 1 151 ? -9.583  10.515  13.073  1.00 55.13  ?  151 LYS   B CA    1 
ATOM   3631 C  C     . LYS   B 1 151 ? -8.593  10.864  11.960  1.00 51.72  ?  151 LYS   B C     1 
ATOM   3632 O  O     . LYS   B 1 151 ? -8.694  10.334  10.861  1.00 52.28  ?  151 LYS   B O     1 
ATOM   3633 C  CB    . LYS   B 1 151 ? -10.582 11.677  13.262  1.00 54.82  ?  151 LYS   B CB    1 
ATOM   3634 N  N     . GLN   B 1 152 ? -7.639  11.744  12.257  1.00 57.37  ?  152 GLN   B N     1 
ATOM   3635 C  CA    . GLN   B 1 152 ? -6.624  12.186  11.281  1.00 59.46  ?  152 GLN   B CA    1 
ATOM   3636 C  C     . GLN   B 1 152 ? -5.639  11.074  10.835  1.00 56.39  ?  152 GLN   B C     1 
ATOM   3637 O  O     . GLN   B 1 152 ? -5.251  11.013  9.666   1.00 55.08  ?  152 GLN   B O     1 
ATOM   3638 C  CB    . GLN   B 1 152 ? -5.859  13.390  11.854  1.00 56.25  ?  152 GLN   B CB    1 
ATOM   3639 N  N     . HIS   B 1 153 ? -5.252  10.198  11.761  1.00 54.38  ?  153 HIS   B N     1 
ATOM   3640 C  CA    . HIS   B 1 153 ? -4.449  9.005   11.405  1.00 50.88  ?  153 HIS   B CA    1 
ATOM   3641 C  C     . HIS   B 1 153 ? -5.166  8.151   10.390  1.00 47.45  ?  153 HIS   B C     1 
ATOM   3642 O  O     . HIS   B 1 153 ? -4.551  7.742   9.408   1.00 43.46  ?  153 HIS   B O     1 
ATOM   3643 C  CB    . HIS   B 1 153 ? -4.079  8.167   12.631  1.00 50.31  ?  153 HIS   B CB    1 
ATOM   3644 C  CG    . HIS   B 1 153 ? -3.068  8.822   13.517  1.00 52.18  ?  153 HIS   B CG    1 
ATOM   3645 N  ND1   . HIS   B 1 153 ? -2.917  8.502   14.849  1.00 51.07  ?  153 HIS   B ND1   1 
ATOM   3646 C  CD2   . HIS   B 1 153 ? -2.161  9.794   13.258  1.00 52.64  ?  153 HIS   B CD2   1 
ATOM   3647 C  CE1   . HIS   B 1 153 ? -1.954  9.243   15.368  1.00 52.70  ?  153 HIS   B CE1   1 
ATOM   3648 N  NE2   . HIS   B 1 153 ? -1.484  10.042  14.426  1.00 53.15  ?  153 HIS   B NE2   1 
ATOM   3649 N  N     . LEU   B 1 154 ? -6.468  7.907   10.597  1.00 50.16  ?  154 LEU   B N     1 
ATOM   3650 C  CA    . LEU   B 1 154 ? -7.254  7.168   9.597   1.00 49.35  ?  154 LEU   B CA    1 
ATOM   3651 C  C     . LEU   B 1 154 ? -7.267  7.857   8.252   1.00 50.26  ?  154 LEU   B C     1 
ATOM   3652 O  O     . LEU   B 1 154 ? -7.086  7.198   7.222   1.00 50.62  ?  154 LEU   B O     1 
ATOM   3653 C  CB    . LEU   B 1 154 ? -8.703  6.926   10.014  1.00 52.28  ?  154 LEU   B CB    1 
ATOM   3654 C  CG    . LEU   B 1 154 ? -9.424  6.117   8.912   1.00 54.21  ?  154 LEU   B CG    1 
ATOM   3655 C  CD1   . LEU   B 1 154 ? -8.993  4.659   8.944   1.00 52.97  ?  154 LEU   B CD1   1 
ATOM   3656 C  CD2   . LEU   B 1 154 ? -10.930 6.222   9.002   1.00 57.89  ?  154 LEU   B CD2   1 
ATOM   3657 N  N     . GLU   B 1 155 ? -7.505  9.170   8.267   1.00 53.86  ?  155 GLU   B N     1 
ATOM   3658 C  CA    . GLU   B 1 155 ? -7.579  9.964   7.040   1.00 59.04  ?  155 GLU   B CA    1 
ATOM   3659 C  C     . GLU   B 1 155 ? -6.331  9.809   6.173   1.00 50.55  ?  155 GLU   B C     1 
ATOM   3660 O  O     . GLU   B 1 155 ? -6.440  9.591   4.965   1.00 54.18  ?  155 GLU   B O     1 
ATOM   3661 C  CB    . GLU   B 1 155 ? -7.886  11.438  7.369   1.00 66.97  ?  155 GLU   B CB    1 
ATOM   3662 C  CG    . GLU   B 1 155 ? -9.290  11.602  7.953   1.00 73.58  ?  155 GLU   B CG    1 
ATOM   3663 C  CD    . GLU   B 1 155 ? -9.711  13.040  8.230   1.00 77.29  ?  155 GLU   B CD    1 
ATOM   3664 O  OE1   . GLU   B 1 155 ? -8.924  13.983  7.966   1.00 77.63  ?  155 GLU   B OE1   1 
ATOM   3665 O  OE2   . GLU   B 1 155 ? -10.850 13.215  8.727   1.00 78.30  ?  155 GLU   B OE2   1 
ATOM   3666 N  N     . LEU   B 1 156 ? -5.153  9.872   6.802   1.00 50.02  ?  156 LEU   B N     1 
ATOM   3667 C  CA    . LEU   B 1 156 ? -3.876  9.633   6.097   1.00 46.27  ?  156 LEU   B CA    1 
ATOM   3668 C  C     . LEU   B 1 156 ? -3.866  8.254   5.433   1.00 42.66  ?  156 LEU   B C     1 
ATOM   3669 O  O     . LEU   B 1 156 ? -3.462  8.113   4.288   1.00 44.55  ?  156 LEU   B O     1 
ATOM   3670 C  CB    . LEU   B 1 156 ? -2.682  9.787   7.061   1.00 45.98  ?  156 LEU   B CB    1 
ATOM   3671 C  CG    . LEU   B 1 156 ? -1.298  9.474   6.476   1.00 46.62  ?  156 LEU   B CG    1 
ATOM   3672 C  CD1   . LEU   B 1 156 ? -1.046  10.209  5.169   1.00 46.48  ?  156 LEU   B CD1   1 
ATOM   3673 C  CD2   . LEU   B 1 156 ? -0.200  9.807   7.468   1.00 48.50  ?  156 LEU   B CD2   1 
ATOM   3674 N  N     . SER   B 1 157 ? -4.355  7.245   6.148   1.00 47.49  ?  157 SER   B N     1 
ATOM   3675 C  CA    . SER   B 1 157 ? -4.379  5.863   5.616   1.00 51.14  ?  157 SER   B CA    1 
ATOM   3676 C  C     . SER   B 1 157 ? -5.225  5.762   4.339   1.00 49.27  ?  157 SER   B C     1 
ATOM   3677 O  O     . SER   B 1 157 ? -4.848  5.081   3.384   1.00 48.78  ?  157 SER   B O     1 
ATOM   3678 C  CB    . SER   B 1 157 ? -4.829  4.847   6.689   1.00 48.84  ?  157 SER   B CB    1 
ATOM   3679 O  OG    . SER   B 1 157 ? -6.234  4.653   6.694   1.00 50.89  ?  157 SER   B OG    1 
ATOM   3680 N  N     . ARG   B 1 158 ? -6.353  6.474   4.321   1.00 57.37  ?  158 ARG   B N     1 
ATOM   3681 C  CA    . ARG   B 1 158 ? -7.224  6.554   3.135   1.00 56.03  ?  158 ARG   B CA    1 
ATOM   3682 C  C     . ARG   B 1 158 ? -6.505  7.210   1.973   1.00 53.02  ?  158 ARG   B C     1 
ATOM   3683 O  O     . ARG   B 1 158 ? -6.582  6.731   0.849   1.00 55.60  ?  158 ARG   B O     1 
ATOM   3684 C  CB    . ARG   B 1 158 ? -8.512  7.319   3.457   1.00 59.19  ?  158 ARG   B CB    1 
ATOM   3685 C  CG    . ARG   B 1 158 ? -9.393  6.603   4.466   1.00 64.54  ?  158 ARG   B CG    1 
ATOM   3686 C  CD    . ARG   B 1 158 ? -10.651 7.384   4.836   1.00 68.00  ?  158 ARG   B CD    1 
ATOM   3687 N  NE    . ARG   B 1 158 ? -11.729 7.213   3.852   1.00 69.77  ?  158 ARG   B NE    1 
ATOM   3688 C  CZ    . ARG   B 1 158 ? -12.176 8.146   3.010   1.00 73.53  ?  158 ARG   B CZ    1 
ATOM   3689 N  NH1   . ARG   B 1 158 ? -13.160 7.849   2.169   1.00 73.35  ?  158 ARG   B NH1   1 
ATOM   3690 N  NH2   . ARG   B 1 158 ? -11.666 9.378   2.992   1.00 77.35  ?  158 ARG   B NH2   1 
ATOM   3691 N  N     . ASP   B 1 159 ? -5.787  8.297   2.256   1.00 52.21  ?  159 ASP   B N     1 
ATOM   3692 C  CA    . ASP   B 1 159 ? -4.952  8.960   1.241   1.00 54.60  ?  159 ASP   B CA    1 
ATOM   3693 C  C     . ASP   B 1 159 ? -3.859  8.031   0.709   1.00 53.16  ?  159 ASP   B C     1 
ATOM   3694 O  O     . ASP   B 1 159 ? -3.661  7.941   -0.512  1.00 52.96  ?  159 ASP   B O     1 
ATOM   3695 C  CB    . ASP   B 1 159 ? -4.331  10.252  1.795   1.00 59.12  ?  159 ASP   B CB    1 
ATOM   3696 C  CG    . ASP   B 1 159 ? -5.355  11.352  2.015   1.00 62.26  ?  159 ASP   B CG    1 
ATOM   3697 O  OD1   . ASP   B 1 159 ? -5.254  12.055  3.046   1.00 65.28  ?  159 ASP   B OD1   1 
ATOM   3698 O  OD2   . ASP   B 1 159 ? -6.255  11.514  1.162   1.00 64.89  ?  159 ASP   B OD2   1 
ATOM   3699 N  N     . ILE   B 1 160 ? -3.174  7.324   1.619   1.00 47.81  ?  160 ILE   B N     1 
ATOM   3700 C  CA    . ILE   B 1 160 ? -2.126  6.359   1.231   1.00 45.24  ?  160 ILE   B CA    1 
ATOM   3701 C  C     . ILE   B 1 160 ? -2.714  5.270   0.331   1.00 40.41  ?  160 ILE   B C     1 
ATOM   3702 O  O     . ILE   B 1 160 ? -2.175  4.994   -0.739  1.00 38.64  ?  160 ILE   B O     1 
ATOM   3703 C  CB    . ILE   B 1 160 ? -1.416  5.736   2.468   1.00 41.27  ?  160 ILE   B CB    1 
ATOM   3704 C  CG1   . ILE   B 1 160 ? -0.549  6.774   3.180   1.00 41.08  ?  160 ILE   B CG1   1 
ATOM   3705 C  CG2   . ILE   B 1 160 ? -0.537  4.559   2.057   1.00 42.05  ?  160 ILE   B CG2   1 
ATOM   3706 C  CD1   . ILE   B 1 160 ? -0.154  6.405   4.596   1.00 39.64  ?  160 ILE   B CD1   1 
ATOM   3707 N  N     . ALA   B 1 161 ? -3.819  4.675   0.775   1.00 41.84  ?  161 ALA   B N     1 
ATOM   3708 C  CA    . ALA   B 1 161 ? -4.490  3.593   0.041   1.00 45.10  ?  161 ALA   B CA    1 
ATOM   3709 C  C     . ALA   B 1 161 ? -4.919  4.018   -1.351  1.00 44.50  ?  161 ALA   B C     1 
ATOM   3710 O  O     . ALA   B 1 161 ? -4.715  3.278   -2.311  1.00 39.13  ?  161 ALA   B O     1 
ATOM   3711 C  CB    . ALA   B 1 161 ? -5.689  3.077   0.823   1.00 48.57  ?  161 ALA   B CB    1 
ATOM   3712 N  N     . GLN   B 1 162 ? -5.485  5.225   -1.443  1.00 49.65  ?  162 GLN   B N     1 
ATOM   3713 C  CA    . GLN   B 1 162 ? -5.853  5.842   -2.733  1.00 51.89  ?  162 GLN   B CA    1 
ATOM   3714 C  C     . GLN   B 1 162 ? -4.636  6.122   -3.614  1.00 47.24  ?  162 GLN   B C     1 
ATOM   3715 O  O     . GLN   B 1 162 ? -4.665  5.874   -4.815  1.00 45.21  ?  162 GLN   B O     1 
ATOM   3716 C  CB    . GLN   B 1 162 ? -6.655  7.138   -2.495  1.00 53.81  ?  162 GLN   B CB    1 
ATOM   3717 C  CG    . GLN   B 1 162 ? -8.077  6.883   -2.015  1.00 56.92  ?  162 GLN   B CG    1 
ATOM   3718 C  CD    . GLN   B 1 162 ? -8.810  8.145   -1.596  1.00 56.51  ?  162 GLN   B CD    1 
ATOM   3719 O  OE1   . GLN   B 1 162 ? -8.251  9.009   -0.939  1.00 55.97  ?  162 GLN   B OE1   1 
ATOM   3720 N  NE2   . GLN   B 1 162 ? -10.076 8.247   -1.970  1.00 61.15  ?  162 GLN   B NE2   1 
ATOM   3721 N  N     . ARG   B 1 163 ? -3.571  6.637   -2.996  1.00 51.58  ?  163 ARG   B N     1 
ATOM   3722 C  CA    . ARG   B 1 163 ? -2.329  6.968   -3.695  1.00 50.29  ?  163 ARG   B CA    1 
ATOM   3723 C  C     . ARG   B 1 163 ? -1.716  5.715   -4.317  1.00 48.38  ?  163 ARG   B C     1 
ATOM   3724 O  O     . ARG   B 1 163 ? -1.323  5.722   -5.493  1.00 48.61  ?  163 ARG   B O     1 
ATOM   3725 C  CB    . ARG   B 1 163 ? -1.337  7.639   -2.742  1.00 50.16  ?  163 ARG   B CB    1 
ATOM   3726 C  CG    . ARG   B 1 163 ? -0.171  8.335   -3.426  1.00 53.59  ?  163 ARG   B CG    1 
ATOM   3727 C  CD    . ARG   B 1 163 ? 0.645   9.154   -2.430  1.00 54.50  ?  163 ARG   B CD    1 
ATOM   3728 N  NE    . ARG   B 1 163 ? -0.140  10.234  -1.824  1.00 52.69  ?  163 ARG   B NE    1 
ATOM   3729 C  CZ    . ARG   B 1 163 ? -0.144  10.575  -0.536  1.00 55.97  ?  163 ARG   B CZ    1 
ATOM   3730 N  NH1   . ARG   B 1 163 ? 0.577   9.922   0.374   1.00 60.54  ?  163 ARG   B NH1   1 
ATOM   3731 N  NH2   . ARG   B 1 163 ? -0.904  11.582  -0.135  1.00 58.09  ?  163 ARG   B NH2   1 
ATOM   3732 N  N     . PHE   B 1 164 ? -1.657  4.641   -3.525  1.00 44.62  ?  164 PHE   B N     1 
ATOM   3733 C  CA    . PHE   B 1 164 ? -1.087  3.370   -3.989  1.00 42.78  ?  164 PHE   B CA    1 
ATOM   3734 C  C     . PHE   B 1 164 ? -1.949  2.787   -5.110  1.00 40.24  ?  164 PHE   B C     1 
ATOM   3735 O  O     . PHE   B 1 164 ? -1.443  2.416   -6.163  1.00 37.99  ?  164 PHE   B O     1 
ATOM   3736 C  CB    . PHE   B 1 164 ? -0.934  2.373   -2.833  1.00 38.33  ?  164 PHE   B CB    1 
ATOM   3737 C  CG    . PHE   B 1 164 ? -0.058  1.194   -3.160  1.00 37.98  ?  164 PHE   B CG    1 
ATOM   3738 C  CD1   . PHE   B 1 164 ? -0.600  0.015   -3.685  1.00 37.48  ?  164 PHE   B CD1   1 
ATOM   3739 C  CD2   . PHE   B 1 164 ? 1.321   1.248   -2.929  1.00 38.43  ?  164 PHE   B CD2   1 
ATOM   3740 C  CE1   . PHE   B 1 164 ? 0.220   -1.078  -3.999  1.00 36.30  ?  164 PHE   B CE1   1 
ATOM   3741 C  CE2   . PHE   B 1 164 ? 2.134   0.155   -3.239  1.00 37.03  ?  164 PHE   B CE2   1 
ATOM   3742 C  CZ    . PHE   B 1 164 ? 1.586   -1.008  -3.773  1.00 36.08  ?  164 PHE   B CZ    1 
ATOM   3743 N  N     . ASN   B 1 165 ? -3.259  2.732   -4.879  1.00 44.14  ?  165 ASN   B N     1 
ATOM   3744 C  CA    . ASN   B 1 165 ? -4.182  2.146   -5.863  1.00 44.43  ?  165 ASN   B CA    1 
ATOM   3745 C  C     . ASN   B 1 165 ? -4.106  2.836   -7.217  1.00 44.98  ?  165 ASN   B C     1 
ATOM   3746 O  O     . ASN   B 1 165 ? -4.120  2.173   -8.267  1.00 44.63  ?  165 ASN   B O     1 
ATOM   3747 C  CB    . ASN   B 1 165 ? -5.627  2.140   -5.340  1.00 44.39  ?  165 ASN   B CB    1 
ATOM   3748 C  CG    . ASN   B 1 165 ? -5.886  1.056   -4.308  1.00 42.06  ?  165 ASN   B CG    1 
ATOM   3749 O  OD1   . ASN   B 1 165 ? -5.044  0.210   -4.050  1.00 40.18  ?  165 ASN   B OD1   1 
ATOM   3750 N  ND2   . ASN   B 1 165 ? -7.071  1.064   -3.741  1.00 42.84  ?  165 ASN   B ND2   1 
ATOM   3751 N  N     . ALA   B 1 166 ? -4.005  4.166   -7.178  1.00 47.65  ?  166 ALA   B N     1 
ATOM   3752 C  CA    . ALA   B 1 166 ? -3.944  4.996   -8.388  1.00 50.39  ?  166 ALA   B CA    1 
ATOM   3753 C  C     . ALA   B 1 166 ? -2.832  4.535   -9.345  1.00 49.28  ?  166 ALA   B C     1 
ATOM   3754 O  O     . ALA   B 1 166 ? -3.040  4.448   -10.565 1.00 46.31  ?  166 ALA   B O     1 
ATOM   3755 C  CB    . ALA   B 1 166 ? -3.774  6.477   -8.012  1.00 50.80  ?  166 ALA   B CB    1 
ATOM   3756 N  N     . LEU   B 1 167 ? -1.680  4.181   -8.773  1.00 47.49  ?  167 LEU   B N     1 
ATOM   3757 C  CA    . LEU   B 1 167 ? -0.518  3.710   -9.531  1.00 45.04  ?  167 LEU   B CA    1 
ATOM   3758 C  C     . LEU   B 1 167 ? -0.590  2.231   -9.921  1.00 43.51  ?  167 LEU   B C     1 
ATOM   3759 O  O     . LEU   B 1 167 ? -0.248  1.853   -11.043 1.00 41.96  ?  167 LEU   B O     1 
ATOM   3760 C  CB    . LEU   B 1 167 ? 0.750   3.947   -8.716  1.00 46.75  ?  167 LEU   B CB    1 
ATOM   3761 C  CG    . LEU   B 1 167 ? 1.060   5.429   -8.451  1.00 51.66  ?  167 LEU   B CG    1 
ATOM   3762 C  CD1   . LEU   B 1 167 ? 1.955   5.594   -7.223  1.00 52.87  ?  167 LEU   B CD1   1 
ATOM   3763 C  CD2   . LEU   B 1 167 ? 1.685   6.086   -9.681  1.00 53.10  ?  167 LEU   B CD2   1 
ATOM   3764 N  N     . TYR   B 1 168 ? -1.046  1.402   -8.986  1.00 40.49  ?  168 TYR   B N     1 
ATOM   3765 C  CA    . TYR   B 1 168 ? -0.895  -0.069  -9.097  1.00 40.80  ?  168 TYR   B CA    1 
ATOM   3766 C  C     . TYR   B 1 168 ? -2.191  -0.871  -9.282  1.00 39.96  ?  168 TYR   B C     1 
ATOM   3767 O  O     . TYR   B 1 168 ? -2.123  -2.066  -9.538  1.00 42.82  ?  168 TYR   B O     1 
ATOM   3768 C  CB    . TYR   B 1 168 ? -0.141  -0.586  -7.863  1.00 41.06  ?  168 TYR   B CB    1 
ATOM   3769 C  CG    . TYR   B 1 168 ? 1.206   0.077   -7.670  1.00 40.88  ?  168 TYR   B CG    1 
ATOM   3770 C  CD1   . TYR   B 1 168 ? 2.221   -0.090  -8.600  1.00 42.25  ?  168 TYR   B CD1   1 
ATOM   3771 C  CD2   . TYR   B 1 168 ? 1.455   0.905   -6.572  1.00 40.86  ?  168 TYR   B CD2   1 
ATOM   3772 C  CE1   . TYR   B 1 168 ? 3.455   0.532   -8.435  1.00 42.32  ?  168 TYR   B CE1   1 
ATOM   3773 C  CE2   . TYR   B 1 168 ? 2.686   1.526   -6.401  1.00 39.00  ?  168 TYR   B CE2   1 
ATOM   3774 C  CZ    . TYR   B 1 168 ? 3.676   1.336   -7.341  1.00 38.32  ?  168 TYR   B CZ    1 
ATOM   3775 O  OH    . TYR   B 1 168 ? 4.892   1.928   -7.168  1.00 39.78  ?  168 TYR   B OH    1 
ATOM   3776 N  N     . GLY   B 1 169 ? -3.353  -0.222  -9.175  1.00 40.86  ?  169 GLY   B N     1 
ATOM   3777 C  CA    . GLY   B 1 169 ? -4.657  -0.917  -9.254  1.00 41.83  ?  169 GLY   B CA    1 
ATOM   3778 C  C     . GLY   B 1 169 ? -5.250  -1.162  -7.878  1.00 41.45  ?  169 GLY   B C     1 
ATOM   3779 O  O     . GLY   B 1 169 ? -4.779  -0.592  -6.897  1.00 42.78  ?  169 GLY   B O     1 
ATOM   3780 N  N     . GLU   B 1 170 ? -6.277  -2.013  -7.805  1.00 45.22  ?  170 GLU   B N     1 
ATOM   3781 C  CA    . GLU   B 1 170 ? -7.093  -2.168  -6.581  1.00 43.70  ?  170 GLU   B CA    1 
ATOM   3782 C  C     . GLU   B 1 170 ? -6.460  -3.149  -5.575  1.00 43.33  ?  170 GLU   B C     1 
ATOM   3783 O  O     . GLU   B 1 170 ? -7.002  -4.244  -5.321  1.00 46.11  ?  170 GLU   B O     1 
ATOM   3784 C  CB    . GLU   B 1 170 ? -8.515  -2.614  -6.960  1.00 46.34  ?  170 GLU   B CB    1 
ATOM   3785 N  N     . ILE   B 1 171 ? -5.318  -2.753  -5.003  1.00 40.45  ?  171 ILE   B N     1 
ATOM   3786 C  CA    . ILE   B 1 171 ? -4.549  -3.612  -4.093  1.00 36.86  ?  171 ILE   B CA    1 
ATOM   3787 C  C     . ILE   B 1 171 ? -5.156  -3.462  -2.699  1.00 35.67  ?  171 ILE   B C     1 
ATOM   3788 O  O     . ILE   B 1 171 ? -5.339  -4.443  -2.004  1.00 33.82  ?  171 ILE   B O     1 
ATOM   3789 C  CB    . ILE   B 1 171 ? -3.035  -3.259  -4.075  1.00 38.88  ?  171 ILE   B CB    1 
ATOM   3790 C  CG1   . ILE   B 1 171 ? -2.453  -3.152  -5.512  1.00 39.59  ?  171 ILE   B CG1   1 
ATOM   3791 C  CG2   . ILE   B 1 171 ? -2.243  -4.268  -3.251  1.00 37.17  ?  171 ILE   B CG2   1 
ATOM   3792 C  CD1   . ILE   B 1 171 ? -2.500  -4.421  -6.338  1.00 42.70  ?  171 ILE   B CD1   1 
ATOM   3793 N  N     . PHE   B 1 172 ? -5.472  -2.218  -2.317  1.00 28.99  ?  172 PHE   B N     1 
ATOM   3794 C  CA    . PHE   B 1 172 ? -6.083  -1.928  -1.035  1.00 34.27  ?  172 PHE   B CA    1 
ATOM   3795 C  C     . PHE   B 1 172 ? -7.567  -1.638  -1.177  1.00 39.30  ?  172 PHE   B C     1 
ATOM   3796 O  O     . PHE   B 1 172 ? -8.007  -1.181  -2.241  1.00 40.19  ?  172 PHE   B O     1 
ATOM   3797 C  CB    . PHE   B 1 172 ? -5.375  -0.743  -0.343  1.00 32.71  ?  172 PHE   B CB    1 
ATOM   3798 C  CG    . PHE   B 1 172 ? -3.888  -0.954  -0.147  1.00 32.24  ?  172 PHE   B CG    1 
ATOM   3799 C  CD1   . PHE   B 1 172 ? -3.414  -2.117  0.441   1.00 31.59  ?  172 PHE   B CD1   1 
ATOM   3800 C  CD2   . PHE   B 1 172 ? -2.965  0.019   -0.541  1.00 33.08  ?  172 PHE   B CD2   1 
ATOM   3801 C  CE1   . PHE   B 1 172 ? -2.042  -2.317  0.634   1.00 30.80  ?  172 PHE   B CE1   1 
ATOM   3802 C  CE2   . PHE   B 1 172 ? -1.599  -0.179  -0.358  1.00 31.55  ?  172 PHE   B CE2   1 
ATOM   3803 C  CZ    . PHE   B 1 172 ? -1.142  -1.345  0.246   1.00 31.57  ?  172 PHE   B CZ    1 
ATOM   3804 N  N     . LYS   B 1 173 ? -8.319  -1.914  -0.104  1.00 37.31  ?  173 LYS   B N     1 
ATOM   3805 C  CA    . LYS   B 1 173 ? -9.612  -1.268  0.128   1.00 42.34  ?  173 LYS   B CA    1 
ATOM   3806 C  C     . LYS   B 1 173 ? -9.358  0.082   0.821   1.00 44.59  ?  173 LYS   B C     1 
ATOM   3807 O  O     . LYS   B 1 173 ? -8.412  0.224   1.615   1.00 38.61  ?  173 LYS   B O     1 
ATOM   3808 C  CB    . LYS   B 1 173 ? -10.521 -2.133  1.015   1.00 41.03  ?  173 LYS   B CB    1 
ATOM   3809 C  CG    . LYS   B 1 173 ? -10.710 -3.576  0.558   1.00 42.27  ?  173 LYS   B CG    1 
ATOM   3810 C  CD    . LYS   B 1 173 ? -11.408 -3.699  -0.786  1.00 47.16  ?  173 LYS   B CD    1 
ATOM   3811 C  CE    . LYS   B 1 173 ? -12.295 -4.941  -0.828  1.00 46.23  ?  173 LYS   B CE    1 
ATOM   3812 N  NZ    . LYS   B 1 173 ? -12.790 -5.187  -2.204  1.00 50.89  ?  173 LYS   B NZ    1 
ATOM   3813 N  N     . VAL   B 1 174 ? -10.207 1.069   0.541   1.00 46.02  ?  174 VAL   B N     1 
ATOM   3814 C  CA    . VAL   B 1 174 ? -10.172 2.351   1.255   1.00 45.33  ?  174 VAL   B CA    1 
ATOM   3815 C  C     . VAL   B 1 174 ? -11.008 2.240   2.547   1.00 46.21  ?  174 VAL   B C     1 
ATOM   3816 O  O     . VAL   B 1 174 ? -12.226 2.104   2.491   1.00 46.10  ?  174 VAL   B O     1 
ATOM   3817 C  CB    . VAL   B 1 174 ? -10.677 3.496   0.358   1.00 49.29  ?  174 VAL   B CB    1 
ATOM   3818 C  CG1   . VAL   B 1 174 ? -10.703 4.836   1.111   1.00 48.63  ?  174 VAL   B CG1   1 
ATOM   3819 C  CG2   . VAL   B 1 174 ? -9.809  3.604   -0.900  1.00 47.30  ?  174 VAL   B CG2   1 
ATOM   3820 N  N     . PRO   B 1 175 ? -10.358 2.317   3.720   1.00 48.68  ?  175 PRO   B N     1 
ATOM   3821 C  CA    . PRO   B 1 175 ? -11.091 2.177   4.988   1.00 51.48  ?  175 PRO   B CA    1 
ATOM   3822 C  C     . PRO   B 1 175 ? -11.969 3.400   5.324   1.00 52.83  ?  175 PRO   B C     1 
ATOM   3823 O  O     . PRO   B 1 175 ? -11.751 4.487   4.784   1.00 56.38  ?  175 PRO   B O     1 
ATOM   3824 C  CB    . PRO   B 1 175 ? -9.961  2.023   6.015   1.00 49.19  ?  175 PRO   B CB    1 
ATOM   3825 C  CG    . PRO   B 1 175 ? -8.854  2.851   5.448   1.00 47.93  ?  175 PRO   B CG    1 
ATOM   3826 C  CD    . PRO   B 1 175 ? -8.942  2.666   3.954   1.00 48.50  ?  175 PRO   B CD    1 
ATOM   3827 N  N     . GLU   B 1 176 ? -12.948 3.200   6.208   1.00 51.05  ?  176 GLU   B N     1 
ATOM   3828 C  CA    . GLU   B 1 176 ? -13.870 4.256   6.636   1.00 51.82  ?  176 GLU   B CA    1 
ATOM   3829 C  C     . GLU   B 1 176 ? -13.975 4.254   8.161   1.00 54.13  ?  176 GLU   B C     1 
ATOM   3830 O  O     . GLU   B 1 176 ? -14.019 3.184   8.773   1.00 52.17  ?  176 GLU   B O     1 
ATOM   3831 C  CB    . GLU   B 1 176 ? -15.256 4.036   6.013   1.00 52.75  ?  176 GLU   B CB    1 
ATOM   3832 C  CG    . GLU   B 1 176 ? -15.287 4.128   4.487   1.00 54.25  ?  176 GLU   B CG    1 
ATOM   3833 C  CD    . GLU   B 1 176 ? -14.928 5.504   3.956   1.00 58.69  ?  176 GLU   B CD    1 
ATOM   3834 O  OE1   . GLU   B 1 176 ? -15.007 6.489   4.725   1.00 60.19  ?  176 GLU   B OE1   1 
ATOM   3835 O  OE2   . GLU   B 1 176 ? -14.556 5.593   2.762   1.00 59.52  ?  176 GLU   B OE2   1 
ATOM   3836 N  N     . PRO   B 1 177 ? -14.029 5.445   8.783   1.00 57.71  ?  177 PRO   B N     1 
ATOM   3837 C  CA    . PRO   B 1 177 ? -14.090 5.515   10.251  1.00 60.02  ?  177 PRO   B CA    1 
ATOM   3838 C  C     . PRO   B 1 177 ? -15.464 5.120   10.807  1.00 58.64  ?  177 PRO   B C     1 
ATOM   3839 O  O     . PRO   B 1 177 ? -16.485 5.393   10.191  1.00 62.69  ?  177 PRO   B O     1 
ATOM   3840 C  CB    . PRO   B 1 177 ? -13.795 6.994   10.547  1.00 59.90  ?  177 PRO   B CB    1 
ATOM   3841 C  CG    . PRO   B 1 177 ? -14.289 7.710   9.334   1.00 61.30  ?  177 PRO   B CG    1 
ATOM   3842 C  CD    . PRO   B 1 177 ? -14.099 6.782   8.162   1.00 60.17  ?  177 PRO   B CD    1 
ATOM   3843 N  N     . PHE   B 1 178 ? -15.465 4.462   11.960  1.00 57.31  ?  178 PHE   B N     1 
ATOM   3844 C  CA    . PHE   B 1 178 ? -16.680 4.169   12.719  1.00 56.11  ?  178 PHE   B CA    1 
ATOM   3845 C  C     . PHE   B 1 178 ? -16.489 4.707   14.153  1.00 58.34  ?  178 PHE   B C     1 
ATOM   3846 O  O     . PHE   B 1 178 ? -15.946 4.031   15.045  1.00 52.76  ?  178 PHE   B O     1 
ATOM   3847 C  CB    . PHE   B 1 178 ? -16.989 2.669   12.688  1.00 57.69  ?  178 PHE   B CB    1 
ATOM   3848 C  CG    . PHE   B 1 178 ? -18.302 2.301   13.322  1.00 60.83  ?  178 PHE   B CG    1 
ATOM   3849 C  CD1   . PHE   B 1 178 ? -18.373 1.942   14.672  1.00 62.33  ?  178 PHE   B CD1   1 
ATOM   3850 C  CD2   . PHE   B 1 178 ? -19.471 2.304   12.574  1.00 62.18  ?  178 PHE   B CD2   1 
ATOM   3851 C  CE1   . PHE   B 1 178 ? -19.586 1.609   15.259  1.00 61.81  ?  178 PHE   B CE1   1 
ATOM   3852 C  CE2   . PHE   B 1 178 ? -20.690 1.972   13.162  1.00 65.13  ?  178 PHE   B CE2   1 
ATOM   3853 C  CZ    . PHE   B 1 178 ? -20.747 1.623   14.506  1.00 62.01  ?  178 PHE   B CZ    1 
ATOM   3854 N  N     . ILE   B 1 179 ? -16.925 5.952   14.344  1.00 56.19  ?  179 ILE   B N     1 
ATOM   3855 C  CA    . ILE   B 1 179 ? -16.807 6.669   15.615  1.00 58.77  ?  179 ILE   B CA    1 
ATOM   3856 C  C     . ILE   B 1 179 ? -18.202 6.732   16.267  1.00 60.66  ?  179 ILE   B C     1 
ATOM   3857 O  O     . ILE   B 1 179 ? -19.157 7.137   15.596  1.00 61.33  ?  179 ILE   B O     1 
ATOM   3858 C  CB    . ILE   B 1 179 ? -16.202 8.085   15.368  1.00 59.37  ?  179 ILE   B CB    1 
ATOM   3859 C  CG1   . ILE   B 1 179 ? -14.706 7.939   15.010  1.00 60.00  ?  179 ILE   B CG1   1 
ATOM   3860 C  CG2   . ILE   B 1 179 ? -16.399 9.004   16.575  1.00 58.47  ?  179 ILE   B CG2   1 
ATOM   3861 C  CD1   . ILE   B 1 179 ? -14.017 9.193   14.518  1.00 59.46  ?  179 ILE   B CD1   1 
ATOM   3862 N  N     . PRO   B 1 180 ? -18.327 6.341   17.565  1.00 60.65  ?  180 PRO   B N     1 
ATOM   3863 C  CA    . PRO   B 1 180 ? -19.648 6.306   18.216  1.00 62.92  ?  180 PRO   B CA    1 
ATOM   3864 C  C     . PRO   B 1 180 ? -20.318 7.679   18.344  1.00 70.14  ?  180 PRO   B C     1 
ATOM   3865 O  O     . PRO   B 1 180 ? -19.644 8.718   18.297  1.00 65.44  ?  180 PRO   B O     1 
ATOM   3866 C  CB    . PRO   B 1 180 ? -19.342 5.753   19.611  1.00 61.52  ?  180 PRO   B CB    1 
ATOM   3867 C  CG    . PRO   B 1 180 ? -17.918 6.113   19.853  1.00 62.25  ?  180 PRO   B CG    1 
ATOM   3868 C  CD    . PRO   B 1 180 ? -17.249 6.008   18.519  1.00 59.44  ?  180 PRO   B CD    1 
ATOM   3869 N  N     . LYS   B 1 181 ? -21.641 7.659   18.504  1.00 75.16  ?  181 LYS   B N     1 
ATOM   3870 C  CA    . LYS   B 1 181 ? -22.439 8.875   18.691  1.00 74.89  ?  181 LYS   B CA    1 
ATOM   3871 C  C     . LYS   B 1 181 ? -22.242 9.473   20.086  1.00 72.69  ?  181 LYS   B C     1 
ATOM   3872 O  O     . LYS   B 1 181 ? -22.231 10.688  20.237  1.00 78.72  ?  181 LYS   B O     1 
ATOM   3873 C  CB    . LYS   B 1 181 ? -23.931 8.594   18.435  1.00 76.60  ?  181 LYS   B CB    1 
ATOM   3874 C  CG    . LYS   B 1 181 ? -24.315 8.343   16.974  1.00 76.22  ?  181 LYS   B CG    1 
ATOM   3875 C  CD    . LYS   B 1 181 ? -23.627 9.274   15.978  1.00 77.43  ?  181 LYS   B CD    1 
ATOM   3876 N  N     . SER   B 1 182 ? -22.072 8.613   21.087  1.00 72.18  ?  182 SER   B N     1 
ATOM   3877 C  CA    . SER   B 1 182 ? -21.850 9.019   22.478  1.00 72.20  ?  182 SER   B CA    1 
ATOM   3878 C  C     . SER   B 1 182 ? -20.559 8.407   23.038  1.00 70.07  ?  182 SER   B C     1 
ATOM   3879 O  O     . SER   B 1 182 ? -20.327 7.210   22.910  1.00 69.04  ?  182 SER   B O     1 
ATOM   3880 C  CB    . SER   B 1 182 ? -23.032 8.586   23.348  1.00 75.67  ?  182 SER   B CB    1 
ATOM   3881 O  OG    . SER   B 1 182 ? -23.086 7.172   23.516  1.00 78.44  ?  182 SER   B OG    1 
ATOM   3882 N  N     . GLY   B 1 183 ? -19.733 9.237   23.665  1.00 68.70  ?  183 GLY   B N     1 
ATOM   3883 C  CA    . GLY   B 1 183 ? -18.505 8.781   24.323  1.00 67.09  ?  183 GLY   B CA    1 
ATOM   3884 C  C     . GLY   B 1 183 ? -17.333 8.496   23.398  1.00 64.15  ?  183 GLY   B C     1 
ATOM   3885 O  O     . GLY   B 1 183 ? -16.538 7.595   23.681  1.00 62.41  ?  183 GLY   B O     1 
ATOM   3886 N  N     . ALA   B 1 184 ? -17.224 9.267   22.310  1.00 58.68  ?  184 ALA   B N     1 
ATOM   3887 C  CA    . ALA   B 1 184 ? -16.089 9.182   21.382  1.00 60.15  ?  184 ALA   B CA    1 
ATOM   3888 C  C     . ALA   B 1 184 ? -14.863 9.925   21.913  1.00 61.34  ?  184 ALA   B C     1 
ATOM   3889 O  O     . ALA   B 1 184 ? -13.750 9.713   21.415  1.00 59.15  ?  184 ALA   B O     1 
ATOM   3890 C  CB    . ALA   B 1 184 ? -16.471 9.730   20.010  1.00 62.60  ?  184 ALA   B CB    1 
ATOM   3891 N  N     . ARG   B 1 185 ? -15.079 10.804  22.898  1.00 66.06  ?  185 ARG   B N     1 
ATOM   3892 C  CA    . ARG   B 1 185 ? -14.014 11.588  23.539  1.00 68.19  ?  185 ARG   B CA    1 
ATOM   3893 C  C     . ARG   B 1 185 ? -14.416 11.939  24.988  1.00 68.16  ?  185 ARG   B C     1 
ATOM   3894 O  O     . ARG   B 1 185 ? -14.826 13.075  25.303  1.00 65.72  ?  185 ARG   B O     1 
ATOM   3895 C  CB    . ARG   B 1 185 ? -13.694 12.849  22.712  1.00 69.07  ?  185 ARG   B CB    1 
ATOM   3896 C  CG    . ARG   B 1 185 ? -12.357 13.497  23.057  1.00 75.54  ?  185 ARG   B CG    1 
ATOM   3897 C  CD    . ARG   B 1 185 ? -11.833 14.402  21.944  1.00 77.15  ?  185 ARG   B CD    1 
ATOM   3898 N  NE    . ARG   B 1 185 ? -10.874 15.375  22.473  1.00 79.69  ?  185 ARG   B NE    1 
ATOM   3899 C  CZ    . ARG   B 1 185 ? -11.187 16.558  23.015  1.00 78.77  ?  185 ARG   B CZ    1 
ATOM   3900 N  NH1   . ARG   B 1 185 ? -12.452 16.972  23.101  1.00 76.44  ?  185 ARG   B NH1   1 
ATOM   3901 N  NH2   . ARG   B 1 185 ? -10.216 17.344  23.477  1.00 77.54  ?  185 ARG   B NH2   1 
ATOM   3902 N  N     . VAL   B 1 186 ? -14.284 10.950  25.869  1.00 61.34  ?  186 VAL   B N     1 
ATOM   3903 C  CA    . VAL   B 1 186 ? -14.646 11.114  27.280  1.00 62.36  ?  186 VAL   B CA    1 
ATOM   3904 C  C     . VAL   B 1 186 ? -13.559 11.975  27.963  1.00 62.71  ?  186 VAL   B C     1 
ATOM   3905 O  O     . VAL   B 1 186 ? -12.352 11.773  27.767  1.00 59.38  ?  186 VAL   B O     1 
ATOM   3906 C  CB    . VAL   B 1 186 ? -14.853 9.754   28.002  1.00 62.93  ?  186 VAL   B CB    1 
ATOM   3907 C  CG1   . VAL   B 1 186 ? -15.389 9.957   29.417  1.00 62.38  ?  186 VAL   B CG1   1 
ATOM   3908 C  CG2   . VAL   B 1 186 ? -15.822 8.851   27.234  1.00 62.05  ?  186 VAL   B CG2   1 
ATOM   3909 N  N     . MET   B 1 187 ? -14.016 12.940  28.754  1.00 64.61  ?  187 MET   B N     1 
ATOM   3910 C  CA    . MET   B 1 187 ? -13.169 13.995  29.324  1.00 64.40  ?  187 MET   B CA    1 
ATOM   3911 C  C     . MET   B 1 187 ? -12.702 13.687  30.750  1.00 58.61  ?  187 MET   B C     1 
ATOM   3912 O  O     . MET   B 1 187 ? -13.354 12.953  31.478  1.00 53.86  ?  187 MET   B O     1 
ATOM   3913 C  CB    . MET   B 1 187 ? -13.931 15.328  29.288  1.00 63.17  ?  187 MET   B CB    1 
ATOM   3914 C  CG    . MET   B 1 187 ? -14.444 15.694  27.898  1.00 67.20  ?  187 MET   B CG    1 
ATOM   3915 S  SD    . MET   B 1 187 ? -13.152 15.654  26.627  1.00 65.78  ?  187 MET   B SD    1 
ATOM   3916 C  CE    . MET   B 1 187 ? -12.024 16.879  27.291  1.00 67.38  ?  187 MET   B CE    1 
ATOM   3917 N  N     . SER   B 1 188 ? -11.561 14.260  31.128  1.00 52.96  ?  188 SER   B N     1 
ATOM   3918 C  CA    . SER   B 1 188 ? -10.959 14.035  32.434  1.00 53.41  ?  188 SER   B CA    1 
ATOM   3919 C  C     . SER   B 1 188 ? -11.825 14.615  33.563  1.00 56.19  ?  188 SER   B C     1 
ATOM   3920 O  O     . SER   B 1 188 ? -12.483 15.654  33.408  1.00 52.17  ?  188 SER   B O     1 
ATOM   3921 C  CB    . SER   B 1 188 ? -9.546  14.615  32.468  1.00 55.18  ?  188 SER   B CB    1 
ATOM   3922 O  OG    . SER   B 1 188 ? -8.726  14.053  31.443  1.00 54.58  ?  188 SER   B OG    1 
ATOM   3923 N  N     . LEU   B 1 189 ? -11.836 13.918  34.692  1.00 57.89  ?  189 LEU   B N     1 
ATOM   3924 C  CA    . LEU   B 1 189 ? -12.760 14.227  35.794  1.00 61.25  ?  189 LEU   B CA    1 
ATOM   3925 C  C     . LEU   B 1 189 ? -12.564 15.607  36.411  1.00 57.50  ?  189 LEU   B C     1 
ATOM   3926 O  O     . LEU   B 1 189 ? -13.543 16.312  36.672  1.00 60.85  ?  189 LEU   B O     1 
ATOM   3927 C  CB    . LEU   B 1 189 ? -12.709 13.130  36.877  1.00 59.57  ?  189 LEU   B CB    1 
ATOM   3928 C  CG    . LEU   B 1 189 ? -13.421 11.812  36.528  1.00 58.56  ?  189 LEU   B CG    1 
ATOM   3929 C  CD1   . LEU   B 1 189 ? -13.374 10.858  37.709  1.00 59.11  ?  189 LEU   B CD1   1 
ATOM   3930 C  CD2   . LEU   B 1 189 ? -14.866 12.023  36.104  1.00 54.87  ?  189 LEU   B CD2   1 
ATOM   3931 N  N     . LEU   B 1 190 ? -11.309 15.977  36.633  1.00 57.24  ?  190 LEU   B N     1 
ATOM   3932 C  CA    . LEU   B 1 190 ? -10.942 17.289  37.191  1.00 58.94  ?  190 LEU   B CA    1 
ATOM   3933 C  C     . LEU   B 1 190 ? -10.522 18.300  36.133  1.00 60.66  ?  190 LEU   B C     1 
ATOM   3934 O  O     . LEU   B 1 190 ? -10.342 19.465  36.465  1.00 62.13  ?  190 LEU   B O     1 
ATOM   3935 C  CB    . LEU   B 1 190 ? -9.827  17.135  38.234  1.00 59.10  ?  190 LEU   B CB    1 
ATOM   3936 C  CG    . LEU   B 1 190 ? -9.928  15.930  39.193  1.00 61.36  ?  190 LEU   B CG    1 
ATOM   3937 C  CD1   . LEU   B 1 190 ? -8.948  16.071  40.350  1.00 61.60  ?  190 LEU   B CD1   1 
ATOM   3938 C  CD2   . LEU   B 1 190 ? -11.331 15.714  39.750  1.00 62.77  ?  190 LEU   B CD2   1 
ATOM   3939 N  N     . GLU   B 1 191 ? -10.355 17.855  34.884  1.00 63.85  ?  191 GLU   B N     1 
ATOM   3940 C  CA    . GLU   B 1 191 ? -10.021 18.730  33.755  1.00 67.98  ?  191 GLU   B CA    1 
ATOM   3941 C  C     . GLU   B 1 191 ? -10.939 18.373  32.572  1.00 70.90  ?  191 GLU   B C     1 
ATOM   3942 O  O     . GLU   B 1 191 ? -10.486 17.747  31.612  1.00 74.68  ?  191 GLU   B O     1 
ATOM   3943 C  CB    . GLU   B 1 191 ? -8.540  18.573  33.367  1.00 68.31  ?  191 GLU   B CB    1 
ATOM   3944 N  N     . PRO   B 1 192 ? -12.227 18.788  32.624  1.00 67.93  ?  192 PRO   B N     1 
ATOM   3945 C  CA    . PRO   B 1 192 ? -13.234 18.388  31.622  1.00 68.09  ?  192 PRO   B CA    1 
ATOM   3946 C  C     . PRO   B 1 192 ? -13.022 18.961  30.203  1.00 70.36  ?  192 PRO   B C     1 
ATOM   3947 O  O     . PRO   B 1 192 ? -13.835 18.701  29.314  1.00 69.72  ?  192 PRO   B O     1 
ATOM   3948 C  CB    . PRO   B 1 192 ? -14.556 18.884  32.237  1.00 68.39  ?  192 PRO   B CB    1 
ATOM   3949 C  CG    . PRO   B 1 192 ? -14.157 20.039  33.085  1.00 69.44  ?  192 PRO   B CG    1 
ATOM   3950 C  CD    . PRO   B 1 192 ? -12.802 19.684  33.641  1.00 70.28  ?  192 PRO   B CD    1 
ATOM   3951 N  N     . THR   B 1 193 ? -11.960 19.750  30.017  1.00 71.03  ?  193 THR   B N     1 
ATOM   3952 C  CA    . THR   B 1 193 ? -11.510 20.218  28.703  1.00 73.76  ?  193 THR   B CA    1 
ATOM   3953 C  C     . THR   B 1 193 ? -10.310 19.412  28.163  1.00 70.78  ?  193 THR   B C     1 
ATOM   3954 O  O     . THR   B 1 193 ? -9.941  19.579  27.002  1.00 66.87  ?  193 THR   B O     1 
ATOM   3955 C  CB    . THR   B 1 193 ? -11.153 21.730  28.753  1.00 76.42  ?  193 THR   B CB    1 
ATOM   3956 O  OG1   . THR   B 1 193 ? -10.025 21.949  29.615  1.00 80.02  ?  193 THR   B OG1   1 
ATOM   3957 C  CG2   . THR   B 1 193 ? -12.335 22.553  29.261  1.00 73.36  ?  193 THR   B CG2   1 
ATOM   3958 N  N     . LYS   B 1 194 ? -9.740  18.532  28.997  1.00 69.20  ?  194 LYS   B N     1 
ATOM   3959 C  CA    . LYS   B 1 194 ? -8.626  17.646  28.637  1.00 69.65  ?  194 LYS   B CA    1 
ATOM   3960 C  C     . LYS   B 1 194 ? -9.130  16.204  28.548  1.00 69.15  ?  194 LYS   B C     1 
ATOM   3961 O  O     . LYS   B 1 194 ? -9.670  15.673  29.519  1.00 71.46  ?  194 LYS   B O     1 
ATOM   3962 C  CB    . LYS   B 1 194 ? -7.514  17.727  29.685  1.00 70.99  ?  194 LYS   B CB    1 
ATOM   3963 N  N     . LYS   B 1 195 ? -8.971  15.588  27.378  1.00 64.53  ?  195 LYS   B N     1 
ATOM   3964 C  CA    . LYS   B 1 195 ? -9.365  14.190  27.125  1.00 65.45  ?  195 LYS   B CA    1 
ATOM   3965 C  C     . LYS   B 1 195 ? -8.878  13.250  28.237  1.00 59.74  ?  195 LYS   B C     1 
ATOM   3966 O  O     . LYS   B 1 195 ? -7.791  13.450  28.792  1.00 55.39  ?  195 LYS   B O     1 
ATOM   3967 C  CB    . LYS   B 1 195 ? -8.796  13.734  25.766  1.00 67.18  ?  195 LYS   B CB    1 
ATOM   3968 C  CG    . LYS   B 1 195 ? -9.199  12.333  25.325  1.00 69.82  ?  195 LYS   B CG    1 
ATOM   3969 C  CD    . LYS   B 1 195 ? -8.523  11.899  24.023  1.00 72.54  ?  195 LYS   B CD    1 
ATOM   3970 C  CE    . LYS   B 1 195 ? -7.041  11.591  24.182  1.00 70.92  ?  195 LYS   B CE    1 
ATOM   3971 N  NZ    . LYS   B 1 195 ? -6.784  10.354  24.983  1.00 67.10  ?  195 LYS   B NZ    1 
ATOM   3972 N  N     . MET   B 1 196 ? -9.685  12.239  28.564  1.00 58.32  ?  196 MET   B N     1 
ATOM   3973 C  CA    . MET   B 1 196 ? -9.296  11.237  29.569  1.00 59.28  ?  196 MET   B CA    1 
ATOM   3974 C  C     . MET   B 1 196 ? -8.156  10.374  29.012  1.00 60.69  ?  196 MET   B C     1 
ATOM   3975 O  O     . MET   B 1 196 ? -8.325  9.704   27.989  1.00 56.99  ?  196 MET   B O     1 
ATOM   3976 C  CB    . MET   B 1 196 ? -10.492 10.365  29.980  1.00 59.71  ?  196 MET   B CB    1 
ATOM   3977 C  CG    . MET   B 1 196 ? -10.333 9.705   31.346  1.00 57.73  ?  196 MET   B CG    1 
ATOM   3978 S  SD    . MET   B 1 196 ? -11.661 8.554   31.825  1.00 56.20  ?  196 MET   B SD    1 
ATOM   3979 C  CE    . MET   B 1 196 ? -13.065 9.660   31.993  1.00 55.07  ?  196 MET   B CE    1 
ATOM   3980 N  N     . SER   B 1 197 ? -6.995  10.437  29.674  1.00 64.39  ?  197 SER   B N     1 
ATOM   3981 C  CA    . SER   B 1 197 ? -5.774  9.729   29.262  1.00 66.29  ?  197 SER   B CA    1 
ATOM   3982 C  C     . SER   B 1 197 ? -5.579  8.457   30.084  1.00 62.61  ?  197 SER   B C     1 
ATOM   3983 O  O     . SER   B 1 197 ? -5.881  8.430   31.271  1.00 64.28  ?  197 SER   B O     1 
ATOM   3984 C  CB    . SER   B 1 197 ? -4.561  10.656  29.427  1.00 65.54  ?  197 SER   B CB    1 
ATOM   3985 O  OG    . SER   B 1 197 ? -3.334  9.975   29.226  1.00 64.47  ?  197 SER   B OG    1 
ATOM   3986 N  N     . LYS   B 1 198 ? -5.049  7.412   29.450  1.00 64.02  ?  198 LYS   B N     1 
ATOM   3987 C  CA    . LYS   B 1 198 ? -4.757  6.143   30.133  1.00 64.15  ?  198 LYS   B CA    1 
ATOM   3988 C  C     . LYS   B 1 198 ? -3.348  6.133   30.762  1.00 64.96  ?  198 LYS   B C     1 
ATOM   3989 O  O     . LYS   B 1 198 ? -2.917  5.123   31.325  1.00 68.98  ?  198 LYS   B O     1 
ATOM   3990 C  CB    . LYS   B 1 198 ? -4.967  4.957   29.173  1.00 64.04  ?  198 LYS   B CB    1 
ATOM   3991 C  CG    . LYS   B 1 198 ? -3.924  4.770   28.088  1.00 63.90  ?  198 LYS   B CG    1 
ATOM   3992 C  CD    . LYS   B 1 198 ? -4.241  3.546   27.235  1.00 64.02  ?  198 LYS   B CD    1 
ATOM   3993 C  CE    . LYS   B 1 198 ? -3.384  3.476   25.976  1.00 62.06  ?  198 LYS   B CE    1 
ATOM   3994 N  NZ    . LYS   B 1 198 ? -1.934  3.540   26.277  1.00 59.67  ?  198 LYS   B NZ    1 
ATOM   3995 N  N     . SER   B 1 199 ? -2.644  7.260   30.648  1.00 67.27  ?  199 SER   B N     1 
ATOM   3996 C  CA    . SER   B 1 199 ? -1.308  7.460   31.231  1.00 69.87  ?  199 SER   B CA    1 
ATOM   3997 C  C     . SER   B 1 199 ? -1.212  8.815   31.954  1.00 72.23  ?  199 SER   B C     1 
ATOM   3998 O  O     . SER   B 1 199 ? -0.123  9.388   32.058  1.00 72.81  ?  199 SER   B O     1 
ATOM   3999 C  CB    . SER   B 1 199 ? -0.234  7.367   30.127  1.00 67.73  ?  199 SER   B CB    1 
ATOM   4000 O  OG    . SER   B 1 199 ? -0.351  8.418   29.174  1.00 64.96  ?  199 SER   B OG    1 
ATOM   4001 N  N     . ASP   B 1 200 ? -2.349  9.314   32.454  1.00 72.95  ?  200 ASP   B N     1 
ATOM   4002 C  CA    . ASP   B 1 200 ? -2.418  10.606  33.145  1.00 68.99  ?  200 ASP   B CA    1 
ATOM   4003 C  C     . ASP   B 1 200 ? -1.611  10.515  34.447  1.00 70.99  ?  200 ASP   B C     1 
ATOM   4004 O  O     . ASP   B 1 200 ? -1.626  9.490   35.131  1.00 65.41  ?  200 ASP   B O     1 
ATOM   4005 C  CB    . ASP   B 1 200 ? -3.884  10.995  33.420  1.00 65.38  ?  200 ASP   B CB    1 
ATOM   4006 C  CG    . ASP   B 1 200 ? -4.060  12.471  33.774  1.00 62.37  ?  200 ASP   B CG    1 
ATOM   4007 O  OD1   . ASP   B 1 200 ? -3.359  12.974  34.670  1.00 59.03  ?  200 ASP   B OD1   1 
ATOM   4008 O  OD2   . ASP   B 1 200 ? -4.926  13.128  33.168  1.00 58.50  ?  200 ASP   B OD2   1 
ATOM   4009 N  N     . ASP   B 1 201 ? -0.879  11.585  34.754  1.00 80.46  ?  201 ASP   B N     1 
ATOM   4010 C  CA    . ASP   B 1 201 ? -0.131  11.703  36.019  1.00 86.00  ?  201 ASP   B CA    1 
ATOM   4011 C  C     . ASP   B 1 201 ? -1.075  11.686  37.226  1.00 86.16  ?  201 ASP   B C     1 
ATOM   4012 O  O     . ASP   B 1 201 ? -0.732  11.136  38.270  1.00 88.19  ?  201 ASP   B O     1 
ATOM   4013 C  CB    . ASP   B 1 201 ? 0.701   13.000  36.059  1.00 89.54  ?  201 ASP   B CB    1 
ATOM   4014 C  CG    . ASP   B 1 201 ? 1.747   13.086  34.949  1.00 89.55  ?  201 ASP   B CG    1 
ATOM   4015 O  OD1   . ASP   B 1 201 ? 2.133   12.041  34.380  1.00 95.11  ?  201 ASP   B OD1   1 
ATOM   4016 O  OD2   . ASP   B 1 201 ? 2.188   14.217  34.652  1.00 80.56  ?  201 ASP   B OD2   1 
ATOM   4017 N  N     . ASN   B 1 202 ? -2.247  12.308  37.062  1.00 87.19  ?  202 ASN   B N     1 
ATOM   4018 C  CA    . ASN   B 1 202 ? -3.293  12.381  38.085  1.00 82.51  ?  202 ASN   B CA    1 
ATOM   4019 C  C     . ASN   B 1 202 ? -4.375  11.326  37.799  1.00 79.20  ?  202 ASN   B C     1 
ATOM   4020 O  O     . ASN   B 1 202 ? -5.121  11.442  36.828  1.00 84.37  ?  202 ASN   B O     1 
ATOM   4021 C  CB    . ASN   B 1 202 ? -3.889  13.802  38.110  1.00 81.08  ?  202 ASN   B CB    1 
ATOM   4022 C  CG    . ASN   B 1 202 ? -4.656  14.113  39.391  1.00 78.16  ?  202 ASN   B CG    1 
ATOM   4023 O  OD1   . ASN   B 1 202 ? -4.896  13.240  40.224  1.00 73.13  ?  202 ASN   B OD1   1 
ATOM   4024 N  ND2   . ASN   B 1 202 ? -5.026  15.376  39.559  1.00 77.08  ?  202 ASN   B ND2   1 
ATOM   4025 N  N     . ARG   B 1 203 ? -4.425  10.290  38.638  1.00 78.01  ?  203 ARG   B N     1 
ATOM   4026 C  CA    . ARG   B 1 203 ? -5.424  9.214   38.542  1.00 77.61  ?  203 ARG   B CA    1 
ATOM   4027 C  C     . ARG   B 1 203 ? -6.853  9.691   38.832  1.00 72.67  ?  203 ARG   B C     1 
ATOM   4028 O  O     . ARG   B 1 203 ? -7.815  9.091   38.353  1.00 71.28  ?  203 ARG   B O     1 
ATOM   4029 C  CB    . ARG   B 1 203 ? -5.061  8.075   39.506  1.00 75.82  ?  203 ARG   B CB    1 
ATOM   4030 N  N     . ASN   B 1 204 ? -6.982  10.779  39.600  1.00 69.65  ?  204 ASN   B N     1 
ATOM   4031 C  CA    . ASN   B 1 204 ? -8.292  11.369  39.941  1.00 64.98  ?  204 ASN   B CA    1 
ATOM   4032 C  C     . ASN   B 1 204 ? -9.080  11.874  38.741  1.00 59.97  ?  204 ASN   B C     1 
ATOM   4033 O  O     . ASN   B 1 204 ? -10.285 12.082  38.840  1.00 63.66  ?  204 ASN   B O     1 
ATOM   4034 C  CB    . ASN   B 1 204 ? -8.126  12.489  40.977  1.00 66.25  ?  204 ASN   B CB    1 
ATOM   4035 C  CG    . ASN   B 1 204 ? -7.675  11.966  42.336  1.00 64.47  ?  204 ASN   B CG    1 
ATOM   4036 O  OD1   . ASN   B 1 204 ? -8.018  10.844  42.723  1.00 63.03  ?  204 ASN   B OD1   1 
ATOM   4037 N  ND2   . ASN   B 1 204 ? -6.907  12.775  43.066  1.00 60.85  ?  204 ASN   B ND2   1 
ATOM   4038 N  N     . ASN   B 1 205 ? -8.393  12.058  37.615  1.00 58.69  ?  205 ASN   B N     1 
ATOM   4039 C  CA    . ASN   B 1 205 ? -9.016  12.420  36.343  1.00 60.16  ?  205 ASN   B CA    1 
ATOM   4040 C  C     . ASN   B 1 205 ? -9.696  11.275  35.598  1.00 54.43  ?  205 ASN   B C     1 
ATOM   4041 O  O     . ASN   B 1 205 ? -10.557 11.525  34.763  1.00 50.89  ?  205 ASN   B O     1 
ATOM   4042 C  CB    . ASN   B 1 205 ? -7.968  13.053  35.415  1.00 63.81  ?  205 ASN   B CB    1 
ATOM   4043 C  CG    . ASN   B 1 205 ? -7.729  14.527  35.721  1.00 63.09  ?  205 ASN   B CG    1 
ATOM   4044 O  OD1   . ASN   B 1 205 ? -8.650  15.340  35.652  1.00 56.71  ?  205 ASN   B OD1   1 
ATOM   4045 N  ND2   . ASN   B 1 205 ? -6.494  14.870  36.054  1.00 63.73  ?  205 ASN   B ND2   1 
ATOM   4046 N  N     . VAL   B 1 206 ? -9.305  10.040  35.899  1.00 56.78  ?  206 VAL   B N     1 
ATOM   4047 C  CA    . VAL   B 1 206 ? -9.678  8.868   35.095  1.00 60.08  ?  206 VAL   B CA    1 
ATOM   4048 C  C     . VAL   B 1 206 ? -10.576 7.884   35.873  1.00 57.49  ?  206 VAL   B C     1 
ATOM   4049 O  O     . VAL   B 1 206 ? -10.455 7.744   37.100  1.00 53.39  ?  206 VAL   B O     1 
ATOM   4050 C  CB    . VAL   B 1 206 ? -8.405  8.136   34.561  1.00 63.46  ?  206 VAL   B CB    1 
ATOM   4051 C  CG1   . VAL   B 1 206 ? -7.631  7.399   35.652  1.00 61.51  ?  206 VAL   B CG1   1 
ATOM   4052 C  CG2   . VAL   B 1 206 ? -8.753  7.148   33.469  1.00 65.04  ?  206 VAL   B CG2   1 
ATOM   4053 N  N     . ILE   B 1 207 ? -11.483 7.240   35.136  1.00 53.42  ?  207 ILE   B N     1 
ATOM   4054 C  CA    . ILE   B 1 207 ? -12.175 6.031   35.563  1.00 49.68  ?  207 ILE   B CA    1 
ATOM   4055 C  C     . ILE   B 1 207 ? -11.501 4.860   34.846  1.00 48.89  ?  207 ILE   B C     1 
ATOM   4056 O  O     . ILE   B 1 207 ? -11.764 4.608   33.682  1.00 49.68  ?  207 ILE   B O     1 
ATOM   4057 C  CB    . ILE   B 1 207 ? -13.682 6.081   35.225  1.00 48.32  ?  207 ILE   B CB    1 
ATOM   4058 C  CG1   . ILE   B 1 207 ? -14.366 7.198   36.016  1.00 47.03  ?  207 ILE   B CG1   1 
ATOM   4059 C  CG2   . ILE   B 1 207 ? -14.349 4.741   35.528  1.00 47.45  ?  207 ILE   B CG2   1 
ATOM   4060 C  CD1   . ILE   B 1 207 ? -15.749 7.558   35.523  1.00 47.92  ?  207 ILE   B CD1   1 
ATOM   4061 N  N     . GLY   B 1 208 ? -10.608 4.180   35.546  1.00 47.19  ?  208 GLY   B N     1 
ATOM   4062 C  CA    . GLY   B 1 208 ? -9.893  3.014   35.028  1.00 48.72  ?  208 GLY   B CA    1 
ATOM   4063 C  C     . GLY   B 1 208 ? -10.758 1.757   34.999  1.00 49.97  ?  208 GLY   B C     1 
ATOM   4064 O  O     . GLY   B 1 208 ? -11.483 1.468   35.958  1.00 51.60  ?  208 GLY   B O     1 
ATOM   4065 N  N     . LEU   B 1 209 ? -10.668 0.992   33.916  1.00 42.70  ?  209 LEU   B N     1 
ATOM   4066 C  CA    . LEU   B 1 209 ? -11.512 -0.201  33.741  1.00 45.64  ?  209 LEU   B CA    1 
ATOM   4067 C  C     . LEU   B 1 209 ? -11.258 -1.315  34.787  1.00 43.93  ?  209 LEU   B C     1 
ATOM   4068 O  O     . LEU   B 1 209 ? -12.165 -2.100  35.114  1.00 41.57  ?  209 LEU   B O     1 
ATOM   4069 C  CB    . LEU   B 1 209 ? -11.358 -0.779  32.309  1.00 42.97  ?  209 LEU   B CB    1 
ATOM   4070 C  CG    . LEU   B 1 209 ? -11.902 0.065   31.142  1.00 43.63  ?  209 LEU   B CG    1 
ATOM   4071 C  CD1   . LEU   B 1 209 ? -11.772 -0.687  29.825  1.00 43.42  ?  209 LEU   B CD1   1 
ATOM   4072 C  CD2   . LEU   B 1 209 ? -13.355 0.506   31.355  1.00 43.89  ?  209 LEU   B CD2   1 
ATOM   4073 N  N     . LEU   B 1 210 ? -10.035 -1.384  35.295  1.00 44.50  ?  210 LEU   B N     1 
ATOM   4074 C  CA    . LEU   B 1 210 ? -9.665  -2.380  36.312  1.00 50.25  ?  210 LEU   B CA    1 
ATOM   4075 C  C     . LEU   B 1 210 ? -9.394  -1.771  37.703  1.00 52.24  ?  210 LEU   B C     1 
ATOM   4076 O  O     . LEU   B 1 210 ? -8.794  -2.419  38.587  1.00 50.28  ?  210 LEU   B O     1 
ATOM   4077 C  CB    . LEU   B 1 210 ? -8.464  -3.206  35.825  1.00 49.88  ?  210 LEU   B CB    1 
ATOM   4078 C  CG    . LEU   B 1 210 ? -8.720  -4.065  34.579  1.00 50.14  ?  210 LEU   B CG    1 
ATOM   4079 C  CD1   . LEU   B 1 210 ? -7.430  -4.743  34.134  1.00 54.75  ?  210 LEU   B CD1   1 
ATOM   4080 C  CD2   . LEU   B 1 210 ? -9.804  -5.097  34.810  1.00 47.49  ?  210 LEU   B CD2   1 
ATOM   4081 N  N     . GLU   B 1 211 ? -9.862  -0.543  37.911  1.00 53.82  ?  211 GLU   B N     1 
ATOM   4082 C  CA    . GLU   B 1 211 ? -9.759  0.107   39.222  1.00 56.64  ?  211 GLU   B CA    1 
ATOM   4083 C  C     . GLU   B 1 211 ? -10.807 -0.429  40.171  1.00 51.36  ?  211 GLU   B C     1 
ATOM   4084 O  O     . GLU   B 1 211 ? -11.892 -0.811  39.753  1.00 53.80  ?  211 GLU   B O     1 
ATOM   4085 C  CB    . GLU   B 1 211 ? -9.981  1.614   39.102  1.00 60.88  ?  211 GLU   B CB    1 
ATOM   4086 C  CG    . GLU   B 1 211 ? -8.771  2.363   38.597  1.00 67.27  ?  211 GLU   B CG    1 
ATOM   4087 C  CD    . GLU   B 1 211 ? -9.064  3.816   38.312  1.00 70.69  ?  211 GLU   B CD    1 
ATOM   4088 O  OE1   . GLU   B 1 211 ? -10.145 4.334   38.701  1.00 69.56  ?  211 GLU   B OE1   1 
ATOM   4089 O  OE2   . GLU   B 1 211 ? -8.210  4.451   37.664  1.00 78.60  ?  211 GLU   B OE2   1 
ATOM   4090 N  N     . ASP   B 1 212 ? -10.490 -0.404  41.457  1.00 51.01  ?  212 ASP   B N     1 
ATOM   4091 C  CA    . ASP   B 1 212 ? -11.464 -0.699  42.499  1.00 51.12  ?  212 ASP   B CA    1 
ATOM   4092 C  C     . ASP   B 1 212 ? -12.701 0.197   42.275  1.00 51.62  ?  212 ASP   B C     1 
ATOM   4093 O  O     . ASP   B 1 212 ? -12.559 1.431   42.215  1.00 54.12  ?  212 ASP   B O     1 
ATOM   4094 C  CB    . ASP   B 1 212 ? -10.815 -0.471  43.877  1.00 52.60  ?  212 ASP   B CB    1 
ATOM   4095 C  CG    . ASP   B 1 212 ? -11.786 -0.601  45.027  1.00 55.03  ?  212 ASP   B CG    1 
ATOM   4096 O  OD1   . ASP   B 1 212 ? -12.861 -1.232  44.883  1.00 56.54  ?  212 ASP   B OD1   1 
ATOM   4097 O  OD2   . ASP   B 1 212 ? -11.451 -0.041  46.087  1.00 65.95  ?  212 ASP   B OD2   1 
ATOM   4098 N  N     . PRO   B 1 213 ? -13.899 -0.411  42.094  1.00 54.22  ?  213 PRO   B N     1 
ATOM   4099 C  CA    . PRO   B 1 213 ? -15.144 0.365   41.945  1.00 54.01  ?  213 PRO   B CA    1 
ATOM   4100 C  C     . PRO   B 1 213 ? -15.363 1.448   43.004  1.00 57.45  ?  213 PRO   B C     1 
ATOM   4101 O  O     . PRO   B 1 213 ? -15.736 2.565   42.656  1.00 64.23  ?  213 PRO   B O     1 
ATOM   4102 C  CB    . PRO   B 1 213 ? -16.227 -0.700  42.052  1.00 53.58  ?  213 PRO   B CB    1 
ATOM   4103 C  CG    . PRO   B 1 213 ? -15.577 -1.917  41.480  1.00 53.82  ?  213 PRO   B CG    1 
ATOM   4104 C  CD    . PRO   B 1 213 ? -14.146 -1.853  41.912  1.00 52.20  ?  213 PRO   B CD    1 
ATOM   4105 N  N     . LYS   B 1 214 ? -15.104 1.125   44.269  1.00 59.15  ?  214 LYS   B N     1 
ATOM   4106 C  CA    . LYS   B 1 214 ? -15.285 2.060   45.390  1.00 58.68  ?  214 LYS   B CA    1 
ATOM   4107 C  C     . LYS   B 1 214 ? -14.495 3.357   45.178  1.00 58.05  ?  214 LYS   B C     1 
ATOM   4108 O  O     . LYS   B 1 214 ? -15.007 4.442   45.436  1.00 57.49  ?  214 LYS   B O     1 
ATOM   4109 C  CB    . LYS   B 1 214 ? -14.890 1.394   46.722  1.00 57.43  ?  214 LYS   B CB    1 
ATOM   4110 N  N     . SER   B 1 215 ? -13.267 3.231   44.674  1.00 60.06  ?  215 SER   B N     1 
ATOM   4111 C  CA    . SER   B 1 215 ? -12.410 4.383   44.327  1.00 60.84  ?  215 SER   B CA    1 
ATOM   4112 C  C     . SER   B 1 215 ? -12.987 5.241   43.184  1.00 61.43  ?  215 SER   B C     1 
ATOM   4113 O  O     . SER   B 1 215 ? -12.775 6.451   43.148  1.00 64.80  ?  215 SER   B O     1 
ATOM   4114 C  CB    . SER   B 1 215 ? -10.988 3.891   43.982  1.00 63.54  ?  215 SER   B CB    1 
ATOM   4115 O  OG    . SER   B 1 215 ? -10.177 4.908   43.420  1.00 68.72  ?  215 SER   B OG    1 
ATOM   4116 N  N     . VAL   B 1 216 ? -13.725 4.607   42.275  1.00 59.64  ?  216 VAL   B N     1 
ATOM   4117 C  CA    . VAL   B 1 216 ? -14.383 5.276   41.153  1.00 60.46  ?  216 VAL   B CA    1 
ATOM   4118 C  C     . VAL   B 1 216 ? -15.580 6.112   41.618  1.00 60.18  ?  216 VAL   B C     1 
ATOM   4119 O  O     . VAL   B 1 216 ? -15.716 7.263   41.213  1.00 61.97  ?  216 VAL   B O     1 
ATOM   4120 C  CB    . VAL   B 1 216 ? -14.811 4.249   40.060  1.00 64.08  ?  216 VAL   B CB    1 
ATOM   4121 C  CG1   . VAL   B 1 216 ? -15.546 4.913   38.897  1.00 65.02  ?  216 VAL   B CG1   1 
ATOM   4122 C  CG2   . VAL   B 1 216 ? -13.590 3.498   39.538  1.00 61.64  ?  216 VAL   B CG2   1 
ATOM   4123 N  N     . VAL   B 1 217 ? -16.425 5.546   42.485  1.00 60.48  ?  217 VAL   B N     1 
ATOM   4124 C  CA    . VAL   B 1 217 ? -17.559 6.287   43.104  1.00 54.48  ?  217 VAL   B CA    1 
ATOM   4125 C  C     . VAL   B 1 217 ? -17.055 7.563   43.820  1.00 49.16  ?  217 VAL   B C     1 
ATOM   4126 O  O     . VAL   B 1 217 ? -17.663 8.615   43.723  1.00 47.59  ?  217 VAL   B O     1 
ATOM   4127 C  CB    . VAL   B 1 217 ? -18.345 5.385   44.086  1.00 57.30  ?  217 VAL   B CB    1 
ATOM   4128 C  CG1   . VAL   B 1 217 ? -19.456 6.152   44.801  1.00 56.99  ?  217 VAL   B CG1   1 
ATOM   4129 C  CG2   . VAL   B 1 217 ? -18.923 4.156   43.365  1.00 53.95  ?  217 VAL   B CG2   1 
ATOM   4130 N  N     . LYS   B 1 218 ? -15.919 7.456   44.503  1.00 49.10  ?  218 LYS   B N     1 
ATOM   4131 C  CA    . LYS   B 1 218 ? -15.248 8.600   45.139  1.00 50.27  ?  218 LYS   B CA    1 
ATOM   4132 C  C     . LYS   B 1 218 ? -14.750 9.647   44.131  1.00 52.35  ?  218 LYS   B C     1 
ATOM   4133 O  O     . LYS   B 1 218 ? -14.838 10.852  44.387  1.00 50.27  ?  218 LYS   B O     1 
ATOM   4134 C  CB    . LYS   B 1 218 ? -14.074 8.128   46.005  1.00 51.36  ?  218 LYS   B CB    1 
ATOM   4135 N  N     . LYS   B 1 219 ? -14.221 9.188   42.992  1.00 52.00  ?  219 LYS   B N     1 
ATOM   4136 C  CA    . LYS   B 1 219 ? -13.763 10.091  41.924  1.00 49.33  ?  219 LYS   B CA    1 
ATOM   4137 C  C     . LYS   B 1 219 ? -14.920 10.832  41.256  1.00 48.24  ?  219 LYS   B C     1 
ATOM   4138 O  O     . LYS   B 1 219 ? -14.804 12.023  40.925  1.00 44.54  ?  219 LYS   B O     1 
ATOM   4139 C  CB    . LYS   B 1 219 ? -12.957 9.318   40.885  1.00 53.25  ?  219 LYS   B CB    1 
ATOM   4140 C  CG    . LYS   B 1 219 ? -11.551 8.938   41.343  1.00 57.16  ?  219 LYS   B CG    1 
ATOM   4141 C  CD    . LYS   B 1 219 ? -11.038 7.729   40.576  1.00 59.31  ?  219 LYS   B CD    1 
ATOM   4142 C  CE    . LYS   B 1 219 ? -9.530  7.627   40.605  1.00 61.65  ?  219 LYS   B CE    1 
ATOM   4143 N  NZ    . LYS   B 1 219 ? -9.065  6.817   39.446  1.00 65.88  ?  219 LYS   B NZ    1 
ATOM   4144 N  N     . ILE   B 1 220 ? -16.043 10.142  41.094  1.00 47.68  ?  220 ILE   B N     1 
ATOM   4145 C  CA    . ILE   B 1 220 ? -17.243 10.723  40.485  1.00 48.72  ?  220 ILE   B CA    1 
ATOM   4146 C  C     . ILE   B 1 220 ? -17.834 11.824  41.372  1.00 48.97  ?  220 ILE   B C     1 
ATOM   4147 O  O     . ILE   B 1 220 ? -18.210 12.880  40.870  1.00 47.10  ?  220 ILE   B O     1 
ATOM   4148 C  CB    . ILE   B 1 220 ? -18.291 9.624   40.161  1.00 51.16  ?  220 ILE   B CB    1 
ATOM   4149 C  CG1   . ILE   B 1 220 ? -17.679 8.641   39.135  1.00 57.40  ?  220 ILE   B CG1   1 
ATOM   4150 C  CG2   . ILE   B 1 220 ? -19.588 10.231  39.638  1.00 50.50  ?  220 ILE   B CG2   1 
ATOM   4151 C  CD1   . ILE   B 1 220 ? -18.589 7.545   38.637  1.00 57.10  ?  220 ILE   B CD1   1 
ATOM   4152 N  N     . LYS   B 1 221 ? -17.905 11.564  42.682  1.00 49.19  ?  221 LYS   B N     1 
ATOM   4153 C  CA    . LYS   B 1 221 ? -18.387 12.541  43.678  1.00 47.53  ?  221 LYS   B CA    1 
ATOM   4154 C  C     . LYS   B 1 221 ? -17.510 13.796  43.688  1.00 47.61  ?  221 LYS   B C     1 
ATOM   4155 O  O     . LYS   B 1 221 ? -18.011 14.915  43.841  1.00 45.81  ?  221 LYS   B O     1 
ATOM   4156 C  CB    . LYS   B 1 221 ? -18.444 11.915  45.092  1.00 44.95  ?  221 LYS   B CB    1 
ATOM   4157 N  N     . ARG   B 1 222 ? -16.209 13.611  43.466  1.00 47.37  ?  222 ARG   B N     1 
ATOM   4158 C  CA    . ARG   B 1 222 ? -15.239 14.709  43.486  1.00 52.79  ?  222 ARG   B CA    1 
ATOM   4159 C  C     . ARG   B 1 222 ? -15.040 15.373  42.118  1.00 53.31  ?  222 ARG   B C     1 
ATOM   4160 O  O     . ARG   B 1 222 ? -14.219 16.284  41.986  1.00 60.40  ?  222 ARG   B O     1 
ATOM   4161 C  CB    . ARG   B 1 222 ? -13.888 14.204  44.041  1.00 51.62  ?  222 ARG   B CB    1 
ATOM   4162 N  N     . ALA   B 1 223 ? -15.801 14.939  41.109  1.00 50.42  ?  223 ALA   B N     1 
ATOM   4163 C  CA    . ALA   B 1 223 ? -15.689 15.480  39.749  1.00 49.30  ?  223 ALA   B CA    1 
ATOM   4164 C  C     . ALA   B 1 223 ? -16.151 16.922  39.733  1.00 48.67  ?  223 ALA   B C     1 
ATOM   4165 O  O     . ALA   B 1 223 ? -17.125 17.252  40.395  1.00 48.33  ?  223 ALA   B O     1 
ATOM   4166 C  CB    . ALA   B 1 223 ? -16.532 14.659  38.778  1.00 49.46  ?  223 ALA   B CB    1 
ATOM   4167 N  N     . VAL   B 1 224 ? -15.448 17.765  38.980  1.00 51.59  ?  224 VAL   B N     1 
ATOM   4168 C  CA    . VAL   B 1 224 ? -15.773 19.203  38.882  1.00 52.23  ?  224 VAL   B CA    1 
ATOM   4169 C  C     . VAL   B 1 224 ? -17.062 19.398  38.115  1.00 50.89  ?  224 VAL   B C     1 
ATOM   4170 O  O     . VAL   B 1 224 ? -17.348 18.627  37.198  1.00 56.39  ?  224 VAL   B O     1 
ATOM   4171 C  CB    . VAL   B 1 224 ? -14.641 20.055  38.247  1.00 51.78  ?  224 VAL   B CB    1 
ATOM   4172 C  CG1   . VAL   B 1 224 ? -13.397 19.992  39.113  1.00 51.19  ?  224 VAL   B CG1   1 
ATOM   4173 C  CG2   . VAL   B 1 224 ? -14.338 19.646  36.806  1.00 53.45  ?  224 VAL   B CG2   1 
ATOM   4174 N  N     . THR   B 1 225 ? -17.830 20.406  38.522  1.00 49.72  ?  225 THR   B N     1 
ATOM   4175 C  CA    . THR   B 1 225 ? -19.141 20.739  37.947  1.00 53.31  ?  225 THR   B CA    1 
ATOM   4176 C  C     . THR   B 1 225 ? -19.093 22.254  37.628  1.00 56.24  ?  225 THR   B C     1 
ATOM   4177 O  O     . THR   B 1 225 ? -18.172 22.692  36.925  1.00 57.05  ?  225 THR   B O     1 
ATOM   4178 C  CB    . THR   B 1 225 ? -20.312 20.347  38.891  1.00 50.97  ?  225 THR   B CB    1 
ATOM   4179 O  OG1   . THR   B 1 225 ? -20.112 20.898  40.205  1.00 47.08  ?  225 THR   B OG1   1 
ATOM   4180 C  CG2   . THR   B 1 225 ? -20.440 18.836  39.006  1.00 53.71  ?  225 THR   B CG2   1 
ATOM   4181 N  N     . ASP   B 1 226 ? -20.018 23.049  38.171  1.00 58.21  ?  226 ASP   B N     1 
ATOM   4182 C  CA    . ASP   B 1 226 ? -20.049 24.499  37.931  1.00 56.78  ?  226 ASP   B CA    1 
ATOM   4183 C  C     . ASP   B 1 226 ? -20.647 25.268  39.127  1.00 53.22  ?  226 ASP   B C     1 
ATOM   4184 O  O     . ASP   B 1 226 ? -21.176 24.684  40.073  1.00 54.09  ?  226 ASP   B O     1 
ATOM   4185 C  CB    . ASP   B 1 226 ? -20.793 24.803  36.619  1.00 56.23  ?  226 ASP   B CB    1 
ATOM   4186 C  CG    . ASP   B 1 226 ? -22.081 24.040  36.496  1.00 59.49  ?  226 ASP   B CG    1 
ATOM   4187 O  OD1   . ASP   B 1 226 ? -22.981 24.265  37.338  1.00 57.07  ?  226 ASP   B OD1   1 
ATOM   4188 O  OD2   . ASP   B 1 226 ? -22.183 23.208  35.556  1.00 61.85  ?  226 ASP   B OD2   1 
ATOM   4189 N  N     . SER   B 1 227 ? -20.554 26.590  39.051  1.00 50.55  ?  227 SER   B N     1 
ATOM   4190 C  CA    . SER   B 1 227 ? -21.074 27.494  40.059  1.00 50.89  ?  227 SER   B CA    1 
ATOM   4191 C  C     . SER   B 1 227 ? -22.546 27.874  39.832  1.00 52.42  ?  227 SER   B C     1 
ATOM   4192 O  O     . SER   B 1 227 ? -23.049 28.790  40.506  1.00 47.05  ?  227 SER   B O     1 
ATOM   4193 C  CB    . SER   B 1 227 ? -20.218 28.770  40.065  1.00 50.34  ?  227 SER   B CB    1 
ATOM   4194 O  OG    . SER   B 1 227 ? -20.191 29.380  38.777  1.00 52.31  ?  227 SER   B OG    1 
ATOM   4195 N  N     . ASP   B 1 228 ? -23.229 27.201  38.891  1.00 51.98  ?  228 ASP   B N     1 
ATOM   4196 C  CA    . ASP   B 1 228 ? -24.628 27.533  38.544  1.00 55.08  ?  228 ASP   B CA    1 
ATOM   4197 C  C     . ASP   B 1 228 ? -25.524 27.605  39.786  1.00 56.71  ?  228 ASP   B C     1 
ATOM   4198 O  O     . ASP   B 1 228 ? -25.477 26.708  40.637  1.00 53.36  ?  228 ASP   B O     1 
ATOM   4199 C  CB    . ASP   B 1 228 ? -25.218 26.525  37.541  1.00 54.59  ?  228 ASP   B CB    1 
ATOM   4200 C  CG    . ASP   B 1 228 ? -24.642 26.681  36.134  1.00 56.53  ?  228 ASP   B CG    1 
ATOM   4201 O  OD1   . ASP   B 1 228 ? -23.637 27.410  35.953  1.00 57.36  ?  228 ASP   B OD1   1 
ATOM   4202 O  OD2   . ASP   B 1 228 ? -25.192 26.067  35.203  1.00 56.39  ?  228 ASP   B OD2   1 
ATOM   4203 N  N     . GLU   B 1 229 ? -26.311 28.682  39.887  1.00 55.64  ?  229 GLU   B N     1 
ATOM   4204 C  CA    . GLU   B 1 229 ? -27.238 28.888  40.999  1.00 56.71  ?  229 GLU   B CA    1 
ATOM   4205 C  C     . GLU   B 1 229 ? -28.634 29.268  40.471  1.00 58.28  ?  229 GLU   B C     1 
ATOM   4206 O  O     . GLU   B 1 229 ? -28.832 30.384  40.008  1.00 60.75  ?  229 GLU   B O     1 
ATOM   4207 C  CB    . GLU   B 1 229 ? -26.713 29.967  41.961  1.00 56.61  ?  229 GLU   B CB    1 
ATOM   4208 C  CG    . GLU   B 1 229 ? -27.455 30.022  43.290  1.00 54.69  ?  229 GLU   B CG    1 
ATOM   4209 C  CD    . GLU   B 1 229 ? -27.399 28.693  44.035  1.00 54.59  ?  229 GLU   B CD    1 
ATOM   4210 O  OE1   . GLU   B 1 229 ? -28.472 28.081  44.273  1.00 52.45  ?  229 GLU   B OE1   1 
ATOM   4211 O  OE2   . GLU   B 1 229 ? -26.271 28.251  44.346  1.00 49.44  ?  229 GLU   B OE2   1 
ATOM   4212 N  N     . PRO   B 1 230 ? -29.613 28.347  40.543  1.00 62.27  ?  230 PRO   B N     1 
ATOM   4213 C  CA    . PRO   B 1 230 ? -29.494 26.995  41.104  1.00 60.08  ?  230 PRO   B CA    1 
ATOM   4214 C  C     . PRO   B 1 230 ? -28.652 26.019  40.265  1.00 58.05  ?  230 PRO   B C     1 
ATOM   4215 O  O     . PRO   B 1 230 ? -28.483 26.212  39.059  1.00 55.75  ?  230 PRO   B O     1 
ATOM   4216 C  CB    . PRO   B 1 230 ? -30.949 26.510  41.170  1.00 64.62  ?  230 PRO   B CB    1 
ATOM   4217 C  CG    . PRO   B 1 230 ? -31.649 27.263  40.084  1.00 66.48  ?  230 PRO   B CG    1 
ATOM   4218 C  CD    . PRO   B 1 230 ? -30.984 28.620  40.061  1.00 64.00  ?  230 PRO   B CD    1 
ATOM   4219 N  N     . PRO   B 1 231 ? -28.126 24.967  40.907  1.00 55.88  ?  231 PRO   B N     1 
ATOM   4220 C  CA    . PRO   B 1 231 ? -27.521 23.884  40.140  1.00 57.61  ?  231 PRO   B CA    1 
ATOM   4221 C  C     . PRO   B 1 231 ? -28.593 23.218  39.264  1.00 60.21  ?  231 PRO   B C     1 
ATOM   4222 O  O     . PRO   B 1 231 ? -29.676 22.909  39.769  1.00 55.42  ?  231 PRO   B O     1 
ATOM   4223 C  CB    . PRO   B 1 231 ? -26.990 22.931  41.221  1.00 55.81  ?  231 PRO   B CB    1 
ATOM   4224 C  CG    . PRO   B 1 231 ? -26.953 23.731  42.483  1.00 56.60  ?  231 PRO   B CG    1 
ATOM   4225 C  CD    . PRO   B 1 231 ? -28.048 24.733  42.359  1.00 55.44  ?  231 PRO   B CD    1 
ATOM   4226 N  N     . VAL   B 1 232 ? -28.298 23.066  37.968  1.00 62.16  ?  232 VAL   B N     1 
ATOM   4227 C  CA    . VAL   B 1 232 ? -29.215 22.460  36.990  1.00 60.86  ?  232 VAL   B CA    1 
ATOM   4228 C  C     . VAL   B 1 232 ? -28.425 21.491  36.118  1.00 60.90  ?  232 VAL   B C     1 
ATOM   4229 O  O     . VAL   B 1 232 ? -27.300 21.811  35.702  1.00 55.03  ?  232 VAL   B O     1 
ATOM   4230 C  CB    . VAL   B 1 232 ? -29.882 23.521  36.089  1.00 61.45  ?  232 VAL   B CB    1 
ATOM   4231 N  N     . VAL   B 1 233 ? -29.022 20.318  35.857  1.00 58.80  ?  233 VAL   B N     1 
ATOM   4232 C  CA    . VAL   B 1 233 ? -28.420 19.269  35.012  1.00 61.80  ?  233 VAL   B CA    1 
ATOM   4233 C  C     . VAL   B 1 233 ? -28.844 19.497  33.542  1.00 58.12  ?  233 VAL   B C     1 
ATOM   4234 O  O     . VAL   B 1 233 ? -29.964 19.167  33.149  1.00 60.17  ?  233 VAL   B O     1 
ATOM   4235 C  CB    . VAL   B 1 233 ? -28.802 17.837  35.495  1.00 57.97  ?  233 VAL   B CB    1 
ATOM   4236 C  CG1   . VAL   B 1 233 ? -28.016 16.775  34.732  1.00 57.84  ?  233 VAL   B CG1   1 
ATOM   4237 C  CG2   . VAL   B 1 233 ? -28.574 17.687  37.000  1.00 56.58  ?  233 VAL   B CG2   1 
ATOM   4238 N  N     . ARG   B 1 234 ? -27.931 20.067  32.760  1.00 57.71  ?  234 ARG   B N     1 
ATOM   4239 C  CA    . ARG   B 1 234 ? -28.156 20.433  31.352  1.00 57.70  ?  234 ARG   B CA    1 
ATOM   4240 C  C     . ARG   B 1 234 ? -26.853 20.262  30.554  1.00 59.36  ?  234 ARG   B C     1 
ATOM   4241 O  O     . ARG   B 1 234 ? -25.750 20.471  31.094  1.00 53.02  ?  234 ARG   B O     1 
ATOM   4242 C  CB    . ARG   B 1 234 ? -28.663 21.884  31.255  1.00 52.75  ?  234 ARG   B CB    1 
ATOM   4243 N  N     . TYR   B 1 235 ? -26.975 19.899  29.274  1.00 62.69  ?  235 TYR   B N     1 
ATOM   4244 C  CA    . TYR   B 1 235 ? -25.810 19.764  28.394  1.00 67.02  ?  235 TYR   B CA    1 
ATOM   4245 C  C     . TYR   B 1 235 ? -25.408 21.134  27.855  1.00 71.12  ?  235 TYR   B C     1 
ATOM   4246 O  O     . TYR   B 1 235 ? -26.121 21.700  27.031  1.00 72.62  ?  235 TYR   B O     1 
ATOM   4247 C  CB    . TYR   B 1 235 ? -26.123 18.812  27.229  1.00 69.64  ?  235 TYR   B CB    1 
ATOM   4248 C  CG    . TYR   B 1 235 ? -24.929 18.015  26.760  1.00 70.39  ?  235 TYR   B CG    1 
ATOM   4249 C  CD1   . TYR   B 1 235 ? -24.485 16.910  27.498  1.00 67.88  ?  235 TYR   B CD1   1 
ATOM   4250 C  CD2   . TYR   B 1 235 ? -24.238 18.351  25.579  1.00 66.49  ?  235 TYR   B CD2   1 
ATOM   4251 C  CE1   . TYR   B 1 235 ? -23.391 16.164  27.082  1.00 68.10  ?  235 TYR   B CE1   1 
ATOM   4252 C  CE2   . TYR   B 1 235 ? -23.136 17.611  25.162  1.00 64.85  ?  235 TYR   B CE2   1 
ATOM   4253 C  CZ    . TYR   B 1 235 ? -22.718 16.520  25.916  1.00 66.00  ?  235 TYR   B CZ    1 
ATOM   4254 O  OH    . TYR   B 1 235 ? -21.633 15.780  25.527  1.00 70.11  ?  235 TYR   B OH    1 
ATOM   4255 N  N     . ASP   B 1 236 ? -24.286 21.673  28.331  1.00 78.30  ?  236 ASP   B N     1 
ATOM   4256 C  CA    . ASP   B 1 236 ? -23.794 22.959  27.842  1.00 82.29  ?  236 ASP   B CA    1 
ATOM   4257 C  C     . ASP   B 1 236 ? -22.268 22.967  27.790  1.00 85.71  ?  236 ASP   B C     1 
ATOM   4258 O  O     . ASP   B 1 236 ? -21.611 23.720  28.511  1.00 105.48 ?  236 ASP   B O     1 
ATOM   4259 C  CB    . ASP   B 1 236 ? -24.356 24.100  28.707  1.00 87.06  ?  236 ASP   B CB    1 
ATOM   4260 C  CG    . ASP   B 1 236 ? -24.174 25.461  28.076  1.00 85.17  ?  236 ASP   B CG    1 
ATOM   4261 O  OD1   . ASP   B 1 236 ? -23.503 25.560  27.027  1.00 86.73  ?  236 ASP   B OD1   1 
ATOM   4262 O  OD2   . ASP   B 1 236 ? -24.695 26.443  28.641  1.00 88.37  ?  236 ASP   B OD2   1 
ATOM   4263 N  N     . VAL   B 1 237 ? -21.720 22.203  26.854  1.00 76.35  ?  237 VAL   B N     1 
ATOM   4264 C  CA    . VAL   B 1 237 ? -20.273 21.873  26.789  1.00 79.04  ?  237 VAL   B CA    1 
ATOM   4265 C  C     . VAL   B 1 237 ? -19.313 23.045  27.043  1.00 80.55  ?  237 VAL   B C     1 
ATOM   4266 O  O     . VAL   B 1 237 ? -18.280 22.871  27.713  1.00 76.79  ?  237 VAL   B O     1 
ATOM   4267 C  CB    . VAL   B 1 237 ? -19.900 21.210  25.435  1.00 78.55  ?  237 VAL   B CB    1 
ATOM   4268 C  CG1   . VAL   B 1 237 ? -18.437 20.774  25.408  1.00 75.74  ?  237 VAL   B CG1   1 
ATOM   4269 C  CG2   . VAL   B 1 237 ? -20.774 19.984  25.169  1.00 77.85  ?  237 VAL   B CG2   1 
ATOM   4270 N  N     . GLN   B 1 238 ? -19.653 24.217  26.507  1.00 83.70  ?  238 GLN   B N     1 
ATOM   4271 C  CA    . GLN   B 1 238 ? -18.816 25.409  26.651  1.00 86.92  ?  238 GLN   B CA    1 
ATOM   4272 C  C     . GLN   B 1 238 ? -18.917 25.974  28.069  1.00 80.21  ?  238 GLN   B C     1 
ATOM   4273 O  O     . GLN   B 1 238 ? -17.941 26.495  28.603  1.00 84.08  ?  238 GLN   B O     1 
ATOM   4274 C  CB    . GLN   B 1 238 ? -19.213 26.472  25.614  1.00 84.03  ?  238 GLN   B CB    1 
ATOM   4275 N  N     . ASN   B 1 239 ? -20.097 25.840  28.667  1.00 70.47  ?  239 ASN   B N     1 
ATOM   4276 C  CA    . ASN   B 1 239 ? -20.386 26.380  29.995  1.00 69.92  ?  239 ASN   B CA    1 
ATOM   4277 C  C     . ASN   B 1 239 ? -20.602 25.363  31.115  1.00 65.11  ?  239 ASN   B C     1 
ATOM   4278 O  O     . ASN   B 1 239 ? -20.655 25.756  32.274  1.00 68.43  ?  239 ASN   B O     1 
ATOM   4279 C  CB    . ASN   B 1 239 ? -21.583 27.317  29.880  1.00 70.93  ?  239 ASN   B CB    1 
ATOM   4280 C  CG    . ASN   B 1 239 ? -21.372 28.360  28.807  1.00 69.84  ?  239 ASN   B CG    1 
ATOM   4281 O  OD1   . ASN   B 1 239 ? -20.607 29.291  29.005  1.00 69.32  ?  239 ASN   B OD1   1 
ATOM   4282 N  ND2   . ASN   B 1 239 ? -21.988 28.173  27.649  1.00 72.57  ?  239 ASN   B ND2   1 
ATOM   4283 N  N     . LYS   B 1 240 ? -20.703 24.073  30.775  1.00 63.30  ?  240 LYS   B N     1 
ATOM   4284 C  CA    . LYS   B 1 240 ? -21.031 23.000  31.724  1.00 58.14  ?  240 LYS   B CA    1 
ATOM   4285 C  C     . LYS   B 1 240 ? -20.292 21.690  31.388  1.00 60.06  ?  240 LYS   B C     1 
ATOM   4286 O  O     . LYS   B 1 240 ? -20.895 20.605  31.377  1.00 54.10  ?  240 LYS   B O     1 
ATOM   4287 C  CB    . LYS   B 1 240 ? -22.542 22.754  31.756  1.00 57.81  ?  240 LYS   B CB    1 
ATOM   4288 C  CG    . LYS   B 1 240 ? -23.378 23.926  32.279  1.00 55.99  ?  240 LYS   B CG    1 
ATOM   4289 C  CD    . LYS   B 1 240 ? -24.858 23.568  32.428  1.00 54.76  ?  240 LYS   B CD    1 
ATOM   4290 C  CE    . LYS   B 1 240 ? -25.137 22.544  33.531  1.00 58.33  ?  240 LYS   B CE    1 
ATOM   4291 N  NZ    . LYS   B 1 240 ? -24.983 23.075  34.926  1.00 53.69  ?  240 LYS   B NZ    1 
ATOM   4292 N  N     . ALA   B 1 241 ? -18.982 21.810  31.152  1.00 58.38  ?  241 ALA   B N     1 
ATOM   4293 C  CA    . ALA   B 1 241 ? -18.144 20.697  30.666  1.00 60.80  ?  241 ALA   B CA    1 
ATOM   4294 C  C     . ALA   B 1 241 ? -18.142 19.494  31.622  1.00 58.15  ?  241 ALA   B C     1 
ATOM   4295 O  O     . ALA   B 1 241 ? -18.246 18.347  31.187  1.00 59.19  ?  241 ALA   B O     1 
ATOM   4296 C  CB    . ALA   B 1 241 ? -16.712 21.180  30.401  1.00 59.50  ?  241 ALA   B CB    1 
ATOM   4297 N  N     . GLY   B 1 242 ? -18.044 19.769  32.921  1.00 53.47  ?  242 GLY   B N     1 
ATOM   4298 C  CA    . GLY   B 1 242 ? -18.049 18.725  33.946  1.00 50.18  ?  242 GLY   B CA    1 
ATOM   4299 C  C     . GLY   B 1 242 ? -19.342 17.921  33.991  1.00 48.38  ?  242 GLY   B C     1 
ATOM   4300 O  O     . GLY   B 1 242 ? -19.310 16.690  33.946  1.00 45.07  ?  242 GLY   B O     1 
ATOM   4301 N  N     . VAL   B 1 243 ? -20.466 18.635  34.077  1.00 45.18  ?  243 VAL   B N     1 
ATOM   4302 C  CA    . VAL   B 1 243 ? -21.801 18.055  34.143  1.00 45.87  ?  243 VAL   B CA    1 
ATOM   4303 C  C     . VAL   B 1 243 ? -22.075 17.268  32.875  1.00 49.99  ?  243 VAL   B C     1 
ATOM   4304 O  O     . VAL   B 1 243 ? -22.576 16.133  32.973  1.00 45.40  ?  243 VAL   B O     1 
ATOM   4305 C  CB    . VAL   B 1 243 ? -22.898 19.144  34.365  1.00 46.35  ?  243 VAL   B CB    1 
ATOM   4306 C  CG1   . VAL   B 1 243 ? -24.299 18.676  33.949  1.00 46.34  ?  243 VAL   B CG1   1 
ATOM   4307 C  CG2   . VAL   B 1 243 ? -22.926 19.593  35.832  1.00 50.13  ?  243 VAL   B CG2   1 
ATOM   4308 N  N     . SER   B 1 244 ? -21.757 17.885  31.716  1.00 47.90  ?  244 SER   B N     1 
ATOM   4309 C  CA    . SER   B 1 244 ? -21.971 17.299  30.397  1.00 48.77  ?  244 SER   B CA    1 
ATOM   4310 C  C     . SER   B 1 244 ? -21.231 15.961  30.249  1.00 50.24  ?  244 SER   B C     1 
ATOM   4311 O  O     . SER   B 1 244 ? -21.825 14.955  29.879  1.00 49.27  ?  244 SER   B O     1 
ATOM   4312 C  CB    . SER   B 1 244 ? -21.509 18.272  29.305  1.00 52.02  ?  244 SER   B CB    1 
ATOM   4313 O  OG    . SER   B 1 244 ? -22.191 19.515  29.401  1.00 56.24  ?  244 SER   B OG    1 
ATOM   4314 N  N     . ASN   B 1 245 ? -19.932 15.968  30.546  1.00 49.42  ?  245 ASN   B N     1 
ATOM   4315 C  CA    . ASN   B 1 245 ? -19.115 14.759  30.479  1.00 49.86  ?  245 ASN   B CA    1 
ATOM   4316 C  C     . ASN   B 1 245 ? -19.704 13.628  31.314  1.00 50.93  ?  245 ASN   B C     1 
ATOM   4317 O  O     . ASN   B 1 245 ? -19.669 12.489  30.878  1.00 54.11  ?  245 ASN   B O     1 
ATOM   4318 C  CB    . ASN   B 1 245 ? -17.667 15.031  30.902  1.00 48.47  ?  245 ASN   B CB    1 
ATOM   4319 C  CG    . ASN   B 1 245 ? -16.731 13.864  30.570  1.00 53.87  ?  245 ASN   B CG    1 
ATOM   4320 O  OD1   . ASN   B 1 245 ? -16.584 13.470  29.390  1.00 52.28  ?  245 ASN   B OD1   1 
ATOM   4321 N  ND2   . ASN   B 1 245 ? -16.065 13.333  31.584  1.00 49.26  ?  245 ASN   B ND2   1 
ATOM   4322 N  N     . LEU   B 1 246 ? -20.243 13.966  32.495  1.00 55.89  ?  246 LEU   B N     1 
ATOM   4323 C  CA    . LEU   B 1 246 ? -20.962 13.032  33.375  1.00 58.90  ?  246 LEU   B CA    1 
ATOM   4324 C  C     . LEU   B 1 246 ? -22.262 12.511  32.750  1.00 62.65  ?  246 LEU   B C     1 
ATOM   4325 O  O     . LEU   B 1 246 ? -22.554 11.309  32.838  1.00 62.72  ?  246 LEU   B O     1 
ATOM   4326 C  CB    . LEU   B 1 246 ? -21.302 13.684  34.730  1.00 61.77  ?  246 LEU   B CB    1 
ATOM   4327 C  CG    . LEU   B 1 246 ? -20.128 14.004  35.661  1.00 61.77  ?  246 LEU   B CG    1 
ATOM   4328 C  CD1   . LEU   B 1 246 ? -20.498 15.087  36.666  1.00 59.09  ?  246 LEU   B CD1   1 
ATOM   4329 C  CD2   . LEU   B 1 246 ? -19.641 12.737  36.363  1.00 61.62  ?  246 LEU   B CD2   1 
ATOM   4330 N  N     . LEU   B 1 247 ? -23.050 13.425  32.178  1.00 59.42  ?  247 LEU   B N     1 
ATOM   4331 C  CA    . LEU   B 1 247 ? -24.267 13.077  31.428  1.00 64.33  ?  247 LEU   B CA    1 
ATOM   4332 C  C     . LEU   B 1 247 ? -23.983 12.144  30.238  1.00 70.34  ?  247 LEU   B C     1 
ATOM   4333 O  O     . LEU   B 1 247 ? -24.737 11.190  30.003  1.00 71.37  ?  247 LEU   B O     1 
ATOM   4334 C  CB    . LEU   B 1 247 ? -24.974 14.344  30.920  1.00 63.25  ?  247 LEU   B CB    1 
ATOM   4335 C  CG    . LEU   B 1 247 ? -25.806 15.109  31.939  1.00 58.07  ?  247 LEU   B CG    1 
ATOM   4336 C  CD1   . LEU   B 1 247 ? -26.214 16.457  31.375  1.00 59.70  ?  247 LEU   B CD1   1 
ATOM   4337 C  CD2   . LEU   B 1 247 ? -27.031 14.302  32.338  1.00 59.35  ?  247 LEU   B CD2   1 
ATOM   4338 N  N     . ASP   B 1 248 ? -22.899 12.425  29.508  1.00 66.51  ?  248 ASP   B N     1 
ATOM   4339 C  CA    . ASP   B 1 248 ? -22.455 11.587  28.385  1.00 66.29  ?  248 ASP   B CA    1 
ATOM   4340 C  C     . ASP   B 1 248 ? -22.013 10.190  28.872  1.00 67.30  ?  248 ASP   B C     1 
ATOM   4341 O  O     . ASP   B 1 248 ? -22.359 9.184   28.249  1.00 69.27  ?  248 ASP   B O     1 
ATOM   4342 C  CB    . ASP   B 1 248 ? -21.320 12.266  27.606  1.00 65.62  ?  248 ASP   B CB    1 
ATOM   4343 N  N     . ILE   B 1 249 ? -21.264 10.138  29.984  1.00 61.58  ?  249 ILE   B N     1 
ATOM   4344 C  CA    . ILE   B 1 249 ? -20.890 8.866   30.632  1.00 59.22  ?  249 ILE   B CA    1 
ATOM   4345 C  C     . ILE   B 1 249 ? -22.140 8.075   31.027  1.00 58.09  ?  249 ILE   B C     1 
ATOM   4346 O  O     . ILE   B 1 249 ? -22.213 6.876   30.781  1.00 55.40  ?  249 ILE   B O     1 
ATOM   4347 C  CB    . ILE   B 1 249 ? -19.946 9.075   31.847  1.00 52.33  ?  249 ILE   B CB    1 
ATOM   4348 C  CG1   . ILE   B 1 249 ? -18.532 9.427   31.353  1.00 49.75  ?  249 ILE   B CG1   1 
ATOM   4349 C  CG2   . ILE   B 1 249 ? -19.893 7.816   32.723  1.00 52.52  ?  249 ILE   B CG2   1 
ATOM   4350 C  CD1   . ILE   B 1 249 ? -17.606 9.949   32.430  1.00 49.40  ?  249 ILE   B CD1   1 
ATOM   4351 N  N     . LEU   B 1 250 ? -23.114 8.768   31.616  1.00 61.43  ?  250 LEU   B N     1 
ATOM   4352 C  CA    . LEU   B 1 250 ? -24.400 8.189   32.004  1.00 64.39  ?  250 LEU   B CA    1 
ATOM   4353 C  C     . LEU   B 1 250 ? -25.125 7.585   30.809  1.00 67.80  ?  250 LEU   B C     1 
ATOM   4354 O  O     . LEU   B 1 250 ? -25.593 6.447   30.887  1.00 70.54  ?  250 LEU   B O     1 
ATOM   4355 C  CB    . LEU   B 1 250 ? -25.286 9.256   32.662  1.00 59.96  ?  250 LEU   B CB    1 
ATOM   4356 N  N     . SER   B 1 251 ? -25.193 8.358   29.720  1.00 71.43  ?  251 SER   B N     1 
ATOM   4357 C  CA    . SER   B 1 251 ? -25.834 7.959   28.453  1.00 71.70  ?  251 SER   B CA    1 
ATOM   4358 C  C     . SER   B 1 251 ? -25.284 6.644   27.889  1.00 73.11  ?  251 SER   B C     1 
ATOM   4359 O  O     . SER   B 1 251 ? -26.025 5.687   27.669  1.00 69.89  ?  251 SER   B O     1 
ATOM   4360 C  CB    . SER   B 1 251 ? -25.659 9.071   27.413  1.00 71.52  ?  251 SER   B CB    1 
ATOM   4361 O  OG    . SER   B 1 251 ? -26.096 8.684   26.121  1.00 73.51  ?  251 SER   B OG    1 
ATOM   4362 N  N     . ALA   B 1 252 ? -23.973 6.613   27.680  1.00 75.05  ?  252 ALA   B N     1 
ATOM   4363 C  CA    . ALA   B 1 252 ? -23.301 5.509   26.996  1.00 77.54  ?  252 ALA   B CA    1 
ATOM   4364 C  C     . ALA   B 1 252 ? -23.218 4.206   27.812  1.00 75.21  ?  252 ALA   B C     1 
ATOM   4365 O  O     . ALA   B 1 252 ? -23.102 3.126   27.234  1.00 72.54  ?  252 ALA   B O     1 
ATOM   4366 C  CB    . ALA   B 1 252 ? -21.910 5.961   26.561  1.00 81.30  ?  252 ALA   B CB    1 
ATOM   4367 N  N     . VAL   B 1 253 ? -23.272 4.317   29.143  1.00 77.86  ?  253 VAL   B N     1 
ATOM   4368 C  CA    . VAL   B 1 253 ? -23.305 3.148   30.053  1.00 73.67  ?  253 VAL   B CA    1 
ATOM   4369 C  C     . VAL   B 1 253 ? -24.709 2.528   30.098  1.00 71.95  ?  253 VAL   B C     1 
ATOM   4370 O  O     . VAL   B 1 253 ? -24.843 1.315   30.198  1.00 68.79  ?  253 VAL   B O     1 
ATOM   4371 C  CB    . VAL   B 1 253 ? -22.843 3.509   31.503  1.00 71.31  ?  253 VAL   B CB    1 
ATOM   4372 C  CG1   . VAL   B 1 253 ? -22.910 2.309   32.443  1.00 70.21  ?  253 VAL   B CG1   1 
ATOM   4373 C  CG2   . VAL   B 1 253 ? -21.414 4.024   31.526  1.00 73.93  ?  253 VAL   B CG2   1 
ATOM   4374 N  N     . THR   B 1 254 ? -25.739 3.374   30.044  1.00 73.43  ?  254 THR   B N     1 
ATOM   4375 C  CA    . THR   B 1 254 ? -27.140 2.948   30.119  1.00 74.66  ?  254 THR   B CA    1 
ATOM   4376 C  C     . THR   B 1 254 ? -27.800 2.746   28.749  1.00 78.75  ?  254 THR   B C     1 
ATOM   4377 O  O     . THR   B 1 254 ? -28.720 1.937   28.622  1.00 84.21  ?  254 THR   B O     1 
ATOM   4378 C  CB    . THR   B 1 254 ? -27.984 3.962   30.924  1.00 73.99  ?  254 THR   B CB    1 
ATOM   4379 O  OG1   . THR   B 1 254 ? -27.785 5.281   30.401  1.00 74.14  ?  254 THR   B OG1   1 
ATOM   4380 C  CG2   . THR   B 1 254 ? -27.612 3.943   32.402  1.00 73.67  ?  254 THR   B CG2   1 
ATOM   4381 N  N     . GLY   B 1 255 ? -27.326 3.473   27.738  1.00 81.48  ?  255 GLY   B N     1 
ATOM   4382 C  CA    . GLY   B 1 255 ? -27.967 3.534   26.416  1.00 84.36  ?  255 GLY   B CA    1 
ATOM   4383 C  C     . GLY   B 1 255 ? -29.026 4.628   26.304  1.00 83.91  ?  255 GLY   B C     1 
ATOM   4384 O  O     . GLY   B 1 255 ? -29.676 4.758   25.266  1.00 88.24  ?  255 GLY   B O     1 
ATOM   4385 N  N     . GLN   B 1 256 ? -29.184 5.425   27.362  1.00 81.72  ?  256 GLN   B N     1 
ATOM   4386 C  CA    . GLN   B 1 256 ? -30.204 6.475   27.424  1.00 80.55  ?  256 GLN   B CA    1 
ATOM   4387 C  C     . GLN   B 1 256 ? -29.737 7.723   26.692  1.00 80.69  ?  256 GLN   B C     1 
ATOM   4388 O  O     . GLN   B 1 256 ? -28.529 7.946   26.535  1.00 76.87  ?  256 GLN   B O     1 
ATOM   4389 C  CB    . GLN   B 1 256 ? -30.507 6.845   28.882  1.00 83.14  ?  256 GLN   B CB    1 
ATOM   4390 C  CG    . GLN   B 1 256 ? -31.010 5.692   29.741  1.00 80.46  ?  256 GLN   B CG    1 
ATOM   4391 C  CD    . GLN   B 1 256 ? -31.439 6.138   31.123  1.00 74.30  ?  256 GLN   B CD    1 
ATOM   4392 O  OE1   . GLN   B 1 256 ? -30.760 5.885   32.116  1.00 67.58  ?  256 GLN   B OE1   1 
ATOM   4393 N  NE2   . GLN   B 1 256 ? -32.573 6.811   31.188  1.00 78.39  ?  256 GLN   B NE2   1 
ATOM   4394 N  N     . SER   B 1 257 ? -30.699 8.546   26.278  1.00 78.84  ?  257 SER   B N     1 
ATOM   4395 C  CA    . SER   B 1 257 ? -30.413 9.794   25.558  1.00 80.40  ?  257 SER   B CA    1 
ATOM   4396 C  C     . SER   B 1 257 ? -30.157 10.962  26.530  1.00 76.38  ?  257 SER   B C     1 
ATOM   4397 O  O     . SER   B 1 257 ? -30.671 10.958  27.652  1.00 76.10  ?  257 SER   B O     1 
ATOM   4398 C  CB    . SER   B 1 257 ? -31.576 10.118  24.615  1.00 77.70  ?  257 SER   B CB    1 
ATOM   4399 O  OG    . SER   B 1 257 ? -32.704 10.576  25.332  1.00 75.04  ?  257 SER   B OG    1 
ATOM   4400 N  N     . ILE   B 1 258 ? -29.368 11.948  26.092  1.00 77.30  ?  258 ILE   B N     1 
ATOM   4401 C  CA    . ILE   B 1 258 ? -29.140 13.190  26.859  1.00 76.64  ?  258 ILE   B CA    1 
ATOM   4402 C  C     . ILE   B 1 258 ? -30.470 13.897  27.150  1.00 78.86  ?  258 ILE   B C     1 
ATOM   4403 O  O     . ILE   B 1 258 ? -30.737 14.239  28.302  1.00 79.74  ?  258 ILE   B O     1 
ATOM   4404 C  CB    . ILE   B 1 258 ? -28.155 14.168  26.167  1.00 70.91  ?  258 ILE   B CB    1 
ATOM   4405 N  N     . PRO   B 1 259 ? -31.329 14.081  26.123  1.00 81.05  ?  259 PRO   B N     1 
ATOM   4406 C  CA    . PRO   B 1 259 ? -32.669 14.639  26.389  1.00 79.69  ?  259 PRO   B CA    1 
ATOM   4407 C  C     . PRO   B 1 259 ? -33.462 13.886  27.467  1.00 76.38  ?  259 PRO   B C     1 
ATOM   4408 O  O     . PRO   B 1 259 ? -34.174 14.516  28.256  1.00 76.72  ?  259 PRO   B O     1 
ATOM   4409 C  CB    . PRO   B 1 259 ? -33.377 14.526  25.031  1.00 81.64  ?  259 PRO   B CB    1 
ATOM   4410 C  CG    . PRO   B 1 259 ? -32.287 14.513  24.020  1.00 82.88  ?  259 PRO   B CG    1 
ATOM   4411 C  CD    . PRO   B 1 259 ? -31.076 13.918  24.675  1.00 82.63  ?  259 PRO   B CD    1 
ATOM   4412 N  N     . GLU   B 1 260 ? -33.332 12.555  27.480  1.00 72.41  ?  260 GLU   B N     1 
ATOM   4413 C  CA    . GLU   B 1 260 ? -33.968 11.682  28.480  1.00 67.17  ?  260 GLU   B CA    1 
ATOM   4414 C  C     . GLU   B 1 260 ? -33.416 11.892  29.893  1.00 65.58  ?  260 GLU   B C     1 
ATOM   4415 O  O     . GLU   B 1 260 ? -34.180 11.952  30.869  1.00 55.52  ?  260 GLU   B O     1 
ATOM   4416 C  CB    . GLU   B 1 260 ? -33.809 10.205  28.084  1.00 68.32  ?  260 GLU   B CB    1 
ATOM   4417 N  N     . LEU   B 1 261 ? -32.083 11.953  29.985  1.00 71.96  ?  261 LEU   B N     1 
ATOM   4418 C  CA    . LEU   B 1 261 ? -31.359 12.212  31.247  1.00 72.17  ?  261 LEU   B CA    1 
ATOM   4419 C  C     . LEU   B 1 261 ? -31.689 13.585  31.830  1.00 68.61  ?  261 LEU   B C     1 
ATOM   4420 O  O     . LEU   B 1 261 ? -31.999 13.702  33.017  1.00 69.34  ?  261 LEU   B O     1 
ATOM   4421 C  CB    . LEU   B 1 261 ? -29.836 12.075  31.048  1.00 70.24  ?  261 LEU   B CB    1 
ATOM   4422 C  CG    . LEU   B 1 261 ? -29.214 10.726  31.419  1.00 70.49  ?  261 LEU   B CG    1 
ATOM   4423 C  CD1   . LEU   B 1 261 ? -30.000 9.543   30.875  1.00 68.93  ?  261 LEU   B CD1   1 
ATOM   4424 C  CD2   . LEU   B 1 261 ? -27.771 10.679  30.931  1.00 71.96  ?  261 LEU   B CD2   1 
ATOM   4425 N  N     . GLU   B 1 262 ? -31.610 14.613  30.985  1.00 70.33  ?  262 GLU   B N     1 
ATOM   4426 C  CA    . GLU   B 1 262 ? -31.994 15.991  31.357  1.00 70.21  ?  262 GLU   B CA    1 
ATOM   4427 C  C     . GLU   B 1 262 ? -33.414 16.032  31.940  1.00 67.85  ?  262 GLU   B C     1 
ATOM   4428 O  O     . GLU   B 1 262 ? -33.664 16.676  32.954  1.00 66.50  ?  262 GLU   B O     1 
ATOM   4429 C  CB    . GLU   B 1 262 ? -31.865 16.928  30.147  1.00 68.61  ?  262 GLU   B CB    1 
ATOM   4430 C  CG    . GLU   B 1 262 ? -30.428 17.373  29.883  1.00 69.98  ?  262 GLU   B CG    1 
ATOM   4431 C  CD    . GLU   B 1 262 ? -30.165 17.837  28.458  1.00 74.25  ?  262 GLU   B CD    1 
ATOM   4432 O  OE1   . GLU   B 1 262 ? -29.243 18.669  28.263  1.00 73.83  ?  262 GLU   B OE1   1 
ATOM   4433 O  OE2   . GLU   B 1 262 ? -30.859 17.359  27.534  1.00 74.02  ?  262 GLU   B OE2   1 
ATOM   4434 N  N     . LYS   B 1 263 ? -34.326 15.299  31.308  1.00 69.92  ?  263 LYS   B N     1 
ATOM   4435 C  CA    . LYS   B 1 263 ? -35.710 15.182  31.775  1.00 66.95  ?  263 LYS   B CA    1 
ATOM   4436 C  C     . LYS   B 1 263 ? -35.777 14.483  33.132  1.00 62.92  ?  263 LYS   B C     1 
ATOM   4437 O  O     . LYS   B 1 263 ? -36.446 14.956  34.050  1.00 61.37  ?  263 LYS   B O     1 
ATOM   4438 C  CB    . LYS   B 1 263 ? -36.546 14.419  30.741  1.00 69.90  ?  263 LYS   B CB    1 
ATOM   4439 N  N     . GLN   B 1 264 ? -35.053 13.370  33.249  1.00 62.18  ?  264 GLN   B N     1 
ATOM   4440 C  CA    . GLN   B 1 264 ? -35.026 12.544  34.467  1.00 62.13  ?  264 GLN   B CA    1 
ATOM   4441 C  C     . GLN   B 1 264 ? -34.465 13.273  35.698  1.00 59.65  ?  264 GLN   B C     1 
ATOM   4442 O  O     . GLN   B 1 264 ? -34.884 13.018  36.826  1.00 55.59  ?  264 GLN   B O     1 
ATOM   4443 C  CB    . GLN   B 1 264 ? -34.219 11.255  34.227  1.00 62.35  ?  264 GLN   B CB    1 
ATOM   4444 N  N     . PHE   B 1 265 ? -33.525 14.185  35.469  1.00 62.15  ?  265 PHE   B N     1 
ATOM   4445 C  CA    . PHE   B 1 265 ? -32.910 14.978  36.539  1.00 59.38  ?  265 PHE   B CA    1 
ATOM   4446 C  C     . PHE   B 1 265 ? -33.557 16.373  36.708  1.00 64.05  ?  265 PHE   B C     1 
ATOM   4447 O  O     . PHE   B 1 265 ? -32.979 17.266  37.351  1.00 62.85  ?  265 PHE   B O     1 
ATOM   4448 C  CB    . PHE   B 1 265 ? -31.409 15.114  36.253  1.00 58.74  ?  265 PHE   B CB    1 
ATOM   4449 C  CG    . PHE   B 1 265 ? -30.638 13.833  36.397  1.00 55.95  ?  265 PHE   B CG    1 
ATOM   4450 C  CD1   . PHE   B 1 265 ? -30.673 13.116  37.592  1.00 56.37  ?  265 PHE   B CD1   1 
ATOM   4451 C  CD2   . PHE   B 1 265 ? -29.847 13.353  35.355  1.00 57.59  ?  265 PHE   B CD2   1 
ATOM   4452 C  CE1   . PHE   B 1 265 ? -29.949 11.942  37.740  1.00 56.24  ?  265 PHE   B CE1   1 
ATOM   4453 C  CE2   . PHE   B 1 265 ? -29.114 12.177  35.500  1.00 55.73  ?  265 PHE   B CE2   1 
ATOM   4454 C  CZ    . PHE   B 1 265 ? -29.168 11.474  36.692  1.00 56.77  ?  265 PHE   B CZ    1 
ATOM   4455 N  N     . GLU   B 1 266 ? -34.756 16.556  36.143  1.00 63.28  ?  266 GLU   B N     1 
ATOM   4456 C  CA    . GLU   B 1 266 ? -35.536 17.789  36.311  1.00 62.19  ?  266 GLU   B CA    1 
ATOM   4457 C  C     . GLU   B 1 266 ? -35.912 17.948  37.776  1.00 60.32  ?  266 GLU   B C     1 
ATOM   4458 O  O     . GLU   B 1 266 ? -36.414 17.002  38.395  1.00 58.27  ?  266 GLU   B O     1 
ATOM   4459 C  CB    . GLU   B 1 266 ? -36.809 17.777  35.450  1.00 58.75  ?  266 GLU   B CB    1 
ATOM   4460 N  N     . GLY   B 1 267 ? -35.630 19.136  38.321  1.00 62.32  ?  267 GLY   B N     1 
ATOM   4461 C  CA    . GLY   B 1 267 ? -35.889 19.462  39.734  1.00 62.53  ?  267 GLY   B CA    1 
ATOM   4462 C  C     . GLY   B 1 267 ? -34.886 18.876  40.721  1.00 59.75  ?  267 GLY   B C     1 
ATOM   4463 O  O     . GLY   B 1 267 ? -35.102 18.938  41.928  1.00 60.23  ?  267 GLY   B O     1 
ATOM   4464 N  N     . LYS   B 1 268 ? -33.796 18.310  40.201  1.00 58.40  ?  268 LYS   B N     1 
ATOM   4465 C  CA    . LYS   B 1 268 ? -32.756 17.638  40.991  1.00 57.67  ?  268 LYS   B CA    1 
ATOM   4466 C  C     . LYS   B 1 268 ? -31.401 18.295  40.666  1.00 57.24  ?  268 LYS   B C     1 
ATOM   4467 O  O     . LYS   B 1 268 ? -31.259 19.001  39.668  1.00 54.53  ?  268 LYS   B O     1 
ATOM   4468 C  CB    . LYS   B 1 268 ? -32.741 16.129  40.681  1.00 54.32  ?  268 LYS   B CB    1 
ATOM   4469 C  CG    . LYS   B 1 268 ? -34.081 15.446  40.950  1.00 56.06  ?  268 LYS   B CG    1 
ATOM   4470 C  CD    . LYS   B 1 268 ? -34.147 14.022  40.397  1.00 60.36  ?  268 LYS   B CD    1 
ATOM   4471 C  CE    . LYS   B 1 268 ? -35.504 13.362  40.630  1.00 61.28  ?  268 LYS   B CE    1 
ATOM   4472 N  NZ    . LYS   B 1 268 ? -36.603 14.017  39.861  1.00 63.60  ?  268 LYS   B NZ    1 
ATOM   4473 N  N     . MET   B 1 269 ? -30.405 18.037  41.507  1.00 56.00  ?  269 MET   B N     1 
ATOM   4474 C  CA    . MET   B 1 269 ? -29.089 18.684  41.414  1.00 51.70  ?  269 MET   B CA    1 
ATOM   4475 C  C     . MET   B 1 269 ? -27.977 17.632  41.174  1.00 51.12  ?  269 MET   B C     1 
ATOM   4476 O  O     . MET   B 1 269 ? -28.269 16.474  40.801  1.00 48.68  ?  269 MET   B O     1 
ATOM   4477 C  CB    . MET   B 1 269 ? -28.875 19.541  42.680  1.00 51.56  ?  269 MET   B CB    1 
ATOM   4478 C  CG    . MET   B 1 269 ? -29.745 20.805  42.711  1.00 53.65  ?  269 MET   B CG    1 
ATOM   4479 S  SD    . MET   B 1 269 ? -29.858 21.613  44.332  1.00 55.29  ?  269 MET   B SD    1 
ATOM   4480 C  CE    . MET   B 1 269 ? -31.399 20.898  44.921  1.00 56.67  ?  269 MET   B CE    1 
ATOM   4481 N  N     . TYR   B 1 270 ? -26.720 18.030  41.394  1.00 48.74  ?  270 TYR   B N     1 
ATOM   4482 C  CA    . TYR   B 1 270 ? -25.548 17.221  41.045  1.00 49.21  ?  270 TYR   B CA    1 
ATOM   4483 C  C     . TYR   B 1 270 ? -25.354 15.991  41.940  1.00 47.79  ?  270 TYR   B C     1 
ATOM   4484 O  O     . TYR   B 1 270 ? -24.680 15.039  41.541  1.00 47.47  ?  270 TYR   B O     1 
ATOM   4485 C  CB    . TYR   B 1 270 ? -24.281 18.099  41.006  1.00 49.55  ?  270 TYR   B CB    1 
ATOM   4486 C  CG    . TYR   B 1 270 ? -24.432 19.372  40.183  1.00 52.69  ?  270 TYR   B CG    1 
ATOM   4487 C  CD1   . TYR   B 1 270 ? -23.721 20.533  40.507  1.00 56.53  ?  270 TYR   B CD1   1 
ATOM   4488 C  CD2   . TYR   B 1 270 ? -25.319 19.434  39.109  1.00 54.33  ?  270 TYR   B CD2   1 
ATOM   4489 C  CE1   . TYR   B 1 270 ? -23.876 21.702  39.761  1.00 56.80  ?  270 TYR   B CE1   1 
ATOM   4490 C  CE2   . TYR   B 1 270 ? -25.479 20.592  38.366  1.00 55.93  ?  270 TYR   B CE2   1 
ATOM   4491 C  CZ    . TYR   B 1 270 ? -24.768 21.721  38.681  1.00 54.98  ?  270 TYR   B CZ    1 
ATOM   4492 O  OH    . TYR   B 1 270 ? -24.973 22.847  37.908  1.00 52.89  ?  270 TYR   B OH    1 
ATOM   4493 N  N     . GLY   B 1 271 ? -25.949 16.016  43.137  1.00 44.08  ?  271 GLY   B N     1 
ATOM   4494 C  CA    . GLY   B 1 271 ? -25.999 14.876  44.024  1.00 40.28  ?  271 GLY   B CA    1 
ATOM   4495 C  C     . GLY   B 1 271 ? -26.748 13.684  43.426  1.00 41.90  ?  271 GLY   B C     1 
ATOM   4496 O  O     . GLY   B 1 271 ? -26.262 12.558  43.478  1.00 37.12  ?  271 GLY   B O     1 
ATOM   4497 N  N     . HIS   B 1 272 ? -27.935 13.934  42.874  1.00 43.01  ?  272 HIS   B N     1 
ATOM   4498 C  CA    . HIS   B 1 272 ? -28.685 12.917  42.135  1.00 47.79  ?  272 HIS   B CA    1 
ATOM   4499 C  C     . HIS   B 1 272 ? -27.925 12.434  40.876  1.00 50.56  ?  272 HIS   B C     1 
ATOM   4500 O  O     . HIS   B 1 272 ? -27.857 11.216  40.607  1.00 51.48  ?  272 HIS   B O     1 
ATOM   4501 C  CB    . HIS   B 1 272 ? -30.079 13.434  41.732  1.00 50.51  ?  272 HIS   B CB    1 
ATOM   4502 C  CG    . HIS   B 1 272 ? -31.127 13.219  42.779  1.00 49.97  ?  272 HIS   B CG    1 
ATOM   4503 N  ND1   . HIS   B 1 272 ? -31.441 14.173  43.725  1.00 48.16  ?  272 HIS   B ND1   1 
ATOM   4504 C  CD2   . HIS   B 1 272 ? -31.919 12.152  43.038  1.00 49.66  ?  272 HIS   B CD2   1 
ATOM   4505 C  CE1   . HIS   B 1 272 ? -32.396 13.708  44.512  1.00 51.38  ?  272 HIS   B CE1   1 
ATOM   4506 N  NE2   . HIS   B 1 272 ? -32.700 12.483  44.120  1.00 50.96  ?  272 HIS   B NE2   1 
ATOM   4507 N  N     . LEU   B 1 273 ? -27.350 13.375  40.125  1.00 49.56  ?  273 LEU   B N     1 
ATOM   4508 C  CA    . LEU   B 1 273 ? -26.536 13.036  38.938  1.00 54.51  ?  273 LEU   B CA    1 
ATOM   4509 C  C     . LEU   B 1 273 ? -25.404 12.070  39.307  1.00 52.11  ?  273 LEU   B C     1 
ATOM   4510 O  O     . LEU   B 1 273 ? -25.364 10.935  38.837  1.00 55.07  ?  273 LEU   B O     1 
ATOM   4511 C  CB    . LEU   B 1 273 ? -25.916 14.281  38.283  1.00 54.61  ?  273 LEU   B CB    1 
ATOM   4512 C  CG    . LEU   B 1 273 ? -24.957 14.002  37.107  1.00 58.54  ?  273 LEU   B CG    1 
ATOM   4513 C  CD1   . LEU   B 1 273 ? -25.708 13.410  35.928  1.00 63.36  ?  273 LEU   B CD1   1 
ATOM   4514 C  CD2   . LEU   B 1 273 ? -24.203 15.241  36.666  1.00 59.66  ?  273 LEU   B CD2   1 
ATOM   4515 N  N     . LYS   B 1 274 ? -24.522 12.531  40.187  1.00 46.46  ?  274 LYS   B N     1 
ATOM   4516 C  CA    . LYS   B 1 274 ? -23.291 11.823  40.509  1.00 49.60  ?  274 LYS   B CA    1 
ATOM   4517 C  C     . LYS   B 1 274 ? -23.557 10.446  41.124  1.00 47.28  ?  274 LYS   B C     1 
ATOM   4518 O  O     . LYS   B 1 274 ? -22.788 9.510   40.904  1.00 46.08  ?  274 LYS   B O     1 
ATOM   4519 C  CB    . LYS   B 1 274 ? -22.401 12.679  41.424  1.00 48.56  ?  274 LYS   B CB    1 
ATOM   4520 C  CG    . LYS   B 1 274 ? -21.737 13.844  40.696  1.00 51.98  ?  274 LYS   B CG    1 
ATOM   4521 C  CD    . LYS   B 1 274 ? -20.821 14.648  41.606  1.00 52.34  ?  274 LYS   B CD    1 
ATOM   4522 C  CE    . LYS   B 1 274 ? -19.974 15.653  40.843  1.00 51.38  ?  274 LYS   B CE    1 
ATOM   4523 N  NZ    . LYS   B 1 274 ? -19.171 16.450  41.805  1.00 52.39  ?  274 LYS   B NZ    1 
ATOM   4524 N  N     . GLY   B 1 275 ? -24.642 10.345  41.892  1.00 45.27  ?  275 GLY   B N     1 
ATOM   4525 C  CA    . GLY   B 1 275 ? -25.106 9.082   42.466  1.00 45.18  ?  275 GLY   B CA    1 
ATOM   4526 C  C     . GLY   B 1 275 ? -25.503 8.090   41.397  1.00 47.23  ?  275 GLY   B C     1 
ATOM   4527 O  O     . GLY   B 1 275 ? -25.220 6.905   41.519  1.00 50.17  ?  275 GLY   B O     1 
ATOM   4528 N  N     . GLU   B 1 276 ? -26.121 8.578   40.327  1.00 54.00  ?  276 GLU   B N     1 
ATOM   4529 C  CA    . GLU   B 1 276 ? -26.592 7.718   39.241  1.00 58.79  ?  276 GLU   B CA    1 
ATOM   4530 C  C     . GLU   B 1 276 ? -25.467 7.247   38.309  1.00 53.87  ?  276 GLU   B C     1 
ATOM   4531 O  O     . GLU   B 1 276 ? -25.431 6.077   37.928  1.00 52.86  ?  276 GLU   B O     1 
ATOM   4532 C  CB    . GLU   B 1 276 ? -27.689 8.426   38.438  1.00 63.68  ?  276 GLU   B CB    1 
ATOM   4533 C  CG    . GLU   B 1 276 ? -28.440 7.516   37.471  1.00 70.62  ?  276 GLU   B CG    1 
ATOM   4534 C  CD    . GLU   B 1 276 ? -28.979 6.271   38.144  1.00 72.58  ?  276 GLU   B CD    1 
ATOM   4535 O  OE1   . GLU   B 1 276 ? -29.478 6.382   39.287  1.00 77.35  ?  276 GLU   B OE1   1 
ATOM   4536 O  OE2   . GLU   B 1 276 ? -28.869 5.186   37.539  1.00 73.93  ?  276 GLU   B OE2   1 
ATOM   4537 N  N     . VAL   B 1 277 ? -24.572 8.159   37.938  1.00 49.25  ?  277 VAL   B N     1 
ATOM   4538 C  CA    . VAL   B 1 277 ? -23.359 7.816   37.177  1.00 51.22  ?  277 VAL   B CA    1 
ATOM   4539 C  C     . VAL   B 1 277 ? -22.505 6.814   37.981  1.00 53.04  ?  277 VAL   B C     1 
ATOM   4540 O  O     . VAL   B 1 277 ? -21.979 5.856   37.429  1.00 57.81  ?  277 VAL   B O     1 
ATOM   4541 C  CB    . VAL   B 1 277 ? -22.526 9.080   36.823  1.00 54.73  ?  277 VAL   B CB    1 
ATOM   4542 C  CG1   . VAL   B 1 277 ? -21.164 8.723   36.249  1.00 57.18  ?  277 VAL   B CG1   1 
ATOM   4543 C  CG2   . VAL   B 1 277 ? -23.262 9.944   35.821  1.00 55.95  ?  277 VAL   B CG2   1 
ATOM   4544 N  N     . ALA   B 1 278 ? -22.391 7.036   39.287  1.00 44.72  ?  278 ALA   B N     1 
ATOM   4545 C  CA    . ALA   B 1 278 ? -21.622 6.173   40.170  1.00 44.78  ?  278 ALA   B CA    1 
ATOM   4546 C  C     . ALA   B 1 278 ? -22.172 4.751   40.253  1.00 44.97  ?  278 ALA   B C     1 
ATOM   4547 O  O     . ALA   B 1 278 ? -21.412 3.808   40.192  1.00 43.96  ?  278 ALA   B O     1 
ATOM   4548 C  CB    . ALA   B 1 278 ? -21.525 6.785   41.558  1.00 42.83  ?  278 ALA   B CB    1 
ATOM   4549 N  N     . ASP   B 1 279 ? -23.485 4.613   40.393  1.00 51.76  ?  279 ASP   B N     1 
ATOM   4550 C  CA    . ASP   B 1 279 ? -24.136 3.301   40.428  1.00 55.90  ?  279 ASP   B CA    1 
ATOM   4551 C  C     . ASP   B 1 279 ? -23.977 2.555   39.109  1.00 55.73  ?  279 ASP   B C     1 
ATOM   4552 O  O     . ASP   B 1 279 ? -23.650 1.365   39.115  1.00 58.51  ?  279 ASP   B O     1 
ATOM   4553 C  CB    . ASP   B 1 279 ? -25.631 3.419   40.799  1.00 59.94  ?  279 ASP   B CB    1 
ATOM   4554 C  CG    . ASP   B 1 279 ? -25.872 3.349   42.315  1.00 66.54  ?  279 ASP   B CG    1 
ATOM   4555 O  OD1   . ASP   B 1 279 ? -26.958 2.865   42.717  1.00 74.67  ?  279 ASP   B OD1   1 
ATOM   4556 O  OD2   . ASP   B 1 279 ? -24.979 3.760   43.104  1.00 64.75  ?  279 ASP   B OD2   1 
ATOM   4557 N  N     . ALA   B 1 280 ? -24.219 3.252   37.993  1.00 55.32  ?  280 ALA   B N     1 
ATOM   4558 C  CA    . ALA   B 1 280 ? -24.049 2.676   36.646  1.00 54.94  ?  280 ALA   B CA    1 
ATOM   4559 C  C     . ALA   B 1 280 ? -22.628 2.093   36.443  1.00 55.63  ?  280 ALA   B C     1 
ATOM   4560 O  O     . ALA   B 1 280 ? -22.455 0.859   36.258  1.00 52.45  ?  280 ALA   B O     1 
ATOM   4561 C  CB    . ALA   B 1 280 ? -24.351 3.726   35.594  1.00 57.00  ?  280 ALA   B CB    1 
ATOM   4562 N  N     . VAL   B 1 281 ? -21.626 2.964   36.578  1.00 49.82  ?  281 VAL   B N     1 
ATOM   4563 C  CA    . VAL   B 1 281 ? -20.239 2.629   36.251  1.00 51.09  ?  281 VAL   B CA    1 
ATOM   4564 C  C     . VAL   B 1 281 ? -19.685 1.596   37.247  1.00 49.59  ?  281 VAL   B C     1 
ATOM   4565 O  O     . VAL   B 1 281 ? -18.978 0.686   36.847  1.00 50.59  ?  281 VAL   B O     1 
ATOM   4566 C  CB    . VAL   B 1 281 ? -19.340 3.890   36.187  1.00 50.52  ?  281 VAL   B CB    1 
ATOM   4567 C  CG1   . VAL   B 1 281 ? -17.917 3.544   35.755  1.00 54.64  ?  281 VAL   B CG1   1 
ATOM   4568 C  CG2   . VAL   B 1 281 ? -19.917 4.922   35.219  1.00 48.81  ?  281 VAL   B CG2   1 
ATOM   4569 N  N     . SER   B 1 282 ? -20.034 1.724   38.530  1.00 52.20  ?  282 SER   B N     1 
ATOM   4570 C  CA    . SER   B 1 282 ? -19.563 0.799   39.576  1.00 51.13  ?  282 SER   B CA    1 
ATOM   4571 C  C     . SER   B 1 282 ? -20.051 -0.634  39.324  1.00 51.91  ?  282 SER   B C     1 
ATOM   4572 O  O     . SER   B 1 282 ? -19.290 -1.600  39.459  1.00 54.18  ?  282 SER   B O     1 
ATOM   4573 C  CB    . SER   B 1 282 ? -19.982 1.286   40.963  1.00 56.08  ?  282 SER   B CB    1 
ATOM   4574 O  OG    . SER   B 1 282 ? -19.485 0.440   41.998  1.00 62.18  ?  282 SER   B OG    1 
ATOM   4575 N  N     . GLY   B 1 283 ? -21.305 -0.764  38.907  1.00 52.63  ?  283 GLY   B N     1 
ATOM   4576 C  CA    . GLY   B 1 283 ? -21.887 -2.073  38.556  1.00 51.92  ?  283 GLY   B CA    1 
ATOM   4577 C  C     . GLY   B 1 283 ? -21.251 -2.726  37.334  1.00 50.88  ?  283 GLY   B C     1 
ATOM   4578 O  O     . GLY   B 1 283 ? -21.085 -3.967  37.298  1.00 47.25  ?  283 GLY   B O     1 
ATOM   4579 N  N     . MET   B 1 284 ? -20.882 -1.891  36.354  1.00 45.91  ?  284 MET   B N     1 
ATOM   4580 C  CA    . MET   B 1 284 ? -20.221 -2.357  35.105  1.00 47.64  ?  284 MET   B CA    1 
ATOM   4581 C  C     . MET   B 1 284 ? -18.803 -2.881  35.362  1.00 45.45  ?  284 MET   B C     1 
ATOM   4582 O  O     . MET   B 1 284 ? -18.478 -4.019  34.990  1.00 42.29  ?  284 MET   B O     1 
ATOM   4583 C  CB    . MET   B 1 284 ? -20.163 -1.228  34.090  1.00 48.99  ?  284 MET   B CB    1 
ATOM   4584 C  CG    . MET   B 1 284 ? -19.789 -1.673  32.689  1.00 54.23  ?  284 MET   B CG    1 
ATOM   4585 S  SD    . MET   B 1 284 ? -19.000 -0.311  31.828  1.00 61.96  ?  284 MET   B SD    1 
ATOM   4586 C  CE    . MET   B 1 284 ? -17.303 -0.535  32.311  1.00 57.63  ?  284 MET   B CE    1 
ATOM   4587 N  N     . LEU   B 1 285 ? -17.993 -2.054  36.028  1.00 44.33  ?  285 LEU   B N     1 
ATOM   4588 C  CA    . LEU   B 1 285 ? -16.621 -2.422  36.412  1.00 47.56  ?  285 LEU   B CA    1 
ATOM   4589 C  C     . LEU   B 1 285 ? -16.514 -3.673  37.284  1.00 46.86  ?  285 LEU   B C     1 
ATOM   4590 O  O     . LEU   B 1 285 ? -15.582 -4.438  37.128  1.00 44.57  ?  285 LEU   B O     1 
ATOM   4591 C  CB    . LEU   B 1 285 ? -15.933 -1.252  37.135  1.00 48.67  ?  285 LEU   B CB    1 
ATOM   4592 C  CG    . LEU   B 1 285 ? -15.735 0.045   36.336  1.00 45.83  ?  285 LEU   B CG    1 
ATOM   4593 C  CD1   . LEU   B 1 285 ? -14.845 0.986   37.130  1.00 48.16  ?  285 LEU   B CD1   1 
ATOM   4594 C  CD2   . LEU   B 1 285 ? -15.107 -0.224  34.980  1.00 48.18  ?  285 LEU   B CD2   1 
ATOM   4595 N  N     . THR   B 1 286 ? -17.471 -3.856  38.198  1.00 51.47  ?  286 THR   B N     1 
ATOM   4596 C  CA    . THR   B 1 286 ? -17.525 -5.039  39.069  1.00 50.30  ?  286 THR   B CA    1 
ATOM   4597 C  C     . THR   B 1 286 ? -17.768 -6.312  38.277  1.00 48.66  ?  286 THR   B C     1 
ATOM   4598 O  O     . THR   B 1 286 ? -17.143 -7.327  38.570  1.00 47.83  ?  286 THR   B O     1 
ATOM   4599 C  CB    . THR   B 1 286 ? -18.594 -4.873  40.173  1.00 48.98  ?  286 THR   B CB    1 
ATOM   4600 O  OG1   . THR   B 1 286 ? -18.287 -3.697  40.924  1.00 47.81  ?  286 THR   B OG1   1 
ATOM   4601 C  CG2   . THR   B 1 286 ? -18.636 -6.070  41.121  1.00 47.55  ?  286 THR   B CG2   1 
ATOM   4602 N  N     . GLU   B 1 287 ? -18.649 -6.250  37.275  1.00 52.23  ?  287 GLU   B N     1 
ATOM   4603 C  CA    . GLU   B 1 287 ? -18.922 -7.396  36.377  1.00 53.08  ?  287 GLU   B CA    1 
ATOM   4604 C  C     . GLU   B 1 287 ? -17.724 -7.685  35.469  1.00 53.51  ?  287 GLU   B C     1 
ATOM   4605 O  O     . GLU   B 1 287 ? -17.272 -8.831  35.363  1.00 55.91  ?  287 GLU   B O     1 
ATOM   4606 C  CB    . GLU   B 1 287 ? -20.161 -7.135  35.510  1.00 54.13  ?  287 GLU   B CB    1 
ATOM   4607 C  CG    . GLU   B 1 287 ? -20.706 -8.363  34.773  1.00 60.85  ?  287 GLU   B CG    1 
ATOM   4608 C  CD    . GLU   B 1 287 ? -20.028 -8.691  33.433  1.00 70.35  ?  287 GLU   B CD    1 
ATOM   4609 O  OE1   . GLU   B 1 287 ? -19.255 -7.864  32.880  1.00 76.38  ?  287 GLU   B OE1   1 
ATOM   4610 O  OE2   . GLU   B 1 287 ? -20.277 -9.808  32.915  1.00 70.37  ?  287 GLU   B OE2   1 
ATOM   4611 N  N     . LEU   B 1 288 ? -17.239 -6.642  34.795  1.00 48.86  ?  288 LEU   B N     1 
ATOM   4612 C  CA    . LEU   B 1 288 ? -16.095 -6.757  33.884  1.00 48.16  ?  288 LEU   B CA    1 
ATOM   4613 C  C     . LEU   B 1 288 ? -14.890 -7.375  34.573  1.00 44.99  ?  288 LEU   B C     1 
ATOM   4614 O  O     . LEU   B 1 288 ? -14.293 -8.319  34.057  1.00 44.52  ?  288 LEU   B O     1 
ATOM   4615 C  CB    . LEU   B 1 288 ? -15.718 -5.380  33.343  1.00 48.78  ?  288 LEU   B CB    1 
ATOM   4616 C  CG    . LEU   B 1 288 ? -14.710 -5.367  32.201  1.00 47.79  ?  288 LEU   B CG    1 
ATOM   4617 C  CD1   . LEU   B 1 288 ? -15.386 -5.812  30.914  1.00 50.43  ?  288 LEU   B CD1   1 
ATOM   4618 C  CD2   . LEU   B 1 288 ? -14.103 -3.991  32.039  1.00 50.15  ?  288 LEU   B CD2   1 
ATOM   4619 N  N     . GLN   B 1 289 ? -14.561 -6.842  35.748  1.00 42.64  ?  289 GLN   B N     1 
ATOM   4620 C  CA    . GLN   B 1 289 ? -13.397 -7.301  36.528  1.00 47.28  ?  289 GLN   B CA    1 
ATOM   4621 C  C     . GLN   B 1 289 ? -13.506 -8.774  36.985  1.00 47.27  ?  289 GLN   B C     1 
ATOM   4622 O  O     . GLN   B 1 289 ? -12.495 -9.474  37.086  1.00 46.48  ?  289 GLN   B O     1 
ATOM   4623 C  CB    . GLN   B 1 289 ? -13.120 -6.357  37.718  1.00 46.44  ?  289 GLN   B CB    1 
ATOM   4624 C  CG    . GLN   B 1 289 ? -12.513 -5.012  37.292  1.00 46.30  ?  289 GLN   B CG    1 
ATOM   4625 C  CD    . GLN   B 1 289 ? -12.465 -3.973  38.400  1.00 50.86  ?  289 GLN   B CD    1 
ATOM   4626 O  OE1   . GLN   B 1 289 ? -12.385 -4.313  39.589  1.00 53.87  ?  289 GLN   B OE1   1 
ATOM   4627 N  NE2   . GLN   B 1 289 ? -12.491 -2.689  38.017  1.00 51.76  ?  289 GLN   B NE2   1 
ATOM   4628 N  N     . GLU   B 1 290 ? -14.731 -9.227  37.236  1.00 50.18  ?  290 GLU   B N     1 
ATOM   4629 C  CA    . GLU   B 1 290 ? -15.003 -10.626 37.559  1.00 48.16  ?  290 GLU   B CA    1 
ATOM   4630 C  C     . GLU   B 1 290 ? -14.617 -11.516 36.374  1.00 46.11  ?  290 GLU   B C     1 
ATOM   4631 O  O     . GLU   B 1 290 ? -13.912 -12.504 36.545  1.00 47.96  ?  290 GLU   B O     1 
ATOM   4632 C  CB    . GLU   B 1 290 ? -16.475 -10.838 37.935  1.00 51.25  ?  290 GLU   B CB    1 
ATOM   4633 N  N     . ARG   B 1 291 ? -15.055 -11.147 35.175  1.00 43.31  ?  291 ARG   B N     1 
ATOM   4634 C  CA    . ARG   B 1 291 ? -14.645 -11.865 33.932  1.00 41.01  ?  291 ARG   B CA    1 
ATOM   4635 C  C     . ARG   B 1 291 ? -13.133 -11.781 33.688  1.00 37.04  ?  291 ARG   B C     1 
ATOM   4636 O  O     . ARG   B 1 291 ? -12.522 -12.792 33.353  1.00 34.22  ?  291 ARG   B O     1 
ATOM   4637 C  CB    . ARG   B 1 291 ? -15.344 -11.320 32.689  1.00 41.82  ?  291 ARG   B CB    1 
ATOM   4638 C  CG    . ARG   B 1 291 ? -16.863 -11.187 32.802  1.00 47.13  ?  291 ARG   B CG    1 
ATOM   4639 C  CD    . ARG   B 1 291 ? -17.474 -11.003 31.425  1.00 45.75  ?  291 ARG   B CD    1 
ATOM   4640 N  NE    . ARG   B 1 291 ? -17.344 -12.225 30.615  1.00 47.17  ?  291 ARG   B NE    1 
ATOM   4641 C  CZ    . ARG   B 1 291 ? -17.007 -12.276 29.316  1.00 45.26  ?  291 ARG   B CZ    1 
ATOM   4642 N  NH1   . ARG   B 1 291 ? -16.917 -13.458 28.696  1.00 41.76  ?  291 ARG   B NH1   1 
ATOM   4643 N  NH2   . ARG   B 1 291 ? -16.740 -11.170 28.631  1.00 40.92  ?  291 ARG   B NH2   1 
ATOM   4644 N  N     . TYR   B 1 292 ? -12.565 -10.581 33.875  1.00 33.01  ?  292 TYR   B N     1 
ATOM   4645 C  CA    . TYR   B 1 292 ? -11.157 -10.306 33.624  1.00 36.43  ?  292 TYR   B CA    1 
ATOM   4646 C  C     . TYR   B 1 292 ? -10.225 -11.249 34.337  1.00 35.73  ?  292 TYR   B C     1 
ATOM   4647 O  O     . TYR   B 1 292 ? -9.302  -11.755 33.718  1.00 35.85  ?  292 TYR   B O     1 
ATOM   4648 C  CB    . TYR   B 1 292 ? -10.792 -8.867  34.003  1.00 35.31  ?  292 TYR   B CB    1 
ATOM   4649 C  CG    . TYR   B 1 292 ? -9.313  -8.566  33.912  1.00 36.15  ?  292 TYR   B CG    1 
ATOM   4650 C  CD1   . TYR   B 1 292 ? -8.522  -8.483  35.067  1.00 37.32  ?  292 TYR   B CD1   1 
ATOM   4651 C  CD2   . TYR   B 1 292 ? -8.689  -8.342  32.674  1.00 35.98  ?  292 TYR   B CD2   1 
ATOM   4652 C  CE1   . TYR   B 1 292 ? -7.160  -8.183  34.993  1.00 36.79  ?  292 TYR   B CE1   1 
ATOM   4653 C  CE2   . TYR   B 1 292 ? -7.328  -8.056  32.594  1.00 33.41  ?  292 TYR   B CE2   1 
ATOM   4654 C  CZ    . TYR   B 1 292 ? -6.565  -7.971  33.746  1.00 37.76  ?  292 TYR   B CZ    1 
ATOM   4655 O  OH    . TYR   B 1 292 ? -5.203  -7.687  33.672  1.00 36.66  ?  292 TYR   B OH    1 
ATOM   4656 N  N     . HIS   B 1 293 ? -10.470 -11.464 35.631  1.00 39.29  ?  293 HIS   B N     1 
ATOM   4657 C  CA    . HIS   B 1 293 ? -9.613  -12.290 36.451  1.00 41.93  ?  293 HIS   B CA    1 
ATOM   4658 C  C     . HIS   B 1 293 ? -9.680  -13.773 36.061  1.00 40.92  ?  293 HIS   B C     1 
ATOM   4659 O  O     . HIS   B 1 293 ? -8.668  -14.464 36.107  1.00 43.18  ?  293 HIS   B O     1 
ATOM   4660 C  CB    . HIS   B 1 293 ? -9.909  -12.064 37.949  1.00 45.35  ?  293 HIS   B CB    1 
ATOM   4661 C  CG    . HIS   B 1 293 ? -9.418  -10.743 38.458  1.00 46.11  ?  293 HIS   B CG    1 
ATOM   4662 N  ND1   . HIS   B 1 293 ? -8.081  -10.403 38.468  1.00 46.18  ?  293 HIS   B ND1   1 
ATOM   4663 C  CD2   . HIS   B 1 293 ? -10.081 -9.673  38.959  1.00 48.42  ?  293 HIS   B CD2   1 
ATOM   4664 C  CE1   . HIS   B 1 293 ? -7.941  -9.179  38.946  1.00 47.32  ?  293 HIS   B CE1   1 
ATOM   4665 N  NE2   . HIS   B 1 293 ? -9.140  -8.713  39.250  1.00 49.91  ?  293 HIS   B NE2   1 
ATOM   4666 N  N     . ARG   B 1 294 ? -10.849 -14.243 35.646  1.00 39.28  ?  294 ARG   B N     1 
ATOM   4667 C  CA    . ARG   B 1 294 ? -10.988 -15.610 35.136  1.00 40.92  ?  294 ARG   B CA    1 
ATOM   4668 C  C     . ARG   B 1 294 ? -10.131 -15.829 33.886  1.00 41.34  ?  294 ARG   B C     1 
ATOM   4669 O  O     . ARG   B 1 294 ? -9.551  -16.913 33.718  1.00 40.41  ?  294 ARG   B O     1 
ATOM   4670 C  CB    . ARG   B 1 294 ? -12.458 -15.952 34.821  1.00 45.51  ?  294 ARG   B CB    1 
ATOM   4671 C  CG    . ARG   B 1 294 ? -13.374 -15.978 36.042  1.00 53.56  ?  294 ARG   B CG    1 
ATOM   4672 C  CD    . ARG   B 1 294 ? -14.788 -16.476 35.741  1.00 54.73  ?  294 ARG   B CD    1 
ATOM   4673 N  NE    . ARG   B 1 294 ? -15.793 -15.567 36.308  1.00 61.62  ?  294 ARG   B NE    1 
ATOM   4674 C  CZ    . ARG   B 1 294 ? -16.683 -14.847 35.615  1.00 66.49  ?  294 ARG   B CZ    1 
ATOM   4675 N  NH1   . ARG   B 1 294 ? -16.758 -14.925 34.279  1.00 69.46  ?  294 ARG   B NH1   1 
ATOM   4676 N  NH2   . ARG   B 1 294 ? -17.527 -14.038 36.268  1.00 63.71  ?  294 ARG   B NH2   1 
ATOM   4677 N  N     . PHE   B 1 295 ? -10.083 -14.809 33.010  1.00 37.32  ?  295 PHE   B N     1 
ATOM   4678 C  CA    . PHE   B 1 295 ? -9.311  -14.859 31.758  1.00 36.08  ?  295 PHE   B CA    1 
ATOM   4679 C  C     . PHE   B 1 295 ? -7.815  -14.628 31.999  1.00 34.02  ?  295 PHE   B C     1 
ATOM   4680 O  O     . PHE   B 1 295 ? -6.980  -15.435 31.552  1.00 27.40  ?  295 PHE   B O     1 
ATOM   4681 C  CB    . PHE   B 1 295 ? -9.836  -13.821 30.742  1.00 36.77  ?  295 PHE   B CB    1 
ATOM   4682 C  CG    . PHE   B 1 295 ? -11.200 -14.142 30.176  1.00 35.74  ?  295 PHE   B CG    1 
ATOM   4683 C  CD1   . PHE   B 1 295 ? -11.441 -15.345 29.522  1.00 35.17  ?  295 PHE   B CD1   1 
ATOM   4684 C  CD2   . PHE   B 1 295 ? -12.236 -13.214 30.254  1.00 36.69  ?  295 PHE   B CD2   1 
ATOM   4685 C  CE1   . PHE   B 1 295 ? -12.698 -15.627 28.981  1.00 34.81  ?  295 PHE   B CE1   1 
ATOM   4686 C  CE2   . PHE   B 1 295 ? -13.487 -13.494 29.708  1.00 37.05  ?  295 PHE   B CE2   1 
ATOM   4687 C  CZ    . PHE   B 1 295 ? -13.719 -14.702 29.080  1.00 34.28  ?  295 PHE   B CZ    1 
ATOM   4688 N  N     . ARG   B 1 296 ? -7.497  -13.552 32.727  1.00 33.94  ?  296 ARG   B N     1 
ATOM   4689 C  CA    . ARG   B 1 296 ? -6.126  -13.088 32.894  1.00 35.02  ?  296 ARG   B CA    1 
ATOM   4690 C  C     . ARG   B 1 296 ? -5.198  -14.087 33.585  1.00 39.30  ?  296 ARG   B C     1 
ATOM   4691 O  O     . ARG   B 1 296 ? -4.017  -14.132 33.272  1.00 38.49  ?  296 ARG   B O     1 
ATOM   4692 C  CB    . ARG   B 1 296 ? -6.090  -11.758 33.631  1.00 34.46  ?  296 ARG   B CB    1 
ATOM   4693 C  CG    . ARG   B 1 296 ? -4.714  -11.092 33.710  1.00 36.14  ?  296 ARG   B CG    1 
ATOM   4694 C  CD    . ARG   B 1 296 ? -4.076  -10.877 32.336  1.00 33.91  ?  296 ARG   B CD    1 
ATOM   4695 N  NE    . ARG   B 1 296 ? -2.734  -10.286 32.435  1.00 35.83  ?  296 ARG   B NE    1 
ATOM   4696 C  CZ    . ARG   B 1 296 ? -1.591  -10.964 32.591  1.00 34.65  ?  296 ARG   B CZ    1 
ATOM   4697 N  NH1   . ARG   B 1 296 ? -1.573  -12.299 32.698  1.00 31.68  ?  296 ARG   B NH1   1 
ATOM   4698 N  NH2   . ARG   B 1 296 ? -0.450  -10.292 32.661  1.00 33.98  ?  296 ARG   B NH2   1 
ATOM   4699 N  N     . ASN   B 1 297 ? -5.756  -14.905 34.476  1.00 38.69  ?  297 ASN   B N     1 
ATOM   4700 C  CA    . ASN   B 1 297 ? -5.003  -15.890 35.239  1.00 41.28  ?  297 ASN   B CA    1 
ATOM   4701 C  C     . ASN   B 1 297 ? -4.932  -17.250 34.566  1.00 39.45  ?  297 ASN   B C     1 
ATOM   4702 O  O     . ASN   B 1 297 ? -4.279  -18.158 35.078  1.00 42.34  ?  297 ASN   B O     1 
ATOM   4703 C  CB    . ASN   B 1 297 ? -5.587  -16.014 36.658  1.00 41.17  ?  297 ASN   B CB    1 
ATOM   4704 C  CG    . ASN   B 1 297 ? -5.447  -14.731 37.467  1.00 42.88  ?  297 ASN   B CG    1 
ATOM   4705 O  OD1   . ASN   B 1 297 ? -4.560  -13.911 37.231  1.00 44.13  ?  297 ASN   B OD1   1 
ATOM   4706 N  ND2   . ASN   B 1 297 ? -6.322  -14.559 38.438  1.00 46.04  ?  297 ASN   B ND2   1 
ATOM   4707 N  N     . ASP   B 1 298 ? -5.546  -17.383 33.387  1.00 35.85  ?  298 ASP   B N     1 
ATOM   4708 C  CA    . ASP   B 1 298 ? -5.539  -18.633 32.622  1.00 32.16  ?  298 ASP   B CA    1 
ATOM   4709 C  C     . ASP   B 1 298 ? -4.569  -18.491 31.459  1.00 32.84  ?  298 ASP   B C     1 
ATOM   4710 O  O     . ASP   B 1 298 ? -4.991  -18.171 30.337  1.00 32.39  ?  298 ASP   B O     1 
ATOM   4711 C  CB    . ASP   B 1 298 ? -6.978  -18.906 32.132  1.00 34.58  ?  298 ASP   B CB    1 
ATOM   4712 C  CG    . ASP   B 1 298 ? -7.155  -20.268 31.461  1.00 31.25  ?  298 ASP   B CG    1 
ATOM   4713 O  OD1   . ASP   B 1 298 ? -8.305  -20.582 31.160  1.00 32.10  ?  298 ASP   B OD1   1 
ATOM   4714 O  OD2   . ASP   B 1 298 ? -6.182  -21.001 31.214  1.00 31.52  ?  298 ASP   B OD2   1 
ATOM   4715 N  N     . GLU   B 1 299 ? -3.276  -18.711 31.726  1.00 34.11  ?  299 GLU   B N     1 
ATOM   4716 C  CA    . GLU   B 1 299 ? -2.209  -18.469 30.737  1.00 32.64  ?  299 GLU   B CA    1 
ATOM   4717 C  C     . GLU   B 1 299 ? -2.375  -19.331 29.505  1.00 33.07  ?  299 GLU   B C     1 
ATOM   4718 O  O     . GLU   B 1 299 ? -2.130  -18.868 28.397  1.00 35.89  ?  299 GLU   B O     1 
ATOM   4719 C  CB    . GLU   B 1 299 ? -0.787  -18.622 31.323  1.00 34.65  ?  299 GLU   B CB    1 
ATOM   4720 C  CG    . GLU   B 1 299 ? -0.307  -20.062 31.621  1.00 37.16  ?  299 GLU   B CG    1 
ATOM   4721 C  CD    . GLU   B 1 299 ? -0.774  -20.614 32.979  1.00 40.20  ?  299 GLU   B CD    1 
ATOM   4722 O  OE1   . GLU   B 1 299 ? -0.336  -21.732 33.374  1.00 42.32  ?  299 GLU   B OE1   1 
ATOM   4723 O  OE2   . GLU   B 1 299 ? -1.602  -19.969 33.657  1.00 44.77  ?  299 GLU   B OE2   1 
ATOM   4724 N  N     . ALA   B 1 300 ? -2.800  -20.583 29.714  1.00 30.61  ?  300 ALA   B N     1 
ATOM   4725 C  CA    . ALA   B 1 300 ? -2.988  -21.542 28.653  1.00 30.80  ?  300 ALA   B CA    1 
ATOM   4726 C  C     . ALA   B 1 300 ? -4.072  -21.105 27.650  1.00 31.75  ?  300 ALA   B C     1 
ATOM   4727 O  O     . ALA   B 1 300 ? -3.980  -21.406 26.443  1.00 28.51  ?  300 ALA   B O     1 
ATOM   4728 C  CB    . ALA   B 1 300 ? -3.322  -22.903 29.250  1.00 32.07  ?  300 ALA   B CB    1 
ATOM   4729 N  N     . PHE   B 1 301 ? -5.107  -20.414 28.152  1.00 32.09  ?  301 PHE   B N     1 
ATOM   4730 C  CA    . PHE   B 1 301 ? -6.184  -19.879 27.302  1.00 32.21  ?  301 PHE   B CA    1 
ATOM   4731 C  C     . PHE   B 1 301 ? -5.672  -18.670 26.495  1.00 32.66  ?  301 PHE   B C     1 
ATOM   4732 O  O     . PHE   B 1 301 ? -5.848  -18.594 25.265  1.00 30.00  ?  301 PHE   B O     1 
ATOM   4733 C  CB    . PHE   B 1 301 ? -7.411  -19.522 28.160  1.00 34.68  ?  301 PHE   B CB    1 
ATOM   4734 C  CG    . PHE   B 1 301 ? -8.570  -18.963 27.383  1.00 36.24  ?  301 PHE   B CG    1 
ATOM   4735 C  CD1   . PHE   B 1 301 ? -9.301  -19.766 26.510  1.00 38.54  ?  301 PHE   B CD1   1 
ATOM   4736 C  CD2   . PHE   B 1 301 ? -8.957  -17.622 27.542  1.00 37.05  ?  301 PHE   B CD2   1 
ATOM   4737 C  CE1   . PHE   B 1 301 ? -10.373 -19.240 25.804  1.00 37.36  ?  301 PHE   B CE1   1 
ATOM   4738 C  CE2   . PHE   B 1 301 ? -10.032 -17.109 26.844  1.00 34.91  ?  301 PHE   B CE2   1 
ATOM   4739 C  CZ    . PHE   B 1 301 ? -10.729 -17.909 25.973  1.00 36.42  ?  301 PHE   B CZ    1 
ATOM   4740 N  N     . LEU   B 1 302 ? -5.002  -17.752 27.186  1.00 32.19  ?  302 LEU   B N     1 
ATOM   4741 C  CA    . LEU   B 1 302 ? -4.418  -16.580 26.536  1.00 31.73  ?  302 LEU   B CA    1 
ATOM   4742 C  C     . LEU   B 1 302 ? -3.418  -16.968 25.434  1.00 35.35  ?  302 LEU   B C     1 
ATOM   4743 O  O     . LEU   B 1 302 ? -3.385  -16.331 24.360  1.00 32.02  ?  302 LEU   B O     1 
ATOM   4744 C  CB    . LEU   B 1 302 ? -3.739  -15.681 27.573  1.00 30.63  ?  302 LEU   B CB    1 
ATOM   4745 C  CG    . LEU   B 1 302 ? -4.601  -15.166 28.731  1.00 29.25  ?  302 LEU   B CG    1 
ATOM   4746 C  CD1   . LEU   B 1 302 ? -3.791  -14.266 29.639  1.00 30.50  ?  302 LEU   B CD1   1 
ATOM   4747 C  CD2   . LEU   B 1 302 ? -5.853  -14.494 28.243  1.00 30.24  ?  302 LEU   B CD2   1 
ATOM   4748 N  N     . GLN   B 1 303 ? -2.622  -18.011 25.708  1.00 33.89  ?  303 GLN   B N     1 
ATOM   4749 C  CA    . GLN   B 1 303 ? -1.609  -18.498 24.793  1.00 35.48  ?  303 GLN   B CA    1 
ATOM   4750 C  C     . GLN   B 1 303 ? -2.252  -19.061 23.528  1.00 34.28  ?  303 GLN   B C     1 
ATOM   4751 O  O     . GLN   B 1 303 ? -1.789  -18.776 22.445  1.00 34.56  ?  303 GLN   B O     1 
ATOM   4752 C  CB    . GLN   B 1 303 ? -0.709  -19.551 25.472  1.00 34.89  ?  303 GLN   B CB    1 
ATOM   4753 C  CG    . GLN   B 1 303 ? 0.299   -18.935 26.447  1.00 36.08  ?  303 GLN   B CG    1 
ATOM   4754 C  CD    . GLN   B 1 303 ? 0.910   -19.940 27.424  1.00 38.84  ?  303 GLN   B CD    1 
ATOM   4755 O  OE1   . GLN   B 1 303 ? 0.656   -21.146 27.360  1.00 37.93  ?  303 GLN   B OE1   1 
ATOM   4756 N  NE2   . GLN   B 1 303 ? 1.738   -19.437 28.334  1.00 38.02  ?  303 GLN   B NE2   1 
ATOM   4757 N  N     . GLN   B 1 304 ? -3.323  -19.832 23.690  1.00 34.12  ?  304 GLN   B N     1 
ATOM   4758 C  CA    . GLN   B 1 304 ? -4.083  -20.394 22.571  1.00 37.46  ?  304 GLN   B CA    1 
ATOM   4759 C  C     . GLN   B 1 304 ? -4.720  -19.316 21.710  1.00 35.64  ?  304 GLN   B C     1 
ATOM   4760 O  O     . GLN   B 1 304 ? -4.596  -19.361 20.479  1.00 38.26  ?  304 GLN   B O     1 
ATOM   4761 C  CB    . GLN   B 1 304 ? -5.164  -21.362 23.062  1.00 39.93  ?  304 GLN   B CB    1 
ATOM   4762 C  CG    . GLN   B 1 304 ? -5.834  -22.174 21.943  1.00 45.11  ?  304 GLN   B CG    1 
ATOM   4763 C  CD    . GLN   B 1 304 ? -4.861  -23.039 21.154  1.00 52.05  ?  304 GLN   B CD    1 
ATOM   4764 O  OE1   . GLN   B 1 304 ? -4.824  -22.980 19.920  1.00 57.52  ?  304 GLN   B OE1   1 
ATOM   4765 N  NE2   . GLN   B 1 304 ? -4.064  -23.851 21.859  1.00 52.25  ?  304 GLN   B NE2   1 
ATOM   4766 N  N     . VAL   B 1 305 ? -5.357  -18.332 22.349  1.00 32.87  ?  305 VAL   B N     1 
ATOM   4767 C  CA    . VAL   B 1 305 ? -6.001  -17.200 21.636  1.00 31.50  ?  305 VAL   B CA    1 
ATOM   4768 C  C     . VAL   B 1 305 ? -4.959  -16.460 20.788  1.00 32.59  ?  305 VAL   B C     1 
ATOM   4769 O  O     . VAL   B 1 305 ? -5.203  -16.149 19.601  1.00 26.89  ?  305 VAL   B O     1 
ATOM   4770 C  CB    . VAL   B 1 305 ? -6.697  -16.229 22.622  1.00 33.14  ?  305 VAL   B CB    1 
ATOM   4771 C  CG1   . VAL   B 1 305 ? -7.174  -14.926 21.950  1.00 31.83  ?  305 VAL   B CG1   1 
ATOM   4772 C  CG2   . VAL   B 1 305 ? -7.875  -16.908 23.307  1.00 34.30  ?  305 VAL   B CG2   1 
ATOM   4773 N  N     . MET   B 1 306 ? -3.791  -16.182 21.391  1.00 32.55  ?  306 MET   B N     1 
ATOM   4774 C  CA    . MET   B 1 306 ? -2.690  -15.542 20.665  1.00 32.92  ?  306 MET   B CA    1 
ATOM   4775 C  C     . MET   B 1 306 ? -2.215  -16.369 19.457  1.00 31.81  ?  306 MET   B C     1 
ATOM   4776 O  O     . MET   B 1 306 ? -1.956  -15.809 18.389  1.00 31.10  ?  306 MET   B O     1 
ATOM   4777 C  CB    . MET   B 1 306 ? -1.518  -15.234 21.594  1.00 33.09  ?  306 MET   B CB    1 
ATOM   4778 C  CG    . MET   B 1 306 ? -1.700  -13.926 22.374  1.00 32.03  ?  306 MET   B CG    1 
ATOM   4779 S  SD    . MET   B 1 306 ? -0.288  -13.453 23.380  1.00 29.95  ?  306 MET   B SD    1 
ATOM   4780 C  CE    . MET   B 1 306 ? -0.067  -14.909 24.397  1.00 32.52  ?  306 MET   B CE    1 
ATOM   4781 N  N     . LYS   B 1 307 ? -2.087  -17.683 19.654  1.00 26.49  ?  307 LYS   B N     1 
ATOM   4782 C  CA    . LYS   B 1 307 ? -1.622  -18.584 18.627  1.00 32.26  ?  307 LYS   B CA    1 
ATOM   4783 C  C     . LYS   B 1 307 ? -2.593  -18.629 17.442  1.00 29.49  ?  307 LYS   B C     1 
ATOM   4784 O  O     . LYS   B 1 307 ? -2.159  -18.509 16.298  1.00 29.18  ?  307 LYS   B O     1 
ATOM   4785 C  CB    . LYS   B 1 307 ? -1.431  -20.016 19.188  1.00 34.97  ?  307 LYS   B CB    1 
ATOM   4786 C  CG    . LYS   B 1 307 ? -0.815  -20.990 18.193  1.00 38.05  ?  307 LYS   B CG    1 
ATOM   4787 C  CD    . LYS   B 1 307 ? -0.493  -22.344 18.809  1.00 43.50  ?  307 LYS   B CD    1 
ATOM   4788 C  CE    . LYS   B 1 307 ? -0.694  -23.461 17.781  1.00 49.48  ?  307 LYS   B CE    1 
ATOM   4789 N  NZ    . LYS   B 1 307 ? 0.238   -24.605 18.015  1.00 52.79  ?  307 LYS   B NZ    1 
ATOM   4790 N  N     . ASP   B 1 308 ? -3.880  -18.856 17.719  1.00 32.23  ?  308 ASP   B N     1 
ATOM   4791 C  CA    . ASP   B 1 308 ? -4.919  -18.943 16.665  1.00 35.31  ?  308 ASP   B CA    1 
ATOM   4792 C  C     . ASP   B 1 308 ? -5.116  -17.584 15.974  1.00 31.15  ?  308 ASP   B C     1 
ATOM   4793 O  O     . ASP   B 1 308 ? -5.231  -17.499 14.740  1.00 28.54  ?  308 ASP   B O     1 
ATOM   4794 C  CB    . ASP   B 1 308 ? -6.260  -19.420 17.238  1.00 40.16  ?  308 ASP   B CB    1 
ATOM   4795 C  CG    . ASP   B 1 308 ? -6.164  -20.756 17.914  1.00 42.14  ?  308 ASP   B CG    1 
ATOM   4796 O  OD1   . ASP   B 1 308 ? -6.997  -21.021 18.800  1.00 45.35  ?  308 ASP   B OD1   1 
ATOM   4797 O  OD2   . ASP   B 1 308 ? -5.243  -21.522 17.579  1.00 51.06  ?  308 ASP   B OD2   1 
ATOM   4798 N  N     . GLY   B 1 309 ? -5.135  -16.526 16.781  1.00 28.22  ?  309 GLY   B N     1 
ATOM   4799 C  CA    . GLY   B 1 309 ? -5.223  -15.167 16.266  1.00 28.90  ?  309 GLY   B CA    1 
ATOM   4800 C  C     . GLY   B 1 309 ? -4.176  -14.879 15.197  1.00 29.54  ?  309 GLY   B C     1 
ATOM   4801 O  O     . GLY   B 1 309 ? -4.502  -14.432 14.106  1.00 33.07  ?  309 GLY   B O     1 
ATOM   4802 N  N     . ALA   B 1 310 ? -2.917  -15.144 15.520  1.00 29.69  ?  310 ALA   B N     1 
ATOM   4803 C  CA    . ALA   B 1 310 ? -1.799  -14.774 14.683  1.00 28.40  ?  310 ALA   B CA    1 
ATOM   4804 C  C     . ALA   B 1 310 ? -1.825  -15.576 13.394  1.00 31.76  ?  310 ALA   B C     1 
ATOM   4805 O  O     . ALA   B 1 310 ? -1.486  -15.064 12.345  1.00 30.76  ?  310 ALA   B O     1 
ATOM   4806 C  CB    . ALA   B 1 310 ? -0.476  -14.973 15.427  1.00 29.58  ?  310 ALA   B CB    1 
ATOM   4807 N  N     . GLU   B 1 311 ? -2.231  -16.848 13.492  1.00 36.49  ?  311 GLU   B N     1 
ATOM   4808 C  CA    . GLU   B 1 311 ? -2.370  -17.697 12.330  1.00 39.27  ?  311 GLU   B CA    1 
ATOM   4809 C  C     . GLU   B 1 311 ? -3.396  -17.148 11.350  1.00 37.63  ?  311 GLU   B C     1 
ATOM   4810 O  O     . GLU   B 1 311 ? -3.129  -17.103 10.151  1.00 37.18  ?  311 GLU   B O     1 
ATOM   4811 C  CB    . GLU   B 1 311 ? -2.729  -19.137 12.734  1.00 45.03  ?  311 GLU   B CB    1 
ATOM   4812 C  CG    . GLU   B 1 311 ? -3.138  -20.013 11.555  1.00 51.31  ?  311 GLU   B CG    1 
ATOM   4813 C  CD    . GLU   B 1 311 ? -3.264  -21.492 11.890  1.00 57.37  ?  311 GLU   B CD    1 
ATOM   4814 O  OE1   . GLU   B 1 311 ? -3.248  -21.855 13.093  1.00 57.99  ?  311 GLU   B OE1   1 
ATOM   4815 O  OE2   . GLU   B 1 311 ? -3.397  -22.284 10.929  1.00 61.90  ?  311 GLU   B OE2   1 
ATOM   4816 N  N     . LYS   B 1 312 ? -4.572  -16.767 11.860  1.00 36.18  ?  312 LYS   B N     1 
ATOM   4817 C  CA    . LYS   B 1 312 ? -5.642  -16.237 11.030  1.00 36.45  ?  312 LYS   B CA    1 
ATOM   4818 C  C     . LYS   B 1 312 ? -5.215  -14.919 10.376  1.00 35.36  ?  312 LYS   B C     1 
ATOM   4819 O  O     . LYS   B 1 312 ? -5.353  -14.746 9.174   1.00 38.93  ?  312 LYS   B O     1 
ATOM   4820 C  CB    . LYS   B 1 312 ? -6.922  -16.049 11.844  1.00 38.36  ?  312 LYS   B CB    1 
ATOM   4821 C  CG    . LYS   B 1 312 ? -7.529  -17.343 12.406  1.00 40.34  ?  312 LYS   B CG    1 
ATOM   4822 C  CD    . LYS   B 1 312 ? -8.726  -17.055 13.300  1.00 43.96  ?  312 LYS   B CD    1 
ATOM   4823 C  CE    . LYS   B 1 312 ? -9.337  -18.319 13.872  1.00 47.43  ?  312 LYS   B CE    1 
ATOM   4824 N  NZ    . LYS   B 1 312 ? -9.984  -18.071 15.202  1.00 47.72  ?  312 LYS   B NZ    1 
ATOM   4825 N  N     . ALA   B 1 313 ? -4.662  -14.009 11.173  1.00 34.75  ?  313 ALA   B N     1 
ATOM   4826 C  CA    . ALA   B 1 313 ? -4.204  -12.707 10.665  1.00 33.65  ?  313 ALA   B CA    1 
ATOM   4827 C  C     . ALA   B 1 313 ? -3.128  -12.862 9.595   1.00 32.89  ?  313 ALA   B C     1 
ATOM   4828 O  O     . ALA   B 1 313 ? -3.227  -12.256 8.549   1.00 33.61  ?  313 ALA   B O     1 
ATOM   4829 C  CB    . ALA   B 1 313 ? -3.722  -11.824 11.804  1.00 33.54  ?  313 ALA   B CB    1 
ATOM   4830 N  N     . SER   B 1 314 ? -2.147  -13.736 9.834   1.00 36.40  ?  314 SER   B N     1 
ATOM   4831 C  CA    . SER   B 1 314 ? -1.059  -13.988 8.882   1.00 36.05  ?  314 SER   B CA    1 
ATOM   4832 C  C     . SER   B 1 314 ? -1.558  -14.478 7.511   1.00 38.73  ?  314 SER   B C     1 
ATOM   4833 O  O     . SER   B 1 314 ? -0.936  -14.200 6.499   1.00 34.95  ?  314 SER   B O     1 
ATOM   4834 C  CB    . SER   B 1 314 ? -0.070  -15.020 9.428   1.00 38.33  ?  314 SER   B CB    1 
ATOM   4835 O  OG    . SER   B 1 314 ? 0.594   -14.524 10.563  1.00 44.73  ?  314 SER   B OG    1 
ATOM   4836 N  N     . ALA   B 1 315 ? -2.652  -15.238 7.498   1.00 43.82  ?  315 ALA   B N     1 
ATOM   4837 C  CA    . ALA   B 1 315 ? -3.259  -15.713 6.257   1.00 47.04  ?  315 ALA   B CA    1 
ATOM   4838 C  C     . ALA   B 1 315 ? -3.795  -14.542 5.422   1.00 44.65  ?  315 ALA   B C     1 
ATOM   4839 O  O     . ALA   B 1 315 ? -3.553  -14.463 4.226   1.00 51.08  ?  315 ALA   B O     1 
ATOM   4840 C  CB    . ALA   B 1 315 ? -4.361  -16.714 6.570   1.00 49.30  ?  315 ALA   B CB    1 
ATOM   4841 N  N     . HIS   B 1 316 ? -4.501  -13.620 6.061   1.00 42.60  ?  316 HIS   B N     1 
ATOM   4842 C  CA    . HIS   B 1 316 ? -4.950  -12.384 5.401   1.00 41.78  ?  316 HIS   B CA    1 
ATOM   4843 C  C     . HIS   B 1 316 ? -3.742  -11.520 4.997   1.00 38.16  ?  316 HIS   B C     1 
ATOM   4844 O  O     . HIS   B 1 316 ? -3.584  -11.176 3.824   1.00 35.77  ?  316 HIS   B O     1 
ATOM   4845 C  CB    . HIS   B 1 316 ? -5.868  -11.578 6.312   1.00 41.77  ?  316 HIS   B CB    1 
ATOM   4846 C  CG    . HIS   B 1 316 ? -7.237  -12.166 6.493   1.00 48.60  ?  316 HIS   B CG    1 
ATOM   4847 N  ND1   . HIS   B 1 316 ? -8.270  -11.922 5.614   1.00 51.02  ?  316 HIS   B ND1   1 
ATOM   4848 C  CD2   . HIS   B 1 316 ? -7.757  -12.940 7.480   1.00 51.71  ?  316 HIS   B CD2   1 
ATOM   4849 C  CE1   . HIS   B 1 316 ? -9.357  -12.549 6.031   1.00 53.86  ?  316 HIS   B CE1   1 
ATOM   4850 N  NE2   . HIS   B 1 316 ? -9.076  -13.167 7.166   1.00 53.86  ?  316 HIS   B NE2   1 
ATOM   4851 N  N     . ALA   B 1 317 ? -2.884  -11.227 5.977   1.00 34.23  ?  317 ALA   B N     1 
ATOM   4852 C  CA    . ALA   B 1 317 ? -1.773  -10.272 5.835   1.00 32.74  ?  317 ALA   B CA    1 
ATOM   4853 C  C     . ALA   B 1 317 ? -0.816  -10.625 4.716   1.00 30.50  ?  317 ALA   B C     1 
ATOM   4854 O  O     . ALA   B 1 317 ? -0.496  -9.759  3.915   1.00 29.65  ?  317 ALA   B O     1 
ATOM   4855 C  CB    . ALA   B 1 317 ? -1.023  -10.120 7.142   1.00 31.61  ?  317 ALA   B CB    1 
ATOM   4856 N  N     . SER   B 1 318 ? -0.400  -11.891 4.666   1.00 30.28  ?  318 SER   B N     1 
ATOM   4857 C  CA    . SER   B 1 318 ? 0.535   -12.383 3.666   1.00 33.09  ?  318 SER   B CA    1 
ATOM   4858 C  C     . SER   B 1 318 ? -0.021  -12.237 2.251   1.00 31.88  ?  318 SER   B C     1 
ATOM   4859 O  O     . SER   B 1 318 ? 0.736   -11.913 1.339   1.00 34.48  ?  318 SER   B O     1 
ATOM   4860 C  CB    . SER   B 1 318 ? 0.935   -13.861 3.921   1.00 32.85  ?  318 SER   B CB    1 
ATOM   4861 O  OG    . SER   B 1 318 ? -0.198  -14.700 3.828   1.00 38.47  ?  318 SER   B OG    1 
ATOM   4862 N  N     . ARG   B 1 319 ? -1.331  -12.478 2.086   1.00 32.30  ?  319 ARG   B N     1 
ATOM   4863 C  CA    . ARG   B 1 319 ? -2.013  -12.347 0.779   1.00 34.72  ?  319 ARG   B CA    1 
ATOM   4864 C  C     . ARG   B 1 319 ? -1.929  -10.917 0.237   1.00 35.12  ?  319 ARG   B C     1 
ATOM   4865 O  O     . ARG   B 1 319 ? -1.566  -10.716 -0.933  1.00 37.91  ?  319 ARG   B O     1 
ATOM   4866 C  CB    . ARG   B 1 319 ? -3.490  -12.776 0.868   1.00 37.69  ?  319 ARG   B CB    1 
ATOM   4867 N  N     . THR   B 1 320 ? -2.228  -9.941  1.097   1.00 33.20  ?  320 THR   B N     1 
ATOM   4868 C  CA    . THR   B 1 320 ? -2.111  -8.518  0.751   1.00 34.69  ?  320 THR   B CA    1 
ATOM   4869 C  C     . THR   B 1 320 ? -0.658  -8.111  0.447   1.00 35.08  ?  320 THR   B C     1 
ATOM   4870 O  O     . THR   B 1 320 ? -0.409  -7.461  -0.564  1.00 34.64  ?  320 THR   B O     1 
ATOM   4871 C  CB    . THR   B 1 320 ? -2.699  -7.634  1.857   1.00 33.96  ?  320 THR   B CB    1 
ATOM   4872 O  OG1   . THR   B 1 320 ? -4.097  -7.890  1.957   1.00 34.77  ?  320 THR   B OG1   1 
ATOM   4873 C  CG2   . THR   B 1 320 ? -2.529  -6.141  1.599   1.00 35.53  ?  320 THR   B CG2   1 
ATOM   4874 N  N     . LEU   B 1 321 ? 0.294   -8.485  1.304   1.00 35.42  ?  321 LEU   B N     1 
ATOM   4875 C  CA    . LEU   B 1 321 ? 1.712   -8.103  1.101   1.00 32.94  ?  321 LEU   B CA    1 
ATOM   4876 C  C     . LEU   B 1 321 ? 2.298   -8.685  -0.191  1.00 29.91  ?  321 LEU   B C     1 
ATOM   4877 O  O     . LEU   B 1 321 ? 3.079   -8.053  -0.847  1.00 32.37  ?  321 LEU   B O     1 
ATOM   4878 C  CB    . LEU   B 1 321 ? 2.581   -8.507  2.291   1.00 32.08  ?  321 LEU   B CB    1 
ATOM   4879 C  CG    . LEU   B 1 321 ? 4.020   -7.954  2.307   1.00 30.30  ?  321 LEU   B CG    1 
ATOM   4880 C  CD1   . LEU   B 1 321 ? 4.028   -6.505  2.750   1.00 31.63  ?  321 LEU   B CD1   1 
ATOM   4881 C  CD2   . LEU   B 1 321 ? 4.951   -8.780  3.187   1.00 27.94  ?  321 LEU   B CD2   1 
ATOM   4882 N  N     . LYS   B 1 322 ? 1.952   -9.918  -0.509  1.00 36.19  ?  322 LYS   B N     1 
ATOM   4883 C  CA    . LYS   B 1 322 ? 2.388   -10.564 -1.761  1.00 38.13  ?  322 LYS   B CA    1 
ATOM   4884 C  C     . LYS   B 1 322 ? 2.004   -9.730  -3.024  1.00 36.27  ?  322 LYS   B C     1 
ATOM   4885 O  O     . LYS   B 1 322 ? 2.790   -9.582  -3.958  1.00 35.49  ?  322 LYS   B O     1 
ATOM   4886 C  CB    . LYS   B 1 322 ? 1.815   -11.996 -1.835  1.00 40.71  ?  322 LYS   B CB    1 
ATOM   4887 C  CG    . LYS   B 1 322 ? 2.036   -12.691 -3.172  1.00 49.04  ?  322 LYS   B CG    1 
ATOM   4888 C  CD    . LYS   B 1 322 ? 1.955   -14.217 -3.092  1.00 52.91  ?  322 LYS   B CD    1 
ATOM   4889 C  CE    . LYS   B 1 322 ? 2.565   -14.860 -4.332  1.00 57.10  ?  322 LYS   B CE    1 
ATOM   4890 N  NZ    . LYS   B 1 322 ? 1.803   -16.065 -4.763  1.00 61.57  ?  322 LYS   B NZ    1 
ATOM   4891 N  N     . ALA   B 1 323 ? 0.792   -9.195  -3.025  1.00 37.66  ?  323 ALA   B N     1 
ATOM   4892 C  CA    . ALA   B 1 323 ? 0.301   -8.350  -4.111  1.00 40.52  ?  323 ALA   B CA    1 
ATOM   4893 C  C     . ALA   B 1 323 ? 0.949   -6.967  -4.109  1.00 39.43  ?  323 ALA   B C     1 
ATOM   4894 O  O     . ALA   B 1 323 ? 1.215   -6.417  -5.173  1.00 33.38  ?  323 ALA   B O     1 
ATOM   4895 C  CB    . ALA   B 1 323 ? -1.221  -8.211  -4.046  1.00 42.91  ?  323 ALA   B CB    1 
ATOM   4896 N  N     . VAL   B 1 324 ? 1.192   -6.408  -2.921  1.00 37.72  ?  324 VAL   B N     1 
ATOM   4897 C  CA    . VAL   B 1 324 ? 1.952   -5.142  -2.796  1.00 37.11  ?  324 VAL   B CA    1 
ATOM   4898 C  C     . VAL   B 1 324 ? 3.360   -5.313  -3.409  1.00 37.71  ?  324 VAL   B C     1 
ATOM   4899 O  O     . VAL   B 1 324 ? 3.798   -4.498  -4.222  1.00 34.64  ?  324 VAL   B O     1 
ATOM   4900 C  CB    . VAL   B 1 324 ? 2.084   -4.671  -1.324  1.00 36.60  ?  324 VAL   B CB    1 
ATOM   4901 C  CG1   . VAL   B 1 324 ? 3.022   -3.459  -1.195  1.00 34.56  ?  324 VAL   B CG1   1 
ATOM   4902 C  CG2   . VAL   B 1 324 ? 0.723   -4.313  -0.746  1.00 37.93  ?  324 VAL   B CG2   1 
ATOM   4903 N  N     . TYR   B 1 325 ? 4.043   -6.389  -3.016  1.00 37.23  ?  325 TYR   B N     1 
ATOM   4904 C  CA    . TYR   B 1 325 ? 5.412   -6.668  -3.477  1.00 40.99  ?  325 TYR   B CA    1 
ATOM   4905 C  C     . TYR   B 1 325 ? 5.460   -6.926  -5.001  1.00 44.35  ?  325 TYR   B C     1 
ATOM   4906 O  O     . TYR   B 1 325 ? 6.382   -6.489  -5.676  1.00 41.66  ?  325 TYR   B O     1 
ATOM   4907 C  CB    . TYR   B 1 325 ? 6.029   -7.827  -2.669  1.00 39.78  ?  325 TYR   B CB    1 
ATOM   4908 C  CG    . TYR   B 1 325 ? 6.628   -7.431  -1.313  1.00 34.48  ?  325 TYR   B CG    1 
ATOM   4909 C  CD1   . TYR   B 1 325 ? 6.434   -6.152  -0.761  1.00 33.22  ?  325 TYR   B CD1   1 
ATOM   4910 C  CD2   . TYR   B 1 325 ? 7.385   -8.339  -0.587  1.00 34.03  ?  325 TYR   B CD2   1 
ATOM   4911 C  CE1   . TYR   B 1 325 ? 6.999   -5.799  0.461   1.00 32.10  ?  325 TYR   B CE1   1 
ATOM   4912 C  CE2   . TYR   B 1 325 ? 7.936   -8.004  0.660   1.00 30.57  ?  325 TYR   B CE2   1 
ATOM   4913 C  CZ    . TYR   B 1 325 ? 7.749   -6.725  1.165   1.00 30.69  ?  325 TYR   B CZ    1 
ATOM   4914 O  OH    . TYR   B 1 325 ? 8.298   -6.343  2.370   1.00 28.61  ?  325 TYR   B OH    1 
ATOM   4915 N  N     . GLU   B 1 326 ? 4.451   -7.623  -5.522  1.00 47.90  ?  326 GLU   B N     1 
ATOM   4916 C  CA    . GLU   B 1 326 ? 4.311   -7.839  -6.958  1.00 48.45  ?  326 GLU   B CA    1 
ATOM   4917 C  C     . GLU   B 1 326 ? 4.146   -6.499  -7.677  1.00 44.94  ?  326 GLU   B C     1 
ATOM   4918 O  O     . GLU   B 1 326 ? 4.872   -6.223  -8.618  1.00 42.91  ?  326 GLU   B O     1 
ATOM   4919 C  CB    . GLU   B 1 326 ? 3.137   -8.779  -7.254  1.00 54.62  ?  326 GLU   B CB    1 
ATOM   4920 C  CG    . GLU   B 1 326 ? 2.928   -9.120  -8.735  1.00 60.49  ?  326 GLU   B CG    1 
ATOM   4921 C  CD    . GLU   B 1 326 ? 4.175   -9.705  -9.398  1.00 65.72  ?  326 GLU   B CD    1 
ATOM   4922 O  OE1   . GLU   B 1 326 ? 4.764   -10.678 -8.848  1.00 68.98  ?  326 GLU   B OE1   1 
ATOM   4923 O  OE2   . GLU   B 1 326 ? 4.569   -9.193  -10.477 1.00 72.42  ?  326 GLU   B OE2   1 
ATOM   4924 N  N     . ALA   B 1 327 ? 3.233   -5.670  -7.182  1.00 42.26  ?  327 ALA   B N     1 
ATOM   4925 C  CA    . ALA   B 1 327 ? 2.961   -4.339  -7.756  1.00 43.43  ?  327 ALA   B CA    1 
ATOM   4926 C  C     . ALA   B 1 327 ? 4.190   -3.424  -7.811  1.00 45.11  ?  327 ALA   B C     1 
ATOM   4927 O  O     . ALA   B 1 327 ? 4.453   -2.792  -8.833  1.00 49.05  ?  327 ALA   B O     1 
ATOM   4928 C  CB    . ALA   B 1 327 ? 1.848   -3.657  -6.994  1.00 38.56  ?  327 ALA   B CB    1 
ATOM   4929 N  N     . ILE   B 1 328 ? 4.942   -3.352  -6.718  1.00 46.76  ?  328 ILE   B N     1 
ATOM   4930 C  CA    . ILE   B 1 328 ? 6.053   -2.380  -6.615  1.00 46.68  ?  328 ILE   B CA    1 
ATOM   4931 C  C     . ILE   B 1 328 ? 7.299   -2.862  -7.349  1.00 43.73  ?  328 ILE   B C     1 
ATOM   4932 O  O     . ILE   B 1 328 ? 8.189   -2.066  -7.626  1.00 48.16  ?  328 ILE   B O     1 
ATOM   4933 C  CB    . ILE   B 1 328 ? 6.393   -1.985  -5.156  1.00 48.61  ?  328 ILE   B CB    1 
ATOM   4934 C  CG1   . ILE   B 1 328 ? 6.885   -3.193  -4.334  1.00 51.66  ?  328 ILE   B CG1   1 
ATOM   4935 C  CG2   . ILE   B 1 328 ? 5.182   -1.325  -4.516  1.00 50.44  ?  328 ILE   B CG2   1 
ATOM   4936 C  CD1   . ILE   B 1 328 ? 7.448   -2.834  -2.974  1.00 52.57  ?  328 ILE   B CD1   1 
ATOM   4937 N  N     . GLY   B 1 329 ? 7.356   -4.159  -7.640  1.00 41.22  ?  329 GLY   B N     1 
ATOM   4938 C  CA    . GLY   B 1 329 ? 8.371   -4.735  -8.524  1.00 42.95  ?  329 GLY   B CA    1 
ATOM   4939 C  C     . GLY   B 1 329 ? 9.458   -5.544  -7.852  1.00 41.22  ?  329 GLY   B C     1 
ATOM   4940 O  O     . GLY   B 1 329 ? 10.535  -5.668  -8.406  1.00 40.74  ?  329 GLY   B O     1 
ATOM   4941 N  N     . PHE   B 1 330 ? 9.193   -6.069  -6.644  1.00 39.40  ?  330 PHE   B N     1 
ATOM   4942 C  CA    . PHE   B 1 330 ? 10.150  -6.924  -5.951  1.00 36.96  ?  330 PHE   B CA    1 
ATOM   4943 C  C     . PHE   B 1 330 ? 10.125  -8.314  -6.584  1.00 33.05  ?  330 PHE   B C     1 
ATOM   4944 O  O     . PHE   B 1 330 ? 9.085   -8.769  -7.055  1.00 36.14  ?  330 PHE   B O     1 
ATOM   4945 C  CB    . PHE   B 1 330 ? 9.839   -7.015  -4.433  1.00 35.85  ?  330 PHE   B CB    1 
ATOM   4946 C  CG    . PHE   B 1 330 ? 10.162  -5.770  -3.636  1.00 34.48  ?  330 PHE   B CG    1 
ATOM   4947 C  CD1   . PHE   B 1 330 ? 9.824   -5.705  -2.281  1.00 39.44  ?  330 PHE   B CD1   1 
ATOM   4948 C  CD2   . PHE   B 1 330 ? 10.779  -4.670  -4.197  1.00 36.66  ?  330 PHE   B CD2   1 
ATOM   4949 C  CE1   . PHE   B 1 330 ? 10.119  -4.587  -1.516  1.00 34.04  ?  330 PHE   B CE1   1 
ATOM   4950 C  CE2   . PHE   B 1 330 ? 11.063  -3.546  -3.442  1.00 34.65  ?  330 PHE   B CE2   1 
ATOM   4951 C  CZ    . PHE   B 1 330 ? 10.738  -3.504  -2.103  1.00 35.78  ?  330 PHE   B CZ    1 
ATOM   4952 N  N     . VAL   B 1 331 ? 11.274  -8.978  -6.607  1.00 32.58  ?  331 VAL   B N     1 
ATOM   4953 C  CA    . VAL   B 1 331 ? 11.351  -10.405 -6.963  1.00 32.47  ?  331 VAL   B CA    1 
ATOM   4954 C  C     . VAL   B 1 331 ? 10.662  -11.165 -5.852  1.00 37.33  ?  331 VAL   B C     1 
ATOM   4955 O  O     . VAL   B 1 331 ? 11.009  -10.986 -4.694  1.00 34.70  ?  331 VAL   B O     1 
ATOM   4956 C  CB    . VAL   B 1 331 ? 12.796  -10.893 -7.133  1.00 32.52  ?  331 VAL   B CB    1 
ATOM   4957 C  CG1   . VAL   B 1 331 ? 12.895  -12.423 -7.118  1.00 33.45  ?  331 VAL   B CG1   1 
ATOM   4958 C  CG2   . VAL   B 1 331 ? 13.387  -10.369 -8.437  1.00 35.72  ?  331 VAL   B CG2   1 
ATOM   4959 N  N     . ALA   B 1 332 ? 9.700   -12.016 -6.211  1.00 42.17  ?  332 ALA   B N     1 
ATOM   4960 C  CA    . ALA   B 1 332 ? 8.873   -12.749 -5.245  1.00 42.70  ?  332 ALA   B CA    1 
ATOM   4961 C  C     . ALA   B 1 332 ? 9.698   -13.832 -4.585  1.00 42.31  ?  332 ALA   B C     1 
ATOM   4962 O  O     . ALA   B 1 332 ? 10.439  -14.517 -5.262  1.00 43.26  ?  332 ALA   B O     1 
ATOM   4963 C  CB    . ALA   B 1 332 ? 7.640   -13.344 -5.935  1.00 44.15  ?  332 ALA   B CB    1 
ATOM   4964 N  N     . LYS   B 1 333 ? 9.575   -13.954 -3.258  1.00 43.26  ?  333 LYS   B N     1 
ATOM   4965 C  CA    . LYS   B 1 333 ? 10.241  -15.006 -2.471  1.00 48.05  ?  333 LYS   B CA    1 
ATOM   4966 C  C     . LYS   B 1 333 ? 9.659   -16.366 -2.828  1.00 52.91  ?  333 LYS   B C     1 
ATOM   4967 O  O     . LYS   B 1 333 ? 8.473   -16.461 -3.115  1.00 56.81  ?  333 LYS   B O     1 
ATOM   4968 C  CB    . LYS   B 1 333 ? 10.036  -14.735 -0.970  1.00 48.64  ?  333 LYS   B CB    1 
ATOM   4969 C  CG    . LYS   B 1 333 ? 10.581  -15.796 -0.021  1.00 49.86  ?  333 LYS   B CG    1 
ATOM   4970 C  CD    . LYS   B 1 333 ? 10.423  -15.386 1.446   1.00 51.67  ?  333 LYS   B CD    1 
ATOM   4971 C  CE    . LYS   B 1 333 ? 10.846  -16.498 2.411   1.00 50.94  ?  333 LYS   B CE    1 
ATOM   4972 N  NZ    . LYS   B 1 333 ? 12.165  -16.222 3.050   1.00 50.38  ?  333 LYS   B NZ    1 
ATOM   4973 N  N     . ARG   B 1 334 ? 10.475  -17.415 -2.797  1.00 62.62  ?  334 ARG   B N     1 
ATOM   4974 C  CA    . ARG   B 1 334 ? 9.982   -18.785 -3.041  1.00 67.12  ?  334 ARG   B CA    1 
ATOM   4975 C  C     . ARG   B 1 334 ? 9.946   -19.589 -1.752  1.00 69.04  ?  334 ARG   B C     1 
ATOM   4976 O  O     . ARG   B 1 334 ? 10.993  -19.895 -1.179  1.00 70.24  ?  334 ARG   B O     1 
ATOM   4977 C  CB    . ARG   B 1 334 ? 10.854  -19.495 -4.078  1.00 71.83  ?  334 ARG   B CB    1 
HETATM 4978 N  N1    . A1EK0 C 2 .   ? 17.513  6.040   -0.596  1.00 41.99  ?  401 A1EK0 A N1    1 
HETATM 4979 C  C2    . A1EK0 C 2 .   ? 17.939  7.258   -0.947  1.00 41.46  ?  401 A1EK0 A C2    1 
HETATM 4980 N  N3    . A1EK0 C 2 .   ? 19.159  7.785   -0.813  1.00 40.69  ?  401 A1EK0 A N3    1 
HETATM 4981 C  C4    . A1EK0 C 2 .   ? 20.029  6.922   -0.271  1.00 43.63  ?  401 A1EK0 A C4    1 
HETATM 4982 C  C7    . A1EK0 C 2 .   ? 23.223  8.106   -1.472  1.00 50.41  ?  401 A1EK0 A C7    1 
HETATM 4983 C  C8    . A1EK0 C 2 .   ? 24.021  9.404   -1.410  1.00 51.68  ?  401 A1EK0 A C8    1 
HETATM 4984 C  C10   . A1EK0 C 2 .   ? 24.667  10.821  0.608   1.00 58.07  ?  401 A1EK0 A C10   1 
HETATM 4985 C  C12   . A1EK0 C 2 .   ? 24.155  11.332  1.861   1.00 53.88  ?  401 A1EK0 A C12   1 
HETATM 4986 C  C13   . A1EK0 C 2 .   ? 23.627  11.721  2.852   1.00 57.16  ?  401 A1EK0 A C13   1 
HETATM 4987 C  C14   . A1EK0 C 2 .   ? 23.060  12.102  4.143   1.00 58.64  ?  401 A1EK0 A C14   1 
HETATM 4988 C  C15   . A1EK0 C 2 .   ? 22.934  8.972   0.709   1.00 50.91  ?  401 A1EK0 A C15   1 
HETATM 4989 C  C16   . A1EK0 C 2 .   ? 21.946  5.983   0.494   1.00 44.71  ?  401 A1EK0 A C16   1 
HETATM 4990 C  C19   . A1EK0 C 2 .   ? 21.157  3.650   0.899   1.00 40.56  ?  401 A1EK0 A C19   1 
HETATM 4991 C  C20   . A1EK0 C 2 .   ? 21.681  3.296   2.138   1.00 40.30  ?  401 A1EK0 A C20   1 
HETATM 4992 C  C21   . A1EK0 C 2 .   ? 21.988  1.971   2.411   1.00 40.08  ?  401 A1EK0 A C21   1 
HETATM 4993 C  C22   . A1EK0 C 2 .   ? 21.770  0.995   1.442   1.00 37.98  ?  401 A1EK0 A C22   1 
HETATM 4994 C  C24   . A1EK0 C 2 .   ? 23.009  -0.732  2.606   1.00 39.19  ?  401 A1EK0 A C24   1 
HETATM 4995 C  C25   . A1EK0 C 2 .   ? 24.356  -0.495  2.365   1.00 36.69  ?  401 A1EK0 A C25   1 
HETATM 4996 C  C26   . A1EK0 C 2 .   ? 25.293  -0.870  3.314   1.00 36.40  ?  401 A1EK0 A C26   1 
HETATM 4997 C  C27   . A1EK0 C 2 .   ? 24.894  -1.474  4.491   1.00 37.14  ?  401 A1EK0 A C27   1 
HETATM 4998 C  C28   . A1EK0 C 2 .   ? 23.548  -1.707  4.724   1.00 37.48  ?  401 A1EK0 A C28   1 
HETATM 4999 C  C29   . A1EK0 C 2 .   ? 22.597  -1.338  3.786   1.00 35.09  ?  401 A1EK0 A C29   1 
HETATM 5000 C  C30   . A1EK0 C 2 .   ? 21.244  1.344   0.206   1.00 38.82  ?  401 A1EK0 A C30   1 
HETATM 5001 C  C31   . A1EK0 C 2 .   ? 20.938  2.668   -0.064  1.00 41.58  ?  401 A1EK0 A C31   1 
HETATM 5002 C  C32   . A1EK0 C 2 .   ? 19.735  5.591   0.130   1.00 42.92  ?  401 A1EK0 A C32   1 
HETATM 5003 C  C33   . A1EK0 C 2 .   ? 18.395  5.177   -0.052  1.00 40.46  ?  401 A1EK0 A C33   1 
HETATM 5004 C  C6    . A1EK0 C 2 .   ? 22.138  8.339   -0.421  1.00 48.62  ?  401 A1EK0 A C6    1 
HETATM 5005 N  N18   . A1EK0 C 2 .   ? 20.927  5.030   0.577   1.00 43.13  ?  401 A1EK0 A N18   1 
HETATM 5006 N  N34   . A1EK0 C 2 .   ? 17.950  3.963   0.257   1.00 38.25  ?  401 A1EK0 A N34   1 
HETATM 5007 N  N5    . A1EK0 C 2 .   ? 21.379  7.128   -0.041  1.00 45.87  ?  401 A1EK0 A N5    1 
HETATM 5008 N  N9    . A1EK0 C 2 .   ? 23.923  9.792   -0.000  1.00 53.91  ?  401 A1EK0 A N9    1 
HETATM 5009 O  O11   . A1EK0 C 2 .   ? 25.698  11.270  0.116   1.00 63.09  ?  401 A1EK0 A O11   1 
HETATM 5010 O  O17   . A1EK0 C 2 .   ? 23.099  5.819   0.855   1.00 43.08  ?  401 A1EK0 A O17   1 
HETATM 5011 O  O23   . A1EK0 C 2 .   ? 22.074  -0.355  1.638   1.00 40.87  ?  401 A1EK0 A O23   1 
HETATM 5012 S  S     . SO4   D 3 .   ? 47.624  10.248  -31.690 1.00 38.17  ?  402 SO4   A S     1 
HETATM 5013 O  O1    . SO4   D 3 .   ? 48.675  11.330  -31.822 1.00 39.21  ?  402 SO4   A O1    1 
HETATM 5014 O  O2    . SO4   D 3 .   ? 46.596  10.380  -32.717 1.00 34.95  ?  402 SO4   A O2    1 
HETATM 5015 O  O3    . SO4   D 3 .   ? 48.327  8.906   -31.796 1.00 36.95  ?  402 SO4   A O3    1 
HETATM 5016 O  O4    . SO4   D 3 .   ? 46.976  10.403  -30.326 1.00 35.27  ?  402 SO4   A O4    1 
HETATM 5017 S  S     . SO4   E 3 .   ? 30.383  4.276   -7.125  1.00 37.54  ?  403 SO4   A S     1 
HETATM 5018 O  O1    . SO4   E 3 .   ? 31.749  4.828   -6.892  1.00 37.28  ?  403 SO4   A O1    1 
HETATM 5019 O  O2    . SO4   E 3 .   ? 30.216  3.837   -8.544  1.00 36.59  ?  403 SO4   A O2    1 
HETATM 5020 O  O3    . SO4   E 3 .   ? 30.202  3.134   -6.137  1.00 37.10  ?  403 SO4   A O3    1 
HETATM 5021 O  O4    . SO4   E 3 .   ? 29.329  5.311   -6.931  1.00 39.16  ?  403 SO4   A O4    1 
HETATM 5022 C  C1    . CLW   F 4 .   ? 11.035  -0.499  9.112   1.00 33.96  ?  401 CLW   B C1    1 
HETATM 5023 C  C2    . CLW   F 4 .   ? 9.670   -0.740  9.202   1.00 33.63  ?  401 CLW   B C2    1 
HETATM 5024 C  C3    . CLW   F 4 .   ? 8.815   0.339   9.231   1.00 32.51  ?  401 CLW   B C3    1 
HETATM 5025 C  C4    . CLW   F 4 .   ? 9.289   1.634   9.174   1.00 36.03  ?  401 CLW   B C4    1 
HETATM 5026 C  C5    . CLW   F 4 .   ? 10.648  1.890   9.087   1.00 35.37  ?  401 CLW   B C5    1 
HETATM 5027 C  C6    . CLW   F 4 .   ? 11.497  0.805   9.059   1.00 33.22  ?  401 CLW   B C6    1 
HETATM 5028 CL CL1   . CLW   F 4 .   ? 13.201  1.088   8.974   1.00 40.76  ?  401 CLW   B CL1   1 
HETATM 5029 O  O1    . CLW   F 4 .   ? 7.439   0.363   9.301   1.00 35.54  ?  401 CLW   B O1    1 
HETATM 5030 C  C7    . CLW   F 4 .   ? 7.056   1.689   9.286   1.00 33.07  ?  401 CLW   B C7    1 
HETATM 5031 N  N1    . CLW   F 4 .   ? 8.169   2.446   9.211   1.00 37.25  ?  401 CLW   B N1    1 
HETATM 5032 O  O2    . CLW   F 4 .   ? 5.902   2.015   9.309   1.00 30.94  ?  401 CLW   B O2    1 
HETATM 5033 P  P     . TYM   G 5 .   ? -4.865  3.721   22.265  1.00 56.37  ?  402 TYM   B P     1 
HETATM 5034 O  O1P   . TYM   G 5 .   ? -4.114  4.900   22.749  1.00 51.57  ?  402 TYM   B O1P   1 
HETATM 5035 O  O2P   . TYM   G 5 .   ? -4.690  2.442   22.990  1.00 51.27  -1 402 TYM   B O2P   1 
HETATM 5036 O  "O5'" . TYM   G 5 .   ? -6.430  4.093   22.271  1.00 53.39  ?  402 TYM   B "O5'" 1 
HETATM 5037 C  "C5'" . TYM   G 5 .   ? -7.431  3.041   22.309  1.00 52.80  ?  402 TYM   B "C5'" 1 
HETATM 5038 C  "C4'" . TYM   G 5 .   ? -8.730  3.501   21.685  1.00 52.77  ?  402 TYM   B "C4'" 1 
HETATM 5039 O  "O4'" . TYM   G 5 .   ? -9.474  4.320   22.614  1.00 50.82  ?  402 TYM   B "O4'" 1 
HETATM 5040 C  "C1'" . TYM   G 5 .   ? -9.759  5.583   22.040  1.00 53.14  ?  402 TYM   B "C1'" 1 
HETATM 5041 N  N9    . TYM   G 5 .   ? -9.702  6.597   23.093  1.00 57.32  ?  402 TYM   B N9    1 
HETATM 5042 C  C4    . TYM   G 5 .   ? -10.752 7.310   23.618  1.00 56.59  ?  402 TYM   B C4    1 
HETATM 5043 N  N3    . TYM   G 5 .   ? -12.037 7.276   23.234  1.00 58.97  ?  402 TYM   B N3    1 
HETATM 5044 C  C2    . TYM   G 5 .   ? -12.785 8.094   23.981  1.00 56.82  ?  402 TYM   B C2    1 
HETATM 5045 N  N1    . TYM   G 5 .   ? -12.409 8.888   24.991  1.00 56.36  ?  402 TYM   B N1    1 
HETATM 5046 C  C6    . TYM   G 5 .   ? -11.105 8.906   25.357  1.00 58.29  ?  402 TYM   B C6    1 
HETATM 5047 N  N6    . TYM   G 5 .   ? -10.748 9.662   26.410  1.00 57.01  ?  402 TYM   B N6    1 
HETATM 5048 C  C5    . TYM   G 5 .   ? -10.212 8.082   24.639  1.00 58.40  ?  402 TYM   B C5    1 
HETATM 5049 N  N7    . TYM   G 5 .   ? -8.846  7.863   24.748  1.00 55.15  ?  402 TYM   B N7    1 
HETATM 5050 C  C8    . TYM   G 5 .   ? -8.598  6.978   23.813  1.00 59.31  ?  402 TYM   B C8    1 
HETATM 5051 C  "C2'" . TYM   G 5 .   ? -8.746  5.772   20.918  1.00 53.11  ?  402 TYM   B "C2'" 1 
HETATM 5052 O  "O2'" . TYM   G 5 .   ? -9.292  6.611   19.910  1.00 56.05  ?  402 TYM   B "O2'" 1 
HETATM 5053 C  "C3'" . TYM   G 5 .   ? -8.586  4.331   20.410  1.00 53.19  ?  402 TYM   B "C3'" 1 
HETATM 5054 O  "O3'" . TYM   G 5 .   ? -9.548  3.944   19.433  1.00 51.80  ?  402 TYM   B "O3'" 1 
HETATM 5055 N  NH3   . TYM   G 5 .   ? -3.128  4.503   17.608  1.00 48.87  ?  402 TYM   B NH3   1 
HETATM 5056 C  CA    . TYM   G 5 .   ? -4.216  3.769   18.317  1.00 47.24  ?  402 TYM   B CA    1 
HETATM 5057 C  CB    . TYM   G 5 .   ? -3.966  2.261   18.286  1.00 45.35  ?  402 TYM   B CB    1 
HETATM 5058 C  CG    . TYM   G 5 .   ? -3.796  1.707   16.903  1.00 40.55  ?  402 TYM   B CG    1 
HETATM 5059 C  CD2   . TYM   G 5 .   ? -4.836  1.431   15.953  1.00 38.72  ?  402 TYM   B CD2   1 
HETATM 5060 C  CE2   . TYM   G 5 .   ? -4.219  0.900   14.806  1.00 40.64  ?  402 TYM   B CE2   1 
HETATM 5061 C  CE3   . TYM   G 5 .   ? -6.212  1.624   15.936  1.00 37.56  ?  402 TYM   B CE3   1 
HETATM 5062 C  CD1   . TYM   G 5 .   ? -2.627  1.345   16.304  1.00 40.91  ?  402 TYM   B CD1   1 
HETATM 5063 N  NE1   . TYM   G 5 .   ? -2.870  0.857   15.047  1.00 42.78  ?  402 TYM   B NE1   1 
HETATM 5064 C  CZ2   . TYM   G 5 .   ? -4.946  0.569   13.669  1.00 37.70  ?  402 TYM   B CZ2   1 
HETATM 5065 C  CZ3   . TYM   G 5 .   ? -6.944  1.294   14.802  1.00 40.58  ?  402 TYM   B CZ3   1 
HETATM 5066 C  CH2   . TYM   G 5 .   ? -6.317  0.772   13.681  1.00 39.34  ?  402 TYM   B CH2   1 
HETATM 5067 C  C     . TYM   G 5 .   ? -4.333  4.320   19.727  1.00 48.61  ?  402 TYM   B C     1 
HETATM 5068 O  O     . TYM   G 5 .   ? -4.314  5.488   19.989  1.00 53.32  ?  402 TYM   B O     1 
HETATM 5069 O  OPP   . TYM   G 5 .   ? -4.475  3.389   20.709  1.00 54.46  ?  402 TYM   B OPP   1 
HETATM 5070 S  S     . SO4   H 3 .   ? -3.008  8.710   26.414  1.00 37.00  ?  403 SO4   B S     1 
HETATM 5071 O  O1    . SO4   H 3 .   ? -2.430  8.431   25.068  1.00 33.74  ?  403 SO4   B O1    1 
HETATM 5072 O  O2    . SO4   H 3 .   ? -4.442  8.194   26.488  1.00 35.45  ?  403 SO4   B O2    1 
HETATM 5073 O  O3    . SO4   H 3 .   ? -2.196  8.145   27.543  1.00 34.39  ?  403 SO4   B O3    1 
HETATM 5074 O  O4    . SO4   H 3 .   ? -3.041  10.246  26.672  1.00 37.16  ?  403 SO4   B O4    1 
HETATM 5075 O  O     . HOH   I 6 .   ? 29.449  3.597   0.519   1.00 50.62  ?  501 HOH   A O     1 
HETATM 5076 O  O     . HOH   I 6 .   ? 10.163  -12.751 11.486  1.00 34.90  ?  502 HOH   A O     1 
HETATM 5077 O  O     . HOH   I 6 .   ? 30.070  -8.295  2.259   1.00 38.09  ?  503 HOH   A O     1 
HETATM 5078 O  O     . HOH   I 6 .   ? 53.608  16.256  -32.607 1.00 40.72  ?  504 HOH   A O     1 
HETATM 5079 O  O     . HOH   I 6 .   ? 55.487  8.323   -24.665 1.00 47.87  ?  505 HOH   A O     1 
HETATM 5080 O  O     . HOH   I 6 .   ? 32.619  3.052   -10.232 1.00 55.03  ?  506 HOH   A O     1 
HETATM 5081 O  O     . HOH   I 6 .   ? 10.463  -7.327  -15.067 1.00 47.09  ?  507 HOH   A O     1 
HETATM 5082 O  O     . HOH   I 6 .   ? 24.726  -16.484 6.644   1.00 51.32  ?  508 HOH   A O     1 
HETATM 5083 O  O     . HOH   I 6 .   ? 9.832   -11.876 23.261  1.00 37.82  ?  509 HOH   A O     1 
HETATM 5084 O  O     . HOH   I 6 .   ? 22.223  -10.876 20.661  1.00 36.83  ?  510 HOH   A O     1 
HETATM 5085 O  O     . HOH   I 6 .   ? 12.153  -9.040  28.932  1.00 36.31  ?  511 HOH   A O     1 
HETATM 5086 O  O     . HOH   I 6 .   ? 26.526  -2.601  -6.084  1.00 45.34  ?  512 HOH   A O     1 
HETATM 5087 O  O     . HOH   I 6 .   ? 37.376  -11.430 -16.373 1.00 53.48  ?  513 HOH   A O     1 
HETATM 5088 O  O     . HOH   I 6 .   ? 12.324  -7.202  5.094   1.00 24.14  ?  514 HOH   A O     1 
HETATM 5089 O  O     . HOH   I 6 .   ? 15.794  -23.846 -8.613  1.00 53.52  ?  515 HOH   A O     1 
HETATM 5090 O  O     . HOH   I 6 .   ? 49.812  15.922  -26.623 1.00 42.74  ?  516 HOH   A O     1 
HETATM 5091 O  O     . HOH   I 6 .   ? 8.566   3.739   -5.115  1.00 48.54  ?  517 HOH   A O     1 
HETATM 5092 O  O     . HOH   I 6 .   ? 15.203  -6.043  28.993  1.00 35.68  ?  518 HOH   A O     1 
HETATM 5093 O  O     . HOH   I 6 .   ? 9.924   -9.863  -2.240  1.00 32.03  ?  519 HOH   A O     1 
HETATM 5094 O  O     . HOH   I 6 .   ? 21.359  -8.046  -18.868 1.00 48.04  ?  520 HOH   A O     1 
HETATM 5095 O  O     . HOH   I 6 .   ? 13.577  -6.934  -5.816  1.00 33.17  ?  521 HOH   A O     1 
HETATM 5096 O  O     . HOH   I 6 .   ? 37.097  -11.237 -9.603  1.00 53.85  ?  522 HOH   A O     1 
HETATM 5097 O  O     . HOH   I 6 .   ? 57.181  16.250  -24.294 1.00 36.06  ?  523 HOH   A O     1 
HETATM 5098 O  O     . HOH   I 6 .   ? 25.952  -9.228  20.495  1.00 35.79  ?  524 HOH   A O     1 
HETATM 5099 O  O     . HOH   I 6 .   ? 8.524   -17.479 19.976  1.00 42.50  ?  525 HOH   A O     1 
HETATM 5100 O  O     . HOH   I 6 .   ? 10.245  -8.087  3.417   1.00 24.10  ?  526 HOH   A O     1 
HETATM 5101 O  O     . HOH   I 6 .   ? 9.781   -14.996 25.781  1.00 41.37  ?  527 HOH   A O     1 
HETATM 5102 O  O     . HOH   I 6 .   ? 33.579  -11.281 0.035   1.00 36.61  ?  528 HOH   A O     1 
HETATM 5103 O  O     . HOH   I 6 .   ? 32.668  -23.292 -2.767  1.00 51.93  ?  529 HOH   A O     1 
HETATM 5104 O  O     . HOH   I 6 .   ? 17.244  4.472   -3.332  1.00 45.82  ?  530 HOH   A O     1 
HETATM 5105 O  O     . HOH   I 6 .   ? 17.012  -14.162 -1.410  1.00 33.20  ?  531 HOH   A O     1 
HETATM 5106 O  O     . HOH   I 6 .   ? 9.500   -4.174  15.425  1.00 28.68  ?  532 HOH   A O     1 
HETATM 5107 O  O     . HOH   I 6 .   ? 26.822  0.600   24.821  1.00 35.26  ?  533 HOH   A O     1 
HETATM 5108 O  O     . HOH   I 6 .   ? 7.161   -8.063  14.133  1.00 27.24  ?  534 HOH   A O     1 
HETATM 5109 O  O     . HOH   I 6 .   ? 17.971  -15.522 20.170  1.00 39.54  ?  535 HOH   A O     1 
HETATM 5110 O  O     . HOH   I 6 .   ? 42.421  -8.518  -19.983 1.00 56.77  ?  536 HOH   A O     1 
HETATM 5111 O  O     . HOH   I 6 .   ? 33.361  -2.314  17.402  1.00 34.24  ?  537 HOH   A O     1 
HETATM 5112 O  O     . HOH   I 6 .   ? 4.614   -16.321 24.377  1.00 31.31  ?  538 HOH   A O     1 
HETATM 5113 O  O     . HOH   I 6 .   ? 58.039  -3.535  -11.786 1.00 46.17  ?  539 HOH   A O     1 
HETATM 5114 O  O     . HOH   I 6 .   ? 11.233  -1.833  26.524  1.00 40.85  ?  540 HOH   A O     1 
HETATM 5115 O  O     . HOH   I 6 .   ? 21.557  5.150   -2.700  1.00 52.55  ?  541 HOH   A O     1 
HETATM 5116 O  O     . HOH   I 6 .   ? 56.965  6.765   -22.246 1.00 59.10  ?  542 HOH   A O     1 
HETATM 5117 O  O     . HOH   I 6 .   ? 7.053   -13.958 25.898  1.00 32.38  ?  543 HOH   A O     1 
HETATM 5118 O  O     . HOH   I 6 .   ? 28.693  -5.239  21.677  1.00 40.36  ?  544 HOH   A O     1 
HETATM 5119 O  O     . HOH   I 6 .   ? 53.338  0.125   -10.447 1.00 43.98  ?  545 HOH   A O     1 
HETATM 5120 O  O     . HOH   I 6 .   ? 44.708  10.626  -13.089 1.00 38.77  ?  546 HOH   A O     1 
HETATM 5121 O  O     . HOH   I 6 .   ? 17.302  -10.554 24.973  1.00 28.20  ?  547 HOH   A O     1 
HETATM 5122 O  O     . HOH   I 6 .   ? 27.271  -16.949 -21.849 1.00 50.21  ?  548 HOH   A O     1 
HETATM 5123 O  O     . HOH   I 6 .   ? 11.507  -12.850 21.372  1.00 32.61  ?  549 HOH   A O     1 
HETATM 5124 O  O     . HOH   I 6 .   ? 26.610  -5.056  13.978  1.00 25.39  ?  550 HOH   A O     1 
HETATM 5125 O  O     . HOH   I 6 .   ? 7.996   -7.860  -14.072 1.00 47.47  ?  551 HOH   A O     1 
HETATM 5126 O  O     . HOH   I 6 .   ? 44.678  15.540  -18.595 1.00 46.09  ?  552 HOH   A O     1 
HETATM 5127 O  O     . HOH   I 6 .   ? 23.711  9.755   15.964  1.00 42.92  ?  553 HOH   A O     1 
HETATM 5128 O  O     . HOH   I 6 .   ? 46.175  0.494   -11.012 1.00 47.93  ?  554 HOH   A O     1 
HETATM 5129 O  O     . HOH   I 6 .   ? 17.562  -7.069  28.176  1.00 35.99  ?  555 HOH   A O     1 
HETATM 5130 O  O     . HOH   I 6 .   ? 27.563  -1.890  0.865   1.00 34.34  ?  556 HOH   A O     1 
HETATM 5131 O  O     . HOH   I 6 .   ? 24.094  -17.382 -0.308  1.00 43.92  ?  557 HOH   A O     1 
HETATM 5132 O  O     . HOH   I 6 .   ? 24.958  -6.362  15.694  1.00 31.35  ?  558 HOH   A O     1 
HETATM 5133 O  O     . HOH   I 6 .   ? 41.667  -1.430  -29.669 1.00 56.90  ?  559 HOH   A O     1 
HETATM 5134 O  O     . HOH   I 6 .   ? 37.849  0.974   13.011  1.00 50.92  ?  560 HOH   A O     1 
HETATM 5135 O  O     . HOH   I 6 .   ? 25.069  6.099   21.288  1.00 36.26  ?  561 HOH   A O     1 
HETATM 5136 O  O     . HOH   I 6 .   ? 36.585  -2.266  -0.469  1.00 56.95  ?  562 HOH   A O     1 
HETATM 5137 O  O     . HOH   I 6 .   ? 19.822  -24.557 -13.582 1.00 51.46  ?  563 HOH   A O     1 
HETATM 5138 O  O     . HOH   I 6 .   ? 29.987  -11.561 15.121  1.00 35.37  ?  564 HOH   A O     1 
HETATM 5139 O  O     . HOH   I 6 .   ? 12.231  -15.143 22.704  1.00 45.10  ?  565 HOH   A O     1 
HETATM 5140 O  O     . HOH   I 6 .   ? 46.567  5.025   -8.757  1.00 62.27  ?  566 HOH   A O     1 
HETATM 5141 O  O     . HOH   I 6 .   ? 14.163  -16.642 -1.792  1.00 43.06  ?  567 HOH   A O     1 
HETATM 5142 O  O     . HOH   I 6 .   ? 16.316  -20.661 8.168   1.00 51.79  ?  568 HOH   A O     1 
HETATM 5143 O  O     . HOH   I 6 .   ? 14.392  -12.400 -16.121 1.00 46.16  ?  569 HOH   A O     1 
HETATM 5144 O  O     . HOH   I 6 .   ? 0.716   -21.589 22.033  1.00 51.42  ?  570 HOH   A O     1 
HETATM 5145 O  O     . HOH   I 6 .   ? 29.934  -17.785 -8.296  1.00 38.68  ?  571 HOH   A O     1 
HETATM 5146 O  O     . HOH   I 6 .   ? 7.618   -12.716 18.620  1.00 28.26  ?  572 HOH   A O     1 
HETATM 5147 O  O     . HOH   I 6 .   ? 22.633  -19.664 8.881   1.00 52.94  ?  573 HOH   A O     1 
HETATM 5148 O  O     . HOH   I 6 .   ? 6.240   -1.700  -14.559 1.00 45.74  ?  574 HOH   A O     1 
HETATM 5149 O  O     . HOH   I 6 .   ? 42.298  16.037  -24.131 1.00 49.97  ?  575 HOH   A O     1 
HETATM 5150 O  O     . HOH   I 6 .   ? 30.785  -4.657  20.005  1.00 36.24  ?  576 HOH   A O     1 
HETATM 5151 O  O     . HOH   I 6 .   ? 48.586  -3.562  -10.731 1.00 42.28  ?  577 HOH   A O     1 
HETATM 5152 O  O     . HOH   I 6 .   ? 49.549  11.533  -28.912 1.00 37.86  ?  578 HOH   A O     1 
HETATM 5153 O  O     . HOH   I 6 .   ? 27.865  -1.561  23.194  1.00 39.60  ?  579 HOH   A O     1 
HETATM 5154 O  O     . HOH   I 6 .   ? 34.464  5.232   18.623  1.00 49.97  ?  580 HOH   A O     1 
HETATM 5155 O  O     . HOH   I 6 .   ? 25.502  -0.474  -4.642  1.00 41.14  ?  581 HOH   A O     1 
HETATM 5156 O  O     . HOH   I 6 .   ? 16.730  -9.594  27.491  1.00 38.50  ?  582 HOH   A O     1 
HETATM 5157 O  O     . HOH   I 6 .   ? 2.849   -15.814 26.683  1.00 36.09  ?  583 HOH   A O     1 
HETATM 5158 O  O     . HOH   I 6 .   ? 9.230   -16.206 16.071  1.00 53.21  ?  584 HOH   A O     1 
HETATM 5159 O  O     . HOH   I 6 .   ? 6.643   -17.015 26.272  1.00 42.95  ?  585 HOH   A O     1 
HETATM 5160 O  O     . HOH   I 6 .   ? 20.549  -14.903 21.225  1.00 37.09  ?  586 HOH   A O     1 
HETATM 5161 O  O     . HOH   I 6 .   ? 48.431  14.028  -28.300 1.00 32.97  ?  587 HOH   A O     1 
HETATM 5162 O  O     . HOH   I 6 .   ? 32.907  -6.589  18.726  1.00 37.30  ?  588 HOH   A O     1 
HETATM 5163 O  O     . HOH   I 6 .   ? 17.551  -13.064 24.731  1.00 42.70  ?  589 HOH   A O     1 
HETATM 5164 O  O     . HOH   I 6 .   ? 38.131  3.677   11.977  1.00 48.65  ?  590 HOH   A O     1 
HETATM 5165 O  O     . HOH   I 6 .   ? 40.709  15.721  -26.574 1.00 55.91  ?  591 HOH   A O     1 
HETATM 5166 O  O     . HOH   J 6 .   ? -8.449  -9.695  4.386   1.00 38.69  ?  501 HOH   B O     1 
HETATM 5167 O  O     . HOH   J 6 .   ? -8.199  -0.698  4.053   1.00 30.66  ?  502 HOH   B O     1 
HETATM 5168 O  O     . HOH   J 6 .   ? 3.319   -1.151  29.010  1.00 38.99  ?  503 HOH   B O     1 
HETATM 5169 O  O     . HOH   J 6 .   ? -5.246  10.966  15.024  1.00 53.19  ?  504 HOH   B O     1 
HETATM 5170 O  O     . HOH   J 6 .   ? 10.779  4.206   22.916  1.00 43.83  ?  505 HOH   B O     1 
HETATM 5171 O  O     . HOH   J 6 .   ? -8.256  -4.871  -2.792  1.00 41.23  ?  506 HOH   B O     1 
HETATM 5172 O  O     . HOH   J 6 .   ? -25.882 25.903  45.532  1.00 44.73  ?  507 HOH   B O     1 
HETATM 5173 O  O     . HOH   J 6 .   ? -23.627 -1.579  11.319  1.00 33.65  ?  508 HOH   B O     1 
HETATM 5174 O  O     . HOH   J 6 .   ? -4.514  13.214  8.358   1.00 58.48  ?  509 HOH   B O     1 
HETATM 5175 O  O     . HOH   J 6 .   ? 6.951   -10.347 19.842  1.00 31.67  ?  510 HOH   B O     1 
HETATM 5176 O  O     . HOH   J 6 .   ? -31.397 19.768  36.958  1.00 47.02  ?  511 HOH   B O     1 
HETATM 5177 O  O     . HOH   J 6 .   ? 5.100   19.682  20.603  1.00 57.20  ?  512 HOH   B O     1 
HETATM 5178 O  O     . HOH   J 6 .   ? -14.735 -13.479 25.505  1.00 42.09  ?  513 HOH   B O     1 
HETATM 5179 O  O     . HOH   J 6 .   ? -26.103 -0.932  30.958  1.00 57.77  ?  514 HOH   B O     1 
HETATM 5180 O  O     . HOH   J 6 .   ? -9.287  -13.604 10.243  1.00 37.67  ?  515 HOH   B O     1 
HETATM 5181 O  O     . HOH   J 6 .   ? -2.308  -12.010 -3.176  1.00 41.71  ?  516 HOH   B O     1 
HETATM 5182 O  O     . HOH   J 6 .   ? -16.973 4.172   47.259  1.00 59.64  ?  517 HOH   B O     1 
HETATM 5183 O  O     . HOH   J 6 .   ? -25.504 -8.708  15.268  1.00 52.77  ?  518 HOH   B O     1 
HETATM 5184 O  O     . HOH   J 6 .   ? -16.234 -11.365 13.685  1.00 37.93  ?  519 HOH   B O     1 
HETATM 5185 O  O     . HOH   J 6 .   ? -15.454 19.804  27.441  1.00 66.21  ?  520 HOH   B O     1 
HETATM 5186 O  O     . HOH   J 6 .   ? 14.076  -17.614 4.377   1.00 37.86  ?  521 HOH   B O     1 
HETATM 5187 O  O     . HOH   J 6 .   ? -19.591 -11.662 22.747  1.00 44.39  ?  522 HOH   B O     1 
HETATM 5188 O  O     . HOH   J 6 .   ? 5.044   -11.059 -4.315  1.00 37.20  ?  523 HOH   B O     1 
HETATM 5189 O  O     . HOH   J 6 .   ? -23.679 28.226  43.092  1.00 41.25  ?  524 HOH   B O     1 
HETATM 5190 O  O     . HOH   J 6 .   ? -2.879  13.072  15.758  1.00 64.36  ?  525 HOH   B O     1 
HETATM 5191 O  O     . HOH   J 6 .   ? 8.964   -3.726  2.712   1.00 29.05  ?  526 HOH   B O     1 
HETATM 5192 O  O     . HOH   J 6 .   ? -22.355 29.705  37.157  1.00 44.65  ?  527 HOH   B O     1 
HETATM 5193 O  O     . HOH   J 6 .   ? 1.322   17.218  25.758  1.00 53.32  ?  528 HOH   B O     1 
HETATM 5194 O  O     . HOH   J 6 .   ? -15.150 -7.929  40.347  1.00 49.59  ?  529 HOH   B O     1 
HETATM 5195 O  O     . HOH   J 6 .   ? -22.694 -8.017  15.450  1.00 39.48  ?  530 HOH   B O     1 
HETATM 5196 O  O     . HOH   J 6 .   ? -23.318 -6.895  21.873  1.00 45.32  ?  531 HOH   B O     1 
HETATM 5197 O  O     . HOH   J 6 .   ? -5.066  5.375   -12.184 1.00 46.37  ?  532 HOH   B O     1 
HETATM 5198 O  O     . HOH   J 6 .   ? -6.643  -2.562  2.312   1.00 34.20  ?  533 HOH   B O     1 
HETATM 5199 O  O     . HOH   J 6 .   ? -12.738 -6.342  2.229   1.00 34.64  ?  534 HOH   B O     1 
HETATM 5200 O  O     . HOH   J 6 .   ? 5.189   -6.817  12.710  1.00 22.86  ?  535 HOH   B O     1 
HETATM 5201 O  O     . HOH   J 6 .   ? 0.225   -23.166 25.516  1.00 47.15  ?  536 HOH   B O     1 
HETATM 5202 O  O     . HOH   J 6 .   ? -11.103 10.678  21.693  1.00 48.00  ?  537 HOH   B O     1 
HETATM 5203 O  O     . HOH   J 6 .   ? -30.761 29.499  44.928  1.00 51.22  ?  538 HOH   B O     1 
HETATM 5204 O  O     . HOH   J 6 .   ? 3.267   -3.167  -11.310 1.00 47.72  ?  539 HOH   B O     1 
HETATM 5205 O  O     . HOH   J 6 .   ? -28.818 21.009  26.839  1.00 57.94  ?  540 HOH   B O     1 
HETATM 5206 O  O     . HOH   J 6 .   ? -11.994 17.331  43.271  1.00 46.94  ?  541 HOH   B O     1 
HETATM 5207 O  O     . HOH   J 6 .   ? 3.378   11.823  13.020  1.00 41.68  ?  542 HOH   B O     1 
HETATM 5208 O  O     . HOH   J 6 .   ? 14.864  6.977   21.678  1.00 50.11  ?  543 HOH   B O     1 
HETATM 5209 O  O     . HOH   J 6 .   ? -26.949 -4.695  14.472  1.00 39.23  ?  544 HOH   B O     1 
HETATM 5210 O  O     . HOH   J 6 .   ? -23.665 24.710  41.333  1.00 43.54  ?  545 HOH   B O     1 
HETATM 5211 O  O     . HOH   J 6 .   ? -7.545  -16.217 8.259   1.00 42.51  ?  546 HOH   B O     1 
HETATM 5212 O  O     . HOH   J 6 .   ? -18.412 -12.151 11.497  1.00 43.41  ?  547 HOH   B O     1 
HETATM 5213 O  O     . HOH   J 6 .   ? -32.445 23.405  40.030  1.00 46.33  ?  548 HOH   B O     1 
HETATM 5214 O  O     . HOH   J 6 .   ? -15.525 3.114   17.698  1.00 49.58  ?  549 HOH   B O     1 
HETATM 5215 O  O     . HOH   J 6 .   ? -17.879 -7.835  1.545   1.00 47.23  ?  550 HOH   B O     1 
HETATM 5216 O  O     . HOH   J 6 .   ? 4.176   -13.345 4.105   1.00 36.76  ?  551 HOH   B O     1 
HETATM 5217 O  O     . HOH   J 6 .   ? -1.083  -13.031 18.564  1.00 26.31  ?  552 HOH   B O     1 
HETATM 5218 O  O     . HOH   J 6 .   ? 0.900   -13.768 32.723  1.00 43.03  ?  553 HOH   B O     1 
HETATM 5219 O  O     . HOH   J 6 .   ? -1.432  -23.208 22.833  1.00 45.88  ?  554 HOH   B O     1 
HETATM 5220 O  O     . HOH   J 6 .   ? -29.302 28.064  36.999  1.00 47.32  ?  555 HOH   B O     1 
HETATM 5221 O  O     . HOH   J 6 .   ? 8.790   6.771   29.069  1.00 49.54  ?  556 HOH   B O     1 
HETATM 5222 O  O     . HOH   J 6 .   ? -32.377 18.647  34.738  1.00 44.99  ?  557 HOH   B O     1 
HETATM 5223 O  O     . HOH   J 6 .   ? 9.370   -12.143 -9.145  1.00 42.34  ?  558 HOH   B O     1 
HETATM 5224 O  O     . HOH   J 6 .   ? 13.966  -7.877  30.556  1.00 41.34  ?  559 HOH   B O     1 
HETATM 5225 O  O     . HOH   J 6 .   ? 8.629   -11.958 -1.275  1.00 40.42  ?  560 HOH   B O     1 
HETATM 5226 O  O     . HOH   J 6 .   ? 6.537   -10.143 -6.381  1.00 41.77  ?  561 HOH   B O     1 
HETATM 5227 O  O     . HOH   J 6 .   ? -16.526 -13.869 8.453   1.00 50.38  ?  562 HOH   B O     1 
HETATM 5228 O  O     . HOH   J 6 .   ? -3.481  -5.082  35.266  1.00 55.42  ?  563 HOH   B O     1 
HETATM 5229 O  O     . HOH   J 6 .   ? 10.226  0.744   24.984  1.00 46.36  ?  564 HOH   B O     1 
HETATM 5230 O  O     . HOH   J 6 .   ? 6.105   -14.638 -2.691  1.00 42.63  ?  565 HOH   B O     1 
HETATM 5231 O  O     . HOH   J 6 .   ? -30.992 31.738  38.388  1.00 47.00  ?  566 HOH   B O     1 
HETATM 5232 O  O     . HOH   J 6 .   ? -25.420 31.046  38.200  1.00 54.19  ?  567 HOH   B O     1 
HETATM 5233 O  O     . HOH   J 6 .   ? -11.903 0.630   -1.951  1.00 47.52  ?  568 HOH   B O     1 
HETATM 5234 O  O     . HOH   J 6 .   ? -17.528 12.035  24.229  1.00 53.89  ?  569 HOH   B O     1 
HETATM 5235 O  O     . HOH   J 6 .   ? -29.426 3.756   41.146  1.00 54.79  ?  570 HOH   B O     1 
HETATM 5236 O  O     . HOH   J 6 .   ? -8.840  -18.860 19.968  1.00 45.93  ?  571 HOH   B O     1 
HETATM 5237 O  O     . HOH   J 6 .   ? 16.693  6.548   23.399  1.00 49.78  ?  572 HOH   B O     1 
HETATM 5238 O  O     . HOH   J 6 .   ? 4.448   -17.859 28.064  1.00 38.55  ?  573 HOH   B O     1 
HETATM 5239 O  O     . HOH   J 6 .   ? -0.572  13.574  32.332  1.00 56.11  ?  574 HOH   B O     1 
HETATM 5240 O  O     . HOH   J 6 .   ? 7.455   -12.286 3.433   1.00 40.23  ?  575 HOH   B O     1 
HETATM 5241 O  O     . HOH   J 6 .   ? -2.357  -23.823 25.077  1.00 47.11  ?  576 HOH   B O     1 
HETATM 5242 O  O     . HOH   J 6 .   ? -2.008  12.820  29.969  1.00 58.53  ?  577 HOH   B O     1 
HETATM 5243 O  O     . HOH   J 6 .   ? -10.854 -20.040 34.447  1.00 44.58  ?  578 HOH   B O     1 
HETATM 5244 O  O     . HOH   J 6 .   ? -25.642 20.581  43.486  1.00 43.02  ?  579 HOH   B O     1 
HETATM 5245 O  O     . HOH   J 6 .   ? -10.054 -15.985 9.223   1.00 49.50  ?  580 HOH   B O     1 
HETATM 5246 O  O     . HOH   J 6 .   ? -17.229 -14.651 24.549  1.00 45.06  ?  581 HOH   B O     1 
HETATM 5247 O  O     . HOH   J 6 .   ? 2.579   -0.555  31.635  1.00 44.29  ?  582 HOH   B O     1 
HETATM 5248 O  O     . HOH   J 6 .   ? 6.204   -12.252 -2.378  1.00 37.01  ?  583 HOH   B O     1 
HETATM 5249 O  O     . HOH   J 6 .   ? -23.567 22.584  43.140  1.00 41.83  ?  584 HOH   B O     1 
HETATM 5250 O  O     . HOH   J 6 .   ? -13.896 -16.512 25.261  1.00 47.79  ?  585 HOH   B O     1 
HETATM 5251 O  O     . HOH   J 6 .   ? 8.219   -14.723 4.509   1.00 40.49  ?  586 HOH   B O     1 
HETATM 5252 O  O     . HOH   J 6 .   ? -32.024 27.594  36.704  1.00 56.92  ?  587 HOH   B O     1 
HETATM 5253 O  O     . HOH   J 6 .   ? 11.060  -13.701 -10.764 1.00 55.08  ?  588 HOH   B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LYS A 3   ? 0.6412 0.6589 0.7135 0.0083  0.0206  -0.0298 3   LYS A N   
2    C CA  . LYS A 3   ? 0.5684 0.5939 0.6371 0.0038  0.0196  -0.0310 3   LYS A CA  
3    C C   . LYS A 3   ? 0.4939 0.5178 0.5525 0.0061  0.0166  -0.0267 3   LYS A C   
4    O O   . LYS A 3   ? 0.4806 0.5056 0.5388 0.0086  0.0173  -0.0256 3   LYS A O   
5    C CB  . LYS A 3   ? 0.6145 0.6513 0.6916 -0.0003 0.0233  -0.0363 3   LYS A CB  
6    C CG  . LYS A 3   ? 0.6001 0.6454 0.6745 -0.0051 0.0226  -0.0380 3   LYS A CG  
7    C CD  . LYS A 3   ? 0.6314 0.6879 0.7144 -0.0092 0.0263  -0.0433 3   LYS A CD  
8    C CE  . LYS A 3   ? 0.6646 0.7234 0.7567 -0.0125 0.0290  -0.0478 3   LYS A CE  
9    N NZ  . LYS A 3   ? 0.6969 0.7672 0.7961 -0.0171 0.0322  -0.0529 3   LYS A NZ  
10   N N   . PRO A 4   ? 0.4291 0.4507 0.4796 0.0052  0.0132  -0.0241 4   PRO A N   
11   C CA  . PRO A 4   ? 0.3979 0.4176 0.4385 0.0075  0.0103  -0.0197 4   PRO A CA  
12   C C   . PRO A 4   ? 0.3802 0.4098 0.4208 0.0053  0.0115  -0.0214 4   PRO A C   
13   O O   . PRO A 4   ? 0.3678 0.4063 0.4129 0.0004  0.0132  -0.0255 4   PRO A O   
14   C CB  . PRO A 4   ? 0.4427 0.4590 0.4759 0.0062  0.0068  -0.0175 4   PRO A CB  
15   C CG  . PRO A 4   ? 0.4482 0.4605 0.4864 0.0052  0.0074  -0.0193 4   PRO A CG  
16   C CD  . PRO A 4   ? 0.4531 0.4721 0.5026 0.0028  0.0117  -0.0245 4   PRO A CD  
17   N N   . ILE A 5   ? 0.3144 0.3421 0.3499 0.0089  0.0105  -0.0181 5   ILE A N   
18   C CA  . ILE A 5   ? 0.3033 0.3393 0.3374 0.0075  0.0113  -0.0188 5   ILE A CA  
19   C C   . ILE A 5   ? 0.2971 0.3342 0.3217 0.0061  0.0081  -0.0162 5   ILE A C   
20   O O   . ILE A 5   ? 0.2791 0.3082 0.2952 0.0094  0.0048  -0.0114 5   ILE A O   
21   C CB  . ILE A 5   ? 0.3111 0.3445 0.3442 0.0122  0.0119  -0.0164 5   ILE A CB  
22   C CG1 . ILE A 5   ? 0.3128 0.3469 0.3564 0.0129  0.0156  -0.0198 5   ILE A CG1 
23   C CG2 . ILE A 5   ? 0.3041 0.3451 0.3340 0.0111  0.0121  -0.0163 5   ILE A CG2 
24   C CD1 . ILE A 5   ? 0.3123 0.3410 0.3552 0.0182  0.0159  -0.0170 5   ILE A CD1 
25   N N   . VAL A 6   ? 0.2868 0.3339 0.3131 0.0012  0.0090  -0.0195 6   VAL A N   
26   C CA  . VAL A 6   ? 0.3450 0.3945 0.3629 -0.0005 0.0063  -0.0175 6   VAL A CA  
27   C C   . VAL A 6   ? 0.3416 0.3982 0.3575 -0.0007 0.0070  -0.0173 6   VAL A C   
28   O O   . VAL A 6   ? 0.3669 0.4314 0.3900 -0.0027 0.0102  -0.0212 6   VAL A O   
29   C CB  . VAL A 6   ? 0.3965 0.4517 0.4173 -0.0060 0.0065  -0.0211 6   VAL A CB  
30   C CG1 . VAL A 6   ? 0.4268 0.4842 0.4390 -0.0078 0.0037  -0.0190 6   VAL A CG1 
31   C CG2 . VAL A 6   ? 0.3992 0.4474 0.4225 -0.0059 0.0060  -0.0213 6   VAL A CG2 
32   N N   . PHE A 7   ? 0.3262 0.3800 0.3323 0.0016  0.0042  -0.0129 7   PHE A N   
33   C CA  . PHE A 7   ? 0.3425 0.4030 0.3455 0.0015  0.0045  -0.0123 7   PHE A CA  
34   C C   . PHE A 7   ? 0.3396 0.4045 0.3356 -0.0013 0.0024  -0.0113 7   PHE A C   
35   O O   . PHE A 7   ? 0.3400 0.3986 0.3281 0.0000  -0.0008 -0.0076 7   PHE A O   
36   C CB  . PHE A 7   ? 0.3474 0.4009 0.3449 0.0072  0.0033  -0.0076 7   PHE A CB  
37   C CG  . PHE A 7   ? 0.3480 0.4081 0.3436 0.0074  0.0042  -0.0073 7   PHE A CG  
38   C CD1 . PHE A 7   ? 0.3545 0.4170 0.3413 0.0069  0.0019  -0.0046 7   PHE A CD1 
39   C CD2 . PHE A 7   ? 0.3132 0.3774 0.3158 0.0080  0.0073  -0.0097 7   PHE A CD2 
40   C CE1 . PHE A 7   ? 0.3527 0.4216 0.3379 0.0071  0.0028  -0.0043 7   PHE A CE1 
41   C CE2 . PHE A 7   ? 0.3119 0.3823 0.3127 0.0082  0.0082  -0.0095 7   PHE A CE2 
42   C CZ  . PHE A 7   ? 0.3005 0.3734 0.2928 0.0077  0.0059  -0.0068 7   PHE A CZ  
43   N N   . SER A 8   ? 0.3666 0.4424 0.3655 -0.0050 0.0042  -0.0146 8   SER A N   
44   C CA  . SER A 8   ? 0.3784 0.4603 0.3714 -0.0080 0.0027  -0.0142 8   SER A CA  
45   C C   . SER A 8   ? 0.3636 0.4527 0.3550 -0.0078 0.0037  -0.0140 8   SER A C   
46   O O   . SER A 8   ? 0.3531 0.4482 0.3519 -0.0087 0.0068  -0.0173 8   SER A O   
47   C CB  . SER A 8   ? 0.3851 0.4749 0.3843 -0.0137 0.0041  -0.0192 8   SER A CB  
48   O OG  . SER A 8   ? 0.4460 0.5300 0.4480 -0.0142 0.0036  -0.0199 8   SER A OG  
49   N N   . GLY A 9   ? 0.3970 0.4856 0.3789 -0.0067 0.0011  -0.0102 9   GLY A N   
50   C CA  . GLY A 9   ? 0.4005 0.4966 0.3796 -0.0071 0.0017  -0.0098 9   GLY A CA  
51   C C   . GLY A 9   ? 0.4496 0.5554 0.4282 -0.0121 0.0018  -0.0124 9   GLY A C   
52   O O   . GLY A 9   ? 0.5203 0.6242 0.4927 -0.0131 -0.0008 -0.0105 9   GLY A O   
53   N N   . ALA A 10  ? 0.4408 0.5572 0.4259 -0.0153 0.0047  -0.0166 10  ALA A N   
54   C CA  . ALA A 10  ? 0.4355 0.5622 0.4207 -0.0201 0.0051  -0.0193 10  ALA A CA  
55   C C   . ALA A 10  ? 0.4829 0.6159 0.4636 -0.0196 0.0053  -0.0179 10  ALA A C   
56   O O   . ALA A 10  ? 0.4286 0.5671 0.4143 -0.0196 0.0079  -0.0200 10  ALA A O   
57   C CB  . ALA A 10  ? 0.4146 0.5493 0.4109 -0.0244 0.0084  -0.0255 10  ALA A CB  
58   N N   . GLN A 11  ? 0.4812 0.6139 0.4527 -0.0193 0.0026  -0.0145 11  GLN A N   
59   C CA  . GLN A 11  ? 0.5344 0.6717 0.5002 -0.0183 0.0023  -0.0123 11  GLN A CA  
60   C C   . GLN A 11  ? 0.5970 0.7478 0.5683 -0.0229 0.0049  -0.0170 11  GLN A C   
61   O O   . GLN A 11  ? 0.5220 0.6780 0.4946 -0.0270 0.0048  -0.0195 11  GLN A O   
62   C CB  . GLN A 11  ? 0.5568 0.6897 0.5116 -0.0170 -0.0013 -0.0076 11  GLN A CB  
63   C CG  . GLN A 11  ? 0.5550 0.6745 0.5044 -0.0124 -0.0038 -0.0029 11  GLN A CG  
64   C CD  . GLN A 11  ? 0.6440 0.7582 0.5826 -0.0110 -0.0074 0.0019  11  GLN A CD  
65   O OE1 . GLN A 11  ? 0.6525 0.7583 0.5884 -0.0098 -0.0095 0.0038  11  GLN A OE1 
66   N NE2 . GLN A 11  ? 0.6726 0.7915 0.6047 -0.0110 -0.0081 0.0039  11  GLN A NE2 
67   N N   . PRO A 12  ? 0.6117 0.7681 0.5862 -0.0224 0.0073  -0.0183 12  PRO A N   
68   C CA  . PRO A 12  ? 0.6940 0.8632 0.6752 -0.0268 0.0101  -0.0234 12  PRO A CA  
69   C C   . PRO A 12  ? 0.7600 0.9365 0.7365 -0.0302 0.0090  -0.0235 12  PRO A C   
70   O O   . PRO A 12  ? 0.9298 1.1161 0.9120 -0.0347 0.0109  -0.0281 12  PRO A O   
71   C CB  . PRO A 12  ? 0.6365 0.8086 0.6188 -0.0246 0.0120  -0.0230 12  PRO A CB  
72   C CG  . PRO A 12  ? 0.6260 0.7883 0.5995 -0.0192 0.0094  -0.0170 12  PRO A CG  
73   C CD  . PRO A 12  ? 0.6423 0.7939 0.6142 -0.0176 0.0074  -0.0151 12  PRO A CD  
74   N N   . SER A 13  ? 0.7875 0.9593 0.7537 -0.0280 0.0059  -0.0186 13  SER A N   
75   C CA  . SER A 13  ? 0.8558 1.0336 0.8168 -0.0308 0.0045  -0.0182 13  SER A CA  
76   C C   . SER A 13  ? 0.9230 1.0976 0.8830 -0.0330 0.0027  -0.0186 13  SER A C   
77   O O   . SER A 13  ? 1.1001 1.2666 1.0621 -0.0318 0.0020  -0.0183 13  SER A O   
78   C CB  . SER A 13  ? 0.9030 1.0776 0.8533 -0.0273 0.0022  -0.0127 13  SER A CB  
79   O OG  . SER A 13  ? 0.9791 1.1603 0.9243 -0.0298 0.0012  -0.0123 13  SER A OG  
80   N N   . GLY A 14  ? 0.9272 1.1082 0.8840 -0.0361 0.0018  -0.0191 14  GLY A N   
81   C CA  . GLY A 14  ? 0.9586 1.1375 0.9142 -0.0385 0.0000  -0.0196 14  GLY A CA  
82   C C   . GLY A 14  ? 0.9566 1.1423 0.9223 -0.0433 0.0024  -0.0256 14  GLY A C   
83   O O   . GLY A 14  ? 0.9845 1.1697 0.9583 -0.0433 0.0046  -0.0284 14  GLY A O   
84   N N   . GLU A 15  ? 0.8581 1.0503 0.8235 -0.0473 0.0019  -0.0275 15  GLU A N   
85   C CA  . GLU A 15  ? 0.8052 1.0039 0.7796 -0.0520 0.0039  -0.0330 15  GLU A CA  
86   C C   . GLU A 15  ? 0.7666 0.9568 0.7414 -0.0520 0.0022  -0.0326 15  GLU A C   
87   O O   . GLU A 15  ? 0.7849 0.9702 0.7524 -0.0514 -0.0007 -0.0294 15  GLU A O   
88   C CB  . GLU A 15  ? 0.7934 1.0033 0.7674 -0.0563 0.0042  -0.0353 15  GLU A CB  
89   N N   . LEU A 16  ? 0.6892 0.8773 0.6724 -0.0526 0.0041  -0.0357 16  LEU A N   
90   C CA  . LEU A 16  ? 0.6307 0.8110 0.6154 -0.0527 0.0029  -0.0358 16  LEU A CA  
91   C C   . LEU A 16  ? 0.6084 0.7936 0.5934 -0.0572 0.0021  -0.0379 16  LEU A C   
92   O O   . LEU A 16  ? 0.6440 0.8398 0.6335 -0.0612 0.0039  -0.0418 16  LEU A O   
93   C CB  . LEU A 16  ? 0.6016 0.7807 0.5963 -0.0530 0.0056  -0.0393 16  LEU A CB  
94   C CG  . LEU A 16  ? 0.6209 0.7932 0.6161 -0.0484 0.0063  -0.0372 16  LEU A CG  
95   C CD1 . LEU A 16  ? 0.5838 0.7562 0.5895 -0.0494 0.0092  -0.0413 16  LEU A CD1 
96   C CD2 . LEU A 16  ? 0.6197 0.7795 0.6067 -0.0438 0.0031  -0.0317 16  LEU A CD2 
97   N N   . THR A 17  ? 0.5615 0.7388 0.5417 -0.0564 -0.0006 -0.0354 17  THR A N   
98   C CA  . THR A 17  ? 0.5527 0.7328 0.5327 -0.0602 -0.0017 -0.0370 17  THR A CA  
99   C C   . THR A 17  ? 0.5005 0.6774 0.4878 -0.0620 -0.0009 -0.0401 17  THR A C   
100  O O   . THR A 17  ? 0.4973 0.6680 0.4883 -0.0597 0.0000  -0.0400 17  THR A O   
101  C CB  . THR A 17  ? 0.5656 0.7394 0.5350 -0.0583 -0.0055 -0.0321 17  THR A CB  
102  O OG1 . THR A 17  ? 0.5793 0.7411 0.5465 -0.0554 -0.0073 -0.0294 17  THR A OG1 
103  C CG2 . THR A 17  ? 0.5695 0.7435 0.5307 -0.0553 -0.0066 -0.0280 17  THR A CG2 
104  N N   . ILE A 18  ? 0.4726 0.6538 0.4619 -0.0660 -0.0012 -0.0426 18  ILE A N   
105  C CA  . ILE A 18  ? 0.4469 0.6249 0.4420 -0.0681 -0.0008 -0.0452 18  ILE A CA  
106  C C   . ILE A 18  ? 0.3825 0.5474 0.3729 -0.0644 -0.0033 -0.0412 18  ILE A C   
107  O O   . ILE A 18  ? 0.4123 0.5726 0.4080 -0.0643 -0.0025 -0.0427 18  ILE A O   
108  C CB  . ILE A 18  ? 0.4134 0.5982 0.4100 -0.0730 -0.0012 -0.0480 18  ILE A CB  
109  C CG1 . ILE A 18  ? 0.4522 0.6342 0.4388 -0.0723 -0.0046 -0.0441 18  ILE A CG1 
110  C CG2 . ILE A 18  ? 0.4301 0.6278 0.4324 -0.0768 0.0016  -0.0524 18  ILE A CG2 
111  C CD1 . ILE A 18  ? 0.4863 0.6745 0.4739 -0.0769 -0.0052 -0.0466 18  ILE A CD1 
112  N N   . GLY A 19  ? 0.4238 0.5831 0.4044 -0.0614 -0.0063 -0.0362 19  GLY A N   
113  C CA  . GLY A 19  ? 0.4854 0.6319 0.4606 -0.0572 -0.0087 -0.0319 19  GLY A CA  
114  C C   . GLY A 19  ? 0.5094 0.6499 0.4875 -0.0534 -0.0074 -0.0310 19  GLY A C   
115  O O   . GLY A 19  ? 0.4881 0.6197 0.4669 -0.0513 -0.0081 -0.0299 19  GLY A O   
116  N N   . ASN A 20  ? 0.5456 0.6913 0.5255 -0.0525 -0.0054 -0.0317 20  ASN A N   
117  C CA  . ASN A 20  ? 0.5652 0.7069 0.5491 -0.0494 -0.0037 -0.0316 20  ASN A CA  
118  C C   . ASN A 20  ? 0.5434 0.6873 0.5383 -0.0518 -0.0008 -0.0365 20  ASN A C   
119  O O   . ASN A 20  ? 0.5376 0.6741 0.5352 -0.0493 -0.0005 -0.0359 20  ASN A O   
120  C CB  . ASN A 20  ? 0.5939 0.7412 0.5772 -0.0480 -0.0022 -0.0312 20  ASN A CB  
121  C CG  . ASN A 20  ? 0.6153 0.7606 0.5878 -0.0454 -0.0049 -0.0262 20  ASN A CG  
122  O OD1 . ASN A 20  ? 0.5944 0.7479 0.5652 -0.0467 -0.0043 -0.0267 20  ASN A OD1 
123  N ND2 . ASN A 20  ? 0.6210 0.7556 0.5862 -0.0417 -0.0077 -0.0215 20  ASN A ND2 
124  N N   . TYR A 21  ? 0.5570 0.7111 0.5581 -0.0566 0.0012  -0.0412 21  TYR A N   
125  C CA  . TYR A 21  ? 0.5941 0.7518 0.6063 -0.0592 0.0044  -0.0463 21  TYR A CA  
126  C C   . TYR A 21  ? 0.6195 0.7710 0.6342 -0.0601 0.0037  -0.0471 21  TYR A C   
127  O O   . TYR A 21  ? 0.6603 0.8066 0.6800 -0.0586 0.0049  -0.0478 21  TYR A O   
128  C CB  . TYR A 21  ? 0.6058 0.7764 0.6239 -0.0641 0.0069  -0.0512 21  TYR A CB  
129  C CG  . TYR A 21  ? 0.5844 0.7583 0.6135 -0.0671 0.0099  -0.0563 21  TYR A CG  
130  C CD1 . TYR A 21  ? 0.5552 0.7276 0.5907 -0.0654 0.0125  -0.0578 21  TYR A CD1 
131  C CD2 . TYR A 21  ? 0.6197 0.7976 0.6524 -0.0715 0.0101  -0.0595 21  TYR A CD2 
132  C CE1 . TYR A 21  ? 0.6143 0.7894 0.6596 -0.0680 0.0153  -0.0624 21  TYR A CE1 
133  C CE2 . TYR A 21  ? 0.6381 0.8186 0.6806 -0.0742 0.0128  -0.0641 21  TYR A CE2 
134  C CZ  . TYR A 21  ? 0.6155 0.7947 0.6643 -0.0724 0.0154  -0.0655 21  TYR A CZ  
135  O OH  . TYR A 21  ? 0.6883 0.8701 0.7468 -0.0750 0.0183  -0.0700 21  TYR A OH  
136  N N   . MET A 22  ? 0.5830 0.7355 0.5945 -0.0627 0.0018  -0.0470 22  MET A N   
137  C CA  . MET A 22  ? 0.6213 0.7687 0.6353 -0.0641 0.0010  -0.0480 22  MET A CA  
138  C C   . MET A 22  ? 0.6420 0.7769 0.6490 -0.0598 -0.0019 -0.0430 22  MET A C   
139  O O   . MET A 22  ? 0.6339 0.7624 0.6430 -0.0596 -0.0024 -0.0432 22  MET A O   
140  C CB  . MET A 22  ? 0.5496 0.7024 0.5625 -0.0685 -0.0001 -0.0496 22  MET A CB  
141  C CG  . MET A 22  ? 0.5908 0.7560 0.6059 -0.0723 0.0014  -0.0528 22  MET A CG  
142  S SD  . MET A 22  ? 0.5672 0.7361 0.5794 -0.0766 -0.0006 -0.0536 22  MET A SD  
143  C CE  . MET A 22  ? 0.6387 0.8028 0.6378 -0.0731 -0.0044 -0.0475 22  MET A CE  
144  N N   . GLY A 23  ? 0.6946 0.8259 0.6930 -0.0563 -0.0040 -0.0385 23  GLY A N   
145  C CA  . GLY A 23  ? 0.7175 0.8372 0.7085 -0.0522 -0.0069 -0.0336 23  GLY A CA  
146  C C   . GLY A 23  ? 0.7555 0.8675 0.7475 -0.0476 -0.0063 -0.0317 23  GLY A C   
147  O O   . GLY A 23  ? 0.8630 0.9649 0.8516 -0.0447 -0.0082 -0.0286 23  GLY A O   
148  N N   . ALA A 24  ? 0.7284 0.8450 0.7252 -0.0469 -0.0037 -0.0333 24  ALA A N   
149  C CA  . ALA A 24  ? 0.6553 0.7649 0.6526 -0.0423 -0.0030 -0.0312 24  ALA A CA  
150  C C   . ALA A 24  ? 0.6763 0.7908 0.6838 -0.0432 0.0008  -0.0354 24  ALA A C   
151  O O   . ALA A 24  ? 0.6304 0.7395 0.6427 -0.0417 0.0019  -0.0361 24  ALA A O   
152  C CB  . ALA A 24  ? 0.6694 0.7771 0.6585 -0.0387 -0.0047 -0.0268 24  ALA A CB  
153  N N   . LEU A 25  ? 0.6420 0.7840 0.5893 -0.0521 0.0129  -0.0468 25  LEU A N   
154  C CA  . LEU A 25  ? 0.5807 0.7203 0.5269 -0.0499 0.0136  -0.0489 25  LEU A CA  
155  C C   . LEU A 25  ? 0.5866 0.7302 0.5326 -0.0483 0.0152  -0.0543 25  LEU A C   
156  O O   . LEU A 25  ? 0.5975 0.7378 0.5437 -0.0443 0.0158  -0.0570 25  LEU A O   
157  C CB  . LEU A 25  ? 0.5851 0.7257 0.5293 -0.0536 0.0132  -0.0465 25  LEU A CB  
158  C CG  . LEU A 25  ? 0.5974 0.7331 0.5407 -0.0515 0.0132  -0.0465 25  LEU A CG  
159  C CD1 . LEU A 25  ? 0.6211 0.7494 0.5662 -0.0464 0.0129  -0.0461 25  LEU A CD1 
160  C CD2 . LEU A 25  ? 0.6037 0.7392 0.5460 -0.0554 0.0121  -0.0420 25  LEU A CD2 
161  N N   . ARG A 26  ? 0.6339 0.7846 0.5795 -0.0514 0.0159  -0.0558 26  ARG A N   
162  C CA  . ARG A 26  ? 0.6406 0.7959 0.5860 -0.0502 0.0177  -0.0608 26  ARG A CA  
163  C C   . ARG A 26  ? 0.5708 0.7242 0.5187 -0.0454 0.0180  -0.0634 26  ARG A C   
164  O O   . ARG A 26  ? 0.5465 0.6994 0.4945 -0.0422 0.0192  -0.0671 26  ARG A O   
165  C CB  . ARG A 26  ? 0.5999 0.7633 0.5448 -0.0544 0.0185  -0.0616 26  ARG A CB  
166  C CG  . ARG A 26  ? 0.6542 0.8224 0.5983 -0.0539 0.0208  -0.0664 26  ARG A CG  
167  C CD  . ARG A 26  ? 0.6241 0.8001 0.5670 -0.0586 0.0217  -0.0667 26  ARG A CD  
168  N NE  . ARG A 26  ? 0.6377 0.8172 0.5832 -0.0595 0.0211  -0.0655 26  ARG A NE  
169  C CZ  . ARG A 26  ? 0.6406 0.8266 0.5858 -0.0637 0.0214  -0.0647 26  ARG A CZ  
170  N NH1 . ARG A 26  ? 0.6468 0.8353 0.5945 -0.0643 0.0207  -0.0636 26  ARG A NH1 
171  N NH2 . ARG A 26  ? 0.6438 0.8335 0.5859 -0.0675 0.0225  -0.0651 26  ARG A NH2 
172  N N   . GLN A 27  ? 0.5764 0.7285 0.5261 -0.0451 0.0167  -0.0612 27  GLN A N   
173  C CA  . GLN A 27  ? 0.6513 0.8001 0.6032 -0.0407 0.0164  -0.0626 27  GLN A CA  
174  C C   . GLN A 27  ? 0.5777 0.7195 0.5293 -0.0361 0.0165  -0.0636 27  GLN A C   
175  O O   . GLN A 27  ? 0.6032 0.7448 0.5556 -0.0326 0.0173  -0.0671 27  GLN A O   
176  C CB  . GLN A 27  ? 0.7107 0.8569 0.6635 -0.0416 0.0147  -0.0589 27  GLN A CB  
177  C CG  . GLN A 27  ? 0.7872 0.9298 0.7417 -0.0378 0.0141  -0.0598 27  GLN A CG  
178  C CD  . GLN A 27  ? 0.7900 0.9283 0.7446 -0.0386 0.0125  -0.0560 27  GLN A CD  
179  O OE1 . GLN A 27  ? 0.7956 0.9336 0.7493 -0.0420 0.0119  -0.0524 27  GLN A OE1 
180  N NE2 . GLN A 27  ? 0.7787 0.9133 0.7342 -0.0355 0.0118  -0.0567 27  GLN A NE2 
181  N N   . TRP A 28  ? 0.5047 0.6409 0.4552 -0.0364 0.0156  -0.0603 28  TRP A N   
182  C CA  . TRP A 28  ? 0.4790 0.6079 0.4294 -0.0322 0.0154  -0.0604 28  TRP A CA  
183  C C   . TRP A 28  ? 0.4729 0.6019 0.4220 -0.0310 0.0166  -0.0634 28  TRP A C   
184  O O   . TRP A 28  ? 0.4650 0.5898 0.4145 -0.0267 0.0170  -0.0654 28  TRP A O   
185  C CB  . TRP A 28  ? 0.4812 0.6043 0.4312 -0.0330 0.0142  -0.0556 28  TRP A CB  
186  C CG  . TRP A 28  ? 0.4238 0.5438 0.3750 -0.0321 0.0131  -0.0534 28  TRP A CG  
187  C CD1 . TRP A 28  ? 0.4476 0.5691 0.3989 -0.0353 0.0124  -0.0503 28  TRP A CD1 
188  C CD2 . TRP A 28  ? 0.4085 0.5230 0.3605 -0.0277 0.0129  -0.0542 28  TRP A CD2 
189  N NE1 . TRP A 28  ? 0.4382 0.5553 0.3902 -0.0333 0.0116  -0.0493 28  TRP A NE1 
190  C CE2 . TRP A 28  ? 0.4425 0.5551 0.3948 -0.0286 0.0119  -0.0516 28  TRP A CE2 
191  C CE3 . TRP A 28  ? 0.3833 0.4938 0.3355 -0.0231 0.0133  -0.0568 28  TRP A CE3 
192  C CZ2 . TRP A 28  ? 0.4374 0.5443 0.3900 -0.0252 0.0114  -0.0516 28  TRP A CZ2 
193  C CZ3 . TRP A 28  ? 0.3966 0.5017 0.3493 -0.0197 0.0127  -0.0567 28  TRP A CZ3 
194  C CH2 . TRP A 28  ? 0.4129 0.5163 0.3657 -0.0209 0.0118  -0.0542 28  TRP A CH2 
195  N N   . VAL A 29  ? 0.4990 0.6327 0.4464 -0.0346 0.0174  -0.0640 29  VAL A N   
196  C CA  . VAL A 29  ? 0.5501 0.6846 0.4958 -0.0338 0.0188  -0.0674 29  VAL A CA  
197  C C   . VAL A 29  ? 0.5551 0.6911 0.5022 -0.0300 0.0202  -0.0720 29  VAL A C   
198  O O   . VAL A 29  ? 0.5507 0.6839 0.4972 -0.0269 0.0211  -0.0748 29  VAL A O   
199  C CB  . VAL A 29  ? 0.5612 0.7016 0.5045 -0.0389 0.0195  -0.0675 29  VAL A CB  
200  C CG1 . VAL A 29  ? 0.5599 0.7012 0.5010 -0.0382 0.0212  -0.0716 29  VAL A CG1 
201  C CG2 . VAL A 29  ? 0.5211 0.6597 0.4630 -0.0425 0.0180  -0.0628 29  VAL A CG2 
202  N N   . ASN A 30  ? 0.5843 0.7246 0.5333 -0.0301 0.0202  -0.0728 30  ASN A N   
203  C CA  . ASN A 30  ? 0.6351 0.7781 0.5861 -0.0269 0.0214  -0.0768 30  ASN A CA  
204  C C   . ASN A 30  ? 0.6418 0.7799 0.5949 -0.0223 0.0205  -0.0769 30  ASN A C   
205  O O   . ASN A 30  ? 0.6848 0.8254 0.6400 -0.0197 0.0211  -0.0796 30  ASN A O   
206  C CB  . ASN A 30  ? 0.7054 0.8565 0.6575 -0.0296 0.0221  -0.0777 30  ASN A CB  
207  C CG  . ASN A 30  ? 0.7377 0.8941 0.6874 -0.0340 0.0234  -0.0783 30  ASN A CG  
208  O OD1 . ASN A 30  ? 0.7639 0.9248 0.7134 -0.0380 0.0231  -0.0764 30  ASN A OD1 
209  N ND2 . ASN A 30  ? 0.7168 0.8724 0.6645 -0.0332 0.0250  -0.0810 30  ASN A ND2 
210  N N   . MET A 31  ? 0.5660 0.6972 0.5187 -0.0212 0.0191  -0.0738 31  MET A N   
211  C CA  . MET A 31  ? 0.5642 0.6897 0.5183 -0.0168 0.0182  -0.0737 31  MET A CA  
212  C C   . MET A 31  ? 0.5391 0.6571 0.4920 -0.0139 0.0181  -0.0732 31  MET A C   
213  O O   . MET A 31  ? 0.5117 0.6237 0.4652 -0.0107 0.0172  -0.0722 31  MET A O   
214  C CB  . MET A 31  ? 0.5786 0.7025 0.5334 -0.0181 0.0165  -0.0703 31  MET A CB  
215  C CG  . MET A 31  ? 0.5716 0.7026 0.5277 -0.0208 0.0165  -0.0708 31  MET A CG  
216  S SD  . MET A 31  ? 0.6093 0.7379 0.5663 -0.0213 0.0146  -0.0677 31  MET A SD  
217  C CE  . MET A 31  ? 0.5892 0.7162 0.5444 -0.0257 0.0139  -0.0630 31  MET A CE  
218  N N   . GLN A 32  ? 0.4986 0.6169 0.4498 -0.0150 0.0190  -0.0740 32  GLN A N   
219  C CA  . GLN A 32  ? 0.5467 0.6582 0.4967 -0.0129 0.0188  -0.0732 32  GLN A CA  
220  C C   . GLN A 32  ? 0.5333 0.6413 0.4842 -0.0077 0.0195  -0.0764 32  GLN A C   
221  O O   . GLN A 32  ? 0.4954 0.5970 0.4457 -0.0052 0.0191  -0.0755 32  GLN A O   
222  C CB  . GLN A 32  ? 0.5212 0.6343 0.4688 -0.0160 0.0194  -0.0732 32  GLN A CB  
223  C CG  . GLN A 32  ? 0.5156 0.6314 0.4624 -0.0211 0.0186  -0.0694 32  GLN A CG  
224  C CD  . GLN A 32  ? 0.5396 0.6560 0.4838 -0.0242 0.0188  -0.0689 32  GLN A CD  
225  O OE1 . GLN A 32  ? 0.5070 0.6183 0.4505 -0.0236 0.0182  -0.0669 32  GLN A OE1 
226  N NE2 . GLN A 32  ? 0.5096 0.6324 0.4523 -0.0278 0.0198  -0.0705 32  GLN A NE2 
227  N N   . ASP A 33  ? 0.5865 0.6986 0.5388 -0.0060 0.0204  -0.0799 33  ASP A N   
228  C CA  . ASP A 33  ? 0.5674 0.6766 0.5209 -0.0010 0.0209  -0.0828 33  ASP A CA  
229  C C   . ASP A 33  ? 0.5208 0.6280 0.4763 0.0015  0.0197  -0.0819 33  ASP A C   
230  O O   . ASP A 33  ? 0.5281 0.6311 0.4843 0.0057  0.0196  -0.0831 33  ASP A O   
231  C CB  . ASP A 33  ? 0.6140 0.7288 0.5681 -0.0003 0.0229  -0.0871 33  ASP A CB  
232  C CG  . ASP A 33  ? 0.6721 0.7870 0.6237 -0.0017 0.0243  -0.0887 33  ASP A CG  
233  O OD1 . ASP A 33  ? 0.7125 0.8332 0.6631 -0.0049 0.0255  -0.0899 33  ASP A OD1 
234  O OD2 . ASP A 33  ? 0.6772 0.7863 0.6275 0.0002  0.0243  -0.0886 33  ASP A OD2 
235  N N   . ASP A 34  ? 0.4924 0.6024 0.4485 -0.0013 0.0187  -0.0797 34  ASP A N   
236  C CA  . ASP A 34  ? 0.4487 0.5567 0.4061 0.0003  0.0173  -0.0786 34  ASP A CA  
237  C C   . ASP A 34  ? 0.4439 0.5436 0.4001 0.0015  0.0161  -0.0752 34  ASP A C   
238  O O   . ASP A 34  ? 0.3800 0.4754 0.3367 0.0047  0.0153  -0.0752 34  ASP A O   
239  C CB  . ASP A 34  ? 0.4795 0.5935 0.4377 -0.0035 0.0168  -0.0774 34  ASP A CB  
240  C CG  . ASP A 34  ? 0.5067 0.6291 0.4664 -0.0045 0.0181  -0.0806 34  ASP A CG  
241  O OD1 . ASP A 34  ? 0.5213 0.6448 0.4828 -0.0011 0.0187  -0.0836 34  ASP A OD1 
242  O OD2 . ASP A 34  ? 0.4768 0.6046 0.4360 -0.0085 0.0186  -0.0801 34  ASP A OD2 
243  N N   . TYR A 35  ? 0.4240 0.5217 0.3786 -0.0010 0.0159  -0.0723 35  TYR A N   
244  C CA  . TYR A 35  ? 0.3983 0.4885 0.3519 -0.0003 0.0150  -0.0687 35  TYR A CA  
245  C C   . TYR A 35  ? 0.3901 0.4769 0.3425 -0.0002 0.0155  -0.0677 35  TYR A C   
246  O O   . TYR A 35  ? 0.4048 0.4955 0.3567 -0.0023 0.0163  -0.0688 35  TYR A O   
247  C CB  . TYR A 35  ? 0.4159 0.5071 0.3692 -0.0041 0.0141  -0.0650 35  TYR A CB  
248  C CG  . TYR A 35  ? 0.4089 0.5038 0.3632 -0.0052 0.0135  -0.0655 35  TYR A CG  
249  C CD1 . TYR A 35  ? 0.4292 0.5322 0.3842 -0.0084 0.0139  -0.0669 35  TYR A CD1 
250  C CD2 . TYR A 35  ? 0.4480 0.5380 0.4021 -0.0033 0.0125  -0.0643 35  TYR A CD2 
251  C CE1 . TYR A 35  ? 0.4453 0.5518 0.4014 -0.0095 0.0132  -0.0671 35  TYR A CE1 
252  C CE2 . TYR A 35  ? 0.5011 0.5943 0.4559 -0.0046 0.0117  -0.0646 35  TYR A CE2 
253  C CZ  . TYR A 35  ? 0.4665 0.5681 0.4225 -0.0076 0.0120  -0.0660 35  TYR A CZ  
254  O OH  . TYR A 35  ? 0.5380 0.6430 0.4949 -0.0090 0.0112  -0.0661 35  TYR A OH  
255  N N   . HIS A 36  ? 0.4220 0.5013 0.3740 0.0022  0.0151  -0.0654 36  HIS A N   
256  C CA  . HIS A 36  ? 0.3885 0.4640 0.3396 0.0019  0.0152  -0.0632 36  HIS A CA  
257  C C   . HIS A 36  ? 0.3433 0.4197 0.2942 -0.0022 0.0146  -0.0589 36  HIS A C   
258  O O   . HIS A 36  ? 0.3153 0.3872 0.2663 -0.0017 0.0140  -0.0558 36  HIS A O   
259  C CB  . HIS A 36  ? 0.4085 0.4758 0.3595 0.0062  0.0151  -0.0623 36  HIS A CB  
260  C CG  . HIS A 36  ? 0.5086 0.5717 0.4592 0.0060  0.0152  -0.0595 36  HIS A CG  
261  N ND1 . HIS A 36  ? 0.5250 0.5868 0.4751 0.0074  0.0158  -0.0612 36  HIS A ND1 
262  C CD2 . HIS A 36  ? 0.4910 0.5507 0.4415 0.0046  0.0147  -0.0549 36  HIS A CD2 
263  C CE1 . HIS A 36  ? 0.5298 0.5879 0.4797 0.0068  0.0156  -0.0578 36  HIS A CE1 
264  N NE2 . HIS A 36  ? 0.5340 0.5909 0.4843 0.0051  0.0150  -0.0539 36  HIS A NE2 
265  N N   . CYS A 37  ? 0.2990 0.3811 0.2494 -0.0062 0.0148  -0.0588 37  CYS A N   
266  C CA  . CYS A 37  ? 0.3050 0.3893 0.2553 -0.0105 0.0142  -0.0550 37  CYS A CA  
267  C C   . CYS A 37  ? 0.3135 0.3942 0.2633 -0.0113 0.0140  -0.0517 37  CYS A C   
268  O O   . CYS A 37  ? 0.3417 0.4227 0.2908 -0.0112 0.0144  -0.0532 37  CYS A O   
269  C CB  . CYS A 37  ? 0.3413 0.4339 0.2911 -0.0146 0.0145  -0.0567 37  CYS A CB  
270  S SG  . CYS A 37  ? 0.4215 0.5193 0.3723 -0.0140 0.0148  -0.0603 37  CYS A SG  
271  N N   . ILE A 38  ? 0.2970 0.3747 0.2474 -0.0124 0.0133  -0.0471 38  ILE A N   
272  C CA  . ILE A 38  ? 0.2997 0.3744 0.2503 -0.0136 0.0130  -0.0430 38  ILE A CA  
273  C C   . ILE A 38  ? 0.3233 0.4022 0.2740 -0.0185 0.0123  -0.0395 38  ILE A C   
274  O O   . ILE A 38  ? 0.3561 0.4349 0.3074 -0.0193 0.0120  -0.0376 38  ILE A O   
275  C CB  . ILE A 38  ? 0.2668 0.3334 0.2182 -0.0100 0.0129  -0.0401 38  ILE A CB  
276  C CG1 . ILE A 38  ? 0.2812 0.3434 0.2324 -0.0052 0.0135  -0.0434 38  ILE A CG1 
277  C CG2 . ILE A 38  ? 0.2652 0.3292 0.2174 -0.0113 0.0126  -0.0353 38  ILE A CG2 
278  C CD1 . ILE A 38  ? 0.2892 0.3438 0.2408 -0.0015 0.0136  -0.0414 38  ILE A CD1 
279  N N   . TYR A 39  ? 0.3712 0.4534 0.3213 -0.0217 0.0121  -0.0385 39  TYR A N   
280  C CA  . TYR A 39  ? 0.3494 0.4355 0.2997 -0.0266 0.0113  -0.0346 39  TYR A CA  
281  C C   . TYR A 39  ? 0.3678 0.4504 0.3190 -0.0272 0.0107  -0.0299 39  TYR A C   
282  O O   . TYR A 39  ? 0.3478 0.4303 0.2983 -0.0274 0.0106  -0.0305 39  TYR A O   
283  C CB  . TYR A 39  ? 0.3347 0.4282 0.2832 -0.0305 0.0114  -0.0373 39  TYR A CB  
284  C CG  . TYR A 39  ? 0.3649 0.4627 0.3130 -0.0305 0.0120  -0.0412 39  TYR A CG  
285  C CD1 . TYR A 39  ? 0.3735 0.4719 0.3211 -0.0276 0.0129  -0.0463 39  TYR A CD1 
286  C CD2 . TYR A 39  ? 0.3468 0.4482 0.2953 -0.0332 0.0116  -0.0396 39  TYR A CD2 
287  C CE1 . TYR A 39  ? 0.3904 0.4931 0.3380 -0.0275 0.0135  -0.0497 39  TYR A CE1 
288  C CE2 . TYR A 39  ? 0.3700 0.4757 0.3185 -0.0333 0.0121  -0.0431 39  TYR A CE2 
289  C CZ  . TYR A 39  ? 0.3894 0.4957 0.3376 -0.0303 0.0131  -0.0480 39  TYR A CZ  
290  O OH  . TYR A 39  ? 0.4584 0.5691 0.4069 -0.0302 0.0136  -0.0512 39  TYR A OH  
291  N N   . CYS A 40  ? 0.3555 0.4351 0.3082 -0.0274 0.0104  -0.0252 40  CYS A N   
292  C CA  . CYS A 40  ? 0.3823 0.4583 0.3366 -0.0276 0.0099  -0.0200 40  CYS A CA  
293  C C   . CYS A 40  ? 0.3858 0.4661 0.3407 -0.0326 0.0090  -0.0156 40  CYS A C   
294  O O   . CYS A 40  ? 0.3362 0.4175 0.2917 -0.0339 0.0089  -0.0139 40  CYS A O   
295  C CB  . CYS A 40  ? 0.3597 0.4284 0.3156 -0.0236 0.0105  -0.0175 40  CYS A CB  
296  S SG  . CYS A 40  ? 0.3486 0.4125 0.3071 -0.0234 0.0103  -0.0106 40  CYS A SG  
297  N N   . ILE A 41  ? 0.3830 0.4660 0.3377 -0.0355 0.0082  -0.0139 41  ILE A N   
298  C CA  . ILE A 41  ? 0.4026 0.4895 0.3581 -0.0403 0.0072  -0.0092 41  ILE A CA  
299  C C   . ILE A 41  ? 0.3544 0.4363 0.3129 -0.0390 0.0070  -0.0032 41  ILE A C   
300  O O   . ILE A 41  ? 0.3866 0.4652 0.3464 -0.0375 0.0069  -0.0009 41  ILE A O   
301  C CB  . ILE A 41  ? 0.4395 0.5311 0.3935 -0.0443 0.0062  -0.0091 41  ILE A CB  
302  C CG1 . ILE A 41  ? 0.4532 0.5496 0.4040 -0.0456 0.0066  -0.0152 41  ILE A CG1 
303  C CG2 . ILE A 41  ? 0.4665 0.5619 0.4214 -0.0492 0.0050  -0.0038 41  ILE A CG2 
304  C CD1 . ILE A 41  ? 0.4745 0.5693 0.4237 -0.0437 0.0070  -0.0190 41  ILE A CD1 
305  N N   . VAL A 42  ? 0.3824 0.4642 0.3420 -0.0398 0.0071  -0.0003 42  VAL A N   
306  C CA  . VAL A 42  ? 0.3938 0.4696 0.3560 -0.0375 0.0076  0.0045  42  VAL A CA  
307  C C   . VAL A 42  ? 0.4355 0.5128 0.4001 -0.0407 0.0067  0.0112  42  VAL A C   
308  O O   . VAL A 42  ? 0.4063 0.4842 0.3722 -0.0425 0.0066  0.0149  42  VAL A O   
309  C CB  . VAL A 42  ? 0.3892 0.4624 0.3510 -0.0358 0.0084  0.0037  42  VAL A CB  
310  C CG1 . VAL A 42  ? 0.3822 0.4517 0.3425 -0.0314 0.0094  -0.0016 42  VAL A CG1 
311  C CG2 . VAL A 42  ? 0.4099 0.4893 0.3706 -0.0400 0.0079  0.0030  42  VAL A CG2 
312  N N   . ASP A 43  ? 0.4259 0.5037 0.3913 -0.0414 0.0060  0.0128  43  ASP A N   
313  C CA  . ASP A 43  ? 0.4217 0.5014 0.3897 -0.0445 0.0049  0.0191  43  ASP A CA  
314  C C   . ASP A 43  ? 0.4273 0.5013 0.3988 -0.0419 0.0057  0.0247  43  ASP A C   
315  O O   . ASP A 43  ? 0.4446 0.5204 0.4185 -0.0445 0.0050  0.0304  43  ASP A O   
316  C CB  . ASP A 43  ? 0.4445 0.5264 0.4121 -0.0462 0.0037  0.0193  43  ASP A CB  
317  C CG  . ASP A 43  ? 0.4556 0.5322 0.4236 -0.0417 0.0045  0.0173  43  ASP A CG  
318  O OD1 . ASP A 43  ? 0.4219 0.4933 0.3897 -0.0371 0.0060  0.0148  43  ASP A OD1 
319  O OD2 . ASP A 43  ? 0.4210 0.4983 0.3893 -0.0427 0.0036  0.0183  43  ASP A OD2 
320  N N   . GLN A 44  ? 0.3776 0.4448 0.3495 -0.0367 0.0072  0.0233  44  GLN A N   
321  C CA  . GLN A 44  ? 0.3676 0.4285 0.3424 -0.0337 0.0084  0.0281  44  GLN A CA  
322  C C   . GLN A 44  ? 0.3677 0.4281 0.3424 -0.0346 0.0090  0.0296  44  GLN A C   
323  O O   . GLN A 44  ? 0.3844 0.4422 0.3619 -0.0344 0.0095  0.0352  44  GLN A O   
324  C CB  . GLN A 44  ? 0.3689 0.4224 0.3437 -0.0280 0.0099  0.0261  44  GLN A CB  
325  C CG  . GLN A 44  ? 0.4043 0.4578 0.3795 -0.0270 0.0094  0.0252  44  GLN A CG  
326  C CD  . GLN A 44  ? 0.3981 0.4444 0.3734 -0.0215 0.0109  0.0236  44  GLN A CD  
327  O OE1 . GLN A 44  ? 0.4123 0.4576 0.3850 -0.0195 0.0112  0.0181  44  GLN A OE1 
328  N NE2 . GLN A 44  ? 0.4105 0.4515 0.3888 -0.0190 0.0121  0.0286  44  GLN A NE2 
329  N N   . HIS A 45  ? 0.3521 0.4151 0.3237 -0.0356 0.0089  0.0248  45  HIS A N   
330  C CA  . HIS A 45  ? 0.3771 0.4408 0.3484 -0.0373 0.0091  0.0259  45  HIS A CA  
331  C C   . HIS A 45  ? 0.4002 0.4700 0.3728 -0.0425 0.0078  0.0301  45  HIS A C   
332  O O   . HIS A 45  ? 0.3825 0.4510 0.3565 -0.0435 0.0081  0.0344  45  HIS A O   
333  C CB  . HIS A 45  ? 0.3715 0.4369 0.3393 -0.0372 0.0092  0.0197  45  HIS A CB  
334  C CG  . HIS A 45  ? 0.3229 0.3812 0.2896 -0.0323 0.0106  0.0168  45  HIS A CG  
335  N ND1 . HIS A 45  ? 0.3184 0.3710 0.2853 -0.0305 0.0117  0.0190  45  HIS A ND1 
336  C CD2 . HIS A 45  ? 0.3076 0.3634 0.2728 -0.0288 0.0111  0.0121  45  HIS A CD2 
337  C CE1 . HIS A 45  ? 0.3328 0.3797 0.2982 -0.0262 0.0128  0.0158  45  HIS A CE1 
338  N NE2 . HIS A 45  ? 0.3023 0.3510 0.2667 -0.0250 0.0124  0.0116  45  HIS A NE2 
339  N N   . ALA A 46  ? 0.4073 0.4834 0.3791 -0.0459 0.0063  0.0290  46  ALA A N   
340  C CA  . ALA A 46  ? 0.4324 0.5151 0.4048 -0.0514 0.0048  0.0326  46  ALA A CA  
341  C C   . ALA A 46  ? 0.4684 0.5495 0.4448 -0.0521 0.0046  0.0403  46  ALA A C   
342  O O   . ALA A 46  ? 0.4870 0.5714 0.4645 -0.0555 0.0039  0.0440  46  ALA A O   
343  C CB  . ALA A 46  ? 0.3878 0.4762 0.3584 -0.0543 0.0034  0.0299  46  ALA A CB  
344  N N   . ILE A 47  ? 0.4684 0.5446 0.4474 -0.0487 0.0052  0.0428  47  ILE A N   
345  C CA  . ILE A 47  ? 0.4607 0.5359 0.4441 -0.0493 0.0050  0.0505  47  ILE A CA  
346  C C   . ILE A 47  ? 0.4662 0.5364 0.4517 -0.0473 0.0066  0.0545  47  ILE A C   
347  O O   . ILE A 47  ? 0.5326 0.6014 0.5220 -0.0473 0.0068  0.0609  47  ILE A O   
348  C CB  . ILE A 47  ? 0.4683 0.5409 0.4541 -0.0468 0.0050  0.0524  47  ILE A CB  
349  C CG1 . ILE A 47  ? 0.4406 0.5053 0.4260 -0.0408 0.0071  0.0495  47  ILE A CG1 
350  C CG2 . ILE A 47  ? 0.4826 0.5608 0.4664 -0.0500 0.0032  0.0497  47  ILE A CG2 
351  C CD1 . ILE A 47  ? 0.4372 0.4980 0.4260 -0.0379 0.0076  0.0532  47  ILE A CD1 
352  N N   . THR A 48  ? 0.4827 0.5501 0.4656 -0.0458 0.0077  0.0507  48  THR A N   
353  C CA  . THR A 48  ? 0.4961 0.5593 0.4801 -0.0448 0.0090  0.0540  48  THR A CA  
354  C C   . THR A 48  ? 0.5175 0.5863 0.5028 -0.0499 0.0078  0.0584  48  THR A C   
355  O O   . THR A 48  ? 0.5631 0.6288 0.5506 -0.0495 0.0087  0.0632  48  THR A O   
356  C CB  . THR A 48  ? 0.4985 0.5584 0.4788 -0.0429 0.0101  0.0485  48  THR A CB  
357  O OG1 . THR A 48  ? 0.5152 0.5820 0.4925 -0.0463 0.0087  0.0437  48  THR A OG1 
358  C CG2 . THR A 48  ? 0.5215 0.5746 0.5006 -0.0376 0.0115  0.0450  48  THR A CG2 
359  N N   . VAL A 49  ? 0.5280 0.6046 0.5117 -0.0544 0.0058  0.0565  49  VAL A N   
360  C CA  . VAL A 49  ? 0.5913 0.6742 0.5761 -0.0596 0.0043  0.0607  49  VAL A CA  
361  C C   . VAL A 49  ? 0.5917 0.6792 0.5786 -0.0621 0.0025  0.0639  49  VAL A C   
362  O O   . VAL A 49  ? 0.5626 0.6526 0.5473 -0.0626 0.0017  0.0598  49  VAL A O   
363  C CB  . VAL A 49  ? 0.6190 0.7078 0.5999 -0.0633 0.0034  0.0559  49  VAL A CB  
364  C CG1 . VAL A 49  ? 0.6695 0.7656 0.6510 -0.0692 0.0015  0.0597  49  VAL A CG1 
365  C CG2 . VAL A 49  ? 0.6102 0.6951 0.5893 -0.0616 0.0048  0.0535  49  VAL A CG2 
366  N N   . ARG A 50  ? 0.6501 0.7388 0.6408 -0.0641 0.0019  0.0711  50  ARG A N   
367  C CA  . ARG A 50  ? 0.6937 0.7871 0.6865 -0.0670 0.0000  0.0747  50  ARG A CA  
368  C C   . ARG A 50  ? 0.7051 0.8064 0.6942 -0.0723 -0.0022 0.0715  50  ARG A C   
369  O O   . ARG A 50  ? 0.7138 0.8187 0.7011 -0.0755 -0.0026 0.0709  50  ARG A O   
370  C CB  . ARG A 50  ? 0.7684 0.8621 0.7663 -0.0683 -0.0004 0.0834  50  ARG A CB  
371  C CG  . ARG A 50  ? 0.8208 0.9175 0.8220 -0.0699 -0.0021 0.0882  50  ARG A CG  
372  C CD  . ARG A 50  ? 0.8293 0.9213 0.8315 -0.0655 -0.0012 0.0867  50  ARG A CD  
373  N NE  . ARG A 50  ? 0.9003 0.9841 0.9034 -0.0597 0.0017  0.0858  50  ARG A NE  
374  C CZ  . ARG A 50  ? 0.8834 0.9624 0.8910 -0.0569 0.0033  0.0917  50  ARG A CZ  
375  N NH1 . ARG A 50  ? 0.8477 0.9295 0.8601 -0.0591 0.0023  0.0992  50  ARG A NH1 
376  N NH2 . ARG A 50  ? 0.9071 0.9782 0.9144 -0.0517 0.0059  0.0900  50  ARG A NH2 
377  N N   . GLN A 51  ? 0.7051 0.8088 0.6929 -0.0733 -0.0034 0.0695  51  GLN A N   
378  C CA  . GLN A 51  ? 0.6763 0.7873 0.6605 -0.0784 -0.0053 0.0665  51  GLN A CA  
379  C C   . GLN A 51  ? 0.6333 0.7464 0.6181 -0.0801 -0.0070 0.0684  51  GLN A C   
380  O O   . GLN A 51  ? 0.6381 0.7471 0.6259 -0.0769 -0.0066 0.0708  51  GLN A O   
381  C CB  . GLN A 51  ? 0.7290 0.8401 0.7081 -0.0773 -0.0044 0.0581  51  GLN A CB  
382  C CG  . GLN A 51  ? 0.7084 0.8137 0.6870 -0.0718 -0.0029 0.0537  51  GLN A CG  
383  C CD  . GLN A 51  ? 0.6922 0.7959 0.6676 -0.0696 -0.0014 0.0471  51  GLN A CD  
384  O OE1 . GLN A 51  ? 0.6487 0.7486 0.6251 -0.0671 0.0000  0.0476  51  GLN A OE1 
385  N NE2 . GLN A 51  ? 0.7015 0.8081 0.6730 -0.0704 -0.0016 0.0409  51  GLN A NE2 
386  N N   . ASP A 52  ? 0.6527 0.7725 0.6346 -0.0855 -0.0090 0.0676  52  ASP A N   
387  C CA  . ASP A 52  ? 0.6624 0.7850 0.6438 -0.0883 -0.0110 0.0689  52  ASP A CA  
388  C C   . ASP A 52  ? 0.6018 0.7212 0.5808 -0.0850 -0.0101 0.0629  52  ASP A C   
389  O O   . ASP A 52  ? 0.6146 0.7338 0.5895 -0.0840 -0.0091 0.0561  52  ASP A O   
390  C CB  . ASP A 52  ? 0.6666 0.7967 0.6442 -0.0949 -0.0130 0.0683  52  ASP A CB  
391  C CG  . ASP A 52  ? 0.7280 0.8612 0.7054 -0.0987 -0.0154 0.0711  52  ASP A CG  
392  O OD1 . ASP A 52  ? 0.8164 0.9514 0.7891 -0.1004 -0.0159 0.0659  52  ASP A OD1 
393  O OD2 . ASP A 52  ? 0.7898 0.9237 0.7718 -0.0998 -0.0167 0.0785  52  ASP A OD2 
394  N N   . ALA A 53  ? 0.5905 0.7073 0.5723 -0.0833 -0.0106 0.0657  53  ALA A N   
395  C CA  . ALA A 53  ? 0.5818 0.6943 0.5622 -0.0794 -0.0096 0.0610  53  ALA A CA  
396  C C   . ALA A 53  ? 0.5918 0.7077 0.5664 -0.0822 -0.0104 0.0547  53  ALA A C   
397  O O   . ALA A 53  ? 0.5592 0.6723 0.5311 -0.0791 -0.0090 0.0484  53  ALA A O   
398  C CB  . ALA A 53  ? 0.5967 0.7068 0.5815 -0.0780 -0.0103 0.0663  53  ALA A CB  
399  N N   . GLN A 54  ? 0.5953 0.7170 0.5680 -0.0881 -0.0127 0.0566  54  GLN A N   
400  C CA  . GLN A 54  ? 0.6322 0.7569 0.5991 -0.0913 -0.0135 0.0511  54  GLN A CA  
401  C C   . GLN A 54  ? 0.5903 0.7169 0.5528 -0.0916 -0.0121 0.0448  54  GLN A C   
402  O O   . GLN A 54  ? 0.5803 0.7067 0.5386 -0.0910 -0.0113 0.0382  54  GLN A O   
403  C CB  . GLN A 54  ? 0.6912 0.8213 0.6569 -0.0978 -0.0163 0.0552  54  GLN A CB  
404  C CG  . GLN A 54  ? 0.7522 0.8809 0.7225 -0.0977 -0.0178 0.0617  54  GLN A CG  
405  C CD  . GLN A 54  ? 0.8083 0.9424 0.7774 -0.1044 -0.0209 0.0658  54  GLN A CD  
406  O OE1 . GLN A 54  ? 0.9105 1.0494 0.8754 -0.1093 -0.0219 0.0645  54  GLN A OE1 
407  N NE2 . GLN A 54  ? 0.8485 0.9818 0.8212 -0.1047 -0.0224 0.0710  54  GLN A NE2 
408  N N   . LYS A 55  ? 0.5646 0.6929 0.5285 -0.0923 -0.0117 0.0468  55  LYS A N   
409  C CA  . LYS A 55  ? 0.5450 0.6748 0.5057 -0.0921 -0.0102 0.0414  55  LYS A CA  
410  C C   . LYS A 55  ? 0.4986 0.6230 0.4595 -0.0859 -0.0079 0.0363  55  LYS A C   
411  O O   . LYS A 55  ? 0.4748 0.6002 0.4319 -0.0853 -0.0068 0.0297  55  LYS A O   
412  C CB  . LYS A 55  ? 0.6076 0.7401 0.5702 -0.0943 -0.0104 0.0455  55  LYS A CB  
413  C CG  . LYS A 55  ? 0.6452 0.7846 0.6055 -0.1011 -0.0124 0.0478  55  LYS A CG  
414  C CD  . LYS A 55  ? 0.7003 0.8421 0.6627 -0.1031 -0.0126 0.0520  55  LYS A CD  
415  C CE  . LYS A 55  ? 0.7421 0.8904 0.7027 -0.1099 -0.0149 0.0556  55  LYS A CE  
416  N NZ  . LYS A 55  ? 0.7732 0.9250 0.7332 -0.1124 -0.0146 0.0562  55  LYS A NZ  
417  N N   . LEU A 56  ? 0.4633 0.5822 0.4286 -0.0813 -0.0070 0.0393  56  LEU A N   
418  C CA  . LEU A 56  ? 0.4557 0.5688 0.4212 -0.0753 -0.0049 0.0350  56  LEU A CA  
419  C C   . LEU A 56  ? 0.4555 0.5673 0.4181 -0.0738 -0.0047 0.0296  56  LEU A C   
420  O O   . LEU A 56  ? 0.4692 0.5799 0.4291 -0.0714 -0.0033 0.0234  56  LEU A O   
421  C CB  . LEU A 56  ? 0.4962 0.6034 0.4666 -0.0711 -0.0042 0.0399  56  LEU A CB  
422  C CG  . LEU A 56  ? 0.4920 0.5925 0.4630 -0.0648 -0.0020 0.0363  56  LEU A CG  
423  C CD1 . LEU A 56  ? 0.4756 0.5766 0.4436 -0.0637 -0.0008 0.0305  56  LEU A CD1 
424  C CD2 . LEU A 56  ? 0.4874 0.5827 0.4630 -0.0615 -0.0011 0.0419  56  LEU A CD2 
425  N N   . ARG A 57  ? 0.4465 0.5584 0.4095 -0.0754 -0.0061 0.0321  57  ARG A N   
426  C CA  . ARG A 57  ? 0.4852 0.5960 0.4452 -0.0745 -0.0060 0.0273  57  ARG A CA  
427  C C   . ARG A 57  ? 0.4990 0.6142 0.4536 -0.0774 -0.0059 0.0212  57  ARG A C   
428  O O   . ARG A 57  ? 0.5426 0.6558 0.4946 -0.0746 -0.0045 0.0151  57  ARG A O   
429  C CB  . ARG A 57  ? 0.4757 0.5867 0.4370 -0.0767 -0.0079 0.0316  57  ARG A CB  
430  C CG  . ARG A 57  ? 0.4690 0.5785 0.4269 -0.0761 -0.0079 0.0268  57  ARG A CG  
431  C CD  . ARG A 57  ? 0.4936 0.6017 0.4535 -0.0771 -0.0096 0.0313  57  ARG A CD  
432  N NE  . ARG A 57  ? 0.5292 0.6326 0.4948 -0.0728 -0.0090 0.0360  57  ARG A NE  
433  C CZ  . ARG A 57  ? 0.4986 0.6028 0.4689 -0.0739 -0.0099 0.0434  57  ARG A CZ  
434  N NH1 . ARG A 57  ? 0.4802 0.5899 0.4505 -0.0794 -0.0119 0.0474  57  ARG A NH1 
435  N NH2 . ARG A 57  ? 0.5032 0.6026 0.4784 -0.0693 -0.0089 0.0469  57  ARG A NH2 
436  N N   . LYS A 58  ? 0.5246 0.6455 0.4774 -0.0830 -0.0072 0.0231  58  LYS A N   
437  C CA  . LYS A 58  ? 0.4947 0.6202 0.4421 -0.0863 -0.0069 0.0177  58  LYS A CA  
438  C C   . LYS A 58  ? 0.4545 0.5798 0.4010 -0.0834 -0.0049 0.0126  58  LYS A C   
439  O O   . LYS A 58  ? 0.4429 0.5687 0.3858 -0.0826 -0.0037 0.0064  58  LYS A O   
440  C CB  . LYS A 58  ? 0.5077 0.6394 0.4535 -0.0929 -0.0087 0.0212  58  LYS A CB  
441  C CG  . LYS A 58  ? 0.5478 0.6840 0.4879 -0.0963 -0.0082 0.0157  58  LYS A CG  
442  C CD  . LYS A 58  ? 0.6385 0.7809 0.5762 -0.1032 -0.0100 0.0186  58  LYS A CD  
443  C CE  . LYS A 58  ? 0.7005 0.8456 0.6409 -0.1046 -0.0102 0.0226  58  LYS A CE  
444  N NZ  . LYS A 58  ? 0.7757 0.9205 0.7162 -0.1015 -0.0081 0.0186  58  LYS A NZ  
445  N N   . ALA A 59  ? 0.4060 0.5305 0.3558 -0.0819 -0.0044 0.0155  59  ALA A N   
446  C CA  . ALA A 59  ? 0.4310 0.5556 0.3804 -0.0796 -0.0027 0.0116  59  ALA A CA  
447  C C   . ALA A 59  ? 0.4183 0.5376 0.3681 -0.0735 -0.0010 0.0070  59  ALA A C   
448  O O   . ALA A 59  ? 0.4079 0.5279 0.3560 -0.0720 0.0003  0.0020  59  ALA A O   
449  C CB  . ALA A 59  ? 0.4317 0.5561 0.3844 -0.0798 -0.0029 0.0166  59  ALA A CB  
450  N N   . THR A 60  ? 0.4110 0.5251 0.3629 -0.0703 -0.0011 0.0087  60  THR A N   
451  C CA  . THR A 60  ? 0.4477 0.5567 0.3996 -0.0648 0.0004  0.0043  60  THR A CA  
452  C C   . THR A 60  ? 0.4435 0.5545 0.3911 -0.0654 0.0009  -0.0020 60  THR A C   
453  O O   . THR A 60  ? 0.4709 0.5813 0.4173 -0.0625 0.0023  -0.0073 60  THR A O   
454  C CB  . THR A 60  ? 0.4462 0.5496 0.4012 -0.0617 0.0001  0.0079  60  THR A CB  
455  O OG1 . THR A 60  ? 0.4154 0.5163 0.3744 -0.0606 0.0000  0.0136  60  THR A OG1 
456  C CG2 . THR A 60  ? 0.4360 0.5341 0.3908 -0.0562 0.0015  0.0034  60  THR A CG2 
457  N N   . LEU A 61  ? 0.4539 0.5676 0.3994 -0.0694 -0.0004 -0.0013 61  LEU A N   
458  C CA  . LEU A 61  ? 0.4615 0.5770 0.4024 -0.0706 0.0001  -0.0070 61  LEU A CA  
459  C C   . LEU A 61  ? 0.4414 0.5625 0.3793 -0.0734 0.0009  -0.0106 61  LEU A C   
460  O O   . LEU A 61  ? 0.4506 0.5723 0.3857 -0.0722 0.0023  -0.0165 61  LEU A O   
461  C CB  . LEU A 61  ? 0.4884 0.6049 0.4274 -0.0744 -0.0015 -0.0050 61  LEU A CB  
462  C CG  . LEU A 61  ? 0.4804 0.5921 0.4224 -0.0723 -0.0024 -0.0011 61  LEU A CG  
463  C CD1 . LEU A 61  ? 0.5122 0.6264 0.4531 -0.0776 -0.0046 0.0030  61  LEU A CD1 
464  C CD2 . LEU A 61  ? 0.4691 0.5758 0.4104 -0.0675 -0.0011 -0.0058 61  LEU A CD2 
465  N N   . ASP A 62  ? 0.4540 0.5791 0.3925 -0.0771 0.0000  -0.0069 62  ASP A N   
466  C CA  . ASP A 62  ? 0.5133 0.6438 0.4496 -0.0796 0.0008  -0.0098 62  ASP A CA  
467  C C   . ASP A 62  ? 0.4943 0.6231 0.4317 -0.0749 0.0027  -0.0140 62  ASP A C   
468  O O   . ASP A 62  ? 0.5301 0.6615 0.4649 -0.0748 0.0040  -0.0193 62  ASP A O   
469  C CB  . ASP A 62  ? 0.4865 0.6209 0.4242 -0.0838 -0.0005 -0.0044 62  ASP A CB  
470  C CG  . ASP A 62  ? 0.5317 0.6692 0.4676 -0.0895 -0.0024 -0.0005 62  ASP A CG  
471  O OD1 . ASP A 62  ? 0.4714 0.6081 0.4047 -0.0905 -0.0029 -0.0020 62  ASP A OD1 
472  O OD2 . ASP A 62  ? 0.4981 0.6386 0.4352 -0.0929 -0.0036 0.0043  62  ASP A OD2 
473  N N   . THR A 63  ? 0.4806 0.6050 0.4219 -0.0711 0.0028  -0.0115 63  THR A N   
474  C CA  . THR A 63  ? 0.4353 0.5576 0.3778 -0.0666 0.0043  -0.0149 63  THR A CA  
475  C C   . THR A 63  ? 0.4480 0.5680 0.3889 -0.0629 0.0056  -0.0208 63  THR A C   
476  O O   . THR A 63  ? 0.4311 0.5529 0.3709 -0.0615 0.0069  -0.0256 63  THR A O   
477  C CB  . THR A 63  ? 0.4372 0.5543 0.3836 -0.0634 0.0041  -0.0107 63  THR A CB  
478  O OG1 . THR A 63  ? 0.4428 0.5626 0.3906 -0.0669 0.0031  -0.0057 63  THR A OG1 
479  C CG2 . THR A 63  ? 0.4464 0.5607 0.3938 -0.0588 0.0054  -0.0141 63  THR A CG2 
480  N N   . LEU A 64  ? 0.4325 0.5487 0.3733 -0.0614 0.0052  -0.0204 64  LEU A N   
481  C CA  . LEU A 64  ? 0.4291 0.5425 0.3686 -0.0577 0.0064  -0.0256 64  LEU A CA  
482  C C   . LEU A 64  ? 0.4882 0.6064 0.4237 -0.0601 0.0074  -0.0307 64  LEU A C   
483  O O   . LEU A 64  ? 0.5386 0.6569 0.4734 -0.0573 0.0089  -0.0357 64  LEU A O   
484  C CB  . LEU A 64  ? 0.4247 0.5334 0.3646 -0.0564 0.0057  -0.0238 64  LEU A CB  
485  C CG  . LEU A 64  ? 0.4216 0.5275 0.3595 -0.0534 0.0068  -0.0288 64  LEU A CG  
486  C CD1 . LEU A 64  ? 0.4520 0.5547 0.3914 -0.0478 0.0082  -0.0324 64  LEU A CD1 
487  C CD2 . LEU A 64  ? 0.4385 0.5403 0.3770 -0.0529 0.0058  -0.0262 64  LEU A CD2 
488  N N   . ALA A 65  ? 0.4635 0.5856 0.3963 -0.0654 0.0065  -0.0294 65  ALA A N   
489  C CA  . ALA A 65  ? 0.4797 0.6060 0.4082 -0.0681 0.0075  -0.0340 65  ALA A CA  
490  C C   . ALA A 65  ? 0.4598 0.5907 0.3881 -0.0683 0.0088  -0.0370 65  ALA A C   
491  O O   . ALA A 65  ? 0.5118 0.6441 0.4383 -0.0669 0.0105  -0.0422 65  ALA A O   
492  C CB  . ALA A 65  ? 0.5231 0.6527 0.4487 -0.0742 0.0060  -0.0311 65  ALA A CB  
493  N N   . LEU A 66  ? 0.4718 0.6049 0.4023 -0.0698 0.0081  -0.0334 66  LEU A N   
494  C CA  . LEU A 66  ? 0.4730 0.6105 0.4037 -0.0703 0.0091  -0.0355 66  LEU A CA  
495  C C   . LEU A 66  ? 0.4564 0.5916 0.3891 -0.0648 0.0106  -0.0394 66  LEU A C   
496  O O   . LEU A 66  ? 0.4565 0.5954 0.3882 -0.0646 0.0120  -0.0437 66  LEU A O   
497  C CB  . LEU A 66  ? 0.5404 0.6800 0.4733 -0.0731 0.0078  -0.0302 66  LEU A CB  
498  C CG  . LEU A 66  ? 0.5613 0.7071 0.4934 -0.0760 0.0084  -0.0313 66  LEU A CG  
499  C CD1 . LEU A 66  ? 0.5870 0.7380 0.5148 -0.0797 0.0093  -0.0348 66  LEU A CD1 
500  C CD2 . LEU A 66  ? 0.5589 0.7062 0.4928 -0.0792 0.0069  -0.0256 66  LEU A CD2 
501  N N   . TYR A 67  ? 0.4226 0.5519 0.3582 -0.0605 0.0102  -0.0378 67  TYR A N   
502  C CA  . TYR A 67  ? 0.4607 0.5871 0.3980 -0.0552 0.0113  -0.0413 67  TYR A CA  
503  C C   . TYR A 67  ? 0.4536 0.5798 0.3888 -0.0530 0.0128  -0.0470 67  TYR A C   
504  O O   . TYR A 67  ? 0.4295 0.5575 0.3650 -0.0507 0.0142  -0.0511 67  TYR A O   
505  C CB  . TYR A 67  ? 0.4687 0.5883 0.4090 -0.0513 0.0106  -0.0382 67  TYR A CB  
506  C CG  . TYR A 67  ? 0.4429 0.5620 0.3856 -0.0512 0.0100  -0.0348 67  TYR A CG  
507  C CD1 . TYR A 67  ? 0.4800 0.6009 0.4233 -0.0551 0.0089  -0.0299 67  TYR A CD1 
508  C CD2 . TYR A 67  ? 0.4985 0.6152 0.4428 -0.0473 0.0107  -0.0367 67  TYR A CD2 
509  C CE1 . TYR A 67  ? 0.4935 0.6135 0.4388 -0.0550 0.0085  -0.0269 67  TYR A CE1 
510  C CE2 . TYR A 67  ? 0.4600 0.5759 0.4062 -0.0474 0.0102  -0.0338 67  TYR A CE2 
511  C CZ  . TYR A 67  ? 0.4772 0.5947 0.4238 -0.0512 0.0091  -0.0289 67  TYR A CZ  
512  O OH  . TYR A 67  ? 0.4652 0.5815 0.4135 -0.0514 0.0087  -0.0260 67  TYR A OH  
513  N N   . LEU A 68  ? 0.5124 0.6368 0.4455 -0.0539 0.0126  -0.0470 68  LEU A N   
514  C CA  . LEU A 68  ? 0.5331 0.6575 0.4636 -0.0526 0.0140  -0.0523 68  LEU A CA  
515  C C   . LEU A 68  ? 0.5433 0.6741 0.4709 -0.0558 0.0154  -0.0558 68  LEU A C   
516  O O   . LEU A 68  ? 0.5697 0.7014 0.4966 -0.0535 0.0172  -0.0607 68  LEU A O   
517  C CB  . LEU A 68  ? 0.5406 0.6617 0.4690 -0.0538 0.0132  -0.0510 68  LEU A CB  
518  C CG  . LEU A 68  ? 0.5541 0.6685 0.4851 -0.0503 0.0123  -0.0482 68  LEU A CG  
519  C CD1 . LEU A 68  ? 0.5439 0.6562 0.4734 -0.0529 0.0109  -0.0451 68  LEU A CD1 
520  C CD2 . LEU A 68  ? 0.5424 0.6528 0.4742 -0.0446 0.0136  -0.0525 68  LEU A CD2 
521  N N   . ALA A 69  ? 0.5653 0.7005 0.4916 -0.0610 0.0146  -0.0530 69  ALA A N   
522  C CA  . ALA A 69  ? 0.5734 0.7150 0.4968 -0.0646 0.0159  -0.0558 69  ALA A CA  
523  C C   . ALA A 69  ? 0.6048 0.7500 0.5306 -0.0629 0.0170  -0.0577 69  ALA A C   
524  O O   . ALA A 69  ? 0.5768 0.7259 0.5011 -0.0631 0.0189  -0.0620 69  ALA A O   
525  C CB  . ALA A 69  ? 0.5475 0.6926 0.4688 -0.0707 0.0145  -0.0518 69  ALA A CB  
526  N N   . CYS A 70  ? 0.5914 0.7352 0.5208 -0.0614 0.0159  -0.0545 70  CYS A N   
527  C CA  . CYS A 70  ? 0.5296 0.6759 0.4616 -0.0594 0.0166  -0.0561 70  CYS A CA  
528  C C   . CYS A 70  ? 0.5142 0.6584 0.4475 -0.0540 0.0181  -0.0608 70  CYS A C   
529  O O   . CYS A 70  ? 0.5437 0.6909 0.4788 -0.0525 0.0190  -0.0629 70  CYS A O   
530  C CB  . CYS A 70  ? 0.4786 0.6230 0.4137 -0.0591 0.0150  -0.0515 70  CYS A CB  
531  S SG  . CYS A 70  ? 0.5623 0.7107 0.4966 -0.0654 0.0136  -0.0464 70  CYS A SG  
532  N N   . GLY A 71  ? 0.4852 0.6245 0.4176 -0.0512 0.0184  -0.0623 71  GLY A N   
533  C CA  . GLY A 71  ? 0.4769 0.6143 0.4100 -0.0463 0.0199  -0.0670 71  GLY A CA  
534  C C   . GLY A 71  ? 0.5171 0.6476 0.4527 -0.0413 0.0192  -0.0661 71  GLY A C   
535  O O   . GLY A 71  ? 0.4700 0.5987 0.4065 -0.0369 0.0203  -0.0698 71  GLY A O   
536  N N   . ILE A 72  ? 0.5158 0.6425 0.4526 -0.0416 0.0174  -0.0614 72  ILE A N   
537  C CA  . ILE A 72  ? 0.5160 0.6356 0.4547 -0.0370 0.0168  -0.0605 72  ILE A CA  
538  C C   . ILE A 72  ? 0.5162 0.6323 0.4532 -0.0352 0.0174  -0.0626 72  ILE A C   
539  O O   . ILE A 72  ? 0.5221 0.6378 0.4569 -0.0382 0.0168  -0.0610 72  ILE A O   
540  C CB  . ILE A 72  ? 0.4794 0.5954 0.4197 -0.0377 0.0150  -0.0547 72  ILE A CB  
541  C CG1 . ILE A 72  ? 0.5103 0.6289 0.4524 -0.0389 0.0145  -0.0527 72  ILE A CG1 
542  C CG2 . ILE A 72  ? 0.5052 0.6138 0.4471 -0.0330 0.0147  -0.0538 72  ILE A CG2 
543  C CD1 . ILE A 72  ? 0.4953 0.6142 0.4391 -0.0354 0.0153  -0.0559 72  ILE A CD1 
544  N N   . ASP A 73  ? 0.5308 0.6441 0.4686 -0.0305 0.0184  -0.0662 73  ASP A N   
545  C CA  . ASP A 73  ? 0.5584 0.6684 0.4946 -0.0283 0.0193  -0.0691 73  ASP A CA  
546  C C   . ASP A 73  ? 0.6120 0.7149 0.5495 -0.0254 0.0181  -0.0663 73  ASP A C   
547  O O   . ASP A 73  ? 0.6043 0.7040 0.5443 -0.0216 0.0179  -0.0658 73  ASP A O   
548  C CB  . ASP A 73  ? 0.5853 0.6965 0.5221 -0.0246 0.0211  -0.0743 73  ASP A CB  
549  C CG  . ASP A 73  ? 0.6600 0.7675 0.5954 -0.0218 0.0221  -0.0776 73  ASP A CG  
550  O OD1 . ASP A 73  ? 0.7153 0.8245 0.6506 -0.0195 0.0239  -0.0820 73  ASP A OD1 
551  O OD2 . ASP A 73  ? 0.7124 0.8152 0.6467 -0.0217 0.0213  -0.0758 73  ASP A OD2 
552  N N   . PRO A 74  ? 0.5913 0.6916 0.5271 -0.0272 0.0174  -0.0644 74  PRO A N   
553  C CA  . PRO A 74  ? 0.5974 0.6911 0.5345 -0.0246 0.0165  -0.0616 74  PRO A CA  
554  C C   . PRO A 74  ? 0.5808 0.6697 0.5184 -0.0193 0.0174  -0.0649 74  PRO A C   
555  O O   . PRO A 74  ? 0.5488 0.6321 0.4877 -0.0165 0.0168  -0.0628 74  PRO A O   
556  C CB  . PRO A 74  ? 0.5976 0.6912 0.5326 -0.0285 0.0155  -0.0591 74  PRO A CB  
557  C CG  . PRO A 74  ? 0.6144 0.7127 0.5460 -0.0317 0.0166  -0.0627 74  PRO A CG  
558  C CD  . PRO A 74  ? 0.5993 0.7028 0.5317 -0.0319 0.0175  -0.0646 74  PRO A CD  
559  N N   . GLU A 75  ? 0.5811 0.6723 0.5177 -0.0178 0.0190  -0.0700 75  GLU A N   
560  C CA  . GLU A 75  ? 0.6104 0.6975 0.5476 -0.0127 0.0200  -0.0734 75  GLU A CA  
561  C C   . GLU A 75  ? 0.5821 0.6688 0.5221 -0.0088 0.0202  -0.0743 75  GLU A C   
562  O O   . GLU A 75  ? 0.6534 0.7354 0.5946 -0.0043 0.0203  -0.0753 75  GLU A O   
563  C CB  . GLU A 75  ? 0.6000 0.6893 0.5346 -0.0129 0.0218  -0.0784 75  GLU A CB  
564  N N   . LYS A 76  ? 0.6133 0.7050 0.5543 -0.0107 0.0200  -0.0737 76  LYS A N   
565  C CA  . LYS A 76  ? 0.6188 0.7107 0.5623 -0.0078 0.0199  -0.0742 76  LYS A CA  
566  C C   . LYS A 76  ? 0.5517 0.6408 0.4968 -0.0082 0.0184  -0.0694 76  LYS A C   
567  O O   . LYS A 76  ? 0.5693 0.6541 0.5158 -0.0046 0.0180  -0.0688 76  LYS A O   
568  C CB  . LYS A 76  ? 0.6598 0.7589 0.6036 -0.0095 0.0209  -0.0768 76  LYS A CB  
569  C CG  . LYS A 76  ? 0.7571 0.8591 0.6998 -0.0086 0.0228  -0.0817 76  LYS A CG  
570  C CD  . LYS A 76  ? 0.8084 0.9069 0.7525 -0.0031 0.0236  -0.0848 76  LYS A CD  
571  C CE  . LYS A 76  ? 0.8371 0.9299 0.7795 -0.0013 0.0239  -0.0856 76  LYS A CE  
572  N NZ  . LYS A 76  ? 0.8782 0.9678 0.8220 0.0041  0.0246  -0.0886 76  LYS A NZ  
573  N N   . SER A 77  ? 0.5077 0.5991 0.4522 -0.0125 0.0176  -0.0660 77  SER A N   
574  C CA  . SER A 77  ? 0.4566 0.5454 0.4023 -0.0133 0.0163  -0.0611 77  SER A CA  
575  C C   . SER A 77  ? 0.4601 0.5440 0.4055 -0.0136 0.0155  -0.0575 77  SER A C   
576  O O   . SER A 77  ? 0.4515 0.5356 0.3953 -0.0149 0.0157  -0.0583 77  SER A O   
577  C CB  . SER A 77  ? 0.4373 0.5319 0.3829 -0.0180 0.0158  -0.0593 77  SER A CB  
578  O OG  . SER A 77  ? 0.3928 0.4918 0.3391 -0.0176 0.0164  -0.0622 77  SER A OG  
579  N N   . THR A 78  ? 0.4269 0.5064 0.3738 -0.0126 0.0147  -0.0534 78  THR A N   
580  C CA  . THR A 78  ? 0.3889 0.4642 0.3363 -0.0131 0.0140  -0.0491 78  THR A CA  
581  C C   . THR A 78  ? 0.4163 0.4951 0.3639 -0.0178 0.0131  -0.0449 78  THR A C   
582  O O   . THR A 78  ? 0.4060 0.4853 0.3546 -0.0185 0.0128  -0.0428 78  THR A O   
583  C CB  . THR A 78  ? 0.3870 0.4552 0.3359 -0.0088 0.0139  -0.0470 78  THR A CB  
584  O OG1 . THR A 78  ? 0.4034 0.4684 0.3521 -0.0044 0.0147  -0.0509 78  THR A OG1 
585  C CG2 . THR A 78  ? 0.3931 0.4571 0.3429 -0.0092 0.0133  -0.0423 78  THR A CG2 
586  N N   . ILE A 79  ? 0.4109 0.4920 0.3573 -0.0213 0.0126  -0.0437 79  ILE A N   
587  C CA  . ILE A 79  ? 0.4096 0.4940 0.3562 -0.0262 0.0116  -0.0393 79  ILE A CA  
588  C C   . ILE A 79  ? 0.3761 0.4571 0.3234 -0.0268 0.0108  -0.0351 79  ILE A C   
589  O O   . ILE A 79  ? 0.3897 0.4693 0.3358 -0.0263 0.0109  -0.0367 79  ILE A O   
590  C CB  . ILE A 79  ? 0.3946 0.4864 0.3389 -0.0306 0.0118  -0.0417 79  ILE A CB  
591  C CG1 . ILE A 79  ? 0.4260 0.5213 0.3705 -0.0356 0.0106  -0.0371 79  ILE A CG1 
592  C CG2 . ILE A 79  ? 0.4163 0.5088 0.3581 -0.0313 0.0122  -0.0448 79  ILE A CG2 
593  C CD1 . ILE A 79  ? 0.4471 0.5496 0.3897 -0.0397 0.0109  -0.0390 79  ILE A CD1 
594  N N   . PHE A 80  ? 0.3357 0.4152 0.2850 -0.0279 0.0100  -0.0297 80  PHE A N   
595  C CA  . PHE A 80  ? 0.3474 0.4233 0.2983 -0.0279 0.0093  -0.0249 80  PHE A CA  
596  C C   . PHE A 80  ? 0.3248 0.4014 0.2778 -0.0304 0.0085  -0.0190 80  PHE A C   
597  O O   . PHE A 80  ? 0.3849 0.4634 0.3382 -0.0312 0.0086  -0.0187 80  PHE A O   
598  C CB  . PHE A 80  ? 0.3761 0.4447 0.3283 -0.0224 0.0100  -0.0251 80  PHE A CB  
599  C CG  . PHE A 80  ? 0.3367 0.4013 0.2907 -0.0193 0.0105  -0.0234 80  PHE A CG  
600  C CD1 . PHE A 80  ? 0.3244 0.3897 0.2777 -0.0176 0.0112  -0.0270 80  PHE A CD1 
601  C CD2 . PHE A 80  ? 0.3172 0.3773 0.2736 -0.0182 0.0104  -0.0181 80  PHE A CD2 
602  C CE1 . PHE A 80  ? 0.3346 0.3960 0.2890 -0.0152 0.0116  -0.0256 80  PHE A CE1 
603  C CE2 . PHE A 80  ? 0.3463 0.4022 0.3039 -0.0155 0.0111  -0.0167 80  PHE A CE2 
604  C CZ  . PHE A 80  ? 0.3676 0.4239 0.3239 -0.0139 0.0116  -0.0206 80  PHE A CZ  
605  N N   . VAL A 81  ? 0.3427 0.4178 0.2972 -0.0317 0.0076  -0.0143 81  VAL A N   
606  C CA  . VAL A 81  ? 0.3611 0.4366 0.3181 -0.0339 0.0069  -0.0079 81  VAL A CA  
607  C C   . VAL A 81  ? 0.3776 0.4461 0.3374 -0.0294 0.0077  -0.0050 81  VAL A C   
608  O O   . VAL A 81  ? 0.3594 0.4235 0.3199 -0.0262 0.0081  -0.0052 81  VAL A O   
609  C CB  . VAL A 81  ? 0.3728 0.4510 0.3302 -0.0381 0.0054  -0.0040 81  VAL A CB  
610  C CG1 . VAL A 81  ? 0.3643 0.4427 0.3248 -0.0401 0.0046  0.0029  81  VAL A CG1 
611  C CG2 . VAL A 81  ? 0.3910 0.4757 0.3450 -0.0427 0.0047  -0.0071 81  VAL A CG2 
612  N N   . GLN A 82  ? 0.3360 0.4037 0.2972 -0.0293 0.0080  -0.0021 82  GLN A N   
613  C CA  . GLN A 82  ? 0.3282 0.3891 0.2914 -0.0252 0.0090  0.0004  82  GLN A CA  
614  C C   . GLN A 82  ? 0.3200 0.3768 0.2859 -0.0236 0.0090  0.0049  82  GLN A C   
615  O O   . GLN A 82  ? 0.3019 0.3526 0.2685 -0.0192 0.0101  0.0046  82  GLN A O   
616  C CB  . GLN A 82  ? 0.3087 0.3702 0.2730 -0.0268 0.0091  0.0037  82  GLN A CB  
617  C CG  . GLN A 82  ? 0.2929 0.3474 0.2580 -0.0226 0.0105  0.0049  82  GLN A CG  
618  C CD  . GLN A 82  ? 0.3313 0.3857 0.2976 -0.0243 0.0106  0.0089  82  GLN A CD  
619  O OE1 . GLN A 82  ? 0.3696 0.4292 0.3365 -0.0287 0.0096  0.0115  82  GLN A OE1 
620  N NE2 . GLN A 82  ? 0.3139 0.3624 0.2803 -0.0211 0.0118  0.0094  82  GLN A NE2 
621  N N   . SER A 83  ? 0.3201 0.3804 0.2875 -0.0274 0.0078  0.0093  83  SER A N   
622  C CA  . SER A 83  ? 0.3277 0.3849 0.2983 -0.0265 0.0077  0.0144  83  SER A CA  
623  C C   . SER A 83  ? 0.3148 0.3696 0.2848 -0.0243 0.0077  0.0121  83  SER A C   
624  O O   . SER A 83  ? 0.3481 0.3993 0.3209 -0.0226 0.0078  0.0159  83  SER A O   
625  C CB  . SER A 83  ? 0.3261 0.3883 0.2985 -0.0315 0.0061  0.0198  83  SER A CB  
626  O OG  . SER A 83  ? 0.3162 0.3837 0.2863 -0.0354 0.0047  0.0174  83  SER A OG  
627  N N   . HIS A 84  ? 0.3173 0.3740 0.2841 -0.0244 0.0075  0.0061  84  HIS A N   
628  C CA  . HIS A 84  ? 0.3301 0.3845 0.2958 -0.0224 0.0076  0.0032  84  HIS A CA  
629  C C   . HIS A 84  ? 0.3477 0.3954 0.3135 -0.0164 0.0092  0.0007  84  HIS A C   
630  O O   . HIS A 84  ? 0.3532 0.3980 0.3186 -0.0141 0.0094  -0.0012 84  HIS A O   
631  C CB  . HIS A 84  ? 0.3502 0.4092 0.3122 -0.0249 0.0070  -0.0023 84  HIS A CB  
632  C CG  . HIS A 84  ? 0.3839 0.4494 0.3451 -0.0309 0.0054  -0.0003 84  HIS A CG  
633  N ND1 . HIS A 84  ? 0.3761 0.4456 0.3338 -0.0337 0.0048  -0.0045 84  HIS A ND1 
634  C CD2 . HIS A 84  ? 0.3781 0.4465 0.3413 -0.0345 0.0043  0.0053  84  HIS A CD2 
635  C CE1 . HIS A 84  ? 0.3804 0.4549 0.3377 -0.0390 0.0034  -0.0016 84  HIS A CE1 
636  N NE2 . HIS A 84  ? 0.4235 0.4976 0.3842 -0.0396 0.0030  0.0045  84  HIS A NE2 
637  N N   . VAL A 85  ? 0.3099 0.3548 0.2761 -0.0141 0.0103  0.0009  85  VAL A N   
638  C CA  . VAL A 85  ? 0.3005 0.3388 0.2664 -0.0086 0.0117  -0.0013 85  VAL A CA  
639  C C   . VAL A 85  ? 0.2953 0.3284 0.2639 -0.0065 0.0127  0.0040  85  VAL A C   
640  O O   . VAL A 85  ? 0.3389 0.3718 0.3073 -0.0068 0.0132  0.0048  85  VAL A O   
641  C CB  . VAL A 85  ? 0.3037 0.3432 0.2669 -0.0077 0.0122  -0.0068 85  VAL A CB  
642  C CG1 . VAL A 85  ? 0.3109 0.3436 0.2735 -0.0022 0.0135  -0.0093 85  VAL A CG1 
643  C CG2 . VAL A 85  ? 0.3039 0.3488 0.2647 -0.0101 0.0114  -0.0116 85  VAL A CG2 
644  N N   . PRO A 86  ? 0.3377 0.3667 0.3087 -0.0045 0.0131  0.0077  86  PRO A N   
645  C CA  . PRO A 86  ? 0.3170 0.3412 0.2908 -0.0025 0.0143  0.0132  86  PRO A CA  
646  C C   . PRO A 86  ? 0.3189 0.3373 0.2913 0.0014  0.0160  0.0115  86  PRO A C   
647  O O   . PRO A 86  ? 0.3174 0.3325 0.2914 0.0022  0.0170  0.0156  86  PRO A O   
648  C CB  . PRO A 86  ? 0.3343 0.3549 0.3104 -0.0002 0.0147  0.0157  86  PRO A CB  
649  C CG  . PRO A 86  ? 0.3407 0.3662 0.3159 -0.0031 0.0130  0.0135  86  PRO A CG  
650  C CD  . PRO A 86  ? 0.3190 0.3477 0.2904 -0.0039 0.0126  0.0071  86  PRO A CD  
651  N N   . GLU A 87  ? 0.3049 0.2633 0.3100 -0.0212 -0.0058 -0.0358 87  GLU A N   
652  C CA  . GLU A 87  ? 0.3189 0.2816 0.3271 -0.0197 -0.0058 -0.0382 87  GLU A CA  
653  C C   . GLU A 87  ? 0.3006 0.2663 0.3171 -0.0205 -0.0086 -0.0382 87  GLU A C   
654  O O   . GLU A 87  ? 0.3163 0.2850 0.3374 -0.0199 -0.0093 -0.0409 87  GLU A O   
655  C CB  . GLU A 87  ? 0.3534 0.3168 0.3542 -0.0176 -0.0034 -0.0375 87  GLU A CB  
656  C CG  . GLU A 87  ? 0.3599 0.3216 0.3539 -0.0166 -0.0006 -0.0385 87  GLU A CG  
657  C CD  . GLU A 87  ? 0.3902 0.3472 0.3771 -0.0170 0.0006  -0.0359 87  GLU A CD  
658  O OE1 . GLU A 87  ? 0.3645 0.3188 0.3523 -0.0186 -0.0009 -0.0338 87  GLU A OE1 
659  O OE2 . GLU A 87  ? 0.4911 0.4469 0.4714 -0.0158 0.0029  -0.0360 87  GLU A OE2 
660  N N   . HIS A 88  ? 0.2892 0.2540 0.3073 -0.0216 -0.0101 -0.0352 88  HIS A N   
661  C CA  . HIS A 88  ? 0.2821 0.2498 0.3084 -0.0224 -0.0129 -0.0345 88  HIS A CA  
662  C C   . HIS A 88  ? 0.3082 0.2770 0.3433 -0.0239 -0.0150 -0.0370 88  HIS A C   
663  O O   . HIS A 88  ? 0.3453 0.3172 0.3864 -0.0236 -0.0166 -0.0390 88  HIS A O   
664  C CB  . HIS A 88  ? 0.2745 0.2412 0.3002 -0.0233 -0.0139 -0.0304 88  HIS A CB  
665  C CG  . HIS A 88  ? 0.2800 0.2464 0.2983 -0.0215 -0.0121 -0.0278 88  HIS A CG  
666  N ND1 . HIS A 88  ? 0.2891 0.2585 0.3098 -0.0207 -0.0133 -0.0256 88  HIS A ND1 
667  C CD2 . HIS A 88  ? 0.2903 0.2539 0.2989 -0.0201 -0.0092 -0.0268 88  HIS A CD2 
668  C CE1 . HIS A 88  ? 0.3182 0.2867 0.3310 -0.0190 -0.0110 -0.0232 88  HIS A CE1 
669  N NE2 . HIS A 88  ? 0.2867 0.2516 0.2920 -0.0186 -0.0085 -0.0240 88  HIS A NE2 
670  N N   . ALA A 89  ? 0.3056 0.2717 0.3414 -0.0255 -0.0150 -0.0369 89  ALA A N   
671  C CA  . ALA A 89  ? 0.2839 0.2507 0.3277 -0.0269 -0.0166 -0.0391 89  ALA A CA  
672  C C   . ALA A 89  ? 0.2981 0.2660 0.3419 -0.0254 -0.0154 -0.0431 89  ALA A C   
673  O O   . ALA A 89  ? 0.2742 0.2442 0.3250 -0.0256 -0.0169 -0.0455 89  ALA A O   
674  C CB  . ALA A 89  ? 0.2828 0.2462 0.3261 -0.0289 -0.0165 -0.0375 89  ALA A CB  
675  N N   . GLN A 90  ? 0.2675 0.2341 0.3034 -0.0240 -0.0128 -0.0436 90  GLN A N   
676  C CA  . GLN A 90  ? 0.2891 0.2571 0.3239 -0.0223 -0.0114 -0.0471 90  GLN A CA  
677  C C   . GLN A 90  ? 0.3062 0.2778 0.3439 -0.0209 -0.0122 -0.0494 90  GLN A C   
678  O O   . GLN A 90  ? 0.3582 0.3315 0.4006 -0.0205 -0.0128 -0.0526 90  GLN A O   
679  C CB  . GLN A 90  ? 0.2915 0.2578 0.3170 -0.0209 -0.0085 -0.0466 90  GLN A CB  
680  C CG  . GLN A 90  ? 0.2855 0.2481 0.3082 -0.0221 -0.0078 -0.0452 90  GLN A CG  
681  C CD  . GLN A 90  ? 0.3225 0.2835 0.3362 -0.0207 -0.0051 -0.0447 90  GLN A CD  
682  O OE1 . GLN A 90  ? 0.3473 0.3063 0.3550 -0.0206 -0.0042 -0.0422 90  GLN A OE1 
683  N NE2 . GLN A 90  ? 0.3278 0.2899 0.3405 -0.0194 -0.0037 -0.0470 90  GLN A NE2 
684  N N   . LEU A 91  ? 0.2680 0.2408 0.3028 -0.0202 -0.0121 -0.0476 91  LEU A N   
685  C CA  . LEU A 91  ? 0.2668 0.2428 0.3042 -0.0192 -0.0131 -0.0492 91  LEU A CA  
686  C C   . LEU A 91  ? 0.2637 0.2412 0.3104 -0.0205 -0.0165 -0.0496 91  LEU A C   
687  O O   . LEU A 91  ? 0.3069 0.2865 0.3575 -0.0199 -0.0176 -0.0524 91  LEU A O   
688  C CB  . LEU A 91  ? 0.2842 0.2613 0.3160 -0.0181 -0.0121 -0.0467 91  LEU A CB  
689  C CG  . LEU A 91  ? 0.2948 0.2753 0.3284 -0.0170 -0.0129 -0.0482 91  LEU A CG  
690  C CD1 . LEU A 91  ? 0.2904 0.2720 0.3230 -0.0158 -0.0116 -0.0523 91  LEU A CD1 
691  C CD2 . LEU A 91  ? 0.3134 0.2948 0.3413 -0.0159 -0.0116 -0.0452 91  LEU A CD2 
692  N N   . GLY A 92  ? 0.2730 0.2494 0.3230 -0.0222 -0.0180 -0.0469 92  GLY A N   
693  C CA  . GLY A 92  ? 0.3032 0.2807 0.3627 -0.0238 -0.0211 -0.0469 92  GLY A CA  
694  C C   . GLY A 92  ? 0.3366 0.3144 0.4018 -0.0240 -0.0218 -0.0508 92  GLY A C   
695  O O   . GLY A 92  ? 0.3643 0.3440 0.4356 -0.0239 -0.0239 -0.0528 92  GLY A O   
696  N N   . TRP A 93  ? 0.3267 0.3024 0.3900 -0.0242 -0.0201 -0.0518 93  TRP A N   
697  C CA  . TRP A 93  ? 0.3410 0.3168 0.4094 -0.0241 -0.0204 -0.0552 93  TRP A CA  
698  C C   . TRP A 93  ? 0.3589 0.3365 0.4260 -0.0220 -0.0199 -0.0589 93  TRP A C   
699  O O   . TRP A 93  ? 0.3265 0.3053 0.3998 -0.0219 -0.0217 -0.0615 93  TRP A O   
700  C CB  . TRP A 93  ? 0.3233 0.2966 0.3891 -0.0244 -0.0185 -0.0552 93  TRP A CB  
701  C CG  . TRP A 93  ? 0.3144 0.2883 0.3849 -0.0238 -0.0186 -0.0586 93  TRP A CG  
702  C CD1 . TRP A 93  ? 0.3325 0.3069 0.3997 -0.0217 -0.0167 -0.0616 93  TRP A CD1 
703  C CD2 . TRP A 93  ? 0.3340 0.3083 0.4137 -0.0250 -0.0207 -0.0596 93  TRP A CD2 
704  N NE1 . TRP A 93  ? 0.3393 0.3141 0.4127 -0.0214 -0.0175 -0.0644 93  TRP A NE1 
705  C CE2 . TRP A 93  ? 0.3375 0.3122 0.4187 -0.0234 -0.0199 -0.0633 93  TRP A CE2 
706  C CE3 . TRP A 93  ? 0.3604 0.3349 0.4474 -0.0272 -0.0232 -0.0576 93  TRP A CE3 
707  C CZ2 . TRP A 93  ? 0.3602 0.3350 0.4495 -0.0240 -0.0214 -0.0650 93  TRP A CZ2 
708  C CZ3 . TRP A 93  ? 0.3504 0.3254 0.4461 -0.0279 -0.0247 -0.0594 93  TRP A CZ3 
709  C CH2 . TRP A 93  ? 0.3438 0.3188 0.4404 -0.0263 -0.0238 -0.0631 93  TRP A CH2 
710  N N   . ALA A 94  ? 0.3284 0.3063 0.3876 -0.0203 -0.0176 -0.0592 94  ALA A N   
711  C CA  . ALA A 94  ? 0.3888 0.3686 0.4462 -0.0184 -0.0169 -0.0626 94  ALA A CA  
712  C C   . ALA A 94  ? 0.3856 0.3675 0.4473 -0.0185 -0.0196 -0.0633 94  ALA A C   
713  O O   . ALA A 94  ? 0.4144 0.3974 0.4790 -0.0176 -0.0204 -0.0668 94  ALA A O   
714  C CB  . ALA A 94  ? 0.3687 0.3489 0.4171 -0.0168 -0.0140 -0.0620 94  ALA A CB  
715  N N   . LEU A 95  ? 0.3480 0.3304 0.4105 -0.0194 -0.0209 -0.0599 95  LEU A N   
716  C CA  . LEU A 95  ? 0.3798 0.3643 0.4463 -0.0196 -0.0237 -0.0598 95  LEU A CA  
717  C C   . LEU A 95  ? 0.3859 0.3705 0.4621 -0.0209 -0.0269 -0.0609 95  LEU A C   
718  O O   . LEU A 95  ? 0.3982 0.3843 0.4785 -0.0209 -0.0294 -0.0622 95  LEU A O   
719  C CB  . LEU A 95  ? 0.3622 0.3474 0.4261 -0.0199 -0.0240 -0.0553 95  LEU A CB  
720  C CG  . LEU A 95  ? 0.3488 0.3344 0.4037 -0.0184 -0.0212 -0.0539 95  LEU A CG  
721  C CD1 . LEU A 95  ? 0.3393 0.3260 0.3933 -0.0186 -0.0221 -0.0495 95  LEU A CD1 
722  C CD2 . LEU A 95  ? 0.3602 0.3476 0.4123 -0.0169 -0.0203 -0.0569 95  LEU A CD2 
723  N N   . ASN A 96  ? 0.3574 0.3404 0.4372 -0.0222 -0.0269 -0.0604 96  ASN A N   
724  C CA  . ASN A 96  ? 0.3701 0.3531 0.4594 -0.0235 -0.0295 -0.0620 96  ASN A CA  
725  C C   . ASN A 96  ? 0.3815 0.3647 0.4725 -0.0221 -0.0298 -0.0668 96  ASN A C   
726  O O   . ASN A 96  ? 0.4085 0.3924 0.5063 -0.0225 -0.0326 -0.0684 96  ASN A O   
727  C CB  . ASN A 96  ? 0.3677 0.3489 0.4597 -0.0250 -0.0288 -0.0608 96  ASN A CB  
728  C CG  . ASN A 96  ? 0.3920 0.3736 0.4894 -0.0272 -0.0309 -0.0570 96  ASN A CG  
729  O OD1 . ASN A 96  ? 0.4466 0.4302 0.5480 -0.0276 -0.0334 -0.0557 96  ASN A OD1 
730  N ND2 . ASN A 96  ? 0.4527 0.4326 0.5507 -0.0286 -0.0300 -0.0551 96  ASN A ND2 
731  N N   . CYS A 97  ? 0.3900 0.3726 0.4747 -0.0205 -0.0269 -0.0689 97  CYS A N   
732  C CA  . CYS A 97  ? 0.4429 0.4255 0.5276 -0.0188 -0.0265 -0.0734 97  CYS A CA  
733  C C   . CYS A 97  ? 0.4492 0.4335 0.5324 -0.0177 -0.0277 -0.0754 97  CYS A C   
734  O O   . CYS A 97  ? 0.5178 0.5022 0.6015 -0.0164 -0.0278 -0.0794 97  CYS A O   
735  C CB  . CYS A 97  ? 0.4565 0.4384 0.5351 -0.0174 -0.0229 -0.0745 97  CYS A CB  
736  S SG  . CYS A 97  ? 0.4390 0.4186 0.5200 -0.0188 -0.0218 -0.0725 97  CYS A SG  
737  N N   . TYR A 98  ? 0.4437 0.4294 0.5250 -0.0182 -0.0286 -0.0725 98  TYR A N   
738  C CA  . TYR A 98  ? 0.4480 0.4354 0.5284 -0.0176 -0.0302 -0.0733 98  TYR A CA  
739  C C   . TYR A 98  ? 0.4433 0.4317 0.5298 -0.0191 -0.0340 -0.0708 98  TYR A C   
740  O O   . TYR A 98  ? 0.4988 0.4886 0.5842 -0.0189 -0.0354 -0.0702 98  TYR A O   
741  C CB  . TYR A 98  ? 0.4592 0.4478 0.5308 -0.0164 -0.0276 -0.0719 98  TYR A CB  
742  C CG  . TYR A 98  ? 0.4840 0.4722 0.5501 -0.0148 -0.0242 -0.0746 98  TYR A CG  
743  C CD1 . TYR A 98  ? 0.4941 0.4832 0.5578 -0.0134 -0.0237 -0.0783 98  TYR A CD1 
744  C CD2 . TYR A 98  ? 0.4198 0.4067 0.4832 -0.0148 -0.0216 -0.0734 98  TYR A CD2 
745  C CE1 . TYR A 98  ? 0.5270 0.5163 0.5861 -0.0117 -0.0207 -0.0806 98  TYR A CE1 
746  C CE2 . TYR A 98  ? 0.4791 0.4659 0.5379 -0.0133 -0.0188 -0.0755 98  TYR A CE2 
747  C CZ  . TYR A 98  ? 0.4713 0.4596 0.5282 -0.0117 -0.0182 -0.0791 98  TYR A CZ  
748  O OH  . TYR A 98  ? 0.4242 0.4129 0.4768 -0.0100 -0.0153 -0.0811 98  TYR A OH  
749  N N   . THR A 99  ? 0.4612 0.4489 0.5541 -0.0207 -0.0356 -0.0691 99  THR A N   
750  C CA  . THR A 99  ? 0.4827 0.4717 0.5825 -0.0222 -0.0392 -0.0664 99  THR A CA  
751  C C   . THR A 99  ? 0.5069 0.4952 0.6156 -0.0230 -0.0419 -0.0693 99  THR A C   
752  O O   . THR A 99  ? 0.5196 0.5064 0.6307 -0.0233 -0.0408 -0.0704 99  THR A O   
753  C CB  . THR A 99  ? 0.4435 0.4327 0.5440 -0.0235 -0.0388 -0.0617 99  THR A CB  
754  O OG1 . THR A 99  ? 0.4167 0.4060 0.5085 -0.0226 -0.0361 -0.0593 99  THR A OG1 
755  C CG2 . THR A 99  ? 0.4419 0.4329 0.5500 -0.0249 -0.0426 -0.0586 99  THR A CG2 
756  N N   . TYR A 100 ? 0.5839 0.5731 0.6972 -0.0232 -0.0454 -0.0702 100 TYR A N   
757  C CA  . TYR A 100 ? 0.6066 0.5950 0.7288 -0.0240 -0.0483 -0.0729 100 TYR A CA  
758  C C   . TYR A 100 ? 0.5830 0.5722 0.7128 -0.0259 -0.0499 -0.0695 100 TYR A C   
759  O O   . TYR A 100 ? 0.5646 0.5556 0.6947 -0.0268 -0.0507 -0.0652 100 TYR A O   
760  C CB  . TYR A 100 ? 0.6251 0.6142 0.7501 -0.0239 -0.0520 -0.0742 100 TYR A CB  
761  C CG  . TYR A 100 ? 0.6708 0.6589 0.7897 -0.0221 -0.0509 -0.0784 100 TYR A CG  
762  C CD1 . TYR A 100 ? 0.6826 0.6685 0.8022 -0.0211 -0.0502 -0.0835 100 TYR A CD1 
763  C CD2 . TYR A 100 ? 0.6782 0.6676 0.7906 -0.0214 -0.0505 -0.0772 100 TYR A CD2 
764  C CE1 . TYR A 100 ? 0.6937 0.6788 0.8076 -0.0194 -0.0492 -0.0873 100 TYR A CE1 
765  C CE2 . TYR A 100 ? 0.6985 0.6872 0.8054 -0.0199 -0.0495 -0.0810 100 TYR A CE2 
766  C CZ  . TYR A 100 ? 0.7137 0.7003 0.8212 -0.0189 -0.0489 -0.0861 100 TYR A CZ  
767  O OH  . TYR A 100 ? 0.7651 0.7513 0.8671 -0.0174 -0.0479 -0.0897 100 TYR A OH  
768  N N   . PHE A 101 ? 0.6685 0.6564 0.8044 -0.0266 -0.0501 -0.0715 101 PHE A N   
769  C CA  . PHE A 101 ? 0.6876 0.6765 0.8326 -0.0287 -0.0521 -0.0688 101 PHE A CA  
770  C C   . PHE A 101 ? 0.6640 0.6553 0.8157 -0.0297 -0.0566 -0.0666 101 PHE A C   
771  O O   . PHE A 101 ? 0.6406 0.6341 0.7965 -0.0312 -0.0580 -0.0623 101 PHE A O   
772  C CB  . PHE A 101 ? 0.7128 0.6999 0.8637 -0.0291 -0.0520 -0.0720 101 PHE A CB  
773  C CG  . PHE A 101 ? 0.7410 0.7294 0.9019 -0.0314 -0.0539 -0.0693 101 PHE A CG  
774  C CD1 . PHE A 101 ? 0.7147 0.7027 0.8758 -0.0325 -0.0516 -0.0671 101 PHE A CD1 
775  C CD2 . PHE A 101 ? 0.7365 0.7265 0.9067 -0.0325 -0.0581 -0.0689 101 PHE A CD2 
776  C CE1 . PHE A 101 ? 0.7009 0.6902 0.8711 -0.0348 -0.0532 -0.0646 101 PHE A CE1 
777  C CE2 . PHE A 101 ? 0.7306 0.7221 0.9102 -0.0346 -0.0598 -0.0664 101 PHE A CE2 
778  C CZ  . PHE A 101 ? 0.7115 0.7028 0.8911 -0.0358 -0.0573 -0.0642 101 PHE A CZ  
779  N N   . GLY A 102 ? 0.7011 0.6922 0.8536 -0.0289 -0.0590 -0.0694 102 GLY A N   
780  C CA  . GLY A 102 ? 0.6957 0.6890 0.8543 -0.0298 -0.0635 -0.0675 102 GLY A CA  
781  C C   . GLY A 102 ? 0.6784 0.6744 0.8344 -0.0300 -0.0640 -0.0621 102 GLY A C   
782  O O   . GLY A 102 ? 0.6686 0.6673 0.8317 -0.0313 -0.0673 -0.0586 102 GLY A O   
783  N N   . GLU A 103 ? 0.6455 0.6411 0.7915 -0.0288 -0.0607 -0.0614 103 GLU A N   
784  C CA  . GLU A 103 ? 0.6394 0.6373 0.7816 -0.0286 -0.0605 -0.0564 103 GLU A CA  
785  C C   . GLU A 103 ? 0.6215 0.6208 0.7663 -0.0298 -0.0599 -0.0520 103 GLU A C   
786  O O   . GLU A 103 ? 0.6724 0.6743 0.8188 -0.0302 -0.0615 -0.0474 103 GLU A O   
787  C CB  . GLU A 103 ? 0.6615 0.6584 0.7921 -0.0269 -0.0566 -0.0569 103 GLU A CB  
788  C CG  . GLU A 103 ? 0.6578 0.6539 0.7849 -0.0258 -0.0572 -0.0605 103 GLU A CG  
789  C CD  . GLU A 103 ? 0.7056 0.7008 0.8220 -0.0241 -0.0530 -0.0617 103 GLU A CD  
790  O OE1 . GLU A 103 ? 0.7388 0.7345 0.8511 -0.0233 -0.0534 -0.0624 103 GLU A OE1 
791  O OE2 . GLU A 103 ? 0.7007 0.6947 0.8127 -0.0238 -0.0493 -0.0620 103 GLU A OE2 
792  N N   . LEU A 104 ? 0.6056 0.6032 0.7508 -0.0304 -0.0576 -0.0533 104 LEU A N   
793  C CA  . LEU A 104 ? 0.5732 0.5718 0.7215 -0.0319 -0.0571 -0.0495 104 LEU A CA  
794  C C   . LEU A 104 ? 0.6249 0.6258 0.7854 -0.0337 -0.0612 -0.0480 104 LEU A C   
795  O O   . LEU A 104 ? 0.6184 0.6218 0.7824 -0.0347 -0.0623 -0.0435 104 LEU A O   
796  C CB  . LEU A 104 ? 0.5378 0.5337 0.6825 -0.0321 -0.0534 -0.0512 104 LEU A CB  
797  C CG  . LEU A 104 ? 0.5258 0.5198 0.6588 -0.0306 -0.0493 -0.0511 104 LEU A CG  
798  C CD1 . LEU A 104 ? 0.5312 0.5226 0.6620 -0.0311 -0.0463 -0.0523 104 LEU A CD1 
799  C CD2 . LEU A 104 ? 0.4904 0.4859 0.6191 -0.0304 -0.0489 -0.0462 104 LEU A CD2 
800  N N   . SER A 105 ? 0.6808 0.6811 0.8478 -0.0340 -0.0633 -0.0517 105 SER A N   
801  C CA  . SER A 105 ? 0.6946 0.6972 0.8738 -0.0357 -0.0674 -0.0506 105 SER A CA  
802  C C   . SER A 105 ? 0.7164 0.7221 0.8992 -0.0356 -0.0715 -0.0477 105 SER A C   
803  O O   . SER A 105 ? 0.7515 0.7603 0.9435 -0.0370 -0.0747 -0.0447 105 SER A O   
804  C CB  . SER A 105 ? 0.6909 0.6914 0.8756 -0.0359 -0.0683 -0.0555 105 SER A CB  
805  O OG  . SER A 105 ? 0.7925 0.7910 0.9728 -0.0343 -0.0686 -0.0595 105 SER A OG  
806  N N   . ARG A 106 ? 0.8090 0.8141 0.9847 -0.0341 -0.0713 -0.0483 106 ARG A N   
807  C CA  . ARG A 106 ? 0.8637 0.8716 1.0419 -0.0339 -0.0750 -0.0452 106 ARG A CA  
808  C C   . ARG A 106 ? 0.8583 0.8696 1.0358 -0.0340 -0.0751 -0.0388 106 ARG A C   
809  O O   . ARG A 106 ? 0.9352 0.9495 1.1162 -0.0339 -0.0784 -0.0354 106 ARG A O   
810  C CB  . ARG A 106 ? 0.8850 0.8913 1.0556 -0.0323 -0.0747 -0.0476 106 ARG A CB  
811  C CG  . ARG A 106 ? 0.8804 0.8855 1.0562 -0.0325 -0.0783 -0.0515 106 ARG A CG  
812  C CD  . ARG A 106 ? 0.8488 0.8523 1.0169 -0.0311 -0.0781 -0.0538 106 ARG A CD  
813  N NE  . ARG A 106 ? 0.8740 0.8739 1.0348 -0.0299 -0.0743 -0.0591 106 ARG A NE  
814  C CZ  . ARG A 106 ? 0.8927 0.8899 1.0563 -0.0299 -0.0743 -0.0643 106 ARG A CZ  
815  N NH1 . ARG A 106 ? 0.8903 0.8877 1.0642 -0.0311 -0.0778 -0.0651 106 ARG A NH1 
816  N NH2 . ARG A 106 ? 0.8675 0.8620 1.0238 -0.0285 -0.0707 -0.0685 106 ARG A NH2 
817  N N   . MET A 107 ? 0.9033 0.9141 1.0762 -0.0340 -0.0715 -0.0372 107 MET A N   
818  C CA  . MET A 107 ? 0.9154 0.9290 1.0873 -0.0341 -0.0712 -0.0313 107 MET A CA  
819  C C   . MET A 107 ? 1.0326 1.0485 1.2145 -0.0360 -0.0731 -0.0291 107 MET A C   
820  O O   . MET A 107 ? 1.1242 1.1383 1.3077 -0.0371 -0.0714 -0.0315 107 MET A O   
821  C CB  . MET A 107 ? 0.8609 0.8720 1.0213 -0.0330 -0.0661 -0.0309 107 MET A CB  
822  C CG  . MET A 107 ? 0.8542 0.8632 1.0047 -0.0312 -0.0639 -0.0330 107 MET A CG  
823  S SD  . MET A 107 ? 0.7785 0.7867 0.9167 -0.0296 -0.0594 -0.0296 107 MET A SD  
824  C CE  . MET A 107 ? 0.8019 0.8081 0.9315 -0.0279 -0.0575 -0.0333 107 MET A CE  
825  N N   . THR A 108 ? 1.0218 1.0421 1.2106 -0.0364 -0.0766 -0.0244 108 THR A N   
826  C CA  . THR A 108 ? 1.0238 1.0476 1.2239 -0.0383 -0.0793 -0.0216 108 THR A CA  
827  C C   . THR A 108 ? 0.9526 0.9747 1.1578 -0.0401 -0.0783 -0.0249 108 THR A C   
828  O O   . THR A 108 ? 0.8580 0.8793 1.0606 -0.0409 -0.0755 -0.0239 108 THR A O   
829  C CB  . THR A 108 ? 1.0940 1.1209 1.2925 -0.0381 -0.0787 -0.0154 108 THR A CB  
830  O OG1 . THR A 108 ? 1.0766 1.1053 1.2711 -0.0363 -0.0797 -0.0122 108 THR A OG1 
831  C CG2 . THR A 108 ? 1.1534 1.1846 1.3632 -0.0397 -0.0816 -0.0119 108 THR A CG2 
832  N N   . TYR A 117 ? 0.8949 0.9117 1.1203 -0.0443 -0.0609 -0.0229 117 TYR A N   
833  C CA  . TYR A 117 ? 0.9196 0.9382 1.1440 -0.0437 -0.0632 -0.0216 117 TYR A CA  
834  C C   . TYR A 117 ? 0.9459 0.9629 1.1650 -0.0444 -0.0627 -0.0232 117 TYR A C   
835  O O   . TYR A 117 ? 0.8941 0.9119 1.1096 -0.0454 -0.0620 -0.0204 117 TYR A O   
836  C CB  . TYR A 117 ? 0.8996 0.9185 1.1283 -0.0422 -0.0660 -0.0234 117 TYR A CB  
837  N N   . ALA A 118 ? 0.9490 0.9634 1.1674 -0.0439 -0.0631 -0.0278 118 ALA A N   
838  C CA  . ALA A 118 ? 0.8728 0.8849 1.0860 -0.0445 -0.0625 -0.0303 118 ALA A CA  
839  C C   . ALA A 118 ? 0.8464 0.8554 1.0566 -0.0455 -0.0594 -0.0323 118 ALA A C   
840  O O   . ALA A 118 ? 0.8674 0.8743 1.0726 -0.0463 -0.0583 -0.0333 118 ALA A O   
841  C CB  . ALA A 118 ? 0.8560 0.8670 1.0696 -0.0433 -0.0645 -0.0344 118 ALA A CB  
842  N N   . GLU A 119 ? 0.8222 0.8306 1.0355 -0.0455 -0.0581 -0.0326 119 GLU A N   
843  C CA  . GLU A 119 ? 0.8436 0.8493 1.0547 -0.0465 -0.0552 -0.0338 119 GLU A CA  
844  C C   . GLU A 119 ? 0.8255 0.8314 1.0323 -0.0482 -0.0535 -0.0299 119 GLU A C   
845  O O   . GLU A 119 ? 0.8675 0.8705 1.0705 -0.0492 -0.0513 -0.0308 119 GLU A O   
846  C CB  . GLU A 119 ? 0.7972 0.8029 1.0132 -0.0461 -0.0545 -0.0340 119 GLU A CB  
847  N N   . ASN A 120 ? 0.8219 0.8308 1.0290 -0.0484 -0.0545 -0.0258 120 ASN A N   
848  C CA  . ASN A 120 ? 0.8219 0.8312 1.0251 -0.0500 -0.0532 -0.0219 120 ASN A CA  
849  C C   . ASN A 120 ? 0.7859 0.7947 0.9843 -0.0506 -0.0538 -0.0213 120 ASN A C   
850  O O   . ASN A 120 ? 0.7346 0.7435 0.9297 -0.0519 -0.0529 -0.0181 120 ASN A O   
851  C CB  . ASN A 120 ? 0.8121 0.8251 1.0185 -0.0499 -0.0538 -0.0177 120 ASN A CB  
852  N N   . ILE A 121 ? 0.7261 0.7344 0.9243 -0.0496 -0.0553 -0.0241 121 ILE A N   
853  C CA  . ILE A 121 ? 0.6553 0.6623 0.8486 -0.0501 -0.0557 -0.0241 121 ILE A CA  
854  C C   . ILE A 121 ? 0.5959 0.5982 0.7841 -0.0510 -0.0535 -0.0272 121 ILE A C   
855  O O   . ILE A 121 ? 0.6614 0.6617 0.8503 -0.0505 -0.0525 -0.0310 121 ILE A O   
856  C CB  . ILE A 121 ? 0.6815 0.6902 0.8764 -0.0488 -0.0584 -0.0255 121 ILE A CB  
857  C CG1 . ILE A 121 ? 0.7182 0.7247 0.9137 -0.0476 -0.0587 -0.0309 121 ILE A CG1 
858  C CG2 . ILE A 121 ? 0.6665 0.6796 0.8664 -0.0478 -0.0606 -0.0221 121 ILE A CG2 
859  C CD1 . ILE A 121 ? 0.7134 0.7196 0.9058 -0.0465 -0.0602 -0.0328 121 ILE A CD1 
860  N N   . ASN A 122 ? 0.5434 0.5439 0.7264 -0.0523 -0.0526 -0.0257 122 ASN A N   
861  C CA  . ASN A 122 ? 0.5192 0.5149 0.6922 -0.0515 -0.0493 -0.0278 122 ASN A CA  
862  C C   . ASN A 122 ? 0.4899 0.4841 0.6561 -0.0483 -0.0484 -0.0314 122 ASN A C   
863  O O   . ASN A 122 ? 0.5205 0.5170 0.6869 -0.0469 -0.0500 -0.0311 122 ASN A O   
864  C CB  . ASN A 122 ? 0.5186 0.5122 0.6833 -0.0523 -0.0474 -0.0244 122 ASN A CB  
865  C CG  . ASN A 122 ? 0.4967 0.4908 0.6541 -0.0505 -0.0474 -0.0225 122 ASN A CG  
866  O OD1 . ASN A 122 ? 0.5225 0.5150 0.6723 -0.0479 -0.0460 -0.0245 122 ASN A OD1 
867  N ND2 . ASN A 122 ? 0.5126 0.5089 0.6720 -0.0517 -0.0487 -0.0183 122 ASN A ND2 
868  N N   . ALA A 123 ? 0.5116 0.5024 0.6722 -0.0473 -0.0458 -0.0345 123 ALA A N   
869  C CA  . ALA A 123 ? 0.5023 0.4916 0.6564 -0.0444 -0.0447 -0.0382 123 ALA A CA  
870  C C   . ALA A 123 ? 0.5283 0.5173 0.6725 -0.0426 -0.0436 -0.0368 123 ALA A C   
871  O O   . ALA A 123 ? 0.5448 0.5338 0.6853 -0.0404 -0.0435 -0.0390 123 ALA A O   
872  C CB  . ALA A 123 ? 0.5405 0.5265 0.6905 -0.0437 -0.0419 -0.0412 123 ALA A CB  
873  N N   . GLY A 124 ? 0.4970 0.4852 0.6368 -0.0435 -0.0428 -0.0330 124 GLY A N   
874  C CA  . GLY A 124 ? 0.5133 0.5013 0.6444 -0.0420 -0.0418 -0.0309 124 GLY A CA  
875  C C   . GLY A 124 ? 0.5153 0.5071 0.6504 -0.0411 -0.0445 -0.0296 124 GLY A C   
876  O O   . GLY A 124 ? 0.4429 0.4347 0.5720 -0.0389 -0.0438 -0.0302 124 GLY A O   
877  N N   . LEU A 125 ? 0.5403 0.5354 0.6858 -0.0428 -0.0475 -0.0276 125 LEU A N   
878  C CA  . LEU A 125 ? 0.5741 0.5734 0.7253 -0.0423 -0.0505 -0.0258 125 LEU A CA  
879  C C   . LEU A 125 ? 0.5843 0.5844 0.7377 -0.0407 -0.0519 -0.0294 125 LEU A C   
880  O O   . LEU A 125 ? 0.7015 0.7041 0.8561 -0.0397 -0.0538 -0.0281 125 LEU A O   
881  C CB  . LEU A 125 ? 0.6403 0.6432 0.8034 -0.0447 -0.0536 -0.0233 125 LEU A CB  
882  C CG  . LEU A 125 ? 0.6849 0.6925 0.8532 -0.0444 -0.0566 -0.0196 125 LEU A CG  
883  C CD1 . LEU A 125 ? 0.7127 0.7200 0.8732 -0.0438 -0.0551 -0.0154 125 LEU A CD1 
884  C CD2 . LEU A 125 ? 0.6802 0.6918 0.8620 -0.0468 -0.0599 -0.0180 125 LEU A CD2 
885  N N   . PHE A 126 ? 0.5843 0.5820 0.7379 -0.0406 -0.0508 -0.0336 126 PHE A N   
886  C CA  . PHE A 126 ? 0.5559 0.5536 0.7108 -0.0392 -0.0518 -0.0376 126 PHE A CA  
887  C C   . PHE A 126 ? 0.5618 0.5571 0.7054 -0.0368 -0.0490 -0.0396 126 PHE A C   
888  O O   . PHE A 126 ? 0.5415 0.5376 0.6843 -0.0353 -0.0501 -0.0413 126 PHE A O   
889  C CB  . PHE A 126 ? 0.5727 0.5692 0.7340 -0.0402 -0.0519 -0.0411 126 PHE A CB  
890  C CG  . PHE A 126 ? 0.5983 0.5942 0.7608 -0.0387 -0.0528 -0.0456 126 PHE A CG  
891  C CD1 . PHE A 126 ? 0.6069 0.5997 0.7626 -0.0371 -0.0500 -0.0494 126 PHE A CD1 
892  C CD2 . PHE A 126 ? 0.6442 0.6427 0.8146 -0.0388 -0.0566 -0.0460 126 PHE A CD2 
893  C CE1 . PHE A 126 ? 0.6391 0.6314 0.7955 -0.0357 -0.0508 -0.0537 126 PHE A CE1 
894  C CE2 . PHE A 126 ? 0.6408 0.6383 0.8118 -0.0375 -0.0576 -0.0502 126 PHE A CE2 
895  C CZ  . PHE A 126 ? 0.6731 0.6675 0.8369 -0.0359 -0.0546 -0.0542 126 PHE A CZ  
896  N N   . ASP A 127 ? 0.4972 0.4896 0.6323 -0.0365 -0.0456 -0.0395 127 ASP A N   
897  C CA  . ASP A 127 ? 0.4760 0.4661 0.6011 -0.0344 -0.0426 -0.0419 127 ASP A CA  
898  C C   . ASP A 127 ? 0.4318 0.4217 0.5477 -0.0331 -0.0409 -0.0389 127 ASP A C   
899  O O   . ASP A 127 ? 0.3989 0.3874 0.5068 -0.0313 -0.0387 -0.0406 127 ASP A O   
900  C CB  . ASP A 127 ? 0.4955 0.4823 0.6171 -0.0348 -0.0398 -0.0438 127 ASP A CB  
901  C CG  . ASP A 127 ? 0.4879 0.4730 0.6031 -0.0327 -0.0375 -0.0477 127 ASP A CG  
902  O OD1 . ASP A 127 ? 0.5157 0.5021 0.6313 -0.0313 -0.0386 -0.0499 127 ASP A OD1 
903  O OD2 . ASP A 127 ? 0.5332 0.5158 0.6432 -0.0325 -0.0348 -0.0484 127 ASP A OD2 
904  N N   . TYR A 128 ? 0.3933 0.3845 0.5103 -0.0340 -0.0419 -0.0345 128 TYR A N   
905  C CA  . TYR A 128 ? 0.4067 0.3972 0.5146 -0.0328 -0.0400 -0.0314 128 TYR A CA  
906  C C   . TYR A 128 ? 0.3963 0.3881 0.4997 -0.0305 -0.0398 -0.0315 128 TYR A C   
907  O O   . TYR A 128 ? 0.4287 0.4191 0.5227 -0.0291 -0.0372 -0.0302 128 TYR A O   
908  C CB  . TYR A 128 ? 0.3899 0.3820 0.5005 -0.0339 -0.0413 -0.0265 128 TYR A CB  
909  C CG  . TYR A 128 ? 0.4673 0.4638 0.5853 -0.0338 -0.0448 -0.0241 128 TYR A CG  
910  C CD1 . TYR A 128 ? 0.4678 0.4670 0.5976 -0.0356 -0.0481 -0.0241 128 TYR A CD1 
911  C CD2 . TYR A 128 ? 0.4690 0.4670 0.5826 -0.0319 -0.0448 -0.0218 128 TYR A CD2 
912  C CE1 . TYR A 128 ? 0.4694 0.4728 0.6064 -0.0355 -0.0516 -0.0218 128 TYR A CE1 
913  C CE2 . TYR A 128 ? 0.4516 0.4537 0.5722 -0.0318 -0.0481 -0.0192 128 TYR A CE2 
914  C CZ  . TYR A 128 ? 0.4439 0.4487 0.5762 -0.0336 -0.0516 -0.0193 128 TYR A CZ  
915  O OH  . TYR A 128 ? 0.4576 0.4666 0.5972 -0.0335 -0.0552 -0.0167 128 TYR A OH  
916  N N   . PRO A 129 ? 0.3974 0.3918 0.5072 -0.0303 -0.0426 -0.0329 129 PRO A N   
917  C CA  . PRO A 129 ? 0.4318 0.4273 0.5369 -0.0284 -0.0424 -0.0327 129 PRO A CA  
918  C C   . PRO A 129 ? 0.4075 0.4006 0.5040 -0.0269 -0.0391 -0.0362 129 PRO A C   
919  O O   . PRO A 129 ? 0.4196 0.4130 0.5095 -0.0253 -0.0377 -0.0352 129 PRO A O   
920  C CB  . PRO A 129 ? 0.4168 0.4151 0.5313 -0.0288 -0.0465 -0.0339 129 PRO A CB  
921  C CG  . PRO A 129 ? 0.4074 0.4071 0.5314 -0.0309 -0.0490 -0.0322 129 PRO A CG  
922  C CD  . PRO A 129 ? 0.4045 0.4012 0.5261 -0.0318 -0.0464 -0.0337 129 PRO A CD  
923  N N   . VAL A 130 ? 0.3744 0.3652 0.4710 -0.0274 -0.0378 -0.0398 130 VAL A N   
924  C CA  . VAL A 130 ? 0.3934 0.3822 0.4825 -0.0260 -0.0347 -0.0430 130 VAL A CA  
925  C C   . VAL A 130 ? 0.3785 0.3651 0.4583 -0.0254 -0.0313 -0.0407 130 VAL A C   
926  O O   . VAL A 130 ? 0.3722 0.3582 0.4444 -0.0239 -0.0289 -0.0414 130 VAL A O   
927  C CB  . VAL A 130 ? 0.4147 0.4019 0.5074 -0.0266 -0.0345 -0.0473 130 VAL A CB  
928  C CG1 . VAL A 130 ? 0.4294 0.4149 0.5144 -0.0250 -0.0313 -0.0504 130 VAL A CG1 
929  C CG2 . VAL A 130 ? 0.4208 0.4097 0.5221 -0.0269 -0.0377 -0.0498 130 VAL A CG2 
930  N N   . LEU A 131 ? 0.4099 0.3953 0.4905 -0.0268 -0.0313 -0.0380 131 LEU A N   
931  C CA  . LEU A 131 ? 0.3834 0.3665 0.4554 -0.0264 -0.0286 -0.0354 131 LEU A CA  
932  C C   . LEU A 131 ? 0.3695 0.3539 0.4364 -0.0248 -0.0280 -0.0322 131 LEU A C   
933  O O   . LEU A 131 ? 0.3534 0.3363 0.4116 -0.0234 -0.0251 -0.0317 131 LEU A O   
934  C CB  . LEU A 131 ? 0.3753 0.3570 0.4500 -0.0284 -0.0292 -0.0328 131 LEU A CB  
935  C CG  . LEU A 131 ? 0.3872 0.3656 0.4529 -0.0283 -0.0266 -0.0303 131 LEU A CG  
936  C CD1 . LEU A 131 ? 0.3630 0.3384 0.4216 -0.0275 -0.0236 -0.0330 131 LEU A CD1 
937  C CD2 . LEU A 131 ? 0.4300 0.4074 0.4994 -0.0305 -0.0277 -0.0279 131 LEU A CD2 
938  N N   . MET A 132 ? 0.3698 0.3573 0.4429 -0.0251 -0.0309 -0.0298 132 MET A N   
939  C CA  . MET A 132 ? 0.3433 0.3327 0.4128 -0.0236 -0.0308 -0.0264 132 MET A CA  
940  C C   . MET A 132 ? 0.2999 0.2896 0.3640 -0.0218 -0.0291 -0.0285 132 MET A C   
941  O O   . MET A 132 ? 0.3614 0.3505 0.4175 -0.0203 -0.0265 -0.0265 132 MET A O   
942  C CB  . MET A 132 ? 0.3706 0.3637 0.4490 -0.0242 -0.0347 -0.0237 132 MET A CB  
943  C CG  . MET A 132 ? 0.3964 0.3919 0.4718 -0.0225 -0.0348 -0.0202 132 MET A CG  
944  S SD  . MET A 132 ? 0.4772 0.4770 0.5616 -0.0230 -0.0390 -0.0154 132 MET A SD  
945  C CE  . MET A 132 ? 0.4649 0.4667 0.5436 -0.0206 -0.0382 -0.0117 132 MET A CE  
946  N N   . ALA A 133 ? 0.2823 0.2729 0.3506 -0.0220 -0.0303 -0.0326 133 ALA A N   
947  C CA  . ALA A 133 ? 0.2811 0.2720 0.3446 -0.0206 -0.0287 -0.0351 133 ALA A CA  
948  C C   . ALA A 133 ? 0.3231 0.3113 0.3771 -0.0196 -0.0245 -0.0361 133 ALA A C   
949  O O   . ALA A 133 ? 0.3061 0.2947 0.3532 -0.0181 -0.0223 -0.0349 133 ALA A O   
950  C CB  . ALA A 133 ? 0.3350 0.3266 0.4043 -0.0210 -0.0306 -0.0398 133 ALA A CB  
951  N N   . ALA A 134 ? 0.3219 0.3075 0.3756 -0.0204 -0.0234 -0.0379 134 ALA A N   
952  C CA  . ALA A 134 ? 0.3100 0.2929 0.3552 -0.0196 -0.0198 -0.0384 134 ALA A CA  
953  C C   . ALA A 134 ? 0.2966 0.2782 0.3345 -0.0188 -0.0178 -0.0343 134 ALA A C   
954  O O   . ALA A 134 ? 0.3610 0.3420 0.3913 -0.0174 -0.0149 -0.0341 134 ALA A O   
955  C CB  . ALA A 134 ? 0.3105 0.2910 0.3578 -0.0209 -0.0196 -0.0403 134 ALA A CB  
956  N N   . ASP A 135 ? 0.3119 0.2931 0.3520 -0.0198 -0.0192 -0.0309 135 ASP A N   
957  C CA  . ASP A 135 ? 0.3062 0.2861 0.3397 -0.0189 -0.0175 -0.0267 135 ASP A CA  
958  C C   . ASP A 135 ? 0.3445 0.3263 0.3730 -0.0169 -0.0159 -0.0250 135 ASP A C   
959  O O   . ASP A 135 ? 0.3295 0.3094 0.3493 -0.0156 -0.0128 -0.0235 135 ASP A O   
960  C CB  . ASP A 135 ? 0.3140 0.2948 0.3525 -0.0200 -0.0199 -0.0230 135 ASP A CB  
961  C CG  . ASP A 135 ? 0.3435 0.3225 0.3865 -0.0221 -0.0213 -0.0236 135 ASP A CG  
962  O OD1 . ASP A 135 ? 0.3355 0.3111 0.3747 -0.0227 -0.0195 -0.0255 135 ASP A OD1 
963  O OD2 . ASP A 135 ? 0.3242 0.3053 0.3750 -0.0234 -0.0242 -0.0220 135 ASP A OD2 
964  N N   . ILE A 136 ? 0.3087 0.2941 0.3428 -0.0168 -0.0182 -0.0250 136 ILE A N   
965  C CA  . ILE A 136 ? 0.3108 0.2985 0.3416 -0.0152 -0.0174 -0.0230 136 ILE A CA  
966  C C   . ILE A 136 ? 0.3191 0.3067 0.3446 -0.0141 -0.0147 -0.0262 136 ILE A C   
967  O O   . ILE A 136 ? 0.3214 0.3087 0.3395 -0.0127 -0.0117 -0.0244 136 ILE A O   
968  C CB  . ILE A 136 ? 0.3460 0.3375 0.3851 -0.0156 -0.0212 -0.0221 136 ILE A CB  
969  C CG1 . ILE A 136 ? 0.3552 0.3477 0.3989 -0.0162 -0.0236 -0.0178 136 ILE A CG1 
970  C CG2 . ILE A 136 ? 0.3489 0.3429 0.3850 -0.0142 -0.0205 -0.0205 136 ILE A CG2 
971  C CD1 . ILE A 136 ? 0.3657 0.3616 0.4198 -0.0173 -0.0281 -0.0177 136 ILE A CD1 
972  N N   . LEU A 137 ? 0.3007 0.2885 0.3299 -0.0148 -0.0156 -0.0309 137 LEU A N   
973  C CA  . LEU A 137 ? 0.2786 0.2672 0.3041 -0.0139 -0.0136 -0.0340 137 LEU A CA  
974  C C   . LEU A 137 ? 0.3112 0.2973 0.3286 -0.0130 -0.0097 -0.0348 137 LEU A C   
975  O O   . LEU A 137 ? 0.2930 0.2803 0.3060 -0.0119 -0.0075 -0.0360 137 LEU A O   
976  C CB  . LEU A 137 ? 0.3227 0.3123 0.3546 -0.0147 -0.0158 -0.0386 137 LEU A CB  
977  C CG  . LEU A 137 ? 0.3271 0.3192 0.3673 -0.0155 -0.0199 -0.0384 137 LEU A CG  
978  C CD1 . LEU A 137 ? 0.3559 0.3485 0.4014 -0.0160 -0.0217 -0.0434 137 LEU A CD1 
979  C CD2 . LEU A 137 ? 0.3426 0.3374 0.3813 -0.0147 -0.0203 -0.0353 137 LEU A CD2 
980  N N   . LEU A 138 ? 0.3437 0.3266 0.3593 -0.0136 -0.0090 -0.0339 138 LEU A N   
981  C CA  . LEU A 138 ? 0.3337 0.3138 0.3420 -0.0130 -0.0058 -0.0344 138 LEU A CA  
982  C C   . LEU A 138 ? 0.3359 0.3158 0.3360 -0.0114 -0.0027 -0.0315 138 LEU A C   
983  O O   . LEU A 138 ? 0.3545 0.3338 0.3491 -0.0105 0.0000  -0.0329 138 LEU A O   
984  C CB  . LEU A 138 ? 0.3494 0.3256 0.3571 -0.0142 -0.0061 -0.0332 138 LEU A CB  
985  C CG  . LEU A 138 ? 0.3440 0.3188 0.3560 -0.0157 -0.0072 -0.0362 138 LEU A CG  
986  C CD1 . LEU A 138 ? 0.3741 0.3455 0.3859 -0.0171 -0.0079 -0.0338 138 LEU A CD1 
987  C CD2 . LEU A 138 ? 0.3369 0.3109 0.3447 -0.0149 -0.0048 -0.0391 138 LEU A CD2 
988  N N   . TYR A 139 ? 0.3491 0.3299 0.3489 -0.0110 -0.0033 -0.0275 139 TYR A N   
989  C CA  . TYR A 139 ? 0.3818 0.3622 0.3741 -0.0093 -0.0004 -0.0240 139 TYR A CA  
990  C C   . TYR A 139 ? 0.3967 0.3811 0.3891 -0.0083 0.0000  -0.0230 139 TYR A C   
991  O O   . TYR A 139 ? 0.3852 0.3699 0.3728 -0.0070 0.0019  -0.0192 139 TYR A O   
992  C CB  . TYR A 139 ? 0.3774 0.3558 0.3683 -0.0093 -0.0009 -0.0196 139 TYR A CB  
993  C CG  . TYR A 139 ? 0.3856 0.3600 0.3760 -0.0105 -0.0012 -0.0206 139 TYR A CG  
994  C CD1 . TYR A 139 ? 0.3807 0.3513 0.3635 -0.0100 0.0016  -0.0209 139 TYR A CD1 
995  C CD2 . TYR A 139 ? 0.3684 0.3430 0.3664 -0.0123 -0.0045 -0.0214 139 TYR A CD2 
996  C CE1 . TYR A 139 ? 0.3718 0.3386 0.3542 -0.0114 0.0010  -0.0217 139 TYR A CE1 
997  C CE2 . TYR A 139 ? 0.3716 0.3427 0.3694 -0.0137 -0.0049 -0.0221 139 TYR A CE2 
998  C CZ  . TYR A 139 ? 0.3572 0.3243 0.3471 -0.0133 -0.0022 -0.0222 139 TYR A CZ  
999  O OH  . TYR A 139 ? 0.3758 0.3393 0.3655 -0.0148 -0.0027 -0.0227 139 TYR A OH  
1000 N N   . GLN A 140 ? 0.3836 0.3708 0.3808 -0.0088 -0.0015 -0.0264 140 GLN A N   
1001 C CA  . GLN A 140 ? 0.3778 0.3688 0.3753 -0.0081 -0.0013 -0.0258 140 GLN A CA  
1002 C C   . GLN A 140 ? 0.3942 0.3866 0.3928 -0.0077 -0.0026 -0.0206 140 GLN A C   
1003 O O   . GLN A 140 ? 0.4021 0.3963 0.3969 -0.0066 -0.0008 -0.0176 140 GLN A O   
1004 C CB  . GLN A 140 ? 0.3768 0.3681 0.3670 -0.0068 0.0027  -0.0262 140 GLN A CB  
1005 C CG  . GLN A 140 ? 0.4193 0.4098 0.4084 -0.0070 0.0039  -0.0310 140 GLN A CG  
1006 C CD  . GLN A 140 ? 0.4229 0.4161 0.4178 -0.0076 0.0018  -0.0353 140 GLN A CD  
1007 O OE1 . GLN A 140 ? 0.3768 0.3732 0.3736 -0.0075 0.0009  -0.0348 140 GLN A OE1 
1008 N NE2 . GLN A 140 ? 0.3569 0.3488 0.3546 -0.0083 0.0009  -0.0392 140 GLN A NE2 
1009 N N   . THR A 141 ? 0.3637 0.3555 0.3678 -0.0087 -0.0056 -0.0194 141 THR A N   
1010 C CA  . THR A 141 ? 0.3676 0.3606 0.3732 -0.0083 -0.0070 -0.0141 141 THR A CA  
1011 C C   . THR A 141 ? 0.3611 0.3583 0.3703 -0.0081 -0.0088 -0.0125 141 THR A C   
1012 O O   . THR A 141 ? 0.3919 0.3908 0.4063 -0.0091 -0.0111 -0.0159 141 THR A O   
1013 C CB  . THR A 141 ? 0.3482 0.3404 0.3604 -0.0096 -0.0104 -0.0138 141 THR A CB  
1014 O OG1 . THR A 141 ? 0.3309 0.3191 0.3393 -0.0098 -0.0086 -0.0148 141 THR A OG1 
1015 C CG2 . THR A 141 ? 0.3131 0.3071 0.3277 -0.0091 -0.0121 -0.0083 141 THR A CG2 
1016 N N   . ASN A 142 ? 0.3222 0.3207 0.3282 -0.0068 -0.0076 -0.0073 142 ASN A N   
1017 C CA  . ASN A 142 ? 0.3399 0.3424 0.3492 -0.0067 -0.0095 -0.0044 142 ASN A CA  
1018 C C   . ASN A 142 ? 0.3583 0.3623 0.3749 -0.0073 -0.0137 -0.0012 142 ASN A C   
1019 O O   . ASN A 142 ? 0.3679 0.3745 0.3914 -0.0084 -0.0173 -0.0019 142 ASN A O   
1020 C CB  . ASN A 142 ? 0.3382 0.3416 0.3404 -0.0050 -0.0059 -0.0001 142 ASN A CB  
1021 C CG  . ASN A 142 ? 0.3555 0.3579 0.3511 -0.0045 -0.0018 -0.0032 142 ASN A CG  
1022 O OD1 . ASN A 142 ? 0.3540 0.3536 0.3428 -0.0034 0.0016  -0.0024 142 ASN A OD1 
1023 N ND2 . ASN A 142 ? 0.3949 0.3991 0.3923 -0.0053 -0.0025 -0.0070 142 ASN A ND2 
1024 N N   . LEU A 143 ? 0.3845 0.3871 0.3999 -0.0066 -0.0132 0.0023  143 LEU A N   
1025 C CA  . LEU A 143 ? 0.3801 0.3847 0.4017 -0.0068 -0.0167 0.0067  143 LEU A CA  
1026 C C   . LEU A 143 ? 0.3826 0.3851 0.4075 -0.0077 -0.0181 0.0055  143 LEU A C   
1027 O O   . LEU A 143 ? 0.3256 0.3246 0.3447 -0.0073 -0.0153 0.0045  143 LEU A O   
1028 C CB  . LEU A 143 ? 0.4014 0.4071 0.4181 -0.0047 -0.0145 0.0134  143 LEU A CB  
1029 C CG  . LEU A 143 ? 0.4143 0.4226 0.4286 -0.0038 -0.0134 0.0158  143 LEU A CG  
1030 C CD1 . LEU A 143 ? 0.4133 0.4217 0.4205 -0.0015 -0.0098 0.0220  143 LEU A CD1 
1031 C CD2 . LEU A 143 ? 0.4473 0.4596 0.4701 -0.0049 -0.0181 0.0171  143 LEU A CD2 
1032 N N   . VAL A 144 ? 0.3896 0.3942 0.4238 -0.0091 -0.0226 0.0054  144 VAL A N   
1033 C CA  . VAL A 144 ? 0.4016 0.4049 0.4400 -0.0101 -0.0243 0.0051  144 VAL A CA  
1034 C C   . VAL A 144 ? 0.4297 0.4365 0.4744 -0.0098 -0.0275 0.0106  144 VAL A C   
1035 O O   . VAL A 144 ? 0.4503 0.4604 0.5028 -0.0106 -0.0314 0.0110  144 VAL A O   
1036 C CB  . VAL A 144 ? 0.3983 0.4010 0.4433 -0.0122 -0.0267 -0.0007 144 VAL A CB  
1037 C CG1 . VAL A 144 ? 0.3922 0.3933 0.4406 -0.0134 -0.0278 -0.0010 144 VAL A CG1 
1038 C CG2 . VAL A 144 ? 0.4182 0.4183 0.4577 -0.0123 -0.0238 -0.0059 144 VAL A CG2 
1039 N N   . PRO A 145 ? 0.4270 0.4331 0.4681 -0.0085 -0.0261 0.0151  145 PRO A N   
1040 C CA  . PRO A 145 ? 0.4760 0.4856 0.5234 -0.0082 -0.0291 0.0204  145 PRO A CA  
1041 C C   . PRO A 145 ? 0.5326 0.5431 0.5896 -0.0104 -0.0330 0.0182  145 PRO A C   
1042 O O   . PRO A 145 ? 0.6090 0.6166 0.6645 -0.0112 -0.0319 0.0162  145 PRO A O   
1043 C CB  . PRO A 145 ? 0.4779 0.4855 0.5175 -0.0062 -0.0258 0.0247  145 PRO A CB  
1044 C CG  . PRO A 145 ? 0.4961 0.4995 0.5250 -0.0053 -0.0210 0.0222  145 PRO A CG  
1045 C CD  . PRO A 145 ? 0.4569 0.4590 0.4880 -0.0073 -0.0215 0.0154  145 PRO A CD  
1046 N N   . VAL A 146 ? 0.5801 0.5944 0.6468 -0.0114 -0.0374 0.0186  146 VAL A N   
1047 C CA  . VAL A 146 ? 0.6259 0.6413 0.7025 -0.0136 -0.0412 0.0163  146 VAL A CA  
1048 C C   . VAL A 146 ? 0.6456 0.6659 0.7312 -0.0135 -0.0454 0.0216  146 VAL A C   
1049 O O   . VAL A 146 ? 0.6325 0.6558 0.7189 -0.0123 -0.0466 0.0254  146 VAL A O   
1050 C CB  . VAL A 146 ? 0.6619 0.6766 0.7430 -0.0154 -0.0429 0.0101  146 VAL A CB  
1051 C CG1 . VAL A 146 ? 0.6975 0.7075 0.7713 -0.0157 -0.0392 0.0048  146 VAL A CG1 
1052 C CG2 . VAL A 146 ? 0.6575 0.6745 0.7399 -0.0150 -0.0446 0.0106  146 VAL A CG2 
1053 N N   . GLY A 147 ? 0.6533 0.6748 0.7460 -0.0149 -0.0478 0.0219  147 GLY A N   
1054 C CA  . GLY A 147 ? 0.6762 0.7030 0.7800 -0.0153 -0.0526 0.0259  147 GLY A CA  
1055 C C   . GLY A 147 ? 0.6408 0.6691 0.7541 -0.0173 -0.0568 0.0221  147 GLY A C   
1056 O O   . GLY A 147 ? 0.7155 0.7407 0.8266 -0.0183 -0.0557 0.0164  147 GLY A O   
1057 N N   . GLU A 148 ? 0.6768 0.7098 0.8007 -0.0179 -0.0616 0.0253  148 GLU A N   
1058 C CA  . GLU A 148 ? 0.6944 0.7289 0.8277 -0.0197 -0.0659 0.0221  148 GLU A CA  
1059 C C   . GLU A 148 ? 0.7380 0.7703 0.8762 -0.0220 -0.0666 0.0162  148 GLU A C   
1060 O O   . GLU A 148 ? 0.7832 0.8142 0.9245 -0.0232 -0.0681 0.0114  148 GLU A O   
1061 C CB  . GLU A 148 ? 0.7233 0.7635 0.8671 -0.0198 -0.0711 0.0275  148 GLU A CB  
1062 N N   . ASP A 149 ? 0.8225 0.8543 0.9612 -0.0226 -0.0653 0.0167  149 ASP A N   
1063 C CA  . ASP A 149 ? 0.8023 0.8318 0.9445 -0.0248 -0.0651 0.0116  149 ASP A CA  
1064 C C   . ASP A 149 ? 0.7369 0.7611 0.8713 -0.0250 -0.0617 0.0054  149 ASP A C   
1065 O O   . ASP A 149 ? 0.6867 0.7094 0.8255 -0.0267 -0.0625 0.0006  149 ASP A O   
1066 C CB  . ASP A 149 ? 0.8720 0.9016 1.0144 -0.0254 -0.0639 0.0138  149 ASP A CB  
1067 C CG  . ASP A 149 ? 0.9621 0.9891 1.0924 -0.0235 -0.0594 0.0163  149 ASP A CG  
1068 O OD1 . ASP A 149 ? 1.0305 1.0542 1.1562 -0.0241 -0.0566 0.0146  149 ASP A OD1 
1069 O OD2 . ASP A 149 ? 1.0804 1.1087 1.2059 -0.0213 -0.0586 0.0201  149 ASP A OD2 
1070 N N   . GLN A 150 ? 0.6724 0.6944 0.7959 -0.0231 -0.0581 0.0057  150 GLN A N   
1071 C CA  . GLN A 150 ? 0.6483 0.6657 0.7636 -0.0230 -0.0544 0.0005  150 GLN A CA  
1072 C C   . GLN A 150 ? 0.6395 0.6566 0.7511 -0.0220 -0.0542 -0.0012 150 GLN A C   
1073 O O   . GLN A 150 ? 0.5716 0.5854 0.6750 -0.0213 -0.0508 -0.0046 150 GLN A O   
1074 C CB  . GLN A 150 ? 0.6278 0.6420 0.7326 -0.0219 -0.0498 0.0016  150 GLN A CB  
1075 C CG  . GLN A 150 ? 0.5979 0.6099 0.7040 -0.0235 -0.0490 -0.0001 150 GLN A CG  
1076 C CD  . GLN A 150 ? 0.5818 0.5913 0.6788 -0.0226 -0.0453 0.0024  150 GLN A CD  
1077 O OE1 . GLN A 150 ? 0.5915 0.6011 0.6817 -0.0205 -0.0434 0.0058  150 GLN A OE1 
1078 N NE2 . GLN A 150 ? 0.6046 0.6116 0.7014 -0.0240 -0.0443 0.0007  150 GLN A NE2 
1079 N N   . LYS A 151 ? 0.6431 0.6636 0.7608 -0.0219 -0.0580 0.0011  151 LYS A N   
1080 C CA  . LYS A 151 ? 0.6158 0.6363 0.7308 -0.0212 -0.0584 -0.0001 151 LYS A CA  
1081 C C   . LYS A 151 ? 0.5917 0.6099 0.7087 -0.0225 -0.0591 -0.0070 151 LYS A C   
1082 O O   . LYS A 151 ? 0.6358 0.6521 0.7465 -0.0218 -0.0570 -0.0100 151 LYS A O   
1083 C CB  . LYS A 151 ? 0.6707 0.6956 0.7923 -0.0210 -0.0627 0.0047  151 LYS A CB  
1084 C CG  . LYS A 151 ? 0.7004 0.7277 0.8180 -0.0191 -0.0616 0.0119  151 LYS A CG  
1085 C CD  . LYS A 151 ? 0.7150 0.7420 0.8247 -0.0177 -0.0595 0.0133  151 LYS A CD  
1086 N N   . GLN A 152 ? 0.5384 0.5570 0.6645 -0.0241 -0.0621 -0.0093 152 GLN A N   
1087 C CA  . GLN A 152 ? 0.5851 0.6013 0.7137 -0.0252 -0.0627 -0.0158 152 GLN A CA  
1088 C C   . GLN A 152 ? 0.5699 0.5820 0.6900 -0.0248 -0.0578 -0.0201 152 GLN A C   
1089 O O   . GLN A 152 ? 0.4958 0.5058 0.6128 -0.0246 -0.0568 -0.0248 152 GLN A O   
1090 C CB  . GLN A 152 ? 0.6572 0.6747 0.7972 -0.0271 -0.0663 -0.0167 152 GLN A CB  
1091 C CG  . GLN A 152 ? 0.7015 0.7171 0.8461 -0.0281 -0.0681 -0.0227 152 GLN A CG  
1092 C CD  . GLN A 152 ? 0.6733 0.6905 0.8299 -0.0299 -0.0720 -0.0230 152 GLN A CD  
1093 O OE1 . GLN A 152 ? 0.6971 0.7162 0.8580 -0.0306 -0.0724 -0.0199 152 GLN A OE1 
1094 N NE2 . GLN A 152 ? 0.6973 0.7138 0.8594 -0.0305 -0.0749 -0.0269 152 GLN A NE2 
1095 N N   . HIS A 153 ? 0.4829 0.4941 0.5989 -0.0246 -0.0549 -0.0180 153 HIS A N   
1096 C CA  . HIS A 153 ? 0.4727 0.4802 0.5809 -0.0243 -0.0505 -0.0211 153 HIS A CA  
1097 C C   . HIS A 153 ? 0.4306 0.4367 0.5285 -0.0226 -0.0471 -0.0218 153 HIS A C   
1098 O O   . HIS A 153 ? 0.3981 0.4017 0.4916 -0.0224 -0.0447 -0.0262 153 HIS A O   
1099 C CB  . HIS A 153 ? 0.4748 0.4815 0.5807 -0.0246 -0.0486 -0.0180 153 HIS A CB  
1100 C CG  . HIS A 153 ? 0.5307 0.5390 0.6465 -0.0264 -0.0515 -0.0171 153 HIS A CG  
1101 N ND1 . HIS A 153 ? 0.5264 0.5386 0.6498 -0.0268 -0.0552 -0.0129 153 HIS A ND1 
1102 C CD2 . HIS A 153 ? 0.4981 0.5047 0.6174 -0.0280 -0.0513 -0.0195 153 HIS A CD2 
1103 C CE1 . HIS A 153 ? 0.5253 0.5384 0.6569 -0.0286 -0.0571 -0.0130 153 HIS A CE1 
1104 N NE2 . HIS A 153 ? 0.5161 0.5258 0.6452 -0.0294 -0.0547 -0.0169 153 HIS A NE2 
1105 N N   . LEU A 154 ? 0.4644 0.4724 0.5587 -0.0213 -0.0468 -0.0172 154 LEU A N   
1106 C CA  . LEU A 154 ? 0.4763 0.4836 0.5615 -0.0198 -0.0437 -0.0172 154 LEU A CA  
1107 C C   . LEU A 154 ? 0.4752 0.4827 0.5617 -0.0199 -0.0451 -0.0212 154 LEU A C   
1108 O O   . LEU A 154 ? 0.4725 0.4783 0.5524 -0.0192 -0.0422 -0.0243 154 LEU A O   
1109 C CB  . LEU A 154 ? 0.4824 0.4921 0.5647 -0.0184 -0.0435 -0.0108 154 LEU A CB  
1110 C CG  . LEU A 154 ? 0.5294 0.5386 0.6022 -0.0168 -0.0399 -0.0100 154 LEU A CG  
1111 C CD1 . LEU A 154 ? 0.5073 0.5129 0.5711 -0.0161 -0.0350 -0.0123 154 LEU A CD1 
1112 C CD2 . LEU A 154 ? 0.5132 0.5249 0.5840 -0.0154 -0.0399 -0.0033 154 LEU A CD2 
1113 N N   . GLU A 155 ? 0.5238 0.5333 0.6187 -0.0209 -0.0496 -0.0213 155 GLU A N   
1114 C CA  . GLU A 155 ? 0.5589 0.5683 0.6553 -0.0212 -0.0513 -0.0253 155 GLU A CA  
1115 C C   . GLU A 155 ? 0.5132 0.5197 0.6090 -0.0216 -0.0498 -0.0318 155 GLU A C   
1116 O O   . GLU A 155 ? 0.5663 0.5717 0.6575 -0.0210 -0.0484 -0.0353 155 GLU A O   
1117 C CB  . GLU A 155 ? 0.6058 0.6175 0.7119 -0.0223 -0.0569 -0.0240 155 GLU A CB  
1118 C CG  . GLU A 155 ? 0.6913 0.7033 0.7970 -0.0223 -0.0588 -0.0262 155 GLU A CG  
1119 C CD  . GLU A 155 ? 0.7394 0.7526 0.8375 -0.0210 -0.0568 -0.0229 155 GLU A CD  
1120 O OE1 . GLU A 155 ? 0.7436 0.7587 0.8400 -0.0203 -0.0560 -0.0170 155 GLU A OE1 
1121 O OE2 . GLU A 155 ? 0.7386 0.7509 0.8322 -0.0208 -0.0557 -0.0260 155 GLU A OE2 
1122 N N   . LEU A 156 ? 0.4622 0.4674 0.5622 -0.0225 -0.0501 -0.0331 156 LEU A N   
1123 C CA  . LEU A 156 ? 0.4722 0.4745 0.5711 -0.0228 -0.0481 -0.0386 156 LEU A CA  
1124 C C   . LEU A 156 ? 0.4616 0.4621 0.5501 -0.0215 -0.0431 -0.0397 156 LEU A C   
1125 O O   . LEU A 156 ? 0.4944 0.4935 0.5797 -0.0209 -0.0415 -0.0442 156 LEU A O   
1126 C CB  . LEU A 156 ? 0.4768 0.4784 0.5819 -0.0241 -0.0489 -0.0388 156 LEU A CB  
1127 C CG  . LEU A 156 ? 0.4681 0.4670 0.5738 -0.0245 -0.0475 -0.0440 156 LEU A CG  
1128 C CD1 . LEU A 156 ? 0.4999 0.4985 0.6090 -0.0244 -0.0496 -0.0485 156 LEU A CD1 
1129 C CD2 . LEU A 156 ? 0.5005 0.4991 0.6129 -0.0261 -0.0484 -0.0434 156 LEU A CD2 
1130 N N   . SER A 157 ? 0.4213 0.4219 0.5046 -0.0208 -0.0408 -0.0356 157 SER A N   
1131 C CA  . SER A 157 ? 0.4121 0.4111 0.4852 -0.0195 -0.0361 -0.0358 157 SER A CA  
1132 C C   . SER A 157 ? 0.4119 0.4120 0.4804 -0.0184 -0.0352 -0.0371 157 SER A C   
1133 O O   . SER A 157 ? 0.3870 0.3859 0.4500 -0.0177 -0.0322 -0.0402 157 SER A O   
1134 C CB  . SER A 157 ? 0.4008 0.3998 0.4696 -0.0190 -0.0343 -0.0306 157 SER A CB  
1135 O OG  . SER A 157 ? 0.4680 0.4665 0.5419 -0.0202 -0.0357 -0.0291 157 SER A OG  
1136 N N   . ARG A 158 ? 0.3980 0.4005 0.4691 -0.0184 -0.0378 -0.0344 158 ARG A N   
1137 C CA  . ARG A 158 ? 0.4045 0.4083 0.4718 -0.0177 -0.0373 -0.0351 158 ARG A CA  
1138 C C   . ARG A 158 ? 0.3878 0.3908 0.4572 -0.0180 -0.0384 -0.0410 158 ARG A C   
1139 O O   . ARG A 158 ? 0.3645 0.3673 0.4281 -0.0172 -0.0358 -0.0436 158 ARG A O   
1140 C CB  . ARG A 158 ? 0.3972 0.4038 0.4675 -0.0178 -0.0403 -0.0303 158 ARG A CB  
1141 C CG  . ARG A 158 ? 0.4617 0.4694 0.5289 -0.0170 -0.0388 -0.0241 158 ARG A CG  
1142 C CD  . ARG A 158 ? 0.5272 0.5379 0.5994 -0.0172 -0.0424 -0.0189 158 ARG A CD  
1143 N NE  . ARG A 158 ? 0.5744 0.5865 0.6481 -0.0176 -0.0447 -0.0200 158 ARG A NE  
1144 C CZ  . ARG A 158 ? 0.5276 0.5404 0.5950 -0.0168 -0.0426 -0.0194 158 ARG A CZ  
1145 N NH1 . ARG A 158 ? 0.5427 0.5551 0.6020 -0.0155 -0.0380 -0.0176 158 ARG A NH1 
1146 N NH2 . ARG A 158 ? 0.5641 0.5780 0.6334 -0.0175 -0.0452 -0.0206 158 ARG A NH2 
1147 N N   . ASP A 159 ? 0.4013 0.4040 0.4790 -0.0192 -0.0422 -0.0432 159 ASP A N   
1148 C CA  . ASP A 159 ? 0.4745 0.4759 0.5544 -0.0194 -0.0433 -0.0491 159 ASP A CA  
1149 C C   . ASP A 159 ? 0.4703 0.4696 0.5457 -0.0187 -0.0395 -0.0531 159 ASP A C   
1150 O O   . ASP A 159 ? 0.4584 0.4572 0.5305 -0.0179 -0.0382 -0.0571 159 ASP A O   
1151 C CB  . ASP A 159 ? 0.4810 0.4820 0.5710 -0.0208 -0.0478 -0.0505 159 ASP A CB  
1152 C CG  . ASP A 159 ? 0.5065 0.5099 0.6021 -0.0216 -0.0523 -0.0468 159 ASP A CG  
1153 O OD1 . ASP A 159 ? 0.5165 0.5215 0.6084 -0.0211 -0.0524 -0.0443 159 ASP A OD1 
1154 O OD2 . ASP A 159 ? 0.5419 0.5456 0.6458 -0.0227 -0.0558 -0.0461 159 ASP A OD2 
1155 N N   . ILE A 160 ? 0.4588 0.4567 0.5342 -0.0189 -0.0378 -0.0519 160 ILE A N   
1156 C CA  . ILE A 160 ? 0.4878 0.4838 0.5592 -0.0183 -0.0343 -0.0551 160 ILE A CA  
1157 C C   . ILE A 160 ? 0.4291 0.4254 0.4913 -0.0169 -0.0305 -0.0553 160 ILE A C   
1158 O O   . ILE A 160 ? 0.4764 0.4721 0.5357 -0.0160 -0.0286 -0.0592 160 ILE A O   
1159 C CB  . ILE A 160 ? 0.4815 0.4758 0.5541 -0.0191 -0.0334 -0.0531 160 ILE A CB  
1160 C CG1 . ILE A 160 ? 0.5226 0.5164 0.6045 -0.0205 -0.0366 -0.0545 160 ILE A CG1 
1161 C CG2 . ILE A 160 ? 0.5062 0.4986 0.5728 -0.0183 -0.0294 -0.0551 160 ILE A CG2 
1162 C CD1 . ILE A 160 ? 0.5074 0.5008 0.5924 -0.0217 -0.0369 -0.0511 160 ILE A CD1 
1163 N N   . ALA A 161 ? 0.4435 0.4411 0.5013 -0.0165 -0.0293 -0.0509 161 ALA A N   
1164 C CA  . ALA A 161 ? 0.4738 0.4720 0.5231 -0.0151 -0.0255 -0.0504 161 ALA A CA  
1165 C C   . ALA A 161 ? 0.4717 0.4714 0.5196 -0.0146 -0.0257 -0.0535 161 ALA A C   
1166 O O   . ALA A 161 ? 0.4535 0.4533 0.4963 -0.0136 -0.0228 -0.0559 161 ALA A O   
1167 C CB  . ALA A 161 ? 0.4915 0.4908 0.5371 -0.0148 -0.0245 -0.0448 161 ALA A CB  
1168 N N   . GLN A 162 ? 0.4796 0.4806 0.5323 -0.0153 -0.0294 -0.0531 162 GLN A N   
1169 C CA  . GLN A 162 ? 0.4917 0.4941 0.5436 -0.0151 -0.0304 -0.0558 162 GLN A CA  
1170 C C   . GLN A 162 ? 0.4837 0.4847 0.5370 -0.0148 -0.0305 -0.0619 162 GLN A C   
1171 O O   . GLN A 162 ? 0.5213 0.5231 0.5703 -0.0139 -0.0287 -0.0647 162 GLN A O   
1172 C CB  . GLN A 162 ? 0.5508 0.5544 0.6080 -0.0162 -0.0349 -0.0535 162 GLN A CB  
1173 C CG  . GLN A 162 ? 0.5655 0.5711 0.6209 -0.0162 -0.0348 -0.0472 162 GLN A CG  
1174 C CD  . GLN A 162 ? 0.5978 0.6049 0.6589 -0.0172 -0.0395 -0.0446 162 GLN A CD  
1175 O OE1 . GLN A 162 ? 0.6031 0.6121 0.6617 -0.0172 -0.0398 -0.0421 162 GLN A OE1 
1176 N NE2 . GLN A 162 ? 0.5961 0.6024 0.6649 -0.0182 -0.0432 -0.0451 162 GLN A NE2 
1177 N N   . ARG A 163 ? 0.4756 0.4748 0.5351 -0.0155 -0.0326 -0.0638 163 ARG A N   
1178 C CA  . ARG A 163 ? 0.5091 0.5066 0.5703 -0.0151 -0.0325 -0.0693 163 ARG A CA  
1179 C C   . ARG A 163 ? 0.4987 0.4959 0.5537 -0.0137 -0.0280 -0.0711 163 ARG A C   
1180 O O   . ARG A 163 ? 0.4869 0.4845 0.5392 -0.0126 -0.0267 -0.0750 163 ARG A O   
1181 C CB  . ARG A 163 ? 0.5122 0.5079 0.5811 -0.0161 -0.0350 -0.0697 163 ARG A CB  
1182 C CG  . ARG A 163 ? 0.5449 0.5387 0.6166 -0.0157 -0.0351 -0.0749 163 ARG A CG  
1183 C CD  . ARG A 163 ? 0.5786 0.5711 0.6582 -0.0170 -0.0375 -0.0744 163 ARG A CD  
1184 N NE  . ARG A 163 ? 0.5597 0.5530 0.6451 -0.0183 -0.0417 -0.0721 163 ARG A NE  
1185 C CZ  . ARG A 163 ? 0.5700 0.5636 0.6613 -0.0196 -0.0438 -0.0688 163 ARG A CZ  
1186 N NH1 . ARG A 163 ? 0.5450 0.5378 0.6371 -0.0200 -0.0421 -0.0673 163 ARG A NH1 
1187 N NH2 . ARG A 163 ? 0.6092 0.6040 0.7057 -0.0206 -0.0478 -0.0668 163 ARG A NH2 
1188 N N   . PHE A 164 ? 0.4431 0.4397 0.4959 -0.0137 -0.0257 -0.0682 164 PHE A N   
1189 C CA  . PHE A 164 ? 0.4406 0.4369 0.4875 -0.0125 -0.0216 -0.0691 164 PHE A CA  
1190 C C   . PHE A 164 ? 0.4027 0.4012 0.4430 -0.0114 -0.0191 -0.0692 164 PHE A C   
1191 O O   . PHE A 164 ? 0.4823 0.4814 0.5195 -0.0103 -0.0170 -0.0724 164 PHE A O   
1192 C CB  . PHE A 164 ? 0.4055 0.4004 0.4507 -0.0130 -0.0199 -0.0655 164 PHE A CB  
1193 C CG  . PHE A 164 ? 0.3705 0.3643 0.4112 -0.0120 -0.0164 -0.0667 164 PHE A CG  
1194 C CD1 . PHE A 164 ? 0.3738 0.3687 0.4073 -0.0110 -0.0131 -0.0655 164 PHE A CD1 
1195 C CD2 . PHE A 164 ? 0.3714 0.3632 0.4154 -0.0123 -0.0166 -0.0689 164 PHE A CD2 
1196 C CE1 . PHE A 164 ? 0.4081 0.4021 0.4378 -0.0101 -0.0101 -0.0665 164 PHE A CE1 
1197 C CE2 . PHE A 164 ? 0.3633 0.3543 0.4034 -0.0115 -0.0136 -0.0697 164 PHE A CE2 
1198 C CZ  . PHE A 164 ? 0.3931 0.3852 0.4261 -0.0104 -0.0105 -0.0685 164 PHE A CZ  
1199 N N   . ASN A 165 ? 0.4290 0.4291 0.4673 -0.0118 -0.0195 -0.0654 165 ASN A N   
1200 C CA  . ASN A 165 ? 0.4432 0.4458 0.4756 -0.0109 -0.0171 -0.0649 165 ASN A CA  
1201 C C   . ASN A 165 ? 0.4450 0.4491 0.4777 -0.0105 -0.0181 -0.0693 165 ASN A C   
1202 O O   . ASN A 165 ? 0.4151 0.4209 0.4430 -0.0094 -0.0153 -0.0709 165 ASN A O   
1203 C CB  . ASN A 165 ? 0.4508 0.4549 0.4818 -0.0114 -0.0177 -0.0596 165 ASN A CB  
1204 C CG  . ASN A 165 ? 0.4362 0.4394 0.4637 -0.0112 -0.0153 -0.0553 165 ASN A CG  
1205 O OD1 . ASN A 165 ? 0.3711 0.3726 0.3964 -0.0107 -0.0130 -0.0561 165 ASN A OD1 
1206 N ND2 . ASN A 165 ? 0.4074 0.4117 0.4343 -0.0115 -0.0158 -0.0504 165 ASN A ND2 
1207 N N   . ALA A 166 ? 0.4252 0.4284 0.4635 -0.0113 -0.0219 -0.0712 166 ALA A N   
1208 C CA  . ALA A 166 ? 0.4570 0.4611 0.4957 -0.0110 -0.0234 -0.0752 166 ALA A CA  
1209 C C   . ALA A 166 ? 0.4480 0.4515 0.4855 -0.0097 -0.0214 -0.0802 166 ALA A C   
1210 O O   . ALA A 166 ? 0.4521 0.4570 0.4869 -0.0088 -0.0207 -0.0832 166 ALA A O   
1211 C CB  . ALA A 166 ? 0.4419 0.4447 0.4870 -0.0123 -0.0283 -0.0759 166 ALA A CB  
1212 N N   . LEU A 167 ? 0.5026 0.5040 0.5421 -0.0094 -0.0206 -0.0809 167 LEU A N   
1213 C CA  . LEU A 167 ? 0.4952 0.4960 0.5338 -0.0080 -0.0185 -0.0848 167 LEU A CA  
1214 C C   . LEU A 167 ? 0.4721 0.4748 0.5045 -0.0068 -0.0142 -0.0839 167 LEU A C   
1215 O O   . LEU A 167 ? 0.4896 0.4936 0.5194 -0.0054 -0.0124 -0.0871 167 LEU A O   
1216 C CB  . LEU A 167 ? 0.5069 0.5048 0.5507 -0.0085 -0.0196 -0.0853 167 LEU A CB  
1217 C CG  . LEU A 167 ? 0.5455 0.5417 0.5963 -0.0095 -0.0238 -0.0868 167 LEU A CG  
1218 C CD1 . LEU A 167 ? 0.5749 0.5688 0.6312 -0.0106 -0.0249 -0.0854 167 LEU A CD1 
1219 C CD2 . LEU A 167 ? 0.5629 0.5586 0.6145 -0.0084 -0.0246 -0.0922 167 LEU A CD2 
1220 N N   . TYR A 168 ? 0.4419 0.4446 0.4717 -0.0073 -0.0127 -0.0795 168 TYR A N   
1221 C CA  . TYR A 168 ? 0.4670 0.4706 0.4913 -0.0062 -0.0086 -0.0785 168 TYR A CA  
1222 C C   . TYR A 168 ? 0.4638 0.4701 0.4825 -0.0060 -0.0064 -0.0754 168 TYR A C   
1223 O O   . TYR A 168 ? 0.4784 0.4858 0.4926 -0.0051 -0.0031 -0.0746 168 TYR A O   
1224 C CB  . TYR A 168 ? 0.4453 0.4462 0.4707 -0.0067 -0.0081 -0.0763 168 TYR A CB  
1225 C CG  . TYR A 168 ? 0.4365 0.4351 0.4672 -0.0068 -0.0098 -0.0792 168 TYR A CG  
1226 C CD1 . TYR A 168 ? 0.4346 0.4308 0.4709 -0.0083 -0.0126 -0.0780 168 TYR A CD1 
1227 C CD2 . TYR A 168 ? 0.4621 0.4611 0.4926 -0.0054 -0.0084 -0.0829 168 TYR A CD2 
1228 C CE1 . TYR A 168 ? 0.4521 0.4465 0.4937 -0.0085 -0.0140 -0.0805 168 TYR A CE1 
1229 C CE2 . TYR A 168 ? 0.4573 0.4543 0.4928 -0.0054 -0.0097 -0.0853 168 TYR A CE2 
1230 C CZ  . TYR A 168 ? 0.4436 0.4382 0.4846 -0.0070 -0.0125 -0.0841 168 TYR A CZ  
1231 O OH  . TYR A 168 ? 0.4275 0.4201 0.4736 -0.0071 -0.0136 -0.0862 168 TYR A OH  
1232 N N   . GLY A 169 ? 0.4754 0.4903 0.4396 -0.0285 -0.0255 -0.0339 169 GLY A N   
1233 C CA  . GLY A 169 ? 0.4880 0.5082 0.4614 -0.0306 -0.0264 -0.0295 169 GLY A CA  
1234 C C   . GLY A 169 ? 0.4868 0.5147 0.4689 -0.0283 -0.0245 -0.0279 169 GLY A C   
1235 O O   . GLY A 169 ? 0.5033 0.5315 0.4837 -0.0256 -0.0230 -0.0296 169 GLY A O   
1236 N N   . GLU A 170 ? 0.4966 0.5304 0.4880 -0.0296 -0.0245 -0.0245 170 GLU A N   
1237 C CA  . GLU A 170 ? 0.5024 0.5432 0.5025 -0.0284 -0.0235 -0.0221 170 GLU A CA  
1238 C C   . GLU A 170 ? 0.4456 0.4944 0.4517 -0.0239 -0.0185 -0.0254 170 GLU A C   
1239 O O   . GLU A 170 ? 0.4792 0.5351 0.4941 -0.0236 -0.0170 -0.0243 170 GLU A O   
1240 C CB  . GLU A 170 ? 0.5572 0.6005 0.5646 -0.0321 -0.0262 -0.0167 170 GLU A CB  
1241 C CG  . GLU A 170 ? 0.5990 0.6346 0.6007 -0.0366 -0.0311 -0.0132 170 GLU A CG  
1242 C CD  . GLU A 170 ? 0.6548 0.6843 0.6489 -0.0366 -0.0327 -0.0134 170 GLU A CD  
1243 O OE1 . GLU A 170 ? 0.6446 0.6769 0.6420 -0.0356 -0.0323 -0.0120 170 GLU A OE1 
1244 O OE2 . GLU A 170 ? 0.6773 0.6991 0.6619 -0.0376 -0.0342 -0.0151 170 GLU A OE2 
1245 N N   . ILE A 171 ? 0.3722 0.4198 0.3733 -0.0204 -0.0162 -0.0296 171 ILE A N   
1246 C CA  . ILE A 171 ? 0.3570 0.4113 0.3622 -0.0159 -0.0114 -0.0334 171 ILE A CA  
1247 C C   . ILE A 171 ? 0.3499 0.4107 0.3628 -0.0143 -0.0101 -0.0314 171 ILE A C   
1248 O O   . ILE A 171 ? 0.3375 0.4066 0.3589 -0.0121 -0.0070 -0.0319 171 ILE A O   
1249 C CB  . ILE A 171 ? 0.3708 0.4207 0.3669 -0.0128 -0.0096 -0.0389 171 ILE A CB  
1250 C CG1 . ILE A 171 ? 0.4258 0.4687 0.4136 -0.0145 -0.0110 -0.0411 171 ILE A CG1 
1251 C CG2 . ILE A 171 ? 0.3365 0.3933 0.3368 -0.0079 -0.0046 -0.0429 171 ILE A CG2 
1252 C CD1 . ILE A 171 ? 0.4341 0.4805 0.4253 -0.0144 -0.0090 -0.0427 171 ILE A CD1 
1253 N N   . PHE A 172 ? 0.3040 0.3610 0.3138 -0.0153 -0.0125 -0.0293 172 PHE A N   
1254 C CA  . PHE A 172 ? 0.3164 0.3785 0.3325 -0.0143 -0.0117 -0.0272 172 PHE A CA  
1255 C C   . PHE A 172 ? 0.3632 0.4263 0.3849 -0.0183 -0.0150 -0.0213 172 PHE A C   
1256 O O   . PHE A 172 ? 0.4099 0.4674 0.4279 -0.0221 -0.0187 -0.0188 172 PHE A O   
1257 C CB  . PHE A 172 ? 0.3421 0.3991 0.3507 -0.0128 -0.0122 -0.0286 172 PHE A CB  
1258 C CG  . PHE A 172 ? 0.3672 0.4232 0.3702 -0.0085 -0.0090 -0.0344 172 PHE A CG  
1259 C CD1 . PHE A 172 ? 0.3349 0.3825 0.3271 -0.0084 -0.0105 -0.0368 172 PHE A CD1 
1260 C CD2 . PHE A 172 ? 0.3070 0.3706 0.3158 -0.0046 -0.0045 -0.0375 172 PHE A CD2 
1261 C CE1 . PHE A 172 ? 0.3756 0.4225 0.3629 -0.0045 -0.0076 -0.0422 172 PHE A CE1 
1262 C CE2 . PHE A 172 ? 0.3136 0.3765 0.3175 -0.0007 -0.0015 -0.0428 172 PHE A CE2 
1263 C CZ  . PHE A 172 ? 0.3390 0.3935 0.3321 -0.0006 -0.0031 -0.0453 172 PHE A CZ  
1264 N N   . LYS A 173 ? 0.3495 0.4198 0.3802 -0.0176 -0.0137 -0.0193 173 LYS A N   
1265 C CA  . LYS A 173 ? 0.3472 0.4179 0.3820 -0.0209 -0.0167 -0.0143 173 LYS A CA  
1266 C C   . LYS A 173 ? 0.3705 0.4361 0.3989 -0.0206 -0.0179 -0.0142 173 LYS A C   
1267 O O   . LYS A 173 ? 0.3567 0.4228 0.3825 -0.0169 -0.0153 -0.0176 173 LYS A O   
1268 C CB  . LYS A 173 ? 0.3790 0.4595 0.4259 -0.0200 -0.0146 -0.0124 173 LYS A CB  
1269 C CG  . LYS A 173 ? 0.4151 0.5018 0.4698 -0.0202 -0.0132 -0.0122 173 LYS A CG  
1270 C CD  . LYS A 173 ? 0.4845 0.5681 0.5397 -0.0247 -0.0171 -0.0086 173 LYS A CD  
1271 C CE  . LYS A 173 ? 0.5173 0.6075 0.5807 -0.0247 -0.0156 -0.0083 173 LYS A CE  
1272 N NZ  . LYS A 173 ? 0.5705 0.6572 0.6336 -0.0290 -0.0194 -0.0051 173 LYS A NZ  
1273 N N   . VAL A 174 ? 0.3323 0.3928 0.3580 -0.0243 -0.0219 -0.0105 174 VAL A N   
1274 C CA  . VAL A 174 ? 0.3576 0.4136 0.3782 -0.0246 -0.0234 -0.0096 174 VAL A CA  
1275 C C   . VAL A 174 ? 0.3410 0.4039 0.3704 -0.0241 -0.0223 -0.0074 174 VAL A C   
1276 O O   . VAL A 174 ? 0.3605 0.4264 0.3965 -0.0270 -0.0240 -0.0035 174 VAL A O   
1277 C CB  . VAL A 174 ? 0.3855 0.4333 0.3997 -0.0290 -0.0282 -0.0065 174 VAL A CB  
1278 C CG1 . VAL A 174 ? 0.4001 0.4430 0.4086 -0.0292 -0.0297 -0.0057 174 VAL A CG1 
1279 C CG2 . VAL A 174 ? 0.4292 0.4705 0.4351 -0.0296 -0.0293 -0.0087 174 VAL A CG2 
1280 N N   . PRO A 175 ? 0.3532 0.4188 0.3830 -0.0205 -0.0193 -0.0098 175 PRO A N   
1281 C CA  . PRO A 175 ? 0.3621 0.4347 0.4005 -0.0199 -0.0179 -0.0079 175 PRO A CA  
1282 C C   . PRO A 175 ? 0.3944 0.4637 0.4320 -0.0233 -0.0213 -0.0038 175 PRO A C   
1283 O O   . PRO A 175 ? 0.4163 0.4772 0.4447 -0.0248 -0.0240 -0.0035 175 PRO A O   
1284 C CB  . PRO A 175 ? 0.3536 0.4279 0.3899 -0.0152 -0.0143 -0.0119 175 PRO A CB  
1285 C CG  . PRO A 175 ? 0.3691 0.4345 0.3935 -0.0146 -0.0155 -0.0145 175 PRO A CG  
1286 C CD  . PRO A 175 ? 0.3806 0.4423 0.4021 -0.0170 -0.0175 -0.0143 175 PRO A CD  
1287 N N   . GLU A 176 ? 0.3801 0.4557 0.4270 -0.0246 -0.0212 -0.0008 176 GLU A N   
1288 C CA  . GLU A 176 ? 0.4168 0.4904 0.4640 -0.0276 -0.0239 0.0029  176 GLU A CA  
1289 C C   . GLU A 176 ? 0.3881 0.4670 0.4401 -0.0254 -0.0214 0.0025  176 GLU A C   
1290 O O   . GLU A 176 ? 0.3626 0.4489 0.4215 -0.0226 -0.0180 0.0008  176 GLU A O   
1291 C CB  . GLU A 176 ? 0.4410 0.5170 0.4952 -0.0318 -0.0265 0.0071  176 GLU A CB  
1292 C CG  . GLU A 176 ? 0.4807 0.5505 0.5296 -0.0347 -0.0298 0.0082  176 GLU A CG  
1293 C CD  . GLU A 176 ? 0.5013 0.5613 0.5394 -0.0366 -0.0329 0.0088  176 GLU A CD  
1294 O OE1 . GLU A 176 ? 0.5364 0.5946 0.5730 -0.0374 -0.0339 0.0103  176 GLU A OE1 
1295 O OE2 . GLU A 176 ? 0.5495 0.6036 0.5806 -0.0374 -0.0345 0.0079  176 GLU A OE2 
1296 N N   . PRO A 177 ? 0.4174 0.4921 0.4653 -0.0265 -0.0230 0.0039  177 PRO A N   
1297 C CA  . PRO A 177 ? 0.4193 0.4989 0.4722 -0.0251 -0.0210 0.0042  177 PRO A CA  
1298 C C   . PRO A 177 ? 0.4259 0.5134 0.4907 -0.0273 -0.0210 0.0074  177 PRO A C   
1299 O O   . PRO A 177 ? 0.4108 0.4977 0.4779 -0.0308 -0.0237 0.0103  177 PRO A O   
1300 C CB  . PRO A 177 ? 0.4454 0.5174 0.4903 -0.0267 -0.0236 0.0055  177 PRO A CB  
1301 C CG  . PRO A 177 ? 0.4515 0.5172 0.4918 -0.0306 -0.0276 0.0079  177 PRO A CG  
1302 C CD  . PRO A 177 ? 0.4351 0.5004 0.4738 -0.0294 -0.0268 0.0056  177 PRO A CD  
1303 N N   . PHE A 178 ? 0.4291 0.5239 0.5012 -0.0252 -0.0180 0.0069  178 PHE A N   
1304 C CA  . PHE A 178 ? 0.4783 0.5809 0.5618 -0.0273 -0.0179 0.0098  178 PHE A CA  
1305 C C   . PHE A 178 ? 0.4991 0.5990 0.5814 -0.0298 -0.0200 0.0125  178 PHE A C   
1306 O O   . PHE A 178 ? 0.5466 0.6474 0.6283 -0.0279 -0.0182 0.0114  178 PHE A O   
1307 C CB  . PHE A 178 ? 0.4614 0.5736 0.5538 -0.0238 -0.0136 0.0078  178 PHE A CB  
1308 C CG  . PHE A 178 ? 0.4633 0.5839 0.5680 -0.0258 -0.0133 0.0105  178 PHE A CG  
1309 C CD1 . PHE A 178 ? 0.4794 0.6040 0.5897 -0.0268 -0.0129 0.0123  178 PHE A CD1 
1310 C CD2 . PHE A 178 ? 0.4684 0.5931 0.5792 -0.0268 -0.0135 0.0112  178 PHE A CD2 
1311 C CE1 . PHE A 178 ? 0.5113 0.6439 0.6332 -0.0287 -0.0128 0.0146  178 PHE A CE1 
1312 C CE2 . PHE A 178 ? 0.4955 0.6281 0.6179 -0.0286 -0.0133 0.0137  178 PHE A CE2 
1313 C CZ  . PHE A 178 ? 0.5050 0.6416 0.6330 -0.0296 -0.0130 0.0153  178 PHE A CZ  
1314 N N   . ILE A 179 ? 0.5273 0.6238 0.6091 -0.0341 -0.0237 0.0159  179 ILE A N   
1315 C CA  . ILE A 179 ? 0.5416 0.6338 0.6203 -0.0369 -0.0263 0.0184  179 ILE A CA  
1316 C C   . ILE A 179 ? 0.5242 0.6234 0.6118 -0.0373 -0.0248 0.0198  179 ILE A C   
1317 O O   . ILE A 179 ? 0.5375 0.6345 0.6215 -0.0367 -0.0243 0.0195  179 ILE A O   
1318 C CB  . ILE A 179 ? 0.5750 0.6620 0.6513 -0.0415 -0.0306 0.0217  179 ILE A CB  
1319 C CG1 . ILE A 179 ? 0.5924 0.6721 0.6596 -0.0413 -0.0322 0.0204  179 ILE A CG1 
1320 C CG2 . ILE A 179 ? 0.5787 0.6610 0.6513 -0.0444 -0.0331 0.0242  179 ILE A CG2 
1321 C CD1 . ILE A 179 ? 0.6125 0.6854 0.6687 -0.0387 -0.0315 0.0175  179 ILE A CD1 
1322 N N   . PRO A 180 ? 0.4863 0.5939 0.5853 -0.0383 -0.0240 0.0213  180 PRO A N   
1323 C CA  . PRO A 180 ? 0.5190 0.6332 0.6268 -0.0393 -0.0230 0.0228  180 PRO A CA  
1324 C C   . PRO A 180 ? 0.5615 0.6793 0.6702 -0.0355 -0.0192 0.0202  180 PRO A C   
1325 O O   . PRO A 180 ? 0.5840 0.7056 0.6943 -0.0318 -0.0161 0.0174  180 PRO A O   
1326 C CB  . PRO A 180 ? 0.5228 0.6455 0.6423 -0.0403 -0.0225 0.0241  180 PRO A CB  
1327 C CG  . PRO A 180 ? 0.5241 0.6423 0.6397 -0.0417 -0.0250 0.0246  180 PRO A CG  
1328 C CD  . PRO A 180 ? 0.4817 0.5929 0.5861 -0.0389 -0.0243 0.0217  180 PRO A CD  
1329 N N   . LYS A 181 ? 0.6373 0.7540 0.7451 -0.0365 -0.0195 0.0213  181 LYS A N   
1330 C CA  . LYS A 181 ? 0.7039 0.8233 0.8121 -0.0333 -0.0163 0.0191  181 LYS A CA  
1331 C C   . LYS A 181 ? 0.7170 0.8470 0.8378 -0.0331 -0.0137 0.0197  181 LYS A C   
1332 O O   . LYS A 181 ? 0.8422 0.9769 0.9715 -0.0362 -0.0150 0.0223  181 LYS A O   
1333 C CB  . LYS A 181 ? 0.6880 0.8004 0.7882 -0.0345 -0.0179 0.0199  181 LYS A CB  
1334 N N   . GLY A 183 ? 0.8749 1.0244 1.0169 -0.0310 -0.0069 0.0193  183 GLY A N   
1335 C CA  . GLY A 183 ? 0.8994 1.0473 1.0427 -0.0353 -0.0096 0.0224  183 GLY A CA  
1336 C C   . GLY A 183 ? 0.8915 1.0398 1.0345 -0.0352 -0.0083 0.0223  183 GLY A C   
1337 O O   . GLY A 183 ? 0.8955 1.0408 1.0374 -0.0388 -0.0107 0.0246  183 GLY A O   
1338 N N   . ALA A 184 ? 0.8519 1.0037 0.9957 -0.0312 -0.0047 0.0195  184 ALA A N   
1339 C CA  . ALA A 184 ? 0.8096 0.9630 0.9542 -0.0307 -0.0030 0.0192  184 ALA A CA  
1340 C C   . ALA A 184 ? 0.8090 0.9531 0.9407 -0.0289 -0.0034 0.0176  184 ALA A C   
1341 O O   . ALA A 184 ? 0.8129 0.9536 0.9380 -0.0255 -0.0025 0.0151  184 ALA A O   
1342 C CB  . ALA A 184 ? 0.7891 0.9522 0.9427 -0.0275 0.0013  0.0172  184 ALA A CB  
1343 N N   . ARG A 185 ? 0.7804 0.9209 0.9090 -0.0310 -0.0046 0.0190  185 ARG A N   
1344 C CA  . ARG A 185 ? 0.7714 0.9031 0.8880 -0.0296 -0.0052 0.0177  185 ARG A CA  
1345 C C   . ARG A 185 ? 0.6981 0.8335 0.8163 -0.0265 -0.0017 0.0156  185 ARG A C   
1346 O O   . ARG A 185 ? 0.7431 0.8819 0.8664 -0.0284 -0.0012 0.0169  185 ARG A O   
1347 C CB  . ARG A 185 ? 0.7637 0.8884 0.8750 -0.0340 -0.0088 0.0205  185 ARG A CB  
1348 N N   . VAL A 186 ? 0.6308 0.7656 0.7449 -0.0218 0.0007  0.0123  186 VAL A N   
1349 C CA  . VAL A 186 ? 0.5822 0.7202 0.6972 -0.0185 0.0040  0.0101  186 VAL A CA  
1350 C C   . VAL A 186 ? 0.5809 0.7090 0.6825 -0.0166 0.0032  0.0084  186 VAL A C   
1351 O O   . VAL A 186 ? 0.5680 0.6913 0.6624 -0.0141 0.0029  0.0064  186 VAL A O   
1352 C CB  . VAL A 186 ? 0.5166 0.6632 0.6389 -0.0145 0.0079  0.0075  186 VAL A CB  
1353 C CG1 . VAL A 186 ? 0.5326 0.6824 0.6557 -0.0110 0.0114  0.0052  186 VAL A CG1 
1354 C CG2 . VAL A 186 ? 0.4781 0.6341 0.6135 -0.0167 0.0085  0.0094  186 VAL A CG2 
1355 N N   . MET A 187 ? 0.5878 0.7129 0.6864 -0.0178 0.0027  0.0093  187 MET A N   
1356 C CA  . MET A 187 ? 0.6143 0.7296 0.7002 -0.0166 0.0015  0.0081  187 MET A CA  
1357 C C   . MET A 187 ? 0.6249 0.7421 0.7099 -0.0126 0.0047  0.0054  187 MET A C   
1358 O O   . MET A 187 ? 0.6259 0.7521 0.7205 -0.0115 0.0077  0.0049  187 MET A O   
1359 C CB  . MET A 187 ? 0.6110 0.7202 0.6927 -0.0212 -0.0017 0.0111  187 MET A CB  
1360 C CG  . MET A 187 ? 0.6459 0.7543 0.7301 -0.0257 -0.0049 0.0142  187 MET A CG  
1361 S SD  . MET A 187 ? 0.6506 0.7514 0.7258 -0.0250 -0.0074 0.0135  187 MET A SD  
1362 C CE  . MET A 187 ? 0.6724 0.7609 0.7323 -0.0244 -0.0093 0.0127  187 MET A CE  
1363 N N   . SER A 188 ? 0.6658 0.7745 0.7392 -0.0106 0.0040  0.0037  188 SER A N   
1364 C CA  . SER A 188 ? 0.6613 0.7703 0.7319 -0.0064 0.0068  0.0009  188 SER A CA  
1365 C C   . SER A 188 ? 0.6261 0.7376 0.7005 -0.0082 0.0076  0.0023  188 SER A C   
1366 O O   . SER A 188 ? 0.6300 0.7372 0.7019 -0.0122 0.0050  0.0049  188 SER A O   
1367 C CB  . SER A 188 ? 0.7167 0.8150 0.7733 -0.0041 0.0053  -0.0011 188 SER A CB  
1368 O OG  . SER A 188 ? 0.7079 0.8042 0.7613 -0.0024 0.0048  -0.0027 188 SER A OG  
1369 N N   . LEU A 189 ? 0.6037 0.7221 0.6838 -0.0052 0.0112  0.0004  189 LEU A N   
1370 C CA  . LEU A 189 ? 0.5779 0.7002 0.6632 -0.0067 0.0125  0.0015  189 LEU A CA  
1371 C C   . LEU A 189 ? 0.6135 0.7270 0.6885 -0.0073 0.0110  0.0017  189 LEU A C   
1372 O O   . LEU A 189 ? 0.6833 0.7969 0.7604 -0.0107 0.0102  0.0039  189 LEU A O   
1373 C CB  . LEU A 189 ? 0.5576 0.6893 0.6510 -0.0029 0.0168  -0.0008 189 LEU A CB  
1374 C CG  . LEU A 189 ? 0.5165 0.6581 0.6213 -0.0023 0.0188  -0.0010 189 LEU A CG  
1375 C CD1 . LEU A 189 ? 0.5093 0.6596 0.6214 0.0015  0.0232  -0.0034 189 LEU A CD1 
1376 C CD2 . LEU A 189 ? 0.5364 0.6827 0.6503 -0.0073 0.0173  0.0025  189 LEU A CD2 
1377 N N   . LEU A 190 ? 0.5965 0.7938 0.8434 0.0510  0.0579  -0.0660 190 LEU A N   
1378 C CA  . LEU A 190 ? 0.5597 0.7623 0.8333 0.0581  0.0633  -0.0606 190 LEU A CA  
1379 C C   . LEU A 190 ? 0.5500 0.7368 0.8291 0.0675  0.0661  -0.0699 190 LEU A C   
1380 O O   . LEU A 190 ? 0.6179 0.8076 0.9182 0.0739  0.0707  -0.0664 190 LEU A O   
1381 C CB  . LEU A 190 ? 0.5890 0.8160 0.8733 0.0578  0.0709  -0.0458 190 LEU A CB  
1382 C CG  . LEU A 190 ? 0.6062 0.8504 0.8847 0.0486  0.0690  -0.0357 190 LEU A CG  
1383 C CD1 . LEU A 190 ? 0.6189 0.8867 0.9102 0.0493  0.0769  -0.0212 190 LEU A CD1 
1384 C CD2 . LEU A 190 ? 0.5810 0.8238 0.8672 0.0444  0.0629  -0.0350 190 LEU A CD2 
1385 N N   . GLU A 191 ? 0.5712 0.7411 0.8309 0.0681  0.0631  -0.0817 191 GLU A N   
1386 C CA  . GLU A 191 ? 0.5184 0.6713 0.7798 0.0764  0.0648  -0.0920 191 GLU A CA  
1387 C C   . GLU A 191 ? 0.6017 0.7331 0.8413 0.0738  0.0570  -0.1062 191 GLU A C   
1388 O O   . GLU A 191 ? 0.6064 0.7312 0.8275 0.0738  0.0571  -0.1123 191 GLU A O   
1389 C CB  . GLU A 191 ? 0.4717 0.6324 0.7309 0.0807  0.0724  -0.0886 191 GLU A CB  
1390 C CG  . GLU A 191 ? 0.4662 0.6176 0.7382 0.0908  0.0773  -0.0935 191 GLU A CG  
1391 C CD  . GLU A 191 ? 0.4731 0.6346 0.7431 0.0943  0.0851  -0.0887 191 GLU A CD  
1392 O OE1 . GLU A 191 ? 0.4542 0.6367 0.7358 0.0937  0.0907  -0.0756 191 GLU A OE1 
1393 O OE2 . GLU A 191 ? 0.4910 0.6402 0.7472 0.0975  0.0855  -0.0977 191 GLU A OE2 
1394 N N   . PRO A 192 ? 0.6380 0.7583 0.8800 0.0717  0.0502  -0.1117 192 PRO A N   
1395 C CA  . PRO A 192 ? 0.6682 0.7694 0.8899 0.0681  0.0422  -0.1242 192 PRO A CA  
1396 C C   . PRO A 192 ? 0.6940 0.7744 0.9061 0.0741  0.0418  -0.1377 192 PRO A C   
1397 O O   . PRO A 192 ? 0.7146 0.7793 0.9086 0.0711  0.0354  -0.1483 192 PRO A O   
1398 C CB  . PRO A 192 ? 0.6488 0.7447 0.8814 0.0661  0.0365  -0.1254 192 PRO A CB  
1399 C CG  . PRO A 192 ? 0.6499 0.7540 0.9099 0.0724  0.0421  -0.1183 192 PRO A CG  
1400 C CD  . PRO A 192 ? 0.6251 0.7501 0.8898 0.0729  0.0499  -0.1063 192 PRO A CD  
1401 N N   . THR A 193 ? 0.7268 0.8073 0.9509 0.0823  0.0485  -0.1372 193 THR A N   
1402 C CA  . THR A 193 ? 0.7706 0.8331 0.9862 0.0885  0.0492  -0.1489 193 THR A CA  
1403 C C   . THR A 193 ? 0.7820 0.8484 0.9788 0.0873  0.0523  -0.1492 193 THR A C   
1404 O O   . THR A 193 ? 0.8432 0.8935 1.0254 0.0896  0.0506  -0.1602 193 THR A O   
1405 C CB  . THR A 193 ? 0.7933 0.8534 1.0312 0.0982  0.0550  -0.1486 193 THR A CB  
1406 O OG1 . THR A 193 ? 0.8690 0.9504 1.1202 0.1000  0.0630  -0.1355 193 THR A OG1 
1407 C CG2 . THR A 193 ? 0.7631 0.8164 1.0184 0.0999  0.0516  -0.1502 193 THR A CG2 
1408 N N   . LYS A 194 ? 0.7869 0.8746 0.9844 0.0839  0.0568  -0.1370 194 LYS A N   
1409 C CA  . LYS A 194 ? 0.7570 0.8514 0.9380 0.0825  0.0602  -0.1355 194 LYS A CA  
1410 C C   . LYS A 194 ? 0.7741 0.8710 0.9331 0.0728  0.0544  -0.1356 194 LYS A C   
1411 O O   . LYS A 194 ? 0.7929 0.9003 0.9555 0.0666  0.0516  -0.1285 194 LYS A O   
1412 C CB  . LYS A 194 ? 0.7482 0.8648 0.9433 0.0847  0.0689  -0.1217 194 LYS A CB  
1413 C CG  . LYS A 194 ? 0.7592 0.8862 0.9388 0.0826  0.0728  -0.1178 194 LYS A CG  
1414 C CD  . LYS A 194 ? 0.7513 0.9004 0.9470 0.0850  0.0814  -0.1040 194 LYS A CD  
1415 N N   . LYS A 195 ? 0.7219 0.8097 0.8586 0.0714  0.0527  -0.1434 195 LYS A N   
1416 C CA  . LYS A 195 ? 0.7097 0.7985 0.8236 0.0624  0.0471  -0.1446 195 LYS A CA  
1417 C C   . LYS A 195 ? 0.7072 0.8202 0.8206 0.0572  0.0510  -0.1306 195 LYS A C   
1418 O O   . LYS A 195 ? 0.6936 0.8191 0.8150 0.0610  0.0585  -0.1233 195 LYS A O   
1419 C CB  . LYS A 195 ? 0.6719 0.7451 0.7631 0.0629  0.0450  -0.1562 195 LYS A CB  
1420 N N   . MET A 196 ? 0.7348 0.8546 0.8393 0.0485  0.0460  -0.1268 196 MET A N   
1421 C CA  . MET A 196 ? 0.7480 0.8905 0.8511 0.0428  0.0490  -0.1136 196 MET A CA  
1422 C C   . MET A 196 ? 0.7755 0.9209 0.8599 0.0419  0.0518  -0.1144 196 MET A C   
1423 O O   . MET A 196 ? 0.7832 0.9160 0.8462 0.0388  0.0469  -0.1238 196 MET A O   
1424 C CB  . MET A 196 ? 0.7067 0.8531 0.8023 0.0336  0.0421  -0.1111 196 MET A CB  
1425 C CG  . MET A 196 ? 0.6739 0.8423 0.7643 0.0266  0.0440  -0.0986 196 MET A CG  
1426 S SD  . MET A 196 ? 0.6615 0.8320 0.7399 0.0156  0.0352  -0.0973 196 MET A SD  
1427 C CE  . MET A 196 ? 0.6687 0.8401 0.7733 0.0176  0.0339  -0.0936 196 MET A CE  
1428 N N   . SER A 197 ? 0.8093 0.9712 0.9021 0.0448  0.0598  -0.1047 197 SER A N   
1429 C CA  . SER A 197 ? 0.8661 1.0323 0.9435 0.0448  0.0636  -0.1044 197 SER A CA  
1430 C C   . SER A 197 ? 0.8822 1.0736 0.9633 0.0411  0.0687  -0.0895 197 SER A C   
1431 O O   . SER A 197 ? 0.8968 1.1019 0.9989 0.0436  0.0736  -0.0795 197 SER A O   
1432 C CB  . SER A 197 ? 0.9092 1.0669 0.9932 0.0544  0.0692  -0.1097 197 SER A CB  
1433 N N   . LYS A 198 ? 0.9225 1.1196 0.9830 0.0352  0.0678  -0.0882 198 LYS A N   
1434 C CA  . LYS A 198 ? 0.9458 1.1663 1.0065 0.0312  0.0725  -0.0746 198 LYS A CA  
1435 C C   . LYS A 198 ? 0.9574 1.1903 1.0353 0.0383  0.0820  -0.0666 198 LYS A C   
1436 O O   . LYS A 198 ? 0.9383 1.1912 1.0282 0.0368  0.0864  -0.0537 198 LYS A O   
1437 C CB  . LYS A 198 ? 0.8943 1.1152 0.9286 0.0256  0.0705  -0.0770 198 LYS A CB  
1438 N N   . SER A 199 ? 1.0835 1.3038 1.1630 0.0461  0.0849  -0.0746 199 SER A N   
1439 C CA  . SER A 199 ? 1.1328 1.3615 1.2284 0.0539  0.0937  -0.0690 199 SER A CA  
1440 C C   . SER A 199 ? 1.1713 1.4089 1.2950 0.0580  0.0974  -0.0610 199 SER A C   
1441 O O   . SER A 199 ? 1.2594 1.5069 1.3975 0.0638  0.1050  -0.0546 199 SER A O   
1442 C CB  . SER A 199 ? 1.1495 1.3595 1.2398 0.0613  0.0947  -0.0812 199 SER A CB  
1443 O OG  . SER A 199 ? 1.1951 1.3847 1.2864 0.0630  0.0887  -0.0926 199 SER A OG  
1444 N N   . ASP A 200 ? 1.1170 1.3511 1.2483 0.0550  0.0921  -0.0614 200 ASP A N   
1445 C CA  . ASP A 200 ? 1.0597 1.3017 1.2173 0.0583  0.0949  -0.0541 200 ASP A CA  
1446 C C   . ASP A 200 ? 0.9567 1.2244 1.1243 0.0551  0.1001  -0.0381 200 ASP A C   
1447 O O   . ASP A 200 ? 0.8571 1.1353 1.0132 0.0471  0.0975  -0.0326 200 ASP A O   
1448 C CB  . ASP A 200 ? 1.0199 1.2511 1.1808 0.0552  0.0873  -0.0591 200 ASP A CB  
1449 C CG  . ASP A 200 ? 0.9858 1.2181 1.1734 0.0607  0.0895  -0.0559 200 ASP A CG  
1450 O OD1 . ASP A 200 ? 0.9825 1.2333 1.1870 0.0615  0.0950  -0.0435 200 ASP A OD1 
1451 O OD2 . ASP A 200 ? 0.9651 1.1795 1.1568 0.0643  0.0858  -0.0657 200 ASP A OD2 
1452 N N   . ASN A 202 ? 0.8940 1.1889 1.1227 0.0583  0.1054  -0.0156 202 ASN A N   
1453 C CA  . ASN A 202 ? 0.8620 1.1610 1.0995 0.0534  0.1008  -0.0114 202 ASN A CA  
1454 C C   . ASN A 202 ? 0.9002 1.1923 1.1153 0.0449  0.0926  -0.0168 202 ASN A C   
1455 O O   . ASN A 202 ? 0.9318 1.2040 1.1370 0.0450  0.0865  -0.0291 202 ASN A O   
1456 C CB  . ASN A 202 ? 0.8713 1.1571 1.1267 0.0593  0.0992  -0.0173 202 ASN A CB  
1457 C CG  . ASN A 202 ? 0.9235 1.2202 1.1975 0.0568  0.0982  -0.0085 202 ASN A CG  
1458 O OD1 . ASN A 202 ? 0.8727 1.1863 1.1462 0.0503  0.0982  0.0017  202 ASN A OD1 
1459 N ND2 . ASN A 202 ? 0.9955 1.2824 1.2865 0.0620  0.0973  -0.0125 202 ASN A ND2 
1460 N N   . ARG A 203 ? 0.8448 1.1533 1.0518 0.0374  0.0924  -0.0076 203 ARG A N   
1461 C CA  . ARG A 203 ? 0.8399 1.1444 1.0262 0.0287  0.0848  -0.0112 203 ARG A CA  
1462 C C   . ARG A 203 ? 0.7770 1.0749 0.9701 0.0255  0.0781  -0.0135 203 ARG A C   
1463 O O   . ARG A 203 ? 0.6925 0.9822 0.8692 0.0192  0.0708  -0.0191 203 ARG A O   
1464 C CB  . ARG A 203 ? 0.8577 1.1825 1.0350 0.0216  0.0866  0.0001  203 ARG A CB  
1465 C CG  . ARG A 203 ? 0.9096 1.2435 1.0808 0.0241  0.0935  0.0039  203 ARG A CG  
1466 C CD  . ARG A 203 ? 0.9206 1.2361 1.0752 0.0279  0.0926  -0.0090 203 ARG A CD  
1467 N NE  . ARG A 203 ? 0.8933 1.1945 1.0253 0.0220  0.0842  -0.0190 203 ARG A NE  
1468 C CZ  . ARG A 203 ? 0.8857 1.1901 0.9956 0.0155  0.0818  -0.0190 203 ARG A CZ  
1469 N NH1 . ARG A 203 ? 0.9452 1.2669 1.0513 0.0137  0.0871  -0.0095 203 ARG A NH1 
1470 N NH2 . ARG A 203 ? 0.8276 1.1176 0.9185 0.0106  0.0740  -0.0287 203 ARG A NH2 
1471 N N   . ASN A 204 ? 0.7234 1.0248 0.9406 0.0298  0.0806  -0.0091 204 ASN A N   
1472 C CA  . ASN A 204 ? 0.7311 1.0239 0.9572 0.0286  0.0747  -0.0125 204 ASN A CA  
1473 C C   . ASN A 204 ? 0.7155 0.9827 0.9345 0.0319  0.0692  -0.0281 204 ASN A C   
1474 O O   . ASN A 204 ? 0.7909 1.0491 1.0117 0.0294  0.0629  -0.0325 204 ASN A O   
1475 C CB  . ASN A 204 ? 0.7003 1.0042 0.9547 0.0328  0.0793  -0.0034 204 ASN A CB  
1476 C CG  . ASN A 204 ? 0.6791 1.0078 0.9411 0.0280  0.0830  0.0120  204 ASN A CG  
1477 O OD1 . ASN A 204 ? 0.6811 1.0180 0.9277 0.0205  0.0805  0.0158  204 ASN A OD1 
1478 N ND2 . ASN A 204 ? 0.6784 1.0191 0.9641 0.0324  0.0887  0.0210  204 ASN A ND2 
1479 N N   . ASN A 205 ? 0.6788 0.9344 0.8895 0.0372  0.0714  -0.0364 205 ASN A N   
1480 C CA  . ASN A 205 ? 0.6637 0.8946 0.8639 0.0399  0.0661  -0.0518 205 ASN A CA  
1481 C C   . ASN A 205 ? 0.6074 0.8287 0.7800 0.0331  0.0593  -0.0596 205 ASN A C   
1482 O O   . ASN A 205 ? 0.6210 0.8224 0.7845 0.0335  0.0534  -0.0719 205 ASN A O   
1483 C CB  . ASN A 205 ? 0.6955 0.9177 0.8991 0.0489  0.0715  -0.0575 205 ASN A CB  
1484 C CG  . ASN A 205 ? 0.7532 0.9723 0.9819 0.0568  0.0748  -0.0571 205 ASN A CG  
1485 O OD1 . ASN A 205 ? 0.7645 0.9730 1.0007 0.0572  0.0701  -0.0621 205 ASN A OD1 
1486 N ND2 . ASN A 205 ? 0.8331 1.0609 1.0745 0.0633  0.0829  -0.0517 205 ASN A ND2 
1487 N N   . VAL A 206 ? 0.5717 0.8071 0.7313 0.0267  0.0600  -0.0526 206 VAL A N   
1488 C CA  . VAL A 206 ? 0.5466 0.7741 0.6792 0.0205  0.0544  -0.0595 206 VAL A CA  
1489 C C   . VAL A 206 ? 0.4905 0.7300 0.6157 0.0109  0.0502  -0.0523 206 VAL A C   
1490 O O   . VAL A 206 ? 0.5263 0.7830 0.6662 0.0092  0.0529  -0.0405 206 VAL A O   
1491 C CB  . VAL A 206 ? 0.6090 0.8396 0.7276 0.0220  0.0591  -0.0598 206 VAL A CB  
1492 C CG1 . VAL A 206 ? 0.6623 0.8845 0.7909 0.0320  0.0647  -0.0647 206 VAL A CG1 
1493 C CG2 . VAL A 206 ? 0.6154 0.8704 0.7361 0.0184  0.0644  -0.0454 206 VAL A CG2 
1494 N N   . ILE A 207 ? 0.5466 0.7767 0.6490 0.0048  0.0435  -0.0595 207 ILE A N   
1495 C CA  . ILE A 207 ? 0.5122 0.7532 0.6025 -0.0049 0.0394  -0.0534 207 ILE A CA  
1496 C C   . ILE A 207 ? 0.4975 0.7378 0.5628 -0.0085 0.0388  -0.0565 207 ILE A C   
1497 O O   . ILE A 207 ? 0.4792 0.7014 0.5283 -0.0079 0.0348  -0.0688 207 ILE A O   
1498 C CB  . ILE A 207 ? 0.4994 0.7293 0.5865 -0.0096 0.0306  -0.0592 207 ILE A CB  
1499 C CG1 . ILE A 207 ? 0.5599 0.7989 0.6718 -0.0085 0.0317  -0.0512 207 ILE A CG1 
1500 C CG2 . ILE A 207 ? 0.4472 0.6813 0.5133 -0.0195 0.0250  -0.0580 207 ILE A CG2 
1501 C CD1 . ILE A 207 ? 0.6084 0.8365 0.7207 -0.0120 0.0237  -0.0566 207 ILE A CD1 
1502 N N   . GLY A 208 ? 0.4889 0.7489 0.5514 -0.0122 0.0430  -0.0452 208 GLY A N   
1503 C CA  . GLY A 208 ? 0.4392 0.7015 0.4786 -0.0162 0.0430  -0.0463 208 GLY A CA  
1504 C C   . GLY A 208 ? 0.4176 0.6772 0.4380 -0.0254 0.0350  -0.0487 208 GLY A C   
1505 O O   . GLY A 208 ? 0.4236 0.6885 0.4512 -0.0298 0.0315  -0.0441 208 GLY A O   
1506 N N   . LEU A 209 ? 0.4144 0.6663 0.4109 -0.0285 0.0322  -0.0556 209 LEU A N   
1507 C CA  . LEU A 209 ? 0.4283 0.6755 0.4043 -0.0372 0.0242  -0.0594 209 LEU A CA  
1508 C C   . LEU A 209 ? 0.4686 0.7366 0.4429 -0.0452 0.0241  -0.0467 209 LEU A C   
1509 O O   . LEU A 209 ? 0.4917 0.7575 0.4534 -0.0525 0.0173  -0.0482 209 LEU A O   
1510 C CB  . LEU A 209 ? 0.4552 0.6904 0.4062 -0.0382 0.0221  -0.0692 209 LEU A CB  
1511 C CG  . LEU A 209 ? 0.4633 0.6755 0.4110 -0.0316 0.0206  -0.0836 209 LEU A CG  
1512 C CD1 . LEU A 209 ? 0.4766 0.6780 0.3974 -0.0345 0.0172  -0.0927 209 LEU A CD1 
1513 C CD2 . LEU A 209 ? 0.4759 0.6728 0.4311 -0.0308 0.0145  -0.0912 209 LEU A CD2 
1514 N N   . LEU A 210 ? 0.4983 0.7858 0.4846 -0.0436 0.0316  -0.0344 210 LEU A N   
1515 C CA  . LEU A 210 ? 0.5853 0.8942 0.5718 -0.0504 0.0328  -0.0212 210 LEU A CA  
1516 C C   . LEU A 210 ? 0.5806 0.9025 0.5916 -0.0499 0.0349  -0.0108 210 LEU A C   
1517 O O   . LEU A 210 ? 0.5954 0.9364 0.6095 -0.0549 0.0367  0.0012  210 LEU A O   
1518 C CB  . LEU A 210 ? 0.5881 0.9110 0.5691 -0.0497 0.0396  -0.0142 210 LEU A CB  
1519 C CG  . LEU A 210 ? 0.5996 0.9129 0.5550 -0.0513 0.0377  -0.0226 210 LEU A CG  
1520 C CD1 . LEU A 210 ? 0.5746 0.9036 0.5275 -0.0502 0.0452  -0.0143 210 LEU A CD1 
1521 C CD2 . LEU A 210 ? 0.5702 0.8791 0.5036 -0.0605 0.0296  -0.0262 210 LEU A CD2 
1522 N N   . GLU A 211 ? 0.5814 0.8929 0.6092 -0.0441 0.0346  -0.0155 211 GLU A N   
1523 C CA  . GLU A 211 ? 0.5591 0.8811 0.6109 -0.0431 0.0363  -0.0068 211 GLU A CA  
1524 C C   . GLU A 211 ? 0.5292 0.8538 0.5773 -0.0512 0.0294  -0.0044 211 GLU A C   
1525 O O   . GLU A 211 ? 0.5759 0.8862 0.6076 -0.0552 0.0220  -0.0138 211 GLU A O   
1526 C CB  . GLU A 211 ? 0.5366 0.8455 0.6066 -0.0346 0.0375  -0.0133 211 GLU A CB  
1527 C CG  . GLU A 211 ? 0.5939 0.9083 0.6774 -0.0264 0.0463  -0.0099 211 GLU A CG  
1528 C CD  . GLU A 211 ? 0.6284 0.9365 0.7355 -0.0186 0.0487  -0.0117 211 GLU A CD  
1529 O OE1 . GLU A 211 ? 0.6205 0.9341 0.7436 -0.0197 0.0474  -0.0064 211 GLU A OE1 
1530 O OE2 . GLU A 211 ? 0.6422 0.9404 0.7522 -0.0112 0.0521  -0.0181 211 GLU A OE2 
1531 N N   . ASP A 212 ? 0.5234 0.8664 0.5871 -0.0536 0.0319  0.0083  212 ASP A N   
1532 C CA  . ASP A 212 ? 0.5704 0.9186 0.6317 -0.0615 0.0260  0.0123  212 ASP A CA  
1533 C C   . ASP A 212 ? 0.5226 0.8582 0.5966 -0.0595 0.0213  0.0064  212 ASP A C   
1534 O O   . ASP A 212 ? 0.5036 0.8322 0.5937 -0.0518 0.0244  0.0032  212 ASP A O   
1535 C CB  . ASP A 212 ? 0.6059 0.9797 0.6772 -0.0655 0.0304  0.0287  212 ASP A CB  
1536 C CG  . ASP A 212 ? 0.6527 1.0374 0.7520 -0.0593 0.0372  0.0372  212 ASP A CG  
1537 O OD1 . ASP A 212 ? 0.7978 1.1708 0.9106 -0.0527 0.0376  0.0312  212 ASP A OD1 
1538 O OD2 . ASP A 212 ? 0.6853 1.0907 0.7933 -0.0611 0.0422  0.0502  212 ASP A OD2 
1539 N N   . PRO A 213 ? 0.6991 0.8453 0.5943 -0.0142 0.0422  -0.0539 213 PRO A N   
1540 C CA  . PRO A 213 ? 0.7159 0.8521 0.6149 -0.0105 0.0416  -0.0451 213 PRO A CA  
1541 C C   . PRO A 213 ? 0.7139 0.8487 0.6129 -0.0031 0.0385  -0.0465 213 PRO A C   
1542 O O   . PRO A 213 ? 0.7657 0.8951 0.6679 -0.0008 0.0358  -0.0411 213 PRO A O   
1543 C CB  . PRO A 213 ? 0.6888 0.8190 0.5883 -0.0114 0.0471  -0.0405 213 PRO A CB  
1544 C CG  . PRO A 213 ? 0.6742 0.8096 0.5717 -0.0179 0.0502  -0.0436 213 PRO A CG  
1545 C CD  . PRO A 213 ? 0.6661 0.8122 0.5600 -0.0183 0.0476  -0.0538 213 PRO A CD  
1546 N N   . LYS A 214 ? 0.6385 0.7784 0.5340 0.0005  0.0388  -0.0538 214 LYS A N   
1547 C CA  . LYS A 214 ? 0.6141 0.7531 0.5090 0.0079  0.0362  -0.0557 214 LYS A CA  
1548 C C   . LYS A 214 ? 0.6236 0.7669 0.5185 0.0094  0.0311  -0.0589 214 LYS A C   
1549 O O   . LYS A 214 ? 0.6336 0.7725 0.5301 0.0144  0.0286  -0.0562 214 LYS A O   
1550 C CB  . LYS A 214 ? 0.6207 0.7651 0.5116 0.0112  0.0380  -0.0629 214 LYS A CB  
1551 N N   . SER A 215 ? 0.6563 0.8081 0.5492 0.0051  0.0297  -0.0648 215 SER A N   
1552 C CA  . SER A 215 ? 0.6577 0.8138 0.5503 0.0055  0.0251  -0.0680 215 SER A CA  
1553 C C   . SER A 215 ? 0.6076 0.7572 0.5043 0.0036  0.0230  -0.0602 215 SER A C   
1554 O O   . SER A 215 ? 0.5799 0.7278 0.4777 0.0070  0.0195  -0.0593 215 SER A O   
1555 C CB  . SER A 215 ? 0.6447 0.8110 0.5344 0.0008  0.0244  -0.0759 215 SER A CB  
1556 O OG  . SER A 215 ? 0.6314 0.8018 0.5206 0.0018  0.0200  -0.0793 215 SER A OG  
1557 N N   . VAL A 216 ? 0.5904 0.7364 0.4893 -0.0018 0.0253  -0.0545 216 VAL A N   
1558 C CA  . VAL A 216 ? 0.6164 0.7563 0.5194 -0.0041 0.0237  -0.0465 216 VAL A CA  
1559 C C   . VAL A 216 ? 0.6565 0.7878 0.5625 0.0018  0.0227  -0.0404 216 VAL A C   
1560 O O   . VAL A 216 ? 0.6386 0.7680 0.5465 0.0031  0.0191  -0.0383 216 VAL A O   
1561 C CB  . VAL A 216 ? 0.6356 0.7725 0.5404 -0.0102 0.0271  -0.0409 216 VAL A CB  
1562 C CG1 . VAL A 216 ? 0.6413 0.7709 0.5508 -0.0118 0.0259  -0.0315 216 VAL A CG1 
1563 C CG2 . VAL A 216 ? 0.6153 0.7604 0.5175 -0.0164 0.0275  -0.0465 216 VAL A CG2 
1564 N N   . VAL A 217 ? 0.6139 0.7402 0.5200 0.0054  0.0258  -0.0382 217 VAL A N   
1565 C CA  . VAL A 217 ? 0.6213 0.7391 0.5299 0.0113  0.0254  -0.0327 217 VAL A CA  
1566 C C   . VAL A 217 ? 0.6213 0.7414 0.5286 0.0168  0.0215  -0.0372 217 VAL A C   
1567 O O   . VAL A 217 ? 0.6106 0.7252 0.5208 0.0193  0.0193  -0.0325 217 VAL A O   
1568 C CB  . VAL A 217 ? 0.6457 0.7585 0.5538 0.0144  0.0297  -0.0307 217 VAL A CB  
1569 C CG1 . VAL A 217 ? 0.6250 0.7302 0.5349 0.0216  0.0290  -0.0269 217 VAL A CG1 
1570 C CG2 . VAL A 217 ? 0.6641 0.7719 0.5747 0.0095  0.0335  -0.0238 217 VAL A CG2 
1571 N N   . LYS A 218 ? 0.6142 0.7423 0.5174 0.0188  0.0209  -0.0460 218 LYS A N   
1572 C CA  . LYS A 218 ? 0.6320 0.7629 0.5335 0.0244  0.0176  -0.0508 218 LYS A CA  
1573 C C   . LYS A 218 ? 0.5921 0.7247 0.4948 0.0223  0.0136  -0.0507 218 LYS A C   
1574 O O   . LYS A 218 ? 0.6617 0.7911 0.5654 0.0266  0.0111  -0.0496 218 LYS A O   
1575 C CB  . LYS A 218 ? 0.6512 0.7912 0.5478 0.0263  0.0180  -0.0604 218 LYS A CB  
1576 C CG  . LYS A 218 ? 0.6890 0.8337 0.5835 0.0313  0.0146  -0.0663 218 LYS A CG  
1577 C CD  . LYS A 218 ? 0.7106 0.8602 0.6012 0.0364  0.0157  -0.0729 218 LYS A CD  
1578 N N   . LYS A 219 ? 0.5741 0.7114 0.4766 0.0156  0.0131  -0.0520 219 LYS A N   
1579 C CA  . LYS A 219 ? 0.5685 0.7077 0.4720 0.0127  0.0094  -0.0519 219 LYS A CA  
1580 C C   . LYS A 219 ? 0.5604 0.6909 0.4687 0.0119  0.0084  -0.0427 219 LYS A C   
1581 O O   . LYS A 219 ? 0.5374 0.6665 0.4468 0.0137  0.0052  -0.0420 219 LYS A O   
1582 C CB  . LYS A 219 ? 0.6223 0.7688 0.5242 0.0057  0.0094  -0.0557 219 LYS A CB  
1583 C CG  . LYS A 219 ? 0.6596 0.8155 0.5569 0.0062  0.0099  -0.0653 219 LYS A CG  
1584 C CD  . LYS A 219 ? 0.6803 0.8439 0.5758 0.0003  0.0085  -0.0702 219 LYS A CD  
1585 C CE  . LYS A 219 ? 0.6548 0.8279 0.5459 0.0015  0.0086  -0.0801 219 LYS A CE  
1586 N NZ  . LYS A 219 ? 0.6427 0.8227 0.5321 -0.0044 0.0071  -0.0846 219 LYS A NZ  
1587 N N   . ILE A 220 ? 0.5317 0.6565 0.4428 0.0095  0.0113  -0.0358 220 ILE A N   
1588 C CA  . ILE A 220 ? 0.5717 0.6880 0.4876 0.0088  0.0108  -0.0265 220 ILE A CA  
1589 C C   . ILE A 220 ? 0.5379 0.6471 0.4555 0.0159  0.0103  -0.0235 220 ILE A C   
1590 O O   . ILE A 220 ? 0.5020 0.6068 0.4225 0.0167  0.0079  -0.0192 220 ILE A O   
1591 C CB  . ILE A 220 ? 0.5531 0.6650 0.4716 0.0046  0.0144  -0.0197 220 ILE A CB  
1592 C CG1 . ILE A 220 ? 0.5547 0.6731 0.4715 -0.0024 0.0153  -0.0223 220 ILE A CG1 
1593 C CG2 . ILE A 220 ? 0.5395 0.6433 0.4631 0.0038  0.0135  -0.0102 220 ILE A CG2 
1594 C CD1 . ILE A 220 ? 0.5636 0.6855 0.4812 -0.0072 0.0118  -0.0223 220 ILE A CD1 
1595 N N   . LYS A 221 ? 0.5656 0.6739 0.4811 0.0210  0.0124  -0.0261 221 LYS A N   
1596 C CA  . LYS A 221 ? 0.5293 0.6312 0.4457 0.0283  0.0122  -0.0240 221 LYS A CA  
1597 C C   . LYS A 221 ? 0.5794 0.6835 0.4948 0.0318  0.0084  -0.0279 221 LYS A C   
1598 O O   . LYS A 221 ? 0.6525 0.7499 0.5702 0.0358  0.0074  -0.0239 221 LYS A O   
1599 C CB  . LYS A 221 ? 0.5334 0.6354 0.4469 0.0330  0.0152  -0.0273 221 LYS A CB  
1600 N N   . ARG A 222 ? 0.6046 0.7176 0.5165 0.0300  0.0065  -0.0354 222 ARG A N   
1601 C CA  . ARG A 222 ? 0.6600 0.7760 0.5705 0.0326  0.0031  -0.0397 222 ARG A CA  
1602 C C   . ARG A 222 ? 0.6363 0.7513 0.5496 0.0281  0.0002  -0.0364 222 ARG A C   
1603 O O   . ARG A 222 ? 0.6286 0.7437 0.5415 0.0305  -0.0025 -0.0381 222 ARG A O   
1604 C CB  . ARG A 222 ? 0.6737 0.8002 0.5794 0.0325  0.0023  -0.0495 222 ARG A CB  
1605 N N   . ALA A 223 ? 0.6105 0.7247 0.5263 0.0217  0.0008  -0.0317 223 ALA A N   
1606 C CA  . ALA A 223 ? 0.5908 0.7049 0.5089 0.0166  -0.0019 -0.0286 223 ALA A CA  
1607 C C   . ALA A 223 ? 0.5634 0.6705 0.4847 0.0199  -0.0037 -0.0238 223 ALA A C   
1608 O O   . ALA A 223 ? 0.5835 0.6829 0.5074 0.0236  -0.0020 -0.0183 223 ALA A O   
1609 C CB  . ALA A 223 ? 0.6027 0.7156 0.5234 0.0102  -0.0003 -0.0230 223 ALA A CB  
1610 N N   . VAL A 224 ? 0.6069 0.7165 0.5278 0.0187  -0.0070 -0.0260 224 VAL A N   
1611 C CA  . VAL A 224 ? 0.6540 0.7575 0.5774 0.0221  -0.0088 -0.0225 224 VAL A CA  
1612 C C   . VAL A 224 ? 0.6186 0.7148 0.5472 0.0193  -0.0084 -0.0131 224 VAL A C   
1613 O O   . VAL A 224 ? 0.6289 0.7269 0.5590 0.0132  -0.0083 -0.0102 224 VAL A O   
1614 C CB  . VAL A 224 ? 0.6729 0.7809 0.5944 0.0208  -0.0122 -0.0272 224 VAL A CB  
1615 C CG1 . VAL A 224 ? 0.6874 0.8016 0.6038 0.0249  -0.0125 -0.0361 224 VAL A CG1 
1616 C CG2 . VAL A 224 ? 0.7080 0.8208 0.6299 0.0129  -0.0140 -0.0269 224 VAL A CG2 
1617 N N   . THR A 225 ? 0.6210 0.7093 0.5526 0.0240  -0.0081 -0.0083 225 THR A N   
1618 C CA  . THR A 225 ? 0.6329 0.7140 0.5699 0.0219  -0.0079 0.0008  225 THR A CA  
1619 C C   . THR A 225 ? 0.6085 0.6861 0.5474 0.0235  -0.0105 0.0023  225 THR A C   
1620 O O   . THR A 225 ? 0.6569 0.7396 0.5939 0.0215  -0.0132 -0.0021 225 THR A O   
1621 C CB  . THR A 225 ? 0.6098 0.6839 0.5490 0.0252  -0.0043 0.0061  225 THR A CB  
1622 O OG1 . THR A 225 ? 0.6312 0.7021 0.5685 0.0327  -0.0033 0.0035  225 THR A OG1 
1623 C CG2 . THR A 225 ? 0.5816 0.6595 0.5191 0.0219  -0.0018 0.0051  225 THR A CG2 
1624 N N   . ASP A 226 ? 0.6344 0.7034 0.5773 0.0268  -0.0098 0.0086  226 ASP A N   
1625 C CA  . ASP A 226 ? 0.5930 0.6579 0.5377 0.0290  -0.0119 0.0100  226 ASP A CA  
1626 C C   . ASP A 226 ? 0.5716 0.6281 0.5178 0.0362  -0.0099 0.0129  226 ASP A C   
1627 O O   . ASP A 226 ? 0.5704 0.6242 0.5164 0.0390  -0.0070 0.0142  226 ASP A O   
1628 C CB  . ASP A 226 ? 0.5870 0.6502 0.5363 0.0231  -0.0138 0.0163  226 ASP A CB  
1629 C CG  . ASP A 226 ? 0.6054 0.6633 0.5593 0.0213  -0.0117 0.0247  226 ASP A CG  
1630 O OD1 . ASP A 226 ? 0.5517 0.6020 0.5080 0.0261  -0.0096 0.0289  226 ASP A OD1 
1631 O OD2 . ASP A 226 ? 0.6454 0.7067 0.6005 0.0151  -0.0119 0.0272  226 ASP A OD2 
1632 N N   . SER A 227 ? 0.5681 0.6203 0.5157 0.0391  -0.0112 0.0138  227 SER A N   
1633 C CA  . SER A 227 ? 0.5631 0.6067 0.5123 0.0460  -0.0096 0.0166  227 SER A CA  
1634 C C   . SER A 227 ? 0.5551 0.5906 0.5105 0.0447  -0.0093 0.0256  227 SER A C   
1635 O O   . SER A 227 ? 0.5670 0.5954 0.5242 0.0495  -0.0088 0.0279  227 SER A O   
1636 C CB  . SER A 227 ? 0.5894 0.6333 0.5357 0.0505  -0.0110 0.0112  227 SER A CB  
1637 O OG  . SER A 227 ? 0.6208 0.6668 0.5684 0.0460  -0.0139 0.0113  227 SER A OG  
1638 N N   . ASP A 228 ? 0.5533 0.5899 0.5120 0.0384  -0.0097 0.0306  228 ASP A N   
1639 C CA  . ASP A 228 ? 0.5214 0.5508 0.4861 0.0369  -0.0094 0.0395  228 ASP A CA  
1640 C C   . ASP A 228 ? 0.5089 0.5299 0.4755 0.0427  -0.0060 0.0436  228 ASP A C   
1641 O O   . ASP A 228 ? 0.4563 0.4782 0.4204 0.0446  -0.0036 0.0419  228 ASP A O   
1642 C CB  . ASP A 228 ? 0.5448 0.5774 0.5124 0.0294  -0.0099 0.0441  228 ASP A CB  
1643 C CG  . ASP A 228 ? 0.5673 0.6071 0.5341 0.0232  -0.0134 0.0414  228 ASP A CG  
1644 O OD1 . ASP A 228 ? 0.5578 0.6000 0.5220 0.0246  -0.0154 0.0361  228 ASP A OD1 
1645 O OD2 . ASP A 228 ? 0.5085 0.5514 0.4771 0.0171  -0.0140 0.0448  228 ASP A OD2 
1646 N N   . GLU A 229 ? 0.5195 0.5325 0.4901 0.0455  -0.0058 0.0487  229 GLU A N   
1647 C CA  . GLU A 229 ? 0.5353 0.5391 0.5082 0.0509  -0.0027 0.0535  229 GLU A CA  
1648 C C   . GLU A 229 ? 0.5142 0.5119 0.4940 0.0481  -0.0026 0.0627  229 GLU A C   
1649 O O   . GLU A 229 ? 0.5105 0.5067 0.4930 0.0468  -0.0047 0.0644  229 GLU A O   
1650 C CB  . GLU A 229 ? 0.5758 0.5751 0.5467 0.0585  -0.0022 0.0500  229 GLU A CB  
1651 C CG  . GLU A 229 ? 0.6062 0.5952 0.5795 0.0645  0.0009  0.0550  229 GLU A CG  
1652 C CD  . GLU A 229 ? 0.6149 0.6028 0.5873 0.0655  0.0039  0.0566  229 GLU A CD  
1653 O OE1 . GLU A 229 ? 0.5896 0.5843 0.5574 0.0648  0.0042  0.0510  229 GLU A OE1 
1654 O OE2 . GLU A 229 ? 0.5990 0.5789 0.5754 0.0669  0.0062  0.0634  229 GLU A OE2 
1655 N N   . PRO A 230 ? 0.4942 0.4885 0.4767 0.0469  -0.0002 0.0686  230 PRO A N   
1656 C CA  . PRO A 230 ? 0.5168 0.5136 0.4962 0.0471  0.0024  0.0668  230 PRO A CA  
1657 C C   . PRO A 230 ? 0.5597 0.5668 0.5359 0.0411  0.0008  0.0622  230 PRO A C   
1658 O O   . PRO A 230 ? 0.5068 0.5183 0.4843 0.0358  -0.0021 0.0625  230 PRO A O   
1659 C CB  . PRO A 230 ? 0.5056 0.4957 0.4899 0.0461  0.0051  0.0757  230 PRO A CB  
1660 C CG  . PRO A 230 ? 0.5307 0.5131 0.5202 0.0478  0.0044  0.0815  230 PRO A CG  
1661 C CD  . PRO A 230 ? 0.5035 0.4910 0.4926 0.0453  0.0006  0.0779  230 PRO A CD  
1662 N N   . PRO A 231 ? 0.5882 0.5993 0.5600 0.0419  0.0025  0.0576  231 PRO A N   
1663 C CA  . PRO A 231 ? 0.6130 0.6332 0.5822 0.0358  0.0016  0.0540  231 PRO A CA  
1664 C C   . PRO A 231 ? 0.5936 0.6134 0.5673 0.0295  0.0018  0.0614  231 PRO A C   
1665 O O   . PRO A 231 ? 0.5874 0.6006 0.5646 0.0305  0.0044  0.0681  231 PRO A O   
1666 C CB  . PRO A 231 ? 0.6225 0.6449 0.5872 0.0385  0.0044  0.0495  231 PRO A CB  
1667 C CG  . PRO A 231 ? 0.6106 0.6277 0.5738 0.0464  0.0053  0.0474  231 PRO A CG  
1668 C CD  . PRO A 231 ? 0.5943 0.6023 0.5628 0.0483  0.0053  0.0547  231 PRO A CD  
1669 N N   . VAL A 232 ? 0.5393 0.5659 0.5128 0.0234  -0.0009 0.0601  232 VAL A N   
1670 C CA  . VAL A 232 ? 0.5659 0.5930 0.5435 0.0172  -0.0011 0.0669  232 VAL A CA  
1671 C C   . VAL A 232 ? 0.5369 0.5732 0.5111 0.0114  -0.0019 0.0626  232 VAL A C   
1672 O O   . VAL A 232 ? 0.5244 0.5671 0.4953 0.0099  -0.0046 0.0562  232 VAL A O   
1673 C CB  . VAL A 232 ? 0.5763 0.6015 0.5583 0.0151  -0.0042 0.0711  232 VAL A CB  
1674 N N   . VAL A 233 ? 0.4937 0.5304 0.4686 0.0082  0.0008  0.0661  233 VAL A N   
1675 C CA  . VAL A 233 ? 0.5173 0.5620 0.4891 0.0027  0.0007  0.0626  233 VAL A CA  
1676 C C   . VAL A 233 ? 0.5490 0.5959 0.5243 -0.0038 -0.0015 0.0678  233 VAL A C   
1677 O O   . VAL A 233 ? 0.5141 0.5586 0.4928 -0.0066 0.0005  0.0748  233 VAL A O   
1678 C CB  . VAL A 233 ? 0.5043 0.5482 0.4746 0.0027  0.0051  0.0633  233 VAL A CB  
1679 C CG1 . VAL A 233 ? 0.5049 0.5563 0.4727 -0.0035 0.0055  0.0610  233 VAL A CG1 
1680 C CG2 . VAL A 233 ? 0.5232 0.5666 0.4892 0.0085  0.0067  0.0570  233 VAL A CG2 
1681 N N   . ARG A 234 ? 0.5968 0.6484 0.5712 -0.0058 -0.0054 0.0642  234 ARG A N   
1682 C CA  . ARG A 234 ? 0.6332 0.6878 0.6103 -0.0118 -0.0081 0.0679  234 ARG A CA  
1683 C C   . ARG A 234 ? 0.5778 0.6412 0.5504 -0.0154 -0.0109 0.0603  234 ARG A C   
1684 O O   . ARG A 234 ? 0.5865 0.6524 0.5551 -0.0124 -0.0118 0.0529  234 ARG A O   
1685 C CB  . ARG A 234 ? 0.6700 0.7195 0.6519 -0.0103 -0.0104 0.0727  234 ARG A CB  
1686 C CG  . ARG A 234 ? 0.7345 0.7752 0.7217 -0.0075 -0.0079 0.0813  234 ARG A CG  
1687 C CD  . ARG A 234 ? 0.7260 0.7662 0.7167 -0.0121 -0.0063 0.0890  234 ARG A CD  
1688 N NE  . ARG A 234 ? 0.7890 0.8349 0.7811 -0.0184 -0.0094 0.0904  234 ARG A NE  
1689 C CZ  . ARG A 234 ? 0.7900 0.8342 0.7870 -0.0204 -0.0118 0.0962  234 ARG A CZ  
1690 N NH1 . ARG A 234 ? 0.8639 0.9007 0.8654 -0.0168 -0.0113 0.1015  234 ARG A NH1 
1691 N NH2 . ARG A 234 ? 0.7805 0.8307 0.7778 -0.0263 -0.0146 0.0968  234 ARG A NH2 
1692 N N   . TYR A 235 ? 0.5947 0.6629 0.5679 -0.0217 -0.0122 0.0623  235 TYR A N   
1693 C CA  . TYR A 235 ? 0.5626 0.6390 0.5317 -0.0259 -0.0148 0.0557  235 TYR A CA  
1694 C C   . TYR A 235 ? 0.5734 0.6508 0.5432 -0.0262 -0.0190 0.0541  235 TYR A C   
1695 O O   . TYR A 235 ? 0.5900 0.6643 0.5643 -0.0277 -0.0205 0.0604  235 TYR A O   
1696 C CB  . TYR A 235 ? 0.5993 0.6799 0.5688 -0.0324 -0.0145 0.0588  235 TYR A CB  
1697 C CG  . TYR A 235 ? 0.6151 0.7042 0.5795 -0.0363 -0.0159 0.0512  235 TYR A CG  
1698 C CD1 . TYR A 235 ? 0.5904 0.6827 0.5502 -0.0356 -0.0133 0.0453  235 TYR A CD1 
1699 C CD2 . TYR A 235 ? 0.6064 0.7002 0.5703 -0.0408 -0.0196 0.0500  235 TYR A CD2 
1700 C CE1 . TYR A 235 ? 0.5796 0.6796 0.5349 -0.0391 -0.0144 0.0384  235 TYR A CE1 
1701 C CE2 . TYR A 235 ? 0.6568 0.7580 0.6159 -0.0444 -0.0208 0.0431  235 TYR A CE2 
1702 C CZ  . TYR A 235 ? 0.6723 0.7766 0.6272 -0.0435 -0.0181 0.0374  235 TYR A CZ  
1703 O OH  . TYR A 235 ? 0.6164 0.7280 0.5666 -0.0470 -0.0192 0.0305  235 TYR A OH  
1704 N N   . ASP A 236 ? 0.5551 0.6365 0.5203 -0.0248 -0.0207 0.0458  236 ASP A N   
1705 C CA  . ASP A 236 ? 0.5462 0.6290 0.5112 -0.0252 -0.0244 0.0432  236 ASP A CA  
1706 C C   . ASP A 236 ? 0.5357 0.6244 0.4945 -0.0243 -0.0252 0.0333  236 ASP A C   
1707 O O   . ASP A 236 ? 0.5625 0.6495 0.5192 -0.0187 -0.0240 0.0291  236 ASP A O   
1708 C CB  . ASP A 236 ? 0.5838 0.6591 0.5522 -0.0199 -0.0245 0.0464  236 ASP A CB  
1709 C CG  . ASP A 236 ? 0.5824 0.6583 0.5508 -0.0204 -0.0280 0.0443  236 ASP A CG  
1710 O OD1 . ASP A 236 ? 0.5764 0.6584 0.5409 -0.0230 -0.0302 0.0381  236 ASP A OD1 
1711 O OD2 . ASP A 236 ? 0.6308 0.7008 0.6033 -0.0182 -0.0285 0.0489  236 ASP A OD2 
1712 N N   . VAL A 237 ? 0.5338 0.6295 0.4900 -0.0297 -0.0271 0.0298  237 VAL A N   
1713 C CA  . VAL A 237 ? 0.5651 0.6672 0.5154 -0.0296 -0.0278 0.0204  237 VAL A CA  
1714 C C   . VAL A 237 ? 0.5903 0.6920 0.5388 -0.0262 -0.0301 0.0155  237 VAL A C   
1715 O O   . VAL A 237 ? 0.5863 0.6903 0.5308 -0.0225 -0.0295 0.0085  237 VAL A O   
1716 C CB  . VAL A 237 ? 0.5338 0.6432 0.4818 -0.0366 -0.0293 0.0181  237 VAL A CB  
1717 C CG1 . VAL A 237 ? 0.5215 0.6373 0.4635 -0.0364 -0.0298 0.0083  237 VAL A CG1 
1718 C CG2 . VAL A 237 ? 0.5455 0.6553 0.4949 -0.0400 -0.0268 0.0227  237 VAL A CG2 
1719 N N   . GLN A 238 ? 0.6431 0.7421 0.5948 -0.0275 -0.0324 0.0193  238 GLN A N   
1720 C CA  . GLN A 238 ? 0.6887 0.7868 0.6390 -0.0247 -0.0345 0.0153  238 GLN A CA  
1721 C C   . GLN A 238 ? 0.6979 0.7902 0.6483 -0.0168 -0.0325 0.0144  238 GLN A C   
1722 O O   . GLN A 238 ? 0.7292 0.8234 0.6756 -0.0131 -0.0324 0.0076  238 GLN A O   
1723 C CB  . GLN A 238 ? 0.7463 0.8424 0.7003 -0.0282 -0.0372 0.0202  238 GLN A CB  
1724 C CG  . GLN A 238 ? 0.7928 0.8866 0.7462 -0.0252 -0.0390 0.0173  238 GLN A CG  
1725 C CD  . GLN A 238 ? 0.8195 0.9125 0.7762 -0.0296 -0.0418 0.0216  238 GLN A CD  
1726 O OE1 . GLN A 238 ? 0.8452 0.9322 0.8059 -0.0274 -0.0419 0.0261  238 GLN A OE1 
1727 N NE2 . GLN A 238 ? 0.8226 0.9215 0.7777 -0.0360 -0.0442 0.0200  238 GLN A NE2 
1728 N N   . ASN A 239 ? 0.6746 0.7601 0.6295 -0.0143 -0.0307 0.0214  239 ASN A N   
1729 C CA  . ASN A 239 ? 0.6694 0.7484 0.6250 -0.0069 -0.0288 0.0218  239 ASN A CA  
1730 C C   . ASN A 239 ? 0.6382 0.7162 0.5923 -0.0027 -0.0254 0.0206  239 ASN A C   
1731 O O   . ASN A 239 ? 0.6204 0.6941 0.5737 0.0038  -0.0238 0.0191  239 ASN A O   
1732 C CB  . ASN A 239 ? 0.6861 0.7575 0.6478 -0.0061 -0.0287 0.0301  239 ASN A CB  
1733 C CG  . ASN A 239 ? 0.6993 0.7711 0.6628 -0.0097 -0.0319 0.0314  239 ASN A CG  
1734 O OD1 . ASN A 239 ? 0.7758 0.8487 0.7367 -0.0082 -0.0335 0.0263  239 ASN A OD1 
1735 N ND2 . ASN A 239 ? 0.6876 0.7587 0.6557 -0.0146 -0.0330 0.0384  239 ASN A ND2 
1736 N N   . LYS A 240 ? 0.5953 0.6768 0.5488 -0.0063 -0.0240 0.0214  240 LYS A N   
1737 C CA  . LYS A 240 ? 0.5540 0.6343 0.5064 -0.0032 -0.0206 0.0211  240 LYS A CA  
1738 C C   . LYS A 240 ? 0.5528 0.6408 0.5012 -0.0071 -0.0200 0.0162  240 LYS A C   
1739 O O   . LYS A 240 ? 0.5534 0.6415 0.5028 -0.0096 -0.0178 0.0195  240 LYS A O   
1740 C CB  . LYS A 240 ? 0.5208 0.5946 0.4784 -0.0033 -0.0183 0.0301  240 LYS A CB  
1741 C CG  . LYS A 240 ? 0.5168 0.5824 0.4789 0.0001  -0.0187 0.0358  240 LYS A CG  
1742 C CD  . LYS A 240 ? 0.5012 0.5610 0.4686 -0.0009 -0.0167 0.0451  240 LYS A CD  
1743 C CE  . LYS A 240 ? 0.5010 0.5580 0.4678 0.0021  -0.0128 0.0463  240 LYS A CE  
1744 N NZ  . LYS A 240 ? 0.4838 0.5354 0.4497 0.0097  -0.0112 0.0444  240 LYS A NZ  
1745 N N   . ALA A 241 ? 0.5977 0.6921 0.5416 -0.0076 -0.0217 0.0083  241 ALA A N   
1746 C CA  . ALA A 241 ? 0.6100 0.7122 0.5499 -0.0116 -0.0216 0.0028  241 ALA A CA  
1747 C C   . ALA A 241 ? 0.5827 0.6856 0.5211 -0.0099 -0.0180 0.0017  241 ALA A C   
1748 O O   . ALA A 241 ? 0.5814 0.6868 0.5198 -0.0144 -0.0166 0.0032  241 ALA A O   
1749 C CB  . ALA A 241 ? 0.6225 0.7306 0.5579 -0.0109 -0.0238 -0.0057 241 ALA A CB  
1750 N N   . GLY A 242 ? 0.5391 0.6393 0.4762 -0.0034 -0.0163 -0.0007 242 GLY A N   
1751 C CA  . GLY A 242 ? 0.5390 0.6397 0.4743 -0.0011 -0.0129 -0.0024 242 GLY A CA  
1752 C C   . GLY A 242 ? 0.4938 0.5902 0.4325 -0.0032 -0.0101 0.0049  242 GLY A C   
1753 O O   . GLY A 242 ? 0.4460 0.5459 0.3832 -0.0063 -0.0080 0.0038  242 GLY A O   
1754 N N   . VAL A 243 ? 0.5168 0.6055 0.4602 -0.0014 -0.0099 0.0125  243 VAL A N   
1755 C CA  . VAL A 243 ? 0.5034 0.5867 0.4508 -0.0030 -0.0072 0.0206  243 VAL A CA  
1756 C C   . VAL A 243 ? 0.4708 0.5575 0.4195 -0.0105 -0.0078 0.0239  243 VAL A C   
1757 O O   . VAL A 243 ? 0.4211 0.5072 0.3705 -0.0129 -0.0049 0.0272  243 VAL A O   
1758 C CB  . VAL A 243 ? 0.5058 0.5803 0.4581 0.0005  -0.0074 0.0278  243 VAL A CB  
1759 C CG1 . VAL A 243 ? 0.5359 0.6050 0.4927 -0.0016 -0.0049 0.0368  243 VAL A CG1 
1760 C CG2 . VAL A 243 ? 0.5313 0.6015 0.4821 0.0083  -0.0061 0.0252  243 VAL A CG2 
1761 N N   . SER A 244 ? 0.4413 0.5315 0.3902 -0.0140 -0.0114 0.0230  244 SER A N   
1762 C CA  . SER A 244 ? 0.4680 0.5620 0.4178 -0.0211 -0.0123 0.0255  244 SER A CA  
1763 C C   . SER A 244 ? 0.4595 0.5603 0.4050 -0.0244 -0.0107 0.0200  244 SER A C   
1764 O O   . SER A 244 ? 0.4969 0.5986 0.4433 -0.0287 -0.0090 0.0236  244 SER A O   
1765 C CB  . SER A 244 ? 0.4913 0.5877 0.4416 -0.0239 -0.0166 0.0248  244 SER A CB  
1766 O OG  . SER A 244 ? 0.5013 0.5912 0.4562 -0.0217 -0.0178 0.0308  244 SER A OG  
1767 N N   . ASN A 245 ? 0.4670 0.5726 0.4078 -0.0221 -0.0112 0.0114  245 ASN A N   
1768 C CA  . ASN A 245 ? 0.4937 0.6058 0.4302 -0.0245 -0.0095 0.0053  245 ASN A CA  
1769 C C   . ASN A 245 ? 0.4766 0.5859 0.4135 -0.0235 -0.0050 0.0079  245 ASN A C   
1770 O O   . ASN A 245 ? 0.4906 0.6028 0.4267 -0.0280 -0.0031 0.0084  245 ASN A O   
1771 C CB  . ASN A 245 ? 0.5310 0.6482 0.4627 -0.0212 -0.0107 -0.0043 245 ASN A CB  
1772 C CG  . ASN A 245 ? 0.5761 0.7011 0.5034 -0.0245 -0.0096 -0.0112 245 ASN A CG  
1773 O OD1 . ASN A 245 ? 0.5871 0.7154 0.5142 -0.0304 -0.0098 -0.0103 245 ASN A OD1 
1774 N ND2 . ASN A 245 ? 0.6067 0.7349 0.5304 -0.0206 -0.0086 -0.0182 245 ASN A ND2 
1775 N N   . LEU A 246 ? 0.4704 0.5739 0.4085 -0.0176 -0.0033 0.0098  246 LEU A N   
1776 C CA  . LEU A 246 ? 0.4576 0.5575 0.3962 -0.0162 0.0011  0.0127  246 LEU A CA  
1777 C C   . LEU A 246 ? 0.4565 0.5530 0.3989 -0.0207 0.0030  0.0211  246 LEU A C   
1778 O O   . LEU A 246 ? 0.4233 0.5206 0.3648 -0.0230 0.0064  0.0217  246 LEU A O   
1779 C CB  . LEU A 246 ? 0.4570 0.5503 0.3968 -0.0091 0.0023  0.0142  246 LEU A CB  
1780 C CG  . LEU A 246 ? 0.4791 0.5756 0.4148 -0.0040 0.0013  0.0058  246 LEU A CG  
1781 C CD1 . LEU A 246 ? 0.5160 0.6051 0.4534 0.0030  0.0022  0.0085  246 LEU A CD1 
1782 C CD2 . LEU A 246 ? 0.4703 0.5732 0.4014 -0.0044 0.0035  -0.0014 246 LEU A CD2 
1783 N N   . LEU A 247 ? 0.4658 0.5590 0.4125 -0.0222 0.0006  0.0274  247 LEU A N   
1784 C CA  . LEU A 247 ? 0.4625 0.5527 0.4130 -0.0264 0.0019  0.0358  247 LEU A CA  
1785 C C   . LEU A 247 ? 0.4462 0.5430 0.3948 -0.0331 0.0017  0.0342  247 LEU A C   
1786 O O   . LEU A 247 ? 0.4249 0.5208 0.3745 -0.0362 0.0049  0.0384  247 LEU A O   
1787 C CB  . LEU A 247 ? 0.4584 0.5439 0.4140 -0.0261 -0.0009 0.0427  247 LEU A CB  
1788 C CG  . LEU A 247 ? 0.4422 0.5192 0.4011 -0.0203 0.0003  0.0473  247 LEU A CG  
1789 C CD1 . LEU A 247 ? 0.4637 0.5373 0.4269 -0.0201 -0.0030 0.0522  247 LEU A CD1 
1790 C CD2 . LEU A 247 ? 0.4214 0.4931 0.3827 -0.0202 0.0047  0.0539  247 LEU A CD2 
1791 N N   . ASP A 248 ? 0.4607 0.5638 0.4066 -0.0353 -0.0017 0.0282  248 ASP A N   
1792 C CA  . ASP A 248 ? 0.4999 0.6097 0.4435 -0.0415 -0.0021 0.0258  248 ASP A CA  
1793 C C   . ASP A 248 ? 0.4860 0.5991 0.4258 -0.0424 0.0017  0.0211  248 ASP A C   
1794 O O   . ASP A 248 ? 0.4722 0.5867 0.4119 -0.0469 0.0038  0.0235  248 ASP A O   
1795 C CB  . ASP A 248 ? 0.5379 0.6535 0.4788 -0.0430 -0.0065 0.0194  248 ASP A CB  
1796 C CG  . ASP A 248 ? 0.5618 0.6761 0.5062 -0.0453 -0.0101 0.0245  248 ASP A CG  
1797 O OD1 . ASP A 248 ? 0.5674 0.6838 0.5106 -0.0445 -0.0136 0.0204  248 ASP A OD1 
1798 O OD2 . ASP A 248 ? 0.5410 0.6521 0.4892 -0.0480 -0.0094 0.0325  248 ASP A OD2 
1799 N N   . ILE A 249 ? 0.5146 0.6289 0.4513 -0.0380 0.0026  0.0146  249 ILE A N   
1800 C CA  . ILE A 249 ? 0.4974 0.6149 0.4303 -0.0383 0.0062  0.0095  249 ILE A CA  
1801 C C   . ILE A 249 ? 0.4588 0.5710 0.3941 -0.0389 0.0109  0.0163  249 ILE A C   
1802 O O   . ILE A 249 ? 0.4273 0.5422 0.3608 -0.0426 0.0138  0.0154  249 ILE A O   
1803 C CB  . ILE A 249 ? 0.5089 0.6281 0.4386 -0.0327 0.0063  0.0020  249 ILE A CB  
1804 C CG1 . ILE A 249 ? 0.5124 0.6377 0.4393 -0.0325 0.0021  -0.0053 249 ILE A CG1 
1805 C CG2 . ILE A 249 ? 0.5224 0.6447 0.4487 -0.0331 0.0104  -0.0026 249 ILE A CG2 
1806 C CD1 . ILE A 249 ? 0.4960 0.6231 0.4200 -0.0268 0.0017  -0.0124 249 ILE A CD1 
1807 N N   . LEU A 250 ? 0.4965 0.6010 0.4357 -0.0353 0.0115  0.0232  250 LEU A N   
1808 C CA  . LEU A 250 ? 0.5001 0.5986 0.4417 -0.0352 0.0160  0.0300  250 LEU A CA  
1809 C C   . LEU A 250 ? 0.5007 0.5989 0.4447 -0.0410 0.0170  0.0366  250 LEU A C   
1810 O O   . LEU A 250 ? 0.4099 0.5077 0.3534 -0.0435 0.0212  0.0385  250 LEU A O   
1811 C CB  . LEU A 250 ? 0.4753 0.5656 0.4207 -0.0297 0.0162  0.0356  250 LEU A CB  
1812 C CG  . LEU A 250 ? 0.5122 0.5955 0.4602 -0.0290 0.0209  0.0428  250 LEU A CG  
1813 C CD1 . LEU A 250 ? 0.5007 0.5858 0.4449 -0.0291 0.0254  0.0385  250 LEU A CD1 
1814 C CD2 . LEU A 250 ? 0.5196 0.5949 0.4710 -0.0232 0.0207  0.0475  250 LEU A CD2 
1815 N N   . SER A 251 ? 0.5013 0.6000 0.4480 -0.0431 0.0132  0.0399  251 SER A N   
1816 C CA  . SER A 251 ? 0.5670 0.6663 0.5158 -0.0487 0.0133  0.0458  251 SER A CA  
1817 C C   . SER A 251 ? 0.5460 0.6522 0.4907 -0.0538 0.0147  0.0409  251 SER A C   
1818 O O   . SER A 251 ? 0.5402 0.6457 0.4857 -0.0574 0.0178  0.0454  251 SER A O   
1819 C CB  . SER A 251 ? 0.5380 0.6379 0.4896 -0.0499 0.0082  0.0485  251 SER A CB  
1820 O OG  . SER A 251 ? 0.5661 0.6668 0.5199 -0.0551 0.0082  0.0545  251 SER A OG  
1821 N N   . ALA A 252 ? 0.5449 0.6575 0.4853 -0.0540 0.0126  0.0318  252 ALA A N   
1822 C CA  . ALA A 252 ? 0.5684 0.6879 0.5045 -0.0586 0.0136  0.0260  252 ALA A CA  
1823 C C   . ALA A 252 ? 0.5468 0.6658 0.4809 -0.0589 0.0192  0.0249  252 ALA A C   
1824 O O   . ALA A 252 ? 0.5583 0.6797 0.4911 -0.0636 0.0216  0.0253  252 ALA A O   
1825 C CB  . ALA A 252 ? 0.5569 0.6829 0.4891 -0.0578 0.0103  0.0161  252 ALA A CB  
1826 N N   . VAL A 253 ? 0.5790 0.6945 0.5129 -0.0540 0.0213  0.0236  253 VAL A N   
1827 C CA  . VAL A 253 ? 0.5914 0.7059 0.5233 -0.0538 0.0268  0.0225  253 VAL A CA  
1828 C C   . VAL A 253 ? 0.5981 0.7062 0.5335 -0.0555 0.0308  0.0321  253 VAL A C   
1829 O O   . VAL A 253 ? 0.6100 0.7192 0.5439 -0.0591 0.0348  0.0325  253 VAL A O   
1830 C CB  . VAL A 253 ? 0.5817 0.6944 0.5122 -0.0479 0.0278  0.0183  253 VAL A CB  
1831 C CG1 . VAL A 253 ? 0.5820 0.6938 0.5103 -0.0481 0.0335  0.0170  253 VAL A CG1 
1832 C CG2 . VAL A 253 ? 0.5776 0.6969 0.5045 -0.0461 0.0242  0.0086  253 VAL A CG2 
1833 N N   . THR A 254 ? 0.6363 0.7378 0.5764 -0.0527 0.0297  0.0398  254 THR A N   
1834 C CA  . THR A 254 ? 0.6273 0.7216 0.5711 -0.0531 0.0336  0.0494  254 THR A CA  
1835 C C   . THR A 254 ? 0.6083 0.7025 0.5552 -0.0578 0.0329  0.0566  254 THR A C   
1836 O O   . THR A 254 ? 0.6502 0.7405 0.5991 -0.0596 0.0368  0.0635  254 THR A O   
1837 C CB  . THR A 254 ? 0.6297 0.7165 0.5773 -0.0475 0.0332  0.0543  254 THR A CB  
1838 O OG1 . THR A 254 ? 0.6178 0.7041 0.5683 -0.0464 0.0279  0.0564  254 THR A OG1 
1839 C CG2 . THR A 254 ? 0.5823 0.6690 0.5268 -0.0425 0.0341  0.0475  254 THR A CG2 
1840 N N   . GLY A 255 ? 0.6208 0.7193 0.5680 -0.0597 0.0279  0.0551  255 GLY A N   
1841 C CA  . GLY A 255 ? 0.6189 0.7175 0.5692 -0.0638 0.0263  0.0620  255 GLY A CA  
1842 C C   . GLY A 255 ? 0.6311 0.7231 0.5873 -0.0616 0.0251  0.0713  255 GLY A C   
1843 O O   . GLY A 255 ? 0.6294 0.7210 0.5886 -0.0647 0.0240  0.0779  255 GLY A O   
1844 N N   . GLN A 256 ? 0.5927 0.6795 0.5505 -0.0562 0.0251  0.0719  256 GLN A N   
1845 C CA  . GLN A 256 ? 0.5732 0.6535 0.5366 -0.0535 0.0237  0.0800  256 GLN A CA  
1846 C C   . GLN A 256 ? 0.5152 0.5985 0.4798 -0.0537 0.0177  0.0784  256 GLN A C   
1847 O O   . GLN A 256 ? 0.5157 0.6035 0.4767 -0.0527 0.0150  0.0702  256 GLN A O   
1848 C CB  . GLN A 256 ? 0.5921 0.6661 0.5563 -0.0475 0.0256  0.0800  256 GLN A CB  
1849 C CG  . GLN A 256 ? 0.6279 0.6987 0.5906 -0.0467 0.0316  0.0807  256 GLN A CG  
1850 C CD  . GLN A 256 ? 0.6667 0.7316 0.6298 -0.0406 0.0329  0.0802  256 GLN A CD  
1851 O OE1 . GLN A 256 ? 0.7127 0.7796 0.6717 -0.0381 0.0336  0.0726  256 GLN A OE1 
1852 N NE2 . GLN A 256 ? 0.6672 0.7247 0.6353 -0.0380 0.0330  0.0882  256 GLN A NE2 
1853 N N   . SER A 257 ? 0.5077 0.5883 0.4772 -0.0548 0.0157  0.0863  257 SER A N   
1854 C CA  . SER A 257 ? 0.4840 0.5671 0.4550 -0.0552 0.0100  0.0855  257 SER A CA  
1855 C C   . SER A 257 ? 0.4759 0.5555 0.4476 -0.0495 0.0079  0.0829  257 SER A C   
1856 O O   . SER A 257 ? 0.4695 0.5432 0.4423 -0.0452 0.0108  0.0846  257 SER A O   
1857 C CB  . SER A 257 ? 0.4973 0.5786 0.4737 -0.0580 0.0085  0.0949  257 SER A CB  
1858 O OG  . SER A 257 ? 0.5239 0.5974 0.5053 -0.0544 0.0098  0.1023  257 SER A OG  
1859 N N   . ILE A 258 ? 0.4775 0.5604 0.4486 -0.0496 0.0032  0.0789  258 ILE A N   
1860 C CA  . ILE A 258 ? 0.5048 0.5844 0.4767 -0.0444 0.0010  0.0767  258 ILE A CA  
1861 C C   . ILE A 258 ? 0.5327 0.6042 0.5106 -0.0415 0.0016  0.0855  258 ILE A C   
1862 O O   . ILE A 258 ? 0.5397 0.6060 0.5181 -0.0362 0.0033  0.0853  258 ILE A O   
1863 C CB  . ILE A 258 ? 0.4758 0.5606 0.4460 -0.0456 -0.0042 0.0712  258 ILE A CB  
1864 C CG1 . ILE A 258 ? 0.5012 0.5931 0.4652 -0.0469 -0.0045 0.0613  258 ILE A CG1 
1865 C CG2 . ILE A 258 ? 0.5446 0.6252 0.5165 -0.0405 -0.0065 0.0705  258 ILE A CG2 
1866 C CD1 . ILE A 258 ? 0.5097 0.6009 0.4702 -0.0426 -0.0016 0.0555  258 ILE A CD1 
1867 N N   . PRO A 259 ? 0.5514 0.6221 0.5339 -0.0447 0.0004  0.0933  259 PRO A N   
1868 C CA  . PRO A 259 ? 0.5888 0.6518 0.5773 -0.0421 0.0011  0.1020  259 PRO A CA  
1869 C C   . PRO A 259 ? 0.6198 0.6765 0.6093 -0.0391 0.0064  0.1059  259 PRO A C   
1870 O O   . PRO A 259 ? 0.5950 0.6448 0.5873 -0.0344 0.0074  0.1090  259 PRO A O   
1871 C CB  . PRO A 259 ? 0.6031 0.6681 0.5954 -0.0472 -0.0005 0.1091  259 PRO A CB  
1872 C CG  . PRO A 259 ? 0.5991 0.6722 0.5878 -0.0513 -0.0042 0.1029  259 PRO A CG  
1873 C CD  . PRO A 259 ? 0.6090 0.6857 0.5914 -0.0507 -0.0023 0.0942  259 PRO A CD  
1874 N N   . GLU A 260 ? 0.6200 0.6789 0.6070 -0.0418 0.0099  0.1055  260 GLU A N   
1875 C CA  . GLU A 260 ? 0.6100 0.6634 0.5971 -0.0394 0.0153  0.1085  260 GLU A CA  
1876 C C   . GLU A 260 ? 0.5980 0.6489 0.5819 -0.0338 0.0164  0.1020  260 GLU A C   
1877 O O   . GLU A 260 ? 0.6700 0.7139 0.6558 -0.0299 0.0193  0.1056  260 GLU A O   
1878 C CB  . GLU A 260 ? 0.6290 0.6859 0.6132 -0.0437 0.0188  0.1080  260 GLU A CB  
1879 C CG  . GLU A 260 ? 0.6905 0.7413 0.6755 -0.0421 0.0248  0.1127  260 GLU A CG  
1880 C CD  . GLU A 260 ? 0.7215 0.7761 0.7025 -0.0458 0.0288  0.1101  260 GLU A CD  
1881 O OE1 . GLU A 260 ? 0.6989 0.7505 0.6775 -0.0436 0.0331  0.1083  260 GLU A OE1 
1882 O OE2 . GLU A 260 ? 0.7410 0.8011 0.7210 -0.0508 0.0277  0.1100  260 GLU A OE2 
1883 N N   . LEU A 261 ? 0.5155 0.5722 0.4946 -0.0335 0.0140  0.0927  261 LEU A N   
1884 C CA  . LEU A 261 ? 0.4910 0.5465 0.4668 -0.0283 0.0148  0.0860  261 LEU A CA  
1885 C C   . LEU A 261 ? 0.5005 0.5508 0.4791 -0.0231 0.0125  0.0873  261 LEU A C   
1886 O O   . LEU A 261 ? 0.4937 0.5385 0.4723 -0.0180 0.0147  0.0873  261 LEU A O   
1887 C CB  . LEU A 261 ? 0.4711 0.5349 0.4409 -0.0295 0.0131  0.0757  261 LEU A CB  
1888 C CG  . LEU A 261 ? 0.4937 0.5624 0.4599 -0.0337 0.0161  0.0727  261 LEU A CG  
1889 C CD1 . LEU A 261 ? 0.5103 0.5875 0.4715 -0.0356 0.0133  0.0632  261 LEU A CD1 
1890 C CD2 . LEU A 261 ? 0.5125 0.5776 0.4769 -0.0310 0.0212  0.0722  261 LEU A CD2 
1891 N N   . GLU A 262 ? 0.5024 0.5542 0.4832 -0.0245 0.0081  0.0885  262 GLU A N   
1892 C CA  . GLU A 262 ? 0.5553 0.6018 0.5395 -0.0203 0.0060  0.0907  262 GLU A CA  
1893 C C   . GLU A 262 ? 0.5982 0.6355 0.5872 -0.0172 0.0091  0.0993  262 GLU A C   
1894 O O   . GLU A 262 ? 0.6297 0.6612 0.6196 -0.0117 0.0095  0.0993  262 GLU A O   
1895 C CB  . GLU A 262 ? 0.5833 0.6327 0.5701 -0.0235 0.0014  0.0924  262 GLU A CB  
1896 C CG  . GLU A 262 ? 0.6006 0.6571 0.5829 -0.0245 -0.0023 0.0835  262 GLU A CG  
1897 C CD  . GLU A 262 ? 0.6159 0.6760 0.6002 -0.0287 -0.0066 0.0850  262 GLU A CD  
1898 O OE1 . GLU A 262 ? 0.6921 0.7532 0.6794 -0.0333 -0.0067 0.0911  262 GLU A OE1 
1899 O OE2 . GLU A 262 ? 0.5947 0.6569 0.5775 -0.0276 -0.0099 0.0800  262 GLU A OE2 
1900 N N   . LYS A 263 ? 0.6157 0.6515 0.6076 -0.0205 0.0116  0.1064  263 LYS A N   
1901 C CA  . LYS A 263 ? 0.6565 0.6836 0.6527 -0.0180 0.0152  0.1146  263 LYS A CA  
1902 C C   . LYS A 263 ? 0.6463 0.6700 0.6393 -0.0144 0.0197  0.1120  263 LYS A C   
1903 O O   . LYS A 263 ? 0.6587 0.6751 0.6536 -0.0094 0.0214  0.1146  263 LYS A O   
1904 C CB  . LYS A 263 ? 0.6469 0.6737 0.6470 -0.0228 0.0166  0.1231  263 LYS A CB  
1905 N N   . GLN A 264 ? 0.6705 0.6996 0.6587 -0.0169 0.0215  0.1067  264 GLN A N   
1906 C CA  . GLN A 264 ? 0.6934 0.7207 0.6779 -0.0142 0.0258  0.1033  264 GLN A CA  
1907 C C   . GLN A 264 ? 0.6845 0.7091 0.6667 -0.0078 0.0251  0.0978  264 GLN A C   
1908 O O   . GLN A 264 ? 0.6478 0.6673 0.6292 -0.0041 0.0287  0.0982  264 GLN A O   
1909 C CB  . GLN A 264 ? 0.7032 0.7382 0.6825 -0.0184 0.0269  0.0971  264 GLN A CB  
1910 C CG  . GLN A 264 ? 0.7553 0.7894 0.7305 -0.0163 0.0314  0.0930  264 GLN A CG  
1911 C CD  . GLN A 264 ? 0.7761 0.8171 0.7473 -0.0213 0.0334  0.0888  264 GLN A CD  
1912 O OE1 . GLN A 264 ? 0.8070 0.8493 0.7798 -0.0261 0.0344  0.0935  264 GLN A OE1 
1913 N NE2 . GLN A 264 ? 0.7853 0.8307 0.7510 -0.0200 0.0340  0.0799  264 GLN A NE2 
1914 N N   . PHE A 265 ? 0.6507 0.6787 0.6320 -0.0065 0.0206  0.0929  265 PHE A N   
1915 C CA  . PHE A 265 ? 0.6506 0.6770 0.6296 -0.0005 0.0195  0.0873  265 PHE A CA  
1916 C C   . PHE A 265 ? 0.6717 0.6920 0.6551 0.0031  0.0172  0.0915  265 PHE A C   
1917 O O   . PHE A 265 ? 0.6156 0.6360 0.5973 0.0072  0.0150  0.0865  265 PHE A O   
1918 C CB  . PHE A 265 ? 0.6202 0.6556 0.5939 -0.0014 0.0166  0.0772  265 PHE A CB  
1919 C CG  . PHE A 265 ? 0.6159 0.6570 0.5847 -0.0039 0.0190  0.0717  265 PHE A CG  
1920 C CD1 . PHE A 265 ? 0.6161 0.6638 0.5838 -0.0102 0.0185  0.0709  265 PHE A CD1 
1921 C CD2 . PHE A 265 ? 0.6083 0.6484 0.5735 0.0000  0.0219  0.0673  265 PHE A CD2 
1922 C CE1 . PHE A 265 ? 0.6252 0.6780 0.5885 -0.0126 0.0210  0.0658  265 PHE A CE1 
1923 C CE2 . PHE A 265 ? 0.5931 0.6387 0.5540 -0.0024 0.0243  0.0622  265 PHE A CE2 
1924 C CZ  . PHE A 265 ? 0.6106 0.6625 0.5705 -0.0088 0.0239  0.0614  265 PHE A CZ  
1925 N N   . GLU A 266 ? 0.6401 0.6551 0.6293 0.0017  0.0178  0.1007  266 GLU A N   
1926 C CA  . GLU A 266 ? 0.6770 0.6858 0.6707 0.0049  0.0159  0.1051  266 GLU A CA  
1927 C C   . GLU A 266 ? 0.6229 0.6239 0.6163 0.0119  0.0184  0.1051  266 GLU A C   
1928 O O   . GLU A 266 ? 0.6032 0.6000 0.5962 0.0133  0.0225  0.1075  266 GLU A O   
1929 C CB  . GLU A 266 ? 0.6929 0.6983 0.6930 0.0016  0.0159  0.1151  266 GLU A CB  
1930 C CG  . GLU A 266 ? 0.7272 0.7299 0.7318 0.0028  0.0124  0.1181  266 GLU A CG  
1931 C CD  . GLU A 266 ? 0.7056 0.7033 0.7170 0.0008  0.0131  0.1286  266 GLU A CD  
1932 N N   . GLY A 267 ? 0.6154 0.6145 0.6087 0.0163  0.0160  0.1021  267 GLY A N   
1933 C CA  . GLY A 267 ? 0.6611 0.6532 0.6534 0.0234  0.0181  0.1010  267 GLY A CA  
1934 C C   . GLY A 267 ? 0.7046 0.6999 0.6905 0.0261  0.0198  0.0931  267 GLY A C   
1935 O O   . GLY A 267 ? 0.6463 0.6359 0.6311 0.0316  0.0224  0.0927  267 GLY A O   
1936 N N   . LYS A 268 ? 0.7310 0.7356 0.7128 0.0223  0.0184  0.0867  268 LYS A N   
1937 C CA  . LYS A 268 ? 0.7208 0.7299 0.6965 0.0240  0.0199  0.0788  268 LYS A CA  
1938 C C   . LYS A 268 ? 0.6723 0.6878 0.6441 0.0257  0.0163  0.0701  268 LYS A C   
1939 O O   . LYS A 268 ? 0.6555 0.6737 0.6286 0.0237  0.0127  0.0697  268 LYS A O   
1940 C CB  . LYS A 268 ? 0.7317 0.7461 0.7055 0.0185  0.0220  0.0782  268 LYS A CB  
1941 C CG  . LYS A 268 ? 0.7936 0.8020 0.7714 0.0164  0.0257  0.0871  268 LYS A CG  
1942 C CD  . LYS A 268 ? 0.8509 0.8514 0.8286 0.0215  0.0297  0.0894  268 LYS A CD  
1943 C CE  . LYS A 268 ? 0.9107 0.9143 0.8835 0.0209  0.0332  0.0848  268 LYS A CE  
1944 N NZ  . LYS A 268 ? 0.9562 0.9609 0.9302 0.0151  0.0360  0.0893  268 LYS A NZ  
1945 N N   . MET A 269 ? 0.6381 0.6555 0.6051 0.0297  0.0175  0.0635  269 MET A N   
1946 C CA  . MET A 269 ? 0.6227 0.6457 0.5852 0.0323  0.0149  0.0547  269 MET A CA  
1947 C C   . MET A 269 ? 0.5946 0.6278 0.5527 0.0280  0.0142  0.0478  269 MET A C   
1948 O O   . MET A 269 ? 0.5878 0.6231 0.5455 0.0237  0.0165  0.0491  269 MET A O   
1949 C CB  . MET A 269 ? 0.6258 0.6447 0.5857 0.0398  0.0167  0.0517  269 MET A CB  
1950 C CG  . MET A 269 ? 0.6292 0.6371 0.5933 0.0443  0.0184  0.0589  269 MET A CG  
1951 S SD  . MET A 269 ? 0.6603 0.6643 0.6286 0.0456  0.0148  0.0621  269 MET A SD  
1952 C CE  . MET A 269 ? 0.7119 0.7070 0.6874 0.0434  0.0168  0.0739  269 MET A CE  
1953 N N   . TYR A 270 ? 0.6944 0.7938 0.6845 -0.0261 0.0265  0.1392  270 TYR A N   
1954 C CA  . TYR A 270 ? 0.6700 0.7590 0.6197 -0.0311 0.0109  0.0999  270 TYR A CA  
1955 C C   . TYR A 270 ? 0.6384 0.7365 0.5321 -0.0278 0.0389  0.0650  270 TYR A C   
1956 O O   . TYR A 270 ? 0.6868 0.7763 0.5524 -0.0319 0.0367  0.0341  270 TYR A O   
1957 C CB  . TYR A 270 ? 0.6231 0.7068 0.5623 -0.0337 -0.0300 0.0944  270 TYR A CB  
1958 C CG  . TYR A 270 ? 0.5606 0.6349 0.5532 -0.0373 -0.0602 0.1275  270 TYR A CG  
1959 C CD1 . TYR A 270 ? 0.5490 0.6144 0.5920 -0.0405 -0.0569 0.1517  270 TYR A CD1 
1960 C CD2 . TYR A 270 ? 0.5650 0.6390 0.5570 -0.0375 -0.0926 0.1340  270 TYR A CD2 
1961 C CE1 . TYR A 270 ? 0.5609 0.6178 0.6526 -0.0436 -0.0844 0.1820  270 TYR A CE1 
1962 C CE2 . TYR A 270 ? 0.5746 0.6400 0.6149 -0.0406 -0.1207 0.1640  270 TYR A CE2 
1963 C CZ  . TYR A 270 ? 0.5675 0.6243 0.6577 -0.0437 -0.1165 0.1881  270 TYR A CZ  
1964 O OH  . TYR A 270 ? 0.5700 0.6182 0.7077 -0.0469 -0.1444 0.2178  270 TYR A OH  
1965 N N   . GLY A 271 ? 0.6772 0.7926 0.5553 -0.0204 0.0660  0.0704  271 GLY A N   
1966 C CA  . GLY A 271 ? 0.6950 0.8200 0.5232 -0.0167 0.0967  0.0403  271 GLY A CA  
1967 C C   . GLY A 271 ? 0.6820 0.8026 0.5154 -0.0184 0.1243  0.0319  271 GLY A C   
1968 O O   . GLY A 271 ? 0.6507 0.7690 0.4429 -0.0198 0.1336  -0.0027 271 GLY A O   
1969 N N   . HIS A 272 ? 0.6402 0.7594 0.5245 -0.0184 0.1364  0.0634  272 HIS A N   
1970 C CA  . HIS A 272 ? 0.6411 0.7548 0.5366 -0.0204 0.1605  0.0585  272 HIS A CA  
1971 C C   . HIS A 272 ? 0.6557 0.7511 0.5435 -0.0285 0.1384  0.0346  272 HIS A C   
1972 O O   . HIS A 272 ? 0.6491 0.7416 0.5090 -0.0301 0.1552  0.0071  272 HIS A O   
1973 C CB  . HIS A 272 ? 0.6203 0.7327 0.5770 -0.0202 0.1705  0.0980  272 HIS A CB  
1974 C CG  . HIS A 272 ? 0.6490 0.7770 0.6258 -0.0134 0.1843  0.1290  272 HIS A CG  
1975 N ND1 . HIS A 272 ? 0.6784 0.8231 0.6367 -0.0065 0.2214  0.1282  272 HIS A ND1 
1976 C CD2 . HIS A 272 ? 0.6471 0.7767 0.6605 -0.0126 0.1653  0.1618  272 HIS A CD2 
1977 C CE1 . HIS A 272 ? 0.6818 0.8377 0.6652 -0.0018 0.2247  0.1594  272 HIS A CE1 
1978 N NE2 . HIS A 272 ? 0.6612 0.8083 0.6779 -0.0053 0.1909  0.1802  272 HIS A NE2 
1979 N N   . LEU A 273 ? 0.6213 0.7045 0.5355 -0.0337 0.1010  0.0461  273 LEU A N   
1980 C CA  . LEU A 273 ? 0.6361 0.7014 0.5455 -0.0418 0.0766  0.0251  273 LEU A CA  
1981 C C   . LEU A 273 ? 0.6351 0.7011 0.4816 -0.0425 0.0744  -0.0188 273 LEU A C   
1982 O O   . LEU A 273 ? 0.5703 0.6291 0.3960 -0.0460 0.0836  -0.0451 273 LEU A O   
1983 C CB  . LEU A 273 ? 0.5992 0.6535 0.5414 -0.0465 0.0349  0.0434  273 LEU A CB  
1984 C CG  . LEU A 273 ? 0.5770 0.6129 0.5137 -0.0551 0.0049  0.0219  273 LEU A CG  
1985 C CD1 . LEU A 273 ? 0.5397 0.5655 0.4908 -0.0595 0.0206  0.0157  273 LEU A CD1 
1986 C CD2 . LEU A 273 ? 0.5404 0.5669 0.5148 -0.0589 -0.0337 0.0453  273 LEU A CD2 
1987 N N   . LYS A 274 ? 0.6109 0.6858 0.4281 -0.0390 0.0628  -0.0258 274 LYS A N   
1988 C CA  . LYS A 274 ? 0.6479 0.7244 0.4044 -0.0393 0.0577  -0.0662 274 LYS A CA  
1989 C C   . LYS A 274 ? 0.6634 0.7418 0.3911 -0.0334 0.0918  -0.0878 274 LYS A C   
1990 O O   . LYS A 274 ? 0.6580 0.7089 0.3888 -0.0234 0.0754  -0.1000 274 LYS A O   
1991 C CB  . LYS A 274 ? 0.6485 0.7364 0.3826 -0.0345 0.0457  -0.0649 274 LYS A CB  
1992 C CG  . LYS A 274 ? 0.6372 0.7158 0.3895 -0.0386 0.0020  -0.0547 274 LYS A CG  
1993 C CD  . LYS A 274 ? 0.6325 0.7233 0.3675 -0.0334 -0.0078 -0.0491 274 LYS A CD  
1994 C CE  . LYS A 274 ? 0.6364 0.7173 0.3787 -0.0378 -0.0526 -0.0475 274 LYS A CE  
1995 N NZ  . LYS A 274 ? 0.6409 0.7334 0.3749 -0.0327 -0.0627 -0.0358 274 LYS A NZ  
1996 N N   . GLY A 275 ? 0.7405 0.8333 0.4764 -0.0278 0.1264  -0.0715 275 GLY A N   
1997 C CA  . GLY A 275 ? 0.7329 0.8102 0.4737 -0.0091 0.1411  -0.0723 275 GLY A CA  
1998 C C   . GLY A 275 ? 0.7569 0.8247 0.5132 -0.0109 0.1425  -0.0789 275 GLY A C   
1999 O O   . GLY A 275 ? 0.7946 0.8465 0.5481 0.0030  0.1331  -0.0851 275 GLY A O   
2000 N N   . GLU A 276 ? 0.7480 0.8237 0.5216 -0.0294 0.1550  -0.0734 276 GLU A N   
2001 C CA  . GLU A 276 ? 0.7825 0.8467 0.5733 -0.0340 0.1592  -0.0788 276 GLU A CA  
2002 C C   . GLU A 276 ? 0.7047 0.7498 0.4864 -0.0372 0.1250  -0.1004 276 GLU A C   
2003 O O   . GLU A 276 ? 0.7047 0.7385 0.4952 -0.0322 0.1192  -0.1060 276 GLU A O   
2004 C CB  . GLU A 276 ? 0.7883 0.8506 0.6278 -0.0436 0.1677  -0.0488 276 GLU A CB  
2005 C CG  . GLU A 276 ? 0.8618 0.9134 0.7215 -0.0480 0.1814  -0.0510 276 GLU A CG  
2006 C CD  . GLU A 276 ? 0.9108 0.9710 0.7580 -0.0357 0.2009  -0.0591 276 GLU A CD  
2007 O OE1 . GLU A 276 ? 0.9802 1.0575 0.8396 -0.0269 0.2184  -0.0397 276 GLU A OE1 
2008 O OE2 . GLU A 276 ? 0.9346 0.9849 0.7709 -0.0303 0.1824  -0.0770 276 GLU A OE2 
2009 N N   . VAL A 277 ? 0.6566 0.7000 0.4253 -0.0454 0.1001  -0.1074 277 VAL A N   
2010 C CA  . VAL A 277 ? 0.6068 0.6307 0.3790 -0.0433 0.0637  -0.1183 277 VAL A CA  
2011 C C   . VAL A 277 ? 0.5763 0.5837 0.3457 -0.0199 0.0547  -0.1150 277 VAL A C   
2012 O O   . VAL A 277 ? 0.5917 0.5971 0.3739 -0.0256 0.0496  -0.1215 277 VAL A O   
2013 C CB  . VAL A 277 ? 0.5764 0.5995 0.3422 -0.0512 0.0329  -0.1194 277 VAL A CB  
2014 C CG1 . VAL A 277 ? 0.5767 0.5721 0.3542 -0.0365 0.0004  -0.1186 277 VAL A CG1 
2015 C CG2 . VAL A 277 ? 0.5642 0.5855 0.3672 -0.0644 0.0216  -0.0974 277 VAL A CG2 
2016 N N   . ALA A 278 ? 0.6003 0.6133 0.3561 -0.0133 0.0611  -0.1128 278 ALA A N   
2017 C CA  . ALA A 278 ? 0.6514 0.6713 0.4073 -0.0161 0.0620  -0.1215 278 ALA A CA  
2018 C C   . ALA A 278 ? 0.6666 0.6924 0.4308 -0.0184 0.0781  -0.1252 278 ALA A C   
2019 O O   . ALA A 278 ? 0.6881 0.7177 0.4600 -0.0251 0.0735  -0.1334 278 ALA A O   
2020 C CB  . ALA A 278 ? 0.6627 0.6871 0.4021 -0.0099 0.0673  -0.1187 278 ALA A CB  
2021 N N   . ASP A 279 ? 0.6957 0.7239 0.4602 -0.0124 0.0977  -0.1171 279 ASP A N   
2022 C CA  . ASP A 279 ? 0.7566 0.7884 0.5299 -0.0145 0.1124  -0.1193 279 ASP A CA  
2023 C C   . ASP A 279 ? 0.7359 0.7613 0.5250 -0.0249 0.1038  -0.1254 279 ASP A C   
2024 O O   . ASP A 279 ? 0.7194 0.7463 0.5145 -0.0319 0.1045  -0.1328 279 ASP A O   
2025 C CB  . ASP A 279 ? 0.7842 0.8245 0.5619 -0.0048 0.1359  -0.1050 279 ASP A CB  
2026 C CG  . ASP A 279 ? 0.8601 0.9115 0.6261 0.0063  0.1492  -0.0963 279 ASP A CG  
2027 O OD1 . ASP A 279 ? 0.8560 0.9046 0.6073 0.0058  0.1423  -0.1044 279 ASP A OD1 
2028 O OD2 . ASP A 279 ? 0.8465 0.9144 0.6233 0.0150  0.1675  -0.0790 279 ASP A OD2 
2029 N N   . ALA A 280 ? 0.6678 0.6863 0.4638 -0.0258 0.0967  -0.1212 280 ALA A N   
2030 C CA  . ALA A 280 ? 0.6694 0.6807 0.4809 -0.0351 0.0880  -0.1257 280 ALA A CA  
2031 C C   . ALA A 280 ? 0.6136 0.6273 0.4305 -0.0427 0.0711  -0.1339 280 ALA A C   
2032 O O   . ALA A 280 ? 0.5866 0.6036 0.4141 -0.0496 0.0736  -0.1384 280 ALA A O   
2033 C CB  . ALA A 280 ? 0.6814 0.6833 0.4971 -0.0338 0.0806  -0.1202 280 ALA A CB  
2034 N N   . VAL A 281 ? 0.6144 0.6285 0.4249 -0.0403 0.0564  -0.1341 281 VAL A N   
2035 C CA  . VAL A 281 ? 0.6182 0.6376 0.4357 -0.0440 0.0434  -0.1386 281 VAL A CA  
2036 C C   . VAL A 281 ? 0.6647 0.6965 0.4829 -0.0470 0.0528  -0.1447 281 VAL A C   
2037 O O   . VAL A 281 ? 0.6774 0.7147 0.5078 -0.0527 0.0524  -0.1481 281 VAL A O   
2038 C CB  . VAL A 281 ? 0.6302 0.6465 0.4395 -0.0394 0.0280  -0.1366 281 VAL A CB  
2039 C CG1 . VAL A 281 ? 0.6191 0.6431 0.4341 -0.0407 0.0201  -0.1405 281 VAL A CG1 
2040 C CG2 . VAL A 281 ? 0.6071 0.6085 0.4184 -0.0383 0.0126  -0.1311 281 VAL A CG2 
2041 N N   . SER A 282 ? 0.7180 0.7539 0.5227 -0.0427 0.0613  -0.1456 282 SER A N   
2042 C CA  . SER A 282 ? 0.7125 0.7583 0.5154 -0.0449 0.0694  -0.1516 282 SER A CA  
2043 C C   . SER A 282 ? 0.6788 0.7245 0.4892 -0.0504 0.0807  -0.1540 282 SER A C   
2044 O O   . SER A 282 ? 0.7641 0.8176 0.5796 -0.0556 0.0825  -0.1596 282 SER A O   
2045 C CB  . SER A 282 ? 0.7451 0.7928 0.5306 -0.0379 0.0774  -0.1508 282 SER A CB  
2046 O OG  . SER A 282 ? 0.7475 0.7954 0.5259 -0.0339 0.0666  -0.1491 282 SER A OG  
2047 N N   . GLY A 283 ? 0.7012 0.7382 0.5130 -0.0494 0.0884  -0.1493 283 GLY A N   
2048 C CA  . GLY A 283 ? 0.7065 0.7409 0.5278 -0.0553 0.0980  -0.1507 283 GLY A CA  
2049 C C   . GLY A 283 ? 0.7576 0.7946 0.5958 -0.0643 0.0890  -0.1536 283 GLY A C   
2050 O O   . GLY A 283 ? 0.7472 0.7870 0.5925 -0.0710 0.0948  -0.1575 283 GLY A O   
2051 N N   . MET A 284 ? 0.7380 0.7738 0.5821 -0.0637 0.0754  -0.1510 284 MET A N   
2052 C CA  . MET A 284 ? 0.6802 0.7192 0.5399 -0.0692 0.0672  -0.1516 284 MET A CA  
2053 C C   . MET A 284 ? 0.6445 0.6968 0.5072 -0.0708 0.0627  -0.1564 284 MET A C   
2054 O O   . MET A 284 ? 0.6427 0.7019 0.5160 -0.0767 0.0651  -0.1593 284 MET A O   
2055 C CB  . MET A 284 ? 0.6434 0.6742 0.5062 -0.0655 0.0541  -0.1462 284 MET A CB  
2056 C CG  . MET A 284 ? 0.6031 0.6353 0.4798 -0.0681 0.0460  -0.1453 284 MET A CG  
2057 S SD  . MET A 284 ? 0.5487 0.5659 0.4253 -0.0618 0.0285  -0.1387 284 MET A SD  
2058 C CE  . MET A 284 ? 0.4926 0.5109 0.3563 -0.0550 0.0179  -0.1391 284 MET A CE  
2059 N N   . LEU A 285 ? 0.6646 0.7206 0.5180 -0.0654 0.0571  -0.1573 285 LEU A N   
2060 C CA  . LEU A 285 ? 0.6738 0.7421 0.5298 -0.0658 0.0531  -0.1617 285 LEU A CA  
2061 C C   . LEU A 285 ? 0.7758 0.8533 0.6322 -0.0712 0.0633  -0.1679 285 LEU A C   
2062 O O   . LEU A 285 ? 0.8477 0.9363 0.7112 -0.0738 0.0614  -0.1718 285 LEU A O   
2063 C CB  . LEU A 285 ? 0.6212 0.6900 0.4657 -0.0591 0.0466  -0.1613 285 LEU A CB  
2064 C CG  . LEU A 285 ? 0.6051 0.6637 0.4473 -0.0536 0.0345  -0.1557 285 LEU A CG  
2065 C CD1 . LEU A 285 ? 0.6348 0.6940 0.4648 -0.0479 0.0296  -0.1557 285 LEU A CD1 
2066 C CD2 . LEU A 285 ? 0.6202 0.6780 0.4741 -0.0536 0.0248  -0.1541 285 LEU A CD2 
2067 N N   . THR A 286 ? 0.8828 0.9548 0.7312 -0.0721 0.0743  -0.1686 286 THR A N   
2068 C CA  . THR A 286 ? 0.8975 0.9751 0.7428 -0.0760 0.0840  -0.1743 286 THR A CA  
2069 C C   . THR A 286 ? 0.8215 0.9044 0.6809 -0.0845 0.0863  -0.1774 286 THR A C   
2070 O O   . THR A 286 ? 0.8118 0.9049 0.6733 -0.0877 0.0873  -0.1826 286 THR A O   
2071 C CB  . THR A 286 ? 0.9096 0.9777 0.7414 -0.0727 0.0962  -0.1733 286 THR A CB  
2072 O OG1 . THR A 286 ? 0.8587 0.9256 0.6763 -0.0643 0.0951  -0.1711 286 THR A OG1 
2073 C CG2 . THR A 286 ? 0.9167 0.9879 0.7449 -0.0764 0.1067  -0.1789 286 THR A CG2 
2074 N N   . GLU A 287 ? 0.7720 0.8482 0.6407 -0.0883 0.0877  -0.1741 287 GLU A N   
2075 C CA  . GLU A 287 ? 0.8109 0.8924 0.6934 -0.0966 0.0899  -0.1764 287 GLU A CA  
2076 C C   . GLU A 287 ? 0.7622 0.8555 0.6564 -0.0967 0.0802  -0.1765 287 GLU A C   
2077 O O   . GLU A 287 ? 0.7773 0.8801 0.6801 -0.1020 0.0818  -0.1800 287 GLU A O   
2078 C CB  . GLU A 287 ? 0.7962 0.8670 0.6857 -0.1006 0.0947  -0.1727 287 GLU A CB  
2079 C CG  . GLU A 287 ? 0.7930 0.8683 0.6956 -0.1096 0.0987  -0.1750 287 GLU A CG  
2080 C CD  . GLU A 287 ? 0.7958 0.8779 0.6949 -0.1139 0.1051  -0.1818 287 GLU A CD  
2081 N N   . LEU A 288 ? 0.7352 0.8268 0.6286 -0.0901 0.0706  -0.1724 288 LEU A N   
2082 C CA  . LEU A 288 ? 0.6736 0.7740 0.5743 -0.0871 0.0614  -0.1723 288 LEU A CA  
2083 C C   . LEU A 288 ? 0.6816 0.7943 0.5792 -0.0869 0.0616  -0.1781 288 LEU A C   
2084 O O   . LEU A 288 ? 0.6729 0.7965 0.5797 -0.0899 0.0613  -0.1811 288 LEU A O   
2085 C CB  . LEU A 288 ? 0.6209 0.7131 0.5176 -0.0790 0.0509  -0.1669 288 LEU A CB  
2086 C CG  . LEU A 288 ? 0.6264 0.7085 0.5297 -0.0782 0.0471  -0.1611 288 LEU A CG  
2087 C CD1 . LEU A 288 ? 0.6511 0.7204 0.5461 -0.0707 0.0378  -0.1559 288 LEU A CD1 
2088 C CD2 . LEU A 288 ? 0.6406 0.7287 0.5553 -0.0781 0.0427  -0.1607 288 LEU A CD2 
2089 N N   . GLN A 289 ? 0.6495 0.7604 0.5340 -0.0831 0.0623  -0.1795 289 GLN A N   
2090 C CA  . GLN A 289 ? 0.7071 0.8285 0.5867 -0.0822 0.0626  -0.1849 289 GLN A CA  
2091 C C   . GLN A 289 ? 0.7601 0.8891 0.6430 -0.0895 0.0711  -0.1907 289 GLN A C   
2092 O O   . GLN A 289 ? 0.7535 0.8946 0.6409 -0.0909 0.0699  -0.1950 289 GLN A O   
2093 C CB  . GLN A 289 ? 0.7111 0.8275 0.5746 -0.0766 0.0632  -0.1847 289 GLN A CB  
2094 C CG  . GLN A 289 ? 0.7275 0.8410 0.5877 -0.0692 0.0530  -0.1809 289 GLN A CG  
2095 C CD  . GLN A 289 ? 0.7120 0.8175 0.5563 -0.0639 0.0539  -0.1788 289 GLN A CD  
2096 O OE1 . GLN A 289 ? 0.7477 0.8521 0.5820 -0.0643 0.0626  -0.1810 289 GLN A OE1 
2097 N NE2 . GLN A 289 ? 0.6750 0.7740 0.5161 -0.0582 0.0452  -0.1742 289 GLN A NE2 
2098 N N   . GLU A 290 ? 0.7866 0.9077 0.6672 -0.0940 0.0795  -0.1907 290 GLU A N   
2099 C CA  . GLU A 290 ? 0.8327 0.9581 0.7157 -0.1011 0.0876  -0.1959 290 GLU A CA  
2100 C C   . GLU A 290 ? 0.8225 0.9589 0.7217 -0.1063 0.0849  -0.1972 290 GLU A C   
2101 O O   . GLU A 290 ? 0.8958 1.0432 0.7976 -0.1090 0.0859  -0.2022 290 GLU A O   
2102 C CB  . GLU A 290 ? 0.9161 1.0287 0.7951 -0.1045 0.0968  -0.1946 290 GLU A CB  
2103 C CG  . GLU A 290 ? 0.9632 1.0769 0.8397 -0.1105 0.1062  -0.2003 290 GLU A CG  
2104 C CD  . GLU A 290 ? 0.9752 1.0944 0.8670 -0.1190 0.1073  -0.2017 290 GLU A CD  
2105 O OE1 . GLU A 290 ? 0.9900 1.1041 0.8911 -0.1214 0.1063  -0.1974 290 GLU A OE1 
2106 O OE2 . GLU A 290 ? 1.0445 1.1732 0.9391 -0.1234 0.1093  -0.2070 290 GLU A OE2 
2107 N N   . ARG A 291 ? 0.7500 0.8832 0.6597 -0.1071 0.0818  -0.1924 291 ARG A N   
2108 C CA  . ARG A 291 ? 0.7074 0.8504 0.6321 -0.1106 0.0794  -0.1926 291 ARG A CA  
2109 C C   . ARG A 291 ? 0.5951 0.7500 0.5231 -0.1056 0.0719  -0.1941 291 ARG A C   
2110 O O   . ARG A 291 ? 0.5913 0.7578 0.5274 -0.1090 0.0728  -0.1977 291 ARG A O   
2111 C CB  . ARG A 291 ? 0.7212 0.8570 0.6543 -0.1106 0.0774  -0.1864 291 ARG A CB  
2112 C CG  . ARG A 291 ? 0.7270 0.8538 0.6616 -0.1176 0.0858  -0.1857 291 ARG A CG  
2113 C CD  . ARG A 291 ? 0.6738 0.7893 0.6110 -0.1153 0.0836  -0.1789 291 ARG A CD  
2114 N NE  . ARG A 291 ? 0.6471 0.7669 0.5937 -0.1112 0.0759  -0.1751 291 ARG A NE  
2115 C CZ  . ARG A 291 ? 0.6319 0.7585 0.5905 -0.1149 0.0769  -0.1749 291 ARG A CZ  
2116 N NH1 . ARG A 291 ? 0.6372 0.7682 0.6014 -0.1238 0.0849  -0.1784 291 ARG A NH1 
2117 N NH2 . ARG A 291 ? 0.5750 0.7029 0.5390 -0.1090 0.0695  -0.1712 291 ARG A NH2 
2118 N N   . TYR A 292 ? 0.5558 0.7070 0.4770 -0.0977 0.0650  -0.1914 292 TYR A N   
2119 C CA  . TYR A 292 ? 0.5587 0.7185 0.4815 -0.0920 0.0577  -0.1925 292 TYR A CA  
2120 C C   . TYR A 292 ? 0.5866 0.7591 0.5083 -0.0947 0.0608  -0.1994 292 TYR A C   
2121 O O   . TYR A 292 ? 0.6296 0.8132 0.5610 -0.0967 0.0603  -0.2019 292 TYR A O   
2122 C CB  . TYR A 292 ? 0.5765 0.7282 0.4897 -0.0836 0.0505  -0.1890 292 TYR A CB  
2123 C CG  . TYR A 292 ? 0.5633 0.7231 0.4767 -0.0781 0.0439  -0.1909 292 TYR A CG  
2124 C CD1 . TYR A 292 ? 0.5888 0.7512 0.5111 -0.0746 0.0378  -0.1892 292 TYR A CD1 
2125 C CD2 . TYR A 292 ? 0.5623 0.7269 0.4668 -0.0762 0.0442  -0.1947 292 TYR A CD2 
2126 C CE1 . TYR A 292 ? 0.5831 0.7523 0.5057 -0.0695 0.0323  -0.1912 292 TYR A CE1 
2127 C CE2 . TYR A 292 ? 0.5913 0.7637 0.4968 -0.0714 0.0386  -0.1966 292 TYR A CE2 
2128 C CZ  . TYR A 292 ? 0.5692 0.7438 0.4840 -0.0682 0.0327  -0.1950 292 TYR A CZ  
2129 O OH  . TYR A 292 ? 0.5319 0.7133 0.4477 -0.0633 0.0273  -0.1970 292 TYR A OH  
2130 N N   . HIS A 293 ? 0.5873 0.7578 0.4969 -0.0946 0.0645  -0.2022 293 HIS A N   
2131 C CA  . HIS A 293 ? 0.6274 0.8083 0.5334 -0.0966 0.0677  -0.2088 293 HIS A CA  
2132 C C   . HIS A 293 ? 0.6680 0.8564 0.5823 -0.1049 0.0738  -0.2130 293 HIS A C   
2133 O O   . HIS A 293 ? 0.7308 0.9314 0.6489 -0.1064 0.0738  -0.2177 293 HIS A O   
2134 C CB  . HIS A 293 ? 0.6315 0.8060 0.5213 -0.0950 0.0721  -0.2105 293 HIS A CB  
2135 C CG  . HIS A 293 ? 0.6445 0.8141 0.5251 -0.0870 0.0662  -0.2074 293 HIS A CG  
2136 N ND1 . HIS A 293 ? 0.6873 0.8648 0.5690 -0.0821 0.0595  -0.2084 293 HIS A ND1 
2137 C CD2 . HIS A 293 ? 0.6493 0.8066 0.5195 -0.0830 0.0663  -0.2033 293 HIS A CD2 
2138 C CE1 . HIS A 293 ? 0.6940 0.8640 0.5663 -0.0758 0.0554  -0.2050 293 HIS A CE1 
2139 N NE2 . HIS A 293 ? 0.6905 0.8485 0.5557 -0.0762 0.0594  -0.2018 293 HIS A NE2 
2140 N N   . ARG A 294 ? 0.6418 0.8227 0.5590 -0.1102 0.0790  -0.2113 294 ARG A N   
2141 C CA  . ARG A 294 ? 0.6851 0.8717 0.6109 -0.1185 0.0846  -0.2146 294 ARG A CA  
2142 C C   . ARG A 294 ? 0.7187 0.9165 0.6598 -0.1191 0.0803  -0.2140 294 ARG A C   
2143 O O   . ARG A 294 ? 0.7632 0.9722 0.7103 -0.1234 0.0825  -0.2186 294 ARG A O   
2144 C CB  . ARG A 294 ? 0.7323 0.9066 0.6576 -0.1235 0.0908  -0.2122 294 ARG A CB  
2145 C CG  . ARG A 294 ? 0.7869 0.9654 0.7217 -0.1324 0.0966  -0.2149 294 ARG A CG  
2146 C CD  . ARG A 294 ? 0.8660 1.0311 0.7944 -0.1372 0.1050  -0.2151 294 ARG A CD  
2147 N NE  . ARG A 294 ? 0.8800 1.0314 0.8044 -0.1336 0.1043  -0.2092 294 ARG A NE  
2148 C CZ  . ARG A 294 ? 0.8990 1.0450 0.8325 -0.1357 0.1039  -0.2043 294 ARG A CZ  
2149 N NH1 . ARG A 294 ? 0.9314 1.0846 0.8787 -0.1413 0.1043  -0.2042 294 ARG A NH1 
2150 N NH2 . ARG A 294 ? 0.8959 1.0295 0.8246 -0.1320 0.1033  -0.1993 294 ARG A NH2 
2151 N N   . PHE A 295 ? 0.6343 0.8283 0.5808 -0.1144 0.0746  -0.2082 295 PHE A N   
2152 C CA  . PHE A 295 ? 0.5814 0.7845 0.5406 -0.1130 0.0703  -0.2071 295 PHE A CA  
2153 C C   . PHE A 295 ? 0.5139 0.7275 0.4730 -0.1075 0.0649  -0.2100 295 PHE A C   
2154 O O   . PHE A 295 ? 0.4650 0.6903 0.4329 -0.1090 0.0648  -0.2129 295 PHE A O   
2155 C CB  . PHE A 295 ? 0.5744 0.7684 0.5374 -0.1082 0.0655  -0.2001 295 PHE A CB  
2156 C CG  . PHE A 295 ? 0.5635 0.7493 0.5304 -0.1138 0.0705  -0.1969 295 PHE A CG  
2157 C CD1 . PHE A 295 ? 0.6219 0.8126 0.5954 -0.1228 0.0779  -0.1999 295 PHE A CD1 
2158 C CD2 . PHE A 295 ? 0.5137 0.6867 0.4782 -0.1098 0.0675  -0.1907 295 PHE A CD2 
2159 C CE1 . PHE A 295 ? 0.6003 0.7829 0.5777 -0.1279 0.0825  -0.1968 295 PHE A CE1 
2160 C CE2 . PHE A 295 ? 0.4998 0.6654 0.4684 -0.1146 0.0722  -0.1876 295 PHE A CE2 
2161 C CZ  . PHE A 295 ? 0.5476 0.7181 0.5228 -0.1238 0.0798  -0.1907 295 PHE A CZ  
2162 N N   . ARG A 296 ? 0.5351 0.7441 0.4842 -0.1011 0.0606  -0.2092 296 ARG A N   
2163 C CA  . ARG A 296 ? 0.5347 0.7517 0.4830 -0.0951 0.0550  -0.2113 296 ARG A CA  
2164 C C   . ARG A 296 ? 0.6137 0.8441 0.5628 -0.0990 0.0586  -0.2183 296 ARG A C   
2165 O O   . ARG A 296 ? 0.5612 0.8020 0.5158 -0.0964 0.0552  -0.2205 296 ARG A O   
2166 C CB  . ARG A 296 ? 0.5327 0.7413 0.4689 -0.0883 0.0506  -0.2091 296 ARG A CB  
2167 C CG  . ARG A 296 ? 0.5168 0.7318 0.4519 -0.0814 0.0440  -0.2106 296 ARG A CG  
2168 C CD  . ARG A 296 ? 0.4893 0.7060 0.4342 -0.0768 0.0380  -0.2081 296 ARG A CD  
2169 N NE  . ARG A 296 ? 0.4869 0.7092 0.4306 -0.0704 0.0322  -0.2099 296 ARG A NE  
2170 C CZ  . ARG A 296 ? 0.4643 0.7008 0.4132 -0.0715 0.0331  -0.2151 296 ARG A CZ  
2171 N NH1 . ARG A 296 ? 0.4799 0.7267 0.4353 -0.0789 0.0394  -0.2193 296 ARG A NH1 
2172 N NH2 . ARG A 296 ? 0.4131 0.6530 0.3604 -0.0651 0.0277  -0.2163 296 ARG A NH2 
2173 N N   . ASN A 297 ? 0.7183 0.9473 0.6610 -0.1050 0.0655  -0.2216 297 ASN A N   
2174 C CA  . ASN A 297 ? 0.8055 1.0452 0.7464 -0.1089 0.0694  -0.2285 297 ASN A CA  
2175 C C   . ASN A 297 ? 0.7607 1.0076 0.7117 -0.1171 0.0746  -0.2314 297 ASN A C   
2176 O O   . ASN A 297 ? 0.8761 1.1274 0.8239 -0.1222 0.0798  -0.2367 297 ASN A O   
2177 C CB  . ASN A 297 ? 0.8212 1.0538 0.7469 -0.1095 0.0739  -0.2307 297 ASN A CB  
2178 C CG  . ASN A 297 ? 0.8561 1.0821 0.7713 -0.1015 0.0690  -0.2279 297 ASN A CG  
2179 O OD1 . ASN A 297 ? 0.8887 1.1182 0.8071 -0.0955 0.0621  -0.2261 297 ASN A OD1 
2180 N ND2 . ASN A 297 ? 0.9350 1.1506 0.8370 -0.1011 0.0730  -0.2275 297 ASN A ND2 
2181 N N   . ASP A 298 ? 0.6956 0.9434 0.6583 -0.1180 0.0731  -0.2280 298 ASP A N   
2182 C CA  . ASP A 298 ? 0.6568 0.9120 0.6304 -0.1253 0.0774  -0.2301 298 ASP A CA  
2183 C C   . ASP A 298 ? 0.6665 0.9310 0.6520 -0.1214 0.0723  -0.2287 298 ASP A C   
2184 O O   . ASP A 298 ? 0.6069 0.8666 0.5985 -0.1193 0.0701  -0.2236 298 ASP A O   
2185 C CB  . ASP A 298 ? 0.6424 0.8870 0.6174 -0.1307 0.0821  -0.2269 298 ASP A CB  
2186 C CG  . ASP A 298 ? 0.6439 0.8951 0.6294 -0.1390 0.0873  -0.2291 298 ASP A CG  
2187 O OD1 . ASP A 298 ? 0.6560 0.9204 0.6484 -0.1403 0.0868  -0.2328 298 ASP A OD1 
2188 O OD2 . ASP A 298 ? 0.5942 0.8372 0.5813 -0.1443 0.0917  -0.2269 298 ASP A OD2 
2189 N N   . GLU A 299 ? 0.6313 0.6043 0.7382 -0.0367 -0.0183 -0.1034 299 GLU A N   
2190 C CA  . GLU A 299 ? 0.6821 0.6505 0.7846 -0.0379 -0.0178 -0.1003 299 GLU A CA  
2191 C C   . GLU A 299 ? 0.6864 0.6460 0.7865 -0.0372 -0.0190 -0.0993 299 GLU A C   
2192 O O   . GLU A 299 ? 0.7089 0.6679 0.8037 -0.0368 -0.0196 -0.0985 299 GLU A O   
2193 C CB  . GLU A 299 ? 0.6957 0.6608 0.8004 -0.0402 -0.0157 -0.0973 299 GLU A CB  
2194 C CG  . GLU A 299 ? 0.7425 0.6990 0.8449 -0.0415 -0.0152 -0.0937 299 GLU A CG  
2195 C CD  . GLU A 299 ? 0.7572 0.7103 0.8622 -0.0436 -0.0131 -0.0910 299 GLU A CD  
2196 O OE1 . GLU A 299 ? 0.8451 0.7898 0.9505 -0.0444 -0.0125 -0.0882 299 GLU A OE1 
2197 N N   . ALA A 300 ? 0.6533 0.6059 0.7574 -0.0369 -0.0190 -0.0994 300 ALA A N   
2198 C CA  . ALA A 300 ? 0.6324 0.5749 0.7348 -0.0360 -0.0194 -0.0981 300 ALA A CA  
2199 C C   . ALA A 300 ? 0.5985 0.5426 0.6962 -0.0335 -0.0215 -0.1006 300 ALA A C   
2200 O O   . ALA A 300 ? 0.6476 0.5859 0.7406 -0.0328 -0.0217 -0.0992 300 ALA A O   
2201 C CB  . ALA A 300 ? 0.6544 0.5893 0.7623 -0.0360 -0.0186 -0.0978 300 ALA A CB  
2202 N N   . PHE A 301 ? 0.5327 0.4846 0.6314 -0.0320 -0.0228 -0.1042 301 PHE A N   
2203 C CA  . PHE A 301 ? 0.5321 0.4882 0.6260 -0.0294 -0.0248 -0.1068 301 PHE A CA  
2204 C C   . PHE A 301 ? 0.5142 0.4754 0.6019 -0.0298 -0.0250 -0.1058 301 PHE A C   
2205 O O   . PHE A 301 ? 0.5532 0.5108 0.6355 -0.0286 -0.0257 -0.1056 301 PHE A O   
2206 C CB  . PHE A 301 ? 0.5540 0.5192 0.6506 -0.0279 -0.0260 -0.1105 301 PHE A CB  
2207 C CG  . PHE A 301 ? 0.5357 0.5074 0.6272 -0.0253 -0.0279 -0.1131 301 PHE A CG  
2208 C CD1 . PHE A 301 ? 0.5302 0.4964 0.6184 -0.0228 -0.0293 -0.1144 301 PHE A CD1 
2209 C CD2 . PHE A 301 ? 0.5454 0.5287 0.6354 -0.0249 -0.0281 -0.1143 301 PHE A CD2 
2210 C CE1 . PHE A 301 ? 0.5170 0.4900 0.6002 -0.0201 -0.0311 -0.1169 301 PHE A CE1 
2211 C CE2 . PHE A 301 ? 0.5381 0.5282 0.6237 -0.0223 -0.0297 -0.1165 301 PHE A CE2 
2212 C CZ  . PHE A 301 ? 0.5588 0.5441 0.6408 -0.0200 -0.0313 -0.1179 301 PHE A CZ  
2213 N N   . LEU A 302 ? 0.5026 0.4713 0.5909 -0.0313 -0.0240 -0.1051 302 LEU A N   
2214 C CA  . LEU A 302 ? 0.4624 0.4362 0.5456 -0.0318 -0.0237 -0.1040 302 LEU A CA  
2215 C C   . LEU A 302 ? 0.5166 0.4820 0.5964 -0.0331 -0.0232 -0.1008 302 LEU A C   
2216 O O   . LEU A 302 ? 0.4017 0.3680 0.4758 -0.0323 -0.0240 -0.1007 302 LEU A O   
2217 C CB  . LEU A 302 ? 0.4571 0.4385 0.5424 -0.0331 -0.0220 -0.1035 302 LEU A CB  
2218 C CG  . LEU A 302 ? 0.4261 0.4171 0.5140 -0.0317 -0.0221 -0.1065 302 LEU A CG  
2219 C CD1 . LEU A 302 ? 0.4144 0.4120 0.5031 -0.0328 -0.0200 -0.1057 302 LEU A CD1 
2220 C CD2 . LEU A 302 ? 0.4392 0.4363 0.5233 -0.0290 -0.0239 -0.1090 302 LEU A CD2 
2221 N N   . GLN A 303 ? 0.5258 0.4830 0.6091 -0.0349 -0.0218 -0.0981 303 GLN A N   
2222 C CA  . GLN A 303 ? 0.4971 0.4451 0.5781 -0.0361 -0.0209 -0.0947 303 GLN A CA  
2223 C C   . GLN A 303 ? 0.5117 0.4516 0.5894 -0.0340 -0.0218 -0.0950 303 GLN A C   
2224 O O   . GLN A 303 ? 0.4795 0.4154 0.5525 -0.0340 -0.0216 -0.0932 303 GLN A O   
2225 C CB  . GLN A 303 ? 0.5288 0.4702 0.6149 -0.0381 -0.0190 -0.0918 303 GLN A CB  
2226 N N   . GLN A 304 ? 0.5034 0.4408 0.5833 -0.0319 -0.0226 -0.0974 304 GLN A N   
2227 C CA  . GLN A 304 ? 0.5673 0.4979 0.6471 -0.0286 -0.0232 -0.0994 304 GLN A CA  
2228 C C   . GLN A 304 ? 0.5357 0.4755 0.6143 -0.0259 -0.0252 -0.1043 304 GLN A C   
2229 O O   . GLN A 304 ? 0.5115 0.4497 0.5963 -0.0228 -0.0256 -0.1078 304 GLN A O   
2230 C CB  . GLN A 304 ? 0.5774 0.5047 0.6637 -0.0263 -0.0235 -0.1022 304 GLN A CB  
2231 C CG  . GLN A 304 ? 0.6307 0.5522 0.7289 -0.0209 -0.0239 -0.1070 304 GLN A CG  
2232 C CD  . GLN A 304 ? 0.7273 0.6379 0.8322 -0.0202 -0.0218 -0.1039 304 GLN A CD  
2233 O OE1 . GLN A 304 ? 0.7236 0.6289 0.8263 -0.0238 -0.0197 -0.0984 304 GLN A OE1 
2234 N NE2 . GLN A 304 ? 0.8175 0.7244 0.9297 -0.0150 -0.0222 -0.1070 304 GLN A NE2 
2235 N N   . VAL A 305 ? 0.5554 0.5043 0.6256 -0.0267 -0.0263 -0.1039 305 VAL A N   
2236 C CA  . VAL A 305 ? 0.5124 0.4714 0.5788 -0.0245 -0.0279 -0.1073 305 VAL A CA  
2237 C C   . VAL A 305 ? 0.4948 0.4548 0.5581 -0.0260 -0.0273 -0.1054 305 VAL A C   
2238 O O   . VAL A 305 ? 0.4457 0.4096 0.5118 -0.0230 -0.0283 -0.1101 305 VAL A O   
2239 C CB  . VAL A 305 ? 0.4944 0.4655 0.5589 -0.0246 -0.0287 -0.1081 305 VAL A CB  
2240 C CG1 . VAL A 305 ? 0.4211 0.4018 0.4791 -0.0226 -0.0299 -0.1097 305 VAL A CG1 
2241 C CG2 . VAL A 305 ? 0.5019 0.4733 0.5709 -0.0228 -0.0296 -0.1109 305 VAL A CG2 
2242 N N   . MET A 306 ? 0.5238 0.4821 0.5848 -0.0297 -0.0257 -0.1003 306 MET A N   
2243 C CA  . MET A 306 ? 0.4821 0.4409 0.5395 -0.0316 -0.0249 -0.0977 306 MET A CA  
2244 C C   . MET A 306 ? 0.5041 0.4551 0.5675 -0.0306 -0.0243 -0.0991 306 MET A C   
2245 O O   . MET A 306 ? 0.5360 0.4908 0.5994 -0.0298 -0.0246 -0.1011 306 MET A O   
2246 C CB  . MET A 306 ? 0.5114 0.4731 0.5729 -0.0344 -0.0233 -0.0954 306 MET A CB  
2247 C CG  . MET A 306 ? 0.4942 0.4684 0.5569 -0.0340 -0.0231 -0.0972 306 MET A CG  
2248 S SD  . MET A 306 ? 0.5008 0.4780 0.5663 -0.0367 -0.0207 -0.0946 306 MET A SD  
2249 C CE  . MET A 306 ? 0.5705 0.5385 0.6425 -0.0381 -0.0199 -0.0933 306 MET A CE  
2250 N N   . LYS A 307 ? 0.4542 0.3955 0.5257 -0.0301 -0.0233 -0.0988 307 LYS A N   
2251 C CA  . LYS A 307 ? 0.5259 0.4583 0.6075 -0.0281 -0.0222 -0.1000 307 LYS A CA  
2252 C C   . LYS A 307 ? 0.5295 0.4641 0.6179 -0.0224 -0.0240 -0.1072 307 LYS A C   
2253 O O   . LYS A 307 ? 0.5247 0.4574 0.6167 -0.0206 -0.0238 -0.1086 307 LYS A O   
2254 C CB  . LYS A 307 ? 0.5550 0.4758 0.6428 -0.0283 -0.0205 -0.0968 307 LYS A CB  
2255 C CG  . LYS A 307 ? 0.6153 0.5248 0.7153 -0.0243 -0.0191 -0.0971 307 LYS A CG  
2256 C CD  . LYS A 307 ? 0.6878 0.5863 0.7905 -0.0260 -0.0164 -0.0907 307 LYS A CD  
2257 C CE  . LYS A 307 ? 0.7476 0.6338 0.8620 -0.0211 -0.0146 -0.0889 307 LYS A CE  
2258 N NZ  . LYS A 307 ? 0.8006 0.6827 0.9223 -0.0159 -0.0150 -0.0918 307 LYS A NZ  
2259 N N   . ASP A 308 ? 0.6095 0.5475 0.6992 -0.0191 -0.0258 -0.1117 308 ASP A N   
2260 C CA  . ASP A 308 ? 0.6161 0.5565 0.7106 -0.0122 -0.0280 -0.1190 308 ASP A CA  
2261 C C   . ASP A 308 ? 0.5253 0.4786 0.6121 -0.0114 -0.0297 -0.1226 308 ASP A C   
2262 O O   . ASP A 308 ? 0.5909 0.5439 0.6805 -0.0063 -0.0305 -0.1270 308 ASP A O   
2263 C CB  . ASP A 308 ? 0.6939 0.6368 0.7895 -0.0092 -0.0297 -0.1225 308 ASP A CB  
2264 C CG  . ASP A 308 ? 0.8106 0.7401 0.9154 -0.0079 -0.0280 -0.1201 308 ASP A CG  
2265 O OD1 . ASP A 308 ? 0.9224 0.8531 1.0287 -0.0058 -0.0291 -0.1226 308 ASP A OD1 
2266 O OD2 . ASP A 308 ? 0.8265 0.7449 0.9367 -0.0092 -0.0254 -0.1151 308 ASP A OD2 
2267 N N   . GLY A 309 ? 0.5136 0.4775 0.5899 -0.0156 -0.0299 -0.1199 309 GLY A N   
2268 C CA  . GLY A 309 ? 0.4495 0.4261 0.5168 -0.0156 -0.0308 -0.1210 309 GLY A CA  
2269 C C   . GLY A 309 ? 0.4322 0.4077 0.4999 -0.0167 -0.0298 -0.1205 309 GLY A C   
2270 O O   . GLY A 309 ? 0.3951 0.3782 0.4609 -0.0130 -0.0311 -0.1253 309 GLY A O   
2271 N N   . ALA A 310 ? 0.4445 0.4112 0.5139 -0.0214 -0.0275 -0.1145 310 ALA A N   
2272 C CA  . ALA A 310 ? 0.4371 0.4026 0.5063 -0.0237 -0.0261 -0.1125 310 ALA A CA  
2273 C C   . ALA A 310 ? 0.4781 0.4358 0.5579 -0.0191 -0.0261 -0.1170 310 ALA A C   
2274 O O   . ALA A 310 ? 0.4688 0.4324 0.5443 -0.0174 -0.0247 -0.1130 310 ALA A O   
2275 C CB  . ALA A 310 ? 0.4292 0.3874 0.4961 -0.0292 -0.0238 -0.1044 310 ALA A CB  
2276 N N   . GLU A 311 ? 0.5219 0.4692 0.6096 -0.0150 -0.0252 -0.1147 311 GLU A N   
2277 C CA  . GLU A 311 ? 0.5561 0.5010 0.6456 -0.0067 -0.0219 -0.1043 311 GLU A CA  
2278 C C   . GLU A 311 ? 0.5447 0.5044 0.6262 0.0008  -0.0223 -0.1027 311 GLU A C   
2279 O O   . GLU A 311 ? 0.5964 0.5602 0.6751 0.0054  -0.0198 -0.0947 311 GLU A O   
2280 C CB  . GLU A 311 ? 0.6439 0.5755 0.7425 -0.0037 -0.0209 -0.1021 311 GLU A CB  
2281 C CG  . GLU A 311 ? 0.7190 0.6477 0.8202 0.0053  -0.0176 -0.0915 311 GLU A CG  
2282 C CD  . GLU A 311 ? 0.8324 0.7514 0.9412 0.0094  -0.0172 -0.0910 311 GLU A CD  
2283 O OE1 . GLU A 311 ? 0.9074 0.8276 1.0170 0.0179  -0.0154 -0.0842 311 GLU A OE1 
2284 O OE2 . GLU A 311 ? 0.8421 0.7525 0.9564 0.0041  -0.0185 -0.0971 311 GLU A OE2 
2285 N N   . LYS A 312 ? 0.5594 0.5272 0.6375 0.0021  -0.0254 -0.1102 312 LYS A N   
2286 C CA  . LYS A 312 ? 0.5476 0.5307 0.6175 0.0089  -0.0261 -0.1099 312 LYS A CA  
2287 C C   . LYS A 312 ? 0.4962 0.4917 0.5569 0.0065  -0.0261 -0.1101 312 LYS A C   
2288 O O   . LYS A 312 ? 0.4832 0.4874 0.5390 0.0122  -0.0243 -0.1038 312 LYS A O   
2289 C CB  . LYS A 312 ? 0.5490 0.5377 0.6169 0.0097  -0.0296 -0.1188 312 LYS A CB  
2290 C CG  . LYS A 312 ? 0.6158 0.5955 0.6915 0.0147  -0.0292 -0.1172 312 LYS A CG  
2291 C CD  . LYS A 312 ? 0.6385 0.6261 0.7112 0.0176  -0.0323 -0.1245 312 LYS A CD  
2292 C CE  . LYS A 312 ? 0.6606 0.6445 0.7357 0.0099  -0.0358 -0.1355 312 LYS A CE  
2293 N NZ  . LYS A 312 ? 0.6679 0.6591 0.7403 0.0130  -0.0389 -0.1424 312 LYS A NZ  
2294 N N   . ALA A 313 ? 0.4534 0.4495 0.5123 -0.0021 -0.0281 -0.1173 313 ALA A N   
2295 C CA  . ALA A 313 ? 0.4352 0.4418 0.4861 -0.0056 -0.0281 -0.1183 313 ALA A CA  
2296 C C   . ALA A 313 ? 0.4360 0.4395 0.4877 -0.0046 -0.0243 -0.1082 313 ALA A C   
2297 O O   . ALA A 313 ? 0.3977 0.4124 0.4425 -0.0014 -0.0230 -0.1044 313 ALA A O   
2298 C CB  . ALA A 313 ? 0.3964 0.4022 0.4460 -0.0149 -0.0302 -0.1251 313 ALA A CB  
2299 N N   . SER A 314 ? 0.4484 0.4371 0.5085 -0.0072 -0.0224 -0.1040 314 SER A N   
2300 C CA  . SER A 314 ? 0.4923 0.4765 0.5540 -0.0069 -0.0189 -0.0948 314 SER A CA  
2301 C C   . SER A 314 ? 0.5339 0.5220 0.5945 0.0025  -0.0163 -0.0852 314 SER A C   
2302 O O   . SER A 314 ? 0.4728 0.4652 0.5304 0.0036  -0.0140 -0.0789 314 SER A O   
2303 C CB  . SER A 314 ? 0.5567 0.5236 0.6278 -0.0114 -0.0175 -0.0925 314 SER A CB  
2304 O OG  . SER A 314 ? 0.6821 0.6463 0.7534 -0.0207 -0.0189 -0.0985 314 SER A OG  
2305 N N   . ALA A 315 ? 0.5479 0.5344 0.6114 0.0090  -0.0165 -0.0841 315 ALA A N   
2306 C CA  . ALA A 315 ? 0.5891 0.5798 0.6519 0.0181  -0.0142 -0.0752 315 ALA A CA  
2307 C C   . ALA A 315 ? 0.5751 0.5835 0.6278 0.0211  -0.0143 -0.0747 315 ALA A C   
2308 O O   . ALA A 315 ? 0.6156 0.6284 0.6665 0.0256  -0.0117 -0.0664 315 ALA A O   
2309 C CB  . ALA A 315 ? 0.5952 0.5824 0.6622 0.0240  -0.0150 -0.0759 315 ALA A CB  
2310 N N   . HIS A 316 ? 0.5415 0.5602 0.5877 0.0185  -0.0173 -0.0837 316 HIS A N   
2311 C CA  . HIS A 316 ? 0.5276 0.5635 0.5636 0.0207  -0.0176 -0.0845 316 HIS A CA  
2312 C C   . HIS A 316 ? 0.4666 0.5070 0.4979 0.0142  -0.0170 -0.0853 316 HIS A C   
2313 O O   . HIS A 316 ? 0.4426 0.4928 0.4684 0.0167  -0.0151 -0.0803 316 HIS A O   
2314 C CB  . HIS A 316 ? 0.5665 0.6114 0.5975 0.0211  -0.0212 -0.0940 316 HIS A CB  
2315 C CG  . HIS A 316 ? 0.6278 0.6905 0.6485 0.0248  -0.0215 -0.0943 316 HIS A CG  
2316 N ND1 . HIS A 316 ? 0.6482 0.7214 0.6620 0.0240  -0.0247 -0.1033 316 HIS A ND1 
2317 C CD2 . HIS A 316 ? 0.6550 0.7272 0.6708 0.0291  -0.0189 -0.0870 316 HIS A CD2 
2318 C CE1 . HIS A 316 ? 0.6029 0.6912 0.6080 0.0277  -0.0240 -0.1013 316 HIS A CE1 
2319 N NE2 . HIS A 316 ? 0.6257 0.7139 0.6319 0.0308  -0.0205 -0.0915 316 HIS A NE2 
2320 N N   . ALA A 317 ? 0.4114 0.4445 0.4452 0.0059  -0.0184 -0.0912 317 ALA A N   
2321 C CA  . ALA A 317 ? 0.3861 0.4218 0.4166 -0.0008 -0.0177 -0.0920 317 ALA A CA  
2322 C C   . ALA A 317 ? 0.3872 0.4182 0.4203 0.0007  -0.0139 -0.0816 317 ALA A C   
2323 O O   . ALA A 317 ? 0.2934 0.3330 0.3209 -0.0006 -0.0126 -0.0795 317 ALA A O   
2324 C CB  . ALA A 317 ? 0.3782 0.4050 0.4126 -0.0097 -0.0197 -0.0995 317 ALA A CB  
2325 N N   . SER A 318 ? 0.3708 0.3888 0.4123 0.0037  -0.0122 -0.0752 318 SER A N   
2326 C CA  . SER A 318 ? 0.3961 0.4078 0.4412 0.0048  -0.0088 -0.0653 318 SER A CA  
2327 C C   . SER A 318 ? 0.4002 0.4235 0.4402 0.0118  -0.0067 -0.0580 318 SER A C   
2328 O O   . SER A 318 ? 0.4279 0.4523 0.4670 0.0111  -0.0042 -0.0518 318 SER A O   
2329 C CB  . SER A 318 ? 0.4071 0.4022 0.4623 0.0067  -0.0075 -0.0604 318 SER A CB  
2330 O OG  . SER A 318 ? 0.4875 0.4835 0.5443 0.0146  -0.0075 -0.0577 318 SER A OG  
2331 N N   . ARG A 319 ? 0.4708 0.5028 0.5076 0.0184  -0.0075 -0.0584 319 ARG A N   
2332 C CA  . ARG A 319 ? 0.4930 0.5368 0.5251 0.0254  -0.0054 -0.0510 319 ARG A CA  
2333 C C   . ARG A 319 ? 0.4155 0.4745 0.4379 0.0225  -0.0055 -0.0539 319 ARG A C   
2334 O O   . ARG A 319 ? 0.4175 0.4836 0.4369 0.0250  -0.0031 -0.0472 319 ARG A O   
2335 C CB  . ARG A 319 ? 0.5552 0.6043 0.5866 0.0334  -0.0062 -0.0505 319 ARG A CB  
2336 C CG  . ARG A 319 ? 0.6790 0.7141 0.7197 0.0371  -0.0059 -0.0474 319 ARG A CG  
2337 C CD  . ARG A 319 ? 0.7402 0.7817 0.7802 0.0457  -0.0063 -0.0457 319 ARG A CD  
2338 N NE  . ARG A 319 ? 0.8113 0.8692 0.8418 0.0466  -0.0082 -0.0517 319 ARG A NE  
2339 C CZ  . ARG A 319 ? 0.8415 0.9029 0.8699 0.0472  -0.0111 -0.0597 319 ARG A CZ  
2340 N NH1 . ARG A 319 ? 0.8442 0.9212 0.8632 0.0478  -0.0127 -0.0645 319 ARG A NH1 
2341 N NH2 . ARG A 319 ? 0.8340 0.8839 0.8694 0.0473  -0.0125 -0.0628 319 ARG A NH2 
2342 N N   . THR A 320 ? 0.3996 0.4637 0.4173 0.0174  -0.0083 -0.0638 320 THR A N   
2343 C CA  . THR A 320 ? 0.3810 0.4586 0.3896 0.0137  -0.0084 -0.0675 320 THR A CA  
2344 C C   . THR A 320 ? 0.3756 0.4482 0.3857 0.0075  -0.0065 -0.0647 320 THR A C   
2345 O O   . THR A 320 ? 0.4019 0.4836 0.4072 0.0079  -0.0044 -0.0605 320 THR A O   
2346 C CB  . THR A 320 ? 0.3611 0.4450 0.3645 0.0096  -0.0121 -0.0791 320 THR A CB  
2347 O OG1 . THR A 320 ? 0.3495 0.4386 0.3512 0.0159  -0.0137 -0.0811 320 THR A OG1 
2348 C CG2 . THR A 320 ? 0.3237 0.4224 0.3171 0.0059  -0.0121 -0.0830 320 THR A CG2 
2349 N N   . LEU A 321 ? 0.3530 0.4114 0.3699 0.0018  -0.0071 -0.0669 321 LEU A N   
2350 C CA  . LEU A 321 ? 0.3222 0.3750 0.3410 -0.0045 -0.0054 -0.0647 321 LEU A CA  
2351 C C   . LEU A 321 ? 0.3225 0.3731 0.3437 -0.0007 -0.0019 -0.0536 321 LEU A C   
2352 O O   . LEU A 321 ? 0.3325 0.3869 0.3509 -0.0037 -0.0001 -0.0510 321 LEU A O   
2353 C CB  . LEU A 321 ? 0.2881 0.3253 0.3144 -0.0108 -0.0066 -0.0684 321 LEU A CB  
2354 C CG  . LEU A 321 ? 0.2673 0.2997 0.2946 -0.0185 -0.0054 -0.0682 321 LEU A CG  
2355 C CD1 . LEU A 321 ? 0.2673 0.3114 0.2868 -0.0239 -0.0069 -0.0759 321 LEU A CD1 
2356 C CD2 . LEU A 321 ? 0.2609 0.2767 0.2966 -0.0238 -0.0060 -0.0698 321 LEU A CD2 
2357 N N   . LYS A 322 ? 0.3745 0.4189 0.4010 0.0060  -0.0009 -0.0470 322 LYS A N   
2358 C CA  . LYS A 322 ? 0.4500 0.4925 0.4791 0.0105  0.0024  -0.0360 322 LYS A CA  
2359 C C   . LYS A 322 ? 0.4180 0.4770 0.4394 0.0142  0.0039  -0.0323 322 LYS A C   
2360 O O   . LYS A 322 ? 0.4507 0.5110 0.4720 0.0140  0.0065  -0.0254 322 LYS A O   
2361 C CB  . LYS A 322 ? 0.5097 0.5431 0.5458 0.0173  0.0029  -0.0306 322 LYS A CB  
2362 C CG  . LYS A 322 ? 0.5847 0.6122 0.6253 0.0211  0.0060  -0.0194 322 LYS A CG  
2363 C CD  . LYS A 322 ? 0.6850 0.7000 0.7338 0.0261  0.0063  -0.0152 322 LYS A CD  
2364 C CE  . LYS A 322 ? 0.7061 0.7178 0.7587 0.0315  0.0092  -0.0035 322 LYS A CE  
2365 N NZ  . LYS A 322 ? 0.7285 0.7298 0.7849 0.0265  0.0109  0.0005  322 LYS A NZ  
2366 N N   . ALA A 323 ? 0.4125 0.4842 0.4276 0.0176  0.0024  -0.0365 323 ALA A N   
2367 C CA  . ALA A 323 ? 0.4208 0.5097 0.4277 0.0206  0.0038  -0.0340 323 ALA A CA  
2368 C C   . ALA A 323 ? 0.3945 0.4906 0.3952 0.0132  0.0040  -0.0385 323 ALA A C   
2369 O O   . ALA A 323 ? 0.4284 0.5326 0.4255 0.0132  0.0064  -0.0337 323 ALA A O   
2370 C CB  . ALA A 323 ? 0.4217 0.5217 0.4235 0.0259  0.0021  -0.0377 323 ALA A CB  
2371 N N   . VAL A 324 ? 0.3451 0.4377 0.3452 0.0067  0.0016  -0.0476 324 VAL A N   
2372 C CA  . VAL A 324 ? 0.3423 0.4402 0.3374 -0.0008 0.0017  -0.0522 324 VAL A CA  
2373 C C   . VAL A 324 ? 0.3826 0.4726 0.3821 -0.0041 0.0044  -0.0456 324 VAL A C   
2374 O O   . VAL A 324 ? 0.3910 0.4894 0.3859 -0.0063 0.0063  -0.0438 324 VAL A O   
2375 C CB  . VAL A 324 ? 0.3493 0.4435 0.3441 -0.0073 -0.0016 -0.0632 324 VAL A CB  
2376 C CG1 . VAL A 324 ? 0.3216 0.4175 0.3137 -0.0157 -0.0013 -0.0672 324 VAL A CG1 
2377 C CG2 . VAL A 324 ? 0.3477 0.4532 0.3359 -0.0047 -0.0042 -0.0702 324 VAL A CG2 
2378 N N   . TYR A 325 ? 0.3667 0.4407 0.3751 -0.0043 0.0047  -0.0420 325 TYR A N   
2379 C CA  . TYR A 325 ? 0.3904 0.4549 0.4037 -0.0077 0.0070  -0.0360 325 TYR A CA  
2380 C C   . TYR A 325 ? 0.3937 0.4638 0.4062 -0.0024 0.0102  -0.0257 325 TYR A C   
2381 O O   . TYR A 325 ? 0.3689 0.4405 0.3804 -0.0057 0.0122  -0.0224 325 TYR A O   
2382 C CB  . TYR A 325 ? 0.3880 0.4339 0.4107 -0.0091 0.0064  -0.0352 325 TYR A CB  
2383 C CG  . TYR A 325 ? 0.4035 0.4418 0.4280 -0.0175 0.0043  -0.0436 325 TYR A CG  
2384 C CD1 . TYR A 325 ? 0.3586 0.4065 0.3768 -0.0221 0.0023  -0.0528 325 TYR A CD1 
2385 C CD2 . TYR A 325 ? 0.4125 0.4342 0.4452 -0.0210 0.0045  -0.0422 325 TYR A CD2 
2386 C CE1 . TYR A 325 ? 0.3557 0.3972 0.3757 -0.0299 0.0005  -0.0601 325 TYR A CE1 
2387 C CE2 . TYR A 325 ? 0.3932 0.4082 0.4278 -0.0289 0.0027  -0.0497 325 TYR A CE2 
2388 C CZ  . TYR A 325 ? 0.3777 0.4027 0.4061 -0.0333 0.0007  -0.0585 325 TYR A CZ  
2389 O OH  . TYR A 325 ? 0.3658 0.3848 0.3961 -0.0412 -0.0012 -0.0660 325 TYR A OH  
2390 N N   . GLU A 326 ? 0.4189 0.4926 0.4318 0.0056  0.0105  -0.0210 326 GLU A N   
2391 C CA  . GLU A 326 ? 0.4579 0.5386 0.4697 0.0111  0.0133  -0.0114 326 GLU A CA  
2392 C C   . GLU A 326 ? 0.4428 0.5410 0.4456 0.0101  0.0144  -0.0124 326 GLU A C   
2393 O O   . GLU A 326 ? 0.4549 0.5567 0.4571 0.0097  0.0170  -0.0062 326 GLU A O   
2394 C CB  . GLU A 326 ? 0.5629 0.6443 0.5770 0.0198  0.0132  -0.0071 326 GLU A CB  
2395 C CG  . GLU A 326 ? 0.6567 0.7466 0.6698 0.0262  0.0159  0.0028  326 GLU A CG  
2396 C CD  . GLU A 326 ? 0.7457 0.8245 0.7658 0.0266  0.0181  0.0119  326 GLU A CD  
2397 O OE1 . GLU A 326 ? 0.7735 0.8597 0.7919 0.0289  0.0205  0.0193  326 GLU A OE1 
2398 O OE2 . GLU A 326 ? 0.7555 0.8182 0.7825 0.0245  0.0175  0.0117  326 GLU A OE2 
2399 N N   . ALA A 327 ? 0.4086 0.5176 0.4046 0.0095  0.0125  -0.0204 327 ALA A N   
2400 C CA  . ALA A 327 ? 0.4363 0.5624 0.4231 0.0080  0.0133  -0.0228 327 ALA A CA  
2401 C C   . ALA A 327 ? 0.3903 0.5157 0.3758 0.0003  0.0145  -0.0243 327 ALA A C   
2402 O O   . ALA A 327 ? 0.3855 0.5196 0.3675 0.0001  0.0170  -0.0200 327 ALA A O   
2403 C CB  . ALA A 327 ? 0.4157 0.5509 0.3960 0.0079  0.0106  -0.0322 327 ALA A CB  
2404 N N   . ILE A 328 ? 0.4206 0.5352 0.4093 -0.0060 0.0127  -0.0304 328 ILE A N   
2405 C CA  . ILE A 328 ? 0.4146 0.5270 0.4029 -0.0138 0.0137  -0.0323 328 ILE A CA  
2406 C C   . ILE A 328 ? 0.4050 0.5103 0.3984 -0.0138 0.0167  -0.0227 328 ILE A C   
2407 O O   . ILE A 328 ? 0.3523 0.4615 0.3435 -0.0181 0.0185  -0.0215 328 ILE A O   
2408 C CB  . ILE A 328 ? 0.4169 0.5178 0.4087 -0.0204 0.0111  -0.0402 328 ILE A CB  
2409 C CG1 . ILE A 328 ? 0.3825 0.4912 0.3687 -0.0215 0.0081  -0.0503 328 ILE A CG1 
2410 C CG2 . ILE A 328 ? 0.4301 0.5272 0.4226 -0.0283 0.0123  -0.0413 328 ILE A CG2 
2411 C CD1 . ILE A 328 ? 0.3591 0.4556 0.3500 -0.0264 0.0052  -0.0576 328 ILE A CD1 
2412 N N   . GLY A 329 ? 0.4081 0.5031 0.4084 -0.0089 0.0170  -0.0162 329 GLY A N   
2413 C CA  . GLY A 329 ? 0.4268 0.5153 0.4321 -0.0076 0.0197  -0.0064 329 GLY A CA  
2414 C C   . GLY A 329 ? 0.4151 0.4853 0.4284 -0.0118 0.0196  -0.0053 329 GLY A C   
2415 O O   . GLY A 329 ? 0.4295 0.4947 0.4460 -0.0128 0.0217  0.0014  329 GLY A O   
2416 N N   . PHE A 330 ? 0.3555 0.4161 0.3720 -0.0146 0.0171  -0.0118 330 PHE A N   
2417 C CA  . PHE A 330 ? 0.3274 0.3706 0.3515 -0.0185 0.0169  -0.0110 330 PHE A CA  
2418 C C   . PHE A 330 ? 0.3760 0.4096 0.4066 -0.0124 0.0181  -0.0022 330 PHE A C   
2419 O O   . PHE A 330 ? 0.3641 0.4017 0.3946 -0.0054 0.0177  0.0002  330 PHE A O   
2420 C CB  . PHE A 330 ? 0.3573 0.3934 0.3834 -0.0221 0.0139  -0.0201 330 PHE A CB  
2421 C CG  . PHE A 330 ? 0.3393 0.3806 0.3608 -0.0295 0.0124  -0.0292 330 PHE A CG  
2422 C CD1 . PHE A 330 ? 0.3572 0.4033 0.3756 -0.0345 0.0140  -0.0289 330 PHE A CD1 
2423 C CD2 . PHE A 330 ? 0.3628 0.4029 0.3840 -0.0318 0.0094  -0.0383 330 PHE A CD2 
2424 C CE1 . PHE A 330 ? 0.3490 0.3995 0.3636 -0.0413 0.0127  -0.0373 330 PHE A CE1 
2425 C CE2 . PHE A 330 ? 0.3503 0.3946 0.3678 -0.0388 0.0079  -0.0467 330 PHE A CE2 
2426 C CZ  . PHE A 330 ? 0.3136 0.3630 0.3278 -0.0435 0.0096  -0.0462 330 PHE A CZ  
2427 N N   . VAL A 331 ? 0.3666 0.3876 0.4030 -0.0150 0.0195  0.0029  331 VAL A N   
2428 C CA  . VAL A 331 ? 0.3673 0.3769 0.4107 -0.0099 0.0204  0.0107  331 VAL A CA  
2429 C C   . VAL A 331 ? 0.3809 0.3815 0.4284 -0.0084 0.0181  0.0062  331 VAL A C   
2430 O O   . VAL A 331 ? 0.3816 0.3762 0.4303 -0.0141 0.0164  -0.0011 331 VAL A O   
2431 C CB  . VAL A 331 ? 0.3723 0.3694 0.4208 -0.0140 0.0221  0.0161  331 VAL A CB  
2432 C CG1 . VAL A 331 ? 0.3788 0.3627 0.4346 -0.0092 0.0228  0.0234  331 VAL A CG1 
2433 C CG2 . VAL A 331 ? 0.3742 0.3803 0.4189 -0.0148 0.0245  0.0214  331 VAL A CG2 
2434 N N   . ALA A 332 ? 0.4284 0.4281 0.4784 -0.0009 0.0182  0.0105  332 ALA A N   
2435 C CA  . ALA A 332 ? 0.4421 0.4344 0.4959 0.0010  0.0162  0.0064  332 ALA A CA  
2436 C C   . ALA A 332 ? 0.4395 0.4131 0.5012 -0.0026 0.0163  0.0072  332 ALA A C   
2437 O O   . ALA A 332 ? 0.4423 0.4079 0.5076 -0.0032 0.0183  0.0141  332 ALA A O   
2438 C CB  . ALA A 332 ? 0.5000 0.4964 0.5545 0.0102  0.0166  0.0115  332 ALA A CB  
2439 N N   . LYS A 333 ? 0.4454 0.4123 0.5096 -0.0049 0.0141  0.0000  333 LYS A N   
2440 C CA  . LYS A 333 ? 0.4897 0.4395 0.5612 -0.0087 0.0141  -0.0003 333 LYS A CA  
2441 C C   . LYS A 333 ? 0.4810 0.4211 0.5586 -0.0024 0.0157  0.0083  333 LYS A C   
2442 O O   . LYS A 333 ? 0.4543 0.3993 0.5317 0.0047  0.0156  0.0107  333 LYS A O   
2443 C CB  . LYS A 333 ? 0.5447 0.4910 0.6176 -0.0120 0.0113  -0.0099 333 LYS A CB  
2444 C CG  . LYS A 333 ? 0.6021 0.5308 0.6828 -0.0157 0.0114  -0.0102 333 LYS A CG  
2445 C CD  . LYS A 333 ? 0.6280 0.5535 0.7098 -0.0218 0.0088  -0.0204 333 LYS A CD  
2446 C CE  . LYS A 333 ? 0.6405 0.5484 0.7302 -0.0261 0.0092  -0.0202 333 LYS A CE  
2447 N NZ  . LYS A 333 ? 0.6223 0.5202 0.7157 -0.0259 0.0120  -0.0110 333 LYS A NZ  
2448 N N   . ARG A 334 ? 0.5007 0.4269 0.5838 -0.0053 0.0171  0.0125  334 ARG A N   
2449 C CA  . ARG A 334 ? 0.5379 0.4544 0.6267 0.0000  0.0188  0.0212  334 ARG A CA  
2450 C C   . ARG A 334 ? 0.5764 0.4813 0.6712 0.0008  0.0178  0.0181  334 ARG A C   
2451 O O   . ARG A 334 ? 0.7535 0.6592 0.8499 0.0076  0.0177  0.0202  334 ARG A O   
2452 C CB  . ARG A 334 ? 0.4797 0.3876 0.5710 -0.0033 0.0210  0.0277  334 ARG A CB  
2453 C CG  . ARG A 334 ? 0.4821 0.4011 0.5675 -0.0061 0.0218  0.0291  334 ARG A CG  
2454 C CD  . ARG A 334 ? 0.4867 0.4171 0.5688 0.0007  0.0232  0.0362  334 ARG A CD  
2455 N NE  . ARG A 334 ? 0.5009 0.4243 0.5881 0.0077  0.0245  0.0444  334 ARG A NE  
2456 C CZ  . ARG A 334 ? 0.4812 0.4136 0.5669 0.0152  0.0252  0.0499  334 ARG A CZ  
2457 N NH1 . ARG A 334 ? 0.4486 0.3977 0.5278 0.0170  0.0249  0.0484  334 ARG A NH1 
2458 N NH2 . ARG A 334 ? 0.4900 0.4148 0.5809 0.0210  0.0263  0.0571  334 ARG A NH2 
2459 N N   . HIS A 335 ? 0.5325 0.4271 0.6305 -0.0061 0.0170  0.0128  335 HIS A N   
2460 C CA  . HIS A 335 ? 0.5677 0.4501 0.6721 -0.0055 0.0163  0.0105  335 HIS A CA  
2461 C C   . HIS A 335 ? 0.5823 0.4606 0.6905 0.0031  0.0180  0.0190  335 HIS A C   
2462 O O   . HIS A 335 ? 0.6034 0.4684 0.7181 0.0039  0.0186  0.0207  335 HIS A O   
2463 C CB  . HIS A 335 ? 0.5450 0.4322 0.6480 -0.0068 0.0135  0.0004  335 HIS A CB  
2464 C CG  . HIS A 335 ? 0.5482 0.4499 0.6463 -0.0002 0.0125  -0.0006 335 HIS A CG  
2465 N ND1 . HIS A 335 ? 0.5444 0.4481 0.6436 0.0084  0.0137  0.0065  335 HIS A ND1 
2466 C CD2 . HIS A 335 ? 0.5110 0.4261 0.6028 -0.0011 0.0104  -0.0078 335 HIS A CD2 
2467 C CE1 . HIS A 335 ? 0.5555 0.4735 0.6492 0.0125  0.0125  0.0039  335 HIS A CE1 
2468 N NE2 . HIS A 335 ? 0.5222 0.4472 0.6112 0.0069  0.0105  -0.0048 335 HIS A NE2 
2469 N N   . THR B 2   ? 0.6502 0.7394 0.6876 -0.0613 -0.0155 0.0464  2   THR B N   
2470 C CA  . THR B 2   ? 0.6402 0.7177 0.6774 -0.0555 -0.0146 0.0415  2   THR B CA  
2471 C C   . THR B 2   ? 0.5704 0.6503 0.6176 -0.0515 -0.0122 0.0465  2   THR B C   
2472 O O   . THR B 2   ? 0.5666 0.6570 0.6222 -0.0524 -0.0111 0.0528  2   THR B O   
2473 C CB  . THR B 2   ? 0.6890 0.7618 0.7242 -0.0535 -0.0153 0.0359  2   THR B CB  
2474 O OG1 . THR B 2   ? 0.7603 0.8407 0.8045 -0.0519 -0.0146 0.0395  2   THR B OG1 
2475 C CG2 . THR B 2   ? 0.7125 0.7848 0.7388 -0.0579 -0.0171 0.0319  2   THR B CG2 
2476 N N   . LYS B 3   ? 0.4951 0.5658 0.5416 -0.0473 -0.0111 0.0439  3   LYS B N   
2477 C CA  . LYS B 3   ? 0.4634 0.5350 0.5188 -0.0435 -0.0085 0.0480  3   LYS B CA  
2478 C C   . LYS B 3   ? 0.4541 0.5261 0.5166 -0.0401 -0.0074 0.0468  3   LYS B C   
2479 O O   . LYS B 3   ? 0.3968 0.4645 0.4557 -0.0393 -0.0088 0.0414  3   LYS B O   
2480 C CB  . LYS B 3   ? 0.4630 0.5247 0.5152 -0.0398 -0.0077 0.0452  3   LYS B CB  
2481 C CG  . LYS B 3   ? 0.4538 0.5141 0.4995 -0.0423 -0.0088 0.0461  3   LYS B CG  
2482 C CD  . LYS B 3   ? 0.4835 0.5360 0.5281 -0.0381 -0.0077 0.0447  3   LYS B CD  
2483 C CE  . LYS B 3   ? 0.4885 0.5370 0.5251 -0.0397 -0.0094 0.0427  3   LYS B CE  
2484 N NZ  . LYS B 3   ? 0.5047 0.5470 0.5411 -0.0353 -0.0083 0.0421  3   LYS B NZ  
2485 N N   . PRO B 4   ? 0.4234 0.5005 0.4966 -0.0380 -0.0046 0.0522  4   PRO B N   
2486 C CA  . PRO B 4   ? 0.3961 0.4716 0.4766 -0.0339 -0.0032 0.0505  4   PRO B CA  
2487 C C   . PRO B 4   ? 0.4002 0.4627 0.4756 -0.0299 -0.0035 0.0428  4   PRO B C   
2488 O O   . PRO B 4   ? 0.4035 0.4594 0.4731 -0.0291 -0.0034 0.0408  4   PRO B O   
2489 C CB  . PRO B 4   ? 0.3874 0.4691 0.4797 -0.0324 0.0006  0.0577  4   PRO B CB  
2490 C CG  . PRO B 4   ? 0.4185 0.5086 0.5104 -0.0366 0.0007  0.0646  4   PRO B CG  
2491 C CD  . PRO B 4   ? 0.4319 0.5157 0.5109 -0.0391 -0.0024 0.0602  4   PRO B CD  
2492 N N   . ILE B 5   ? 0.3582 0.4177 0.4359 -0.0273 -0.0038 0.0391  5   ILE B N   
2493 C CA  . ILE B 5   ? 0.3497 0.3981 0.4223 -0.0241 -0.0044 0.0318  5   ILE B CA  
2494 C C   . ILE B 5   ? 0.3521 0.3973 0.4324 -0.0198 -0.0016 0.0315  5   ILE B C   
2495 O O   . ILE B 5   ? 0.3540 0.4049 0.4448 -0.0187 0.0002  0.0350  5   ILE B O   
2496 C CB  . ILE B 5   ? 0.3642 0.4106 0.4331 -0.0242 -0.0068 0.0278  5   ILE B CB  
2497 C CG1 . ILE B 5   ? 0.3781 0.4243 0.4368 -0.0282 -0.0091 0.0262  5   ILE B CG1 
2498 C CG2 . ILE B 5   ? 0.3385 0.3747 0.4043 -0.0207 -0.0069 0.0214  5   ILE B CG2 
2499 C CD1 . ILE B 5   ? 0.4038 0.4519 0.4605 -0.0295 -0.0111 0.0249  5   ILE B CD1 
2500 N N   . VAL B 6   ? 0.3583 0.3952 0.4338 -0.0177 -0.0010 0.0275  6   VAL B N   
2501 C CA  . VAL B 6   ? 0.3467 0.3785 0.4272 -0.0136 0.0014  0.0252  6   VAL B CA  
2502 C C   . VAL B 6   ? 0.3247 0.3484 0.3996 -0.0118 -0.0003 0.0178  6   VAL B C   
2503 O O   . VAL B 6   ? 0.3023 0.3215 0.3675 -0.0127 -0.0023 0.0141  6   VAL B O   
2504 C CB  . VAL B 6   ? 0.3721 0.4008 0.4509 -0.0125 0.0033  0.0260  6   VAL B CB  
2505 C CG1 . VAL B 6   ? 0.3820 0.4041 0.4635 -0.0085 0.0056  0.0220  6   VAL B CG1 
2506 C CG2 . VAL B 6   ? 0.3980 0.4347 0.4833 -0.0141 0.0054  0.0342  6   VAL B CG2 
2507 N N   . PHE B 7   ? 0.3026 0.3249 0.3840 -0.0092 0.0007  0.0162  7   PHE B N   
2508 C CA  . PHE B 7   ? 0.3373 0.3522 0.4148 -0.0072 -0.0005 0.0098  7   PHE B CA  
2509 C C   . PHE B 7   ? 0.3529 0.3640 0.4364 -0.0039 0.0021  0.0075  7   PHE B C   
2510 O O   . PHE B 7   ? 0.3410 0.3561 0.4351 -0.0029 0.0044  0.0107  7   PHE B O   
2511 C CB  . PHE B 7   ? 0.3196 0.3361 0.3980 -0.0077 -0.0027 0.0095  7   PHE B CB  
2512 C CG  . PHE B 7   ? 0.3284 0.3372 0.4014 -0.0060 -0.0042 0.0036  7   PHE B CG  
2513 C CD1 . PHE B 7   ? 0.3296 0.3359 0.4090 -0.0033 -0.0033 0.0015  7   PHE B CD1 
2514 C CD2 . PHE B 7   ? 0.3253 0.3296 0.3874 -0.0073 -0.0062 0.0003  7   PHE B CD2 
2515 C CE1 . PHE B 7   ? 0.3473 0.3469 0.4217 -0.0020 -0.0047 -0.0034 7   PHE B CE1 
2516 C CE2 . PHE B 7   ? 0.3652 0.3630 0.4227 -0.0059 -0.0073 -0.0043 7   PHE B CE2 
2517 C CZ  . PHE B 7   ? 0.3333 0.3288 0.3968 -0.0033 -0.0067 -0.0061 7   PHE B CZ  
2518 N N   . SER B 8   ? 0.3847 0.3886 0.4618 -0.0024 0.0020  0.0019  8   SER B N   
2519 C CA  . SER B 8   ? 0.4078 0.4074 0.4894 0.0004  0.0039  -0.0018 8   SER B CA  
2520 C C   . SER B 8   ? 0.4110 0.4037 0.4844 0.0012  0.0022  -0.0084 8   SER B C   
2521 O O   . SER B 8   ? 0.3409 0.3320 0.4052 -0.0001 0.0001  -0.0098 8   SER B O   
2522 C CB  . SER B 8   ? 0.4316 0.4308 0.5168 0.0018  0.0073  -0.0006 8   SER B CB  
2523 O OG  . SER B 8   ? 0.4018 0.3989 0.4950 0.0040  0.0099  -0.0026 8   SER B OG  
2524 N N   . GLY B 9   ? 0.4182 0.4073 0.4954 0.0033  0.0033  -0.0121 9   GLY B N   
2525 C CA  . GLY B 9   ? 0.4302 0.4135 0.5006 0.0041  0.0019  -0.0182 9   GLY B CA  
2526 C C   . GLY B 9   ? 0.4276 0.4073 0.5001 0.0061  0.0044  -0.0224 9   GLY B C   
2527 O O   . GLY B 9   ? 0.4067 0.3875 0.4878 0.0072  0.0072  -0.0211 9   GLY B O   
2528 N N   . ALA B 10  ? 0.4316 0.4074 0.4963 0.0064  0.0036  -0.0275 10  ALA B N   
2529 C CA  . ALA B 10  ? 0.4355 0.4078 0.5012 0.0080  0.0053  -0.0326 10  ALA B CA  
2530 C C   . ALA B 10  ? 0.4795 0.4488 0.5395 0.0077  0.0032  -0.0371 10  ALA B C   
2531 O O   . ALA B 10  ? 0.4103 0.3796 0.4625 0.0065  0.0010  -0.0370 10  ALA B O   
2532 C CB  . ALA B 10  ? 0.4330 0.4049 0.4948 0.0089  0.0072  -0.0338 10  ALA B CB  
2533 N N   . GLN B 11  ? 0.4870 0.4536 0.5510 0.0085  0.0040  -0.0408 11  GLN B N   
2534 C CA  . GLN B 11  ? 0.5278 0.4917 0.5872 0.0081  0.0020  -0.0449 11  GLN B CA  
2535 C C   . GLN B 11  ? 0.5217 0.4848 0.5726 0.0080  0.0023  -0.0491 11  GLN B C   
2536 O O   . GLN B 11  ? 0.5117 0.4747 0.5633 0.0091  0.0046  -0.0513 11  GLN B O   
2537 C CB  . GLN B 11  ? 0.5702 0.5318 0.6372 0.0089  0.0030  -0.0478 11  GLN B CB  
2538 C CG  . GLN B 11  ? 0.5799 0.5426 0.6555 0.0092  0.0022  -0.0440 11  GLN B CG  
2539 C CD  . GLN B 11  ? 0.5700 0.5302 0.6529 0.0100  0.0030  -0.0472 11  GLN B CD  
2540 O OE1 . GLN B 11  ? 0.5704 0.5276 0.6503 0.0099  0.0035  -0.0527 11  GLN B OE1 
2541 N NE2 . GLN B 11  ? 0.5564 0.5183 0.6493 0.0108  0.0030  -0.0438 11  GLN B NE2 
2542 N N   . PRO B 12  ? 0.5160 0.4789 0.5593 0.0069  0.0001  -0.0500 12  PRO B N   
2543 C CA  . PRO B 12  ? 0.5491 0.5124 0.5852 0.0069  0.0004  -0.0538 12  PRO B CA  
2544 C C   . PRO B 12  ? 0.5860 0.5473 0.6227 0.0068  0.0007  -0.0590 12  PRO B C   
2545 O O   . PRO B 12  ? 0.6327 0.5941 0.6642 0.0058  -0.0007 -0.0607 12  PRO B O   
2546 C CB  . PRO B 12  ? 0.5421 0.5065 0.5714 0.0055  -0.0016 -0.0515 12  PRO B CB  
2547 C CG  . PRO B 12  ? 0.5300 0.4925 0.5625 0.0049  -0.0034 -0.0490 12  PRO B CG  
2548 C CD  . PRO B 12  ? 0.5156 0.4783 0.5568 0.0058  -0.0024 -0.0469 12  PRO B CD  
2549 N N   . SER B 13  ? 0.5850 0.5447 0.6285 0.0078  0.0027  -0.0613 13  SER B N   
2550 C CA  . SER B 13  ? 0.6338 0.5913 0.6789 0.0076  0.0033  -0.0668 13  SER B CA  
2551 C C   . SER B 13  ? 0.7058 0.6628 0.7531 0.0089  0.0066  -0.0704 13  SER B C   
2552 O O   . SER B 13  ? 0.7081 0.6654 0.7602 0.0101  0.0086  -0.0677 13  SER B O   
2553 C CB  . SER B 13  ? 0.6139 0.5688 0.6667 0.0075  0.0025  -0.0660 13  SER B CB  
2554 O OG  . SER B 13  ? 0.6429 0.5980 0.7045 0.0087  0.0042  -0.0626 13  SER B OG  
2555 N N   . GLY B 14  ? 0.7564 0.7132 0.8004 0.0084  0.0072  -0.0763 14  GLY B N   
2556 C CA  . GLY B 14  ? 0.7797 0.7359 0.8249 0.0096  0.0105  -0.0804 14  GLY B CA  
2557 C C   . GLY B 14  ? 0.7345 0.6938 0.7756 0.0111  0.0115  -0.0783 14  GLY B C   
2558 O O   . GLY B 14  ? 0.7445 0.7072 0.7793 0.0108  0.0096  -0.0762 14  GLY B O   
2559 N N   . GLU B 15  ? 0.7566 0.7147 0.8018 0.0128  0.0148  -0.0786 15  GLU B N   
2560 C CA  . GLU B 15  ? 0.7372 0.6978 0.7791 0.0147  0.0161  -0.0768 15  GLU B CA  
2561 C C   . GLU B 15  ? 0.6949 0.6540 0.7438 0.0161  0.0185  -0.0719 15  GLU B C   
2562 O O   . GLU B 15  ? 0.6861 0.6421 0.7413 0.0168  0.0218  -0.0735 15  GLU B O   
2563 C CB  . GLU B 15  ? 0.7688 0.7300 0.8072 0.0156  0.0181  -0.0830 15  GLU B CB  
2564 C CG  . GLU B 15  ? 0.8502 0.8142 0.8820 0.0139  0.0160  -0.0878 15  GLU B CG  
2565 C CD  . GLU B 15  ? 0.8839 0.8488 0.9130 0.0144  0.0181  -0.0946 15  GLU B CD  
2566 O OE1 . GLU B 15  ? 0.9636 0.9260 0.9959 0.0161  0.0214  -0.0961 15  GLU B OE1 
2567 O OE2 . GLU B 15  ? 0.9013 0.8698 0.9249 0.0130  0.0167  -0.0983 15  GLU B OE2 
2568 N N   . LEU B 16  ? 0.6276 0.5890 0.6755 0.0163  0.0173  -0.0658 16  LEU B N   
2569 C CA  . LEU B 16  ? 0.6303 0.5915 0.6846 0.0172  0.0192  -0.0600 16  LEU B CA  
2570 C C   . LEU B 16  ? 0.6369 0.5968 0.6929 0.0195  0.0231  -0.0609 16  LEU B C   
2571 O O   . LEU B 16  ? 0.6209 0.5819 0.6711 0.0208  0.0233  -0.0635 16  LEU B O   
2572 C CB  . LEU B 16  ? 0.6615 0.6260 0.7128 0.0168  0.0169  -0.0538 16  LEU B CB  
2573 C CG  . LEU B 16  ? 0.6829 0.6483 0.7333 0.0146  0.0135  -0.0518 16  LEU B CG  
2574 C CD1 . LEU B 16  ? 0.7068 0.6754 0.7539 0.0139  0.0117  -0.0464 16  LEU B CD1 
2575 C CD2 . LEU B 16  ? 0.6863 0.6503 0.7452 0.0138  0.0142  -0.0500 16  LEU B CD2 
2576 N N   . THR B 17  ? 0.6035 0.5612 0.6680 0.0200  0.0264  -0.0581 17  THR B N   
2577 C CA  . THR B 17  ? 0.6064 0.5617 0.6741 0.0221  0.0309  -0.0590 17  THR B CA  
2578 C C   . THR B 17  ? 0.6286 0.5854 0.6996 0.0233  0.0327  -0.0509 17  THR B C   
2579 O O   . THR B 17  ? 0.5989 0.5588 0.6705 0.0222  0.0305  -0.0450 17  THR B O   
2580 C CB  . THR B 17  ? 0.6150 0.5664 0.6913 0.0217  0.0344  -0.0624 17  THR B CB  
2581 O OG1 . THR B 17  ? 0.6480 0.5999 0.7341 0.0216  0.0366  -0.0559 17  THR B OG1 
2582 C CG2 . THR B 17  ? 0.6214 0.5718 0.6966 0.0198  0.0318  -0.0682 17  THR B CG2 
2583 N N   . ILE B 18  ? 0.6372 0.5919 0.7104 0.0255  0.0369  -0.0504 18  ILE B N   
2584 C CA  . ILE B 18  ? 0.6697 0.6254 0.7471 0.0267  0.0394  -0.0422 18  ILE B CA  
2585 C C   . ILE B 18  ? 0.6671 0.6239 0.7545 0.0251  0.0409  -0.0367 18  ILE B C   
2586 O O   . ILE B 18  ? 0.6524 0.6122 0.7427 0.0249  0.0413  -0.0288 18  ILE B O   
2587 C CB  . ILE B 18  ? 0.6956 0.6479 0.7743 0.0295  0.0445  -0.0429 18  ILE B CB  
2588 C CG1 . ILE B 18  ? 0.7036 0.6576 0.7825 0.0312  0.0457  -0.0344 18  ILE B CG1 
2589 C CG2 . ILE B 18  ? 0.6945 0.6427 0.7826 0.0294  0.0497  -0.0449 18  ILE B CG2 
2590 C CD1 . ILE B 18  ? 0.7247 0.6818 0.7942 0.0324  0.0418  -0.0338 18  ILE B CD1 
2591 N N   . GLY B 19  ? 0.7049 0.6598 0.7981 0.0240  0.0419  -0.0408 19  GLY B N   
2592 C CA  . GLY B 19  ? 0.7034 0.6603 0.8069 0.0226  0.0429  -0.0362 19  GLY B CA  
2593 C C   . GLY B 19  ? 0.6389 0.6005 0.7399 0.0207  0.0380  -0.0320 19  GLY B C   
2594 O O   . GLY B 19  ? 0.6626 0.6282 0.7684 0.0201  0.0386  -0.0243 19  GLY B O   
2595 N N   . ASN B 20  ? 0.6784 0.6399 0.7717 0.0197  0.0334  -0.0369 20  ASN B N   
2596 C CA  . ASN B 20  ? 0.6676 0.6329 0.7565 0.0179  0.0287  -0.0338 20  ASN B CA  
2597 C C   . ASN B 20  ? 0.6032 0.5718 0.6882 0.0179  0.0278  -0.0274 20  ASN B C   
2598 O O   . ASN B 20  ? 0.5895 0.5620 0.6760 0.0163  0.0261  -0.0219 20  ASN B O   
2599 C CB  . ASN B 20  ? 0.6969 0.6609 0.7767 0.0171  0.0246  -0.0400 20  ASN B CB  
2600 C CG  . ASN B 20  ? 0.7040 0.6651 0.7869 0.0166  0.0246  -0.0458 20  ASN B CG  
2601 O OD1 . ASN B 20  ? 0.6883 0.6465 0.7675 0.0172  0.0252  -0.0523 20  ASN B OD1 
2602 N ND2 . ASN B 20  ? 0.6625 0.6247 0.7524 0.0157  0.0240  -0.0434 20  ASN B ND2 
2603 N N   . TYR B 21  ? 0.5674 0.5345 0.6477 0.0197  0.0292  -0.0282 21  TYR B N   
2604 C CA  . TYR B 21  ? 0.5602 0.5301 0.6370 0.0201  0.0285  -0.0222 21  TYR B CA  
2605 C C   . TYR B 21  ? 0.5666 0.5389 0.6516 0.0199  0.0316  -0.0139 21  TYR B C   
2606 O O   . TYR B 21  ? 0.5889 0.5654 0.6739 0.0183  0.0298  -0.0078 21  TYR B O   
2607 C CB  . TYR B 21  ? 0.5609 0.5289 0.6317 0.0228  0.0294  -0.0248 21  TYR B CB  
2608 C CG  . TYR B 21  ? 0.5717 0.5425 0.6389 0.0234  0.0283  -0.0187 21  TYR B CG  
2609 C CD1 . TYR B 21  ? 0.6056 0.5792 0.6662 0.0222  0.0240  -0.0182 21  TYR B CD1 
2610 C CD2 . TYR B 21  ? 0.6151 0.5857 0.6858 0.0251  0.0317  -0.0130 21  TYR B CD2 
2611 C CE1 . TYR B 21  ? 0.6129 0.5892 0.6707 0.0227  0.0229  -0.0127 21  TYR B CE1 
2612 C CE2 . TYR B 21  ? 0.6085 0.5818 0.6761 0.0257  0.0304  -0.0070 21  TYR B CE2 
2613 C CZ  . TYR B 21  ? 0.5997 0.5758 0.6609 0.0245  0.0259  -0.0071 21  TYR B CZ  
2614 O OH  . TYR B 21  ? 0.6449 0.6237 0.7033 0.0250  0.0245  -0.0014 21  TYR B OH  
2615 N N   . MET B 22  ? 0.6031 0.5729 0.6948 0.0216  0.0366  -0.0135 22  MET B N   
2616 C CA  . MET B 22  ? 0.6700 0.6422 0.7704 0.0216  0.0406  -0.0051 22  MET B CA  
2617 C C   . MET B 22  ? 0.6714 0.6484 0.7808 0.0193  0.0407  -0.0005 22  MET B C   
2618 O O   . MET B 22  ? 0.6671 0.6488 0.7814 0.0183  0.0420  0.0079  22  MET B O   
2619 C CB  . MET B 22  ? 0.6887 0.6564 0.7947 0.0240  0.0465  -0.0065 22  MET B CB  
2620 C CG  . MET B 22  ? 0.7582 0.7223 0.8566 0.0267  0.0472  -0.0090 22  MET B CG  
2621 S SD  . MET B 22  ? 0.8983 0.8663 0.9911 0.0271  0.0449  -0.0005 22  MET B SD  
2622 C CE  . MET B 22  ? 0.9409 0.9042 1.0267 0.0311  0.0464  -0.0049 22  MET B CE  
2623 N N   . GLY B 23  ? 0.6592 0.6354 0.7707 0.0184  0.0392  -0.0057 23  GLY B N   
2624 C CA  . GLY B 23  ? 0.6643 0.6454 0.7846 0.0166  0.0390  -0.0017 23  GLY B CA  
2625 C C   . GLY B 23  ? 0.6503 0.6360 0.7657 0.0143  0.0337  0.0002  23  GLY B C   
2626 O O   . GLY B 23  ? 0.6788 0.6701 0.8014 0.0127  0.0336  0.0053  23  GLY B O   
2627 N N   . ALA B 24  ? 0.5864 0.5698 0.6900 0.0139  0.0296  -0.0038 24  ALA B N   
2628 C CA  . ALA B 24  ? 0.5637 0.5502 0.6617 0.0117  0.0247  -0.0032 24  ALA B CA  
2629 C C   . ALA B 24  ? 0.5507 0.5374 0.6387 0.0113  0.0222  -0.0023 24  ALA B C   
2630 O O   . ALA B 24  ? 0.5455 0.5366 0.6339 0.0099  0.0219  0.0042  24  ALA B O   
2631 C CB  . ALA B 24  ? 0.5460 0.5294 0.6412 0.0116  0.0221  -0.0101 24  ALA B CB  
2632 N N   . LEU B 25  ? 0.5623 0.5447 0.6421 0.0125  0.0207  -0.0085 25  LEU B N   
2633 C CA  . LEU B 25  ? 0.5798 0.5628 0.6503 0.0123  0.0179  -0.0084 25  LEU B CA  
2634 C C   . LEU B 25  ? 0.5377 0.5232 0.6087 0.0126  0.0191  -0.0017 25  LEU B C   
2635 O O   . LEU B 25  ? 0.5513 0.5398 0.6184 0.0109  0.0167  0.0018  25  LEU B O   
2636 C CB  . LEU B 25  ? 0.5585 0.5376 0.6224 0.0143  0.0174  -0.0154 25  LEU B CB  
2637 C CG  . LEU B 25  ? 0.6204 0.5966 0.6838 0.0141  0.0166  -0.0222 25  LEU B CG  
2638 C CD1 . LEU B 25  ? 0.6266 0.6004 0.6830 0.0157  0.0161  -0.0285 25  LEU B CD1 
2639 C CD2 . LEU B 25  ? 0.6084 0.5861 0.6706 0.0117  0.0134  -0.0219 25  LEU B CD2 
2640 N N   . ARG B 26  ? 0.5525 0.5367 0.6283 0.0147  0.0230  0.0004  26  ARG B N   
2641 C CA  . ARG B 26  ? 0.5949 0.5812 0.6712 0.0152  0.0244  0.0075  26  ARG B CA  
2642 C C   . ARG B 26  ? 0.5576 0.5498 0.6370 0.0120  0.0233  0.0149  26  ARG B C   
2643 O O   . ARG B 26  ? 0.5900 0.5847 0.6656 0.0111  0.0216  0.0193  26  ARG B O   
2644 C CB  . ARG B 26  ? 0.6667 0.6507 0.7493 0.0177  0.0296  0.0096  26  ARG B CB  
2645 C CG  . ARG B 26  ? 0.7165 0.7030 0.8010 0.0181  0.0315  0.0186  26  ARG B CG  
2646 C CD  . ARG B 26  ? 0.7782 0.7626 0.8700 0.0204  0.0373  0.0216  26  ARG B CD  
2647 N NE  . ARG B 26  ? 0.8310 0.8154 0.9320 0.0196  0.0404  0.0205  26  ARG B NE  
2648 C CZ  . ARG B 26  ? 0.8486 0.8323 0.9587 0.0208  0.0461  0.0242  26  ARG B CZ  
2649 N NH1 . ARG B 26  ? 0.7423 0.7264 0.8614 0.0201  0.0488  0.0228  26  ARG B NH1 
2650 N NH2 . ARG B 26  ? 0.8641 0.8465 0.9747 0.0227  0.0495  0.0297  26  ARG B NH2 
2651 N N   . GLN B 27  ? 0.5666 0.5615 0.6532 0.0104  0.0242  0.0162  27  GLN B N   
2652 C CA  . GLN B 27  ? 0.5759 0.5777 0.6660 0.0071  0.0232  0.0231  27  GLN B CA  
2653 C C   . GLN B 27  ? 0.5605 0.5636 0.6424 0.0047  0.0182  0.0208  27  GLN B C   
2654 O O   . GLN B 27  ? 0.5389 0.5461 0.6184 0.0024  0.0165  0.0258  27  GLN B O   
2655 C CB  . GLN B 27  ? 0.5970 0.6023 0.6976 0.0063  0.0254  0.0249  27  GLN B CB  
2656 C CG  . GLN B 27  ? 0.6035 0.6097 0.7145 0.0079  0.0311  0.0299  27  GLN B CG  
2657 C CD  . GLN B 27  ? 0.6351 0.6337 0.7453 0.0113  0.0339  0.0244  27  GLN B CD  
2658 O OE1 . GLN B 27  ? 0.6789 0.6754 0.7874 0.0130  0.0361  0.0268  27  GLN B OE1 
2659 N NE2 . GLN B 27  ? 0.6669 0.6614 0.7778 0.0123  0.0336  0.0168  27  GLN B NE2 
2660 N N   . TRP B 28  ? 0.5118 0.5110 0.5892 0.0051  0.0160  0.0134  28  TRP B N   
2661 C CA  . TRP B 28  ? 0.5299 0.5293 0.5995 0.0031  0.0119  0.0106  28  TRP B CA  
2662 C C   . TRP B 28  ? 0.5030 0.5031 0.5660 0.0026  0.0103  0.0128  28  TRP B C   
2663 O O   . TRP B 28  ? 0.5726 0.5761 0.6328 -0.0003 0.0080  0.0156  28  TRP B O   
2664 C CB  . TRP B 28  ? 0.5053 0.4997 0.5701 0.0043  0.0104  0.0026  28  TRP B CB  
2665 C CG  . TRP B 28  ? 0.5098 0.5031 0.5801 0.0046  0.0110  -0.0003 28  TRP B CG  
2666 C CD1 . TRP B 28  ? 0.4991 0.4953 0.5793 0.0046  0.0134  0.0032  28  TRP B CD1 
2667 C CD2 . TRP B 28  ? 0.4944 0.4838 0.5612 0.0052  0.0095  -0.0068 28  TRP B CD2 
2668 N NE1 . TRP B 28  ? 0.4991 0.4930 0.5823 0.0053  0.0132  -0.0011 28  TRP B NE1 
2669 C CE2 . TRP B 28  ? 0.4688 0.4583 0.5435 0.0056  0.0107  -0.0072 28  TRP B CE2 
2670 C CE3 . TRP B 28  ? 0.4622 0.4483 0.5205 0.0055  0.0074  -0.0120 28  TRP B CE3 
2671 C CZ2 . TRP B 28  ? 0.4782 0.4643 0.5520 0.0062  0.0096  -0.0127 28  TRP B CZ2 
2672 C CZ3 . TRP B 28  ? 0.5088 0.4919 0.5660 0.0059  0.0065  -0.0171 28  TRP B CZ3 
2673 C CH2 . TRP B 28  ? 0.4887 0.4715 0.5534 0.0062  0.0074  -0.0175 28  TRP B CH2 
2674 N N   . VAL B 29  ? 0.4683 0.4652 0.5291 0.0055  0.0116  0.0116  29  VAL B N   
2675 C CA  . VAL B 29  ? 0.5124 0.5095 0.5674 0.0060  0.0102  0.0132  29  VAL B CA  
2676 C C   . VAL B 29  ? 0.4585 0.4603 0.5159 0.0040  0.0105  0.0217  29  VAL B C   
2677 O O   . VAL B 29  ? 0.4714 0.4754 0.5243 0.0021  0.0080  0.0236  29  VAL B O   
2678 C CB  . VAL B 29  ? 0.4955 0.4889 0.5490 0.0102  0.0120  0.0105  29  VAL B CB  
2679 C CG1 . VAL B 29  ? 0.4973 0.4915 0.5457 0.0112  0.0105  0.0124  29  VAL B CG1 
2680 C CG2 . VAL B 29  ? 0.4962 0.4858 0.5471 0.0116  0.0117  0.0023  29  VAL B CG2 
2681 N N   . ASN B 30  ? 0.4755 0.4793 0.5404 0.0042  0.0136  0.0268  30  ASN B N   
2682 C CA  . ASN B 30  ? 0.5250 0.5340 0.5934 0.0025  0.0145  0.0359  30  ASN B CA  
2683 C C   . ASN B 30  ? 0.5060 0.5214 0.5755 -0.0022 0.0125  0.0395  30  ASN B C   
2684 O O   . ASN B 30  ? 0.4831 0.5031 0.5526 -0.0045 0.0120  0.0462  30  ASN B O   
2685 C CB  . ASN B 30  ? 0.5526 0.5620 0.6296 0.0042  0.0193  0.0406  30  ASN B CB  
2686 C CG  . ASN B 30  ? 0.6062 0.6098 0.6823 0.0087  0.0218  0.0384  30  ASN B CG  
2687 O OD1 . ASN B 30  ? 0.6130 0.6142 0.6826 0.0105  0.0200  0.0368  30  ASN B OD1 
2688 N ND2 . ASN B 30  ? 0.6167 0.6184 0.6997 0.0107  0.0261  0.0384  30  ASN B ND2 
2689 N N   . MET B 31  ? 0.4721 0.4878 0.5423 -0.0036 0.0114  0.0352  31  MET B N   
2690 C CA  . MET B 31  ? 0.4566 0.4789 0.5285 -0.0078 0.0097  0.0383  31  MET B CA  
2691 C C   . MET B 31  ? 0.4525 0.4749 0.5158 -0.0106 0.0057  0.0357  31  MET B C   
2692 O O   . MET B 31  ? 0.4489 0.4769 0.5126 -0.0143 0.0042  0.0381  31  MET B O   
2693 C CB  . MET B 31  ? 0.4772 0.5004 0.5552 -0.0075 0.0106  0.0358  31  MET B CB  
2694 C CG  . MET B 31  ? 0.4959 0.5202 0.5842 -0.0053 0.0151  0.0391  31  MET B CG  
2695 S SD  . MET B 31  ? 0.5230 0.5469 0.6184 -0.0043 0.0159  0.0348  31  MET B SD  
2696 C CE  . MET B 31  ? 0.4806 0.5161 0.5835 -0.0081 0.0157  0.0425  31  MET B CE  
2697 N N   . GLN B 32  ? 0.4268 0.4437 0.4830 -0.0089 0.0043  0.0310  32  GLN B N   
2698 C CA  . GLN B 32  ? 0.4665 0.4820 0.5151 -0.0109 0.0011  0.0265  32  GLN B CA  
2699 C C   . GLN B 32  ? 0.4872 0.5074 0.5329 -0.0150 -0.0008 0.0308  32  GLN B C   
2700 O O   . GLN B 32  ? 0.5346 0.5551 0.5758 -0.0177 -0.0030 0.0280  32  GLN B O   
2701 C CB  . GLN B 32  ? 0.4748 0.4844 0.5178 -0.0078 0.0006  0.0211  32  GLN B CB  
2702 C CG  . GLN B 32  ? 0.4875 0.4923 0.5310 -0.0048 0.0016  0.0149  32  GLN B CG  
2703 C CD  . GLN B 32  ? 0.4962 0.4969 0.5342 -0.0022 0.0011  0.0100  32  GLN B CD  
2704 O OE1 . GLN B 32  ? 0.5289 0.5279 0.5623 -0.0030 -0.0004 0.0055  32  GLN B OE1 
2705 N NE2 . GLN B 32  ? 0.4779 0.4776 0.5166 0.0010  0.0025  0.0112  32  GLN B NE2 
2706 N N   . ASP B 33  ? 0.5215 0.5451 0.5693 -0.0154 0.0000  0.0374  33  ASP B N   
2707 C CA  . ASP B 33  ? 0.5223 0.5510 0.5676 -0.0198 -0.0019 0.0421  33  ASP B CA  
2708 C C   . ASP B 33  ? 0.4572 0.4940 0.5081 -0.0235 -0.0013 0.0479  33  ASP B C   
2709 O O   . ASP B 33  ? 0.4561 0.4974 0.5046 -0.0279 -0.0033 0.0485  33  ASP B O   
2710 C CB  . ASP B 33  ? 0.5517 0.5804 0.5961 -0.0187 -0.0018 0.0468  33  ASP B CB  
2711 C CG  . ASP B 33  ? 0.5785 0.6012 0.6175 -0.0156 -0.0028 0.0417  33  ASP B CG  
2712 O OD1 . ASP B 33  ? 0.6622 0.6818 0.7026 -0.0113 -0.0013 0.0423  33  ASP B OD1 
2713 O OD2 . ASP B 33  ? 0.5829 0.6042 0.6167 -0.0175 -0.0049 0.0372  33  ASP B OD2 
2714 N N   . ASP B 34  ? 0.4243 0.4633 0.4831 -0.0216 0.0017  0.0520  34  ASP B N   
2715 C CA  . ASP B 34  ? 0.4402 0.4881 0.5063 -0.0245 0.0030  0.0583  34  ASP B CA  
2716 C C   . ASP B 34  ? 0.4421 0.4928 0.5084 -0.0267 0.0015  0.0547  34  ASP B C   
2717 O O   . ASP B 34  ? 0.4276 0.4868 0.4961 -0.0307 0.0008  0.0591  34  ASP B O   
2718 C CB  . ASP B 34  ? 0.4470 0.4958 0.5225 -0.0213 0.0073  0.0626  34  ASP B CB  
2719 C CG  . ASP B 34  ? 0.4813 0.5296 0.5579 -0.0199 0.0092  0.0689  34  ASP B CG  
2720 O OD1 . ASP B 34  ? 0.4312 0.4796 0.5017 -0.0216 0.0070  0.0707  34  ASP B OD1 
2721 O OD2 . ASP B 34  ? 0.4636 0.5113 0.5474 -0.0169 0.0132  0.0719  34  ASP B OD2 
2722 N N   . TYR B 35  ? 0.4377 0.4817 0.5018 -0.0241 0.0010  0.0471  35  TYR B N   
2723 C CA  . TYR B 35  ? 0.4419 0.4873 0.5062 -0.0253 -0.0004 0.0435  35  TYR B CA  
2724 C C   . TYR B 35  ? 0.4433 0.4808 0.4986 -0.0247 -0.0028 0.0352  35  TYR B C   
2725 O O   . TYR B 35  ? 0.4628 0.4937 0.5133 -0.0225 -0.0029 0.0317  35  TYR B O   
2726 C CB  . TYR B 35  ? 0.4503 0.4963 0.5237 -0.0224 0.0021  0.0436  35  TYR B CB  
2727 C CG  . TYR B 35  ? 0.4458 0.4990 0.5295 -0.0223 0.0055  0.0517  35  TYR B CG  
2728 C CD1 . TYR B 35  ? 0.4890 0.5387 0.5772 -0.0188 0.0088  0.0532  35  TYR B CD1 
2729 C CD2 . TYR B 35  ? 0.4946 0.5588 0.5839 -0.0258 0.0057  0.0582  35  TYR B CD2 
2730 C CE1 . TYR B 35  ? 0.4615 0.5177 0.5598 -0.0187 0.0126  0.0612  35  TYR B CE1 
2731 C CE2 . TYR B 35  ? 0.4733 0.5451 0.5731 -0.0258 0.0093  0.0664  35  TYR B CE2 
2732 C CZ  . TYR B 35  ? 0.4674 0.5348 0.5717 -0.0222 0.0129  0.0681  35  TYR B CZ  
2733 O OH  . TYR B 35  ? 0.4432 0.5177 0.5579 -0.0222 0.0171  0.0766  35  TYR B OH  
2734 N N   . HIS B 36  ? 0.4207 0.4595 0.4742 -0.0266 -0.0045 0.0325  36  HIS B N   
2735 C CA  . HIS B 36  ? 0.3894 0.4211 0.4357 -0.0259 -0.0062 0.0253  36  HIS B CA  
2736 C C   . HIS B 36  ? 0.3558 0.3824 0.4055 -0.0217 -0.0051 0.0215  36  HIS B C   
2737 O O   . HIS B 36  ? 0.3463 0.3757 0.4017 -0.0212 -0.0047 0.0222  36  HIS B O   
2738 C CB  . HIS B 36  ? 0.3783 0.4135 0.4217 -0.0295 -0.0082 0.0246  36  HIS B CB  
2739 C CG  . HIS B 36  ? 0.3792 0.4072 0.4153 -0.0291 -0.0096 0.0180  36  HIS B CG  
2740 N ND1 . HIS B 36  ? 0.3858 0.4104 0.4137 -0.0311 -0.0107 0.0153  36  HIS B ND1 
2741 C CD2 . HIS B 36  ? 0.3511 0.3749 0.3872 -0.0268 -0.0098 0.0142  36  HIS B CD2 
2742 C CE1 . HIS B 36  ? 0.3934 0.4119 0.4167 -0.0301 -0.0111 0.0101  36  HIS B CE1 
2743 N NE2 . HIS B 36  ? 0.3838 0.4019 0.4117 -0.0276 -0.0108 0.0095  36  HIS B NE2 
2744 N N   . CYS B 37  ? 0.3428 0.3625 0.3892 -0.0187 -0.0045 0.0175  37  CYS B N   
2745 C CA  . CYS B 37  ? 0.3573 0.3723 0.4070 -0.0148 -0.0030 0.0141  37  CYS B CA  
2746 C C   . CYS B 37  ? 0.3378 0.3468 0.3817 -0.0139 -0.0044 0.0077  37  CYS B C   
2747 O O   . CYS B 37  ? 0.3350 0.3410 0.3715 -0.0147 -0.0055 0.0050  37  CYS B O   
2748 C CB  . CYS B 37  ? 0.4119 0.4243 0.4625 -0.0120 -0.0011 0.0144  37  CYS B CB  
2749 S SG  . CYS B 37  ? 0.4167 0.4355 0.4754 -0.0124 0.0014  0.0226  37  CYS B SG  
2750 N N   . ILE B 38  ? 0.3314 0.3390 0.3791 -0.0122 -0.0041 0.0057  38  ILE B N   
2751 C CA  . ILE B 38  ? 0.3086 0.3107 0.3515 -0.0113 -0.0053 0.0004  38  ILE B CA  
2752 C C   . ILE B 38  ? 0.3365 0.3350 0.3835 -0.0078 -0.0038 -0.0025 38  ILE B C   
2753 O O   . ILE B 38  ? 0.3732 0.3741 0.4285 -0.0067 -0.0026 -0.0006 38  ILE B O   
2754 C CB  . ILE B 38  ? 0.2847 0.2889 0.3280 -0.0131 -0.0070 0.0011  38  ILE B CB  
2755 C CG1 . ILE B 38  ? 0.2787 0.2868 0.3179 -0.0169 -0.0083 0.0036  38  ILE B CG1 
2756 C CG2 . ILE B 38  ? 0.2678 0.2661 0.3064 -0.0119 -0.0080 -0.0036 38  ILE B CG2 
2757 C CD1 . ILE B 38  ? 0.2962 0.3096 0.3387 -0.0186 -0.0095 0.0063  38  ILE B CD1 
2758 N N   . TYR B 39  ? 0.3367 0.3301 0.3784 -0.0062 -0.0036 -0.0069 39  TYR B N   
2759 C CA  . TYR B 39  ? 0.3312 0.3211 0.3755 -0.0033 -0.0023 -0.0105 39  TYR B CA  
2760 C C   . TYR B 39  ? 0.3576 0.3432 0.3971 -0.0028 -0.0035 -0.0151 39  TYR B C   
2761 O O   . TYR B 39  ? 0.3425 0.3266 0.3748 -0.0039 -0.0046 -0.0165 39  TYR B O   
2762 C CB  . TYR B 39  ? 0.3499 0.3388 0.3928 -0.0015 -0.0006 -0.0112 39  TYR B CB  
2763 C CG  . TYR B 39  ? 0.3565 0.3494 0.4044 -0.0019 0.0008  -0.0058 39  TYR B CG  
2764 C CD1 . TYR B 39  ? 0.3788 0.3741 0.4355 -0.0013 0.0026  -0.0029 39  TYR B CD1 
2765 C CD2 . TYR B 39  ? 0.3663 0.3611 0.4106 -0.0029 0.0004  -0.0031 39  TYR B CD2 
2766 C CE1 . TYR B 39  ? 0.3989 0.3986 0.4606 -0.0018 0.0043  0.0029  39  TYR B CE1 
2767 C CE2 . TYR B 39  ? 0.3886 0.3873 0.4373 -0.0034 0.0017  0.0025  39  TYR B CE2 
2768 C CZ  . TYR B 39  ? 0.3876 0.3888 0.4449 -0.0029 0.0037  0.0057  39  TYR B CZ  
2769 O OH  . TYR B 39  ? 0.4313 0.4370 0.4932 -0.0036 0.0053  0.0121  39  TYR B OH  
2770 N N   . CYS B 40  ? 0.3465 0.3303 0.3903 -0.0013 -0.0033 -0.0169 40  CYS B N   
2771 C CA  . CYS B 40  ? 0.4224 0.4027 0.4631 -0.0011 -0.0046 -0.0201 40  CYS B CA  
2772 C C   . CYS B 40  ? 0.4257 0.4027 0.4673 0.0011  -0.0035 -0.0245 40  CYS B C   
2773 O O   . CYS B 40  ? 0.4180 0.3954 0.4666 0.0025  -0.0019 -0.0246 40  CYS B O   
2774 C CB  . CYS B 40  ? 0.4064 0.3882 0.4519 -0.0016 -0.0059 -0.0177 40  CYS B CB  
2775 S SG  . CYS B 40  ? 0.4623 0.4397 0.5035 -0.0014 -0.0078 -0.0203 40  CYS B SG  
2776 N N   . ILE B 41  ? 0.4379 0.4120 0.4729 0.0011  -0.0042 -0.0279 41  ILE B N   
2777 C CA  . ILE B 41  ? 0.4705 0.4418 0.5056 0.0026  -0.0036 -0.0323 41  ILE B CA  
2778 C C   . ILE B 41  ? 0.4585 0.4279 0.4956 0.0025  -0.0052 -0.0325 41  ILE B C   
2779 O O   . ILE B 41  ? 0.4801 0.4481 0.5119 0.0014  -0.0066 -0.0321 41  ILE B O   
2780 C CB  . ILE B 41  ? 0.4690 0.4396 0.4965 0.0027  -0.0034 -0.0353 41  ILE B CB  
2781 C CG1 . ILE B 41  ? 0.4930 0.4660 0.5195 0.0033  -0.0020 -0.0345 41  ILE B CG1 
2782 C CG2 . ILE B 41  ? 0.4790 0.4477 0.5063 0.0037  -0.0029 -0.0398 41  ILE B CG2 
2783 C CD1 . ILE B 41  ? 0.5278 0.5017 0.5478 0.0033  -0.0018 -0.0360 41  ILE B CD1 
2784 N N   . VAL B 42  ? 0.4164 0.3855 0.4614 0.0037  -0.0046 -0.0329 42  VAL B N   
2785 C CA  . VAL B 42  ? 0.4168 0.3849 0.4659 0.0039  -0.0061 -0.0319 42  VAL B CA  
2786 C C   . VAL B 42  ? 0.4181 0.3825 0.4649 0.0044  -0.0068 -0.0360 42  VAL B C   
2787 O O   . VAL B 42  ? 0.3457 0.3088 0.3987 0.0055  -0.0062 -0.0380 42  VAL B O   
2788 C CB  . VAL B 42  ? 0.4120 0.3827 0.4724 0.0050  -0.0051 -0.0293 42  VAL B CB  
2789 C CG1 . VAL B 42  ? 0.4816 0.4570 0.5439 0.0039  -0.0052 -0.0243 42  VAL B CG1 
2790 C CG2 . VAL B 42  ? 0.4277 0.3980 0.4936 0.0063  -0.0022 -0.0318 42  VAL B CG2 
2791 N N   . ASP B 43  ? 0.3895 0.3523 0.4275 0.0034  -0.0079 -0.0369 43  ASP B N   
2792 C CA  . ASP B 43  ? 0.4125 0.3725 0.4470 0.0034  -0.0086 -0.0400 43  ASP B CA  
2793 C C   . ASP B 43  ? 0.4129 0.3709 0.4516 0.0038  -0.0105 -0.0387 43  ASP B C   
2794 O O   . ASP B 43  ? 0.4459 0.4018 0.4860 0.0043  -0.0108 -0.0416 43  ASP B O   
2795 C CB  . ASP B 43  ? 0.3897 0.3497 0.4147 0.0021  -0.0087 -0.0402 43  ASP B CB  
2796 C CG  . ASP B 43  ? 0.3990 0.3589 0.4204 0.0010  -0.0098 -0.0360 43  ASP B CG  
2797 O OD1 . ASP B 43  ? 0.3558 0.3166 0.3815 0.0010  -0.0105 -0.0330 43  ASP B OD1 
2798 O OD2 . ASP B 43  ? 0.4058 0.3652 0.4204 -0.0001 -0.0097 -0.0357 43  ASP B OD2 
2799 N N   . GLN B 44  ? 0.3683 0.3272 0.4093 0.0039  -0.0118 -0.0343 44  GLN B N   
2800 C CA  . GLN B 44  ? 0.3496 0.3075 0.3963 0.0049  -0.0136 -0.0322 44  GLN B CA  
2801 C C   . GLN B 44  ? 0.3375 0.2962 0.3953 0.0066  -0.0127 -0.0335 44  GLN B C   
2802 O O   . GLN B 44  ? 0.3267 0.2834 0.3884 0.0075  -0.0138 -0.0342 44  GLN B O   
2803 C CB  . GLN B 44  ? 0.3169 0.2765 0.3639 0.0047  -0.0151 -0.0272 44  GLN B CB  
2804 C CG  . GLN B 44  ? 0.3293 0.2865 0.3663 0.0034  -0.0161 -0.0258 44  GLN B CG  
2805 C CD  . GLN B 44  ? 0.2980 0.2569 0.3347 0.0030  -0.0172 -0.0213 44  GLN B CD  
2806 O OE1 . GLN B 44  ? 0.3068 0.2691 0.3444 0.0021  -0.0164 -0.0202 44  GLN B OE1 
2807 N NE2 . GLN B 44  ? 0.3027 0.2595 0.3382 0.0035  -0.0191 -0.0187 44  GLN B NE2 
2808 N N   . HIS B 45  ? 0.3198 0.2813 0.3827 0.0069  -0.0104 -0.0336 45  HIS B N   
2809 C CA  . HIS B 45  ? 0.3399 0.3021 0.4137 0.0084  -0.0086 -0.0350 45  HIS B CA  
2810 C C   . HIS B 45  ? 0.3574 0.3161 0.4296 0.0084  -0.0074 -0.0411 45  HIS B C   
2811 O O   . HIS B 45  ? 0.3692 0.3266 0.4492 0.0094  -0.0067 -0.0429 45  HIS B O   
2812 C CB  . HIS B 45  ? 0.3585 0.3248 0.4380 0.0086  -0.0060 -0.0328 45  HIS B CB  
2813 C CG  . HIS B 45  ? 0.3590 0.3301 0.4464 0.0091  -0.0065 -0.0270 45  HIS B CG  
2814 N ND1 . HIS B 45  ? 0.3241 0.2987 0.4079 0.0079  -0.0073 -0.0230 45  HIS B ND1 
2815 C CD2 . HIS B 45  ? 0.3821 0.3557 0.4812 0.0107  -0.0063 -0.0246 45  HIS B CD2 
2816 C CE1 . HIS B 45  ? 0.3471 0.3267 0.4398 0.0086  -0.0077 -0.0184 45  HIS B CE1 
2817 N NE2 . HIS B 45  ? 0.3416 0.3209 0.4441 0.0105  -0.0070 -0.0190 45  HIS B NE2 
2818 N N   . ALA B 46  ? 0.3375 0.2950 0.4000 0.0072  -0.0070 -0.0440 46  ALA B N   
2819 C CA  . ALA B 46  ? 0.3741 0.3295 0.4339 0.0070  -0.0058 -0.0498 46  ALA B CA  
2820 C C   . ALA B 46  ? 0.4190 0.3715 0.4781 0.0067  -0.0076 -0.0522 46  ALA B C   
2821 O O   . ALA B 46  ? 0.4555 0.4065 0.5167 0.0066  -0.0064 -0.0570 46  ALA B O   
2822 C CB  . ALA B 46  ? 0.3929 0.3492 0.4427 0.0060  -0.0053 -0.0513 46  ALA B CB  
2823 N N   . ILE B 47  ? 0.4385 0.3903 0.4945 0.0063  -0.0103 -0.0488 47  ILE B N   
2824 C CA  . ILE B 47  ? 0.4396 0.3888 0.4941 0.0059  -0.0124 -0.0499 47  ILE B CA  
2825 C C   . ILE B 47  ? 0.4334 0.3813 0.4986 0.0074  -0.0131 -0.0493 47  ILE B C   
2826 O O   . ILE B 47  ? 0.4723 0.4179 0.5373 0.0072  -0.0152 -0.0493 47  ILE B O   
2827 C CB  . ILE B 47  ? 0.4256 0.3741 0.4719 0.0049  -0.0147 -0.0460 47  ILE B CB  
2828 C CG1 . ILE B 47  ? 0.4207 0.3701 0.4702 0.0060  -0.0160 -0.0402 47  ILE B CG1 
2829 C CG2 . ILE B 47  ? 0.4520 0.4019 0.4884 0.0034  -0.0136 -0.0471 47  ILE B CG2 
2830 C CD1 . ILE B 47  ? 0.4596 0.4070 0.5047 0.0058  -0.0186 -0.0362 47  ILE B CD1 
2831 N N   . THR B 48  ? 0.4313 0.3812 0.5064 0.0088  -0.0114 -0.0481 48  THR B N   
2832 C CA  . THR B 48  ? 0.4251 0.3745 0.5126 0.0104  -0.0110 -0.0483 48  THR B CA  
2833 C C   . THR B 48  ? 0.4686 0.4152 0.5581 0.0099  -0.0092 -0.0550 48  THR B C   
2834 O O   . THR B 48  ? 0.4307 0.3761 0.5294 0.0108  -0.0091 -0.0561 48  THR B O   
2835 C CB  . THR B 48  ? 0.4373 0.3906 0.5357 0.0120  -0.0089 -0.0449 48  THR B CB  
2836 O OG1 . THR B 48  ? 0.4262 0.3806 0.5226 0.0114  -0.0058 -0.0469 48  THR B OG1 
2837 C CG2 . THR B 48  ? 0.4660 0.4226 0.5643 0.0126  -0.0111 -0.0382 48  THR B CG2 
2838 N N   . VAL B 49  ? 0.5367 0.4829 0.6182 0.0084  -0.0075 -0.0594 49  VAL B N   
2839 C CA  . VAL B 49  ? 0.5357 0.4796 0.6155 0.0073  -0.0063 -0.0662 49  VAL B CA  
2840 C C   . VAL B 49  ? 0.5679 0.5117 0.6347 0.0052  -0.0083 -0.0675 49  VAL B C   
2841 O O   . VAL B 49  ? 0.5275 0.4734 0.5869 0.0048  -0.0085 -0.0653 49  VAL B O   
2842 C CB  . VAL B 49  ? 0.5816 0.5260 0.6636 0.0075  -0.0022 -0.0700 49  VAL B CB  
2843 C CG1 . VAL B 49  ? 0.6075 0.5499 0.6855 0.0061  -0.0009 -0.0775 49  VAL B CG1 
2844 C CG2 . VAL B 49  ? 0.5808 0.5256 0.6766 0.0094  0.0004  -0.0681 49  VAL B CG2 
2845 N N   . ARG B 50  ? 0.5574 0.4994 0.6222 0.0039  -0.0096 -0.0710 50  ARG B N   
2846 C CA  . ARG B 50  ? 0.5920 0.5346 0.6457 0.0019  -0.0116 -0.0711 50  ARG B CA  
2847 C C   . ARG B 50  ? 0.5610 0.5064 0.6064 0.0007  -0.0096 -0.0744 50  ARG B C   
2848 O O   . ARG B 50  ? 0.5491 0.4948 0.5961 0.0006  -0.0072 -0.0797 50  ARG B O   
2849 C CB  . ARG B 50  ? 0.6188 0.5593 0.6729 0.0004  -0.0132 -0.0742 50  ARG B CB  
2850 C CG  . ARG B 50  ? 0.6671 0.6084 0.7111 -0.0016 -0.0156 -0.0723 50  ARG B CG  
2851 C CD  . ARG B 50  ? 0.6495 0.5909 0.6908 -0.0008 -0.0177 -0.0647 50  ARG B CD  
2852 N NE  . ARG B 50  ? 0.6498 0.5887 0.7002 0.0015  -0.0193 -0.0607 50  ARG B NE  
2853 C CZ  . ARG B 50  ? 0.6427 0.5791 0.6970 0.0018  -0.0217 -0.0592 50  ARG B CZ  
2854 N NH1 . ARG B 50  ? 0.6382 0.5735 0.7017 0.0043  -0.0230 -0.0551 50  ARG B NH1 
2855 N NH2 . ARG B 50  ? 0.6518 0.5874 0.7014 -0.0004 -0.0230 -0.0615 50  ARG B NH2 
2856 N N   . GLN B 51  ? 0.5639 0.5117 0.6011 0.0001  -0.0104 -0.0709 51  GLN B N   
2857 C CA  . GLN B 51  ? 0.5531 0.5046 0.5832 -0.0005 -0.0087 -0.0727 51  GLN B CA  
2858 C C   . GLN B 51  ? 0.5200 0.4741 0.5412 -0.0026 -0.0098 -0.0726 51  GLN B C   
2859 O O   . GLN B 51  ? 0.5103 0.4633 0.5294 -0.0033 -0.0119 -0.0686 51  GLN B O   
2860 C CB  . GLN B 51  ? 0.5533 0.5063 0.5822 0.0007  -0.0082 -0.0680 51  GLN B CB  
2861 C CG  . GLN B 51  ? 0.5764 0.5280 0.6136 0.0026  -0.0072 -0.0663 51  GLN B CG  
2862 C CD  . GLN B 51  ? 0.6101 0.5622 0.6508 0.0034  -0.0042 -0.0706 51  GLN B CD  
2863 O OE1 . GLN B 51  ? 0.6028 0.5574 0.6383 0.0033  -0.0028 -0.0726 51  GLN B OE1 
2864 N NE2 . GLN B 51  ? 0.6260 0.5759 0.6762 0.0045  -0.0030 -0.0717 51  GLN B NE2 
2865 N N   . ASP B 52  ? 0.4883 0.4462 0.5047 -0.0036 -0.0081 -0.0768 52  ASP B N   
2866 C CA  . ASP B 52  ? 0.5242 0.4868 0.5324 -0.0053 -0.0084 -0.0757 52  ASP B CA  
2867 C C   . ASP B 52  ? 0.5236 0.4880 0.5285 -0.0046 -0.0081 -0.0698 52  ASP B C   
2868 O O   . ASP B 52  ? 0.4932 0.4581 0.4998 -0.0030 -0.0068 -0.0694 52  ASP B O   
2869 C CB  . ASP B 52  ? 0.5334 0.5010 0.5386 -0.0060 -0.0063 -0.0815 52  ASP B CB  
2870 C CG  . ASP B 52  ? 0.5536 0.5277 0.5514 -0.0077 -0.0061 -0.0801 52  ASP B CG  
2871 O OD1 . ASP B 52  ? 0.6321 0.6081 0.6270 -0.0101 -0.0071 -0.0811 52  ASP B OD1 
2872 O OD2 . ASP B 52  ? 0.6219 0.6000 0.6172 -0.0067 -0.0048 -0.0776 52  ASP B OD2 
2873 N N   . ALA B 53  ? 0.4579 0.4230 0.4584 -0.0058 -0.0092 -0.0653 53  ALA B N   
2874 C CA  . ALA B 53  ? 0.4855 0.4511 0.4834 -0.0053 -0.0089 -0.0597 53  ALA B CA  
2875 C C   . ALA B 53  ? 0.5025 0.4734 0.4979 -0.0047 -0.0066 -0.0605 53  ALA B C   
2876 O O   . ALA B 53  ? 0.4571 0.4273 0.4535 -0.0035 -0.0060 -0.0580 53  ALA B O   
2877 C CB  . ALA B 53  ? 0.5152 0.4811 0.5084 -0.0070 -0.0098 -0.0550 53  ALA B CB  
2878 N N   . GLN B 54  ? 0.4837 0.4602 0.4762 -0.0055 -0.0052 -0.0639 54  GLN B N   
2879 C CA  . GLN B 54  ? 0.4986 0.4810 0.4895 -0.0046 -0.0031 -0.0646 54  GLN B CA  
2880 C C   . GLN B 54  ? 0.5019 0.4827 0.4970 -0.0024 -0.0023 -0.0676 54  GLN B C   
2881 O O   . GLN B 54  ? 0.4876 0.4701 0.4828 -0.0010 -0.0012 -0.0657 54  GLN B O   
2882 C CB  . GLN B 54  ? 0.5696 0.5596 0.5568 -0.0059 -0.0019 -0.0672 54  GLN B CB  
2883 C CG  . GLN B 54  ? 0.5965 0.5913 0.5794 -0.0076 -0.0012 -0.0624 54  GLN B CG  
2884 C CD  . GLN B 54  ? 0.6139 0.6041 0.5956 -0.0094 -0.0030 -0.0592 54  GLN B CD  
2885 O OE1 . GLN B 54  ? 0.6900 0.6786 0.6720 -0.0107 -0.0045 -0.0619 54  GLN B OE1 
2886 N NE2 . GLN B 54  ? 0.6993 0.6872 0.6798 -0.0095 -0.0029 -0.0532 54  GLN B NE2 
2887 N N   . LYS B 55  ? 0.4788 0.4560 0.4775 -0.0022 -0.0027 -0.0720 55  LYS B N   
2888 C CA  . LYS B 55  ? 0.4973 0.4722 0.5008 -0.0002 -0.0016 -0.0744 55  LYS B CA  
2889 C C   . LYS B 55  ? 0.4560 0.4274 0.4628 0.0011  -0.0020 -0.0698 55  LYS B C   
2890 O O   . LYS B 55  ? 0.4599 0.4323 0.4683 0.0027  -0.0008 -0.0694 55  LYS B O   
2891 C CB  . LYS B 55  ? 0.5478 0.5190 0.5556 -0.0003 -0.0015 -0.0795 55  LYS B CB  
2892 C CG  . LYS B 55  ? 0.6439 0.6190 0.6490 -0.0011 -0.0002 -0.0855 55  LYS B CG  
2893 C CD  . LYS B 55  ? 0.7301 0.7009 0.7399 -0.0014 0.0003  -0.0910 55  LYS B CD  
2894 C CE  . LYS B 55  ? 0.7919 0.7602 0.8068 0.0009  0.0026  -0.0931 55  LYS B CE  
2895 N NZ  . LYS B 55  ? 0.8754 0.8427 0.8918 0.0004  0.0044  -0.1003 55  LYS B NZ  
2896 N N   . LEU B 56  ? 0.4438 0.4117 0.4518 0.0003  -0.0039 -0.0664 56  LEU B N   
2897 C CA  . LEU B 56  ? 0.4306 0.3958 0.4417 0.0011  -0.0045 -0.0619 56  LEU B CA  
2898 C C   . LEU B 56  ? 0.4061 0.3741 0.4133 0.0012  -0.0039 -0.0583 56  LEU B C   
2899 O O   . LEU B 56  ? 0.4075 0.3756 0.4170 0.0023  -0.0033 -0.0567 56  LEU B O   
2900 C CB  . LEU B 56  ? 0.4322 0.3937 0.4447 0.0004  -0.0067 -0.0589 56  LEU B CB  
2901 C CG  . LEU B 56  ? 0.4386 0.3976 0.4552 0.0011  -0.0077 -0.0545 56  LEU B CG  
2902 C CD1 . LEU B 56  ? 0.4212 0.3795 0.4451 0.0026  -0.0066 -0.0557 56  LEU B CD1 
2903 C CD2 . LEU B 56  ? 0.4408 0.3965 0.4589 0.0007  -0.0099 -0.0520 56  LEU B CD2 
2904 N N   . ARG B 57  ? 0.4287 0.3994 0.4304 0.0000  -0.0038 -0.0568 57  ARG B N   
2905 C CA  . ARG B 57  ? 0.4254 0.3992 0.4238 0.0000  -0.0028 -0.0537 57  ARG B CA  
2906 C C   . ARG B 57  ? 0.4665 0.4441 0.4658 0.0016  -0.0011 -0.0556 57  ARG B C   
2907 O O   . ARG B 57  ? 0.4103 0.3880 0.4107 0.0024  -0.0008 -0.0532 57  ARG B O   
2908 C CB  . ARG B 57  ? 0.4478 0.4248 0.4412 -0.0014 -0.0022 -0.0520 57  ARG B CB  
2909 C CG  . ARG B 57  ? 0.4402 0.4193 0.4312 -0.0017 -0.0009 -0.0479 57  ARG B CG  
2910 C CD  . ARG B 57  ? 0.4730 0.4527 0.4601 -0.0034 -0.0004 -0.0445 57  ARG B CD  
2911 N NE  . ARG B 57  ? 0.4827 0.4563 0.4698 -0.0042 -0.0024 -0.0422 57  ARG B NE  
2912 C CZ  . ARG B 57  ? 0.5283 0.5008 0.5124 -0.0056 -0.0024 -0.0391 57  ARG B CZ  
2913 N NH1 . ARG B 57  ? 0.6169 0.5945 0.5978 -0.0066 -0.0004 -0.0377 57  ARG B NH1 
2914 N NH2 . ARG B 57  ? 0.5104 0.4772 0.4949 -0.0058 -0.0044 -0.0369 57  ARG B NH2 
2915 N N   . LYS B 58  ? 0.4531 0.4340 0.4519 0.0021  -0.0002 -0.0597 58  LYS B N   
2916 C CA  . LYS B 58  ? 0.4536 0.4383 0.4531 0.0040  0.0014  -0.0617 58  LYS B CA  
2917 C C   . LYS B 58  ? 0.4239 0.4049 0.4281 0.0055  0.0015  -0.0619 58  LYS B C   
2918 O O   . LYS B 58  ? 0.4209 0.4036 0.4258 0.0069  0.0023  -0.0601 58  LYS B O   
2919 C CB  . LYS B 58  ? 0.4744 0.4631 0.4725 0.0040  0.0023  -0.0666 58  LYS B CB  
2920 C CG  . LYS B 58  ? 0.5066 0.5002 0.5050 0.0063  0.0040  -0.0685 58  LYS B CG  
2921 C CD  . LYS B 58  ? 0.5507 0.5508 0.5463 0.0060  0.0049  -0.0724 58  LYS B CD  
2922 C CE  . LYS B 58  ? 0.5700 0.5753 0.5660 0.0087  0.0066  -0.0743 58  LYS B CE  
2923 N NZ  . LYS B 58  ? 0.6179 0.6181 0.6175 0.0107  0.0071  -0.0752 58  LYS B NZ  
2924 N N   . ALA B 59  ? 0.3897 0.3660 0.3977 0.0052  0.0009  -0.0636 59  ALA B N   
2925 C CA  . ALA B 59  ? 0.4082 0.3813 0.4217 0.0065  0.0015  -0.0632 59  ALA B CA  
2926 C C   . ALA B 59  ? 0.4155 0.3875 0.4306 0.0064  0.0008  -0.0580 59  ALA B C   
2927 O O   . ALA B 59  ? 0.3827 0.3544 0.4015 0.0075  0.0017  -0.0566 59  ALA B O   
2928 C CB  . ALA B 59  ? 0.3897 0.3587 0.4079 0.0061  0.0013  -0.0659 59  ALA B CB  
2929 N N   . THR B 60  ? 0.4366 0.4081 0.4491 0.0049  -0.0007 -0.0550 60  THR B N   
2930 C CA  . THR B 60  ? 0.4415 0.4124 0.4546 0.0043  -0.0015 -0.0503 60  THR B CA  
2931 C C   . THR B 60  ? 0.4326 0.4069 0.4433 0.0050  -0.0005 -0.0487 60  THR B C   
2932 O O   . THR B 60  ? 0.4540 0.4284 0.4671 0.0054  -0.0003 -0.0462 60  THR B O   
2933 C CB  . THR B 60  ? 0.4420 0.4111 0.4522 0.0026  -0.0031 -0.0478 60  THR B CB  
2934 O OG1 . THR B 60  ? 0.3792 0.3452 0.3922 0.0024  -0.0042 -0.0489 60  THR B OG1 
2935 C CG2 . THR B 60  ? 0.4361 0.4046 0.4467 0.0018  -0.0038 -0.0435 60  THR B CG2 
2936 N N   . LEU B 61  ? 0.4889 0.4666 0.4955 0.0052  0.0003  -0.0500 61  LEU B N   
2937 C CA  . LEU B 61  ? 0.4676 0.4494 0.4727 0.0061  0.0013  -0.0486 61  LEU B CA  
2938 C C   . LEU B 61  ? 0.4550 0.4384 0.4627 0.0085  0.0025  -0.0502 61  LEU B C   
2939 O O   . LEU B 61  ? 0.4566 0.4416 0.4651 0.0095  0.0029  -0.0478 61  LEU B O   
2940 C CB  . LEU B 61  ? 0.4682 0.4542 0.4692 0.0058  0.0021  -0.0489 61  LEU B CB  
2941 C CG  . LEU B 61  ? 0.4649 0.4494 0.4631 0.0036  0.0016  -0.0467 61  LEU B CG  
2942 C CD1 . LEU B 61  ? 0.5060 0.4954 0.5011 0.0032  0.0029  -0.0469 61  LEU B CD1 
2943 C CD2 . LEU B 61  ? 0.4565 0.4395 0.4545 0.0026  0.0013  -0.0428 61  LEU B CD2 
2944 N N   . ASP B 62  ? 0.4763 0.4588 0.4854 0.0093  0.0031  -0.0542 62  ASP B N   
2945 C CA  . ASP B 62  ? 0.4962 0.4789 0.5083 0.0115  0.0045  -0.0557 62  ASP B CA  
2946 C C   . ASP B 62  ? 0.4801 0.4596 0.4966 0.0117  0.0046  -0.0522 62  ASP B C   
2947 O O   . ASP B 62  ? 0.4766 0.4575 0.4945 0.0133  0.0055  -0.0502 62  ASP B O   
2948 C CB  . ASP B 62  ? 0.4844 0.4655 0.4976 0.0118  0.0054  -0.0609 62  ASP B CB  
2949 C CG  . ASP B 62  ? 0.4887 0.4742 0.4977 0.0117  0.0056  -0.0645 62  ASP B CG  
2950 O OD1 . ASP B 62  ? 0.5152 0.4994 0.5242 0.0110  0.0058  -0.0688 62  ASP B OD1 
2951 O OD2 . ASP B 62  ? 0.4850 0.4756 0.4910 0.0122  0.0057  -0.0630 62  ASP B OD2 
2952 N N   . THR B 63  ? 0.5207 0.4969 0.5399 0.0101  0.0036  -0.0511 63  THR B N   
2953 C CA  . THR B 63  ? 0.5022 0.4766 0.5264 0.0100  0.0038  -0.0474 63  THR B CA  
2954 C C   . THR B 63  ? 0.4763 0.4529 0.4989 0.0094  0.0030  -0.0427 63  THR B C   
2955 O O   . THR B 63  ? 0.4614 0.4386 0.4869 0.0102  0.0039  -0.0397 63  THR B O   
2956 C CB  . THR B 63  ? 0.4791 0.4507 0.5068 0.0086  0.0027  -0.0471 63  THR B CB  
2957 O OG1 . THR B 63  ? 0.4605 0.4301 0.4898 0.0090  0.0034  -0.0517 63  THR B OG1 
2958 C CG2 . THR B 63  ? 0.4838 0.4550 0.5178 0.0085  0.0032  -0.0430 63  THR B CG2 
2959 N N   . LEU B 64  ? 0.4637 0.4414 0.4817 0.0081  0.0018  -0.0420 64  LEU B N   
2960 C CA  . LEU B 64  ? 0.4639 0.4435 0.4800 0.0073  0.0012  -0.0382 64  LEU B CA  
2961 C C   . LEU B 64  ? 0.4314 0.4140 0.4473 0.0094  0.0023  -0.0374 64  LEU B C   
2962 O O   . LEU B 64  ? 0.4265 0.4098 0.4442 0.0094  0.0024  -0.0338 64  LEU B O   
2963 C CB  . LEU B 64  ? 0.4956 0.4757 0.5071 0.0056  0.0004  -0.0381 64  LEU B CB  
2964 C CG  . LEU B 64  ? 0.5049 0.4868 0.5142 0.0046  0.0002  -0.0349 64  LEU B CG  
2965 C CD1 . LEU B 64  ? 0.5142 0.4950 0.5256 0.0028  -0.0008 -0.0314 64  LEU B CD1 
2966 C CD2 . LEU B 64  ? 0.5273 0.5096 0.5324 0.0032  0.0002  -0.0353 64  LEU B CD2 
2967 N N   . ALA B 65  ? 0.3894 0.3742 0.4032 0.0111  0.0032  -0.0406 65  ALA B N   
2968 C CA  . ALA B 65  ? 0.3827 0.3709 0.3965 0.0137  0.0042  -0.0400 65  ALA B CA  
2969 C C   . ALA B 65  ? 0.3818 0.3686 0.3995 0.0155  0.0054  -0.0391 65  ALA B C   
2970 O O   . ALA B 65  ? 0.3734 0.3619 0.3919 0.0171  0.0058  -0.0361 65  ALA B O   
2971 C CB  . ALA B 65  ? 0.3872 0.3790 0.3986 0.0151  0.0051  -0.0437 65  ALA B CB  
2972 N N   . LEU B 66  ? 0.4107 0.3941 0.4310 0.0153  0.0060  -0.0414 66  LEU B N   
2973 C CA  . LEU B 66  ? 0.4059 0.3876 0.4307 0.0168  0.0078  -0.0402 66  LEU B CA  
2974 C C   . LEU B 66  ? 0.4085 0.3898 0.4365 0.0157  0.0075  -0.0342 66  LEU B C   
2975 O O   . LEU B 66  ? 0.3998 0.3817 0.4299 0.0173  0.0087  -0.0310 66  LEU B O   
2976 C CB  . LEU B 66  ? 0.4467 0.4250 0.4744 0.0166  0.0089  -0.0442 66  LEU B CB  
2977 C CG  . LEU B 66  ? 0.5205 0.4968 0.5529 0.0186  0.0117  -0.0443 66  LEU B CG  
2978 C CD1 . LEU B 66  ? 0.5623 0.5407 0.5927 0.0215  0.0130  -0.0441 66  LEU B CD1 
2979 C CD2 . LEU B 66  ? 0.5688 0.5421 0.6030 0.0185  0.0130  -0.0499 66  LEU B CD2 
2980 N N   . TYR B 67  ? 0.4200 0.4008 0.4481 0.0129  0.0059  -0.0325 67  TYR B N   
2981 C CA  . TYR B 67  ? 0.4201 0.4020 0.4505 0.0113  0.0052  -0.0269 67  TYR B CA  
2982 C C   . TYR B 67  ? 0.4095 0.3941 0.4373 0.0118  0.0047  -0.0236 67  TYR B C   
2983 O O   . TYR B 67  ? 0.4098 0.3954 0.4403 0.0121  0.0054  -0.0191 67  TYR B O   
2984 C CB  . TYR B 67  ? 0.4286 0.4102 0.4579 0.0083  0.0033  -0.0263 67  TYR B CB  
2985 C CG  . TYR B 67  ? 0.4508 0.4304 0.4839 0.0075  0.0032  -0.0277 67  TYR B CG  
2986 C CD1 . TYR B 67  ? 0.4850 0.4626 0.5225 0.0091  0.0050  -0.0302 67  TYR B CD1 
2987 C CD2 . TYR B 67  ? 0.4791 0.4587 0.5115 0.0051  0.0014  -0.0264 67  TYR B CD2 
2988 C CE1 . TYR B 67  ? 0.4909 0.4668 0.5326 0.0084  0.0049  -0.0313 67  TYR B CE1 
2989 C CE2 . TYR B 67  ? 0.4887 0.4668 0.5251 0.0046  0.0012  -0.0272 67  TYR B CE2 
2990 C CZ  . TYR B 67  ? 0.4903 0.4667 0.5316 0.0063  0.0028  -0.0296 67  TYR B CZ  
2991 O OH  . TYR B 67  ? 0.4652 0.4405 0.5112 0.0059  0.0024  -0.0300 67  TYR B OH  
2992 N N   . LEU B 68  ? 0.3872 0.3732 0.4103 0.0118  0.0037  -0.0255 68  LEU B N   
2993 C CA  . LEU B 68  ? 0.4026 0.3915 0.4238 0.0125  0.0032  -0.0227 68  LEU B CA  
2994 C C   . LEU B 68  ? 0.4467 0.4369 0.4695 0.0160  0.0046  -0.0216 68  LEU B C   
2995 O O   . LEU B 68  ? 0.4697 0.4612 0.4937 0.0164  0.0045  -0.0169 68  LEU B O   
2996 C CB  . LEU B 68  ? 0.4196 0.4102 0.4367 0.0121  0.0026  -0.0252 68  LEU B CB  
2997 C CG  . LEU B 68  ? 0.4486 0.4378 0.4636 0.0086  0.0013  -0.0252 68  LEU B CG  
2998 C CD1 . LEU B 68  ? 0.4665 0.4568 0.4781 0.0084  0.0015  -0.0281 68  LEU B CD1 
2999 C CD2 . LEU B 68  ? 0.4368 0.4270 0.4516 0.0064  0.0003  -0.0210 68  LEU B CD2 
3000 N N   . ALA B 69  ? 0.4489 0.4385 0.4718 0.0184  0.0060  -0.0257 69  ALA B N   
3001 C CA  . ALA B 69  ? 0.4546 0.4450 0.4788 0.0220  0.0076  -0.0252 69  ALA B CA  
3002 C C   . ALA B 69  ? 0.4698 0.4579 0.4983 0.0224  0.0091  -0.0212 69  ALA B C   
3003 O O   . ALA B 69  ? 0.4597 0.4487 0.4893 0.0248  0.0100  -0.0178 69  ALA B O   
3004 C CB  . ALA B 69  ? 0.4675 0.4578 0.4906 0.0239  0.0088  -0.0312 69  ALA B CB  
3005 N N   . CYS B 70  ? 0.5332 0.5188 0.5647 0.0200  0.0094  -0.0209 70  CYS B N   
3006 C CA  . CYS B 70  ? 0.4927 0.4771 0.5295 0.0199  0.0112  -0.0162 70  CYS B CA  
3007 C C   . CYS B 70  ? 0.4783 0.4651 0.5157 0.0185  0.0101  -0.0092 70  CYS B C   
3008 O O   . CYS B 70  ? 0.4769 0.4638 0.5182 0.0190  0.0118  -0.0041 70  CYS B O   
3009 C CB  . CYS B 70  ? 0.5132 0.4955 0.5539 0.0178  0.0119  -0.0176 70  CYS B CB  
3010 S SG  . CYS B 70  ? 0.5882 0.5668 0.6312 0.0197  0.0145  -0.0241 70  CYS B SG  
3011 N N   . GLY B 71  ? 0.4548 0.4437 0.4883 0.0168  0.0076  -0.0088 71  GLY B N   
3012 C CA  . GLY B 71  ? 0.4196 0.4111 0.4531 0.0149  0.0062  -0.0028 71  GLY B CA  
3013 C C   . GLY B 71  ? 0.4301 0.4224 0.4632 0.0105  0.0045  -0.0019 71  GLY B C   
3014 O O   . GLY B 71  ? 0.4060 0.4007 0.4392 0.0083  0.0035  0.0030  71  GLY B O   
3015 N N   . ILE B 72  ? 0.3966 0.3872 0.4291 0.0093  0.0041  -0.0064 72  ILE B N   
3016 C CA  . ILE B 72  ? 0.3988 0.3902 0.4301 0.0055  0.0023  -0.0059 72  ILE B CA  
3017 C C   . ILE B 72  ? 0.4308 0.4233 0.4569 0.0044  0.0006  -0.0066 72  ILE B C   
3018 O O   . ILE B 72  ? 0.4243 0.4161 0.4475 0.0062  0.0007  -0.0104 72  ILE B O   
3019 C CB  . ILE B 72  ? 0.4157 0.4048 0.4476 0.0049  0.0022  -0.0104 72  ILE B CB  
3020 C CG1 . ILE B 72  ? 0.4216 0.4095 0.4595 0.0062  0.0043  -0.0104 72  ILE B CG1 
3021 C CG2 . ILE B 72  ? 0.4060 0.3960 0.4366 0.0013  0.0004  -0.0093 72  ILE B CG2 
3022 C CD1 . ILE B 72  ? 0.4569 0.4476 0.5006 0.0047  0.0051  -0.0043 72  ILE B CD1 
3023 N N   . ASP B 73  ? 0.4403 0.4349 0.4657 0.0013  -0.0007 -0.0029 73  ASP B N   
3024 C CA  . ASP B 73  ? 0.4608 0.4566 0.4823 0.0000  -0.0020 -0.0026 73  ASP B CA  
3025 C C   . ASP B 73  ? 0.4689 0.4638 0.4873 -0.0034 -0.0031 -0.0048 73  ASP B C   
3026 O O   . ASP B 73  ? 0.4269 0.4231 0.4463 -0.0065 -0.0039 -0.0024 73  ASP B O   
3027 C CB  . ASP B 73  ? 0.4990 0.4977 0.5216 -0.0011 -0.0025 0.0033  73  ASP B CB  
3028 C CG  . ASP B 73  ? 0.5539 0.5538 0.5734 -0.0019 -0.0036 0.0037  73  ASP B CG  
3029 O OD1 . ASP B 73  ? 0.6003 0.5991 0.6168 -0.0018 -0.0036 -0.0004 73  ASP B OD1 
3030 O OD2 . ASP B 73  ? 0.5683 0.5705 0.5887 -0.0026 -0.0042 0.0084  73  ASP B OD2 
3031 N N   . PRO B 74  ? 0.4589 0.4521 0.4739 -0.0029 -0.0030 -0.0089 74  PRO B N   
3032 C CA  . PRO B 74  ? 0.5064 0.4984 0.5182 -0.0060 -0.0037 -0.0106 74  PRO B CA  
3033 C C   . PRO B 74  ? 0.4987 0.4923 0.5086 -0.0097 -0.0048 -0.0079 74  PRO B C   
3034 O O   . PRO B 74  ? 0.4739 0.4666 0.4815 -0.0127 -0.0053 -0.0087 74  PRO B O   
3035 C CB  . PRO B 74  ? 0.5086 0.4992 0.5176 -0.0044 -0.0028 -0.0144 74  PRO B CB  
3036 C CG  . PRO B 74  ? 0.5126 0.5054 0.5230 -0.0012 -0.0021 -0.0139 74  PRO B CG  
3037 C CD  . PRO B 74  ? 0.4911 0.4844 0.5051 0.0004  -0.0021 -0.0114 74  PRO B CD  
3038 N N   . GLU B 75  ? 0.5531 0.5491 0.5640 -0.0095 -0.0050 -0.0048 75  GLU B N   
3039 C CA  . GLU B 75  ? 0.5489 0.5469 0.5583 -0.0132 -0.0060 -0.0021 75  GLU B CA  
3040 C C   . GLU B 75  ? 0.5559 0.5565 0.5674 -0.0160 -0.0070 0.0019  75  GLU B C   
3041 O O   . GLU B 75  ? 0.6257 0.6282 0.6355 -0.0199 -0.0080 0.0036  75  GLU B O   
3042 C CB  . GLU B 75  ? 0.5672 0.5670 0.5773 -0.0117 -0.0060 0.0000  75  GLU B CB  
3043 N N   . LYS B 76  ? 0.5229 0.5242 0.5385 -0.0140 -0.0064 0.0036  76  LYS B N   
3044 C CA  . LYS B 76  ? 0.5010 0.5058 0.5201 -0.0161 -0.0067 0.0081  76  LYS B CA  
3045 C C   . LYS B 76  ? 0.4969 0.5014 0.5180 -0.0166 -0.0066 0.0064  76  LYS B C   
3046 O O   . LYS B 76  ? 0.4849 0.4927 0.5071 -0.0198 -0.0073 0.0088  76  LYS B O   
3047 C CB  . LYS B 76  ? 0.5205 0.5269 0.5442 -0.0134 -0.0055 0.0123  76  LYS B CB  
3048 C CG  . LYS B 76  ? 0.5268 0.5348 0.5496 -0.0132 -0.0060 0.0158  76  LYS B CG  
3049 C CD  . LYS B 76  ? 0.5547 0.5639 0.5820 -0.0103 -0.0046 0.0205  76  LYS B CD  
3050 C CE  . LYS B 76  ? 0.5791 0.5896 0.6055 -0.0095 -0.0052 0.0244  76  LYS B CE  
3051 N NZ  . LYS B 76  ? 0.5814 0.5921 0.6117 -0.0060 -0.0036 0.0289  76  LYS B NZ  
3052 N N   . SER B 77  ? 0.4448 0.4456 0.4666 -0.0134 -0.0057 0.0026  77  SER B N   
3053 C CA  . SER B 77  ? 0.4522 0.4522 0.4765 -0.0132 -0.0055 0.0010  77  SER B CA  
3054 C C   . SER B 77  ? 0.3823 0.3783 0.4020 -0.0133 -0.0061 -0.0039 77  SER B C   
3055 O O   . SER B 77  ? 0.3399 0.3335 0.3554 -0.0125 -0.0059 -0.0066 77  SER B O   
3056 C CB  . SER B 77  ? 0.4564 0.4552 0.4858 -0.0096 -0.0038 0.0007  77  SER B CB  
3057 O OG  . SER B 77  ? 0.4296 0.4316 0.4631 -0.0092 -0.0028 0.0057  77  SER B OG  
3058 N N   . THR B 78  ? 0.4074 0.4033 0.4286 -0.0141 -0.0067 -0.0045 78  THR B N   
3059 C CA  . THR B 78  ? 0.4180 0.4098 0.4358 -0.0137 -0.0070 -0.0084 78  THR B CA  
3060 C C   . THR B 78  ? 0.4253 0.4145 0.4461 -0.0102 -0.0061 -0.0111 78  THR B C   
3061 O O   . THR B 78  ? 0.4024 0.3931 0.4293 -0.0090 -0.0056 -0.0096 78  THR B O   
3062 C CB  . THR B 78  ? 0.4028 0.3960 0.4210 -0.0160 -0.0083 -0.0073 78  THR B CB  
3063 O OG1 . THR B 78  ? 0.4240 0.4199 0.4391 -0.0196 -0.0091 -0.0052 78  THR B OG1 
3064 C CG2 . THR B 78  ? 0.4084 0.3970 0.4228 -0.0155 -0.0086 -0.0107 78  THR B CG2 
3065 N N   . ILE B 79  ? 0.4007 0.3866 0.4175 -0.0087 -0.0056 -0.0147 79  ILE B N   
3066 C CA  . ILE B 79  ? 0.3947 0.3781 0.4130 -0.0058 -0.0048 -0.0179 79  ILE B CA  
3067 C C   . ILE B 79  ? 0.3795 0.3598 0.3937 -0.0063 -0.0053 -0.0205 79  ILE B C   
3068 O O   . ILE B 79  ? 0.3418 0.3213 0.3509 -0.0074 -0.0052 -0.0212 79  ILE B O   
3069 C CB  . ILE B 79  ? 0.4165 0.4000 0.4337 -0.0035 -0.0035 -0.0195 79  ILE B CB  
3070 C CG1 . ILE B 79  ? 0.4561 0.4425 0.4753 -0.0035 -0.0031 -0.0160 79  ILE B CG1 
3071 C CG2 . ILE B 79  ? 0.4221 0.4040 0.4420 -0.0008 -0.0025 -0.0224 79  ILE B CG2 
3072 C CD1 . ILE B 79  ? 0.4963 0.4833 0.5142 -0.0011 -0.0021 -0.0169 79  ILE B CD1 
3073 N N   . PHE B 80  ? 0.3595 0.3382 0.3763 -0.0055 -0.0058 -0.0215 80  PHE B N   
3074 C CA  . PHE B 80  ? 0.3480 0.3235 0.3614 -0.0059 -0.0065 -0.0232 80  PHE B CA  
3075 C C   . PHE B 80  ? 0.3510 0.3246 0.3677 -0.0040 -0.0066 -0.0252 80  PHE B C   
3076 O O   . PHE B 80  ? 0.3303 0.3050 0.3529 -0.0026 -0.0061 -0.0252 80  PHE B O   
3077 C CB  . PHE B 80  ? 0.3544 0.3301 0.3665 -0.0082 -0.0078 -0.0207 80  PHE B CB  
3078 C CG  . PHE B 80  ? 0.3491 0.3266 0.3675 -0.0080 -0.0088 -0.0185 80  PHE B CG  
3079 C CD1 . PHE B 80  ? 0.3202 0.3020 0.3439 -0.0083 -0.0085 -0.0158 80  PHE B CD1 
3080 C CD2 . PHE B 80  ? 0.3102 0.2857 0.3297 -0.0073 -0.0099 -0.0186 80  PHE B CD2 
3081 C CE1 . PHE B 80  ? 0.3317 0.3164 0.3624 -0.0080 -0.0090 -0.0133 80  PHE B CE1 
3082 C CE2 . PHE B 80  ? 0.3340 0.3120 0.3605 -0.0067 -0.0107 -0.0164 80  PHE B CE2 
3083 C CZ  . PHE B 80  ? 0.3618 0.3448 0.3942 -0.0071 -0.0101 -0.0137 80  PHE B CZ  
3084 N N   . VAL B 81  ? 0.3635 0.3343 0.3763 -0.0039 -0.0069 -0.0270 81  VAL B N   
3085 C CA  . VAL B 81  ? 0.3557 0.3242 0.3707 -0.0025 -0.0073 -0.0289 81  VAL B CA  
3086 C C   . VAL B 81  ? 0.3384 0.3058 0.3555 -0.0031 -0.0090 -0.0266 81  VAL B C   
3087 O O   . VAL B 81  ? 0.3268 0.2932 0.3397 -0.0045 -0.0096 -0.0248 81  VAL B O   
3088 C CB  . VAL B 81  ? 0.3138 0.2808 0.3235 -0.0023 -0.0066 -0.0315 81  VAL B CB  
3089 C CG1 . VAL B 81  ? 0.3173 0.2820 0.3284 -0.0014 -0.0073 -0.0334 81  VAL B CG1 
3090 C CG2 . VAL B 81  ? 0.2879 0.2573 0.2968 -0.0013 -0.0050 -0.0336 81  VAL B CG2 
3091 N N   . GLN B 82  ? 0.2923 0.2599 0.3162 -0.0017 -0.0095 -0.0265 82  GLN B N   
3092 C CA  . GLN B 82  ? 0.2938 0.2619 0.3221 -0.0016 -0.0111 -0.0238 82  GLN B CA  
3093 C C   . GLN B 82  ? 0.2807 0.2455 0.3040 -0.0021 -0.0125 -0.0230 82  GLN B C   
3094 O O   . GLN B 82  ? 0.2941 0.2595 0.3175 -0.0027 -0.0137 -0.0200 82  GLN B O   
3095 C CB  . GLN B 82  ? 0.2880 0.2564 0.3250 0.0004  -0.0109 -0.0246 82  GLN B CB  
3096 C CG  . GLN B 82  ? 0.2930 0.2637 0.3374 0.0010  -0.0121 -0.0213 82  GLN B CG  
3097 C CD  . GLN B 82  ? 0.3345 0.3050 0.3880 0.0031  -0.0116 -0.0225 82  GLN B CD  
3098 O OE1 . GLN B 82  ? 0.3535 0.3210 0.4061 0.0039  -0.0108 -0.0264 82  GLN B OE1 
3099 N NE2 . GLN B 82  ? 0.3391 0.3132 0.4016 0.0041  -0.0120 -0.0191 82  GLN B NE2 
3100 N N   . SER B 83  ? 0.2627 0.2243 0.2819 -0.0017 -0.0122 -0.0254 83  SER B N   
3101 C CA  . SER B 83  ? 0.2581 0.2162 0.2729 -0.0019 -0.0133 -0.0242 83  SER B CA  
3102 C C   . SER B 83  ? 0.2756 0.2328 0.2830 -0.0038 -0.0126 -0.0226 83  SER B C   
3103 O O   . SER B 83  ? 0.2801 0.2344 0.2840 -0.0041 -0.0132 -0.0207 83  SER B O   
3104 C CB  . SER B 83  ? 0.3016 0.2575 0.3147 -0.0012 -0.0130 -0.0269 83  SER B CB  
3105 O OG  . SER B 83  ? 0.3003 0.2569 0.3082 -0.0020 -0.0112 -0.0292 83  SER B OG  
3106 N N   . HIS B 84  ? 0.2904 0.2499 0.2959 -0.0050 -0.0113 -0.0230 84  HIS B N   
3107 C CA  . HIS B 84  ? 0.3062 0.2649 0.3053 -0.0070 -0.0102 -0.0218 84  HIS B CA  
3108 C C   . HIS B 84  ? 0.3123 0.2716 0.3117 -0.0083 -0.0113 -0.0190 84  HIS B C   
3109 O O   . HIS B 84  ? 0.3327 0.2909 0.3271 -0.0101 -0.0104 -0.0180 84  HIS B O   
3110 C CB  . HIS B 84  ? 0.3201 0.2811 0.3175 -0.0077 -0.0084 -0.0234 84  HIS B CB  
3111 C CG  . HIS B 84  ? 0.3168 0.2781 0.3130 -0.0066 -0.0071 -0.0260 84  HIS B CG  
3112 N ND1 . HIS B 84  ? 0.3079 0.2718 0.3029 -0.0067 -0.0054 -0.0273 84  HIS B ND1 
3113 C CD2 . HIS B 84  ? 0.3401 0.3001 0.3364 -0.0055 -0.0073 -0.0274 84  HIS B CD2 
3114 C CE1 . HIS B 84  ? 0.3178 0.2824 0.3121 -0.0056 -0.0045 -0.0294 84  HIS B CE1 
3115 N NE2 . HIS B 84  ? 0.2927 0.2551 0.2877 -0.0050 -0.0056 -0.0297 84  HIS B NE2 
3116 N N   . VAL B 85  ? 0.3138 0.2754 0.3196 -0.0073 -0.0129 -0.0177 85  VAL B N   
3117 C CA  . VAL B 85  ? 0.3078 0.2720 0.3155 -0.0083 -0.0141 -0.0148 85  VAL B CA  
3118 C C   . VAL B 85  ? 0.2861 0.2498 0.2983 -0.0064 -0.0160 -0.0127 85  VAL B C   
3119 O O   . VAL B 85  ? 0.3033 0.2699 0.3236 -0.0047 -0.0168 -0.0124 85  VAL B O   
3120 C CB  . VAL B 85  ? 0.3105 0.2802 0.3234 -0.0089 -0.0139 -0.0143 85  VAL B CB  
3121 C CG1 . VAL B 85  ? 0.3071 0.2811 0.3226 -0.0101 -0.0151 -0.0111 85  VAL B CG1 
3122 C CG2 . VAL B 85  ? 0.3007 0.2708 0.3094 -0.0104 -0.0123 -0.0160 85  VAL B CG2 
3123 N N   . PRO B 86  ? 0.2976 0.2577 0.3052 -0.0065 -0.0166 -0.0111 86  PRO B N   
3124 C CA  . PRO B 86  ? 0.2857 0.2451 0.2975 -0.0043 -0.0186 -0.0087 86  PRO B CA  
3125 C C   . PRO B 86  ? 0.2738 0.2391 0.2940 -0.0034 -0.0201 -0.0062 86  PRO B C   
3126 O O   . PRO B 86  ? 0.2299 0.1957 0.2563 -0.0009 -0.0217 -0.0045 86  PRO B O   
3127 C CB  . PRO B 86  ? 0.3044 0.2593 0.3086 -0.0051 -0.0185 -0.0068 86  PRO B CB  
3128 C CG  . PRO B 86  ? 0.2950 0.2470 0.2916 -0.0071 -0.0161 -0.0090 86  PRO B CG  
3129 C CD  . PRO B 86  ? 0.3054 0.2618 0.3042 -0.0085 -0.0152 -0.0110 86  PRO B CD  
3130 N N   . GLU B 87  ? 0.2586 0.2288 0.2794 -0.0054 -0.0196 -0.0056 87  GLU B N   
3131 C CA  . GLU B 87  ? 0.2797 0.2570 0.3083 -0.0050 -0.0207 -0.0025 87  GLU B CA  
3132 C C   . GLU B 87  ? 0.2347 0.2157 0.2744 -0.0025 -0.0209 -0.0021 87  GLU B C   
3133 O O   . GLU B 87  ? 0.2472 0.2333 0.2949 -0.0011 -0.0220 0.0011  87  GLU B O   
3134 C CB  . GLU B 87  ? 0.2881 0.2704 0.3148 -0.0082 -0.0199 -0.0020 87  GLU B CB  
3135 C CG  . GLU B 87  ? 0.3137 0.2941 0.3318 -0.0107 -0.0200 -0.0016 87  GLU B CG  
3136 C CD  . GLU B 87  ? 0.3374 0.3113 0.3459 -0.0124 -0.0183 -0.0046 87  GLU B CD  
3137 O OE1 . GLU B 87  ? 0.3524 0.3228 0.3600 -0.0115 -0.0173 -0.0070 87  GLU B OE1 
3138 O OE2 . GLU B 87  ? 0.4548 0.4275 0.4567 -0.0149 -0.0177 -0.0046 87  GLU B OE2 
3139 N N   . HIS B 88  ? 0.2690 0.2476 0.3094 -0.0020 -0.0195 -0.0052 88  HIS B N   
3140 C CA  . HIS B 88  ? 0.2482 0.2288 0.2985 0.0002  -0.0191 -0.0056 88  HIS B CA  
3141 C C   . HIS B 88  ? 0.2830 0.2620 0.3388 0.0031  -0.0206 -0.0046 88  HIS B C   
3142 O O   . HIS B 88  ? 0.3165 0.3005 0.3834 0.0050  -0.0209 -0.0021 88  HIS B O   
3143 C CB  . HIS B 88  ? 0.2964 0.2737 0.3442 0.0000  -0.0172 -0.0098 88  HIS B CB  
3144 C CG  . HIS B 88  ? 0.2999 0.2801 0.3454 -0.0021 -0.0156 -0.0101 88  HIS B CG  
3145 N ND1 . HIS B 88  ? 0.3245 0.3084 0.3769 -0.0016 -0.0140 -0.0098 88  HIS B ND1 
3146 C CD2 . HIS B 88  ? 0.3108 0.2905 0.3482 -0.0045 -0.0153 -0.0103 88  HIS B CD2 
3147 C CE1 . HIS B 88  ? 0.3296 0.3154 0.3781 -0.0037 -0.0130 -0.0096 88  HIS B CE1 
3148 N NE2 . HIS B 88  ? 0.3237 0.3071 0.3632 -0.0055 -0.0139 -0.0100 88  HIS B NE2 
3149 N N   . ALA B 89  ? 0.3201 0.2926 0.3690 0.0034  -0.0216 -0.0059 89  ALA B N   
3150 C CA  . ALA B 89  ? 0.2740 0.2441 0.3271 0.0061  -0.0234 -0.0045 89  ALA B CA  
3151 C C   . ALA B 89  ? 0.2963 0.2702 0.3526 0.0072  -0.0253 0.0004  89  ALA B C   
3152 O O   . ALA B 89  ? 0.2527 0.2291 0.3184 0.0099  -0.0267 0.0029  89  ALA B O   
3153 C CB  . ALA B 89  ? 0.2966 0.2594 0.3408 0.0058  -0.0237 -0.0065 89  ALA B CB  
3154 N N   . GLN B 90  ? 0.2550 0.2295 0.3041 0.0050  -0.0253 0.0017  90  GLN B N   
3155 C CA  . GLN B 90  ? 0.2845 0.2626 0.3351 0.0057  -0.0270 0.0060  90  GLN B CA  
3156 C C   . GLN B 90  ? 0.2906 0.2786 0.3536 0.0068  -0.0272 0.0089  90  GLN B C   
3157 O O   . GLN B 90  ? 0.3342 0.3258 0.4053 0.0097  -0.0288 0.0124  90  GLN B O   
3158 C CB  . GLN B 90  ? 0.3106 0.2876 0.3508 0.0026  -0.0264 0.0059  90  GLN B CB  
3159 C CG  . GLN B 90  ? 0.3022 0.2703 0.3310 0.0017  -0.0259 0.0044  90  GLN B CG  
3160 C CD  . GLN B 90  ? 0.2956 0.2627 0.3151 -0.0015 -0.0247 0.0040  90  GLN B CD  
3161 O OE1 . GLN B 90  ? 0.3583 0.3256 0.3741 -0.0041 -0.0229 0.0012  90  GLN B OE1 
3162 N NE2 . GLN B 90  ? 0.2934 0.2595 0.3093 -0.0014 -0.0255 0.0068  90  GLN B NE2 
3163 N N   . LEU B 91  ? 0.3011 0.2938 0.3663 0.0048  -0.0254 0.0079  91  LEU B N   
3164 C CA  . LEU B 91  ? 0.3069 0.3097 0.3841 0.0055  -0.0249 0.0112  91  LEU B CA  
3165 C C   . LEU B 91  ? 0.2742 0.2782 0.3635 0.0089  -0.0246 0.0116  91  LEU B C   
3166 O O   . LEU B 91  ? 0.2635 0.2752 0.3647 0.0110  -0.0250 0.0156  91  LEU B O   
3167 C CB  . LEU B 91  ? 0.3249 0.3321 0.4012 0.0024  -0.0228 0.0105  91  LEU B CB  
3168 C CG  . LEU B 91  ? 0.3290 0.3478 0.4180 0.0027  -0.0219 0.0148  91  LEU B CG  
3169 C CD1 . LEU B 91  ? 0.3394 0.3658 0.4326 0.0034  -0.0237 0.0195  91  LEU B CD1 
3170 C CD2 . LEU B 91  ? 0.3562 0.3785 0.4426 -0.0007 -0.0199 0.0146  91  LEU B CD2 
3171 N N   . GLY B 92  ? 0.2544 0.2512 0.3413 0.0092  -0.0237 0.0074  92  GLY B N   
3172 C CA  . GLY B 92  ? 0.2893 0.2856 0.3866 0.0120  -0.0232 0.0066  92  GLY B CA  
3173 C C   . GLY B 92  ? 0.3103 0.3073 0.4144 0.0154  -0.0256 0.0097  92  GLY B C   
3174 O O   . GLY B 92  ? 0.3532 0.3553 0.4709 0.0179  -0.0251 0.0118  92  GLY B O   
3175 N N   . TRP B 93  ? 0.3194 0.3111 0.4148 0.0156  -0.0279 0.0102  93  TRP B N   
3176 C CA  . TRP B 93  ? 0.3493 0.3415 0.4505 0.0190  -0.0304 0.0140  93  TRP B CA  
3177 C C   . TRP B 93  ? 0.3614 0.3645 0.4729 0.0205  -0.0310 0.0195  93  TRP B C   
3178 O O   . TRP B 93  ? 0.3374 0.3457 0.4624 0.0239  -0.0316 0.0225  93  TRP B O   
3179 C CB  . TRP B 93  ? 0.3412 0.3259 0.4305 0.0190  -0.0326 0.0146  93  TRP B CB  
3180 C CG  . TRP B 93  ? 0.3408 0.3282 0.4373 0.0226  -0.0352 0.0197  93  TRP B CG  
3181 C CD1 . TRP B 93  ? 0.3316 0.3237 0.4276 0.0233  -0.0366 0.0240  93  TRP B CD1 
3182 C CD2 . TRP B 93  ? 0.3316 0.3191 0.4391 0.0264  -0.0365 0.0212  93  TRP B CD2 
3183 N NE1 . TRP B 93  ? 0.3200 0.3150 0.4257 0.0276  -0.0389 0.0285  93  TRP B NE1 
3184 C CE2 . TRP B 93  ? 0.3519 0.3440 0.4650 0.0295  -0.0389 0.0269  93  TRP B CE2 
3185 C CE3 . TRP B 93  ? 0.3820 0.3659 0.4948 0.0273  -0.0360 0.0181  93  TRP B CE3 
3186 C CZ2 . TRP B 93  ? 0.3717 0.3650 0.4961 0.0338  -0.0409 0.0300  93  TRP B CZ2 
3187 C CZ3 . TRP B 93  ? 0.3615 0.3463 0.4855 0.0313  -0.0379 0.0208  93  TRP B CZ3 
3188 C CH2 . TRP B 93  ? 0.3867 0.3762 0.5166 0.0346  -0.0403 0.0269  93  TRP B CH2 
3189 N N   . ALA B 94  ? 0.3658 0.3725 0.4708 0.0180  -0.0309 0.0207  94  ALA B N   
3190 C CA  . ALA B 94  ? 0.3871 0.4054 0.5007 0.0188  -0.0313 0.0258  94  ALA B CA  
3191 C C   . ALA B 94  ? 0.3665 0.3943 0.4960 0.0199  -0.0292 0.0277  94  ALA B C   
3192 O O   . ALA B 94  ? 0.4172 0.4540 0.5593 0.0227  -0.0297 0.0325  94  ALA B O   
3193 C CB  . ALA B 94  ? 0.4203 0.4409 0.5238 0.0149  -0.0310 0.0259  94  ALA B CB  
3194 N N   . LEU B 95  ? 0.3915 0.4171 0.5206 0.0180  -0.0265 0.0242  95  LEU B N   
3195 C CA  . LEU B 95  ? 0.3929 0.4265 0.5363 0.0187  -0.0237 0.0259  95  LEU B CA  
3196 C C   . LEU B 95  ? 0.3854 0.4179 0.5417 0.0226  -0.0232 0.0258  95  LEU B C   
3197 O O   . LEU B 95  ? 0.4110 0.4520 0.5825 0.0242  -0.0210 0.0289  95  LEU B O   
3198 C CB  . LEU B 95  ? 0.4087 0.4399 0.5464 0.0153  -0.0209 0.0224  95  LEU B CB  
3199 C CG  . LEU B 95  ? 0.4262 0.4614 0.5556 0.0114  -0.0205 0.0233  95  LEU B CG  
3200 C CD1 . LEU B 95  ? 0.4395 0.4743 0.5685 0.0092  -0.0173 0.0212  95  LEU B CD1 
3201 C CD2 . LEU B 95  ? 0.4035 0.4517 0.5409 0.0113  -0.0209 0.0294  95  LEU B CD2 
3202 N N   . ASN B 96  ? 0.3732 0.3958 0.5239 0.0240  -0.0252 0.0227  96  ASN B N   
3203 C CA  . ASN B 96  ? 0.4045 0.4263 0.5672 0.0278  -0.0256 0.0233  96  ASN B CA  
3204 C C   . ASN B 96  ? 0.3881 0.4203 0.5650 0.0314  -0.0269 0.0300  96  ASN B C   
3205 O O   . ASN B 96  ? 0.4065 0.4423 0.5949 0.0332  -0.0249 0.0312  96  ASN B O   
3206 C CB  . ASN B 96  ? 0.4243 0.4345 0.5773 0.0285  -0.0283 0.0200  96  ASN B CB  
3207 C CG  . ASN B 96  ? 0.4607 0.4630 0.6112 0.0274  -0.0265 0.0139  96  ASN B CG  
3208 O OD1 . ASN B 96  ? 0.4557 0.4607 0.6144 0.0272  -0.0234 0.0123  96  ASN B OD1 
3209 N ND2 . ASN B 96  ? 0.5242 0.5168 0.6634 0.0268  -0.0284 0.0108  96  ASN B ND2 
3210 N N   . CYS B 97  ? 0.3904 0.4262 0.5618 0.0313  -0.0293 0.0335  97  CYS B N   
3211 C CA  . CYS B 97  ? 0.4100 0.4529 0.5833 0.0323  -0.0291 0.0379  97  CYS B CA  
3212 C C   . CYS B 97  ? 0.4480 0.5029 0.6288 0.0310  -0.0257 0.0412  97  CYS B C   
3213 O O   . CYS B 97  ? 0.4651 0.5245 0.6438 0.0311  -0.0246 0.0436  97  CYS B O   
3214 C CB  . CYS B 97  ? 0.4285 0.4698 0.5908 0.0323  -0.0324 0.0397  97  CYS B CB  
3215 S SG  . CYS B 97  ? 0.3851 0.4112 0.5356 0.0334  -0.0360 0.0368  97  CYS B SG  
3216 N N   . TYR B 98  ? 0.4364 0.4962 0.6249 0.0297  -0.0239 0.0412  98  TYR B N   
3217 C CA  . TYR B 98  ? 0.4438 0.5141 0.6392 0.0281  -0.0201 0.0444  98  TYR B CA  
3218 C C   . TYR B 98  ? 0.4512 0.5204 0.6561 0.0282  -0.0162 0.0426  98  TYR B C   
3219 O O   . TYR B 98  ? 0.4729 0.5494 0.6837 0.0266  -0.0128 0.0449  98  TYR B O   
3220 C CB  . TYR B 98  ? 0.4242 0.5031 0.6190 0.0256  -0.0210 0.0470  98  TYR B CB  
3221 C CG  . TYR B 98  ? 0.4040 0.4842 0.5897 0.0254  -0.0246 0.0487  98  TYR B CG  
3222 C CD1 . TYR B 98  ? 0.4074 0.4946 0.5905 0.0249  -0.0235 0.0519  98  TYR B CD1 
3223 C CD2 . TYR B 98  ? 0.3999 0.4698 0.5717 0.0244  -0.0276 0.0451  98  TYR B CD2 
3224 C CE1 . TYR B 98  ? 0.4112 0.4994 0.5861 0.0248  -0.0264 0.0530  98  TYR B CE1 
3225 C CE2 . TYR B 98  ? 0.4246 0.4952 0.5883 0.0243  -0.0305 0.0468  98  TYR B CE2 
3226 C CZ  . TYR B 98  ? 0.4099 0.4914 0.5786 0.0251  -0.0305 0.0516  98  TYR B CZ  
3227 O OH  . TYR B 98  ? 0.4783 0.5603 0.6386 0.0250  -0.0330 0.0529  98  TYR B OH  
3228 N N   . THR B 99  ? 0.4880 0.5476 0.6938 0.0299  -0.0166 0.0384  99  THR B N   
3229 C CA  . THR B 99  ? 0.5110 0.5680 0.7255 0.0302  -0.0129 0.0357  99  THR B CA  
3230 C C   . THR B 99  ? 0.5744 0.6265 0.7890 0.0313  -0.0123 0.0347  99  THR B C   
3231 O O   . THR B 99  ? 0.6130 0.6588 0.8208 0.0323  -0.0156 0.0330  99  THR B O   
3232 C CB  . THR B 99  ? 0.4999 0.5470 0.7096 0.0299  -0.0138 0.0296  99  THR B CB  
3233 O OG1 . THR B 99  ? 0.5294 0.5762 0.7256 0.0259  -0.0137 0.0288  99  THR B OG1 
3234 C CG2 . THR B 99  ? 0.4970 0.5407 0.7146 0.0301  -0.0096 0.0261  99  THR B CG2 
3235 N N   . TYR B 100 ? 0.5910 0.6460 0.8131 0.0309  -0.0081 0.0359  100 TYR B N   
3236 C CA  . TYR B 100 ? 0.6315 0.6828 0.8550 0.0315  -0.0073 0.0351  100 TYR B CA  
3237 C C   . TYR B 100 ? 0.6200 0.6631 0.8483 0.0322  -0.0066 0.0296  100 TYR B C   
3238 O O   . TYR B 100 ? 0.5793 0.6210 0.8125 0.0321  -0.0047 0.0269  100 TYR B O   
3239 C CB  . TYR B 100 ? 0.6816 0.7392 0.9109 0.0307  -0.0032 0.0390  100 TYR B CB  
3240 C CG  . TYR B 100 ? 0.7127 0.7781 0.9372 0.0301  -0.0037 0.0439  100 TYR B CG  
3241 C CD1 . TYR B 100 ? 0.7760 0.8416 0.9960 0.0307  -0.0048 0.0453  100 TYR B CD1 
3242 C CD2 . TYR B 100 ? 0.7463 0.8191 0.9708 0.0288  -0.0028 0.0469  100 TYR B CD2 
3243 C CE1 . TYR B 100 ? 0.7881 0.8605 1.0037 0.0303  -0.0050 0.0490  100 TYR B CE1 
3244 C CE2 . TYR B 100 ? 0.7704 0.8502 0.9904 0.0282  -0.0032 0.0509  100 TYR B CE2 
3245 C CZ  . TYR B 100 ? 0.7951 0.8745 1.0108 0.0291  -0.0043 0.0517  100 TYR B CZ  
3246 O OH  . TYR B 100 ? 0.7897 0.8758 1.0010 0.0286  -0.0046 0.0549  100 TYR B OH  
3247 N N   . PHE B 101 ? 0.6861 0.7241 0.9127 0.0328  -0.0080 0.0279  101 PHE B N   
3248 C CA  . PHE B 101 ? 0.6699 0.7001 0.9006 0.0333  -0.0075 0.0224  101 PHE B CA  
3249 C C   . PHE B 101 ? 0.6109 0.6425 0.8530 0.0326  -0.0022 0.0214  101 PHE B C   
3250 O O   . PHE B 101 ? 0.6329 0.6593 0.8788 0.0330  -0.0008 0.0161  101 PHE B O   
3251 C CB  . PHE B 101 ? 0.6942 0.7209 0.9213 0.0335  -0.0098 0.0223  101 PHE B CB  
3252 C CG  . PHE B 101 ? 0.7567 0.7758 0.9872 0.0338  -0.0099 0.0167  101 PHE B CG  
3253 C CD1 . PHE B 101 ? 0.7685 0.7805 0.9909 0.0344  -0.0141 0.0137  101 PHE B CD1 
3254 C CD2 . PHE B 101 ? 0.7812 0.8001 1.0224 0.0332  -0.0058 0.0147  101 PHE B CD2 
3255 C CE1 . PHE B 101 ? 0.8219 0.8272 1.0470 0.0344  -0.0144 0.0084  101 PHE B CE1 
3256 C CE2 . PHE B 101 ? 0.8084 0.8205 1.0528 0.0333  -0.0059 0.0091  101 PHE B CE2 
3257 C CZ  . PHE B 101 ? 0.8325 0.8380 1.0687 0.0338  -0.0103 0.0059  101 PHE B CZ  
3258 N N   . GLY B 102 ? 0.5986 0.6366 0.8452 0.0318  0.0010  0.0261  102 GLY B N   
3259 C CA  . GLY B 102 ? 0.5688 0.6081 0.8258 0.0310  0.0065  0.0262  102 GLY B CA  
3260 C C   . GLY B 102 ? 0.5896 0.6297 0.8497 0.0308  0.0092  0.0247  102 GLY B C   
3261 O O   . GLY B 102 ? 0.5704 0.6066 0.8372 0.0308  0.0127  0.0207  102 GLY B O   
3262 N N   . GLU B 103 ? 0.6083 0.6534 0.8634 0.0306  0.0075  0.0277  103 GLU B N   
3263 C CA  . GLU B 103 ? 0.5890 0.6357 0.8461 0.0302  0.0096  0.0268  103 GLU B CA  
3264 C C   . GLU B 103 ? 0.6153 0.6533 0.8722 0.0315  0.0089  0.0191  103 GLU B C   
3265 O O   . GLU B 103 ? 0.6970 0.7337 0.9581 0.0315  0.0126  0.0166  103 GLU B O   
3266 C CB  . GLU B 103 ? 0.6279 0.6814 0.8788 0.0296  0.0069  0.0308  103 GLU B CB  
3267 C CG  . GLU B 103 ? 0.6393 0.7016 0.8898 0.0282  0.0085  0.0378  103 GLU B CG  
3268 C CD  . GLU B 103 ? 0.6455 0.7143 0.8888 0.0274  0.0052  0.0413  103 GLU B CD  
3269 O OE1 . GLU B 103 ? 0.6390 0.7048 0.8764 0.0281  0.0008  0.0388  103 GLU B OE1 
3270 O OE2 . GLU B 103 ? 0.5875 0.6642 0.8306 0.0260  0.0070  0.0465  103 GLU B OE2 
3271 N N   . LEU B 104 ? 0.5665 0.5977 0.8172 0.0327  0.0043  0.0153  104 LEU B N   
3272 C CA  . LEU B 104 ? 0.5340 0.5547 0.7797 0.0335  0.0030  0.0075  104 LEU B CA  
3273 C C   . LEU B 104 ? 0.5605 0.5748 0.8131 0.0341  0.0059  0.0020  104 LEU B C   
3274 O O   . LEU B 104 ? 0.5758 0.5824 0.8209 0.0322  0.0078  -0.0043 104 LEU B O   
3275 C CB  . LEU B 104 ? 0.5045 0.5198 0.7361 0.0333  -0.0032 0.0063  104 LEU B CB  
3276 C CG  . LEU B 104 ? 0.4873 0.5069 0.7084 0.0317  -0.0059 0.0103  104 LEU B CG  
3277 C CD1 . LEU B 104 ? 0.4939 0.5076 0.7016 0.0317  -0.0114 0.0093  104 LEU B CD1 
3278 C CD2 . LEU B 104 ? 0.4884 0.5066 0.6988 0.0283  -0.0036 0.0082  104 LEU B CD2 
3279 N N   . SER B 105 ? 0.6303 0.6465 0.8869 0.0334  0.0061  0.0043  105 SER B N   
3280 C CA  . SER B 105 ? 0.6819 0.6927 0.9445 0.0331  0.0087  -0.0005 105 SER B CA  
3281 C C   . SER B 105 ? 0.7064 0.7172 0.9777 0.0326  0.0154  -0.0026 105 SER B C   
3282 O O   . SER B 105 ? 0.6901 0.6935 0.9628 0.0326  0.0175  -0.0096 105 SER B O   
3283 C CB  . SER B 105 ? 0.6518 0.6658 0.9175 0.0324  0.0079  0.0035  105 SER B CB  
3284 O OG  . SER B 105 ? 0.6943 0.7165 0.9645 0.0315  0.0107  0.0104  105 SER B OG  
3285 N N   . ARG B 106 ? 0.7251 0.7437 1.0007 0.0319  0.0187  0.0035  106 ARG B N   
3286 C CA  . ARG B 106 ? 0.8131 0.8327 1.0968 0.0311  0.0255  0.0035  106 ARG B CA  
3287 C C   . ARG B 106 ? 0.8032 0.8185 1.0845 0.0319  0.0280  -0.0014 106 ARG B C   
3288 O O   . ARG B 106 ? 0.7819 0.7972 1.0689 0.0313  0.0339  -0.0016 106 ARG B O   
3289 C CB  . ARG B 106 ? 0.8651 0.8942 1.1524 0.0298  0.0280  0.0127  106 ARG B CB  
3290 C CG  . ARG B 106 ? 0.9245 0.9600 1.2057 0.0298  0.0256  0.0172  106 ARG B CG  
3291 C CD  . ARG B 106 ? 0.9609 1.0049 1.2447 0.0283  0.0287  0.0255  106 ARG B CD  
3292 N NE  . ARG B 106 ? 0.9664 1.0138 1.2492 0.0279  0.0270  0.0304  106 ARG B NE  
3293 C CZ  . ARG B 106 ? 0.9142 0.9691 1.1931 0.0273  0.0260  0.0371  106 ARG B CZ  
3294 N NH1 . ARG B 106 ? 0.9057 0.9663 1.1816 0.0265  0.0263  0.0403  106 ARG B NH1 
3295 N NH2 . ARG B 106 ? 0.9265 0.9832 1.2040 0.0273  0.0246  0.0403  106 ARG B NH2 
3296 N N   . MET B 107 ? 0.7928 0.8029 1.0592 0.0314  0.0232  -0.0050 107 MET B N   
3297 C CA  . MET B 107 ? 0.7834 0.7885 1.0341 0.0286  0.0238  -0.0084 107 MET B CA  
3298 C C   . MET B 107 ? 0.8678 0.8631 1.1148 0.0277  0.0268  -0.0167 107 MET B C   
3299 O O   . MET B 107 ? 0.9525 0.9407 1.1954 0.0277  0.0244  -0.0228 107 MET B O   
3300 C CB  . MET B 107 ? 0.7675 0.7697 0.9993 0.0269  0.0175  -0.0094 107 MET B CB  
3301 C CG  . MET B 107 ? 0.7195 0.7311 0.9521 0.0270  0.0151  -0.0016 107 MET B CG  
3302 S SD  . MET B 107 ? 0.6568 0.6761 0.8907 0.0253  0.0192  0.0042  107 MET B SD  
3303 C CE  . MET B 107 ? 0.6014 0.6336 0.8425 0.0261  0.0167  0.0133  107 MET B CE  
3304 N N   . THR B 108 ? 0.8445 0.8398 1.0928 0.0268  0.0321  -0.0166 108 THR B N   
3305 C CA  . THR B 108 ? 0.8662 0.8530 1.1115 0.0260  0.0359  -0.0240 108 THR B CA  
3306 C C   . THR B 108 ? 0.8960 0.8739 1.1219 0.0241  0.0317  -0.0318 108 THR B C   
3307 O O   . THR B 108 ? 0.9521 0.9230 1.1766 0.0238  0.0324  -0.0391 108 THR B O   
3308 C CB  . THR B 108 ? 0.8663 0.8552 1.1145 0.0255  0.0419  -0.0210 108 THR B CB  
3309 O OG1 . THR B 108 ? 0.8935 0.8897 1.1623 0.0273  0.0474  -0.0150 108 THR B OG1 
3310 C CG2 . THR B 108 ? 0.8687 0.8481 1.1087 0.0244  0.0450  -0.0291 108 THR B CG2 
3311 N N   . GLN B 109 ? 0.8654 0.8439 1.0766 0.0227  0.0279  -0.0303 109 GLN B N   
3312 C CA  . GLN B 109 ? 0.8570 0.8284 1.0503 0.0209  0.0241  -0.0368 109 GLN B CA  
3313 C C   . GLN B 109 ? 0.7802 0.7480 0.9721 0.0211  0.0199  -0.0406 109 GLN B C   
3314 O O   . GLN B 109 ? 0.7591 0.7203 0.9443 0.0201  0.0195  -0.0477 109 GLN B O   
3315 C CB  . GLN B 109 ? 0.8663 0.8398 1.0458 0.0195  0.0207  -0.0339 109 GLN B CB  
3316 C CG  . GLN B 109 ? 0.8703 0.8376 1.0325 0.0178  0.0167  -0.0398 109 GLN B CG  
3317 C CD  . GLN B 109 ? 0.8716 0.8410 1.0215 0.0166  0.0131  -0.0367 109 GLN B CD  
3318 O OE1 . GLN B 109 ? 0.8833 0.8558 1.0314 0.0161  0.0148  -0.0333 109 GLN B OE1 
3319 N NE2 . GLN B 109 ? 0.7948 0.7622 0.9359 0.0159  0.0083  -0.0378 109 GLN B NE2 
3320 N N   . PHE B 110 ? 0.7199 0.6922 0.9183 0.0225  0.0169  -0.0355 110 PHE B N   
3321 C CA  . PHE B 110 ? 0.7743 0.7433 0.9726 0.0230  0.0129  -0.0380 110 PHE B CA  
3322 C C   . PHE B 110 ? 0.7903 0.7547 0.9975 0.0234  0.0159  -0.0439 110 PHE B C   
3323 O O   . PHE B 110 ? 0.7082 0.6663 0.9073 0.0222  0.0137  -0.0501 110 PHE B O   
3324 C CB  . PHE B 110 ? 0.7455 0.7208 0.9527 0.0251  0.0100  -0.0310 110 PHE B CB  
3325 C CG  . PHE B 110 ? 0.7870 0.7588 0.9949 0.0260  0.0060  -0.0329 110 PHE B CG  
3326 C CD1 . PHE B 110 ? 0.7670 0.7333 0.9588 0.0244  0.0013  -0.0359 110 PHE B CD1 
3327 C CD2 . PHE B 110 ? 0.7666 0.7406 0.9915 0.0285  0.0072  -0.0314 110 PHE B CD2 
3328 C CE1 . PHE B 110 ? 0.7230 0.6860 0.9151 0.0251  -0.0023 -0.0370 110 PHE B CE1 
3329 C CE2 . PHE B 110 ? 0.7446 0.7152 0.9701 0.0294  0.0033  -0.0328 110 PHE B CE2 
3330 C CZ  . PHE B 110 ? 0.7382 0.7032 0.9469 0.0276  -0.0016 -0.0355 110 PHE B CZ  
3331 N N   . LYS B 111 ? 0.7946 0.7625 1.0185 0.0250  0.0212  -0.0417 111 LYS B N   
3332 C CA  . LYS B 111 ? 0.8075 0.7712 1.0417 0.0254  0.0252  -0.0471 111 LYS B CA  
3333 C C   . LYS B 111 ? 0.8399 0.7956 1.0621 0.0230  0.0268  -0.0560 111 LYS B C   
3334 O O   . LYS B 111 ? 0.8375 0.7875 1.0566 0.0220  0.0254  -0.0626 111 LYS B O   
3335 C CB  . LYS B 111 ? 0.7680 0.7373 1.0216 0.0273  0.0318  -0.0426 111 LYS B CB  
3336 N N   . ASP B 112 ? 0.8646 0.8206 1.0801 0.0221  0.0296  -0.0557 112 ASP B N   
3337 C CA  . ASP B 112 ? 0.9069 0.8565 1.1112 0.0202  0.0316  -0.0633 112 ASP B CA  
3338 C C   . ASP B 112 ? 0.8973 0.8428 1.0839 0.0181  0.0260  -0.0684 112 ASP B C   
3339 O O   . ASP B 112 ? 0.8593 0.7994 1.0404 0.0166  0.0265  -0.0761 112 ASP B O   
3340 C CB  . ASP B 112 ? 0.9182 0.8698 1.1192 0.0201  0.0351  -0.0603 112 ASP B CB  
3341 N N   . LYS B 113 ? 0.8956 0.8440 1.0737 0.0180  0.0209  -0.0638 113 LYS B N   
3342 C CA  . LYS B 113 ? 0.8770 0.8226 1.0398 0.0162  0.0156  -0.0669 113 LYS B CA  
3343 C C   . LYS B 113 ? 0.8516 0.7940 1.0168 0.0159  0.0129  -0.0704 113 LYS B C   
3344 O O   . LYS B 113 ? 0.8168 0.7551 0.9723 0.0139  0.0114  -0.0767 113 LYS B O   
3345 C CB  . LYS B 113 ? 0.8607 0.8104 1.0168 0.0165  0.0114  -0.0603 113 LYS B CB  
3346 C CG  . LYS B 113 ? 0.8908 0.8435 1.0410 0.0161  0.0127  -0.0570 113 LYS B CG  
3347 C CD  . LYS B 113 ? 0.9048 0.8541 1.0406 0.0144  0.0126  -0.0623 113 LYS B CD  
3348 C CE  . LYS B 113 ? 0.9316 0.8839 1.0619 0.0143  0.0137  -0.0586 113 LYS B CE  
3349 N NZ  . LYS B 113 ? 0.9046 0.8543 1.0223 0.0130  0.0138  -0.0637 113 LYS B NZ  
3350 N N   . SER B 114 ? 0.8493 0.7943 1.0276 0.0179  0.0122  -0.0660 114 SER B N   
3351 C CA  . SER B 114 ? 0.8700 0.8125 1.0528 0.0181  0.0094  -0.0679 114 SER B CA  
3352 C C   . SER B 114 ? 0.8665 0.8037 1.0521 0.0167  0.0123  -0.0764 114 SER B C   
3353 O O   . SER B 114 ? 0.8594 0.7929 1.0386 0.0150  0.0093  -0.0809 114 SER B O   
3354 C CB  . SER B 114 ? 0.8545 0.8017 1.0543 0.0212  0.0092  -0.0613 114 SER B CB  
3355 O OG  . SER B 114 ? 0.8793 0.8314 1.0763 0.0223  0.0060  -0.0537 114 SER B OG  
3356 N N   . ALA B 115 ? 0.8916 0.8287 1.0867 0.0173  0.0183  -0.0782 115 ALA B N   
3357 C CA  . ALA B 115 ? 0.8860 0.8180 1.0850 0.0160  0.0221  -0.0865 115 ALA B CA  
3358 C C   . ALA B 115 ? 0.8733 0.8012 1.0550 0.0129  0.0212  -0.0940 115 ALA B C   
3359 O O   . ALA B 115 ? 0.8840 0.8077 1.0633 0.0110  0.0209  -0.1012 115 ALA B O   
3360 C CB  . ALA B 115 ? 0.8798 0.8129 1.0923 0.0174  0.0294  -0.0859 115 ALA B CB  
3361 N N   . ARG B 116 ? 0.8772 0.8070 1.0472 0.0125  0.0205  -0.0920 116 ARG B N   
3362 C CA  . ARG B 116 ? 0.9310 0.8585 1.0852 0.0101  0.0199  -0.0980 116 ARG B CA  
3363 C C   . ARG B 116 ? 0.9267 0.8540 1.0684 0.0082  0.0139  -0.0989 116 ARG B C   
3364 O O   . ARG B 116 ? 0.9396 0.8645 1.0725 0.0058  0.0133  -0.1056 116 ARG B O   
3365 C CB  . ARG B 116 ? 0.9713 0.9015 1.1191 0.0108  0.0215  -0.0945 116 ARG B CB  
3366 C CG  . ARG B 116 ? 0.9901 0.9198 1.1215 0.0089  0.0201  -0.0986 116 ARG B CG  
3367 C CD  . ARG B 116 ? 0.9875 0.9189 1.1162 0.0100  0.0233  -0.0965 116 ARG B CD  
3368 N NE  . ARG B 116 ? 1.0295 0.9595 1.1467 0.0086  0.0241  -0.1029 116 ARG B NE  
3369 C CZ  . ARG B 116 ? 1.0058 0.9382 1.1121 0.0086  0.0231  -0.1016 116 ARG B CZ  
3370 N NH1 . ARG B 116 ? 0.9948 0.9306 1.0995 0.0096  0.0213  -0.0943 116 ARG B NH1 
3371 N NH2 . ARG B 116 ? 1.0299 0.9616 1.1272 0.0075  0.0240  -0.1077 116 ARG B NH2 
3372 N N   . TYR B 117 ? 0.9180 0.8481 1.0588 0.0093  0.0097  -0.0918 117 TYR B N   
3373 C CA  . TYR B 117 ? 0.8834 0.8132 1.0143 0.0079  0.0042  -0.0910 117 TYR B CA  
3374 C C   . TYR B 117 ? 0.8489 0.7783 0.9904 0.0092  0.0016  -0.0876 117 TYR B C   
3375 O O   . TYR B 117 ? 0.8429 0.7748 0.9863 0.0110  -0.0013 -0.0805 117 TYR B O   
3376 C CB  . TYR B 117 ? 0.8634 0.7963 0.9832 0.0079  0.0015  -0.0857 117 TYR B CB  
3377 C CG  . TYR B 117 ? 0.8515 0.7856 0.9633 0.0073  0.0042  -0.0879 117 TYR B CG  
3378 C CD1 . TYR B 117 ? 0.8504 0.7836 0.9513 0.0050  0.0043  -0.0941 117 TYR B CD1 
3379 C CD2 . TYR B 117 ? 0.8313 0.7680 0.9467 0.0090  0.0065  -0.0834 117 TYR B CD2 
3380 C CE1 . TYR B 117 ? 0.8653 0.7999 0.9595 0.0049  0.0067  -0.0957 117 TYR B CE1 
3381 C CE2 . TYR B 117 ? 0.8336 0.7712 0.9420 0.0087  0.0088  -0.0849 117 TYR B CE2 
3382 C CZ  . TYR B 117 ? 0.8471 0.7835 0.9451 0.0068  0.0089  -0.0911 117 TYR B CZ  
3383 O OH  . TYR B 117 ? 0.8424 0.7801 0.9338 0.0069  0.0110  -0.0924 117 TYR B OH  
3384 N N   . ALA B 118 ? 0.8005 0.7268 0.9495 0.0085  0.0029  -0.0930 118 ALA B N   
3385 C CA  . ALA B 118 ? 0.7936 0.7191 0.9538 0.0099  0.0008  -0.0907 118 ALA B CA  
3386 C C   . ALA B 118 ? 0.7469 0.6717 0.8976 0.0087  -0.0053 -0.0885 118 ALA B C   
3387 O O   . ALA B 118 ? 0.7243 0.6500 0.8818 0.0108  -0.0083 -0.0828 118 ALA B O   
3388 C CB  . ALA B 118 ? 0.7649 0.6868 0.9351 0.0091  0.0042  -0.0978 118 ALA B CB  
3389 N N   . GLU B 119 ? 0.7209 0.6448 0.8563 0.0056  -0.0067 -0.0923 119 GLU B N   
3390 C CA  . GLU B 119 ? 0.7802 0.7039 0.9048 0.0041  -0.0119 -0.0898 119 GLU B CA  
3391 C C   . GLU B 119 ? 0.7813 0.7077 0.8981 0.0053  -0.0144 -0.0821 119 GLU B C   
3392 O O   . GLU B 119 ? 0.7660 0.6925 0.8725 0.0038  -0.0180 -0.0796 119 GLU B O   
3393 C CB  . GLU B 119 ? 0.7693 0.6921 0.8812 0.0000  -0.0119 -0.0968 119 GLU B CB  
3394 N N   . ASN B 120 ? 0.7210 0.6500 0.8426 0.0076  -0.0124 -0.0782 120 ASN B N   
3395 C CA  . ASN B 120 ? 0.7151 0.6467 0.8303 0.0087  -0.0144 -0.0713 120 ASN B CA  
3396 C C   . ASN B 120 ? 0.6980 0.6328 0.8245 0.0117  -0.0126 -0.0663 120 ASN B C   
3397 O O   . ASN B 120 ? 0.6476 0.5847 0.7709 0.0119  -0.0106 -0.0650 120 ASN B O   
3398 C CB  . ASN B 120 ? 0.7104 0.6430 0.8110 0.0064  -0.0137 -0.0735 120 ASN B CB  
3399 C CG  . ASN B 120 ? 0.7117 0.6466 0.8051 0.0070  -0.0156 -0.0670 120 ASN B CG  
3400 O OD1 . ASN B 120 ? 0.7155 0.6505 0.8112 0.0085  -0.0184 -0.0610 120 ASN B OD1 
3401 N ND2 . ASN B 120 ? 0.6747 0.6114 0.7597 0.0060  -0.0139 -0.0680 120 ASN B ND2 
3402 N N   . ILE B 121 ? 0.7115 0.6468 0.8514 0.0142  -0.0132 -0.0632 121 ILE B N   
3403 C CA  . ILE B 121 ? 0.7564 0.6962 0.9084 0.0172  -0.0119 -0.0572 121 ILE B CA  
3404 C C   . ILE B 121 ? 0.6675 0.6093 0.8157 0.0187  -0.0162 -0.0497 121 ILE B C   
3405 O O   . ILE B 121 ? 0.6576 0.6002 0.8142 0.0210  -0.0186 -0.0454 121 ILE B O   
3406 C CB  . ILE B 121 ? 0.7713 0.7119 0.9421 0.0195  -0.0097 -0.0575 121 ILE B CB  
3407 C CG1 . ILE B 121 ? 0.8092 0.7464 0.9825 0.0177  -0.0054 -0.0659 121 ILE B CG1 
3408 C CG2 . ILE B 121 ? 0.7320 0.6787 0.9153 0.0224  -0.0075 -0.0511 121 ILE B CG2 
3409 C CD1 . ILE B 121 ? 0.8219 0.7591 1.0136 0.0195  -0.0025 -0.0671 121 ILE B CD1 
3410 N N   . ASN B 122 ? 0.6083 0.5509 0.7439 0.0173  -0.0169 -0.0481 122 ASN B N   
3411 C CA  . ASN B 122 ? 0.5364 0.4799 0.6655 0.0181  -0.0206 -0.0417 122 ASN B CA  
3412 C C   . ASN B 122 ? 0.4926 0.4418 0.6299 0.0204  -0.0200 -0.0355 122 ASN B C   
3413 O O   . ASN B 122 ? 0.5250 0.4776 0.6703 0.0210  -0.0165 -0.0361 122 ASN B O   
3414 C CB  . ASN B 122 ? 0.5146 0.4563 0.6266 0.0153  -0.0215 -0.0429 122 ASN B CB  
3415 C CG  . ASN B 122 ? 0.4778 0.4217 0.5857 0.0142  -0.0183 -0.0448 122 ASN B CG  
3416 O OD1 . ASN B 122 ? 0.4556 0.4031 0.5650 0.0151  -0.0179 -0.0405 122 ASN B OD1 
3417 N ND2 . ASN B 122 ? 0.4376 0.3797 0.5403 0.0121  -0.0161 -0.0510 122 ASN B ND2 
3418 N N   . ALA B 123 ? 0.4415 0.3919 0.5764 0.0217  -0.0234 -0.0295 123 ALA B N   
3419 C CA  . ALA B 123 ? 0.4088 0.3653 0.5511 0.0240  -0.0235 -0.0231 123 ALA B CA  
3420 C C   . ALA B 123 ? 0.4388 0.3984 0.5748 0.0224  -0.0214 -0.0226 123 ALA B C   
3421 O O   . ALA B 123 ? 0.4189 0.3845 0.5628 0.0237  -0.0203 -0.0185 123 ALA B O   
3422 C CB  . ALA B 123 ? 0.3861 0.3422 0.5255 0.0256  -0.0277 -0.0173 123 ALA B CB  
3423 N N   . GLY B 124 ? 0.4711 0.4270 0.5931 0.0196  -0.0210 -0.0263 124 GLY B N   
3424 C CA  . GLY B 124 ? 0.5013 0.4595 0.6172 0.0179  -0.0189 -0.0267 124 GLY B CA  
3425 C C   . GLY B 124 ? 0.5238 0.4849 0.6486 0.0180  -0.0148 -0.0289 124 GLY B C   
3426 O O   . GLY B 124 ? 0.4879 0.4535 0.6146 0.0179  -0.0131 -0.0262 124 GLY B O   
3427 N N   . LEU B 125 ? 0.5951 0.5534 0.7255 0.0182  -0.0131 -0.0336 125 LEU B N   
3428 C CA  . LEU B 125 ? 0.6048 0.5648 0.7442 0.0185  -0.0086 -0.0361 125 LEU B CA  
3429 C C   . LEU B 125 ? 0.5935 0.5598 0.7489 0.0209  -0.0071 -0.0306 125 LEU B C   
3430 O O   . LEU B 125 ? 0.6752 0.6456 0.8363 0.0210  -0.0036 -0.0290 125 LEU B O   
3431 C CB  . LEU B 125 ? 0.6440 0.5990 0.7854 0.0180  -0.0073 -0.0427 125 LEU B CB  
3432 C CG  . LEU B 125 ? 0.6791 0.6337 0.8243 0.0174  -0.0024 -0.0471 125 LEU B CG  
3433 C CD1 . LEU B 125 ? 0.7076 0.6612 0.8397 0.0154  -0.0015 -0.0494 125 LEU B CD1 
3434 C CD2 . LEU B 125 ? 0.7385 0.6883 0.8873 0.0170  -0.0013 -0.0535 125 LEU B CD2 
3435 N N   . PHE B 126 ? 0.5352 0.5027 0.6979 0.0230  -0.0097 -0.0273 126 PHE B N   
3436 C CA  . PHE B 126 ? 0.5560 0.5311 0.7344 0.0257  -0.0089 -0.0212 126 PHE B CA  
3437 C C   . PHE B 126 ? 0.5091 0.4906 0.6848 0.0255  -0.0095 -0.0153 126 PHE B C   
3438 O O   . PHE B 126 ? 0.5593 0.5481 0.7460 0.0264  -0.0067 -0.0112 126 PHE B O   
3439 C CB  . PHE B 126 ? 0.5276 0.5024 0.7127 0.0282  -0.0123 -0.0186 126 PHE B CB  
3440 C CG  . PHE B 126 ? 0.5349 0.5182 0.7377 0.0315  -0.0115 -0.0122 126 PHE B CG  
3441 C CD1 . PHE B 126 ? 0.5505 0.5370 0.7699 0.0329  -0.0072 -0.0126 126 PHE B CD1 
3442 C CD2 . PHE B 126 ? 0.5295 0.5181 0.7331 0.0332  -0.0147 -0.0056 126 PHE B CD2 
3443 C CE1 . PHE B 126 ? 0.5330 0.5287 0.7672 0.0351  -0.0061 -0.0062 126 PHE B CE1 
3444 C CE2 . PHE B 126 ? 0.5606 0.5584 0.7793 0.0357  -0.0138 0.0006  126 PHE B CE2 
3445 C CZ  . PHE B 126 ? 0.5256 0.5271 0.7553 0.0352  -0.0093 0.0004  126 PHE B CZ  
3446 N N   . ASP B 127 ? 0.5374 0.5163 0.6988 0.0241  -0.0128 -0.0148 127 ASP B N   
3447 C CA  . ASP B 127 ? 0.5252 0.5094 0.6826 0.0237  -0.0142 -0.0096 127 ASP B CA  
3448 C C   . ASP B 127 ? 0.5109 0.4947 0.6575 0.0207  -0.0125 -0.0113 127 ASP B C   
3449 O O   . ASP B 127 ? 0.4440 0.4316 0.5857 0.0197  -0.0134 -0.0077 127 ASP B O   
3450 C CB  . ASP B 127 ? 0.5358 0.5167 0.6843 0.0240  -0.0188 -0.0078 127 ASP B CB  
3451 C CG  . ASP B 127 ? 0.5258 0.5129 0.6753 0.0248  -0.0206 -0.0015 127 ASP B CG  
3452 O OD1 . ASP B 127 ? 0.5539 0.5380 0.6909 0.0236  -0.0230 -0.0009 127 ASP B OD1 
3453 O OD2 . ASP B 127 ? 0.5321 0.5275 0.6952 0.0267  -0.0193 0.0028  127 ASP B OD2 
3454 N N   . TYR B 128 ? 0.4805 0.4599 0.6238 0.0194  -0.0099 -0.0168 128 TYR B N   
3455 C CA  . TYR B 128 ? 0.4905 0.4696 0.6263 0.0173  -0.0076 -0.0187 128 TYR B CA  
3456 C C   . TYR B 128 ? 0.5012 0.4882 0.6417 0.0169  -0.0061 -0.0131 128 TYR B C   
3457 O O   . TYR B 128 ? 0.5011 0.4885 0.6316 0.0149  -0.0067 -0.0125 128 TYR B O   
3458 C CB  . TYR B 128 ? 0.5027 0.4782 0.6415 0.0172  -0.0041 -0.0241 128 TYR B CB  
3459 C CG  . TYR B 128 ? 0.5640 0.5380 0.6942 0.0153  -0.0019 -0.0268 128 TYR B CG  
3460 C CD1 . TYR B 128 ? 0.5383 0.5062 0.6575 0.0140  -0.0023 -0.0328 128 TYR B CD1 
3461 C CD2 . TYR B 128 ? 0.5935 0.5727 0.7271 0.0149  0.0007  -0.0231 128 TYR B CD2 
3462 C CE1 . TYR B 128 ? 0.5521 0.5191 0.6640 0.0128  -0.0003 -0.0350 128 TYR B CE1 
3463 C CE2 . TYR B 128 ? 0.5902 0.5678 0.7161 0.0135  0.0026  -0.0252 128 TYR B CE2 
3464 C CZ  . TYR B 128 ? 0.5917 0.5633 0.7072 0.0127  0.0020  -0.0312 128 TYR B CZ  
3465 O OH  . TYR B 128 ? 0.5027 0.4734 0.6112 0.0118  0.0037  -0.0328 128 TYR B OH  
3466 N N   . PRO B 129 ? 0.4875 0.4812 0.6435 0.0187  -0.0040 -0.0090 129 PRO B N   
3467 C CA  . PRO B 129 ? 0.5104 0.5126 0.6714 0.0181  -0.0021 -0.0034 129 PRO B CA  
3468 C C   . PRO B 129 ? 0.4578 0.4647 0.6133 0.0171  -0.0054 0.0011  129 PRO B C   
3469 O O   . PRO B 129 ? 0.3929 0.4051 0.5466 0.0154  -0.0044 0.0043  129 PRO B O   
3470 C CB  . PRO B 129 ? 0.5154 0.5243 0.6956 0.0205  0.0009  0.0003  129 PRO B CB  
3471 C CG  . PRO B 129 ? 0.5106 0.5126 0.6945 0.0218  0.0020  -0.0051 129 PRO B CG  
3472 C CD  . PRO B 129 ? 0.5146 0.5091 0.6852 0.0213  -0.0026 -0.0091 129 PRO B CD  
3473 N N   . VAL B 130 ? 0.4342 0.4391 0.5868 0.0182  -0.0091 0.0014  130 VAL B N   
3474 C CA  . VAL B 130 ? 0.4261 0.4354 0.5745 0.0177  -0.0121 0.0057  130 VAL B CA  
3475 C C   . VAL B 130 ? 0.4464 0.4505 0.5774 0.0147  -0.0135 0.0031  130 VAL B C   
3476 O O   . VAL B 130 ? 0.4338 0.4426 0.5607 0.0129  -0.0141 0.0061  130 VAL B O   
3477 C CB  . VAL B 130 ? 0.4136 0.4223 0.5653 0.0203  -0.0154 0.0076  130 VAL B CB  
3478 C CG1 . VAL B 130 ? 0.4170 0.4316 0.5662 0.0200  -0.0178 0.0126  130 VAL B CG1 
3479 C CG2 . VAL B 130 ? 0.4261 0.4394 0.5957 0.0236  -0.0139 0.0098  130 VAL B CG2 
3480 N N   . LEU B 131 ? 0.4061 0.4013 0.5277 0.0140  -0.0138 -0.0024 131 LEU B N   
3481 C CA  . LEU B 131 ? 0.3780 0.3686 0.4848 0.0113  -0.0143 -0.0052 131 LEU B CA  
3482 C C   . LEU B 131 ? 0.3804 0.3746 0.4869 0.0095  -0.0116 -0.0048 131 LEU B C   
3483 O O   . LEU B 131 ? 0.3861 0.3812 0.4840 0.0072  -0.0121 -0.0040 131 LEU B O   
3484 C CB  . LEU B 131 ? 0.3285 0.3105 0.4274 0.0112  -0.0146 -0.0108 131 LEU B CB  
3485 C CG  . LEU B 131 ? 0.3578 0.3356 0.4420 0.0088  -0.0152 -0.0132 131 LEU B CG  
3486 C CD1 . LEU B 131 ? 0.3496 0.3273 0.4273 0.0081  -0.0178 -0.0102 131 LEU B CD1 
3487 C CD2 . LEU B 131 ? 0.3726 0.3437 0.4507 0.0087  -0.0151 -0.0185 131 LEU B CD2 
3488 N N   . MET B 132 ? 0.3798 0.3755 0.4952 0.0104  -0.0085 -0.0054 132 MET B N   
3489 C CA  . MET B 132 ? 0.3766 0.3755 0.4929 0.0091  -0.0056 -0.0044 132 MET B CA  
3490 C C   . MET B 132 ? 0.3708 0.3789 0.4918 0.0080  -0.0054 0.0019  132 MET B C   
3491 O O   . MET B 132 ? 0.4413 0.4515 0.5569 0.0057  -0.0047 0.0031  132 MET B O   
3492 C CB  . MET B 132 ? 0.4008 0.3992 0.5266 0.0106  -0.0019 -0.0060 132 MET B CB  
3493 C CG  . MET B 132 ? 0.4705 0.4715 0.5972 0.0095  0.0015  -0.0045 132 MET B CG  
3494 S SD  . MET B 132 ? 0.5105 0.5092 0.6469 0.0112  0.0064  -0.0070 132 MET B SD  
3495 C CE  . MET B 132 ? 0.5500 0.5561 0.6915 0.0101  0.0099  -0.0007 132 MET B CE  
3496 N N   . ALA B 133 ? 0.3726 0.3868 0.5034 0.0094  -0.0062 0.0060  133 ALA B N   
3497 C CA  . ALA B 133 ? 0.3150 0.3389 0.4495 0.0082  -0.0066 0.0121  133 ALA B CA  
3498 C C   . ALA B 133 ? 0.3712 0.3934 0.4920 0.0057  -0.0097 0.0116  133 ALA B C   
3499 O O   . ALA B 133 ? 0.3400 0.3669 0.4573 0.0031  -0.0093 0.0140  133 ALA B O   
3500 C CB  . ALA B 133 ? 0.3132 0.3441 0.4611 0.0107  -0.0071 0.0163  133 ALA B CB  
3501 N N   . ALA B 134 ? 0.3251 0.3408 0.4385 0.0064  -0.0125 0.0087  134 ALA B N   
3502 C CA  . ALA B 134 ? 0.3223 0.3351 0.4228 0.0042  -0.0149 0.0080  134 ALA B CA  
3503 C C   . ALA B 134 ? 0.3407 0.3501 0.4309 0.0014  -0.0138 0.0053  134 ALA B C   
3504 O O   . ALA B 134 ? 0.3795 0.3916 0.4635 -0.0012 -0.0145 0.0067  134 ALA B O   
3505 C CB  . ALA B 134 ? 0.3386 0.3436 0.4329 0.0056  -0.0173 0.0053  134 ALA B CB  
3506 N N   . ASP B 135 ? 0.3331 0.3365 0.4212 0.0021  -0.0123 0.0011  135 ASP B N   
3507 C CA  . ASP B 135 ? 0.3540 0.3548 0.4344 0.0002  -0.0110 -0.0012 135 ASP B CA  
3508 C C   . ASP B 135 ? 0.3626 0.3708 0.4458 -0.0019 -0.0097 0.0029  135 ASP B C   
3509 O O   . ASP B 135 ? 0.4114 0.4195 0.4864 -0.0044 -0.0102 0.0028  135 ASP B O   
3510 C CB  . ASP B 135 ? 0.3712 0.3676 0.4538 0.0018  -0.0089 -0.0050 135 ASP B CB  
3511 C CG  . ASP B 135 ? 0.4092 0.3980 0.4868 0.0031  -0.0100 -0.0097 135 ASP B CG  
3512 O OD1 . ASP B 135 ? 0.4310 0.4167 0.5110 0.0044  -0.0083 -0.0130 135 ASP B OD1 
3513 O OD2 . ASP B 135 ? 0.3694 0.3554 0.4405 0.0027  -0.0123 -0.0101 135 ASP B OD2 
3514 N N   . ILE B 136 ? 0.2964 0.3112 0.3917 -0.0008 -0.0079 0.0067  136 ILE B N   
3515 C CA  . ILE B 136 ? 0.3311 0.3541 0.4309 -0.0027 -0.0062 0.0115  136 ILE B CA  
3516 C C   . ILE B 136 ? 0.3422 0.3723 0.4406 -0.0050 -0.0082 0.0155  136 ILE B C   
3517 O O   . ILE B 136 ? 0.3897 0.4224 0.4821 -0.0081 -0.0084 0.0169  136 ILE B O   
3518 C CB  . ILE B 136 ? 0.3129 0.3417 0.4278 -0.0007 -0.0030 0.0151  136 ILE B CB  
3519 C CG1 . ILE B 136 ? 0.3483 0.3703 0.4641 0.0011  -0.0005 0.0112  136 ILE B CG1 
3520 C CG2 . ILE B 136 ? 0.3458 0.3846 0.4663 -0.0028 -0.0012 0.0216  136 ILE B CG2 
3521 C CD1 . ILE B 136 ? 0.3478 0.3727 0.4783 0.0037  0.0026  0.0130  136 ILE B CD1 
3522 N N   . LEU B 137 ? 0.3320 0.3653 0.4357 -0.0036 -0.0097 0.0172  137 LEU B N   
3523 C CA  . LEU B 137 ? 0.3252 0.3671 0.4295 -0.0056 -0.0113 0.0215  137 LEU B CA  
3524 C C   . LEU B 137 ? 0.3540 0.3917 0.4444 -0.0083 -0.0138 0.0190  137 LEU B C   
3525 O O   . LEU B 137 ? 0.2960 0.3403 0.3845 -0.0109 -0.0148 0.0219  137 LEU B O   
3526 C CB  . LEU B 137 ? 0.3695 0.4164 0.4842 -0.0027 -0.0122 0.0243  137 LEU B CB  
3527 C CG  . LEU B 137 ? 0.3490 0.4017 0.4800 0.0002  -0.0095 0.0276  137 LEU B CG  
3528 C CD1 . LEU B 137 ? 0.3467 0.4062 0.4877 0.0027  -0.0109 0.0311  137 LEU B CD1 
3529 C CD2 . LEU B 137 ? 0.3459 0.4076 0.4840 -0.0017 -0.0064 0.0323  137 LEU B CD2 
3530 N N   . LEU B 138 ? 0.3372 0.3642 0.4180 -0.0077 -0.0146 0.0137  138 LEU B N   
3531 C CA  . LEU B 138 ? 0.3618 0.3837 0.4297 -0.0101 -0.0162 0.0111  138 LEU B CA  
3532 C C   . LEU B 138 ? 0.3757 0.4003 0.4377 -0.0140 -0.0156 0.0117  138 LEU B C   
3533 O O   . LEU B 138 ? 0.4458 0.4706 0.5003 -0.0167 -0.0169 0.0114  138 LEU B O   
3534 C CB  . LEU B 138 ? 0.3514 0.3623 0.4113 -0.0088 -0.0164 0.0059  138 LEU B CB  
3535 C CG  . LEU B 138 ? 0.3471 0.3527 0.4057 -0.0065 -0.0180 0.0046  138 LEU B CG  
3536 C CD1 . LEU B 138 ? 0.3402 0.3364 0.3920 -0.0056 -0.0175 0.0000  138 LEU B CD1 
3537 C CD2 . LEU B 138 ? 0.3171 0.3231 0.3696 -0.0080 -0.0197 0.0059  138 LEU B CD2 
3538 N N   . TYR B 139 ? 0.3826 0.4087 0.4478 -0.0142 -0.0137 0.0123  139 TYR B N   
3539 C CA  . TYR B 139 ? 0.3837 0.4107 0.4429 -0.0175 -0.0132 0.0126  139 TYR B CA  
3540 C C   . TYR B 139 ? 0.3785 0.4165 0.4443 -0.0197 -0.0124 0.0183  139 TYR B C   
3541 O O   . TYR B 139 ? 0.3980 0.4376 0.4611 -0.0221 -0.0117 0.0194  139 TYR B O   
3542 C CB  . TYR B 139 ? 0.3855 0.4058 0.4421 -0.0161 -0.0116 0.0094  139 TYR B CB  
3543 C CG  . TYR B 139 ? 0.3666 0.3776 0.4160 -0.0145 -0.0123 0.0041  139 TYR B CG  
3544 C CD1 . TYR B 139 ? 0.3788 0.3851 0.4177 -0.0165 -0.0131 0.0014  139 TYR B CD1 
3545 C CD2 . TYR B 139 ? 0.3913 0.3985 0.4448 -0.0112 -0.0121 0.0022  139 TYR B CD2 
3546 C CE1 . TYR B 139 ? 0.4037 0.4022 0.4366 -0.0152 -0.0134 -0.0026 139 TYR B CE1 
3547 C CE2 . TYR B 139 ? 0.3673 0.3666 0.4142 -0.0100 -0.0128 -0.0020 139 TYR B CE2 
3548 C CZ  . TYR B 139 ? 0.3832 0.3785 0.4200 -0.0120 -0.0133 -0.0041 139 TYR B CZ  
3549 O OH  . TYR B 139 ? 0.3795 0.3680 0.4108 -0.0109 -0.0135 -0.0075 139 TYR B OH  
3550 N N   . GLN B 140 ? 0.3707 0.4169 0.4454 -0.0191 -0.0127 0.0223  140 GLN B N   
3551 C CA  . GLN B 140 ? 0.4054 0.4641 0.4879 -0.0213 -0.0118 0.0286  140 GLN B CA  
3552 C C   . GLN B 140 ? 0.3995 0.4596 0.4876 -0.0208 -0.0089 0.0311  140 GLN B C   
3553 O O   . GLN B 140 ? 0.4084 0.4743 0.4962 -0.0238 -0.0082 0.0348  140 GLN B O   
3554 C CB  . GLN B 140 ? 0.4054 0.4681 0.4797 -0.0260 -0.0134 0.0294  140 GLN B CB  
3555 C CG  . GLN B 140 ? 0.4057 0.4675 0.4746 -0.0267 -0.0158 0.0274  140 GLN B CG  
3556 C CD  . GLN B 140 ? 0.4199 0.4904 0.4993 -0.0246 -0.0162 0.0313  140 GLN B CD  
3557 O OE1 . GLN B 140 ? 0.4083 0.4906 0.4971 -0.0255 -0.0152 0.0370  140 GLN B OE1 
3558 N NE2 . GLN B 140 ? 0.3798 0.4450 0.4583 -0.0216 -0.0176 0.0289  140 GLN B NE2 
3559 N N   . THR B 141 ? 0.4013 0.4559 0.4943 -0.0171 -0.0073 0.0291  141 THR B N   
3560 C CA  . THR B 141 ? 0.4508 0.5038 0.5473 -0.0161 -0.0044 0.0302  141 THR B CA  
3561 C C   . THR B 141 ? 0.4506 0.5150 0.5596 -0.0165 -0.0017 0.0377  141 THR B C   
3562 O O   . THR B 141 ? 0.4780 0.5491 0.5976 -0.0151 -0.0010 0.0408  141 THR B O   
3563 C CB  . THR B 141 ? 0.4416 0.4859 0.5403 -0.0120 -0.0033 0.0256  141 THR B CB  
3564 O OG1 . THR B 141 ? 0.3877 0.4221 0.4748 -0.0118 -0.0055 0.0192  141 THR B OG1 
3565 C CG2 . THR B 141 ? 0.4282 0.4709 0.5308 -0.0108 0.0000  0.0266  141 THR B CG2 
3566 N N   . ASN B 142 ? 0.4348 0.5015 0.5431 -0.0184 0.0000  0.0410  142 ASN B N   
3567 C CA  . ASN B 142 ? 0.3794 0.4564 0.4994 -0.0189 0.0033  0.0489  142 ASN B CA  
3568 C C   . ASN B 142 ? 0.3960 0.4686 0.5232 -0.0155 0.0072  0.0490  142 ASN B C   
3569 O O   . ASN B 142 ? 0.3950 0.4739 0.5356 -0.0138 0.0103  0.0533  142 ASN B O   
3570 C CB  . ASN B 142 ? 0.3691 0.4519 0.4845 -0.0232 0.0030  0.0534  142 ASN B CB  
3571 C CG  . ASN B 142 ? 0.3634 0.4509 0.4721 -0.0269 -0.0005 0.0531  142 ASN B CG  
3572 O OD1 . ASN B 142 ? 0.3510 0.4330 0.4478 -0.0292 -0.0029 0.0492  142 ASN B OD1 
3573 N ND2 . ASN B 142 ? 0.3973 0.4954 0.5140 -0.0275 -0.0005 0.0571  142 ASN B ND2 
3574 N N   . LEU B 143 ? 0.4115 0.4736 0.5305 -0.0143 0.0072  0.0441  143 LEU B N   
3575 C CA  . LEU B 143 ? 0.4263 0.4830 0.5503 -0.0111 0.0109  0.0432  143 LEU B CA  
3576 C C   . LEU B 143 ? 0.4082 0.4533 0.5269 -0.0081 0.0099  0.0347  143 LEU B C   
3577 O O   . LEU B 143 ? 0.4050 0.4444 0.5127 -0.0088 0.0067  0.0296  143 LEU B O   
3578 C CB  . LEU B 143 ? 0.4086 0.4642 0.5285 -0.0122 0.0124  0.0461  143 LEU B CB  
3579 C CG  . LEU B 143 ? 0.4378 0.5047 0.5656 -0.0146 0.0148  0.0558  143 LEU B CG  
3580 C CD1 . LEU B 143 ? 0.4495 0.5143 0.5710 -0.0158 0.0153  0.0583  143 LEU B CD1 
3581 C CD2 . LEU B 143 ? 0.4401 0.5121 0.5832 -0.0124 0.0197  0.0607  143 LEU B CD2 
3582 N N   . VAL B 144 ? 0.4236 0.4659 0.5507 -0.0050 0.0129  0.0334  144 VAL B N   
3583 C CA  . VAL B 144 ? 0.4475 0.4795 0.5705 -0.0023 0.0125  0.0255  144 VAL B CA  
3584 C C   . VAL B 144 ? 0.4403 0.4678 0.5667 -0.0001 0.0166  0.0247  144 VAL B C   
3585 O O   . VAL B 144 ? 0.4713 0.5009 0.6093 0.0016  0.0203  0.0269  144 VAL B O   
3586 C CB  . VAL B 144 ? 0.4497 0.4817 0.5790 -0.0006 0.0115  0.0231  144 VAL B CB  
3587 C CG1 . VAL B 144 ? 0.4608 0.4824 0.5840 0.0015  0.0104  0.0150  144 VAL B CG1 
3588 C CG2 . VAL B 144 ? 0.4695 0.5067 0.5964 -0.0025 0.0079  0.0248  144 VAL B CG2 
3589 N N   . PRO B 145 ? 0.4613 0.4825 0.5779 0.0001  0.0161  0.0215  145 PRO B N   
3590 C CA  . PRO B 145 ? 0.4941 0.5108 0.6127 0.0023  0.0198  0.0205  145 PRO B CA  
3591 C C   . PRO B 145 ? 0.5160 0.5249 0.6343 0.0049  0.0204  0.0129  145 PRO B C   
3592 O O   . PRO B 145 ? 0.5313 0.5344 0.6397 0.0052  0.0175  0.0067  145 PRO B O   
3593 C CB  . PRO B 145 ? 0.4762 0.4905 0.5841 0.0015  0.0184  0.0206  145 PRO B CB  
3594 C CG  . PRO B 145 ? 0.4540 0.4673 0.5522 -0.0003 0.0136  0.0172  145 PRO B CG  
3595 C CD  . PRO B 145 ? 0.4623 0.4814 0.5661 -0.0018 0.0123  0.0196  145 PRO B CD  
3596 N N   . VAL B 146 ? 0.5404 0.5495 0.6699 0.0067  0.0243  0.0134  146 VAL B N   
3597 C CA  . VAL B 146 ? 0.6313 0.6337 0.7621 0.0088  0.0251  0.0064  146 VAL B CA  
3598 C C   . VAL B 146 ? 0.6282 0.6285 0.7674 0.0108  0.0309  0.0069  146 VAL B C   
3599 O O   . VAL B 146 ? 0.6078 0.6122 0.7523 0.0106  0.0343  0.0135  146 VAL B O   
3600 C CB  . VAL B 146 ? 0.6315 0.6361 0.7689 0.0090  0.0235  0.0054  146 VAL B CB  
3601 C CG1 . VAL B 146 ? 0.6537 0.6576 0.7809 0.0075  0.0180  0.0030  146 VAL B CG1 
3602 C CG2 . VAL B 146 ? 0.6363 0.6501 0.7877 0.0087  0.0261  0.0132  146 VAL B CG2 
3603 N N   . GLY B 147 ? 0.5890 0.5830 0.7290 0.0125  0.0320  0.0001  147 GLY B N   
3604 C CA  . GLY B 147 ? 0.6097 0.6012 0.7591 0.0144  0.0378  -0.0003 147 GLY B CA  
3605 C C   . GLY B 147 ? 0.6070 0.6031 0.7717 0.0148  0.0405  0.0028  147 GLY B C   
3606 O O   . GLY B 147 ? 0.6163 0.6166 0.7832 0.0141  0.0372  0.0039  147 GLY B O   
3607 N N   . GLU B 148 ? 0.6272 0.6226 0.8030 0.0163  0.0466  0.0042  148 GLU B N   
3608 C CA  . GLU B 148 ? 0.6420 0.6426 0.8347 0.0170  0.0504  0.0080  148 GLU B CA  
3609 C C   . GLU B 148 ? 0.6529 0.6513 0.8485 0.0176  0.0477  0.0021  148 GLU B C   
3610 O O   . GLU B 148 ? 0.6455 0.6503 0.8527 0.0180  0.0479  0.0060  148 GLU B O   
3611 C CB  . GLU B 148 ? 0.6500 0.6486 0.8532 0.0185  0.0581  0.0096  148 GLU B CB  
3612 N N   . ASP B 149 ? 0.6608 0.6508 0.8459 0.0179  0.0449  -0.0068 149 ASP B N   
3613 C CA  . ASP B 149 ? 0.7183 0.7054 0.9048 0.0183  0.0421  -0.0126 149 ASP B CA  
3614 C C   . ASP B 149 ? 0.6897 0.6815 0.8738 0.0175  0.0364  -0.0102 149 ASP B C   
3615 O O   . ASP B 149 ? 0.7453 0.7367 0.9344 0.0182  0.0347  -0.0124 149 ASP B O   
3616 C CB  . ASP B 149 ? 0.7250 0.7027 0.9000 0.0184  0.0405  -0.0224 149 ASP B CB  
3617 C CG  . ASP B 149 ? 0.7809 0.7566 0.9388 0.0171  0.0359  -0.0244 149 ASP B CG  
3618 O OD1 . ASP B 149 ? 0.8372 0.8138 0.9904 0.0169  0.0371  -0.0213 149 ASP B OD1 
3619 O OD2 . ASP B 149 ? 0.7719 0.7450 0.9213 0.0165  0.0311  -0.0290 149 ASP B OD2 
3620 N N   . GLN B 150 ? 0.6793 0.6757 0.8562 0.0160  0.0337  -0.0054 150 GLN B N   
3621 C CA  . GLN B 150 ? 0.6264 0.6274 0.8000 0.0150  0.0285  -0.0029 150 GLN B CA  
3622 C C   . GLN B 150 ? 0.6127 0.6245 0.7979 0.0147  0.0297  0.0061  150 GLN B C   
3623 O O   . GLN B 150 ? 0.6131 0.6296 0.7955 0.0138  0.0257  0.0087  150 GLN B O   
3624 C CB  . GLN B 150 ? 0.6238 0.6222 0.7805 0.0132  0.0243  -0.0046 150 GLN B CB  
3625 C CG  . GLN B 150 ? 0.6185 0.6080 0.7633 0.0133  0.0220  -0.0130 150 GLN B CG  
3626 C CD  . GLN B 150 ? 0.6077 0.5945 0.7543 0.0140  0.0195  -0.0171 150 GLN B CD  
3627 O OE1 . GLN B 150 ? 0.5575 0.5470 0.7026 0.0135  0.0158  -0.0151 150 GLN B OE1 
3628 N NE2 . GLN B 150 ? 0.6142 0.5958 0.7645 0.0152  0.0217  -0.0225 150 GLN B NE2 
3629 N N   . LYS B 151 ? 0.6409 0.6571 0.8395 0.0156  0.0355  0.0108  151 LYS B N   
3630 C CA  . LYS B 151 ? 0.6187 0.6468 0.8294 0.0151  0.0376  0.0204  151 LYS B CA  
3631 C C   . LYS B 151 ? 0.5703 0.6049 0.7901 0.0161  0.0351  0.0225  151 LYS B C   
3632 O O   . LYS B 151 ? 0.5746 0.6175 0.7944 0.0148  0.0326  0.0280  151 LYS B O   
3633 C CB  . LYS B 151 ? 0.6089 0.6400 0.8339 0.0162  0.0451  0.0249  151 LYS B CB  
3634 N N   . GLN B 152 ? 0.6407 0.6714 0.8678 0.0182  0.0358  0.0183  152 GLN B N   
3635 C CA  . GLN B 152 ? 0.6620 0.6983 0.8989 0.0198  0.0335  0.0203  152 GLN B CA  
3636 C C   . GLN B 152 ? 0.6280 0.6627 0.8520 0.0189  0.0263  0.0180  152 GLN B C   
3637 O O   . GLN B 152 ? 0.6068 0.6497 0.8363 0.0194  0.0240  0.0228  152 GLN B O   
3638 C CB  . GLN B 152 ? 0.6195 0.6508 0.8669 0.0222  0.0360  0.0157  152 GLN B CB  
3639 N N   . HIS B 153 ? 0.6113 0.6360 0.8188 0.0178  0.0231  0.0111  153 HIS B N   
3640 C CA  . HIS B 153 ? 0.5722 0.5949 0.7662 0.0167  0.0170  0.0094  153 HIS B CA  
3641 C C   . HIS B 153 ? 0.5271 0.5580 0.7178 0.0146  0.0156  0.0156  153 HIS B C   
3642 O O   . HIS B 153 ? 0.4753 0.5106 0.6652 0.0145  0.0120  0.0180  153 HIS B O   
3643 C CB  . HIS B 153 ? 0.5742 0.5859 0.7516 0.0156  0.0147  0.0017  153 HIS B CB  
3644 C CG  . HIS B 153 ? 0.6001 0.6040 0.7784 0.0171  0.0145  -0.0048 153 HIS B CG  
3645 N ND1 . HIS B 153 ? 0.5926 0.5877 0.7602 0.0165  0.0144  -0.0118 153 HIS B ND1 
3646 C CD2 . HIS B 153 ? 0.6022 0.6065 0.7914 0.0192  0.0145  -0.0053 153 HIS B CD2 
3647 C CE1 . HIS B 153 ? 0.6137 0.6039 0.7849 0.0178  0.0143  -0.0165 153 HIS B CE1 
3648 N NE2 . HIS B 153 ? 0.6132 0.6085 0.7976 0.0195  0.0143  -0.0127 153 HIS B NE2 
3649 N N   . LEU B 154 ? 0.5612 0.5944 0.7502 0.0130  0.0184  0.0183  154 LEU B N   
3650 C CA  . LEU B 154 ? 0.5488 0.5907 0.7356 0.0106  0.0174  0.0246  154 LEU B CA  
3651 C C   . LEU B 154 ? 0.5511 0.6055 0.7529 0.0113  0.0184  0.0321  154 LEU B C   
3652 O O   . LEU B 154 ? 0.5547 0.6154 0.7535 0.0100  0.0151  0.0352  154 LEU B O   
3653 C CB  . LEU B 154 ? 0.5864 0.6294 0.7706 0.0088  0.0206  0.0274  154 LEU B CB  
3654 C CG  . LEU B 154 ? 0.6085 0.6610 0.7901 0.0060  0.0190  0.0339  154 LEU B CG  
3655 C CD1 . LEU B 154 ? 0.6002 0.6476 0.7648 0.0039  0.0137  0.0298  154 LEU B CD1 
3656 C CD2 . LEU B 154 ? 0.6525 0.7098 0.8372 0.0045  0.0230  0.0395  154 LEU B CD2 
3657 N N   . GLU B 155 ? 0.5900 0.6484 0.8081 0.0134  0.0232  0.0349  155 GLU B N   
3658 C CA  . GLU B 155 ? 0.6454 0.7172 0.8805 0.0145  0.0251  0.0427  155 GLU B CA  
3659 C C   . GLU B 155 ? 0.5367 0.6113 0.7727 0.0159  0.0203  0.0424  155 GLU B C   
3660 O O   . GLU B 155 ? 0.5776 0.6633 0.8176 0.0151  0.0189  0.0485  155 GLU B O   
3661 C CB  . GLU B 155 ? 0.7392 0.8130 0.9921 0.0169  0.0314  0.0447  155 GLU B CB  
3662 C CG  . GLU B 155 ? 0.8227 0.8966 1.0765 0.0155  0.0367  0.0475  155 GLU B CG  
3663 C CD  . GLU B 155 ? 0.8628 0.9392 1.1348 0.0176  0.0440  0.0503  155 GLU B CD  
3664 O OE1 . GLU B 155 ? 0.8655 0.9403 1.1438 0.0196  0.0441  0.0493  155 GLU B OE1 
3665 O OE2 . GLU B 155 ? 0.8754 0.9513 1.1484 0.0167  0.0487  0.0530  155 GLU B OE2 
3666 N N   . LEU B 156 ? 0.5349 0.5993 0.7662 0.0177  0.0177  0.0356  156 LEU B N   
3667 C CA  . LEU B 156 ? 0.4877 0.5527 0.7177 0.0192  0.0128  0.0351  156 LEU B CA  
3668 C C   . LEU B 156 ? 0.4461 0.5127 0.6619 0.0165  0.0083  0.0360  156 LEU B C   
3669 O O   . LEU B 156 ? 0.4662 0.5409 0.6856 0.0170  0.0059  0.0402  156 LEU B O   
3670 C CB  . LEU B 156 ? 0.4900 0.5424 0.7146 0.0209  0.0107  0.0273  156 LEU B CB  
3671 C CG  . LEU B 156 ? 0.4997 0.5508 0.7211 0.0225  0.0055  0.0266  156 LEU B CG  
3672 C CD1 . LEU B 156 ? 0.4881 0.5517 0.7262 0.0250  0.0056  0.0337  156 LEU B CD1 
3673 C CD2 . LEU B 156 ? 0.5282 0.5679 0.7465 0.0241  0.0041  0.0198  156 LEU B CD2 
3674 N N   . SER B 157 ? 0.5149 0.5743 0.7152 0.0137  0.0074  0.0321  157 SER B N   
3675 C CA  . SER B 157 ? 0.5657 0.6255 0.7518 0.0109  0.0035  0.0323  157 SER B CA  
3676 C C   . SER B 157 ? 0.5353 0.6091 0.7277 0.0091  0.0042  0.0401  157 SER B C   
3677 O O   . SER B 157 ? 0.5291 0.6073 0.7170 0.0080  0.0009  0.0418  157 SER B O   
3678 C CB  . SER B 157 ? 0.5453 0.5953 0.7153 0.0084  0.0031  0.0270  157 SER B CB  
3679 O OG  . SER B 157 ? 0.5696 0.6243 0.7396 0.0061  0.0058  0.0305  157 SER B OG  
3680 N N   . ARG B 158 ? 0.6318 0.7129 0.8350 0.0087  0.0088  0.0449  158 ARG B N   
3681 C CA  . ARG B 158 ? 0.6071 0.7033 0.8185 0.0069  0.0103  0.0533  158 ARG B CA  
3682 C C   . ARG B 158 ? 0.5610 0.6679 0.7857 0.0093  0.0094  0.0579  158 ARG B C   
3683 O O   . ARG B 158 ? 0.5905 0.7072 0.8147 0.0077  0.0073  0.0621  158 ARG B O   
3684 C CB  . ARG B 158 ? 0.6419 0.7434 0.8637 0.0064  0.0161  0.0580  158 ARG B CB  
3685 C CG  . ARG B 158 ? 0.7167 0.8096 0.9257 0.0039  0.0168  0.0549  158 ARG B CG  
3686 C CD  . ARG B 158 ? 0.7559 0.8530 0.9748 0.0037  0.0228  0.0600  158 ARG B CD  
3687 N NE  . ARG B 158 ? 0.7722 0.8831 0.9957 0.0008  0.0242  0.0687  158 ARG B NE  
3688 C CZ  . ARG B 158 ? 0.8112 0.9339 1.0486 0.0013  0.0277  0.0764  158 ARG B CZ  
3689 N NH1 . ARG B 158 ? 0.8087 0.9383 1.0401 -0.0016 0.0275  0.0820  158 ARG B NH1 
3690 N NH2 . ARG B 158 ? 0.8591 0.9777 1.1020 0.0049  0.0295  0.0753  158 ARG B NH2 
3691 N N   . ASP B 159 ? 0.5474 0.6524 0.7839 0.0132  0.0109  0.0569  159 ASP B N   
3692 C CA  . ASP B 159 ? 0.5768 0.6836 0.8140 0.0153  0.0094  0.0586  159 ASP B CA  
3693 C C   . ASP B 159 ? 0.5607 0.6673 0.7917 0.0158  0.0037  0.0569  159 ASP B C   
3694 O O   . ASP B 159 ? 0.5582 0.6698 0.7842 0.0152  0.0019  0.0599  159 ASP B O   
3695 C CB  . ASP B 159 ? 0.6350 0.7338 0.8776 0.0183  0.0116  0.0559  159 ASP B CB  
3696 C CG  . ASP B 159 ? 0.6728 0.7721 0.9209 0.0179  0.0173  0.0587  159 ASP B CG  
3697 O OD1 . ASP B 159 ? 0.7112 0.8037 0.9654 0.0194  0.0201  0.0553  159 ASP B OD1 
3698 O OD2 . ASP B 159 ? 0.7044 0.8105 0.9507 0.0161  0.0189  0.0641  159 ASP B OD2 
3699 N N   . ILE B 160 ? 0.4995 0.5950 0.7219 0.0161  0.0008  0.0505  160 ILE B N   
3700 C CA  . ILE B 160 ? 0.4729 0.5634 0.6827 0.0160  -0.0045 0.0477  160 ILE B CA  
3701 C C   . ILE B 160 ? 0.4124 0.5097 0.6133 0.0122  -0.0062 0.0505  160 ILE B C   
3702 O O   . ILE B 160 ? 0.3877 0.4914 0.5891 0.0127  -0.0090 0.0534  160 ILE B O   
3703 C CB  . ILE B 160 ? 0.4333 0.5069 0.6279 0.0157  -0.0065 0.0394  160 ILE B CB  
3704 C CG1 . ILE B 160 ? 0.4302 0.4975 0.6330 0.0194  -0.0058 0.0366  160 ILE B CG1 
3705 C CG2 . ILE B 160 ? 0.4496 0.5182 0.6298 0.0148  -0.0112 0.0373  160 ILE B CG2 
3706 C CD1 . ILE B 160 ? 0.4210 0.4735 0.6115 0.0188  -0.0063 0.0288  160 ILE B CD1 
3707 N N   . ALA B 161 ? 0.4337 0.5295 0.6267 0.0085  -0.0046 0.0497  161 ALA B N   
3708 C CA  . ALA B 161 ? 0.4761 0.5776 0.6599 0.0043  -0.0060 0.0517  161 ALA B CA  
3709 C C   . ALA B 161 ? 0.4586 0.5777 0.6546 0.0040  -0.0053 0.0597  161 ALA B C   
3710 O O   . ALA B 161 ? 0.3907 0.5150 0.5810 0.0022  -0.0082 0.0611  161 ALA B O   
3711 C CB  . ALA B 161 ? 0.5239 0.6216 0.6999 0.0009  -0.0039 0.0502  161 ALA B CB  
3712 N N   . GLN B 162 ? 0.5149 0.6434 0.7283 0.0057  -0.0013 0.0650  162 GLN B N   
3713 C CA  . GLN B 162 ? 0.5408 0.6769 0.7540 0.0055  0.0002  0.0698  162 GLN B CA  
3714 C C   . GLN B 162 ? 0.4834 0.6177 0.6937 0.0084  -0.0025 0.0688  162 GLN B C   
3715 O O   . GLN B 162 ? 0.4574 0.5978 0.6628 0.0072  -0.0037 0.0711  162 GLN B O   
3716 C CB  . GLN B 162 ? 0.5636 0.6987 0.7824 0.0065  0.0053  0.0720  162 GLN B CB  
3717 C CG  . GLN B 162 ? 0.6016 0.7402 0.8211 0.0033  0.0083  0.0747  162 GLN B CG  
3718 C CD  . GLN B 162 ? 0.5954 0.7312 0.8205 0.0047  0.0134  0.0767  162 GLN B CD  
3719 O OE1 . GLN B 162 ? 0.5890 0.7178 0.8197 0.0078  0.0150  0.0741  162 GLN B OE1 
3720 N NE2 . GLN B 162 ? 0.6531 0.7940 0.8765 0.0023  0.0158  0.0814  162 GLN B NE2 
3721 N N   . ARG B 163 ? 0.5404 0.6659 0.7533 0.0120  -0.0032 0.0652  163 ARG B N   
3722 C CA  . ARG B 163 ? 0.5264 0.6484 0.7359 0.0148  -0.0055 0.0641  163 ARG B CA  
3723 C C   . ARG B 163 ? 0.5039 0.6281 0.7061 0.0139  -0.0101 0.0637  163 ARG B C   
3724 O O   . ARG B 163 ? 0.5073 0.6348 0.7049 0.0142  -0.0112 0.0652  163 ARG B O   
3725 C CB  . ARG B 163 ? 0.5272 0.6387 0.7399 0.0182  -0.0056 0.0601  163 ARG B CB  
3726 C CG  . ARG B 163 ? 0.5729 0.6805 0.7825 0.0207  -0.0068 0.0595  163 ARG B CG  
3727 C CD  . ARG B 163 ? 0.5867 0.6844 0.7998 0.0233  -0.0062 0.0559  163 ARG B CD  
3728 N NE  . ARG B 163 ? 0.5612 0.6585 0.7822 0.0231  -0.0017 0.0564  163 ARG B NE  
3729 C CZ  . ARG B 163 ? 0.6031 0.6940 0.8297 0.0239  -0.0002 0.0531  163 ARG B CZ  
3730 N NH1 . ARG B 163 ? 0.6637 0.7476 0.8889 0.0250  -0.0030 0.0487  163 ARG B NH1 
3731 N NH2 . ARG B 163 ? 0.6276 0.7186 0.8611 0.0236  0.0043  0.0541  163 ARG B NH2 
3732 N N   . PHE B 164 ? 0.4573 0.5796 0.6586 0.0126  -0.0127 0.0616  164 PHE B N   
3733 C CA  . PHE B 164 ? 0.4368 0.5593 0.6295 0.0113  -0.0173 0.0607  164 PHE B CA  
3734 C C   . PHE B 164 ? 0.4012 0.5362 0.5914 0.0073  -0.0173 0.0648  164 PHE B C   
3735 O O   . PHE B 164 ? 0.3737 0.5116 0.5582 0.0073  -0.0194 0.0657  164 PHE B O   
3736 C CB  . PHE B 164 ? 0.3923 0.4975 0.5667 0.0090  -0.0182 0.0530  164 PHE B CB  
3737 C CG  . PHE B 164 ? 0.3954 0.4931 0.5545 0.0080  -0.0219 0.0498  164 PHE B CG  
3738 C CD1 . PHE B 164 ? 0.3924 0.4919 0.5397 0.0034  -0.0228 0.0492  164 PHE B CD1 
3739 C CD2 . PHE B 164 ? 0.4051 0.4936 0.5616 0.0116  -0.0243 0.0476  164 PHE B CD2 
3740 C CE1 . PHE B 164 ? 0.3844 0.4767 0.5179 0.0025  -0.0256 0.0463  164 PHE B CE1 
3741 C CE2 . PHE B 164 ? 0.3943 0.4758 0.5369 0.0107  -0.0272 0.0452  164 PHE B CE2 
3742 C CZ  . PHE B 164 ? 0.3854 0.4686 0.5166 0.0062  -0.0277 0.0445  164 PHE B CZ  
3743 N N   . ASN B 165 ? 0.4484 0.5888 0.6400 0.0037  -0.0145 0.0665  165 ASN B N   
3744 C CA  . ASN B 165 ? 0.4494 0.6012 0.6374 -0.0009 -0.0144 0.0701  165 ASN B CA  
3745 C C   . ASN B 165 ? 0.4557 0.6115 0.6419 0.0007  -0.0132 0.0725  165 ASN B C   
3746 O O   . ASN B 165 ? 0.4510 0.6132 0.6314 -0.0015 -0.0150 0.0737  165 ASN B O   
3747 C CB  . ASN B 165 ? 0.4472 0.6026 0.6367 -0.0046 -0.0111 0.0719  165 ASN B CB  
3748 C CG  . ASN B 165 ? 0.4289 0.5688 0.6005 -0.0077 -0.0119 0.0650  165 ASN B CG  
3749 O OD1 . ASN B 165 ? 0.4133 0.5415 0.5718 -0.0077 -0.0148 0.0592  165 ASN B OD1 
3750 N ND2 . ASN B 165 ? 0.4386 0.5791 0.6101 -0.0104 -0.0091 0.0660  165 ASN B ND2 
3751 N N   . ALA B 166 ? 0.4891 0.6410 0.6803 0.0042  -0.0101 0.0730  166 ALA B N   
3752 C CA  . ALA B 166 ? 0.5231 0.6779 0.7135 0.0056  -0.0087 0.0752  166 ALA B CA  
3753 C C   . ALA B 166 ? 0.5110 0.6656 0.6958 0.0070  -0.0120 0.0741  166 ALA B C   
3754 O O   . ALA B 166 ? 0.4723 0.6334 0.6537 0.0059  -0.0120 0.0762  166 ALA B O   
3755 C CB  . ALA B 166 ? 0.5284 0.6772 0.7248 0.0090  -0.0055 0.0750  166 ALA B CB  
3756 N N   . LEU B 167 ? 0.4913 0.6384 0.6746 0.0093  -0.0148 0.0708  167 LEU B N   
3757 C CA  . LEU B 167 ? 0.4630 0.6080 0.6404 0.0110  -0.0179 0.0696  167 LEU B CA  
3758 C C   . LEU B 167 ? 0.4438 0.5942 0.6150 0.0078  -0.0213 0.0698  167 LEU B C   
3759 O O   . LEU B 167 ? 0.4247 0.5789 0.5908 0.0075  -0.0226 0.0706  167 LEU B O   
3760 C CB  . LEU B 167 ? 0.4886 0.6220 0.6658 0.0149  -0.0195 0.0662  167 LEU B CB  
3761 C CG  . LEU B 167 ? 0.5510 0.6789 0.7328 0.0178  -0.0167 0.0655  167 LEU B CG  
3762 C CD1 . LEU B 167 ? 0.5697 0.6867 0.7525 0.0203  -0.0178 0.0621  167 LEU B CD1 
3763 C CD2 . LEU B 167 ? 0.5701 0.6986 0.7490 0.0195  -0.0163 0.0662  167 LEU B CD2 
3764 N N   . TYR B 168 ? 0.4055 0.5562 0.5768 0.0049  -0.0227 0.0690  168 TYR B N   
3765 C CA  . TYR B 168 ? 0.4106 0.5643 0.5752 0.0014  -0.0268 0.0684  168 TYR B CA  
3766 C C   . TYR B 168 ? 0.3998 0.5602 0.5583 -0.0053 -0.0259 0.0686  168 TYR B C   
3767 O O   . TYR B 168 ? 0.4428 0.5980 0.5862 -0.0089 -0.0275 0.0648  168 TYR B O   
3768 C CB  . TYR B 168 ? 0.4239 0.5584 0.5776 0.0024  -0.0279 0.0618  168 TYR B CB  
3769 C CG  . TYR B 168 ? 0.4219 0.5502 0.5813 0.0084  -0.0295 0.0619  168 TYR B CG  
3770 C CD1 . TYR B 168 ? 0.4390 0.5692 0.5972 0.0111  -0.0322 0.0637  168 TYR B CD1 
3771 C CD2 . TYR B 168 ? 0.4220 0.5426 0.5879 0.0115  -0.0282 0.0603  168 TYR B CD2 
3772 C CE1 . TYR B 168 ? 0.4439 0.5632 0.6007 0.0160  -0.0324 0.0620  168 TYR B CE1 
3773 C CE2 . TYR B 168 ? 0.3999 0.5134 0.5687 0.0165  -0.0293 0.0597  168 TYR B CE2 
3774 C CZ  . TYR B 168 ? 0.3944 0.5057 0.5561 0.0184  -0.0310 0.0599  168 TYR B CZ  
3775 O OH  . TYR B 168 ? 0.4172 0.5182 0.5762 0.0222  -0.0311 0.0579  168 TYR B OH  
3776 N N   . GLY B 169 ? 0.4058 0.5743 0.5725 -0.0068 -0.0226 0.0720  169 GLY B N   
3777 C CA  . GLY B 169 ? 0.4174 0.5926 0.5793 -0.0132 -0.0216 0.0729  169 GLY B CA  
3778 C C   . GLY B 169 ? 0.4194 0.5813 0.5743 -0.0149 -0.0198 0.0685  169 GLY B C   
3779 O O   . GLY B 169 ? 0.4385 0.5904 0.5966 -0.0111 -0.0189 0.0661  169 GLY B O   
3780 N N   . GLU B 170 ? 0.4701 0.6323 0.6156 -0.0205 -0.0193 0.0674  170 GLU B N   
3781 C CA  . GLU B 170 ? 0.4556 0.6085 0.5965 -0.0221 -0.0172 0.0648  170 GLU B CA  
3782 C C   . GLU B 170 ? 0.4626 0.5960 0.5876 -0.0221 -0.0188 0.0564  170 GLU B C   
3783 O O   . GLU B 170 ? 0.5039 0.6319 0.6163 -0.0264 -0.0193 0.0530  170 GLU B O   
3784 C CB  . GLU B 170 ? 0.4863 0.6491 0.6253 -0.0280 -0.0161 0.0682  170 GLU B CB  
3785 N N   . ILE B 171 ? 0.4291 0.5526 0.5552 -0.0173 -0.0195 0.0533  171 ILE B N   
3786 C CA  . ILE B 171 ? 0.3941 0.5002 0.5063 -0.0169 -0.0209 0.0461  171 ILE B CA  
3787 C C   . ILE B 171 ? 0.3823 0.4799 0.4933 -0.0167 -0.0187 0.0434  171 ILE B C   
3788 O O   . ILE B 171 ? 0.3662 0.4540 0.4649 -0.0191 -0.0189 0.0387  171 ILE B O   
3789 C CB  . ILE B 171 ? 0.4215 0.5209 0.5351 -0.0119 -0.0226 0.0444  171 ILE B CB  
3790 C CG1 . ILE B 171 ? 0.4255 0.5355 0.5435 -0.0110 -0.0246 0.0484  171 ILE B CG1 
3791 C CG2 . ILE B 171 ? 0.4102 0.4931 0.5089 -0.0121 -0.0238 0.0377  171 ILE B CG2 
3792 C CD1 . ILE B 171 ? 0.4687 0.5796 0.5741 -0.0153 -0.0263 0.0469  171 ILE B CD1 
3793 N N   . PHE B 172 ? 0.2918 0.3936 0.4162 -0.0139 -0.0163 0.0466  172 PHE B N   
3794 C CA  . PHE B 172 ? 0.3609 0.4557 0.4856 -0.0135 -0.0139 0.0446  172 PHE B CA  
3795 C C   . PHE B 172 ? 0.4192 0.5240 0.5500 -0.0162 -0.0112 0.0497  172 PHE B C   
3796 O O   . PHE B 172 ? 0.4224 0.5417 0.5627 -0.0172 -0.0106 0.0560  172 PHE B O   
3797 C CB  . PHE B 172 ? 0.3393 0.4298 0.4740 -0.0084 -0.0127 0.0438  172 PHE B CB  
3798 C CG  . PHE B 172 ? 0.3384 0.4191 0.4676 -0.0055 -0.0153 0.0394  172 PHE B CG  
3799 C CD1 . PHE B 172 ? 0.3393 0.4079 0.4529 -0.0070 -0.0170 0.0336  172 PHE B CD1 
3800 C CD2 . PHE B 172 ? 0.3444 0.4281 0.4845 -0.0013 -0.0159 0.0415  172 PHE B CD2 
3801 C CE1 . PHE B 172 ? 0.3340 0.3937 0.4425 -0.0045 -0.0192 0.0303  172 PHE B CE1 
3802 C CE2 . PHE B 172 ? 0.3298 0.4043 0.4646 0.0012  -0.0184 0.0381  172 PHE B CE2 
3803 C CZ  . PHE B 172 ? 0.3395 0.4019 0.4583 -0.0004 -0.0199 0.0326  172 PHE B CZ  
3804 N N   . LYS B 173 ? 0.3981 0.4957 0.5237 -0.0174 -0.0096 0.0474  173 LYS B N   
3805 C CA  . LYS B 173 ? 0.4567 0.5613 0.5908 -0.0183 -0.0062 0.0525  173 LYS B CA  
3806 C C   . LYS B 173 ? 0.4817 0.5843 0.6282 -0.0137 -0.0033 0.0531  173 LYS B C   
3807 O O   . LYS B 173 ? 0.4104 0.5021 0.5543 -0.0106 -0.0040 0.0476  173 LYS B O   
3808 C CB  . LYS B 173 ? 0.4461 0.5435 0.5694 -0.0210 -0.0058 0.0500  173 LYS B CB  
3809 C CG  . LYS B 173 ? 0.4667 0.5630 0.5764 -0.0255 -0.0085 0.0479  173 LYS B CG  
3810 C CD  . LYS B 173 ? 0.5225 0.6337 0.6358 -0.0295 -0.0089 0.0540  173 LYS B CD  
3811 C CE  . LYS B 173 ? 0.5148 0.6251 0.6166 -0.0346 -0.0100 0.0532  173 LYS B CE  
3812 N NZ  . LYS B 173 ? 0.5686 0.6930 0.6719 -0.0389 -0.0109 0.0582  173 LYS B NZ  
3813 N N   . VAL B 174 ? 0.4916 0.6050 0.6520 -0.0135 0.0003  0.0599  174 VAL B N   
3814 C CA  . VAL B 174 ? 0.4794 0.5910 0.6521 -0.0096 0.0039  0.0607  174 VAL B CA  
3815 C C   . VAL B 174 ? 0.4952 0.5978 0.6626 -0.0100 0.0064  0.0584  174 VAL B C   
3816 O O   . VAL B 174 ? 0.4918 0.5999 0.6598 -0.0127 0.0084  0.0630  174 VAL B O   
3817 C CB  . VAL B 174 ? 0.5179 0.6456 0.7091 -0.0089 0.0074  0.0695  174 VAL B CB  
3818 C CG1 . VAL B 174 ? 0.5058 0.6314 0.7106 -0.0050 0.0119  0.0704  174 VAL B CG1 
3819 C CG2 . VAL B 174 ? 0.4878 0.6248 0.6845 -0.0080 0.0048  0.0718  174 VAL B CG2 
3820 N N   . PRO B 175 ? 0.5325 0.6218 0.6952 -0.0074 0.0062  0.0515  175 PRO B N   
3821 C CA  . PRO B 175 ? 0.5727 0.6535 0.7299 -0.0075 0.0083  0.0489  175 PRO B CA  
3822 C C   . PRO B 175 ? 0.5837 0.6689 0.7546 -0.0060 0.0137  0.0539  175 PRO B C   
3823 O O   . PRO B 175 ? 0.6213 0.7140 0.8068 -0.0040 0.0161  0.0579  175 PRO B O   
3824 C CB  . PRO B 175 ? 0.5507 0.6179 0.7005 -0.0049 0.0065  0.0403  175 PRO B CB  
3825 C CG  . PRO B 175 ? 0.5307 0.6006 0.6900 -0.0021 0.0059  0.0405  175 PRO B CG  
3826 C CD  . PRO B 175 ? 0.5322 0.6147 0.6957 -0.0040 0.0044  0.0464  175 PRO B CD  
3827 N N   . GLU B 176 ? 0.5642 0.6448 0.7306 -0.0067 0.0159  0.0539  176 GLU B N   
3828 C CA  . GLU B 176 ? 0.5692 0.6526 0.7470 -0.0055 0.0215  0.0587  176 GLU B CA  
3829 C C   . GLU B 176 ? 0.6050 0.6754 0.7763 -0.0036 0.0229  0.0527  176 GLU B C   
3830 O O   . GLU B 176 ? 0.5873 0.6502 0.7447 -0.0046 0.0200  0.0482  176 GLU B O   
3831 C CB  . GLU B 176 ? 0.5767 0.6706 0.7569 -0.0088 0.0233  0.0674  176 GLU B CB  
3832 C CG  . GLU B 176 ? 0.5881 0.6971 0.7761 -0.0109 0.0226  0.0742  176 GLU B CG  
3833 C CD  . GLU B 176 ? 0.6354 0.7528 0.8418 -0.0082 0.0261  0.0786  176 GLU B CD  
3834 O OE1 . GLU B 176 ? 0.6529 0.7661 0.8678 -0.0053 0.0305  0.0782  176 GLU B OE1 
3835 O OE2 . GLU B 176 ? 0.6401 0.7687 0.8526 -0.0090 0.0247  0.0823  176 GLU B OE2 
3836 N N   . PRO B 177 ? 0.6476 0.7157 0.8294 -0.0007 0.0275  0.0527  177 PRO B N   
3837 C CA  . PRO B 177 ? 0.6828 0.7389 0.8587 0.0012  0.0290  0.0467  177 PRO B CA  
3838 C C   . PRO B 177 ? 0.6673 0.7225 0.8384 0.0000  0.0311  0.0503  177 PRO B C   
3839 O O   . PRO B 177 ? 0.7131 0.7773 0.8915 -0.0015 0.0340  0.0587  177 PRO B O   
3840 C CB  . PRO B 177 ? 0.6766 0.7322 0.8670 0.0043  0.0338  0.0466  177 PRO B CB  
3841 C CG  . PRO B 177 ? 0.6847 0.7541 0.8902 0.0036  0.0368  0.0560  177 PRO B CG  
3842 C CD  . PRO B 177 ? 0.6696 0.7468 0.8698 0.0008  0.0320  0.0586  177 PRO B CD  
3843 N N   . PHE B 178 ? 0.6578 0.7028 0.8171 0.0007  0.0297  0.0441  178 PHE B N   
3844 C CA  . PHE B 178 ? 0.6450 0.6873 0.7998 0.0005  0.0318  0.0466  178 PHE B CA  
3845 C C   . PHE B 178 ? 0.6771 0.7089 0.8307 0.0037  0.0344  0.0403  178 PHE B C   
3846 O O   . PHE B 178 ? 0.6128 0.6364 0.7553 0.0046  0.0315  0.0328  178 PHE B O   
3847 C CB  . PHE B 178 ? 0.6699 0.7112 0.8108 -0.0019 0.0272  0.0459  178 PHE B CB  
3848 C CG  . PHE B 178 ? 0.7115 0.7514 0.8484 -0.0021 0.0290  0.0498  178 PHE B CG  
3849 C CD1 . PHE B 178 ? 0.7364 0.7667 0.8651 0.0000  0.0288  0.0443  178 PHE B CD1 
3850 C CD2 . PHE B 178 ? 0.7241 0.7729 0.8656 -0.0045 0.0307  0.0593  178 PHE B CD2 
3851 C CE1 . PHE B 178 ? 0.7313 0.7605 0.8566 0.0003  0.0304  0.0483  178 PHE B CE1 
3852 C CE2 . PHE B 178 ? 0.7632 0.8105 0.9010 -0.0045 0.0322  0.0635  178 PHE B CE2 
3853 C CZ  . PHE B 178 ? 0.7297 0.7670 0.8595 -0.0019 0.0320  0.0580  178 PHE B CZ  
3854 N N   . ILE B 179 ? 0.6454 0.6784 0.8111 0.0055  0.0402  0.0436  179 ILE B N   
3855 C CA  . ILE B 179 ? 0.6807 0.7047 0.8475 0.0084  0.0437  0.0381  179 ILE B CA  
3856 C C   . ILE B 179 ? 0.7053 0.7280 0.8716 0.0090  0.0477  0.0430  179 ILE B C   
3857 O O   . ILE B 179 ? 0.7084 0.7387 0.8833 0.0080  0.0513  0.0523  179 ILE B O   
3858 C CB  . ILE B 179 ? 0.6829 0.7084 0.8644 0.0101  0.0477  0.0377  179 ILE B CB  
3859 C CG1 . ILE B 179 ? 0.6919 0.7162 0.8716 0.0101  0.0430  0.0314  179 ILE B CG1 
3860 C CG2 . ILE B 179 ? 0.6729 0.6906 0.8581 0.0127  0.0529  0.0340  179 ILE B CG2 
3861 C CD1 . ILE B 179 ? 0.6790 0.7065 0.8736 0.0116  0.0458  0.0318  179 ILE B CD1 
3862 N N   . PRO B 180 ? 0.7114 0.7251 0.8680 0.0107  0.0474  0.0374  180 PRO B N   
3863 C CA  . PRO B 180 ? 0.7412 0.7532 0.8963 0.0116  0.0508  0.0422  180 PRO B CA  
3864 C C   . PRO B 180 ? 0.8279 0.8407 0.9963 0.0132  0.0585  0.0473  180 PRO B C   
3865 O O   . PRO B 180 ? 0.7655 0.7775 0.9434 0.0142  0.0615  0.0444  180 PRO B O   
3866 C CB  . PRO B 180 ? 0.7307 0.7330 0.8739 0.0136  0.0488  0.0336  180 PRO B CB  
3867 C CG  . PRO B 180 ? 0.7413 0.7395 0.8846 0.0143  0.0472  0.0245  180 PRO B CG  
3868 C CD  . PRO B 180 ? 0.7020 0.7071 0.8495 0.0120  0.0442  0.0267  180 PRO B CD  
3869 N N   . LYS B 181 ? 0.8908 0.9051 1.0601 0.0133  0.0618  0.0550  181 LYS B N   
3870 C CA  . LYS B 181 ? 0.8832 0.8979 1.0645 0.0148  0.0698  0.0610  181 LYS B CA  
3871 C C   . LYS B 181 ? 0.8594 0.8633 1.0390 0.0181  0.0732  0.0534  181 LYS B C   
3872 O O   . LYS B 181 ? 0.9325 0.9351 1.1234 0.0195  0.0794  0.0537  181 LYS B O   
3873 C CB  . LYS B 181 ? 0.9029 0.9225 1.0848 0.0139  0.0721  0.0724  181 LYS B CB  
3874 C CG  . LYS B 181 ? 0.8922 0.9243 1.0796 0.0104  0.0708  0.0819  181 LYS B CG  
3875 C CD  . LYS B 181 ? 0.9003 0.9399 1.1018 0.0095  0.0731  0.0833  181 LYS B CD  
3876 N N   . SER B 182 ? 0.8600 0.8568 1.0259 0.0193  0.0692  0.0465  182 SER B N   
3877 C CA  . SER B 182 ? 0.8647 0.8518 1.0269 0.0222  0.0716  0.0384  182 SER B CA  
3878 C C   . SER B 182 ? 0.8427 0.8250 0.9946 0.0223  0.0657  0.0269  182 SER B C   
3879 O O   . SER B 182 ? 0.8326 0.8163 0.9745 0.0212  0.0596  0.0255  182 SER B O   
3880 C CB  . SER B 182 ? 0.9120 0.8955 1.0675 0.0241  0.0731  0.0421  182 SER B CB  
3881 O OG  . SER B 182 ? 0.9513 0.9352 1.0938 0.0236  0.0665  0.0409  182 SER B OG  
3882 N N   . GLY B 183 ? 0.8262 0.8029 0.9811 0.0235  0.0679  0.0188  183 GLY B N   
3883 C CA  . GLY B 183 ? 0.8105 0.7826 0.9562 0.0237  0.0631  0.0079  183 GLY B CA  
3884 C C   . GLY B 183 ? 0.7718 0.7477 0.9181 0.0215  0.0582  0.0056  183 GLY B C   
3885 O O   . GLY B 183 ? 0.7537 0.7280 0.8896 0.0209  0.0527  -0.0003 183 GLY B O   
3886 N N   . ALA B 184 ? 1.0014 0.5693 0.6590 -0.0447 0.0536  -0.0147 184 ALA B N   
3887 C CA  . ALA B 184 ? 1.0233 0.5897 0.6725 -0.0510 0.0591  -0.0180 184 ALA B CA  
3888 C C   . ALA B 184 ? 1.0398 0.6086 0.6821 -0.0571 0.0695  -0.0259 184 ALA B C   
3889 O O   . ALA B 184 ? 1.0128 0.5836 0.6509 -0.0625 0.0758  -0.0292 184 ALA B O   
3890 C CB  . ALA B 184 ? 1.0594 0.6189 0.7005 -0.0519 0.0534  -0.0172 184 ALA B CB  
3891 N N   . ARG B 185 ? 1.0988 0.6697 0.7416 -0.0560 0.0708  -0.0293 185 ARG B N   
3892 C CA  . ARG B 185 ? 1.1241 0.7026 0.7643 -0.0602 0.0801  -0.0375 185 ARG B CA  
3893 C C   . ARG B 185 ? 1.1146 0.7090 0.7662 -0.0547 0.0804  -0.0392 185 ARG B C   
3894 O O   . ARG B 185 ? 1.0860 0.6774 0.7337 -0.0543 0.0781  -0.0420 185 ARG B O   
3895 C CB  . ARG B 185 ? 1.1403 0.7140 0.7702 -0.0653 0.0800  -0.0392 185 ARG B CB  
3896 C CG  . ARG B 185 ? 1.2187 0.8027 0.8487 -0.0706 0.0900  -0.0462 185 ARG B CG  
3897 C CD  . ARG B 185 ? 1.2449 0.8219 0.8647 -0.0767 0.0908  -0.0461 185 ARG B CD  
3898 N NE  . ARG B 185 ? 1.2726 0.8599 0.8954 -0.0802 0.0979  -0.0520 185 ARG B NE  
3899 C CZ  . ARG B 185 ? 1.2601 0.8494 0.8833 -0.0791 0.0962  -0.0542 185 ARG B CZ  
3900 N NH1 . ARG B 185 ? 1.2345 0.8154 0.8545 -0.0748 0.0874  -0.0512 185 ARG B NH1 
3901 N NH2 . ARG B 185 ? 1.2388 0.8399 0.8674 -0.0819 0.1028  -0.0595 185 ARG B NH2 
3902 N N   . VAL B 186 ? 1.0120 0.6345 0.6842 -0.0493 0.0817  -0.0352 186 VAL B N   
3903 C CA  . VAL B 186 ? 1.0086 0.6605 0.7002 -0.0423 0.0808  -0.0335 186 VAL B CA  
3904 C C   . VAL B 186 ? 1.0081 0.6740 0.7005 -0.0446 0.0898  -0.0424 186 VAL B C   
3905 O O   . VAL B 186 ? 0.9668 0.6342 0.6553 -0.0491 0.0981  -0.0482 186 VAL B O   
3906 C CB  . VAL B 186 ? 1.0008 0.6772 0.7132 -0.0359 0.0793  -0.0263 186 VAL B CB  
3907 C CG1 . VAL B 186 ? 0.9781 0.6826 0.7094 -0.0287 0.0775  -0.0239 186 VAL B CG1 
3908 C CG2 . VAL B 186 ? 0.9948 0.6565 0.7063 -0.0339 0.0711  -0.0180 186 VAL B CG2 
3909 N N   . MET B 187 ? 1.0270 0.7031 0.7248 -0.0413 0.0878  -0.0439 187 MET B N   
3910 C CA  . MET B 187 ? 1.0213 0.7072 0.7184 -0.0431 0.0950  -0.0524 187 MET B CA  
3911 C C   . MET B 187 ? 0.9285 0.6507 0.6477 -0.0369 0.0997  -0.0531 187 MET B C   
3912 O O   . MET B 187 ? 0.8567 0.5975 0.5923 -0.0303 0.0955  -0.0463 187 MET B O   
3913 C CB  . MET B 187 ? 1.0123 0.6865 0.7014 -0.0434 0.0893  -0.0543 187 MET B CB  
3914 C CG  . MET B 187 ? 1.0836 0.7202 0.7497 -0.0492 0.0838  -0.0540 187 MET B CG  
3915 S SD  . MET B 187 ? 1.0786 0.6944 0.7262 -0.0593 0.0919  -0.0588 187 MET B SD  
3916 C CE  . MET B 187 ? 1.0896 0.7257 0.7446 -0.0614 0.0995  -0.0660 187 MET B CE  
3917 N N   . SER B 188 ? 0.8539 0.5854 0.5729 -0.0390 0.1087  -0.0617 188 SER B N   
3918 C CA  . SER B 188 ? 0.8422 0.6066 0.5807 -0.0331 0.1142  -0.0640 188 SER B CA  
3919 C C   . SER B 188 ? 0.8656 0.6505 0.6190 -0.0258 0.1092  -0.0609 188 SER B C   
3920 O O   . SER B 188 ? 0.8202 0.5949 0.5671 -0.0265 0.1043  -0.0616 188 SER B O   
3921 C CB  . SER B 188 ? 0.8656 0.6320 0.5989 -0.0373 0.1250  -0.0751 188 SER B CB  
3922 O OG  . SER B 188 ? 0.8672 0.6174 0.5892 -0.0444 0.1289  -0.0778 188 SER B OG  
3923 N N   . LEU B 189 ? 0.8708 0.6845 0.6442 -0.0187 0.1099  -0.0576 189 LEU B N   
3924 C CA  . LEU B 189 ? 0.9008 0.7361 0.6903 -0.0113 0.1045  -0.0533 189 LEU B CA  
3925 C C   . LEU B 189 ? 0.8493 0.6941 0.6414 -0.0099 0.1065  -0.0600 189 LEU B C   
3926 O O   . LEU B 189 ? 0.8903 0.7366 0.6852 -0.0075 0.0993  -0.0579 189 LEU B O   
3927 C CB  . LEU B 189 ? 0.8634 0.7272 0.6728 -0.0044 0.1057  -0.0485 189 LEU B CB  
3928 C CG  . LEU B 189 ? 0.8513 0.7104 0.6631 -0.0035 0.0999  -0.0391 189 LEU B CG  
3929 C CD1 . LEU B 189 ? 0.8421 0.7304 0.6734 0.0034  0.1010  -0.0347 189 LEU B CD1 
3930 C CD2 . LEU B 189 ? 0.8103 0.6559 0.6186 -0.0032 0.0898  -0.0326 189 LEU B CD2 
3931 N N   . LEU B 190 ? 0.8439 0.6953 0.6355 -0.0112 0.1160  -0.0686 190 LEU B N   
3932 C CA  . LEU B 190 ? 0.8614 0.7222 0.6557 -0.0099 0.1191  -0.0760 190 LEU B CA  
3933 C C   . LEU B 190 ? 0.8995 0.7328 0.6727 -0.0182 0.1213  -0.0828 190 LEU B C   
3934 O O   . LEU B 190 ? 0.9165 0.7541 0.6902 -0.0177 0.1226  -0.0885 190 LEU B O   
3935 C CB  . LEU B 190 ? 0.8496 0.7374 0.6585 -0.0051 0.1285  -0.0818 190 LEU B CB  
3936 C CG  . LEU B 190 ? 0.8637 0.7766 0.6909 0.0020  0.1283  -0.0761 190 LEU B CG  
3937 C CD1 . LEU B 190 ? 0.8523 0.7930 0.6952 0.0081  0.1358  -0.0825 190 LEU B CD1 
3938 C CD2 . LEU B 190 ? 0.8743 0.7982 0.7127 0.0073  0.1186  -0.0665 190 LEU B CD2 
3939 N N   . GLU B 191 ? 0.9551 0.7607 0.7103 -0.0256 0.1218  -0.0823 191 GLU B N   
3940 C CA  . GLU B 191 ? 1.0231 0.8011 0.7588 -0.0341 0.1221  -0.0869 191 GLU B CA  
3941 C C   . GLU B 191 ? 1.0768 0.8232 0.7937 -0.0388 0.1152  -0.0816 191 GLU B C   
3942 O O   . GLU B 191 ? 1.1339 0.8634 0.8402 -0.0445 0.1174  -0.0811 191 GLU B O   
3943 C CB  . GLU B 191 ? 1.0226 0.8070 0.7659 -0.0385 0.1267  -0.0892 191 GLU B CB  
3944 N N   . PRO B 192 ? 1.0405 0.7823 0.7581 -0.0360 0.1047  -0.0763 192 PRO B N   
3945 C CA  . PRO B 192 ? 1.0552 0.7714 0.7606 -0.0385 0.0958  -0.0699 192 PRO B CA  
3946 C C   . PRO B 192 ? 1.1055 0.7840 0.7838 -0.0477 0.0959  -0.0738 192 PRO B C   
3947 O O   . PRO B 192 ? 1.1092 0.7641 0.7759 -0.0497 0.0886  -0.0692 192 PRO B O   
3948 C CB  . PRO B 192 ? 1.0530 0.7777 0.7679 -0.0326 0.0853  -0.0658 192 PRO B CB  
3949 C CG  . PRO B 192 ? 1.0582 0.8000 0.7801 -0.0307 0.0881  -0.0723 192 PRO B CG  
3950 C CD  . PRO B 192 ? 1.0595 0.8208 0.7901 -0.0301 0.1002  -0.0769 192 PRO B CD  
3951 N N   . THR B 193 ? 1.1132 0.7947 0.7910 -0.0523 0.1016  -0.0786 193 THR B N   
3952 C CA  . THR B 193 ? 1.1576 0.8202 0.8247 -0.0603 0.1005  -0.0766 193 THR B CA  
3953 C C   . THR B 193 ? 1.1182 0.7837 0.7875 -0.0648 0.1081  -0.0765 193 THR B C   
3954 O O   . THR B 193 ? 1.0772 0.7271 0.7366 -0.0713 0.1079  -0.0742 193 THR B O   
3955 C CB  . THR B 193 ? 1.1898 0.8559 0.8581 -0.0624 0.0999  -0.0799 193 THR B CB  
3956 O OG1 . THR B 193 ? 1.2216 0.9132 0.9056 -0.0607 0.1078  -0.0851 193 THR B OG1 
3957 C CG2 . THR B 193 ? 1.1522 0.8161 0.8190 -0.0582 0.0912  -0.0804 193 THR B CG2 
3958 N N   . LYS B 194 ? 1.0867 0.7732 0.7693 -0.0609 0.1141  -0.0787 194 LYS B N   
3959 C CA  . LYS B 194 ? 1.0887 0.7813 0.7764 -0.0642 0.1201  -0.0793 194 LYS B CA  
3960 C C   . LYS B 194 ? 1.0850 0.7726 0.7698 -0.0618 0.1192  -0.0758 194 LYS B C   
3961 O O   . LYS B 194 ? 1.1079 0.8080 0.7993 -0.0549 0.1194  -0.0756 194 LYS B O   
3962 C CB  . LYS B 194 ? 1.0889 0.8118 0.7968 -0.0608 0.1262  -0.0845 194 LYS B CB  
3963 N N   . LYS B 195 ? 1.0356 0.7057 0.7106 -0.0673 0.1182  -0.0726 195 LYS B N   
3964 C CA  . LYS B 195 ? 1.0504 0.7139 0.7224 -0.0657 0.1169  -0.0691 195 LYS B CA  
3965 C C   . LYS B 195 ? 0.9645 0.6535 0.6517 -0.0602 0.1222  -0.0717 195 LYS B C   
3966 O O   . LYS B 195 ? 0.8975 0.6083 0.5988 -0.0601 0.1273  -0.0761 195 LYS B O   
3967 C CB  . LYS B 195 ? 1.0798 0.7290 0.7439 -0.0728 0.1171  -0.0667 195 LYS B CB  
3968 C CG  . LYS B 195 ? 1.1174 0.7575 0.7778 -0.0717 0.1145  -0.0628 195 LYS B CG  
3969 C CD  . LYS B 195 ? 1.1570 0.7876 0.8116 -0.0784 0.1152  -0.0609 195 LYS B CD  
3970 C CE  . LYS B 195 ? 1.1265 0.7757 0.7924 -0.0818 0.1223  -0.0663 195 LYS B CE  
3971 N NZ  . LYS B 195 ? 1.0687 0.7344 0.7464 -0.0773 0.1243  -0.0683 195 LYS B NZ  
3972 N N   . MET B 196 ? 0.9441 0.6363 0.6355 -0.0547 0.1184  -0.0660 196 MET B N   
3973 C CA  . MET B 196 ? 0.9397 0.6614 0.6514 -0.0487 0.1207  -0.0645 196 MET B CA  
3974 C C   . MET B 196 ? 0.9597 0.6788 0.6675 -0.0537 0.1266  -0.0694 196 MET B C   
3975 O O   . MET B 196 ? 0.9217 0.6230 0.6207 -0.0574 0.1233  -0.0660 196 MET B O   
3976 C CB  . MET B 196 ? 0.9372 0.6689 0.6626 -0.0415 0.1116  -0.0530 196 MET B CB  
3977 C CG  . MET B 196 ? 0.8937 0.6587 0.6412 -0.0339 0.1131  -0.0509 196 MET B CG  
3978 S SD  . MET B 196 ? 0.8650 0.6421 0.6284 -0.0262 0.1032  -0.0375 196 MET B SD  
3979 C CE  . MET B 196 ? 0.8533 0.6238 0.6153 -0.0234 0.0957  -0.0337 196 MET B CE  
3980 N N   . SER B 197 ? 0.9947 0.7362 0.7158 -0.0532 0.1324  -0.0755 197 SER B N   
3981 C CA  . SER B 197 ? 1.0137 0.7626 0.7423 -0.0572 0.1342  -0.0785 197 SER B CA  
3982 C C   . SER B 197 ? 0.9566 0.7251 0.6972 -0.0515 0.1355  -0.0783 197 SER B C   
3983 O O   . SER B 197 ? 0.9680 0.7554 0.7190 -0.0442 0.1369  -0.0776 197 SER B O   
3984 C CB  . SER B 197 ? 0.9959 0.7585 0.7358 -0.0597 0.1365  -0.0841 197 SER B CB  
3985 O OG  . SER B 197 ? 0.9755 0.7490 0.7251 -0.0622 0.1378  -0.0876 197 SER B OG  
3986 N N   . LYS B 198 ? 0.9758 0.7409 0.7156 -0.0548 0.1349  -0.0787 198 LYS B N   
3987 C CA  . LYS B 198 ? 0.9677 0.7509 0.7187 -0.0501 0.1356  -0.0788 198 LYS B CA  
3988 C C   . LYS B 198 ? 0.9631 0.7716 0.7334 -0.0491 0.1367  -0.0853 198 LYS B C   
3989 O O   . LYS B 198 ? 1.0052 0.8297 0.7860 -0.0455 0.1364  -0.0865 198 LYS B O   
3990 C CB  . LYS B 198 ? 0.9748 0.7422 0.7162 -0.0534 0.1328  -0.0757 198 LYS B CB  
3991 C CG  . LYS B 198 ? 0.9758 0.7365 0.7157 -0.0613 0.1322  -0.0799 198 LYS B CG  
3992 C CD  . LYS B 198 ? 0.9853 0.7313 0.7160 -0.0635 0.1290  -0.0769 198 LYS B CD  
3993 C CE  . LYS B 198 ? 0.9641 0.7016 0.6924 -0.0718 0.1277  -0.0792 198 LYS B CE  
3994 N NZ  . LYS B 198 ? 0.9213 0.6805 0.6656 -0.0734 0.1296  -0.0860 198 LYS B NZ  
3995 N N   . SER B 199 ? 0.9904 0.8012 0.7644 -0.0520 0.1375  -0.0892 199 SER B N   
3996 C CA  . SER B 199 ? 1.0105 0.8428 0.8014 -0.0503 0.1377  -0.0951 199 SER B CA  
3997 C C   . SER B 199 ? 1.0350 0.8770 0.8325 -0.0471 0.1387  -0.0968 199 SER B C   
3998 O O   . SER B 199 ? 1.0364 0.8876 0.8425 -0.0479 0.1387  -0.1013 199 SER B O   
3999 C CB  . SER B 199 ? 0.9867 0.8113 0.7755 -0.0582 0.1374  -0.0986 199 SER B CB  
4000 O OG  . SER B 199 ? 0.9618 0.7678 0.7387 -0.0650 0.1386  -0.0978 199 SER B OG  
4001 N N   . ASP B 200 ? 1.0462 0.8861 0.8396 -0.0432 0.1391  -0.0932 200 ASP B N   
4002 C CA  . ASP B 200 ? 0.9912 0.8398 0.7902 -0.0399 0.1395  -0.0945 200 ASP B CA  
4003 C C   . ASP B 200 ? 1.0001 0.8778 0.8194 -0.0318 0.1387  -0.0975 200 ASP B C   
4004 O O   . ASP B 200 ? 0.9221 0.8135 0.7495 -0.0265 0.1380  -0.0964 200 ASP B O   
4005 C CB  . ASP B 200 ? 0.9510 0.7918 0.7414 -0.0370 0.1395  -0.0897 200 ASP B CB  
4006 C CG  . ASP B 200 ? 0.9116 0.7548 0.7033 -0.0358 0.1393  -0.0912 200 ASP B CG  
4007 O OD1 . ASP B 200 ? 0.8570 0.7216 0.6642 -0.0309 0.1392  -0.0944 200 ASP B OD1 
4008 O OD2 . ASP B 200 ? 0.8742 0.6973 0.6511 -0.0392 0.1385  -0.0891 200 ASP B OD2 
4009 N N   . ASP B 201 ? 1.1150 1.0008 0.9415 -0.0309 0.1384  -0.1010 201 ASP B N   
4010 C CA  . ASP B 201 ? 1.1707 1.0820 1.0148 -0.0223 0.1366  -0.1033 201 ASP B CA  
4011 C C   . ASP B 201 ? 1.1653 1.0920 1.0166 -0.0135 0.1361  -0.0997 201 ASP B C   
4012 O O   . ASP B 201 ? 1.1801 1.1266 1.0440 -0.0057 0.1343  -0.0994 201 ASP B O   
4013 C CB  . ASP B 201 ? 1.2133 1.1274 1.0614 -0.0229 0.1363  -0.1068 201 ASP B CB  
4014 C CG  . ASP B 201 ? 1.2193 1.1210 1.0623 -0.0313 0.1373  -0.1102 201 ASP B CG  
4015 O OD1 . ASP B 201 ? 1.2919 1.1890 1.1327 -0.0349 0.1372  -0.1108 201 ASP B OD1 
4016 O OD2 . ASP B 201 ? 1.1074 1.0047 0.9489 -0.0344 0.1382  -0.1122 201 ASP B OD2 
4017 N N   . ASN B 202 ? 1.1844 1.1013 1.0271 -0.0147 0.1373  -0.0968 202 ASN B N   
4018 C CA  . ASN B 202 ? 1.1190 1.0489 0.9673 -0.0073 0.1372  -0.0930 202 ASN B CA  
4019 C C   . ASN B 202 ? 1.0834 1.0033 0.9226 -0.0084 0.1388  -0.0878 202 ASN B C   
4020 O O   . ASN B 202 ? 1.1624 1.0585 0.9847 -0.0144 0.1397  -0.0858 202 ASN B O   
4021 C CB  . ASN B 202 ? 1.1037 1.0290 0.9481 -0.0077 0.1371  -0.0933 202 ASN B CB  
4022 C CG  . ASN B 202 ? 1.0561 1.0019 0.9118 0.0012  0.1362  -0.0907 202 ASN B CG  
4023 O OD1 . ASN B 202 ? 0.9838 0.9459 0.8491 0.0074  0.1361  -0.0876 202 ASN B OD1 
4024 N ND2 . ASN B 202 ? 1.0425 0.9884 0.8977 0.0020  0.1354  -0.0918 202 ASN B ND2 
4025 N N   . ARG B 203 ? 1.0591 0.9962 0.9087 -0.0023 0.1387  -0.0854 203 ARG B N   
4026 C CA  . ARG B 203 ? 1.0583 0.9892 0.9013 -0.0018 0.1405  -0.0794 203 ARG B CA  
4027 C C   . ARG B 203 ? 0.9988 0.9261 0.8364 0.0009  0.1418  -0.0740 203 ARG B C   
4028 O O   . ARG B 203 ? 0.9851 0.9028 0.8202 -0.0001 0.1346  -0.0644 203 ARG B O   
4029 C CB  . ARG B 203 ? 1.0235 0.9764 0.8809 0.0047  0.1400  -0.0781 203 ARG B CB  
4030 N N   . ASN B 204 ? 0.9527 0.8941 0.7997 0.0051  0.1409  -0.0755 204 ASN B N   
4031 C CA  . ASN B 204 ? 0.8925 0.8355 0.7410 0.0082  0.1367  -0.0691 204 ASN B CA  
4032 C C   . ASN B 204 ? 0.8435 0.7589 0.6761 0.0016  0.1311  -0.0658 204 ASN B C   
4033 O O   . ASN B 204 ? 0.8895 0.8043 0.7249 0.0037  0.1234  -0.0583 204 ASN B O   
4034 C CB  . ASN B 204 ? 0.8985 0.8612 0.7576 0.0136  0.1397  -0.0743 204 ASN B CB  
4035 C CG  . ASN B 204 ? 0.8580 0.8525 0.7390 0.0222  0.1385  -0.0732 204 ASN B CG  
4036 O OD1 . ASN B 204 ? 0.8360 0.8377 0.7210 0.0253  0.1398  -0.0683 204 ASN B OD1 
4037 N ND2 . ASN B 204 ? 0.8022 0.8142 0.6957 0.0269  0.1353  -0.0769 204 ASN B ND2 
4038 N N   . ASN B 205 ? 0.8406 0.7328 0.6563 -0.0063 0.1349  -0.0717 205 ASN B N   
4039 C CA  . ASN B 205 ? 0.8750 0.7376 0.6732 -0.0131 0.1301  -0.0690 205 ASN B CA  
4040 C C   . ASN B 205 ? 0.8081 0.6575 0.6023 -0.0148 0.1235  -0.0601 205 ASN B C   
4041 O O   . ASN B 205 ? 0.7738 0.6023 0.5573 -0.0180 0.1172  -0.0556 205 ASN B O   
4042 C CB  . ASN B 205 ? 0.9337 0.7763 0.7145 -0.0214 0.1373  -0.0792 205 ASN B CB  
4043 C CG  . ASN B 205 ? 0.9210 0.7695 0.7064 -0.0212 0.1365  -0.0836 205 ASN B CG  
4044 O OD1 . ASN B 205 ? 0.8470 0.6848 0.6230 -0.0212 0.1343  -0.0828 205 ASN B OD1 
4045 N ND2 . ASN B 205 ? 0.9190 0.7840 0.7185 -0.0207 0.1373  -0.0880 205 ASN B ND2 
4046 N N   . VAL B 206 ? 0.8310 0.6925 0.6340 -0.0125 0.1246  -0.0578 206 VAL B N   
4047 C CA  . VAL B 206 ? 0.8783 0.7271 0.6773 -0.0147 0.1196  -0.0508 206 VAL B CA  
4048 C C   . VAL B 206 ? 0.8342 0.7006 0.6493 -0.0077 0.1132  -0.0404 206 VAL B C   
4049 O O   . VAL B 206 ? 0.7688 0.6607 0.5990 -0.0014 0.1150  -0.0402 206 VAL B O   
4050 C CB  . VAL B 206 ? 0.9245 0.7687 0.7180 -0.0194 0.1256  -0.0574 206 VAL B CB  
4051 C CG1 . VAL B 206 ? 0.8859 0.7566 0.6948 -0.0141 0.1297  -0.0603 206 VAL B CG1 
4052 C CG2 . VAL B 206 ? 0.9530 0.7791 0.7390 -0.0232 0.1203  -0.0514 206 VAL B CG2 
4053 N N   . ILE B 207 ? 0.7888 0.6408 0.6001 -0.0088 0.1058  -0.0320 207 ILE B N   
4054 C CA  . ILE B 207 ? 0.7333 0.5971 0.5571 -0.0039 0.1002  -0.0223 207 ILE B CA  
4055 C C   . ILE B 207 ? 0.7271 0.5834 0.5472 -0.0072 0.1008  -0.0221 207 ILE B C   
4056 O O   . ILE B 207 ? 0.7481 0.5822 0.5572 -0.0116 0.0975  -0.0199 207 ILE B O   
4057 C CB  . ILE B 207 ? 0.7199 0.5730 0.5432 -0.0024 0.0912  -0.0133 207 ILE B CB  
4058 C CG1 . ILE B 207 ? 0.6984 0.5616 0.5271 0.0011  0.0896  -0.0139 207 ILE B CG1 
4059 C CG2 . ILE B 207 ? 0.7016 0.5647 0.5368 0.0020  0.0856  -0.0034 207 ILE B CG2 
4060 C CD1 . ILE B 207 ? 0.7161 0.5642 0.5406 0.0013  0.0811  -0.0084 207 ILE B CD1 
4061 N N   . GLY B 208 ? 0.6964 0.5711 0.5256 -0.0049 0.1050  -0.0253 208 GLY B N   
4062 C CA  . GLY B 208 ? 0.7172 0.5888 0.5451 -0.0075 0.1052  -0.0261 208 GLY B CA  
4063 C C   . GLY B 208 ? 0.7293 0.6037 0.5655 -0.0042 0.0972  -0.0146 208 GLY B C   
4064 O O   . GLY B 208 ? 0.7400 0.6314 0.5890 0.0019  0.0940  -0.0077 208 GLY B O   
4065 N N   . LEU B 209 ? 0.6448 0.5034 0.4741 -0.0082 0.0941  -0.0127 209 LEU B N   
4066 C CA  . LEU B 209 ? 0.6796 0.5384 0.5162 -0.0053 0.0861  -0.0018 209 LEU B CA  
4067 C C   . LEU B 209 ? 0.6447 0.5277 0.4967 -0.0002 0.0850  0.0015  209 LEU B C   
4068 O O   . LEU B 209 ? 0.6093 0.4991 0.4709 0.0041  0.0788  0.0116  209 LEU B O   
4069 C CB  . LEU B 209 ? 0.6565 0.4934 0.4827 -0.0107 0.0831  -0.0012 209 LEU B CB  
4070 C CG  . LEU B 209 ? 0.6790 0.4888 0.4898 -0.0151 0.0817  -0.0014 209 LEU B CG  
4071 C CD1 . LEU B 209 ? 0.6853 0.4764 0.4882 -0.0193 0.0782  0.0001  209 LEU B CD1 
4072 C CD2 . LEU B 209 ? 0.6824 0.4889 0.4963 -0.0109 0.0761  0.0066  209 LEU B CD2 
4073 N N   . LEU B 210 ? 0.6474 0.5424 0.5012 -0.0007 0.0909  -0.0073 210 LEU B N   
4074 C CA  . LEU B 210 ? 0.7085 0.6254 0.5753 0.0041  0.0902  -0.0058 210 LEU B CA  
4075 C C   . LEU B 210 ? 0.7239 0.6619 0.5990 0.0092  0.0953  -0.0098 210 LEU B C   
4076 O O   . LEU B 210 ? 0.6902 0.6460 0.5741 0.0128  0.0965  -0.0118 210 LEU B O   
4077 C CB  . LEU B 210 ? 0.7055 0.6205 0.5693 0.0005  0.0913  -0.0129 210 LEU B CB  
4078 C CG  . LEU B 210 ? 0.7159 0.6143 0.5748 -0.0034 0.0851  -0.0080 210 LEU B CG  
4079 C CD1 . LEU B 210 ? 0.7754 0.6734 0.6314 -0.0075 0.0866  -0.0170 210 LEU B CD1 
4080 C CD2 . LEU B 210 ? 0.6770 0.5810 0.5463 0.0014  0.0766  0.0053  210 LEU B CD2 
4081 N N   . GLU B 211 ? 0.7452 0.6817 0.6180 0.0097  0.0979  -0.0108 211 GLU B N   
4082 C CA  . GLU B 211 ? 0.7711 0.7281 0.6529 0.0151  0.1021  -0.0136 211 GLU B CA  
4083 C C   . GLU B 211 ? 0.6945 0.6676 0.5893 0.0213  0.0969  -0.0028 211 GLU B C   
4084 O O   . GLU B 211 ? 0.7279 0.6931 0.6232 0.0212  0.0904  0.0066  211 GLU B O   
4085 C CB  . GLU B 211 ? 0.8292 0.7794 0.7046 0.0136  0.1055  -0.0180 211 GLU B CB  
4086 C CG  . GLU B 211 ? 0.9167 0.8577 0.7815 0.0086  0.1131  -0.0308 211 GLU B CG  
4087 C CD  . GLU B 211 ? 0.9660 0.8969 0.8229 0.0063  0.1154  -0.0343 211 GLU B CD  
4088 O OE1 . GLU B 211 ? 0.9490 0.8836 0.8104 0.0095  0.1114  -0.0280 211 GLU B OE1 
4089 O OE2 . GLU B 211 ? 1.0741 0.9926 0.9198 0.0010  0.1210  -0.0437 211 GLU B OE2 
4090 N N   . ASP B 212 ? 0.6793 0.6746 0.5845 0.0268  0.0999  -0.0048 212 ASP B N   
4091 C CA  . ASP B 212 ? 0.6707 0.6832 0.5883 0.0327  0.0962  0.0044  212 ASP B CA  
4092 C C   . ASP B 212 ? 0.6799 0.6854 0.5962 0.0323  0.0930  0.0094  212 ASP B C   
4093 O O   . ASP B 212 ? 0.7141 0.7165 0.6259 0.0312  0.0967  0.0031  212 ASP B O   
4094 C CB  . ASP B 212 ? 0.6785 0.7145 0.6055 0.0384  0.1014  -0.0008 212 ASP B CB  
4095 C CG  . ASP B 212 ? 0.6989 0.7537 0.6383 0.0443  0.0984  0.0077  212 ASP B CG  
4096 O OD1 . ASP B 212 ? 0.7178 0.7701 0.6602 0.0444  0.0920  0.0182  212 ASP B OD1 
4097 O OD2 . ASP B 212 ? 0.8290 0.9015 0.7754 0.0490  0.1028  0.0034  212 ASP B OD2 
4098 N N   . PRO B 213 ? 0.7127 0.7149 0.6325 0.0330  0.0860  0.0201  213 PRO B N   
4099 C CA  . PRO B 213 ? 0.7120 0.7085 0.6316 0.0331  0.0821  0.0245  213 PRO B CA  
4100 C C   . PRO B 213 ? 0.7475 0.7611 0.6742 0.0369  0.0848  0.0215  213 PRO B C   
4101 O O   . PRO B 213 ? 0.8380 0.8430 0.7594 0.0352  0.0846  0.0183  213 PRO B O   
4102 C CB  . PRO B 213 ? 0.7032 0.7023 0.6303 0.0352  0.0752  0.0359  213 PRO B CB  
4103 C CG  . PRO B 213 ? 0.7094 0.7017 0.6338 0.0333  0.0742  0.0373  213 PRO B CG  
4104 C CD  . PRO B 213 ? 0.6861 0.6876 0.6096 0.0334  0.0809  0.0281  213 PRO B CD  
4105 N N   . LYS B 214 ? 0.7572 0.7946 0.6955 0.0421  0.0872  0.0221  214 LYS B N   
4106 C CA  . LYS B 214 ? 0.7419 0.7989 0.6890 0.0465  0.0897  0.0196  214 LYS B CA  
4107 C C   . LYS B 214 ? 0.7375 0.7901 0.6780 0.0449  0.0953  0.0087  214 LYS B C   
4108 O O   . LYS B 214 ? 0.7284 0.7849 0.6710 0.0459  0.0948  0.0070  214 LYS B O   
4109 C CB  . LYS B 214 ? 0.7137 0.7955 0.6728 0.0522  0.0922  0.0210  214 LYS B CB  
4110 N N   . SER B 215 ? 0.7684 0.8126 0.7011 0.0421  0.1004  0.0012  215 SER B N   
4111 C CA  . SER B 215 ? 0.7833 0.8204 0.7081 0.0396  0.1064  -0.0097 215 SER B CA  
4112 C C   . SER B 215 ? 0.8026 0.8164 0.7152 0.0340  0.1035  -0.0102 215 SER B C   
4113 O O   . SER B 215 ? 0.8472 0.8589 0.7561 0.0331  0.1064  -0.0168 215 SER B O   
4114 C CB  . SER B 215 ? 0.8210 0.8534 0.7400 0.0373  0.1121  -0.0177 215 SER B CB  
4115 O OG  . SER B 215 ? 0.8935 0.9149 0.8028 0.0335  0.1178  -0.0281 215 SER B OG  
4116 N N   . VAL B 216 ? 0.7876 0.7842 0.6942 0.0307  0.0974  -0.0031 216 VAL B N   
4117 C CA  . VAL B 216 ? 0.8100 0.7826 0.7045 0.0258  0.0935  -0.0027 216 VAL B CA  
4118 C C   . VAL B 216 ? 0.8026 0.7812 0.7027 0.0285  0.0887  0.0005  216 VAL B C   
4119 O O   . VAL B 216 ? 0.8315 0.7993 0.7239 0.0261  0.0884  -0.0043 216 VAL B O   
4120 C CB  . VAL B 216 ? 0.8648 0.8177 0.7522 0.0223  0.0883  0.0038  216 VAL B CB  
4121 C CG1 . VAL B 216 ? 0.8896 0.8166 0.7641 0.0178  0.0838  0.0043  216 VAL B CG1 
4122 C CG2 . VAL B 216 ? 0.8379 0.7847 0.7194 0.0190  0.0927  -0.0005 216 VAL B CG2 
4123 N N   . VAL B 217 ? 0.7962 0.7922 0.7096 0.0333  0.0847  0.0080  217 VAL B N   
4124 C CA  . VAL B 217 ? 0.7142 0.7203 0.6354 0.0363  0.0800  0.0105  217 VAL B CA  
4125 C C   . VAL B 217 ? 0.6411 0.6609 0.5659 0.0384  0.0845  0.0024  217 VAL B C   
4126 O O   . VAL B 217 ? 0.6230 0.6390 0.5460 0.0378  0.0811  0.0001  217 VAL B O   
4127 C CB  . VAL B 217 ? 0.7382 0.7646 0.6743 0.0412  0.0767  0.0191  217 VAL B CB  
4128 C CG1 . VAL B 217 ? 0.7269 0.7663 0.6723 0.0442  0.0722  0.0205  217 VAL B CG1 
4129 C CG2 . VAL B 217 ? 0.7012 0.7140 0.6347 0.0395  0.0718  0.0273  217 VAL B CG2 
4130 N N   . LYS B 218 ? 0.6336 0.6686 0.5632 0.0410  0.0917  -0.0024 218 LYS B N   
4131 C CA  . LYS B 218 ? 0.6431 0.6908 0.5762 0.0433  0.0970  -0.0110 218 LYS B CA  
4132 C C   . LYS B 218 ? 0.6816 0.7078 0.5998 0.0377  0.0992  -0.0190 218 LYS B C   
4133 O O   . LYS B 218 ? 0.6534 0.6838 0.5727 0.0386  0.0993  -0.0239 218 LYS B O   
4134 C CB  . LYS B 218 ? 0.6481 0.7144 0.5888 0.0474  0.1044  -0.0150 218 LYS B CB  
4135 N N   . LYS B 219 ? 0.6894 0.6927 0.5937 0.0320  0.1007  -0.0203 219 LYS B N   
4136 C CA  . LYS B 219 ? 0.6688 0.6487 0.5569 0.0257  0.1028  -0.0274 219 LYS B CA  
4137 C C   . LYS B 219 ? 0.6633 0.6260 0.5437 0.0230  0.0951  -0.0247 219 LYS B C   
4138 O O   . LYS B 219 ? 0.6222 0.5754 0.4946 0.0204  0.0957  -0.0309 219 LYS B O   
4139 C CB  . LYS B 219 ? 0.7290 0.6897 0.6047 0.0202  0.1060  -0.0291 219 LYS B CB  
4140 C CG  . LYS B 219 ? 0.7733 0.7460 0.6525 0.0214  0.1146  -0.0361 219 LYS B CG  
4141 C CD  . LYS B 219 ? 0.8069 0.7674 0.6794 0.0176  0.1152  -0.0348 219 LYS B CD  
4142 C CE  . LYS B 219 ? 0.8363 0.7997 0.7064 0.0161  0.1238  -0.0450 219 LYS B CE  
4143 N NZ  . LYS B 219 ? 0.9004 0.8439 0.7587 0.0098  0.1237  -0.0457 219 LYS B NZ  
4144 N N   . ILE B 220 ? 0.6565 0.6155 0.5396 0.0238  0.0877  -0.0160 220 ILE B N   
4145 C CA  . ILE B 220 ? 0.6773 0.6199 0.5539 0.0219  0.0794  -0.0135 220 ILE B CA  
4146 C C   . ILE B 220 ? 0.6717 0.6310 0.5579 0.0256  0.0765  -0.0159 220 ILE B C   
4147 O O   . ILE B 220 ? 0.6557 0.6009 0.5330 0.0230  0.0727  -0.0197 220 ILE B O   
4148 C CB  . ILE B 220 ? 0.7095 0.6457 0.5885 0.0226  0.0726  -0.0040 220 ILE B CB  
4149 C CG1 . ILE B 220 ? 0.7984 0.7158 0.6668 0.0184  0.0748  -0.0025 220 ILE B CG1 
4150 C CG2 . ILE B 220 ? 0.7080 0.6289 0.5819 0.0215  0.0636  -0.0023 220 ILE B CG2 
4151 C CD1 . ILE B 220 ? 0.7974 0.7055 0.6668 0.0187  0.0684  0.0064  220 ILE B CD1 
4152 N N   . LYS B 221 ? 0.6587 0.6478 0.5626 0.0318  0.0778  -0.0137 221 LYS B N   
4153 C CA  . LYS B 221 ? 0.6268 0.6367 0.5426 0.0361  0.0754  -0.0160 221 LYS B CA  
4154 C C   . LYS B 221 ? 0.6294 0.6391 0.5405 0.0351  0.0803  -0.0255 221 LYS B C   
4155 O O   . LYS B 221 ? 0.6055 0.6172 0.5178 0.0355  0.0759  -0.0289 221 LYS B O   
4156 C CB  . LYS B 221 ? 0.5767 0.6191 0.5120 0.0429  0.0773  -0.0120 221 LYS B CB  
4157 N N   . ARG B 222 ? 0.6294 0.6355 0.5348 0.0334  0.0889  -0.0303 222 ARG B N   
4158 C CA  . ARG B 222 ? 0.6993 0.7056 0.6008 0.0324  0.0949  -0.0399 222 ARG B CA  
4159 C C   . ARG B 222 ? 0.7237 0.6976 0.6041 0.0246  0.0944  -0.0444 222 ARG B C   
4160 O O   . ARG B 222 ? 0.8165 0.7870 0.6913 0.0227  0.0995  -0.0525 222 ARG B O   
4161 C CB  . ARG B 222 ? 0.6779 0.6986 0.5850 0.0350  0.1049  -0.0442 222 ARG B CB  
4162 N N   . ALA B 223 ? 0.6988 0.6490 0.5677 0.0202  0.0882  -0.0393 223 ALA B N   
4163 C CA  . ALA B 223 ? 0.7028 0.6201 0.5504 0.0127  0.0871  -0.0429 223 ALA B CA  
4164 C C   . ALA B 223 ? 0.6976 0.6103 0.5414 0.0119  0.0824  -0.0475 223 ALA B C   
4165 O O   . ALA B 223 ? 0.6850 0.6115 0.5399 0.0162  0.0755  -0.0450 223 ALA B O   
4166 C CB  . ALA B 223 ? 0.7152 0.6103 0.5537 0.0096  0.0806  -0.0359 223 ALA B CB  
4167 N N   . VAL B 224 ? 0.7461 0.6397 0.5744 0.0064  0.0860  -0.0547 224 VAL B N   
4168 C CA  . VAL B 224 ? 0.7584 0.6452 0.5810 0.0049  0.0816  -0.0599 224 VAL B CA  
4169 C C   . VAL B 224 ? 0.7522 0.6167 0.5646 0.0024  0.0703  -0.0562 224 VAL B C   
4170 O O   . VAL B 224 ? 0.8327 0.6757 0.6341 -0.0010 0.0683  -0.0520 224 VAL B O   
4171 C CB  . VAL B 224 ? 0.7631 0.6338 0.5705 -0.0009 0.0889  -0.0687 224 VAL B CB  
4172 C CG1 . VAL B 224 ? 0.7437 0.6385 0.5630 0.0025  0.0997  -0.0738 224 VAL B CG1 
4173 C CG2 . VAL B 224 ? 0.8031 0.6397 0.5882 -0.0091 0.0905  -0.0687 224 VAL B CG2 
4174 N N   . THR B 225 ? 0.7339 0.6045 0.5509 0.0046  0.0627  -0.0583 225 THR B N   
4175 C CA  . THR B 225 ? 0.7880 0.6401 0.5973 0.0032  0.0506  -0.0563 225 THR B CA  
4176 C C   . THR B 225 ? 0.8332 0.6724 0.6313 -0.0001 0.0470  -0.0639 225 THR B C   
4177 O O   . THR B 225 ? 0.8547 0.6758 0.6371 -0.0056 0.0531  -0.0688 225 THR B O   
4178 C CB  . THR B 225 ? 0.7441 0.6196 0.5728 0.0098  0.0431  -0.0510 225 THR B CB  
4179 O OG1 . THR B 225 ? 0.6773 0.5864 0.5251 0.0154  0.0449  -0.0536 225 THR B OG1 
4180 C CG2 . THR B 225 ? 0.7741 0.6562 0.6103 0.0119  0.0457  -0.0430 225 THR B CG2 
4181 N N   . ASP B 226 ? 0.8519 0.7015 0.6583 0.0032  0.0376  -0.0654 226 ASP B N   
4182 C CA  . ASP B 226 ? 0.8405 0.6794 0.6376 0.0005  0.0327  -0.0727 226 ASP B CA  
4183 C C   . ASP B 226 ? 0.7786 0.6477 0.5957 0.0066  0.0261  -0.0749 226 ASP B C   
4184 O O   . ASP B 226 ? 0.7742 0.6700 0.6110 0.0126  0.0244  -0.0707 226 ASP B O   
4185 C CB  . ASP B 226 ? 0.8542 0.6540 0.6283 -0.0054 0.0237  -0.0733 226 ASP B CB  
4186 C CG  . ASP B 226 ? 0.8956 0.6913 0.6736 -0.0029 0.0146  -0.0676 226 ASP B CG  
4187 O OD1 . ASP B 226 ? 0.8526 0.6692 0.6467 0.0021  0.0068  -0.0674 226 ASP B OD1 
4188 O OD2 . ASP B 226 ? 0.9375 0.7097 0.7028 -0.0060 0.0153  -0.0636 226 ASP B OD2 
4189 N N   . SER B 227 ? 0.7485 0.6124 0.5598 0.0049  0.0222  -0.0818 227 SER B N   
4190 C CA  . SER B 227 ? 0.7384 0.6282 0.5668 0.0100  0.0150  -0.0852 227 SER B CA  
4191 C C   . SER B 227 ? 0.7619 0.6418 0.5881 0.0100  -0.0005 -0.0856 227 SER B C   
4192 O O   . SER B 227 ? 0.6844 0.5813 0.5218 0.0131  -0.0086 -0.0897 227 SER B O   
4193 C CB  . SER B 227 ? 0.7335 0.6224 0.5568 0.0081  0.0180  -0.0929 227 SER B CB  
4194 O OG  . SER B 227 ? 0.7803 0.6302 0.5770 0.0002  0.0145  -0.0964 227 SER B OG  
4195 N N   . ASP B 228 ? 0.7701 0.6227 0.5823 0.0067  -0.0051 -0.0819 228 ASP B N   
4196 C CA  . ASP B 228 ? 0.8154 0.6541 0.6233 0.0064  -0.0200 -0.0833 228 ASP B CA  
4197 C C   . ASP B 228 ? 0.8161 0.6896 0.6491 0.0131  -0.0272 -0.0831 228 ASP B C   
4198 O O   . ASP B 228 ? 0.7586 0.6591 0.6099 0.0178  -0.0216 -0.0777 228 ASP B O   
4199 C CB  . ASP B 228 ? 0.8231 0.6337 0.6175 0.0038  -0.0222 -0.0782 228 ASP B CB  
4200 C CG  . ASP B 228 ? 0.8705 0.6406 0.6367 -0.0035 -0.0193 -0.0798 228 ASP B CG  
4201 O OD1 . ASP B 228 ? 0.8858 0.6506 0.6430 -0.0070 -0.0132 -0.0841 228 ASP B OD1 
4202 O OD2 . ASP B 228 ? 0.8820 0.6254 0.6350 -0.0058 -0.0229 -0.0769 228 ASP B OD2 
4203 N N   . GLU B 229 ? 0.8026 0.6754 0.6362 0.0134  -0.0398 -0.0893 229 GLU B N   
4204 C CA  . GLU B 229 ? 0.7979 0.7024 0.6544 0.0191  -0.0483 -0.0905 229 GLU B CA  
4205 C C   . GLU B 229 ? 0.8268 0.7120 0.6758 0.0177  -0.0644 -0.0946 229 GLU B C   
4206 O O   . GLU B 229 ? 0.8675 0.7359 0.7047 0.0149  -0.0733 -0.1016 229 GLU B O   
4207 C CB  . GLU B 229 ? 0.7824 0.7154 0.6533 0.0222  -0.0478 -0.0957 229 GLU B CB  
4208 C CG  . GLU B 229 ? 0.7357 0.7084 0.6339 0.0288  -0.0536 -0.0960 229 GLU B CG  
4209 C CD  . GLU B 229 ? 0.7212 0.7175 0.6356 0.0330  -0.0448 -0.0880 229 GLU B CD  
4210 O OE1 . GLU B 229 ? 0.6892 0.6919 0.6119 0.0347  -0.0512 -0.0853 229 GLU B OE1 
4211 O OE2 . GLU B 229 ? 0.6511 0.6582 0.5691 0.0344  -0.0317 -0.0846 229 GLU B OE2 
4212 N N   . PRO B 230 ? 0.8742 0.7616 0.7300 0.0197  -0.0684 -0.0906 230 PRO B N   
4213 C CA  . PRO B 230 ? 0.8354 0.7423 0.7052 0.0230  -0.0591 -0.0821 230 PRO B CA  
4214 C C   . PRO B 230 ? 0.8217 0.7069 0.6769 0.0199  -0.0476 -0.0758 230 PRO B C   
4215 O O   . PRO B 230 ? 0.8123 0.6615 0.6444 0.0148  -0.0487 -0.0774 230 PRO B O   
4216 C CB  . PRO B 230 ? 0.8905 0.7977 0.7672 0.0249  -0.0697 -0.0816 230 PRO B CB  
4217 C CG  . PRO B 230 ? 0.9327 0.8042 0.7893 0.0210  -0.0820 -0.0883 230 PRO B CG  
4218 C CD  . PRO B 230 ? 0.9042 0.7735 0.7539 0.0189  -0.0836 -0.0951 230 PRO B CD  
4219 N N   . PRO B 231 ? 0.7826 0.6896 0.6509 0.0228  -0.0369 -0.0688 231 PRO B N   
4220 C CA  . PRO B 231 ? 0.8148 0.7028 0.6714 0.0202  -0.0278 -0.0627 231 PRO B CA  
4221 C C   . PRO B 231 ? 0.8596 0.7218 0.7064 0.0188  -0.0354 -0.0601 231 PRO B C   
4222 O O   . PRO B 231 ? 0.7902 0.6655 0.6501 0.0221  -0.0425 -0.0590 231 PRO B O   
4223 C CB  . PRO B 231 ? 0.7743 0.6957 0.6507 0.0248  -0.0176 -0.0564 231 PRO B CB  
4224 C CG  . PRO B 231 ? 0.7663 0.7224 0.6620 0.0292  -0.0189 -0.0602 231 PRO B CG  
4225 C CD  . PRO B 231 ? 0.7543 0.7040 0.6484 0.0287  -0.0330 -0.0666 231 PRO B CD  
4226 N N   . VAL B 232 ? 0.9039 0.7298 0.7282 0.0139  -0.0341 -0.0598 232 VAL B N   
4227 C CA  . VAL B 232 ? 0.9007 0.6981 0.7135 0.0127  -0.0408 -0.0577 232 VAL B CA  
4228 C C   . VAL B 232 ? 0.9120 0.6898 0.7121 0.0097  -0.0314 -0.0520 232 VAL B C   
4229 O O   . VAL B 232 ? 0.8449 0.6128 0.6331 0.0058  -0.0238 -0.0535 232 VAL B O   
4230 C CB  . VAL B 232 ? 0.9248 0.6908 0.7191 0.0095  -0.0527 -0.0653 232 VAL B CB  
4231 N N   . VAL B 233 ? 0.8859 0.6590 0.6893 0.0115  -0.0322 -0.0459 233 VAL B N   
4232 C CA  . VAL B 233 ? 0.9333 0.6885 0.7264 0.0092  -0.0247 -0.0400 233 VAL B CA  
4233 C C   . VAL B 233 ? 0.9090 0.6211 0.6782 0.0054  -0.0313 -0.0426 233 VAL B C   
4234 O O   . VAL B 233 ? 0.9396 0.6387 0.7080 0.0074  -0.0399 -0.0419 233 VAL B O   
4235 C CB  . VAL B 233 ? 0.8733 0.6463 0.6828 0.0134  -0.0220 -0.0316 233 VAL B CB  
4236 C CG1 . VAL B 233 ? 0.8793 0.6381 0.6801 0.0111  -0.0138 -0.0258 233 VAL B CG1 
4237 C CG2 . VAL B 233 ? 0.8341 0.6489 0.6670 0.0176  -0.0173 -0.0296 233 VAL B CG2 
4238 N N   . ARG B 234 ? 0.9173 0.6079 0.6673 0.0000  -0.0270 -0.0458 234 ARG B N   
4239 C CA  . ARG B 234 ? 0.9398 0.5882 0.6645 -0.0043 -0.0324 -0.0489 234 ARG B CA  
4240 C C   . ARG B 234 ? 0.9717 0.6034 0.6801 -0.0100 -0.0220 -0.0479 234 ARG B C   
4241 O O   . ARG B 234 ? 0.8840 0.5336 0.5970 -0.0115 -0.0125 -0.0488 234 ARG B O   
4242 C CB  . ARG B 234 ? 0.8843 0.5206 0.5994 -0.0059 -0.0424 -0.0576 234 ARG B CB  
4243 N N   . TYR B 235 ? 1.0316 0.6291 0.7212 -0.0129 -0.0237 -0.0468 235 TYR B N   
4244 C CA  . TYR B 235 ? 1.0960 0.6793 0.7713 -0.0187 -0.0146 -0.0456 235 TYR B CA  
4245 C C   . TYR B 235 ? 1.1503 0.7330 0.8188 -0.0233 -0.0153 -0.0489 235 TYR B C   
4246 O O   . TYR B 235 ? 1.1711 0.7495 0.8386 -0.0232 -0.0230 -0.0474 235 TYR B O   
4247 C CB  . TYR B 235 ? 1.1322 0.7069 0.8068 -0.0185 -0.0155 -0.0383 235 TYR B CB  
4248 C CG  . TYR B 235 ? 1.1452 0.7157 0.8136 -0.0222 -0.0046 -0.0353 235 TYR B CG  
4249 C CD1 . TYR B 235 ? 1.1086 0.6865 0.7841 -0.0202 0.0024  -0.0327 235 TYR B CD1 
4250 C CD2 . TYR B 235 ? 1.1012 0.6654 0.7596 -0.0274 -0.0013 -0.0344 235 TYR B CD2 
4251 C CE1 . TYR B 235 ? 1.1131 0.6897 0.7847 -0.0236 0.0120  -0.0303 235 TYR B CE1 
4252 C CE2 . TYR B 235 ? 1.0830 0.6446 0.7364 -0.0309 0.0083  -0.0324 235 TYR B CE2 
4253 C CZ  . TYR B 235 ? 1.0945 0.6599 0.7533 -0.0294 0.0148  -0.0310 235 TYR B CZ  
4254 O OH  . TYR B 235 ? 1.1482 0.7125 0.8032 -0.0330 0.0239  -0.0297 235 TYR B OH  
4255 N N   . ASP B 236 ? 1.2409 0.8289 0.9053 -0.0267 -0.0071 -0.0534 236 ASP B N   
4256 C CA  . ASP B 236 ? 1.2935 0.8809 0.9521 -0.0310 -0.0069 -0.0559 236 ASP B CA  
4257 C C   . ASP B 236 ? 1.3386 0.9273 0.9908 -0.0361 0.0060  -0.0576 236 ASP B C   
4258 O O   . ASP B 236 ? 1.5847 1.1842 1.2388 -0.0372 0.0103  -0.0632 236 ASP B O   
4259 C CB  . ASP B 236 ? 1.3479 0.9465 1.0136 -0.0286 -0.0144 -0.0617 236 ASP B CB  
4260 C CG  . ASP B 236 ? 1.3261 0.9224 0.9875 -0.0321 -0.0172 -0.0629 236 ASP B CG  
4261 O OD1 . ASP B 236 ? 1.3526 0.9386 1.0043 -0.0366 -0.0124 -0.0599 236 ASP B OD1 
4262 O OD2 . ASP B 236 ? 1.3615 0.9669 1.0295 -0.0302 -0.0244 -0.0672 236 ASP B OD2 
4263 N N   . VAL B 237 ? 1.2254 0.8047 0.8709 -0.0392 0.0116  -0.0530 237 VAL B N   
4264 C CA  . VAL B 237 ? 1.2602 0.8416 0.9012 -0.0438 0.0245  -0.0543 237 VAL B CA  
4265 C C   . VAL B 237 ? 1.2775 0.8663 0.9169 -0.0476 0.0300  -0.0596 237 VAL B C   
4266 O O   . VAL B 237 ? 1.2250 0.8253 0.8676 -0.0488 0.0403  -0.0637 237 VAL B O   
4267 C CB  . VAL B 237 ? 1.2610 0.8302 0.8934 -0.0474 0.0272  -0.0487 237 VAL B CB  
4268 C CG1 . VAL B 237 ? 1.2251 0.7979 0.8547 -0.0521 0.0401  -0.0504 237 VAL B CG1 
4269 C CG2 . VAL B 237 ? 1.2525 0.8169 0.8886 -0.0432 0.0223  -0.0433 237 VAL B CG2 
4270 N N   . GLN B 238 ? 1.3203 0.9041 0.9560 -0.0491 0.0233  -0.0596 238 GLN B N   
4271 C CA  . GLN B 238 ? 1.3593 0.9490 0.9940 -0.0526 0.0273  -0.0640 238 GLN B CA  
4272 C C   . GLN B 238 ? 1.2648 0.8724 0.9106 -0.0487 0.0265  -0.0705 238 GLN B C   
4273 O O   . GLN B 238 ? 1.3086 0.9282 0.9579 -0.0503 0.0341  -0.0752 238 GLN B O   
4274 C CB  . GLN B 238 ? 1.3292 0.9074 0.9560 -0.0549 0.0200  -0.0617 238 GLN B CB  
4275 N N   . ASN B 239 ? 1.1381 0.7491 0.7902 -0.0434 0.0174  -0.0709 239 ASN B N   
4276 C CA  . ASN B 239 ? 1.1218 0.7507 0.7841 -0.0389 0.0146  -0.0771 239 ASN B CA  
4277 C C   . ASN B 239 ? 1.0539 0.6961 0.7239 -0.0334 0.0177  -0.0787 239 ASN B C   
4278 O O   . ASN B 239 ? 1.0791 0.7524 0.7686 -0.0284 0.0171  -0.0801 239 ASN B O   
4279 C CB  . ASN B 239 ? 1.1342 0.7610 0.7996 -0.0368 0.0005  -0.0773 239 ASN B CB  
4280 C CG  . ASN B 239 ? 1.1263 0.7425 0.7847 -0.0414 -0.0018 -0.0754 239 ASN B CG  
4281 O OD1 . ASN B 239 ? 1.1173 0.7402 0.7763 -0.0437 0.0020  -0.0791 239 ASN B OD1 
4282 N ND2 . ASN B 239 ? 1.1686 0.7689 0.8199 -0.0424 -0.0071 -0.0697 239 ASN B ND2 
4283 N N   . LYS B 240 ? 1.0314 0.6705 0.7032 -0.0326 0.0204  -0.0723 240 LYS B N   
4284 C CA  . LYS B 240 ? 0.9476 0.6177 0.6437 -0.0255 0.0216  -0.0660 240 LYS B CA  
4285 C C   . LYS B 240 ? 0.9719 0.6419 0.6682 -0.0268 0.0312  -0.0610 240 LYS B C   
4286 O O   . LYS B 240 ? 0.8927 0.5660 0.5969 -0.0234 0.0287  -0.0545 240 LYS B O   
4287 C CB  . LYS B 240 ? 0.9425 0.6097 0.6442 -0.0212 0.0090  -0.0626 240 LYS B CB  
4288 C CG  . LYS B 240 ? 0.9158 0.5893 0.6221 -0.0189 -0.0017 -0.0677 240 LYS B CG  
4289 C CD  . LYS B 240 ? 0.8971 0.5717 0.6119 -0.0141 -0.0136 -0.0649 240 LYS B CD  
4290 C CE  . LYS B 240 ? 0.9219 0.6317 0.6627 -0.0076 -0.0109 -0.0588 240 LYS B CE  
4291 N NZ  . LYS B 240 ? 0.8435 0.5910 0.6055 -0.0032 -0.0096 -0.0609 240 LYS B NZ  
4292 N N   . ALA B 241 ? 0.9541 0.6214 0.6427 -0.0315 0.0421  -0.0646 241 ALA B N   
4293 C CA  . ALA B 241 ? 0.9873 0.6505 0.6725 -0.0341 0.0511  -0.0618 241 ALA B CA  
4294 C C   . ALA B 241 ? 0.9353 0.6300 0.6440 -0.0276 0.0543  -0.0558 241 ALA B C   
4295 O O   . ALA B 241 ? 0.9504 0.6394 0.6591 -0.0274 0.0548  -0.0502 241 ALA B O   
4296 C CB  . ALA B 241 ? 0.9759 0.6344 0.6506 -0.0402 0.0623  -0.0685 241 ALA B CB  
4297 N N   . GLY B 242 ? 0.8587 0.5860 0.5871 -0.0221 0.0561  -0.0568 242 GLY B N   
4298 C CA  . GLY B 242 ? 0.7991 0.5576 0.5498 -0.0157 0.0590  -0.0514 242 GLY B CA  
4299 C C   . GLY B 242 ? 0.7733 0.5328 0.5320 -0.0115 0.0500  -0.0437 242 GLY B C   
4300 O O   . GLY B 242 ? 0.7281 0.4919 0.4925 -0.0101 0.0521  -0.0379 242 GLY B O   
4301 N N   . VAL B 243 ? 0.7342 0.4895 0.4931 -0.0097 0.0398  -0.0443 243 VAL B N   
4302 C CA  . VAL B 243 ? 0.7402 0.4960 0.5067 -0.0058 0.0305  -0.0386 243 VAL B CA  
4303 C C   . VAL B 243 ? 0.8073 0.5329 0.5589 -0.0090 0.0283  -0.0347 243 VAL B C   
4304 O O   . VAL B 243 ? 0.7439 0.4759 0.5051 -0.0057 0.0267  -0.0280 243 VAL B O   
4305 C CB  . VAL B 243 ? 0.7467 0.5006 0.5139 -0.0041 0.0194  -0.0422 243 VAL B CB  
4306 C CG1 . VAL B 243 ? 0.7511 0.4918 0.5179 -0.0020 0.0088  -0.0383 243 VAL B CG1 
4307 C CG2 . VAL B 243 ? 0.7750 0.5661 0.5638 0.0012  0.0200  -0.0438 243 VAL B CG2 
4308 N N   . SER B 244 ? 0.7992 0.4927 0.5279 -0.0153 0.0280  -0.0391 244 SER B N   
4309 C CA  . SER B 244 ? 0.8265 0.4880 0.5385 -0.0187 0.0257  -0.0364 244 SER B CA  
4310 C C   . SER B 244 ? 0.8414 0.5093 0.5581 -0.0190 0.0337  -0.0313 244 SER B C   
4311 O O   . SER B 244 ? 0.8301 0.4923 0.5497 -0.0168 0.0301  -0.0252 244 SER B O   
4312 C CB  . SER B 244 ? 0.8870 0.5160 0.5735 -0.0260 0.0261  -0.0427 244 SER B CB  
4313 O OG  . SER B 244 ? 0.9447 0.5663 0.6259 -0.0259 0.0179  -0.0478 244 SER B OG  
4314 N N   . ASN B 245 ? 0.8266 0.5066 0.5444 -0.0215 0.0441  -0.0343 245 ASN B N   
4315 C CA  . ASN B 245 ? 0.8279 0.5159 0.5507 -0.0219 0.0516  -0.0309 245 ASN B CA  
4316 C C   . ASN B 245 ? 0.8262 0.5388 0.5702 -0.0151 0.0493  -0.0232 245 ASN B C   
4317 O O   . ASN B 245 ? 0.8675 0.5759 0.6126 -0.0149 0.0498  -0.0180 245 ASN B O   
4318 C CB  . ASN B 245 ? 0.8053 0.5071 0.5291 -0.0247 0.0628  -0.0367 245 ASN B CB  
4319 C CG  . ASN B 245 ? 0.8731 0.5766 0.5973 -0.0267 0.0700  -0.0350 245 ASN B CG  
4320 O OD1 . ASN B 245 ? 0.8663 0.5446 0.5755 -0.0315 0.0698  -0.0344 245 ASN B OD1 
4321 N ND2 . ASN B 245 ? 0.7994 0.5320 0.5402 -0.0232 0.0762  -0.0349 245 ASN B ND2 
4322 N N   . LEU B 246 ? 0.8751 0.6129 0.6356 -0.0097 0.0467  -0.0227 246 LEU B N   
4323 C CA  . LEU B 246 ? 0.8986 0.6601 0.6793 -0.0033 0.0437  -0.0156 246 LEU B CA  
4324 C C   . LEU B 246 ? 0.9523 0.6971 0.7310 -0.0016 0.0342  -0.0102 246 LEU B C   
4325 O O   . LEU B 246 ? 0.9477 0.6996 0.7359 0.0013  0.0335  -0.0033 246 LEU B O   
4326 C CB  . LEU B 246 ? 0.9197 0.7102 0.7170 0.0016  0.0424  -0.0172 246 LEU B CB  
4327 C CG  . LEU B 246 ? 0.9089 0.7237 0.7146 0.0024  0.0517  -0.0215 246 LEU B CG  
4328 C CD1 . LEU B 246 ? 0.8649 0.6994 0.6810 0.0059  0.0490  -0.0253 246 LEU B CD1 
4329 C CD2 . LEU B 246 ? 0.8944 0.7320 0.7148 0.0059  0.0572  -0.0164 246 LEU B CD2 
4330 N N   . LEU B 247 ? 0.9223 0.6460 0.6895 -0.0030 0.0265  -0.0136 247 LEU B N   
4331 C CA  . LEU B 247 ? 0.9931 0.6959 0.7554 -0.0016 0.0172  -0.0103 247 LEU B CA  
4332 C C   . LEU B 247 ? 1.0807 0.7603 0.8316 -0.0042 0.0187  -0.0066 247 LEU B C   
4333 O O   . LEU B 247 ? 1.0927 0.7693 0.8496 -0.0009 0.0143  -0.0005 247 LEU B O   
4334 C CB  . LEU B 247 ? 0.9913 0.6720 0.7399 -0.0034 0.0090  -0.0164 247 LEU B CB  
4335 C CG  . LEU B 247 ? 0.9150 0.6150 0.6764 0.0005  0.0028  -0.0191 247 LEU B CG  
4336 C CD1 . LEU B 247 ? 0.9488 0.6256 0.6940 -0.0024 -0.0044 -0.0266 247 LEU B CD1 
4337 C CD2 . LEU B 247 ? 0.9227 0.6330 0.6991 0.0061  -0.0038 -0.0138 247 LEU B CD2 
4338 N N   . ASP B 248 ? 1.0426 0.7066 0.7778 -0.0101 0.0249  -0.0104 248 ASP B N   
4339 C CA  . ASP B 248 ? 1.0503 0.6938 0.7745 -0.0133 0.0273  -0.0077 248 ASP B CA  
4340 C C   . ASP B 248 ? 1.0503 0.7161 0.7906 -0.0105 0.0321  -0.0014 248 ASP B C   
4341 O O   . ASP B 248 ? 1.0783 0.7346 0.8191 -0.0092 0.0293  0.0041  248 ASP B O   
4342 C CB  . ASP B 248 ? 1.0547 0.6794 0.7592 -0.0208 0.0336  -0.0142 248 ASP B CB  
4343 N N   . ILE B 249 ? 0.9637 0.6588 0.7171 -0.0093 0.0388  -0.0024 249 ILE B N   
4344 C CA  . ILE B 249 ? 0.9205 0.6393 0.6904 -0.0060 0.0426  0.0033  249 ILE B CA  
4345 C C   . ILE B 249 ? 0.8983 0.6263 0.6826 0.0001  0.0354  0.0110  249 ILE B C   
4346 O O   . ILE B 249 ? 0.8621 0.5910 0.6519 0.0017  0.0347  0.0172  249 ILE B O   
4347 C CB  . ILE B 249 ? 0.8194 0.5680 0.6008 -0.0050 0.0505  0.0000  249 ILE B CB  
4348 C CG1 . ILE B 249 ? 0.7938 0.5339 0.5625 -0.0111 0.0590  -0.0070 249 ILE B CG1 
4349 C CG2 . ILE B 249 ? 0.8068 0.5816 0.6072 -0.0002 0.0520  0.0065  249 ILE B CG2 
4350 C CD1 . ILE B 249 ? 0.7785 0.5431 0.5555 -0.0103 0.0666  -0.0125 249 ILE B CD1 
4351 N N   . LEU B 250 ? 0.9365 0.6709 0.7267 0.0032  0.0298  0.0103  250 LEU B N   
4352 C CA  . LEU B 250 ? 0.9670 0.7092 0.7702 0.0086  0.0227  0.0162  250 LEU B CA  
4353 C C   . LEU B 250 ? 1.0220 0.7373 0.8169 0.0088  0.0165  0.0198  250 LEU B C   
4354 O O   . LEU B 250 ? 1.0510 0.7728 0.8566 0.0123  0.0144  0.0268  250 LEU B O   
4355 C CB  . LEU B 250 ? 0.9071 0.6563 0.7146 0.0108  0.0172  0.0125  250 LEU B CB  
4356 N N   . SER B 251 ? 1.0844 0.7694 0.8600 0.0051  0.0136  0.0150  251 SER B N   
4357 C CA  . SER B 251 ? 1.1015 0.7566 0.8661 0.0051  0.0076  0.0171  251 SER B CA  
4358 C C   . SER B 251 ? 1.1196 0.7724 0.8858 0.0047  0.0109  0.0229  251 SER B C   
4359 O O   . SER B 251 ? 1.0767 0.7279 0.8508 0.0088  0.0064  0.0290  251 SER B O   
4360 C CB  . SER B 251 ? 1.1175 0.7411 0.8588 0.0000  0.0060  0.0101  251 SER B CB  
4361 O OG  . SER B 251 ? 1.1569 0.7503 0.8858 -0.0003 0.0012  0.0117  251 SER B OG  
4362 N N   . ALA B 252 ? 1.1462 0.7998 0.9055 -0.0001 0.0187  0.0205  252 ALA B N   
4363 C CA  . ALA B 252 ? 1.1798 0.8285 0.9378 -0.0016 0.0217  0.0242  252 ALA B CA  
4364 C C   . ALA B 252 ? 1.1344 0.8105 0.9127 0.0026  0.0232  0.0313  252 ALA B C   
4365 O O   . ALA B 252 ? 1.1014 0.7729 0.8818 0.0032  0.0224  0.0361  252 ALA B O   
4366 C CB  . ALA B 252 ? 1.2343 0.8760 0.9785 -0.0086 0.0296  0.0180  252 ALA B CB  
4367 N N   . VAL B 253 ? 1.1537 0.8579 0.9467 0.0055  0.0253  0.0319  253 VAL B N   
4368 C CA  . VAL B 253 ? 1.0853 0.8163 0.8976 0.0098  0.0262  0.0387  253 VAL B CA  
4369 C C   . VAL B 253 ? 1.0602 0.7907 0.8828 0.0153  0.0183  0.0454  253 VAL B C   
4370 O O   . VAL B 253 ? 1.0136 0.7530 0.8470 0.0181  0.0172  0.0523  253 VAL B O   
4371 C CB  . VAL B 253 ? 1.0413 0.8028 0.8654 0.0111  0.0314  0.0366  253 VAL B CB  
4372 C CG1 . VAL B 253 ? 1.0125 0.7999 0.8551 0.0154  0.0320  0.0437  253 VAL B CG1 
4373 C CG2 . VAL B 253 ? 1.0765 0.8404 0.8924 0.0063  0.0397  0.0297  253 VAL B CG2 
4374 N N   . THR B 254 ? 1.0834 0.8038 0.9027 0.0167  0.0128  0.0430  254 THR B N   
4375 C CA  . THR B 254 ? 1.0962 0.8156 0.9249 0.0218  0.0052  0.0476  254 THR B CA  
4376 C C   . THR B 254 ? 1.1621 0.8500 0.9800 0.0224  -0.0011 0.0483  254 THR B C   
4377 O O   . THR B 254 ? 1.2286 0.9153 1.0556 0.0269  -0.0062 0.0537  254 THR B O   
4378 C CB  . THR B 254 ? 1.0832 0.8115 0.9164 0.0236  0.0018  0.0436  254 THR B CB  
4379 O OG1 . THR B 254 ? 1.0970 0.8065 0.9135 0.0198  0.0012  0.0356  254 THR B OG1 
4380 C CG2 . THR B 254 ? 1.0627 0.8254 0.9111 0.0249  0.0067  0.0446  254 THR B CG2 
4381 N N   . GLY B 255 ? 1.2116 0.8740 1.0102 0.0180  -0.0005 0.0429  255 GLY B N   
4382 C CA  . GLY B 255 ? 1.2596 0.8966 1.0492 0.0181  -0.0066 0.0411  255 GLY B CA  
4383 C C   . GLY B 255 ? 1.2567 0.8875 1.0439 0.0189  -0.0131 0.0348  255 GLY B C   
4384 O O   . GLY B 255 ? 1.3110 0.9406 1.1012 0.0186  -0.0177 0.0310  255 GLY B O   
4385 N N   . GLN B 256 ? 1.2293 0.8618 1.0139 0.0198  -0.0131 0.0330  256 GLN B N   
4386 C CA  . GLN B 256 ? 1.2191 0.8419 0.9996 0.0211  -0.0203 0.0271  256 GLN B CA  
4387 C C   . GLN B 256 ? 1.2301 0.8408 0.9949 0.0153  -0.0199 0.0186  256 GLN B C   
4388 O O   . GLN B 256 ? 1.1875 0.7924 0.9408 0.0106  -0.0130 0.0174  256 GLN B O   
4389 C CB  . GLN B 256 ? 1.2362 0.8899 1.0327 0.0230  -0.0198 0.0262  256 GLN B CB  
4390 C CG  . GLN B 256 ? 1.1865 0.8659 1.0048 0.0278  -0.0196 0.0337  256 GLN B CG  
4391 C CD  . GLN B 256 ? 1.0940 0.8020 0.9271 0.0297  -0.0199 0.0322  256 GLN B CD  
4392 O OE1 . GLN B 256 ? 0.9961 0.7315 0.8401 0.0295  -0.0135 0.0348  256 GLN B OE1 
4393 N NE2 . GLN B 256 ? 1.1478 0.8495 0.9813 0.0317  -0.0278 0.0274  256 GLN B NE2 
4394 N N   . SER B 257 ? 1.2077 0.8157 0.9721 0.0157  -0.0271 0.0127  257 SER B N   
4395 C CA  . SER B 257 ? 1.2353 0.8339 0.9855 0.0108  -0.0279 0.0053  257 SER B CA  
4396 C C   . SER B 257 ? 1.1891 0.7827 0.9304 0.0093  -0.0279 0.0004  257 SER B C   
4397 O O   . SER B 257 ? 1.1821 0.7796 0.9299 0.0133  -0.0306 0.0011  257 SER B O   
4398 C CB  . SER B 257 ? 1.1995 0.7990 0.9539 0.0122  -0.0354 0.0020  257 SER B CB  
4399 O OG  . SER B 257 ? 1.1625 0.7652 0.9234 0.0157  -0.0423 -0.0008 257 SER B OG  
4400 N N   . ILE B 258 ? 1.2079 0.7940 0.9350 0.0038  -0.0250 -0.0047 258 ILE B N   
4401 C CA  . ILE B 258 ? 1.2032 0.7861 0.9225 0.0019  -0.0254 -0.0109 258 ILE B CA  
4402 C C   . ILE B 258 ? 1.2282 0.8144 0.9537 0.0053  -0.0358 -0.0150 258 ILE B C   
4403 O O   . ILE B 258 ? 1.2365 0.8272 0.9661 0.0077  -0.0382 -0.0176 258 ILE B O   
4404 C CB  . ILE B 258 ? 1.1380 0.7141 0.8423 -0.0047 -0.0211 -0.0155 258 ILE B CB  
4405 N N   . PRO B 259 ? 1.2552 0.8416 0.9828 0.0058  -0.0420 -0.0159 259 PRO B N   
4406 C CA  . PRO B 259 ? 1.2339 0.8249 0.9690 0.0091  -0.0517 -0.0198 259 PRO B CA  
4407 C C   . PRO B 259 ? 1.1848 0.7833 0.9339 0.0148  -0.0551 -0.0178 259 PRO B C   
4408 O O   . PRO B 259 ? 1.1863 0.7888 0.9398 0.0170  -0.0617 -0.0226 259 PRO B O   
4409 C CB  . PRO B 259 ? 1.2582 0.8488 0.9948 0.0094  -0.0551 -0.0191 259 PRO B CB  
4410 C CG  . PRO B 259 ? 1.2800 0.8638 1.0052 0.0049  -0.0486 -0.0174 259 PRO B CG  
4411 C CD  . PRO B 259 ? 1.2782 0.8608 1.0005 0.0031  -0.0402 -0.0144 259 PRO B CD  
4412 N N   . GLU B 260 ? 1.1311 0.7325 0.8878 0.0173  -0.0509 -0.0108 260 GLU B N   
4413 C CA  . GLU B 260 ? 1.0576 0.6666 0.8280 0.0231  -0.0529 -0.0066 260 GLU B CA  
4414 C C   . GLU B 260 ? 1.0246 0.6612 0.8060 0.0231  -0.0479 -0.0058 260 GLU B C   
4415 O O   . GLU B 260 ? 0.8842 0.5432 0.6820 0.0263  -0.0515 -0.0067 260 GLU B O   
4416 C CB  . GLU B 260 ? 1.0677 0.6815 0.8466 0.0249  -0.0481 0.0021  260 GLU B CB  
4417 N N   . LEU B 261 ? 1.1044 0.7483 0.8815 0.0192  -0.0385 -0.0042 261 LEU B N   
4418 C CA  . LEU B 261 ? 1.0913 0.7692 0.8814 0.0186  -0.0317 -0.0038 261 LEU B CA  
4419 C C   . LEU B 261 ? 1.0440 0.7288 0.8342 0.0181  -0.0368 -0.0119 261 LEU B C   
4420 O O   . LEU B 261 ? 1.0375 0.7520 0.8451 0.0208  -0.0372 -0.0120 261 LEU B O   
4421 C CB  . LEU B 261 ? 1.0690 0.7481 0.8517 0.0144  -0.0210 -0.0021 261 LEU B CB  
4422 C CG  . LEU B 261 ? 1.0618 0.7598 0.8568 0.0158  -0.0132 0.0061  261 LEU B CG  
4423 C CD1 . LEU B 261 ? 1.0439 0.7320 0.8430 0.0191  -0.0171 0.0124  261 LEU B CD1 
4424 C CD2 . LEU B 261 ? 1.0865 0.7777 0.8700 0.0109  -0.0042 0.0057  261 LEU B CD2 
4425 N N   . GLU B 262 ? 1.0817 0.7387 0.8519 0.0145  -0.0409 -0.0186 262 GLU B N   
4426 C CA  . GLU B 262 ? 1.0806 0.7389 0.8482 0.0137  -0.0477 -0.0271 262 GLU B CA  
4427 C C   . GLU B 262 ? 1.0424 0.7115 0.8240 0.0184  -0.0576 -0.0294 262 GLU B C   
4428 O O   . GLU B 262 ? 1.0133 0.7064 0.8071 0.0197  -0.0601 -0.0331 262 GLU B O   
4429 C CB  . GLU B 262 ? 1.0817 0.7019 0.8233 0.0093  -0.0522 -0.0335 262 GLU B CB  
4430 C CG  . GLU B 262 ? 1.1047 0.7205 0.8337 0.0037  -0.0427 -0.0344 262 GLU B CG  
4431 C CD  . GLU B 262 ? 1.1747 0.7627 0.8837 -0.0011 -0.0436 -0.0360 262 GLU B CD  
4432 O OE1 . GLU B 262 ? 1.1735 0.7591 0.8726 -0.0059 -0.0389 -0.0390 262 GLU B OE1 
4433 O OE2 . GLU B 262 ? 1.1715 0.7573 0.8838 0.0003  -0.0471 -0.0321 262 GLU B OE2 
4434 N N   . LYS B 263 ? 1.0746 0.7267 0.8551 0.0211  -0.0631 -0.0274 263 LYS B N   
4435 C CA  . LYS B 263 ? 1.0297 0.6904 0.8236 0.0256  -0.0721 -0.0297 263 LYS B CA  
4436 C C   . LYS B 263 ? 0.9568 0.6582 0.7759 0.0286  -0.0671 -0.0242 263 LYS B C   
4437 O O   . LYS B 263 ? 0.9257 0.6480 0.7580 0.0304  -0.0721 -0.0283 263 LYS B O   
4438 C CB  . LYS B 263 ? 1.0786 0.7115 0.8659 0.0281  -0.0775 -0.0282 263 LYS B CB  
4439 N N   . GLN B 264 ? 0.9417 0.6540 0.7669 0.0289  -0.0575 -0.0152 264 GLN B N   
4440 C CA  . GLN B 264 ? 0.9215 0.6701 0.7689 0.0316  -0.0520 -0.0088 264 GLN B CA  
4441 C C   . GLN B 264 ? 0.8761 0.6562 0.7342 0.0311  -0.0481 -0.0111 264 GLN B C   
4442 O O   . GLN B 264 ? 0.8085 0.6183 0.6853 0.0338  -0.0478 -0.0093 264 GLN B O   
4443 C CB  . GLN B 264 ? 0.9232 0.6736 0.7721 0.0316  -0.0428 0.0007  264 GLN B CB  
4444 N N   . PHE B 265 ? 0.9142 0.6873 0.7601 0.0276  -0.0450 -0.0152 265 PHE B N   
4445 C CA  . PHE B 265 ? 0.8670 0.6675 0.7217 0.0273  -0.0413 -0.0181 265 PHE B CA  
4446 C C   . PHE B 265 ? 0.9276 0.7262 0.7800 0.0269  -0.0510 -0.0278 265 PHE B C   
4447 O O   . PHE B 265 ? 0.9059 0.7207 0.7614 0.0261  -0.0490 -0.0317 265 PHE B O   
4448 C CB  . PHE B 265 ? 0.8638 0.6602 0.7080 0.0238  -0.0314 -0.0171 265 PHE B CB  
4449 C CG  . PHE B 265 ? 0.8229 0.6297 0.6731 0.0245  -0.0216 -0.0086 265 PHE B CG  
4450 C CD1 . PHE B 265 ? 0.8104 0.6505 0.6809 0.0281  -0.0175 -0.0034 265 PHE B CD1 
4451 C CD2 . PHE B 265 ? 0.8564 0.6402 0.6916 0.0213  -0.0165 -0.0062 265 PHE B CD2 
4452 C CE1 . PHE B 265 ? 0.8040 0.6533 0.6796 0.0286  -0.0092 0.0040  265 PHE B CE1 
4453 C CE2 . PHE B 265 ? 0.8274 0.6215 0.6684 0.0218  -0.0082 0.0010  265 PHE B CE2 
4454 C CZ  . PHE B 265 ? 0.8231 0.6497 0.6842 0.0256  -0.0048 0.0060  265 PHE B CZ  
4455 N N   . GLU B 266 ? 0.9259 0.7049 0.7734 0.0277  -0.0619 -0.0321 266 GLU B N   
4456 C CA  . GLU B 266 ? 0.9130 0.6902 0.7596 0.0277  -0.0729 -0.0418 266 GLU B CA  
4457 C C   . GLU B 266 ? 0.8683 0.6856 0.7382 0.0307  -0.0737 -0.0427 266 GLU B C   
4458 O O   . GLU B 266 ? 0.8306 0.6669 0.7165 0.0336  -0.0719 -0.0375 266 GLU B O   
4459 C CB  . GLU B 266 ? 0.8817 0.6308 0.7199 0.0287  -0.0845 -0.0464 266 GLU B CB  
4460 N N   . GLY B 267 ? 0.8886 0.7187 0.7605 0.0298  -0.0761 -0.0490 267 GLY B N   
4461 C CA  . GLY B 267 ? 0.8709 0.7402 0.7648 0.0325  -0.0770 -0.0507 267 GLY B CA  
4462 C C   . GLY B 267 ? 0.8205 0.7213 0.7283 0.0341  -0.0644 -0.0433 267 GLY B C   
4463 O O   . GLY B 267 ? 0.8090 0.7435 0.7361 0.0369  -0.0641 -0.0432 267 GLY B O   
4464 N N   . LYS B 268 ? 0.8105 0.7000 0.7083 0.0324  -0.0544 -0.0375 268 LYS B N   
4465 C CA  . LYS B 268 ? 0.7894 0.7041 0.6978 0.0338  -0.0421 -0.0307 268 LYS B CA  
4466 C C   . LYS B 268 ? 0.7906 0.6975 0.6869 0.0310  -0.0351 -0.0329 268 LYS B C   
4467 O O   . LYS B 268 ? 0.7720 0.6501 0.6498 0.0275  -0.0386 -0.0377 268 LYS B O   
4468 C CB  . LYS B 268 ? 0.7485 0.6577 0.6577 0.0344  -0.0366 -0.0215 268 LYS B CB  
4469 C CG  . LYS B 268 ? 0.7646 0.6800 0.6853 0.0370  -0.0431 -0.0194 268 LYS B CG  
4470 C CD  . LYS B 268 ? 0.8238 0.7272 0.7424 0.0374  -0.0392 -0.0110 268 LYS B CD  
4471 C CE  . LYS B 268 ? 0.8301 0.7384 0.7600 0.0398  -0.0455 -0.0094 268 LYS B CE  
4472 N NZ  . LYS B 268 ? 0.8703 0.7545 0.7916 0.0393  -0.0573 -0.0171 268 LYS B NZ  
4473 N N   . MET B 269 ? 0.7630 0.6951 0.6695 0.0327  -0.0251 -0.0296 269 MET B N   
4474 C CA  . MET B 269 ? 0.7117 0.6423 0.6104 0.0308  -0.0176 -0.0326 269 MET B CA  
4475 C C   . MET B 269 ? 0.7065 0.6344 0.6013 0.0299  -0.0058 -0.0263 269 MET B C   
4476 O O   . MET B 269 ? 0.6786 0.5984 0.5727 0.0299  -0.0049 -0.0199 269 MET B O   
4477 C CB  . MET B 269 ? 0.6932 0.6574 0.6084 0.0341  -0.0172 -0.0366 269 MET B CB  
4478 C CG  . MET B 269 ? 0.7204 0.6826 0.6355 0.0338  -0.0291 -0.0447 269 MET B CG  
4479 S SD  . MET B 269 ? 0.7181 0.7249 0.6578 0.0389  -0.0310 -0.0485 269 MET B SD  
4480 C CE  . MET B 269 ? 0.7252 0.7472 0.6807 0.0417  -0.0391 -0.0456 269 MET B CE  
4481 N N   . TYR B 270 ? 0.6746 0.6097 0.5676 0.0292  0.0027  -0.0286 270 TYR B N   
4482 C CA  . TYR B 270 ? 0.6846 0.6139 0.5713 0.0275  0.0134  -0.0250 270 TYR B CA  
4483 C C   . TYR B 270 ? 0.6527 0.6075 0.5556 0.0315  0.0195  -0.0178 270 TYR B C   
4484 O O   . TYR B 270 ? 0.6527 0.6001 0.5508 0.0302  0.0260  -0.0137 270 TYR B O   
4485 C CB  . TYR B 270 ? 0.6914 0.6201 0.5711 0.0254  0.0205  -0.0312 270 TYR B CB  
4486 C CG  . TYR B 270 ? 0.7448 0.6491 0.6081 0.0212  0.0145  -0.0384 270 TYR B CG  
4487 C CD1 . TYR B 270 ? 0.7911 0.7028 0.6539 0.0208  0.0171  -0.0452 270 TYR B CD1 
4488 C CD2 . TYR B 270 ? 0.7807 0.6544 0.6293 0.0180  0.0058  -0.0386 270 TYR B CD2 
4489 C CE1 . TYR B 270 ? 0.8073 0.6961 0.6546 0.0167  0.0110  -0.0517 270 TYR B CE1 
4490 C CE2 . TYR B 270 ? 0.8141 0.6643 0.6468 0.0142  -0.0003 -0.0453 270 TYR B CE2 
4491 C CZ  . TYR B 270 ? 0.8000 0.6573 0.6316 0.0133  0.0021  -0.0517 270 TYR B CZ  
4492 O OH  . TYR B 270 ? 0.7876 0.6199 0.6023 0.0092  -0.0047 -0.0581 270 TYR B OH  
4493 N N   . GLY B 271 ? 0.5895 0.5739 0.5113 0.0362  0.0170  -0.0166 271 GLY B N   
4494 C CA  . GLY B 271 ? 0.5284 0.5364 0.4656 0.0401  0.0210  -0.0096 271 GLY B CA  
4495 C C   . GLY B 271 ? 0.5548 0.5482 0.4891 0.0391  0.0179  -0.0026 271 GLY B C   
4496 O O   . GLY B 271 ? 0.4925 0.4891 0.4288 0.0397  0.0237  0.0033  271 GLY B O   
4497 N N   . HIS B 272 ? 0.5755 0.5533 0.5056 0.0380  0.0083  -0.0037 272 HIS B N   
4498 C CA  . HIS B 272 ? 0.6434 0.6031 0.5692 0.0371  0.0046  0.0018  272 HIS B CA  
4499 C C   . HIS B 272 ? 0.6941 0.6246 0.6022 0.0333  0.0087  0.0034  272 HIS B C   
4500 O O   . HIS B 272 ? 0.7069 0.6335 0.6157 0.0336  0.0113  0.0102  272 HIS B O   
4501 C CB  . HIS B 272 ? 0.6830 0.6295 0.6067 0.0368  -0.0069 -0.0017 272 HIS B CB  
4502 C CG  . HIS B 272 ? 0.6615 0.6335 0.6038 0.0403  -0.0113 -0.0001 272 HIS B CG  
4503 N ND1 . HIS B 272 ? 0.6272 0.6219 0.5807 0.0422  -0.0148 -0.0054 272 HIS B ND1 
4504 C CD2 . HIS B 272 ? 0.6520 0.6308 0.6039 0.0422  -0.0128 0.0061  272 HIS B CD2 
4505 C CE1 . HIS B 272 ? 0.6564 0.6706 0.6252 0.0448  -0.0181 -0.0028 272 HIS B CE1 
4506 N NE2 . HIS B 272 ? 0.6544 0.6593 0.6224 0.0447  -0.0168 0.0042  272 HIS B NE2 
4507 N N   . LEU B 273 ? 0.6932 0.6040 0.5858 0.0297  0.0090  -0.0028 273 LEU B N   
4508 C CA  . LEU B 273 ? 0.7709 0.6545 0.6458 0.0255  0.0134  -0.0023 273 LEU B CA  
4509 C C   . LEU B 273 ? 0.7341 0.6316 0.6142 0.0261  0.0235  0.0021  273 LEU B C   
4510 O O   . LEU B 273 ? 0.7748 0.6642 0.6533 0.0258  0.0249  0.0079  273 LEU B O   
4511 C CB  . LEU B 273 ? 0.7837 0.6488 0.6424 0.0213  0.0139  -0.0102 273 LEU B CB  
4512 C CG  . LEU B 273 ? 0.8485 0.6871 0.6887 0.0163  0.0194  -0.0106 273 LEU B CG  
4513 C CD1 . LEU B 273 ? 0.9231 0.7324 0.7519 0.0147  0.0134  -0.0073 273 LEU B CD1 
4514 C CD2 . LEU B 273 ? 0.8720 0.6971 0.6978 0.0121  0.0217  -0.0185 273 LEU B CD2 
4515 N N   . LYS B 274 ? 0.6528 0.5722 0.5401 0.0274  0.0300  -0.0012 274 LYS B N   
4516 C CA  . LYS B 274 ? 0.6879 0.6187 0.5781 0.0278  0.0397  0.0005  274 LYS B CA  
4517 C C   . LYS B 274 ? 0.6484 0.5961 0.5520 0.0313  0.0407  0.0089  274 LYS B C   
4518 O O   . LYS B 274 ? 0.6345 0.5803 0.5362 0.0305  0.0461  0.0119  274 LYS B O   
4519 C CB  . LYS B 274 ? 0.6653 0.6175 0.5621 0.0295  0.0457  -0.0054 274 LYS B CB  
4520 C CG  . LYS B 274 ? 0.7200 0.6535 0.6014 0.0251  0.0475  -0.0135 274 LYS B CG  
4521 C CD  . LYS B 274 ? 0.7147 0.6701 0.6038 0.0274  0.0539  -0.0195 274 LYS B CD  
4522 C CE  . LYS B 274 ? 0.7143 0.6505 0.5873 0.0225  0.0574  -0.0274 274 LYS B CE  
4523 N NZ  . LYS B 274 ? 0.7161 0.6755 0.5988 0.0256  0.0631  -0.0334 274 LYS B NZ  
4524 N N   . GLY B 275 ? 0.6130 0.5771 0.5301 0.0349  0.0353  0.0121  275 GLY B N   
4525 C CA  . GLY B 275 ? 0.6028 0.5816 0.5323 0.0380  0.0351  0.0203  275 GLY B CA  
4526 C C   . GLY B 275 ? 0.6391 0.5947 0.5606 0.0359  0.0320  0.0257  275 GLY B C   
4527 O O   . GLY B 275 ? 0.6730 0.6341 0.5990 0.0369  0.0350  0.0318  275 GLY B O   
4528 N N   . GLU B 276 ? 0.7379 0.6669 0.6471 0.0332  0.0260  0.0231  276 GLU B N   
4529 C CA  . GLU B 276 ? 0.8090 0.7143 0.7105 0.0318  0.0223  0.0278  276 GLU B CA  
4530 C C   . GLU B 276 ? 0.7568 0.6445 0.6454 0.0283  0.0277  0.0279  276 GLU B C   
4531 O O   . GLU B 276 ? 0.7453 0.6282 0.6349 0.0286  0.0281  0.0340  276 GLU B O   
4532 C CB  . GLU B 276 ? 0.8816 0.7638 0.7742 0.0307  0.0134  0.0243  276 GLU B CB  
4533 C CG  . GLU B 276 ? 0.9780 0.8388 0.8663 0.0308  0.0084  0.0293  276 GLU B CG  
4534 C CD  . GLU B 276 ? 0.9914 0.8705 0.8956 0.0345  0.0082  0.0374  276 GLU B CD  
4535 O OE1 . GLU B 276 ? 1.0388 0.9429 0.9574 0.0372  0.0074  0.0380  276 GLU B OE1 
4536 O OE2 . GLU B 276 ? 1.0125 0.8816 0.9150 0.0345  0.0089  0.0431  276 GLU B OE2 
4537 N N   . VAL B 277 ? 0.7053 0.5836 0.5822 0.0249  0.0316  0.0210  277 VAL B N   
4538 C CA  . VAL B 277 ? 0.7386 0.6036 0.6040 0.0211  0.0379  0.0197  277 VAL B CA  
4539 C C   . VAL B 277 ? 0.7501 0.6382 0.6269 0.0232  0.0446  0.0232  277 VAL B C   
4540 O O   . VAL B 277 ? 0.8143 0.6947 0.6876 0.0218  0.0468  0.0263  277 VAL B O   
4541 C CB  . VAL B 277 ? 0.7909 0.6454 0.6432 0.0171  0.0416  0.0107  277 VAL B CB  
4542 C CG1 . VAL B 277 ? 0.8279 0.6740 0.6706 0.0132  0.0494  0.0084  277 VAL B CG1 
4543 C CG2 . VAL B 277 ? 0.8206 0.6469 0.6582 0.0142  0.0347  0.0073  277 VAL B CG2 
4544 N N   . ALA B 278 ? 0.6307 0.5471 0.5213 0.0269  0.0473  0.0227  278 ALA B N   
4545 C CA  . ALA B 278 ? 0.6203 0.5594 0.5218 0.0295  0.0532  0.0254  278 ALA B CA  
4546 C C   . ALA B 278 ? 0.6186 0.5620 0.5282 0.0317  0.0502  0.0346  278 ALA B C   
4547 O O   . ALA B 278 ? 0.6049 0.5506 0.5150 0.0314  0.0538  0.0368  278 ALA B O   
4548 C CB  . ALA B 278 ? 0.5817 0.5494 0.4962 0.0335  0.0559  0.0229  278 ALA B CB  
4549 N N   . ASP B 279 ? 0.7020 0.6464 0.6181 0.0338  0.0435  0.0393  279 ASP B N   
4550 C CA  . ASP B 279 ? 0.7509 0.6981 0.6748 0.0358  0.0402  0.0481  279 ASP B CA  
4551 C C   . ASP B 279 ? 0.7608 0.6828 0.6740 0.0330  0.0385  0.0506  279 ASP B C   
4552 O O   . ASP B 279 ? 0.7931 0.7194 0.7105 0.0337  0.0396  0.0561  279 ASP B O   
4553 C CB  . ASP B 279 ? 0.7976 0.7497 0.7302 0.0383  0.0333  0.0513  279 ASP B CB  
4554 C CG  . ASP B 279 ? 0.8651 0.8490 0.8140 0.0422  0.0349  0.0534  279 ASP B CG  
4555 O OD1 . ASP B 279 ? 0.9623 0.9540 0.9209 0.0443  0.0305  0.0586  279 ASP B OD1 
4556 O OD2 . ASP B 279 ? 0.8356 0.8367 0.7878 0.0431  0.0407  0.0498  279 ASP B OD2 
4557 N N   . ALA B 280 ? 0.7688 0.6649 0.6683 0.0299  0.0354  0.0467  280 ALA B N   
4558 C CA  . ALA B 280 ? 0.7764 0.6467 0.6644 0.0271  0.0337  0.0483  280 ALA B CA  
4559 C C   . ALA B 280 ? 0.7859 0.6577 0.6699 0.0246  0.0403  0.0470  280 ALA B C   
4560 O O   . ALA B 280 ? 0.7438 0.6170 0.6321 0.0254  0.0398  0.0527  280 ALA B O   
4561 C CB  . ALA B 280 ? 0.8168 0.6599 0.6891 0.0239  0.0305  0.0426  280 ALA B CB  
4562 N N   . VAL B 281 ? 0.7140 0.5876 0.5914 0.0220  0.0462  0.0393  281 VAL B N   
4563 C CA  . VAL B 281 ? 0.7328 0.6044 0.6040 0.0188  0.0525  0.0357  281 VAL B CA  
4564 C C   . VAL B 281 ? 0.7010 0.5976 0.5856 0.0220  0.0557  0.0392  281 VAL B C   
4565 O O   . VAL B 281 ? 0.7151 0.6088 0.5981 0.0205  0.0572  0.0402  281 VAL B O   
4566 C CB  . VAL B 281 ? 0.7303 0.5979 0.5913 0.0154  0.0583  0.0258  281 VAL B CB  
4567 C CG1 . VAL B 281 ? 0.7862 0.6499 0.6401 0.0115  0.0649  0.0209  281 VAL B CG1 
4568 C CG2 . VAL B 281 ? 0.7220 0.5639 0.5687 0.0121  0.0545  0.0224  281 VAL B CG2 
4569 N N   . SER B 282 ? 0.7217 0.6424 0.6194 0.0263  0.0563  0.0409  282 SER B N   
4570 C CA  . SER B 282 ? 0.6960 0.6406 0.6061 0.0297  0.0591  0.0442  282 SER B CA  
4571 C C   . SER B 282 ? 0.7046 0.6476 0.6201 0.0309  0.0543  0.0533  282 SER B C   
4572 O O   . SER B 282 ? 0.7302 0.6798 0.6485 0.0311  0.0562  0.0547  282 SER B O   
4573 C CB  . SER B 282 ? 0.7463 0.7158 0.6688 0.0341  0.0600  0.0446  282 SER B CB  
4574 O OG  . SER B 282 ? 0.8125 0.8042 0.7458 0.0374  0.0629  0.0473  282 SER B OG  
4575 N N   . GLY B 283 ? 0.7167 0.6497 0.6334 0.0318  0.0479  0.0589  283 GLY B N   
4576 C CA  . GLY B 283 ? 0.7071 0.6365 0.6290 0.0331  0.0428  0.0676  283 GLY B CA  
4577 C C   . GLY B 283 ? 0.7035 0.6137 0.6161 0.0299  0.0422  0.0674  283 GLY B C   
4578 O O   . GLY B 283 ? 0.6542 0.5686 0.5724 0.0309  0.0404  0.0730  283 GLY B O   
4579 N N   . MET B 284 ? 0.6520 0.5417 0.5506 0.0259  0.0435  0.0609  284 MET B N   
4580 C CA  . MET B 284 ? 0.6840 0.5541 0.5721 0.0221  0.0433  0.0595  284 MET B CA  
4581 C C   . MET B 284 ? 0.6526 0.5333 0.5410 0.0203  0.0486  0.0556  284 MET B C   
4582 O O   . MET B 284 ? 0.6120 0.4920 0.5030 0.0201  0.0465  0.0591  284 MET B O   
4583 C CB  . MET B 284 ? 0.7143 0.5604 0.5864 0.0179  0.0439  0.0529  284 MET B CB  
4584 C CG  . MET B 284 ? 0.7923 0.6152 0.6532 0.0141  0.0424  0.0524  284 MET B CG  
4585 S SD  . MET B 284 ? 0.9039 0.7056 0.7448 0.0077  0.0472  0.0416  284 MET B SD  
4586 C CE  . MET B 284 ? 0.8434 0.6610 0.6851 0.0048  0.0557  0.0348  284 MET B CE  
4587 N N   . LEU B 285 ? 0.6354 0.5268 0.5222 0.0194  0.0551  0.0480  285 LEU B N   
4588 C CA  . LEU B 285 ? 0.6722 0.5752 0.5598 0.0183  0.0607  0.0425  285 LEU B CA  
4589 C C   . LEU B 285 ? 0.6522 0.5754 0.5531 0.0222  0.0591  0.0483  285 LEU B C   
4590 O O   . LEU B 285 ? 0.6225 0.5479 0.5230 0.0208  0.0603  0.0460  285 LEU B O   
4591 C CB  . LEU B 285 ? 0.6834 0.5964 0.5692 0.0180  0.0677  0.0336  285 LEU B CB  
4592 C CG  . LEU B 285 ? 0.6586 0.5526 0.5300 0.0134  0.0705  0.0261  285 LEU B CG  
4593 C CD1 . LEU B 285 ? 0.6836 0.5908 0.5553 0.0136  0.0780  0.0170  285 LEU B CD1 
4594 C CD2 . LEU B 285 ? 0.7002 0.5720 0.5585 0.0077  0.0708  0.0228  285 LEU B CD2 
4595 N N   . THR B 286 ? 0.7020 0.6396 0.6141 0.0268  0.0564  0.0552  286 THR B N   
4596 C CA  . THR B 286 ? 0.6769 0.6330 0.6013 0.0305  0.0544  0.0618  286 THR B CA  
4597 C C   . THR B 286 ? 0.6590 0.6055 0.5845 0.0300  0.0484  0.0686  286 THR B C   
4598 O O   . THR B 286 ? 0.6437 0.5997 0.5739 0.0307  0.0477  0.0700  286 THR B O   
4599 C CB  . THR B 286 ? 0.6511 0.6235 0.5865 0.0350  0.0528  0.0677  286 THR B CB  
4600 O OG1 . THR B 286 ? 0.6329 0.6157 0.5681 0.0358  0.0582  0.0609  286 THR B OG1 
4601 C CG2 . THR B 286 ? 0.6228 0.6141 0.5698 0.0386  0.0511  0.0745  286 THR B CG2 
4602 N N   . GLU B 287 ? 0.7118 0.6397 0.6331 0.0289  0.0437  0.0725  287 GLU B N   
4603 C CA  . GLU B 287 ? 0.7259 0.6428 0.6482 0.0286  0.0377  0.0788  287 GLU B CA  
4604 C C   . GLU B 287 ? 0.7378 0.6440 0.6514 0.0244  0.0392  0.0728  287 GLU B C   
4605 O O   . GLU B 287 ? 0.7652 0.6759 0.6833 0.0246  0.0364  0.0754  287 GLU B O   
4606 C CB  . GLU B 287 ? 0.7464 0.6446 0.6658 0.0291  0.0327  0.0832  287 GLU B CB  
4607 C CG  . GLU B 287 ? 0.8326 0.7226 0.7567 0.0305  0.0258  0.0913  287 GLU B CG  
4608 C CD  . GLU B 287 ? 0.9622 0.8338 0.8771 0.0270  0.0244  0.0884  287 GLU B CD  
4609 O OE1 . GLU B 287 ? 1.0464 0.9068 0.9490 0.0227  0.0287  0.0800  287 GLU B OE1 
4610 O OE2 . GLU B 287 ? 0.9617 0.8299 0.8820 0.0284  0.0189  0.0948  287 GLU B OE2 
4611 N N   . LEU B 288 ? 0.6879 0.5797 0.5888 0.0203  0.0432  0.0645  288 LEU B N   
4612 C CA  . LEU B 288 ? 0.6860 0.5665 0.5773 0.0153  0.0453  0.0575  288 LEU B CA  
4613 C C   . LEU B 288 ? 0.6385 0.5363 0.5345 0.0152  0.0484  0.0530  288 LEU B C   
4614 O O   . LEU B 288 ? 0.6331 0.5290 0.5294 0.0136  0.0458  0.0527  288 LEU B O   
4615 C CB  . LEU B 288 ? 0.7035 0.5693 0.5807 0.0109  0.0506  0.0486  288 LEU B CB  
4616 C CG  . LEU B 288 ? 0.7004 0.5501 0.5654 0.0049  0.0528  0.0413  288 LEU B CG  
4617 C CD1 . LEU B 288 ? 0.7424 0.5710 0.6026 0.0039  0.0465  0.0467  288 LEU B CD1 
4618 C CD2 . LEU B 288 ? 0.7372 0.5786 0.5898 0.0007  0.0598  0.0312  288 LEU B CD2 
4619 N N   . GLN B 289 ? 0.6017 0.5166 0.5017 0.0173  0.0535  0.0492  289 GLN B N   
4620 C CA  . GLN B 289 ? 0.6535 0.5851 0.5577 0.0178  0.0569  0.0435  289 GLN B CA  
4621 C C   . GLN B 289 ? 0.6456 0.5897 0.5608 0.0211  0.0511  0.0510  289 GLN B C   
4622 O O   . GLN B 289 ? 0.6331 0.5835 0.5493 0.0202  0.0512  0.0463  289 GLN B O   
4623 C CB  . GLN B 289 ? 0.6369 0.5839 0.5436 0.0203  0.0635  0.0381  289 GLN B CB  
4624 C CG  . GLN B 289 ? 0.6424 0.5791 0.5377 0.0163  0.0702  0.0276  289 GLN B CG  
4625 C CD  . GLN B 289 ? 0.6942 0.6453 0.5929 0.0193  0.0758  0.0235  289 GLN B CD  
4626 O OE1 . GLN B 289 ? 0.7221 0.6935 0.6311 0.0240  0.0766  0.0251  289 GLN B OE1 
4627 N NE2 . GLN B 289 ? 0.7120 0.6525 0.6020 0.0167  0.0795  0.0180  289 GLN B NE2 
4628 N N   . GLU B 290 ? 0.6788 0.6258 0.6019 0.0247  0.0459  0.0620  290 GLU B N   
4629 C CA  . GLU B 290 ? 0.6468 0.6031 0.5799 0.0276  0.0397  0.0704  290 GLU B CA  
4630 C C   . GLU B 290 ? 0.6260 0.5697 0.5562 0.0246  0.0346  0.0707  290 GLU B C   
4631 O O   . GLU B 290 ? 0.6454 0.5971 0.5796 0.0247  0.0320  0.0699  290 GLU B O   
4632 C CB  . GLU B 290 ? 0.6821 0.6417 0.6235 0.0314  0.0354  0.0817  290 GLU B CB  
4633 N N   . ARG B 291 ? 0.5995 0.5234 0.5226 0.0221  0.0331  0.0713  291 ARG B N   
4634 C CA  . ARG B 291 ? 0.5761 0.4866 0.4954 0.0189  0.0287  0.0706  291 ARG B CA  
4635 C C   . ARG B 291 ? 0.5280 0.4389 0.4404 0.0144  0.0328  0.0588  291 ARG B C   
4636 O O   . ARG B 291 ? 0.4906 0.4038 0.4059 0.0133  0.0286  0.0580  291 ARG B O   
4637 C CB  . ARG B 291 ? 0.5967 0.4845 0.5079 0.0170  0.0272  0.0722  291 ARG B CB  
4638 C CG  . ARG B 291 ? 0.6634 0.5476 0.5798 0.0212  0.0236  0.0818  291 ARG B CG  
4639 C CD  . ARG B 291 ? 0.6562 0.5167 0.5655 0.0198  0.0201  0.0836  291 ARG B CD  
4640 N NE  . ARG B 291 ? 0.6742 0.5303 0.5876 0.0200  0.0137  0.0878  291 ARG B NE  
4641 C CZ  . ARG B 291 ? 0.6586 0.4970 0.5639 0.0167  0.0120  0.0849  291 ARG B CZ  
4642 N NH1 . ARG B 291 ? 0.6125 0.4501 0.5240 0.0176  0.0055  0.0892  291 ARG B NH1 
4643 N NH2 . ARG B 291 ? 0.6140 0.4357 0.5051 0.0125  0.0165  0.0776  291 ARG B NH2 
4644 N N   . TYR B 292 ? 0.4805 0.3895 0.3843 0.0118  0.0407  0.0494  292 TYR B N   
4645 C CA  . TYR B 292 ? 0.5266 0.4346 0.4229 0.0072  0.0458  0.0368  292 TYR B CA  
4646 C C   . TYR B 292 ? 0.5097 0.4347 0.4131 0.0084  0.0446  0.0331  292 TYR B C   
4647 O O   . TYR B 292 ? 0.5134 0.4350 0.4138 0.0047  0.0434  0.0265  292 TYR B O   
4648 C CB  . TYR B 292 ? 0.5153 0.4224 0.4038 0.0056  0.0547  0.0281  292 TYR B CB  
4649 C CG  . TYR B 292 ? 0.5278 0.4361 0.4097 0.0012  0.0609  0.0143  292 TYR B CG  
4650 C CD1 . TYR B 292 ? 0.5350 0.4614 0.4217 0.0036  0.0655  0.0075  292 TYR B CD1 
4651 C CD2 . TYR B 292 ? 0.5352 0.4262 0.4057 -0.0053 0.0624  0.0072  292 TYR B CD2 
4652 C CE1 . TYR B 292 ? 0.5299 0.4571 0.4108 -0.0001 0.0714  -0.0063 292 TYR B CE1 
4653 C CE2 . TYR B 292 ? 0.5042 0.3965 0.3687 -0.0097 0.0684  -0.0064 292 TYR B CE2 
4654 C CZ  . TYR B 292 ? 0.5515 0.4617 0.4214 -0.0071 0.0729  -0.0134 292 TYR B CZ  
4655 O OH  . TYR B 292 ? 0.5391 0.4504 0.4034 -0.0112 0.0791  -0.0280 292 TYR B OH  
4656 N N   . HIS B 293 ? 0.5459 0.4887 0.4583 0.0135  0.0448  0.0369  293 HIS B N   
4657 C CA  . HIS B 293 ? 0.5718 0.5309 0.4905 0.0154  0.0437  0.0331  293 HIS B CA  
4658 C C   . HIS B 293 ? 0.5565 0.5167 0.4816 0.0159  0.0343  0.0394  293 HIS B C   
4659 O O   . HIS B 293 ? 0.5828 0.5489 0.5089 0.0146  0.0324  0.0326  293 HIS B O   
4660 C CB  . HIS B 293 ? 0.6067 0.5838 0.5326 0.0209  0.0465  0.0358  293 HIS B CB  
4661 C CG  . HIS B 293 ? 0.6170 0.5971 0.5379 0.0206  0.0557  0.0264  293 HIS B CG  
4662 N ND1 . HIS B 293 ? 0.6193 0.6007 0.5348 0.0181  0.0612  0.0127  293 HIS B ND1 
4663 C CD2 . HIS B 293 ? 0.6457 0.6278 0.5664 0.0227  0.0602  0.0283  293 HIS B CD2 
4664 C CE1 . HIS B 293 ? 0.6338 0.6178 0.5463 0.0188  0.0689  0.0069  293 HIS B CE1 
4665 N NE2 . HIS B 293 ? 0.6653 0.6501 0.5810 0.0215  0.0681  0.0163  293 HIS B NE2 
4666 N N   . ARG B 294 ? 0.5361 0.4906 0.4658 0.0177  0.0283  0.0515  294 ARG B N   
4667 C CA  . ARG B 294 ? 0.5549 0.5089 0.4910 0.0182  0.0190  0.0579  294 ARG B CA  
4668 C C   . ARG B 294 ? 0.5663 0.5085 0.4959 0.0128  0.0173  0.0502  294 ARG B C   
4669 O O   . ARG B 294 ? 0.5513 0.4987 0.4855 0.0123  0.0111  0.0490  294 ARG B O   
4670 C CB  . ARG B 294 ? 0.6130 0.5611 0.5550 0.0212  0.0135  0.0718  294 ARG B CB  
4671 C CG  . ARG B 294 ? 0.7080 0.6691 0.6580 0.0263  0.0138  0.0804  294 ARG B CG  
4672 C CD  . ARG B 294 ? 0.7221 0.6783 0.6791 0.0293  0.0078  0.0935  294 ARG B CD  
4673 N NE  . ARG B 294 ? 0.8089 0.7660 0.7664 0.0316  0.0119  0.0974  294 ARG B NE  
4674 C CZ  . ARG B 294 ? 0.8767 0.8193 0.8304 0.0313  0.0124  0.0998  294 ARG B CZ  
4675 N NH1 . ARG B 294 ? 0.9219 0.8467 0.8707 0.0291  0.0093  0.0995  294 ARG B NH1 
4676 N NH2 . ARG B 294 ? 0.8399 0.7859 0.7947 0.0334  0.0157  0.1022  294 ARG B NH2 
4677 N N   . PHE B 295 ? 0.5241 0.4505 0.4432 0.0087  0.0223  0.0451  295 PHE B N   
4678 C CA  . PHE B 295 ? 0.5153 0.4288 0.4267 0.0029  0.0218  0.0374  295 PHE B CA  
4679 C C   . PHE B 295 ? 0.4890 0.4085 0.3952 -0.0010 0.0271  0.0224  295 PHE B C   
4680 O O   . PHE B 295 ? 0.4041 0.3255 0.3115 -0.0037 0.0229  0.0167  295 PHE B O   
4681 C CB  . PHE B 295 ? 0.5346 0.4274 0.4352 -0.0001 0.0254  0.0375  295 PHE B CB  
4682 C CG  . PHE B 295 ? 0.5235 0.4065 0.4281 0.0031  0.0192  0.0504  295 PHE B CG  
4683 C CD1 . PHE B 295 ? 0.5144 0.3959 0.4261 0.0043  0.0103  0.0569  295 PHE B CD1 
4684 C CD2 . PHE B 295 ? 0.5394 0.4140 0.4406 0.0050  0.0220  0.0553  295 PHE B CD2 
4685 C CE1 . PHE B 295 ? 0.5116 0.3836 0.4274 0.0077  0.0048  0.0681  295 PHE B CE1 
4686 C CE2 . PHE B 295 ? 0.5462 0.4108 0.4509 0.0082  0.0162  0.0659  295 PHE B CE2 
4687 C CZ  . PHE B 295 ? 0.5090 0.3723 0.4212 0.0097  0.0079  0.0724  295 PHE B CZ  
4688 N N   . ARG B 296 ? 0.4882 0.4115 0.3897 -0.0010 0.0358  0.0157  296 ARG B N   
4689 C CA  . ARG B 296 ? 0.5028 0.4295 0.3983 -0.0047 0.0425  0.0003  296 ARG B CA  
4690 C C   . ARG B 296 ? 0.5493 0.4920 0.4519 -0.0032 0.0390  -0.0056 296 ARG B C   
4691 O O   . ARG B 296 ? 0.5405 0.4830 0.4388 -0.0074 0.0410  -0.0185 296 ARG B O   
4692 C CB  . ARG B 296 ? 0.4965 0.4255 0.3874 -0.0038 0.0521  -0.0045 296 ARG B CB  
4693 C CG  . ARG B 296 ? 0.5197 0.4500 0.4034 -0.0078 0.0602  -0.0211 296 ARG B CG  
4694 C CD  . ARG B 296 ? 0.5007 0.4141 0.3735 -0.0157 0.0617  -0.0293 296 ARG B CD  
4695 N NE  . ARG B 296 ? 0.5266 0.4417 0.3930 -0.0198 0.0697  -0.0460 296 ARG B NE  
4696 C CZ  . ARG B 296 ? 0.5079 0.4318 0.3769 -0.0212 0.0687  -0.0569 296 ARG B CZ  
4697 N NH1 . ARG B 296 ? 0.4644 0.3970 0.3424 -0.0189 0.0595  -0.0528 296 ARG B NH1 
4698 N NH2 . ARG B 296 ? 0.5013 0.4256 0.3642 -0.0249 0.0769  -0.0724 296 ARG B NH2 
4699 N N   . ASN B 297 ? 0.5337 0.4894 0.4469 0.0027  0.0334  0.0038  297 ASN B N   
4700 C CA  . ASN B 297 ? 0.5592 0.5300 0.4792 0.0049  0.0290  -0.0005 297 ASN B CA  
4701 C C   . ASN B 297 ? 0.5345 0.5046 0.4597 0.0038  0.0183  0.0031  297 ASN B C   
4702 O O   . ASN B 297 ? 0.5656 0.5470 0.4961 0.0053  0.0131  -0.0008 297 ASN B O   
4703 C CB  . ASN B 297 ? 0.5504 0.5359 0.4780 0.0117  0.0290  0.0072  297 ASN B CB  
4704 C CG  . ASN B 297 ? 0.5720 0.5616 0.4958 0.0133  0.0394  0.0015  297 ASN B CG  
4705 O OD1 . ASN B 297 ? 0.5916 0.5770 0.5080 0.0099  0.0465  -0.0112 297 ASN B OD1 
4706 N ND2 . ASN B 297 ? 0.6072 0.6056 0.5366 0.0186  0.0401  0.0107  297 ASN B ND2 
4707 N N   . ASP B 298 ? 0.4938 0.4507 0.4176 0.0014  0.0145  0.0097  298 ASP B N   
4708 C CA  . ASP B 298 ? 0.4456 0.4014 0.3751 0.0004  0.0040  0.0136  298 ASP B CA  
4709 C C   . ASP B 298 ? 0.4599 0.4058 0.3818 -0.0065 0.0049  0.0016  298 ASP B C   
4710 O O   . ASP B 298 ? 0.4609 0.3920 0.3779 -0.0096 0.0051  0.0046  298 ASP B O   
4711 C CB  . ASP B 298 ? 0.4771 0.4252 0.4113 0.0034  -0.0011 0.0298  298 ASP B CB  
4712 C CG  . ASP B 298 ? 0.4320 0.3808 0.3747 0.0039  -0.0128 0.0362  298 ASP B CG  
4713 O OD1 . ASP B 298 ? 0.4425 0.3866 0.3905 0.0071  -0.0172 0.0491  298 ASP B OD1 
4714 O OD2 . ASP B 298 ? 0.4331 0.3869 0.3775 0.0014  -0.0177 0.0282  298 ASP B OD2 
4715 N N   . GLU B 299 ? 0.4484 0.3807 0.4669 -0.0062 0.0172  0.0233  299 GLU B N   
4716 C CA  . GLU B 299 ? 0.4292 0.3656 0.4454 -0.0035 0.0157  0.0200  299 GLU B CA  
4717 C C   . GLU B 299 ? 0.4357 0.3715 0.4492 -0.0067 0.0131  0.0167  299 GLU B C   
4718 O O   . GLU B 299 ? 0.4685 0.4119 0.4832 -0.0071 0.0116  0.0154  299 GLU B O   
4719 C CB  . GLU B 299 ? 0.4584 0.3887 0.4693 0.0023  0.0163  0.0174  299 GLU B CB  
4720 C CG  . GLU B 299 ? 0.4968 0.4147 0.5003 0.0032  0.0156  0.0139  299 GLU B CG  
4721 C CD  . GLU B 299 ? 0.5389 0.4477 0.5410 0.0031  0.0174  0.0161  299 GLU B CD  
4722 O OE1 . GLU B 299 ? 0.5713 0.4695 0.5673 0.0043  0.0170  0.0136  299 GLU B OE1 
4723 O OE2 . GLU B 299 ? 0.5940 0.5060 0.6011 0.0015  0.0191  0.0202  299 GLU B OE2 
4724 N N   . ALA B 300 ? 0.4087 0.3356 0.4186 -0.0090 0.0126  0.0154  300 ALA B N   
4725 C CA  . ALA B 300 ? 0.4126 0.3378 0.4197 -0.0121 0.0103  0.0121  300 ALA B CA  
4726 C C   . ALA B 300 ? 0.4196 0.3544 0.4322 -0.0170 0.0091  0.0137  300 ALA B C   
4727 O O   . ALA B 300 ? 0.3780 0.3159 0.3894 -0.0187 0.0070  0.0110  300 ALA B O   
4728 C CB  . ALA B 300 ? 0.4341 0.3475 0.4368 -0.0136 0.0105  0.0110  300 ALA B CB  
4729 N N   . PHE B 301 ? 0.4205 0.3597 0.4390 -0.0192 0.0105  0.0181  301 PHE B N   
4730 C CA  . PHE B 301 ? 0.4169 0.3656 0.4413 -0.0236 0.0095  0.0200  301 PHE B CA  
4731 C C   . PHE B 301 ? 0.4179 0.3775 0.4453 -0.0218 0.0087  0.0205  301 PHE B C   
4732 O O   . PHE B 301 ? 0.3819 0.3478 0.4102 -0.0241 0.0067  0.0192  301 PHE B O   
4733 C CB  . PHE B 301 ? 0.4461 0.3958 0.4759 -0.0263 0.0112  0.0244  301 PHE B CB  
4734 C CG  . PHE B 301 ? 0.4605 0.4197 0.4966 -0.0308 0.0102  0.0265  301 PHE B CG  
4735 C CD1 . PHE B 301 ? 0.4899 0.4489 0.5254 -0.0352 0.0084  0.0248  301 PHE B CD1 
4736 C CD2 . PHE B 301 ? 0.4655 0.4339 0.5083 -0.0307 0.0111  0.0304  301 PHE B CD2 
4737 C CE1 . PHE B 301 ? 0.4700 0.4380 0.5115 -0.0393 0.0074  0.0267  301 PHE B CE1 
4738 C CE2 . PHE B 301 ? 0.4335 0.4106 0.4822 -0.0347 0.0101  0.0324  301 PHE B CE2 
4739 C CZ  . PHE B 301 ? 0.4529 0.4298 0.5009 -0.0390 0.0082  0.0306  301 PHE B CZ  
4740 N N   . LEU B 302 ? 0.4109 0.3725 0.4396 -0.0177 0.0104  0.0221  302 LEU B N   
4741 C CA  . LEU B 302 ? 0.4011 0.3723 0.4323 -0.0155 0.0101  0.0225  302 LEU B CA  
4742 C C   . LEU B 302 ? 0.4485 0.4199 0.4748 -0.0142 0.0081  0.0179  302 LEU B C   
4743 O O   . LEU B 302 ? 0.4026 0.3827 0.4310 -0.0151 0.0067  0.0176  302 LEU B O   
4744 C CB  . LEU B 302 ? 0.3864 0.3582 0.4191 -0.0109 0.0125  0.0244  302 LEU B CB  
4745 C CG  . LEU B 302 ? 0.3672 0.3394 0.4050 -0.0118 0.0148  0.0290  302 LEU B CG  
4746 C CD1 . LEU B 302 ? 0.3822 0.3555 0.4211 -0.0069 0.0171  0.0304  302 LEU B CD1 
4747 C CD2 . LEU B 302 ? 0.3744 0.3555 0.4192 -0.0161 0.0144  0.0323  302 LEU B CD2 
4748 N N   . GLN B 303 ? 0.4354 0.3971 0.4551 -0.0120 0.0078  0.0143  303 GLN B N   
4749 C CA  . GLN B 303 ? 0.4577 0.4181 0.4723 -0.0106 0.0060  0.0095  303 GLN B CA  
4750 C C   . GLN B 303 ? 0.4414 0.4048 0.4561 -0.0153 0.0036  0.0078  303 GLN B C   
4751 O O   . GLN B 303 ? 0.4433 0.4124 0.4574 -0.0153 0.0020  0.0057  303 GLN B O   
4752 C CB  . GLN B 303 ? 0.4564 0.4051 0.4644 -0.0074 0.0064  0.0062  303 GLN B CB  
4753 C CG  . GLN B 303 ? 0.4724 0.4192 0.4794 -0.0018 0.0083  0.0066  303 GLN B CG  
4754 C CD  . GLN B 303 ? 0.5132 0.4479 0.5145 0.0010  0.0090  0.0046  303 GLN B CD  
4755 O OE1 . GLN B 303 ? 0.5055 0.4325 0.5031 -0.0011 0.0080  0.0026  303 GLN B OE1 
4756 N NE2 . GLN B 303 ? 0.5038 0.4366 0.5043 0.0058  0.0107  0.0051  303 GLN B NE2 
4757 N N   . GLN B 304 ? 0.4405 0.4001 0.4559 -0.0193 0.0034  0.0088  304 GLN B N   
4758 C CA  . GLN B 304 ? 0.4816 0.4442 0.4976 -0.0242 0.0013  0.0074  304 GLN B CA  
4759 C C   . GLN B 304 ? 0.4526 0.4273 0.4743 -0.0266 0.0004  0.0099  304 GLN B C   
4760 O O   . GLN B 304 ? 0.4843 0.4640 0.5053 -0.0282 -0.0017 0.0077  304 GLN B O   
4761 C CB  . GLN B 304 ? 0.5150 0.4711 0.5311 -0.0279 0.0016  0.0083  304 GLN B CB  
4762 C CG  . GLN B 304 ? 0.5803 0.5377 0.5960 -0.0327 -0.0005 0.0060  304 GLN B CG  
4763 C CD  . GLN B 304 ? 0.6715 0.6250 0.6812 -0.0317 -0.0022 0.0008  304 GLN B CD  
4764 O OE1 . GLN B 304 ? 0.7387 0.6984 0.7486 -0.0336 -0.0042 -0.0011 304 GLN B OE1 
4765 N NE2 . GLN B 304 ? 0.6793 0.6225 0.6836 -0.0288 -0.0015 -0.0016 304 GLN B NE2 
4766 N N   . VAL B 305 ? 0.4140 0.3935 0.4414 -0.0266 0.0019  0.0145  305 VAL B N   
4767 C CA  . VAL B 305 ? 0.3907 0.3820 0.4242 -0.0286 0.0013  0.0173  305 VAL B CA  
4768 C C   . VAL B 305 ? 0.4028 0.4004 0.4351 -0.0259 0.0004  0.0157  305 VAL B C   
4769 O O   . VAL B 305 ? 0.3276 0.3327 0.3613 -0.0282 -0.0015 0.0152  305 VAL B O   
4770 C CB  . VAL B 305 ? 0.4082 0.4030 0.4479 -0.0284 0.0034  0.0224  305 VAL B CB  
4771 C CG1 . VAL B 305 ? 0.3855 0.3925 0.4314 -0.0296 0.0028  0.0254  305 VAL B CG1 
4772 C CG2 . VAL B 305 ? 0.4240 0.4137 0.4654 -0.0320 0.0041  0.0241  305 VAL B CG2 
4773 N N   . MET B 306 ? 0.4043 0.3986 0.4337 -0.0209 0.0018  0.0146  306 MET B N   
4774 C CA  . MET B 306 ? 0.4079 0.4072 0.4357 -0.0179 0.0012  0.0125  306 MET B CA  
4775 C C   . MET B 306 ? 0.3959 0.3940 0.4188 -0.0193 -0.0013 0.0077  306 MET B C   
4776 O O   . MET B 306 ? 0.3843 0.3899 0.4077 -0.0197 -0.0026 0.0069  306 MET B O   
4777 C CB  . MET B 306 ? 0.4123 0.4073 0.4376 -0.0123 0.0032  0.0118  306 MET B CB  
4778 C CG  . MET B 306 ? 0.3952 0.3958 0.4261 -0.0103 0.0054  0.0162  306 MET B CG  
4779 S SD  . MET B 306 ? 0.3709 0.3678 0.3993 -0.0036 0.0078  0.0152  306 MET B SD  
4780 C CE  . MET B 306 ? 0.4099 0.3929 0.4327 -0.0026 0.0083  0.0130  306 MET B CE  
4781 N N   . LYS B 307 ? 0.3332 0.3219 0.3513 -0.0199 -0.0018 0.0047  307 LYS B N   
4782 C CA  . LYS B 307 ? 0.4085 0.3951 0.4220 -0.0212 -0.0040 -0.0001 307 LYS B CA  
4783 C C   . LYS B 307 ? 0.3702 0.3639 0.3864 -0.0264 -0.0060 0.0003  307 LYS B C   
4784 O O   . LYS B 307 ? 0.3652 0.3637 0.3799 -0.0270 -0.0078 -0.0021 307 LYS B O   
4785 C CB  . LYS B 307 ? 0.4485 0.4233 0.4569 -0.0211 -0.0039 -0.0030 307 LYS B CB  
4786 C CG  . LYS B 307 ? 0.4902 0.4621 0.4936 -0.0220 -0.0060 -0.0083 307 LYS B CG  
4787 C CD  . LYS B 307 ? 0.5649 0.5248 0.5632 -0.0212 -0.0058 -0.0112 307 LYS B CD  
4788 C CE  . LYS B 307 ? 0.6421 0.6003 0.6378 -0.0250 -0.0079 -0.0150 307 LYS B CE  
4789 N NZ  . LYS B 307 ? 0.6894 0.6374 0.6790 -0.0228 -0.0082 -0.0195 307 LYS B NZ  
4790 N N   . ASP B 308 ? 0.4037 0.3975 0.4234 -0.0301 -0.0059 0.0032  308 ASP B N   
4791 C CA  . ASP B 308 ? 0.4397 0.4399 0.4622 -0.0352 -0.0078 0.0037  308 ASP B CA  
4792 C C   . ASP B 308 ? 0.3814 0.3934 0.4086 -0.0355 -0.0084 0.0064  308 ASP B C   
4793 O O   . ASP B 308 ? 0.3463 0.3645 0.3735 -0.0378 -0.0105 0.0050  308 ASP B O   
4794 C CB  . ASP B 308 ? 0.5008 0.4984 0.5265 -0.0388 -0.0073 0.0062  308 ASP B CB  
4795 C CG  . ASP B 308 ? 0.5312 0.5172 0.5525 -0.0388 -0.0066 0.0038  308 ASP B CG  
4796 O OD1 . ASP B 308 ? 0.5725 0.5545 0.5959 -0.0403 -0.0053 0.0062  308 ASP B OD1 
4797 O OD2 . ASP B 308 ? 0.6478 0.6287 0.6637 -0.0374 -0.0074 -0.0005 308 ASP B OD2 
4798 N N   . GLY B 309 ? 0.3421 0.3570 0.3730 -0.0330 -0.0065 0.0102  309 GLY B N   
4799 C CA  . GLY B 309 ? 0.3457 0.3712 0.3810 -0.0326 -0.0067 0.0129  309 GLY B CA  
4800 C C   . GLY B 309 ? 0.3536 0.3831 0.3856 -0.0310 -0.0081 0.0098  309 GLY B C   
4801 O O   . GLY B 309 ? 0.3951 0.4325 0.4288 -0.0333 -0.0098 0.0101  309 GLY B O   
4802 N N   . ALA B 310 ? 0.3591 0.3828 0.3862 -0.0270 -0.0072 0.0066  310 ALA B N   
4803 C CA  . ALA B 310 ? 0.3427 0.3697 0.3667 -0.0248 -0.0080 0.0036  310 ALA B CA  
4804 C C   . ALA B 310 ? 0.3861 0.4138 0.4068 -0.0281 -0.0107 -0.0002 310 ALA B C   
4805 O O   . ALA B 310 ? 0.3713 0.4057 0.3917 -0.0285 -0.0120 -0.0013 310 ALA B O   
4806 C CB  . ALA B 310 ? 0.3615 0.3813 0.3810 -0.0197 -0.0065 0.0008  310 ALA B CB  
4807 N N   . GLU B 311 ? 0.4490 0.4698 0.4675 -0.0305 -0.0114 -0.0021 311 GLU B N   
4808 C CA  . GLU B 311 ? 0.4850 0.5063 0.5009 -0.0341 -0.0138 -0.0056 311 GLU B CA  
4809 C C   . GLU B 311 ? 0.4596 0.4907 0.4797 -0.0383 -0.0155 -0.0032 311 GLU B C   
4810 O O   . GLU B 311 ? 0.4527 0.4887 0.4712 -0.0398 -0.0174 -0.0055 311 GLU B O   
4811 C CB  . GLU B 311 ? 0.5619 0.5739 0.5752 -0.0360 -0.0140 -0.0078 311 GLU B CB  
4812 C CG  . GLU B 311 ? 0.6416 0.6549 0.6533 -0.0405 -0.0164 -0.0108 311 GLU B CG  
4813 C CD  . GLU B 311 ? 0.7226 0.7262 0.7310 -0.0419 -0.0164 -0.0137 311 GLU B CD  
4814 O OE1 . GLU B 311 ? 0.7333 0.7289 0.7410 -0.0399 -0.0146 -0.0128 311 GLU B OE1 
4815 O OE2 . GLU B 311 ? 0.7805 0.7844 0.7870 -0.0451 -0.0183 -0.0170 311 GLU B OE2 
4816 N N   . LYS B 312 ? 0.4384 0.4722 0.4639 -0.0402 -0.0148 0.0012  312 LYS B N   
4817 C CA  . LYS B 312 ? 0.4373 0.4803 0.4673 -0.0442 -0.0164 0.0038  312 LYS B CA  
4818 C C   . LYS B 312 ? 0.4199 0.4721 0.4516 -0.0426 -0.0168 0.0054  312 LYS B C   
4819 O O   . LYS B 312 ? 0.4629 0.5217 0.4946 -0.0450 -0.0188 0.0045  312 LYS B O   
4820 C CB  . LYS B 312 ? 0.4594 0.5029 0.4950 -0.0461 -0.0154 0.0082  312 LYS B CB  
4821 C CG  . LYS B 312 ? 0.4879 0.5228 0.5222 -0.0484 -0.0151 0.0070  312 LYS B CG  
4822 C CD  . LYS B 312 ? 0.5316 0.5670 0.5715 -0.0500 -0.0138 0.0114  312 LYS B CD  
4823 C CE  . LYS B 312 ? 0.5790 0.6058 0.6175 -0.0524 -0.0133 0.0101  312 LYS B CE  
4824 N NZ  . LYS B 312 ? 0.5825 0.6060 0.6247 -0.0519 -0.0110 0.0138  312 LYS B NZ  
4825 N N   . ALA B 313 ? 0.4115 0.4642 0.4447 -0.0385 -0.0147 0.0075  313 ALA B N   
4826 C CA  . ALA B 313 ? 0.3942 0.4552 0.4290 -0.0366 -0.0146 0.0091  313 ALA B CA  
4827 C C   . ALA B 313 ? 0.3860 0.4480 0.4156 -0.0358 -0.0160 0.0046  313 ALA B C   
4828 O O   . ALA B 313 ? 0.3922 0.4621 0.4227 -0.0374 -0.0175 0.0050  313 ALA B O   
4829 C CB  . ALA B 313 ? 0.3924 0.4526 0.4293 -0.0322 -0.0119 0.0117  313 ALA B CB  
4830 N N   . SER B 314 ? 0.4351 0.4889 0.4591 -0.0337 -0.0156 0.0002  314 SER B N   
4831 C CA  . SER B 314 ? 0.4323 0.4862 0.4511 -0.0329 -0.0169 -0.0046 314 SER B CA  
4832 C C   . SER B 314 ? 0.4652 0.5234 0.4831 -0.0376 -0.0197 -0.0065 314 SER B C   
4833 O O   . SER B 314 ? 0.4167 0.4790 0.4321 -0.0377 -0.0209 -0.0089 314 SER B O   
4834 C CB  . SER B 314 ? 0.4665 0.5101 0.4799 -0.0303 -0.0161 -0.0091 314 SER B CB  
4835 O OG  . SER B 314 ? 0.5486 0.5887 0.5621 -0.0255 -0.0137 -0.0080 314 SER B OG  
4836 N N   . ALA B 315 ? 0.5295 0.5862 0.5491 -0.0415 -0.0206 -0.0057 315 ALA B N   
4837 C CA  . ALA B 315 ? 0.5689 0.6300 0.5882 -0.0462 -0.0233 -0.0072 315 ALA B CA  
4838 C C   . ALA B 315 ? 0.5337 0.6060 0.5568 -0.0478 -0.0244 -0.0039 315 ALA B C   
4839 O O   . ALA B 315 ? 0.6142 0.6914 0.6353 -0.0495 -0.0263 -0.0060 315 ALA B O   
4840 C CB  . ALA B 315 ? 0.5984 0.6555 0.6192 -0.0497 -0.0237 -0.0068 315 ALA B CB  
4841 N N   . HIS B 316 ? 0.5046 0.5807 0.5331 -0.0472 -0.0233 0.0012  316 HIS B N   
4842 C CA  . HIS B 316 ? 0.4896 0.5761 0.5220 -0.0481 -0.0241 0.0047  316 HIS B CA  
4843 C C   . HIS B 316 ? 0.4435 0.5330 0.4733 -0.0447 -0.0236 0.0035  316 HIS B C   
4844 O O   . HIS B 316 ? 0.4117 0.5074 0.4402 -0.0462 -0.0253 0.0025  316 HIS B O   
4845 C CB  . HIS B 316 ? 0.4864 0.5756 0.5253 -0.0478 -0.0226 0.0103  316 HIS B CB  
4846 C CG  . HIS B 316 ? 0.5719 0.6606 0.6143 -0.0518 -0.0234 0.0121  316 HIS B CG  
4847 N ND1 . HIS B 316 ? 0.5988 0.6951 0.6445 -0.0558 -0.0256 0.0139  316 HIS B ND1 
4848 C CD2 . HIS B 316 ? 0.6132 0.6949 0.6565 -0.0524 -0.0223 0.0124  316 HIS B CD2 
4849 C CE1 . HIS B 316 ? 0.6346 0.7287 0.6832 -0.0587 -0.0257 0.0150  316 HIS B CE1 
4850 N NE2 . HIS B 316 ? 0.6381 0.7232 0.6852 -0.0567 -0.0237 0.0142  316 HIS B NE2 
4851 N N   . ALA B 317 ? 0.3956 0.4805 0.4244 -0.0402 -0.0211 0.0034  317 ALA B N   
4852 C CA  . ALA B 317 ? 0.3764 0.4641 0.4037 -0.0364 -0.0200 0.0029  317 ALA B CA  
4853 C C   . ALA B 317 ? 0.3497 0.4377 0.3713 -0.0366 -0.0215 -0.0021 317 ALA B C   
4854 O O   . ALA B 317 ? 0.3369 0.4315 0.3583 -0.0364 -0.0220 -0.0018 317 ALA B O   
4855 C CB  . ALA B 317 ? 0.3642 0.4457 0.3910 -0.0316 -0.0171 0.0030  317 ALA B CB  
4856 N N   . SER B 318 ? 0.3510 0.4316 0.3680 -0.0373 -0.0222 -0.0068 318 SER B N   
4857 C CA  . SER B 318 ? 0.3887 0.4685 0.4002 -0.0376 -0.0235 -0.0121 318 SER B CA  
4858 C C   . SER B 318 ? 0.3706 0.4584 0.3824 -0.0419 -0.0262 -0.0121 318 SER B C   
4859 O O   . SER B 318 ? 0.4035 0.4946 0.4121 -0.0417 -0.0269 -0.0146 318 SER B O   
4860 C CB  . SER B 318 ? 0.3902 0.4605 0.3974 -0.0379 -0.0238 -0.0168 318 SER B CB  
4861 O OG  . SER B 318 ? 0.4612 0.5304 0.4701 -0.0421 -0.0251 -0.0160 318 SER B OG  
4862 N N   . ARG B 319 ? 0.3738 0.4644 0.3892 -0.0458 -0.0275 -0.0093 319 ARG B N   
4863 C CA  . ARG B 319 ? 0.4016 0.5000 0.4177 -0.0502 -0.0301 -0.0089 319 ARG B CA  
4864 C C   . ARG B 319 ? 0.4030 0.5103 0.4211 -0.0493 -0.0302 -0.0059 319 ARG B C   
4865 O O   . ARG B 319 ? 0.4376 0.5496 0.4530 -0.0507 -0.0318 -0.0078 319 ARG B O   
4866 C CB  . ARG B 319 ? 0.4373 0.5371 0.4577 -0.0541 -0.0312 -0.0061 319 ARG B CB  
4867 N N   . THR B 320 ? 0.3765 0.4859 0.3992 -0.0469 -0.0283 -0.0012 320 THR B N   
4868 C CA  . THR B 320 ? 0.3920 0.5093 0.4169 -0.0454 -0.0280 0.0020  320 THR B CA  
4869 C C   . THR B 320 ? 0.3987 0.5153 0.4189 -0.0421 -0.0270 -0.0013 320 THR B C   
4870 O O   . THR B 320 ? 0.3915 0.5143 0.4105 -0.0428 -0.0280 -0.0015 320 THR B O   
4871 C CB  . THR B 320 ? 0.3802 0.4990 0.4111 -0.0434 -0.0259 0.0075  320 THR B CB  
4872 O OG1 . THR B 320 ? 0.3883 0.5091 0.4238 -0.0470 -0.0271 0.0106  320 THR B OG1 
4873 C CG2 . THR B 320 ? 0.3967 0.5233 0.4302 -0.0416 -0.0252 0.0109  320 THR B CG2 
4874 N N   . LEU B 321 ? 0.4064 0.5154 0.4239 -0.0384 -0.0249 -0.0040 321 LEU B N   
4875 C CA  . LEU B 321 ? 0.3768 0.4848 0.3900 -0.0349 -0.0238 -0.0074 321 LEU B CA  
4876 C C   . LEU B 321 ? 0.3400 0.4485 0.3478 -0.0372 -0.0259 -0.0125 321 LEU B C   
4877 O O   . LEU B 321 ? 0.3709 0.4828 0.3762 -0.0361 -0.0258 -0.0141 321 LEU B O   
4878 C CB  . LEU B 321 ? 0.3694 0.4687 0.3808 -0.0307 -0.0214 -0.0096 321 LEU B CB  
4879 C CG  . LEU B 321 ? 0.3483 0.4467 0.3562 -0.0264 -0.0197 -0.0126 321 LEU B CG  
4880 C CD1 . LEU B 321 ? 0.3619 0.4658 0.3739 -0.0236 -0.0176 -0.0082 321 LEU B CD1 
4881 C CD2 . LEU B 321 ? 0.3228 0.4116 0.3273 -0.0231 -0.0182 -0.0166 321 LEU B CD2 
4882 N N   . LYS B 322 ? 0.4215 0.5263 0.4274 -0.0404 -0.0277 -0.0153 322 LYS B N   
4883 C CA  . LYS B 322 ? 0.4473 0.5529 0.4485 -0.0431 -0.0298 -0.0201 322 LYS B CA  
4884 C C   . LYS B 322 ? 0.4203 0.5357 0.4221 -0.0459 -0.0316 -0.0183 322 LYS B C   
4885 O O   . LYS B 322 ? 0.4111 0.5287 0.4089 -0.0462 -0.0324 -0.0216 322 LYS B O   
4886 C CB  . LYS B 322 ? 0.4820 0.5827 0.4822 -0.0465 -0.0314 -0.0225 322 LYS B CB  
4887 C CG  . LYS B 322 ? 0.5882 0.6906 0.5844 -0.0502 -0.0338 -0.0270 322 LYS B CG  
4888 C CD  . LYS B 322 ? 0.6404 0.7357 0.6344 -0.0522 -0.0347 -0.0310 322 LYS B CD  
4889 C CE  . LYS B 322 ? 0.6948 0.7908 0.6840 -0.0548 -0.0366 -0.0365 322 LYS B CE  
4890 N NZ  . LYS B 322 ? 0.7518 0.8464 0.7410 -0.0592 -0.0384 -0.0383 322 LYS B NZ  
4891 N N   . ALA B 323 ? 0.4344 0.5555 0.4412 -0.0479 -0.0324 -0.0131 323 ALA B N   
4892 C CA  . ALA B 323 ? 0.4671 0.5975 0.4751 -0.0504 -0.0341 -0.0106 323 ALA B CA  
4893 C C   . ALA B 323 ? 0.4517 0.5865 0.4601 -0.0471 -0.0325 -0.0086 323 ALA B C   
4894 O O   . ALA B 323 ? 0.3738 0.5142 0.3802 -0.0482 -0.0336 -0.0091 323 ALA B O   
4895 C CB  . ALA B 323 ? 0.4939 0.6289 0.5076 -0.0535 -0.0353 -0.0057 323 ALA B CB  
4896 N N   . VAL B 324 ? 0.4299 0.5622 0.4410 -0.0430 -0.0298 -0.0062 324 VAL B N   
4897 C CA  . VAL B 324 ? 0.4211 0.5565 0.4324 -0.0393 -0.0278 -0.0048 324 VAL B CA  
4898 C C   . VAL B 324 ? 0.4316 0.5647 0.4365 -0.0378 -0.0275 -0.0106 324 VAL B C   
4899 O O   . VAL B 324 ? 0.3915 0.5298 0.3947 -0.0377 -0.0276 -0.0107 324 VAL B O   
4900 C CB  . VAL B 324 ? 0.4146 0.5466 0.4295 -0.0350 -0.0247 -0.0021 324 VAL B CB  
4901 C CG1 . VAL B 324 ? 0.3879 0.5226 0.4026 -0.0310 -0.0223 -0.0016 324 VAL B CG1 
4902 C CG2 . VAL B 324 ? 0.4281 0.5633 0.4497 -0.0364 -0.0248 0.0038  324 VAL B CG2 
4903 N N   . TYR B 325 ? 0.4294 0.5544 0.4307 -0.0368 -0.0271 -0.0154 325 TYR B N   
4904 C CA  . TYR B 325 ? 0.4801 0.6018 0.4754 -0.0352 -0.0267 -0.0213 325 TYR B CA  
4905 C C   . TYR B 325 ? 0.5225 0.6484 0.5141 -0.0393 -0.0294 -0.0242 325 TYR B C   
4906 O O   . TYR B 325 ? 0.4890 0.6168 0.4770 -0.0384 -0.0291 -0.0270 325 TYR B O   
4907 C CB  . TYR B 325 ? 0.4689 0.5809 0.4617 -0.0334 -0.0258 -0.0255 325 TYR B CB  
4908 C CG  . TYR B 325 ? 0.4029 0.5102 0.3971 -0.0281 -0.0227 -0.0247 325 TYR B CG  
4909 C CD1 . TYR B 325 ? 0.3840 0.4958 0.3824 -0.0256 -0.0208 -0.0198 325 TYR B CD1 
4910 C CD2 . TYR B 325 ? 0.4010 0.4995 0.3923 -0.0257 -0.0218 -0.0288 325 TYR B CD2 
4911 C CE1 . TYR B 325 ? 0.3707 0.4785 0.3704 -0.0208 -0.0179 -0.0192 325 TYR B CE1 
4912 C CE2 . TYR B 325 ? 0.3583 0.4526 0.3508 -0.0209 -0.0190 -0.0280 325 TYR B CE2 
4913 C CZ  . TYR B 325 ? 0.3568 0.4559 0.3535 -0.0185 -0.0170 -0.0233 325 TYR B CZ  
4914 O OH  . TYR B 325 ? 0.3313 0.4267 0.3292 -0.0138 -0.0142 -0.0226 325 TYR B OH  
4915 N N   . GLU B 326 ? 0.5666 0.6942 0.5593 -0.0437 -0.0318 -0.0235 326 GLU B N   
4916 C CA  . GLU B 326 ? 0.5728 0.7053 0.5627 -0.0479 -0.0345 -0.0256 326 GLU B CA  
4917 C C   . GLU B 326 ? 0.5252 0.6663 0.5162 -0.0482 -0.0348 -0.0220 326 GLU B C   
4918 O O   . GLU B 326 ? 0.4999 0.6436 0.4868 -0.0488 -0.0353 -0.0249 326 GLU B O   
4919 C CB  . GLU B 326 ? 0.6502 0.7831 0.6419 -0.0525 -0.0369 -0.0248 326 GLU B CB  
4920 C CG  . GLU B 326 ? 0.7239 0.8617 0.7128 -0.0572 -0.0398 -0.0271 326 GLU B CG  
4921 C CD  . GLU B 326 ? 0.7934 0.9278 0.7760 -0.0572 -0.0400 -0.0339 326 GLU B CD  
4922 O OE1 . GLU B 326 ? 0.8380 0.9645 0.8185 -0.0559 -0.0392 -0.0380 326 GLU B OE1 
4923 O OE2 . GLU B 326 ? 0.8774 1.0170 0.8572 -0.0585 -0.0410 -0.0352 326 GLU B OE2 
4924 N N   . ALA B 327 ? 0.4879 0.6333 0.4844 -0.0477 -0.0343 -0.0159 327 ALA B N   
4925 C CA  . ALA B 327 ? 0.4994 0.6532 0.4977 -0.0479 -0.0345 -0.0119 327 ALA B CA  
4926 C C   . ALA B 327 ? 0.5213 0.6756 0.5169 -0.0442 -0.0323 -0.0133 327 ALA B C   
4927 O O   . ALA B 327 ? 0.5703 0.7299 0.5635 -0.0453 -0.0331 -0.0136 327 ALA B O   
4928 C CB  . ALA B 327 ? 0.4344 0.5914 0.4395 -0.0474 -0.0339 -0.0053 327 ALA B CB  
4929 N N   . ILE B 328 ? 0.5440 0.6927 0.5398 -0.0398 -0.0295 -0.0144 328 ILE B N   
4930 C CA  . ILE B 328 ? 0.5435 0.6929 0.5375 -0.0358 -0.0270 -0.0153 328 ILE B CA  
4931 C C   . ILE B 328 ? 0.5093 0.6557 0.4965 -0.0358 -0.0272 -0.0221 328 ILE B C   
4932 O O   . ILE B 328 ? 0.5656 0.7137 0.5505 -0.0336 -0.0257 -0.0234 328 ILE B O   
4933 C CB  . ILE B 328 ? 0.5681 0.7135 0.5653 -0.0309 -0.0237 -0.0137 328 ILE B CB  
4934 C CG1 . ILE B 328 ? 0.6106 0.7467 0.6057 -0.0294 -0.0231 -0.0178 328 ILE B CG1 
4935 C CG2 . ILE B 328 ? 0.5877 0.7371 0.5917 -0.0311 -0.0234 -0.0068 328 ILE B CG2 
4936 C CD1 . ILE B 328 ? 0.6228 0.7546 0.6199 -0.0243 -0.0198 -0.0171 328 ILE B CD1 
4937 N N   . GLY B 329 ? 0.4800 0.6218 0.4642 -0.0382 -0.0289 -0.0264 329 GLY B N   
4938 C CA  . GLY B 329 ? 0.5047 0.6444 0.4827 -0.0393 -0.0298 -0.0329 329 GLY B CA  
4939 C C   . GLY B 329 ? 0.4868 0.6178 0.4617 -0.0363 -0.0283 -0.0384 329 GLY B C   
4940 O O   . GLY B 329 ? 0.4828 0.6123 0.4529 -0.0358 -0.0280 -0.0436 329 GLY B O   
4941 N N   . PHE B 330 ? 0.4646 0.5900 0.4422 -0.0343 -0.0272 -0.0373 330 PHE B N   
4942 C CA  . PHE B 330 ? 0.4375 0.5542 0.4124 -0.0316 -0.0260 -0.0423 330 PHE B CA  
4943 C C   . PHE B 330 ? 0.3903 0.5034 0.3619 -0.0352 -0.0284 -0.0470 330 PHE B C   
4944 O O   . PHE B 330 ? 0.4281 0.5438 0.4013 -0.0394 -0.0306 -0.0451 330 PHE B O   
4945 C CB  . PHE B 330 ? 0.4238 0.5356 0.4026 -0.0283 -0.0241 -0.0393 330 PHE B CB  
4946 C CG  . PHE B 330 ? 0.4050 0.5187 0.3865 -0.0238 -0.0212 -0.0360 330 PHE B CG  
4947 C CD1 . PHE B 330 ? 0.4676 0.5780 0.4531 -0.0210 -0.0193 -0.0327 330 PHE B CD1 
4948 C CD2 . PHE B 330 ? 0.4312 0.5501 0.4115 -0.0225 -0.0201 -0.0361 330 PHE B CD2 
4949 C CE1 . PHE B 330 ? 0.3976 0.5098 0.3859 -0.0169 -0.0165 -0.0298 330 PHE B CE1 
4950 C CE2 . PHE B 330 ? 0.4043 0.5250 0.3874 -0.0184 -0.0173 -0.0331 330 PHE B CE2 
4951 C CZ  . PHE B 330 ? 0.4184 0.5358 0.4055 -0.0156 -0.0155 -0.0300 330 PHE B CZ  
4952 N N   . VAL B 331 ? 0.3879 0.4951 0.3550 -0.0338 -0.0280 -0.0532 331 VAL B N   
4953 C CA  . VAL B 331 ? 0.3891 0.4913 0.3534 -0.0365 -0.0299 -0.0581 331 VAL B CA  
4954 C C   . VAL B 331 ? 0.4515 0.5481 0.4189 -0.0359 -0.0296 -0.0559 331 VAL B C   
4955 O O   . VAL B 331 ? 0.4192 0.5113 0.3878 -0.0317 -0.0274 -0.0550 331 VAL B O   
4956 C CB  . VAL B 331 ? 0.3931 0.4900 0.3524 -0.0346 -0.0292 -0.0653 331 VAL B CB  
4957 C CG1 . VAL B 331 ? 0.4078 0.4979 0.3650 -0.0364 -0.0307 -0.0699 331 VAL B CG1 
4958 C CG2 . VAL B 331 ? 0.4330 0.5353 0.3887 -0.0365 -0.0300 -0.0681 331 VAL B CG2 
4959 N N   . ALA B 332 ? 0.5123 0.6092 0.4808 -0.0401 -0.0317 -0.0553 332 ALA B N   
4960 C CA  . ALA B 332 ? 0.5196 0.6117 0.4912 -0.0403 -0.0316 -0.0529 332 ALA B CA  
4961 C C   . ALA B 332 ? 0.5188 0.6013 0.4875 -0.0381 -0.0309 -0.0578 332 ALA B C   
4962 O O   . ALA B 332 ? 0.5330 0.6132 0.4977 -0.0392 -0.0319 -0.0635 332 ALA B O   
4963 C CB  . ALA B 332 ? 0.5362 0.6319 0.5096 -0.0457 -0.0341 -0.0512 332 ALA B CB  
4964 N N   . LYS B 333 ? 0.5319 0.6089 0.5028 -0.0349 -0.0292 -0.0556 333 LYS B N   
4965 C CA  . LYS B 333 ? 0.5966 0.6638 0.5651 -0.0325 -0.0285 -0.0597 333 LYS B CA  
4966 C C   . LYS B 333 ? 0.6596 0.7235 0.6274 -0.0366 -0.0305 -0.0618 333 LYS B C   
4967 O O   . LYS B 333 ? 0.7067 0.7745 0.6775 -0.0403 -0.0318 -0.0584 333 LYS B O   
4968 C CB  . LYS B 333 ? 0.6046 0.6675 0.5761 -0.0286 -0.0263 -0.0558 333 LYS B CB  
4969 C CG  . LYS B 333 ? 0.6240 0.6767 0.5936 -0.0261 -0.0255 -0.0590 333 LYS B CG  
4970 C CD  . LYS B 333 ? 0.6472 0.6964 0.6197 -0.0220 -0.0232 -0.0550 333 LYS B CD  
4971 C CE  . LYS B 333 ? 0.6421 0.6808 0.6125 -0.0198 -0.0226 -0.0578 333 LYS B CE  
4972 N NZ  . LYS B 333 ? 0.6374 0.6717 0.6053 -0.0144 -0.0207 -0.0608 333 LYS B NZ  
4973 N N   . ARG B 334 ? 0.7861 0.8429 0.7503 -0.0360 -0.0308 -0.0675 334 ARG B N   
4974 C CA  . ARG B 334 ? 0.8447 0.8974 0.8082 -0.0396 -0.0325 -0.0699 334 ARG B CA  
4975 C C   . ARG B 334 ? 0.8719 0.9154 0.8358 -0.0372 -0.0313 -0.0698 334 ARG B C   
4976 O O   . ARG B 334 ? 0.8903 0.9271 0.8515 -0.0334 -0.0302 -0.0733 334 ARG B O   
4977 C CB  . ARG B 334 ? 0.9061 0.9578 0.8652 -0.0415 -0.0339 -0.0767 334 ARG B CB  
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