data_9D8U
# 
_entry.id   9D8U 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9D8U         pdb_00009d8u 10.2210/pdb9d8u/pdb 
WWPDB D_1000287571 ?            ?                   
# 
_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       2025-03-26 
_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                        9D8U 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'The X-ray co-crystal structure of human CDK6 and Palbociclib'     5L2I unspecified 
PDB 'Crystal structure of CDK4 cyclin D1 in complex with atirmociclib' 9CSK unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              eric.johnson2@pfizer.com 
_pdbx_contact_author.name_first         Eric 
_pdbx_contact_author.name_last          Johnson 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2909-865X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Johnson, E.' 1 0000-0002-2909-865X 
'Chen, P.'    2 ?                   
'Ferre, R.A.' 3 ?                   
'Deihl, W.'   4 ?                   
'Yu, X.'      5 ?                   
'He, Y.-A.'   6 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Cancer Cell' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1535-6108 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            43 
_citation.language                  ? 
_citation.page_first                464 
_citation.page_last                 481.e14 
_citation.title                     'CDK4 selective inhibition improves preclinical anti-tumor efficacy and safety.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ccell.2025.02.006 
_citation.pdbx_database_id_PubMed   40068598 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Palmer, C.L.'      1  ? 
primary 'Boras, B.'         2  ? 
primary 'Pascual, B.'       3  ? 
primary 'Li, N.'            4  ? 
primary 'Li, D.'            5  ? 
primary 'Garza, S.'         6  ? 
primary 'Huser, N.'         7  ? 
primary 'Yuan, J.T.'        8  ? 
primary 'Cianfrogna, J.A.'  9  ? 
primary 'Sung, T.'          10 ? 
primary 'McMillan, E.'      11 ? 
primary 'Wei, N.'           12 ? 
primary 'Carmody, J.'       13 ? 
primary 'Kang, A.N.'        14 ? 
primary 'Darensburg, S.'    15 ? 
primary 'Dodd, T.'          16 ? 
primary 'Oakley, J.V.'      17 ? 
primary 'Solowiej, J.'      18 ? 
primary 'Nguyen, L.'        19 ? 
primary 'Orr, S.T.M.'       20 ? 
primary 'Chen, P.'          21 ? 
primary 'Johnson, E.'       22 ? 
primary 'Yu, X.'            23 ? 
primary 'Diehl, W.C.'       24 ? 
primary 'Gallego, G.M.'     25 ? 
primary 'Jalaie, M.'        26 ? 
primary 'Ferre, R.A.'       27 ? 
primary 'Cho-Schultz, S.'   28 ? 
primary 'Shen, H.'          29 ? 
primary 'Deal, J.G.'        30 ? 
primary 'Zhang, Q.'         31 ? 
primary 'Baffi, T.R.'       32 ? 
primary 'Xu, M.'            33 ? 
primary 'Roh, W.'           34 ? 
primary 'Lapira-Miller, J.' 35 ? 
primary 'Goudeau, J.'       36 ? 
primary 'Yu, Y.'            37 ? 
primary 'Gupta, R.'         38 ? 
primary 'Kim, K.'           39 ? 
primary 'Dann, S.G.'        40 ? 
primary 'Kan, Z.'           41 ? 
primary 'Kath, J.C.'        42 ? 
primary 'Nair, S.K.'        43 ? 
primary 'Miller, N.'        44 ? 
primary 'Murray, B.W.'      45 ? 
primary 'Nager, A.R.'       46 ? 
primary 'Quinlan, C.'       47 ? 
primary 'Petroski, M.D.'    48 ? 
primary 'Zhang, C.'         49 ? 
primary 'Sacaan, A.'        50 ? 
primary 'VanArsdale, T.'    51 ? 
primary 'Anders, L.'        52 ? 
# 
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 'Cyclin-dependent kinase 6' 35019.215 1  2.7.11.22 ? ? ? 
2 non-polymer syn Atirmociclib                463.933   1  ?         ? ? ? 
3 water       nat water                       18.015    89 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cell division protein kinase 6,Serine/threonine-protein kinase PLSTIRE' 
# 
_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       
;MEKDGLCRADQQYECVAEIGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLF
DVCTVSRTDRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIK
LADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGE
EDWPRDVALPRQAFHSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYFQHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MEKDGLCRADQQYECVAEIGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLF
DVCTVSRTDRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIK
LADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGE
EDWPRDVALPRQAFHSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYFQHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 Atirmociclib A1AZ4 
3 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   GLU n 
1 3   LYS n 
1 4   ASP n 
1 5   GLY n 
1 6   LEU n 
1 7   CYS n 
1 8   ARG n 
1 9   ALA n 
1 10  ASP n 
1 11  GLN n 
1 12  GLN n 
1 13  TYR n 
1 14  GLU n 
1 15  CYS n 
1 16  VAL n 
1 17  ALA n 
1 18  GLU n 
1 19  ILE n 
1 20  GLY n 
1 21  GLU n 
1 22  GLY n 
1 23  ALA n 
1 24  TYR n 
1 25  GLY n 
1 26  LYS n 
1 27  VAL n 
1 28  PHE n 
1 29  LYS n 
1 30  ALA n 
1 31  ARG n 
1 32  ASP n 
1 33  LEU n 
1 34  LYS n 
1 35  ASN n 
1 36  GLY n 
1 37  GLY n 
1 38  ARG n 
1 39  PHE n 
1 40  VAL n 
1 41  ALA n 
1 42  LEU n 
1 43  LYS n 
1 44  ARG n 
1 45  VAL n 
1 46  ARG n 
1 47  VAL n 
1 48  GLN n 
1 49  THR n 
1 50  GLY n 
1 51  GLU n 
1 52  GLU n 
1 53  GLY n 
1 54  MET n 
1 55  PRO n 
1 56  LEU n 
1 57  SER n 
1 58  THR n 
1 59  ILE n 
1 60  ARG n 
1 61  GLU n 
1 62  VAL n 
1 63  ALA n 
1 64  VAL n 
1 65  LEU n 
1 66  ARG n 
1 67  HIS n 
1 68  LEU n 
1 69  GLU n 
1 70  THR n 
1 71  PHE n 
1 72  GLU n 
1 73  HIS n 
1 74  PRO n 
1 75  ASN n 
1 76  VAL n 
1 77  VAL n 
1 78  ARG n 
1 79  LEU n 
1 80  PHE n 
1 81  ASP n 
1 82  VAL n 
1 83  CYS n 
1 84  THR n 
1 85  VAL n 
1 86  SER n 
1 87  ARG n 
1 88  THR n 
1 89  ASP n 
1 90  ARG n 
1 91  GLU n 
1 92  THR n 
1 93  LYS n 
1 94  LEU n 
1 95  THR n 
1 96  LEU n 
1 97  VAL n 
1 98  PHE n 
1 99  GLU n 
1 100 HIS n 
1 101 VAL n 
1 102 ASP n 
1 103 GLN n 
1 104 ASP n 
1 105 LEU n 
1 106 THR n 
1 107 THR n 
1 108 TYR n 
1 109 LEU n 
1 110 ASP n 
1 111 LYS n 
1 112 VAL n 
1 113 PRO n 
1 114 GLU n 
1 115 PRO n 
1 116 GLY n 
1 117 VAL n 
1 118 PRO n 
1 119 THR n 
1 120 GLU n 
1 121 THR n 
1 122 ILE n 
1 123 LYS n 
1 124 ASP n 
1 125 MET n 
1 126 MET n 
1 127 PHE n 
1 128 GLN n 
1 129 LEU n 
1 130 LEU n 
1 131 ARG n 
1 132 GLY n 
1 133 LEU n 
1 134 ASP n 
1 135 PHE n 
1 136 LEU n 
1 137 HIS n 
1 138 SER n 
1 139 HIS n 
1 140 ARG n 
1 141 VAL n 
1 142 VAL n 
1 143 HIS n 
1 144 ARG n 
1 145 ASP n 
1 146 LEU n 
1 147 LYS n 
1 148 PRO n 
1 149 GLN n 
1 150 ASN n 
1 151 ILE n 
1 152 LEU n 
1 153 VAL n 
1 154 THR n 
1 155 SER n 
1 156 SER n 
1 157 GLY n 
1 158 GLN n 
1 159 ILE n 
1 160 LYS n 
1 161 LEU n 
1 162 ALA n 
1 163 ASP n 
1 164 PHE n 
1 165 GLY n 
1 166 LEU n 
1 167 ALA n 
1 168 ARG n 
1 169 ILE n 
1 170 TYR n 
1 171 SER n 
1 172 PHE n 
1 173 GLN n 
1 174 MET n 
1 175 ALA n 
1 176 LEU n 
1 177 THR n 
1 178 SER n 
1 179 VAL n 
1 180 VAL n 
1 181 VAL n 
1 182 THR n 
1 183 LEU n 
1 184 TRP n 
1 185 TYR n 
1 186 ARG n 
1 187 ALA n 
1 188 PRO n 
1 189 GLU n 
1 190 VAL n 
1 191 LEU n 
1 192 LEU n 
1 193 GLN n 
1 194 SER n 
1 195 SER n 
1 196 TYR n 
1 197 ALA n 
1 198 THR n 
1 199 PRO n 
1 200 VAL n 
1 201 ASP n 
1 202 LEU n 
1 203 TRP n 
1 204 SER n 
1 205 VAL n 
1 206 GLY n 
1 207 CYS n 
1 208 ILE n 
1 209 PHE n 
1 210 ALA n 
1 211 GLU n 
1 212 MET n 
1 213 PHE n 
1 214 ARG n 
1 215 ARG n 
1 216 LYS n 
1 217 PRO n 
1 218 LEU n 
1 219 PHE n 
1 220 ARG n 
1 221 GLY n 
1 222 SER n 
1 223 SER n 
1 224 ASP n 
1 225 VAL n 
1 226 ASP n 
1 227 GLN n 
1 228 LEU n 
1 229 GLY n 
1 230 LYS n 
1 231 ILE n 
1 232 LEU n 
1 233 ASP n 
1 234 VAL n 
1 235 ILE n 
1 236 GLY n 
1 237 LEU n 
1 238 PRO n 
1 239 GLY n 
1 240 GLU n 
1 241 GLU n 
1 242 ASP n 
1 243 TRP n 
1 244 PRO n 
1 245 ARG n 
1 246 ASP n 
1 247 VAL n 
1 248 ALA n 
1 249 LEU n 
1 250 PRO n 
1 251 ARG n 
1 252 GLN n 
1 253 ALA n 
1 254 PHE n 
1 255 HIS n 
1 256 SER n 
1 257 LYS n 
1 258 SER n 
1 259 ALA n 
1 260 GLN n 
1 261 PRO n 
1 262 ILE n 
1 263 GLU n 
1 264 LYS n 
1 265 PHE n 
1 266 VAL n 
1 267 THR n 
1 268 ASP n 
1 269 ILE n 
1 270 ASP n 
1 271 GLU n 
1 272 LEU n 
1 273 GLY n 
1 274 LYS n 
1 275 ASP n 
1 276 LEU n 
1 277 LEU n 
1 278 LEU n 
1 279 LYS n 
1 280 CYS n 
1 281 LEU n 
1 282 THR n 
1 283 PHE n 
1 284 ASN n 
1 285 PRO n 
1 286 ALA n 
1 287 LYS n 
1 288 ARG n 
1 289 ILE n 
1 290 SER n 
1 291 ALA n 
1 292 TYR n 
1 293 SER n 
1 294 ALA n 
1 295 LEU n 
1 296 SER n 
1 297 HIS n 
1 298 PRO n 
1 299 TYR n 
1 300 PHE n 
1 301 GLN n 
1 302 HIS n 
1 303 HIS n 
1 304 HIS n 
1 305 HIS n 
1 306 HIS n 
1 307 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                   307 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CDK6, CDKN6' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AZ4 non-polymer         . Atirmociclib    ? 'C22 H27 Cl F N5 O3' 463.933 
ALA   'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'         133.103 
CYS   'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'       121.158 
GLN   'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER           ? 'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE          ? 'C3 H7 N O3'         105.093 
THR   'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE          ? 'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   ?   ?   ?   A . n 
A 1 4   ASP 4   4   ?   ?   ?   A . n 
A 1 5   GLY 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   CYS 7   7   ?   ?   ?   A . n 
A 1 8   ARG 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  ASP 10  10  ?   ?   ?   A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  TYR 13  13  13  TYR TYR A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  CYS 15  15  15  CYS CYS A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  TYR 24  24  24  TYR ALA A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  LYS 26  26  26  LYS LYS A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  ASN 35  35  35  ASN ASN A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  ARG 44  44  44  ARG ARG A . n 
A 1 45  VAL 45  45  45  VAL ALA A . n 
A 1 46  ARG 46  46  46  ARG ALA A . n 
A 1 47  VAL 47  47  47  VAL ALA A . n 
A 1 48  GLN 48  48  ?   ?   ?   A . n 
A 1 49  THR 49  49  ?   ?   ?   A . n 
A 1 50  GLY 50  50  ?   ?   ?   A . n 
A 1 51  GLU 51  51  ?   ?   ?   A . n 
A 1 52  GLU 52  52  ?   ?   ?   A . n 
A 1 53  GLY 53  53  ?   ?   ?   A . n 
A 1 54  MET 54  54  ?   ?   ?   A . n 
A 1 55  PRO 55  55  55  PRO ALA A . n 
A 1 56  LEU 56  56  56  LEU ALA A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  HIS 67  67  67  HIS HIS A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  HIS 73  73  73  HIS HIS A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  CYS 83  83  83  CYS CYS A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  VAL 85  85  ?   ?   ?   A . n 
A 1 86  SER 86  86  ?   ?   ?   A . n 
A 1 87  ARG 87  87  ?   ?   ?   A . n 
A 1 88  THR 88  88  ?   ?   ?   A . n 
A 1 89  ASP 89  89  ?   ?   ?   A . n 
A 1 90  ARG 90  90  ?   ?   ?   A . n 
A 1 91  GLU 91  91  ?   ?   ?   A . n 
A 1 92  THR 92  92  ?   ?   ?   A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 MET 125 125 125 MET MET A . n 
A 1 126 MET 126 126 126 MET MET A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 HIS 137 137 137 HIS HIS A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 HIS 139 139 139 HIS HIS A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 PHE 164 164 164 PHE PHE A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 ARG 168 168 ?   ?   ?   A . n 
A 1 169 ILE 169 169 ?   ?   ?   A . n 
A 1 170 TYR 170 170 ?   ?   ?   A . n 
A 1 171 SER 171 171 ?   ?   ?   A . n 
A 1 172 PHE 172 172 ?   ?   ?   A . n 
A 1 173 GLN 173 173 ?   ?   ?   A . n 
A 1 174 MET 174 174 ?   ?   ?   A . n 
A 1 175 ALA 175 175 ?   ?   ?   A . n 
A 1 176 LEU 176 176 ?   ?   ?   A . n 
A 1 177 THR 177 177 ?   ?   ?   A . n 
A 1 178 SER 178 178 ?   ?   ?   A . n 
A 1 179 VAL 179 179 ?   ?   ?   A . n 
A 1 180 VAL 180 180 ?   ?   ?   A . n 
A 1 181 VAL 181 181 181 VAL ALA A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 TRP 184 184 184 TRP TRP A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 GLN 193 193 193 GLN GLN A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 TRP 203 203 203 TRP TRP A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 GLY 206 206 206 GLY GLY A . n 
A 1 207 CYS 207 207 207 CYS CYS A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 PHE 213 213 213 PHE PHE A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 LYS 216 216 216 LYS LYS A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 ASP 233 233 233 ASP ASP A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 TRP 243 243 243 TRP TRP A . n 
A 1 244 PRO 244 244 244 PRO PRO A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 ARG 251 251 251 ARG ARG A . n 
A 1 252 GLN 252 252 252 GLN GLN A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 GLN 260 260 260 GLN GLN A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 PHE 265 265 265 PHE PHE A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 ASP 268 268 268 ASP ASP A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 ASP 275 275 275 ASP ASP A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 CYS 280 280 280 CYS CYS A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 THR 282 282 282 THR THR A . n 
A 1 283 PHE 283 283 283 PHE PHE A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 ILE 289 289 289 ILE ILE A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 LEU 295 295 295 LEU LEU A . n 
A 1 296 SER 296 296 296 SER SER A . n 
A 1 297 HIS 297 297 297 HIS HIS A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 GLN 301 301 301 GLN GLN A . n 
A 1 302 HIS 302 302 ?   ?   ?   A . n 
A 1 303 HIS 303 303 ?   ?   ?   A . n 
A 1 304 HIS 304 304 ?   ?   ?   A . n 
A 1 305 HIS 305 305 ?   ?   ?   A . n 
A 1 306 HIS 306 306 ?   ?   ?   A . n 
A 1 307 HIS 307 307 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AZ4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AZ4 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1AZ4 1  401 401 A1AZ4 060 A . 
C 3 HOH   1  501 90  HOH   HOH A . 
C 3 HOH   2  502 10  HOH   HOH A . 
C 3 HOH   3  503 4   HOH   HOH A . 
C 3 HOH   4  504 83  HOH   HOH A . 
C 3 HOH   5  505 52  HOH   HOH A . 
C 3 HOH   6  506 5   HOH   HOH A . 
C 3 HOH   7  507 26  HOH   HOH A . 
C 3 HOH   8  508 58  HOH   HOH A . 
C 3 HOH   9  509 63  HOH   HOH A . 
C 3 HOH   10 510 59  HOH   HOH A . 
C 3 HOH   11 511 57  HOH   HOH A . 
C 3 HOH   12 512 65  HOH   HOH A . 
C 3 HOH   13 513 21  HOH   HOH A . 
C 3 HOH   14 514 81  HOH   HOH A . 
C 3 HOH   15 515 54  HOH   HOH A . 
C 3 HOH   16 516 25  HOH   HOH A . 
C 3 HOH   17 517 27  HOH   HOH A . 
C 3 HOH   18 518 86  HOH   HOH A . 
C 3 HOH   19 519 61  HOH   HOH A . 
C 3 HOH   20 520 16  HOH   HOH A . 
C 3 HOH   21 521 22  HOH   HOH A . 
C 3 HOH   22 522 15  HOH   HOH A . 
C 3 HOH   23 523 20  HOH   HOH A . 
C 3 HOH   24 524 55  HOH   HOH A . 
C 3 HOH   25 525 71  HOH   HOH A . 
C 3 HOH   26 526 3   HOH   HOH A . 
C 3 HOH   27 527 72  HOH   HOH A . 
C 3 HOH   28 528 28  HOH   HOH A . 
C 3 HOH   29 529 17  HOH   HOH A . 
C 3 HOH   30 530 41  HOH   HOH A . 
C 3 HOH   31 531 82  HOH   HOH A . 
C 3 HOH   32 532 9   HOH   HOH A . 
C 3 HOH   33 533 12  HOH   HOH A . 
C 3 HOH   34 534 1   HOH   HOH A . 
C 3 HOH   35 535 85  HOH   HOH A . 
C 3 HOH   36 536 84  HOH   HOH A . 
C 3 HOH   37 537 42  HOH   HOH A . 
C 3 HOH   38 538 32  HOH   HOH A . 
C 3 HOH   39 539 11  HOH   HOH A . 
C 3 HOH   40 540 6   HOH   HOH A . 
C 3 HOH   41 541 88  HOH   HOH A . 
C 3 HOH   42 542 47  HOH   HOH A . 
C 3 HOH   43 543 18  HOH   HOH A . 
C 3 HOH   44 544 39  HOH   HOH A . 
C 3 HOH   45 545 24  HOH   HOH A . 
C 3 HOH   46 546 35  HOH   HOH A . 
C 3 HOH   47 547 29  HOH   HOH A . 
C 3 HOH   48 548 36  HOH   HOH A . 
C 3 HOH   49 549 7   HOH   HOH A . 
C 3 HOH   50 550 66  HOH   HOH A . 
C 3 HOH   51 551 30  HOH   HOH A . 
C 3 HOH   52 552 50  HOH   HOH A . 
C 3 HOH   53 553 73  HOH   HOH A . 
C 3 HOH   54 554 33  HOH   HOH A . 
C 3 HOH   55 555 14  HOH   HOH A . 
C 3 HOH   56 556 45  HOH   HOH A . 
C 3 HOH   57 557 38  HOH   HOH A . 
C 3 HOH   58 558 78  HOH   HOH A . 
C 3 HOH   59 559 23  HOH   HOH A . 
C 3 HOH   60 560 13  HOH   HOH A . 
C 3 HOH   61 561 89  HOH   HOH A . 
C 3 HOH   62 562 75  HOH   HOH A . 
C 3 HOH   63 563 69  HOH   HOH A . 
C 3 HOH   64 564 34  HOH   HOH A . 
C 3 HOH   65 565 56  HOH   HOH A . 
C 3 HOH   66 566 31  HOH   HOH A . 
C 3 HOH   67 567 70  HOH   HOH A . 
C 3 HOH   68 568 87  HOH   HOH A . 
C 3 HOH   69 569 19  HOH   HOH A . 
C 3 HOH   70 570 62  HOH   HOH A . 
C 3 HOH   71 571 40  HOH   HOH A . 
C 3 HOH   72 572 67  HOH   HOH A . 
C 3 HOH   73 573 2   HOH   HOH A . 
C 3 HOH   74 574 79  HOH   HOH A . 
C 3 HOH   75 575 76  HOH   HOH A . 
C 3 HOH   76 576 46  HOH   HOH A . 
C 3 HOH   77 577 37  HOH   HOH A . 
C 3 HOH   78 578 51  HOH   HOH A . 
C 3 HOH   79 579 43  HOH   HOH A . 
C 3 HOH   80 580 49  HOH   HOH A . 
C 3 HOH   81 581 64  HOH   HOH A . 
C 3 HOH   82 582 80  HOH   HOH A . 
C 3 HOH   83 583 8   HOH   HOH A . 
C 3 HOH   84 584 77  HOH   HOH A . 
C 3 HOH   85 585 74  HOH   HOH A . 
C 3 HOH   86 586 48  HOH   HOH A . 
C 3 HOH   87 587 68  HOH   HOH A . 
C 3 HOH   88 588 44  HOH   HOH A . 
C 3 HOH   89 589 60  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A TYR 24  ? CG  ? A TYR 24  CG  
2  1 Y 1 A TYR 24  ? CD1 ? A TYR 24  CD1 
3  1 Y 1 A TYR 24  ? CD2 ? A TYR 24  CD2 
4  1 Y 1 A TYR 24  ? CE1 ? A TYR 24  CE1 
5  1 Y 1 A TYR 24  ? CE2 ? A TYR 24  CE2 
6  1 Y 1 A TYR 24  ? CZ  ? A TYR 24  CZ  
7  1 Y 1 A TYR 24  ? OH  ? A TYR 24  OH  
8  1 Y 1 A VAL 45  ? CG1 ? A VAL 45  CG1 
9  1 Y 1 A VAL 45  ? CG2 ? A VAL 45  CG2 
10 1 Y 1 A ARG 46  ? CG  ? A ARG 46  CG  
11 1 Y 1 A ARG 46  ? CD  ? A ARG 46  CD  
12 1 Y 1 A ARG 46  ? NE  ? A ARG 46  NE  
13 1 Y 1 A ARG 46  ? CZ  ? A ARG 46  CZ  
14 1 Y 1 A ARG 46  ? NH1 ? A ARG 46  NH1 
15 1 Y 1 A ARG 46  ? NH2 ? A ARG 46  NH2 
16 1 Y 1 A VAL 47  ? CG1 ? A VAL 47  CG1 
17 1 Y 1 A VAL 47  ? CG2 ? A VAL 47  CG2 
18 1 Y 1 A PRO 55  ? CG  ? A PRO 55  CG  
19 1 Y 1 A PRO 55  ? CD  ? A PRO 55  CD  
20 1 Y 1 A LEU 56  ? CG  ? A LEU 56  CG  
21 1 Y 1 A LEU 56  ? CD1 ? A LEU 56  CD1 
22 1 Y 1 A LEU 56  ? CD2 ? A LEU 56  CD2 
23 1 Y 1 A VAL 181 ? CG1 ? A VAL 181 CG1 
24 1 Y 1 A VAL 181 ? CG2 ? A VAL 181 CG2 
25 1 Y 1 A LYS 257 ? CG  ? A LYS 257 CG  
26 1 Y 1 A LYS 257 ? CD  ? A LYS 257 CD  
27 1 Y 1 A LYS 257 ? CE  ? A LYS 257 CE  
28 1 Y 1 A LYS 257 ? NZ  ? A LYS 257 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER     ? ? ? '2.11.8 (21-NOV-2022)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless    ? ? ? .                      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS        ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? autoBUSTER ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9D8U 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     102.100 
_cell.length_a_esd                 ? 
_cell.length_b                     102.100 
_cell.length_b_esd                 ? 
_cell.length_c                     59.900 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9D8U 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                79 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 4' 
_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                   9D8U 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.81 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Well Ingredients:
Salt: 0.133 M  Ammonium Nitrate
Precipitant: 5.09 %w/v PEG 3350
Buffer: 0.1 M MES (pH 6.00)

Plate setup temperature: 21 C
Plate incubation temperature: 13 C

Drop volume from well: 0.3 uL
Drop protein volume: 0.3 uL
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            286.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     98.15 
_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         2019-06-04 
_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   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9D8U 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.852 
_reflns.d_resolution_low                               72.196 
_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                                     14833 
_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                           94.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.021 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.852 
_reflns_shell.d_res_low                                     2.103 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             741 
_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                               5.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.470 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.615 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          73.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.92830 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            0.92830 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -1.85660 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               52.71 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.943 
_refine.correlation_coeff_Fo_to_Fc_free          0.929 
_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                                 9D8U 
_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                            2.000 
_refine.ls_d_res_low                             29.95 
_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                     14532 
_refine.ls_number_reflns_R_free                  946 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    69.4 
_refine.ls_percent_reflns_R_free                 6.510 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2194 
_refine.ls_R_factor_R_free                       0.2533 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2170 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.222 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.218 
_refine.pdbx_overall_SU_R_Blow_DPI               0.298 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.304 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        9D8U 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.30 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.000 
_refine_hist.d_res_low                        29.95 
_refine_hist.number_atoms_solvent             90 
_refine_hist.number_atoms_total               2206 
_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        2084 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_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' ? 0.008 ? 2164 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.00  ? 2935 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 748  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 382  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2164 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.07  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 20.11 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 274  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 1705 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.00 
_refine_ls_shell.d_res_low                        2.08 
_refine_ls_shell.number_reflns_all                310 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             273 
_refine_ls_shell.percent_reflns_obs               14.23 
_refine_ls_shell.percent_reflns_R_free            11.94 
_refine_ls_shell.R_factor_all                     0.2921 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2997 
_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   48 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2335 
# 
_struct.entry_id                     9D8U 
_struct.title                        'Crystal structure of CDK6 in complex with atirmociclib' 
_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        9D8U 
_struct_keywords.text            'Kinase, Inhibitor, Cancer, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CDK6_HUMAN 
_struct_ref.pdbx_db_accession          Q00534 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEKDGLCRADQQYECVAEIGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLF
DVCTVSRTDRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIK
LADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGE
EDWPRDVALPRQAFHSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYFQ
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9D8U 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 301 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q00534 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  301 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       301 
# 
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 9D8U HIS A 302 ? UNP Q00534 ? ? 'expression tag' 302 1 
1 9D8U HIS A 303 ? UNP Q00534 ? ? 'expression tag' 303 2 
1 9D8U HIS A 304 ? UNP Q00534 ? ? 'expression tag' 304 3 
1 9D8U HIS A 305 ? UNP Q00534 ? ? 'expression tag' 305 4 
1 9D8U HIS A 306 ? UNP Q00534 ? ? 'expression tag' 306 5 
1 9D8U HIS A 307 ? UNP Q00534 ? ? 'expression tag' 307 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 LYS A 34  ? GLY A 36  ? LYS A 34  GLY A 36  5 ? 3  
HELX_P HELX_P2  AA2 LEU A 56  ? GLU A 72  ? LEU A 56  GLU A 72  1 ? 17 
HELX_P HELX_P3  AA3 LEU A 105 ? VAL A 112 ? LEU A 105 VAL A 112 1 ? 8  
HELX_P HELX_P4  AA4 PRO A 118 ? HIS A 139 ? PRO A 118 HIS A 139 1 ? 22 
HELX_P HELX_P5  AA5 ALA A 187 ? LEU A 192 ? ALA A 187 LEU A 192 1 ? 6  
HELX_P HELX_P6  AA6 THR A 198 ? ARG A 215 ? THR A 198 ARG A 215 1 ? 18 
HELX_P HELX_P7  AA7 SER A 223 ? GLY A 236 ? SER A 223 GLY A 236 1 ? 14 
HELX_P HELX_P8  AA8 GLY A 239 ? TRP A 243 ? GLY A 239 TRP A 243 5 ? 5  
HELX_P HELX_P9  AA9 PRO A 250 ? PHE A 254 ? PRO A 250 PHE A 254 5 ? 5  
HELX_P HELX_P10 AB1 PRO A 261 ? PHE A 265 ? PRO A 261 PHE A 265 5 ? 5  
HELX_P HELX_P11 AB2 ASP A 270 ? LEU A 281 ? ASP A 270 LEU A 281 1 ? 12 
HELX_P HELX_P12 AB3 SER A 290 ? LEU A 295 ? SER A 290 LEU A 295 1 ? 6  
HELX_P HELX_P13 AB4 HIS A 297 ? GLN A 301 ? HIS A 297 GLN A 301 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           114 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            114 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    115 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     115 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.69 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
# 
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 TYR A 13  ? GLY A 22  ? TYR A 13  GLY A 22  
AA1 2 GLY A 25  ? ASP A 32  ? GLY A 25  ASP A 32  
AA1 3 PHE A 39  ? VAL A 45  ? PHE A 39  VAL A 45  
AA1 4 LEU A 94  ? GLU A 99  ? LEU A 94  GLU A 99  
AA1 5 LEU A 79  ? CYS A 83  ? LEU A 79  CYS A 83  
AA2 1 GLN A 103 ? ASP A 104 ? GLN A 103 ASP A 104 
AA2 2 ILE A 151 ? VAL A 153 ? ILE A 151 VAL A 153 
AA2 3 ILE A 159 ? LEU A 161 ? ILE A 159 LEU A 161 
# 
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 GLY A 22  ? N GLY A 22  O GLY A 25  ? O GLY A 25  
AA1 2 3 N ALA A 30  ? N ALA A 30  O VAL A 40  ? O VAL A 40  
AA1 3 4 N LYS A 43  ? N LYS A 43  O LEU A 96  ? O LEU A 96  
AA1 4 5 O THR A 95  ? O THR A 95  N CYS A 83  ? N CYS A 83  
AA2 1 2 N GLN A 103 ? N GLN A 103 O VAL A 153 ? O VAL A 153 
AA2 2 3 N LEU A 152 ? N LEU A 152 O LYS A 160 ? O LYS A 160 
# 
_pdbx_entry_details.entry_id                   9D8U 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 144 ? ? 80.72   -17.06  
2 1 ASP A 145 ? ? -140.67 52.63   
3 1 LYS A 257 ? ? 54.47   -122.11 
4 1 LEU A 281 ? ? -89.66  41.23   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ALA 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    23 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   TYR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    24 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -80.35 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         18.0023 
_pdbx_refine_tls.origin_y         36.9825 
_pdbx_refine_tls.origin_z         0.5186 
_pdbx_refine_tls.T[1][1]          -0.0339 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.1108 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0329 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0101 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0219 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0815 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.2282 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2280 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0522 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.1705 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0629 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.0802 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0048 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1448 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0213 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0980 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0313 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0894 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0777 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0066 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0264 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
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 GLU 2   ? A GLU 2   
3  1 Y 1 A LYS 3   ? A LYS 3   
4  1 Y 1 A ASP 4   ? A ASP 4   
5  1 Y 1 A GLY 5   ? A GLY 5   
6  1 Y 1 A LEU 6   ? A LEU 6   
7  1 Y 1 A CYS 7   ? A CYS 7   
8  1 Y 1 A ARG 8   ? A ARG 8   
9  1 Y 1 A ALA 9   ? A ALA 9   
10 1 Y 1 A ASP 10  ? A ASP 10  
11 1 Y 1 A GLN 48  ? A GLN 48  
12 1 Y 1 A THR 49  ? A THR 49  
13 1 Y 1 A GLY 50  ? A GLY 50  
14 1 Y 1 A GLU 51  ? A GLU 51  
15 1 Y 1 A GLU 52  ? A GLU 52  
16 1 Y 1 A GLY 53  ? A GLY 53  
17 1 Y 1 A MET 54  ? A MET 54  
18 1 Y 1 A VAL 85  ? A VAL 85  
19 1 Y 1 A SER 86  ? A SER 86  
20 1 Y 1 A ARG 87  ? A ARG 87  
21 1 Y 1 A THR 88  ? A THR 88  
22 1 Y 1 A ASP 89  ? A ASP 89  
23 1 Y 1 A ARG 90  ? A ARG 90  
24 1 Y 1 A GLU 91  ? A GLU 91  
25 1 Y 1 A THR 92  ? A THR 92  
26 1 Y 1 A ARG 168 ? A ARG 168 
27 1 Y 1 A ILE 169 ? A ILE 169 
28 1 Y 1 A TYR 170 ? A TYR 170 
29 1 Y 1 A SER 171 ? A SER 171 
30 1 Y 1 A PHE 172 ? A PHE 172 
31 1 Y 1 A GLN 173 ? A GLN 173 
32 1 Y 1 A MET 174 ? A MET 174 
33 1 Y 1 A ALA 175 ? A ALA 175 
34 1 Y 1 A LEU 176 ? A LEU 176 
35 1 Y 1 A THR 177 ? A THR 177 
36 1 Y 1 A SER 178 ? A SER 178 
37 1 Y 1 A VAL 179 ? A VAL 179 
38 1 Y 1 A VAL 180 ? A VAL 180 
39 1 Y 1 A HIS 302 ? A HIS 302 
40 1 Y 1 A HIS 303 ? A HIS 303 
41 1 Y 1 A HIS 304 ? A HIS 304 
42 1 Y 1 A HIS 305 ? A HIS 305 
43 1 Y 1 A HIS 306 ? A HIS 306 
44 1 Y 1 A HIS 307 ? A HIS 307 
# 
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 
A1AZ4 C12  C  Y N 1   
A1AZ4 C10  C  Y N 2   
A1AZ4 C28  C  Y N 3   
A1AZ4 C11  C  Y N 4   
A1AZ4 C7   C  Y N 5   
A1AZ4 C13  C  Y N 6   
A1AZ4 C8   C  Y N 7   
A1AZ4 C29  C  Y N 8   
A1AZ4 C14  C  Y N 9   
A1AZ4 C5   C  Y N 10  
A1AZ4 C16  C  Y N 11  
A1AZ4 C20  C  N N 12  
A1AZ4 C21  C  N N 13  
A1AZ4 C23  C  N N 14  
A1AZ4 C18  C  N R 15  
A1AZ4 C24  C  N S 16  
A1AZ4 C1   C  N N 17  
A1AZ4 C3   C  N N 18  
A1AZ4 C32  C  N N 19  
A1AZ4 C33  C  N N 20  
A1AZ4 C2   C  N N 21  
A1AZ4 C31  C  N N 22  
A1AZ4 N27  N  Y N 23  
A1AZ4 N6   N  Y N 24  
A1AZ4 N15  N  Y N 25  
A1AZ4 N4   N  Y N 26  
A1AZ4 N17  N  N N 27  
A1AZ4 O22  O  N N 28  
A1AZ4 O26  O  N N 29  
A1AZ4 O34  O  N N 30  
A1AZ4 F9   F  N N 31  
A1AZ4 CL30 CL N N 32  
A1AZ4 H1   H  N N 33  
A1AZ4 H2   H  N N 34  
A1AZ4 H3   H  N N 35  
A1AZ4 H4   H  N N 36  
A1AZ4 H5   H  N N 37  
A1AZ4 H6   H  N N 38  
A1AZ4 H7   H  N N 39  
A1AZ4 H8   H  N N 40  
A1AZ4 H9   H  N N 41  
A1AZ4 H10  H  N N 42  
A1AZ4 H11  H  N N 43  
A1AZ4 H12  H  N N 44  
A1AZ4 H13  H  N N 45  
A1AZ4 H14  H  N N 46  
A1AZ4 H15  H  N N 47  
A1AZ4 H16  H  N N 48  
A1AZ4 H17  H  N N 49  
A1AZ4 H18  H  N N 50  
A1AZ4 H19  H  N N 51  
A1AZ4 H20  H  N N 52  
A1AZ4 H21  H  N N 53  
A1AZ4 H22  H  N N 54  
A1AZ4 H23  H  N N 55  
A1AZ4 H24  H  N N 56  
A1AZ4 H25  H  N N 57  
A1AZ4 H26  H  N N 58  
A1AZ4 H27  H  N N 59  
ALA   N    N  N N 60  
ALA   CA   C  N S 61  
ALA   C    C  N N 62  
ALA   O    O  N N 63  
ALA   CB   C  N N 64  
ALA   OXT  O  N N 65  
ALA   H    H  N N 66  
ALA   H2   H  N N 67  
ALA   HA   H  N N 68  
ALA   HB1  H  N N 69  
ALA   HB2  H  N N 70  
ALA   HB3  H  N N 71  
ALA   HXT  H  N N 72  
ARG   N    N  N N 73  
ARG   CA   C  N S 74  
ARG   C    C  N N 75  
ARG   O    O  N N 76  
ARG   CB   C  N N 77  
ARG   CG   C  N N 78  
ARG   CD   C  N N 79  
ARG   NE   N  N N 80  
ARG   CZ   C  N N 81  
ARG   NH1  N  N N 82  
ARG   NH2  N  N N 83  
ARG   OXT  O  N N 84  
ARG   H    H  N N 85  
ARG   H2   H  N N 86  
ARG   HA   H  N N 87  
ARG   HB2  H  N N 88  
ARG   HB3  H  N N 89  
ARG   HG2  H  N N 90  
ARG   HG3  H  N N 91  
ARG   HD2  H  N N 92  
ARG   HD3  H  N N 93  
ARG   HE   H  N N 94  
ARG   HH11 H  N N 95  
ARG   HH12 H  N N 96  
ARG   HH21 H  N N 97  
ARG   HH22 H  N N 98  
ARG   HXT  H  N N 99  
ASN   N    N  N N 100 
ASN   CA   C  N S 101 
ASN   C    C  N N 102 
ASN   O    O  N N 103 
ASN   CB   C  N N 104 
ASN   CG   C  N N 105 
ASN   OD1  O  N N 106 
ASN   ND2  N  N N 107 
ASN   OXT  O  N N 108 
ASN   H    H  N N 109 
ASN   H2   H  N N 110 
ASN   HA   H  N N 111 
ASN   HB2  H  N N 112 
ASN   HB3  H  N N 113 
ASN   HD21 H  N N 114 
ASN   HD22 H  N N 115 
ASN   HXT  H  N N 116 
ASP   N    N  N N 117 
ASP   CA   C  N S 118 
ASP   C    C  N N 119 
ASP   O    O  N N 120 
ASP   CB   C  N N 121 
ASP   CG   C  N N 122 
ASP   OD1  O  N N 123 
ASP   OD2  O  N N 124 
ASP   OXT  O  N N 125 
ASP   H    H  N N 126 
ASP   H2   H  N N 127 
ASP   HA   H  N N 128 
ASP   HB2  H  N N 129 
ASP   HB3  H  N N 130 
ASP   HD2  H  N N 131 
ASP   HXT  H  N N 132 
CYS   N    N  N N 133 
CYS   CA   C  N R 134 
CYS   C    C  N N 135 
CYS   O    O  N N 136 
CYS   CB   C  N N 137 
CYS   SG   S  N N 138 
CYS   OXT  O  N N 139 
CYS   H    H  N N 140 
CYS   H2   H  N N 141 
CYS   HA   H  N N 142 
CYS   HB2  H  N N 143 
CYS   HB3  H  N N 144 
CYS   HG   H  N N 145 
CYS   HXT  H  N N 146 
GLN   N    N  N N 147 
GLN   CA   C  N S 148 
GLN   C    C  N N 149 
GLN   O    O  N N 150 
GLN   CB   C  N N 151 
GLN   CG   C  N N 152 
GLN   CD   C  N N 153 
GLN   OE1  O  N N 154 
GLN   NE2  N  N N 155 
GLN   OXT  O  N N 156 
GLN   H    H  N N 157 
GLN   H2   H  N N 158 
GLN   HA   H  N N 159 
GLN   HB2  H  N N 160 
GLN   HB3  H  N N 161 
GLN   HG2  H  N N 162 
GLN   HG3  H  N N 163 
GLN   HE21 H  N N 164 
GLN   HE22 H  N N 165 
GLN   HXT  H  N N 166 
GLU   N    N  N N 167 
GLU   CA   C  N S 168 
GLU   C    C  N N 169 
GLU   O    O  N N 170 
GLU   CB   C  N N 171 
GLU   CG   C  N N 172 
GLU   CD   C  N N 173 
GLU   OE1  O  N N 174 
GLU   OE2  O  N N 175 
GLU   OXT  O  N N 176 
GLU   H    H  N N 177 
GLU   H2   H  N N 178 
GLU   HA   H  N N 179 
GLU   HB2  H  N N 180 
GLU   HB3  H  N N 181 
GLU   HG2  H  N N 182 
GLU   HG3  H  N N 183 
GLU   HE2  H  N N 184 
GLU   HXT  H  N N 185 
GLY   N    N  N N 186 
GLY   CA   C  N N 187 
GLY   C    C  N N 188 
GLY   O    O  N N 189 
GLY   OXT  O  N N 190 
GLY   H    H  N N 191 
GLY   H2   H  N N 192 
GLY   HA2  H  N N 193 
GLY   HA3  H  N N 194 
GLY   HXT  H  N N 195 
HIS   N    N  N N 196 
HIS   CA   C  N S 197 
HIS   C    C  N N 198 
HIS   O    O  N N 199 
HIS   CB   C  N N 200 
HIS   CG   C  Y N 201 
HIS   ND1  N  Y N 202 
HIS   CD2  C  Y N 203 
HIS   CE1  C  Y N 204 
HIS   NE2  N  Y N 205 
HIS   OXT  O  N N 206 
HIS   H    H  N N 207 
HIS   H2   H  N N 208 
HIS   HA   H  N N 209 
HIS   HB2  H  N N 210 
HIS   HB3  H  N N 211 
HIS   HD1  H  N N 212 
HIS   HD2  H  N N 213 
HIS   HE1  H  N N 214 
HIS   HE2  H  N N 215 
HIS   HXT  H  N N 216 
HOH   O    O  N N 217 
HOH   H1   H  N N 218 
HOH   H2   H  N N 219 
ILE   N    N  N N 220 
ILE   CA   C  N S 221 
ILE   C    C  N N 222 
ILE   O    O  N N 223 
ILE   CB   C  N S 224 
ILE   CG1  C  N N 225 
ILE   CG2  C  N N 226 
ILE   CD1  C  N N 227 
ILE   OXT  O  N N 228 
ILE   H    H  N N 229 
ILE   H2   H  N N 230 
ILE   HA   H  N N 231 
ILE   HB   H  N N 232 
ILE   HG12 H  N N 233 
ILE   HG13 H  N N 234 
ILE   HG21 H  N N 235 
ILE   HG22 H  N N 236 
ILE   HG23 H  N N 237 
ILE   HD11 H  N N 238 
ILE   HD12 H  N N 239 
ILE   HD13 H  N N 240 
ILE   HXT  H  N N 241 
LEU   N    N  N N 242 
LEU   CA   C  N S 243 
LEU   C    C  N N 244 
LEU   O    O  N N 245 
LEU   CB   C  N N 246 
LEU   CG   C  N N 247 
LEU   CD1  C  N N 248 
LEU   CD2  C  N N 249 
LEU   OXT  O  N N 250 
LEU   H    H  N N 251 
LEU   H2   H  N N 252 
LEU   HA   H  N N 253 
LEU   HB2  H  N N 254 
LEU   HB3  H  N N 255 
LEU   HG   H  N N 256 
LEU   HD11 H  N N 257 
LEU   HD12 H  N N 258 
LEU   HD13 H  N N 259 
LEU   HD21 H  N N 260 
LEU   HD22 H  N N 261 
LEU   HD23 H  N N 262 
LEU   HXT  H  N N 263 
LYS   N    N  N N 264 
LYS   CA   C  N S 265 
LYS   C    C  N N 266 
LYS   O    O  N N 267 
LYS   CB   C  N N 268 
LYS   CG   C  N N 269 
LYS   CD   C  N N 270 
LYS   CE   C  N N 271 
LYS   NZ   N  N N 272 
LYS   OXT  O  N N 273 
LYS   H    H  N N 274 
LYS   H2   H  N N 275 
LYS   HA   H  N N 276 
LYS   HB2  H  N N 277 
LYS   HB3  H  N N 278 
LYS   HG2  H  N N 279 
LYS   HG3  H  N N 280 
LYS   HD2  H  N N 281 
LYS   HD3  H  N N 282 
LYS   HE2  H  N N 283 
LYS   HE3  H  N N 284 
LYS   HZ1  H  N N 285 
LYS   HZ2  H  N N 286 
LYS   HZ3  H  N N 287 
LYS   HXT  H  N N 288 
MET   N    N  N N 289 
MET   CA   C  N S 290 
MET   C    C  N N 291 
MET   O    O  N N 292 
MET   CB   C  N N 293 
MET   CG   C  N N 294 
MET   SD   S  N N 295 
MET   CE   C  N N 296 
MET   OXT  O  N N 297 
MET   H    H  N N 298 
MET   H2   H  N N 299 
MET   HA   H  N N 300 
MET   HB2  H  N N 301 
MET   HB3  H  N N 302 
MET   HG2  H  N N 303 
MET   HG3  H  N N 304 
MET   HE1  H  N N 305 
MET   HE2  H  N N 306 
MET   HE3  H  N N 307 
MET   HXT  H  N N 308 
PHE   N    N  N N 309 
PHE   CA   C  N S 310 
PHE   C    C  N N 311 
PHE   O    O  N N 312 
PHE   CB   C  N N 313 
PHE   CG   C  Y N 314 
PHE   CD1  C  Y N 315 
PHE   CD2  C  Y N 316 
PHE   CE1  C  Y N 317 
PHE   CE2  C  Y N 318 
PHE   CZ   C  Y N 319 
PHE   OXT  O  N N 320 
PHE   H    H  N N 321 
PHE   H2   H  N N 322 
PHE   HA   H  N N 323 
PHE   HB2  H  N N 324 
PHE   HB3  H  N N 325 
PHE   HD1  H  N N 326 
PHE   HD2  H  N N 327 
PHE   HE1  H  N N 328 
PHE   HE2  H  N N 329 
PHE   HZ   H  N N 330 
PHE   HXT  H  N N 331 
PRO   N    N  N N 332 
PRO   CA   C  N S 333 
PRO   C    C  N N 334 
PRO   O    O  N N 335 
PRO   CB   C  N N 336 
PRO   CG   C  N N 337 
PRO   CD   C  N N 338 
PRO   OXT  O  N N 339 
PRO   H    H  N N 340 
PRO   HA   H  N N 341 
PRO   HB2  H  N N 342 
PRO   HB3  H  N N 343 
PRO   HG2  H  N N 344 
PRO   HG3  H  N N 345 
PRO   HD2  H  N N 346 
PRO   HD3  H  N N 347 
PRO   HXT  H  N N 348 
SER   N    N  N N 349 
SER   CA   C  N S 350 
SER   C    C  N N 351 
SER   O    O  N N 352 
SER   CB   C  N N 353 
SER   OG   O  N N 354 
SER   OXT  O  N N 355 
SER   H    H  N N 356 
SER   H2   H  N N 357 
SER   HA   H  N N 358 
SER   HB2  H  N N 359 
SER   HB3  H  N N 360 
SER   HG   H  N N 361 
SER   HXT  H  N N 362 
THR   N    N  N N 363 
THR   CA   C  N S 364 
THR   C    C  N N 365 
THR   O    O  N N 366 
THR   CB   C  N R 367 
THR   OG1  O  N N 368 
THR   CG2  C  N N 369 
THR   OXT  O  N N 370 
THR   H    H  N N 371 
THR   H2   H  N N 372 
THR   HA   H  N N 373 
THR   HB   H  N N 374 
THR   HG1  H  N N 375 
THR   HG21 H  N N 376 
THR   HG22 H  N N 377 
THR   HG23 H  N N 378 
THR   HXT  H  N N 379 
TRP   N    N  N N 380 
TRP   CA   C  N S 381 
TRP   C    C  N N 382 
TRP   O    O  N N 383 
TRP   CB   C  N N 384 
TRP   CG   C  Y N 385 
TRP   CD1  C  Y N 386 
TRP   CD2  C  Y N 387 
TRP   NE1  N  Y N 388 
TRP   CE2  C  Y N 389 
TRP   CE3  C  Y N 390 
TRP   CZ2  C  Y N 391 
TRP   CZ3  C  Y N 392 
TRP   CH2  C  Y N 393 
TRP   OXT  O  N N 394 
TRP   H    H  N N 395 
TRP   H2   H  N N 396 
TRP   HA   H  N N 397 
TRP   HB2  H  N N 398 
TRP   HB3  H  N N 399 
TRP   HD1  H  N N 400 
TRP   HE1  H  N N 401 
TRP   HE3  H  N N 402 
TRP   HZ2  H  N N 403 
TRP   HZ3  H  N N 404 
TRP   HH2  H  N N 405 
TRP   HXT  H  N N 406 
TYR   N    N  N N 407 
TYR   CA   C  N S 408 
TYR   C    C  N N 409 
TYR   O    O  N N 410 
TYR   CB   C  N N 411 
TYR   CG   C  Y N 412 
TYR   CD1  C  Y N 413 
TYR   CD2  C  Y N 414 
TYR   CE1  C  Y N 415 
TYR   CE2  C  Y N 416 
TYR   CZ   C  Y N 417 
TYR   OH   O  N N 418 
TYR   OXT  O  N N 419 
TYR   H    H  N N 420 
TYR   H2   H  N N 421 
TYR   HA   H  N N 422 
TYR   HB2  H  N N 423 
TYR   HB3  H  N N 424 
TYR   HD1  H  N N 425 
TYR   HD2  H  N N 426 
TYR   HE1  H  N N 427 
TYR   HE2  H  N N 428 
TYR   HH   H  N N 429 
TYR   HXT  H  N N 430 
VAL   N    N  N N 431 
VAL   CA   C  N S 432 
VAL   C    C  N N 433 
VAL   O    O  N N 434 
VAL   CB   C  N N 435 
VAL   CG1  C  N N 436 
VAL   CG2  C  N N 437 
VAL   OXT  O  N N 438 
VAL   H    H  N N 439 
VAL   H2   H  N N 440 
VAL   HA   H  N N 441 
VAL   HB   H  N N 442 
VAL   HG11 H  N N 443 
VAL   HG12 H  N N 444 
VAL   HG13 H  N N 445 
VAL   HG21 H  N N 446 
VAL   HG22 H  N N 447 
VAL   HG23 H  N N 448 
VAL   HXT  H  N N 449 
# 
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 
A1AZ4 F9   C8   sing N N 1   
A1AZ4 CL30 C29  sing N N 2   
A1AZ4 C8   C10  doub Y N 3   
A1AZ4 C8   C7   sing Y N 4   
A1AZ4 C32  C31  sing N N 5   
A1AZ4 N6   C7   sing Y N 6   
A1AZ4 N6   C5   doub Y N 7   
A1AZ4 C10  C11  sing Y N 8   
A1AZ4 C7   C13  doub Y N 9   
A1AZ4 C29  C28  doub Y N 10  
A1AZ4 C29  C14  sing Y N 11  
A1AZ4 C5   C31  sing N N 12  
A1AZ4 C5   N4   sing Y N 13  
A1AZ4 C31  O34  sing N N 14  
A1AZ4 C31  C33  sing N N 15  
A1AZ4 C11  C14  sing N N 16  
A1AZ4 C11  C12  doub Y N 17  
A1AZ4 C28  N27  sing Y N 18  
A1AZ4 C13  N4   sing Y N 19  
A1AZ4 C13  C12  sing Y N 20  
A1AZ4 C14  N15  doub Y N 21  
A1AZ4 N4   C2   sing N N 22  
A1AZ4 N27  C16  doub Y N 23  
A1AZ4 C1   C2   sing N N 24  
A1AZ4 C2   C3   sing N N 25  
A1AZ4 N15  C16  sing Y N 26  
A1AZ4 C16  N17  sing N N 27  
A1AZ4 N17  C18  sing N N 28  
A1AZ4 C20  C18  sing N N 29  
A1AZ4 C20  C21  sing N N 30  
A1AZ4 C18  C24  sing N N 31  
A1AZ4 C21  O22  sing N N 32  
A1AZ4 C24  O26  sing N N 33  
A1AZ4 C24  C23  sing N N 34  
A1AZ4 O22  C23  sing N N 35  
A1AZ4 C12  H1   sing N N 36  
A1AZ4 C10  H2   sing N N 37  
A1AZ4 C28  H3   sing N N 38  
A1AZ4 C20  H4   sing N N 39  
A1AZ4 C20  H5   sing N N 40  
A1AZ4 C21  H6   sing N N 41  
A1AZ4 C21  H7   sing N N 42  
A1AZ4 C23  H8   sing N N 43  
A1AZ4 C23  H9   sing N N 44  
A1AZ4 C18  H10  sing N N 45  
A1AZ4 C24  H11  sing N N 46  
A1AZ4 C1   H12  sing N N 47  
A1AZ4 C1   H13  sing N N 48  
A1AZ4 C1   H14  sing N N 49  
A1AZ4 C3   H15  sing N N 50  
A1AZ4 C3   H16  sing N N 51  
A1AZ4 C3   H17  sing N N 52  
A1AZ4 C32  H18  sing N N 53  
A1AZ4 C32  H19  sing N N 54  
A1AZ4 C32  H20  sing N N 55  
A1AZ4 C33  H21  sing N N 56  
A1AZ4 C33  H22  sing N N 57  
A1AZ4 C33  H23  sing N N 58  
A1AZ4 C2   H24  sing N N 59  
A1AZ4 N17  H25  sing N N 60  
A1AZ4 O26  H26  sing N N 61  
A1AZ4 O34  H27  sing N N 62  
ALA   N    CA   sing N N 63  
ALA   N    H    sing N N 64  
ALA   N    H2   sing N N 65  
ALA   CA   C    sing N N 66  
ALA   CA   CB   sing N N 67  
ALA   CA   HA   sing N N 68  
ALA   C    O    doub N N 69  
ALA   C    OXT  sing N N 70  
ALA   CB   HB1  sing N N 71  
ALA   CB   HB2  sing N N 72  
ALA   CB   HB3  sing N N 73  
ALA   OXT  HXT  sing N N 74  
ARG   N    CA   sing N N 75  
ARG   N    H    sing N N 76  
ARG   N    H2   sing N N 77  
ARG   CA   C    sing N N 78  
ARG   CA   CB   sing N N 79  
ARG   CA   HA   sing N N 80  
ARG   C    O    doub N N 81  
ARG   C    OXT  sing N N 82  
ARG   CB   CG   sing N N 83  
ARG   CB   HB2  sing N N 84  
ARG   CB   HB3  sing N N 85  
ARG   CG   CD   sing N N 86  
ARG   CG   HG2  sing N N 87  
ARG   CG   HG3  sing N N 88  
ARG   CD   NE   sing N N 89  
ARG   CD   HD2  sing N N 90  
ARG   CD   HD3  sing N N 91  
ARG   NE   CZ   sing N N 92  
ARG   NE   HE   sing N N 93  
ARG   CZ   NH1  sing N N 94  
ARG   CZ   NH2  doub N N 95  
ARG   NH1  HH11 sing N N 96  
ARG   NH1  HH12 sing N N 97  
ARG   NH2  HH21 sing N N 98  
ARG   NH2  HH22 sing N N 99  
ARG   OXT  HXT  sing N N 100 
ASN   N    CA   sing N N 101 
ASN   N    H    sing N N 102 
ASN   N    H2   sing N N 103 
ASN   CA   C    sing N N 104 
ASN   CA   CB   sing N N 105 
ASN   CA   HA   sing N N 106 
ASN   C    O    doub N N 107 
ASN   C    OXT  sing N N 108 
ASN   CB   CG   sing N N 109 
ASN   CB   HB2  sing N N 110 
ASN   CB   HB3  sing N N 111 
ASN   CG   OD1  doub N N 112 
ASN   CG   ND2  sing N N 113 
ASN   ND2  HD21 sing N N 114 
ASN   ND2  HD22 sing N N 115 
ASN   OXT  HXT  sing N N 116 
ASP   N    CA   sing N N 117 
ASP   N    H    sing N N 118 
ASP   N    H2   sing N N 119 
ASP   CA   C    sing N N 120 
ASP   CA   CB   sing N N 121 
ASP   CA   HA   sing N N 122 
ASP   C    O    doub N N 123 
ASP   C    OXT  sing N N 124 
ASP   CB   CG   sing N N 125 
ASP   CB   HB2  sing N N 126 
ASP   CB   HB3  sing N N 127 
ASP   CG   OD1  doub N N 128 
ASP   CG   OD2  sing N N 129 
ASP   OD2  HD2  sing N N 130 
ASP   OXT  HXT  sing N N 131 
CYS   N    CA   sing N N 132 
CYS   N    H    sing N N 133 
CYS   N    H2   sing N N 134 
CYS   CA   C    sing N N 135 
CYS   CA   CB   sing N N 136 
CYS   CA   HA   sing N N 137 
CYS   C    O    doub N N 138 
CYS   C    OXT  sing N N 139 
CYS   CB   SG   sing N N 140 
CYS   CB   HB2  sing N N 141 
CYS   CB   HB3  sing N N 142 
CYS   SG   HG   sing N N 143 
CYS   OXT  HXT  sing N N 144 
GLN   N    CA   sing N N 145 
GLN   N    H    sing N N 146 
GLN   N    H2   sing N N 147 
GLN   CA   C    sing N N 148 
GLN   CA   CB   sing N N 149 
GLN   CA   HA   sing N N 150 
GLN   C    O    doub N N 151 
GLN   C    OXT  sing N N 152 
GLN   CB   CG   sing N N 153 
GLN   CB   HB2  sing N N 154 
GLN   CB   HB3  sing N N 155 
GLN   CG   CD   sing N N 156 
GLN   CG   HG2  sing N N 157 
GLN   CG   HG3  sing N N 158 
GLN   CD   OE1  doub N N 159 
GLN   CD   NE2  sing N N 160 
GLN   NE2  HE21 sing N N 161 
GLN   NE2  HE22 sing N N 162 
GLN   OXT  HXT  sing N N 163 
GLU   N    CA   sing N N 164 
GLU   N    H    sing N N 165 
GLU   N    H2   sing N N 166 
GLU   CA   C    sing N N 167 
GLU   CA   CB   sing N N 168 
GLU   CA   HA   sing N N 169 
GLU   C    O    doub N N 170 
GLU   C    OXT  sing N N 171 
GLU   CB   CG   sing N N 172 
GLU   CB   HB2  sing N N 173 
GLU   CB   HB3  sing N N 174 
GLU   CG   CD   sing N N 175 
GLU   CG   HG2  sing N N 176 
GLU   CG   HG3  sing N N 177 
GLU   CD   OE1  doub N N 178 
GLU   CD   OE2  sing N N 179 
GLU   OE2  HE2  sing N N 180 
GLU   OXT  HXT  sing N N 181 
GLY   N    CA   sing N N 182 
GLY   N    H    sing N N 183 
GLY   N    H2   sing N N 184 
GLY   CA   C    sing N N 185 
GLY   CA   HA2  sing N N 186 
GLY   CA   HA3  sing N N 187 
GLY   C    O    doub N N 188 
GLY   C    OXT  sing N N 189 
GLY   OXT  HXT  sing N N 190 
HIS   N    CA   sing N N 191 
HIS   N    H    sing N N 192 
HIS   N    H2   sing N N 193 
HIS   CA   C    sing N N 194 
HIS   CA   CB   sing N N 195 
HIS   CA   HA   sing N N 196 
HIS   C    O    doub N N 197 
HIS   C    OXT  sing N N 198 
HIS   CB   CG   sing N N 199 
HIS   CB   HB2  sing N N 200 
HIS   CB   HB3  sing N N 201 
HIS   CG   ND1  sing Y N 202 
HIS   CG   CD2  doub Y N 203 
HIS   ND1  CE1  doub Y N 204 
HIS   ND1  HD1  sing N N 205 
HIS   CD2  NE2  sing Y N 206 
HIS   CD2  HD2  sing N N 207 
HIS   CE1  NE2  sing Y N 208 
HIS   CE1  HE1  sing N N 209 
HIS   NE2  HE2  sing N N 210 
HIS   OXT  HXT  sing N N 211 
HOH   O    H1   sing N N 212 
HOH   O    H2   sing N N 213 
ILE   N    CA   sing N N 214 
ILE   N    H    sing N N 215 
ILE   N    H2   sing N N 216 
ILE   CA   C    sing N N 217 
ILE   CA   CB   sing N N 218 
ILE   CA   HA   sing N N 219 
ILE   C    O    doub N N 220 
ILE   C    OXT  sing N N 221 
ILE   CB   CG1  sing N N 222 
ILE   CB   CG2  sing N N 223 
ILE   CB   HB   sing N N 224 
ILE   CG1  CD1  sing N N 225 
ILE   CG1  HG12 sing N N 226 
ILE   CG1  HG13 sing N N 227 
ILE   CG2  HG21 sing N N 228 
ILE   CG2  HG22 sing N N 229 
ILE   CG2  HG23 sing N N 230 
ILE   CD1  HD11 sing N N 231 
ILE   CD1  HD12 sing N N 232 
ILE   CD1  HD13 sing N N 233 
ILE   OXT  HXT  sing N N 234 
LEU   N    CA   sing N N 235 
LEU   N    H    sing N N 236 
LEU   N    H2   sing N N 237 
LEU   CA   C    sing N N 238 
LEU   CA   CB   sing N N 239 
LEU   CA   HA   sing N N 240 
LEU   C    O    doub N N 241 
LEU   C    OXT  sing N N 242 
LEU   CB   CG   sing N N 243 
LEU   CB   HB2  sing N N 244 
LEU   CB   HB3  sing N N 245 
LEU   CG   CD1  sing N N 246 
LEU   CG   CD2  sing N N 247 
LEU   CG   HG   sing N N 248 
LEU   CD1  HD11 sing N N 249 
LEU   CD1  HD12 sing N N 250 
LEU   CD1  HD13 sing N N 251 
LEU   CD2  HD21 sing N N 252 
LEU   CD2  HD22 sing N N 253 
LEU   CD2  HD23 sing N N 254 
LEU   OXT  HXT  sing N N 255 
LYS   N    CA   sing N N 256 
LYS   N    H    sing N N 257 
LYS   N    H2   sing N N 258 
LYS   CA   C    sing N N 259 
LYS   CA   CB   sing N N 260 
LYS   CA   HA   sing N N 261 
LYS   C    O    doub N N 262 
LYS   C    OXT  sing N N 263 
LYS   CB   CG   sing N N 264 
LYS   CB   HB2  sing N N 265 
LYS   CB   HB3  sing N N 266 
LYS   CG   CD   sing N N 267 
LYS   CG   HG2  sing N N 268 
LYS   CG   HG3  sing N N 269 
LYS   CD   CE   sing N N 270 
LYS   CD   HD2  sing N N 271 
LYS   CD   HD3  sing N N 272 
LYS   CE   NZ   sing N N 273 
LYS   CE   HE2  sing N N 274 
LYS   CE   HE3  sing N N 275 
LYS   NZ   HZ1  sing N N 276 
LYS   NZ   HZ2  sing N N 277 
LYS   NZ   HZ3  sing N N 278 
LYS   OXT  HXT  sing N N 279 
MET   N    CA   sing N N 280 
MET   N    H    sing N N 281 
MET   N    H2   sing N N 282 
MET   CA   C    sing N N 283 
MET   CA   CB   sing N N 284 
MET   CA   HA   sing N N 285 
MET   C    O    doub N N 286 
MET   C    OXT  sing N N 287 
MET   CB   CG   sing N N 288 
MET   CB   HB2  sing N N 289 
MET   CB   HB3  sing N N 290 
MET   CG   SD   sing N N 291 
MET   CG   HG2  sing N N 292 
MET   CG   HG3  sing N N 293 
MET   SD   CE   sing N N 294 
MET   CE   HE1  sing N N 295 
MET   CE   HE2  sing N N 296 
MET   CE   HE3  sing N N 297 
MET   OXT  HXT  sing N N 298 
PHE   N    CA   sing N N 299 
PHE   N    H    sing N N 300 
PHE   N    H2   sing N N 301 
PHE   CA   C    sing N N 302 
PHE   CA   CB   sing N N 303 
PHE   CA   HA   sing N N 304 
PHE   C    O    doub N N 305 
PHE   C    OXT  sing N N 306 
PHE   CB   CG   sing N N 307 
PHE   CB   HB2  sing N N 308 
PHE   CB   HB3  sing N N 309 
PHE   CG   CD1  doub Y N 310 
PHE   CG   CD2  sing Y N 311 
PHE   CD1  CE1  sing Y N 312 
PHE   CD1  HD1  sing N N 313 
PHE   CD2  CE2  doub Y N 314 
PHE   CD2  HD2  sing N N 315 
PHE   CE1  CZ   doub Y N 316 
PHE   CE1  HE1  sing N N 317 
PHE   CE2  CZ   sing Y N 318 
PHE   CE2  HE2  sing N N 319 
PHE   CZ   HZ   sing N N 320 
PHE   OXT  HXT  sing N N 321 
PRO   N    CA   sing N N 322 
PRO   N    CD   sing N N 323 
PRO   N    H    sing N N 324 
PRO   CA   C    sing N N 325 
PRO   CA   CB   sing N N 326 
PRO   CA   HA   sing N N 327 
PRO   C    O    doub N N 328 
PRO   C    OXT  sing N N 329 
PRO   CB   CG   sing N N 330 
PRO   CB   HB2  sing N N 331 
PRO   CB   HB3  sing N N 332 
PRO   CG   CD   sing N N 333 
PRO   CG   HG2  sing N N 334 
PRO   CG   HG3  sing N N 335 
PRO   CD   HD2  sing N N 336 
PRO   CD   HD3  sing N N 337 
PRO   OXT  HXT  sing N N 338 
SER   N    CA   sing N N 339 
SER   N    H    sing N N 340 
SER   N    H2   sing N N 341 
SER   CA   C    sing N N 342 
SER   CA   CB   sing N N 343 
SER   CA   HA   sing N N 344 
SER   C    O    doub N N 345 
SER   C    OXT  sing N N 346 
SER   CB   OG   sing N N 347 
SER   CB   HB2  sing N N 348 
SER   CB   HB3  sing N N 349 
SER   OG   HG   sing N N 350 
SER   OXT  HXT  sing N N 351 
THR   N    CA   sing N N 352 
THR   N    H    sing N N 353 
THR   N    H2   sing N N 354 
THR   CA   C    sing N N 355 
THR   CA   CB   sing N N 356 
THR   CA   HA   sing N N 357 
THR   C    O    doub N N 358 
THR   C    OXT  sing N N 359 
THR   CB   OG1  sing N N 360 
THR   CB   CG2  sing N N 361 
THR   CB   HB   sing N N 362 
THR   OG1  HG1  sing N N 363 
THR   CG2  HG21 sing N N 364 
THR   CG2  HG22 sing N N 365 
THR   CG2  HG23 sing N N 366 
THR   OXT  HXT  sing N N 367 
TRP   N    CA   sing N N 368 
TRP   N    H    sing N N 369 
TRP   N    H2   sing N N 370 
TRP   CA   C    sing N N 371 
TRP   CA   CB   sing N N 372 
TRP   CA   HA   sing N N 373 
TRP   C    O    doub N N 374 
TRP   C    OXT  sing N N 375 
TRP   CB   CG   sing N N 376 
TRP   CB   HB2  sing N N 377 
TRP   CB   HB3  sing N N 378 
TRP   CG   CD1  doub Y N 379 
TRP   CG   CD2  sing Y N 380 
TRP   CD1  NE1  sing Y N 381 
TRP   CD1  HD1  sing N N 382 
TRP   CD2  CE2  doub Y N 383 
TRP   CD2  CE3  sing Y N 384 
TRP   NE1  CE2  sing Y N 385 
TRP   NE1  HE1  sing N N 386 
TRP   CE2  CZ2  sing Y N 387 
TRP   CE3  CZ3  doub Y N 388 
TRP   CE3  HE3  sing N N 389 
TRP   CZ2  CH2  doub Y N 390 
TRP   CZ2  HZ2  sing N N 391 
TRP   CZ3  CH2  sing Y N 392 
TRP   CZ3  HZ3  sing N N 393 
TRP   CH2  HH2  sing N N 394 
TRP   OXT  HXT  sing N N 395 
TYR   N    CA   sing N N 396 
TYR   N    H    sing N N 397 
TYR   N    H2   sing N N 398 
TYR   CA   C    sing N N 399 
TYR   CA   CB   sing N N 400 
TYR   CA   HA   sing N N 401 
TYR   C    O    doub N N 402 
TYR   C    OXT  sing N N 403 
TYR   CB   CG   sing N N 404 
TYR   CB   HB2  sing N N 405 
TYR   CB   HB3  sing N N 406 
TYR   CG   CD1  doub Y N 407 
TYR   CG   CD2  sing Y N 408 
TYR   CD1  CE1  sing Y N 409 
TYR   CD1  HD1  sing N N 410 
TYR   CD2  CE2  doub Y N 411 
TYR   CD2  HD2  sing N N 412 
TYR   CE1  CZ   doub Y N 413 
TYR   CE1  HE1  sing N N 414 
TYR   CE2  CZ   sing Y N 415 
TYR   CE2  HE2  sing N N 416 
TYR   CZ   OH   sing N N 417 
TYR   OH   HH   sing N N 418 
TYR   OXT  HXT  sing N N 419 
VAL   N    CA   sing N N 420 
VAL   N    H    sing N N 421 
VAL   N    H2   sing N N 422 
VAL   CA   C    sing N N 423 
VAL   CA   CB   sing N N 424 
VAL   CA   HA   sing N N 425 
VAL   C    O    doub N N 426 
VAL   C    OXT  sing N N 427 
VAL   CB   CG1  sing N N 428 
VAL   CB   CG2  sing N N 429 
VAL   CB   HB   sing N N 430 
VAL   CG1  HG11 sing N N 431 
VAL   CG1  HG12 sing N N 432 
VAL   CG1  HG13 sing N N 433 
VAL   CG2  HG21 sing N N 434 
VAL   CG2  HG22 sing N N 435 
VAL   CG2  HG23 sing N N 436 
VAL   OXT  HXT  sing N N 437 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5L2I 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9D8U 
_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]   0.009794 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009794 
_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]   0.016694 
_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 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . GLN   A 1 11  ? 12.249 5.114  11.565  1.00 69.54 ? 11  GLN   A N    1 
ATOM   2    C  CA   . GLN   A 1 11  ? 12.888 5.989  10.580  1.00 69.99 ? 11  GLN   A CA   1 
ATOM   3    C  C    . GLN   A 1 11  ? 14.273 6.496  11.084  1.00 69.08 ? 11  GLN   A C    1 
ATOM   4    O  O    . GLN   A 1 11  ? 14.623 6.280  12.243  1.00 69.60 ? 11  GLN   A O    1 
ATOM   5    C  CB   . GLN   A 1 11  ? 11.947 7.169  10.239  1.00 72.37 ? 11  GLN   A CB   1 
ATOM   6    C  CG   . GLN   A 1 11  ? 10.678 6.768  9.501   1.00 77.04 ? 11  GLN   A CG   1 
ATOM   7    C  CD   . GLN   A 1 11  ? 9.751  7.939  9.249   1.00 82.70 ? 11  GLN   A CD   1 
ATOM   8    O  OE1  . GLN   A 1 11  ? 9.780  8.945  9.978   1.00 84.62 ? 11  GLN   A OE1  1 
ATOM   9    N  NE2  . GLN   A 1 11  ? 8.899  7.833  8.229   1.00 83.05 ? 11  GLN   A NE2  1 
ATOM   10   N  N    . GLN   A 1 12  ? 15.023 7.202  10.229  1.00 67.28 ? 12  GLN   A N    1 
ATOM   11   C  CA   . GLN   A 1 12  ? 16.367 7.722  10.615  1.00 65.50 ? 12  GLN   A CA   1 
ATOM   12   C  C    . GLN   A 1 12  ? 16.243 9.135  11.195  1.00 62.59 ? 12  GLN   A C    1 
ATOM   13   O  O    . GLN   A 1 12  ? 17.188 9.574  11.873  1.00 62.03 ? 12  GLN   A O    1 
ATOM   14   C  CB   . GLN   A 1 12  ? 17.295 7.711  9.399   1.00 67.81 ? 12  GLN   A CB   1 
ATOM   15   C  CG   . GLN   A 1 12  ? 18.659 8.333  9.658   1.00 72.74 ? 12  GLN   A CG   1 
ATOM   16   C  CD   . GLN   A 1 12  ? 19.509 8.384  8.412   1.00 77.30 ? 12  GLN   A CD   1 
ATOM   17   O  OE1  . GLN   A 1 12  ? 20.606 7.834  8.360   1.00 78.14 ? 12  GLN   A OE1  1 
ATOM   18   N  NE2  . GLN   A 1 12  ? 19.004 9.056  7.391   1.00 77.69 ? 12  GLN   A NE2  1 
ATOM   19   N  N    . TYR   A 1 13  ? 15.130 9.819  10.935  1.00 60.69 ? 13  TYR   A N    1 
ATOM   20   C  CA   . TYR   A 1 13  ? 14.896 11.178 11.429  1.00 59.31 ? 13  TYR   A CA   1 
ATOM   21   C  C    . TYR   A 1 13  ? 13.657 11.225 12.287  1.00 59.91 ? 13  TYR   A C    1 
ATOM   22   O  O    . TYR   A 1 13  ? 12.706 10.487 12.040  1.00 60.32 ? 13  TYR   A O    1 
ATOM   23   C  CB   . TYR   A 1 13  ? 14.781 12.181 10.265  1.00 57.80 ? 13  TYR   A CB   1 
ATOM   24   C  CG   . TYR   A 1 13  ? 16.046 12.258 9.443   1.00 56.64 ? 13  TYR   A CG   1 
ATOM   25   C  CD1  . TYR   A 1 13  ? 17.167 12.916 9.921   1.00 56.75 ? 13  TYR   A CD1  1 
ATOM   26   C  CD2  . TYR   A 1 13  ? 16.145 11.611 8.215   1.00 56.79 ? 13  TYR   A CD2  1 
ATOM   27   C  CE1  . TYR   A 1 13  ? 18.358 12.935 9.203   1.00 57.15 ? 13  TYR   A CE1  1 
ATOM   28   C  CE2  . TYR   A 1 13  ? 17.328 11.638 7.475   1.00 57.02 ? 13  TYR   A CE2  1 
ATOM   29   C  CZ   . TYR   A 1 13  ? 18.437 12.295 7.979   1.00 57.49 ? 13  TYR   A CZ   1 
ATOM   30   O  OH   . TYR   A 1 13  ? 19.626 12.339 7.287   1.00 57.32 ? 13  TYR   A OH   1 
ATOM   31   N  N    . GLU   A 1 14  ? 13.666 12.068 13.315  1.00 60.18 ? 14  GLU   A N    1 
ATOM   32   C  CA   . GLU   A 1 14  ? 12.525 12.178 14.213  1.00 61.15 ? 14  GLU   A CA   1 
ATOM   33   C  C    . GLU   A 1 14  ? 12.101 13.629 14.368  1.00 62.29 ? 14  GLU   A C    1 
ATOM   34   O  O    . GLU   A 1 14  ? 12.815 14.396 15.003  1.00 62.57 ? 14  GLU   A O    1 
ATOM   35   C  CB   . GLU   A 1 14  ? 12.875 11.567 15.564  1.00 63.17 ? 14  GLU   A CB   1 
ATOM   36   C  CG   . GLU   A 1 14  ? 11.721 11.587 16.539  1.00 67.85 ? 14  GLU   A CG   1 
ATOM   37   C  CD   . GLU   A 1 14  ? 12.191 11.554 17.975  1.00 73.43 ? 14  GLU   A CD   1 
ATOM   38   O  OE1  . GLU   A 1 14  ? 12.809 10.543 18.380  1.00 73.25 ? 14  GLU   A OE1  1 
ATOM   39   O  OE2  . GLU   A 1 14  ? 11.954 12.552 18.693  1.00 75.90 ? 14  GLU   A OE2  1 
ATOM   40   N  N    . CYS   A 1 15  ? 10.949 14.014 13.782  1.00 62.86 ? 15  CYS   A N    1 
ATOM   41   C  CA   . CYS   A 1 15  ? 10.462 15.395 13.836  1.00 63.71 ? 15  CYS   A CA   1 
ATOM   42   C  C    . CYS   A 1 15  ? 10.116 15.816 15.239  1.00 63.33 ? 15  CYS   A C    1 
ATOM   43   O  O    . CYS   A 1 15  ? 9.415  15.096 15.944  1.00 63.71 ? 15  CYS   A O    1 
ATOM   44   C  CB   . CYS   A 1 15  ? 9.283  15.615 12.886  1.00 65.47 ? 15  CYS   A CB   1 
ATOM   45   S  SG   . CYS   A 1 15  ? 9.626  15.199 11.153  1.00 70.99 ? 15  CYS   A SG   1 
ATOM   46   N  N    . VAL   A 1 16  ? 10.598 16.987 15.651  1.00 62.78 ? 16  VAL   A N    1 
ATOM   47   C  CA   . VAL   A 1 16  ? 10.324 17.507 16.981  1.00 62.85 ? 16  VAL   A CA   1 
ATOM   48   C  C    . VAL   A 1 16  ? 9.491  18.790 16.952  1.00 63.11 ? 16  VAL   A C    1 
ATOM   49   O  O    . VAL   A 1 16  ? 8.817  19.100 17.932  1.00 63.96 ? 16  VAL   A O    1 
ATOM   50   C  CB   . VAL   A 1 16  ? 11.610 17.677 17.827  1.00 63.55 ? 16  VAL   A CB   1 
ATOM   51   C  CG1  . VAL   A 1 16  ? 12.362 16.351 17.966  1.00 63.87 ? 16  VAL   A CG1  1 
ATOM   52   C  CG2  . VAL   A 1 16  ? 12.517 18.760 17.249  1.00 63.94 ? 16  VAL   A CG2  1 
ATOM   53   N  N    . ALA   A 1 17  ? 9.526  19.547 15.851  1.00 62.62 ? 17  ALA   A N    1 
ATOM   54   C  CA   . ALA   A 1 17  ? 8.777  20.807 15.752  1.00 62.61 ? 17  ALA   A CA   1 
ATOM   55   C  C    . ALA   A 1 17  ? 8.612  21.239 14.303  1.00 62.70 ? 17  ALA   A C    1 
ATOM   56   O  O    . ALA   A 1 17  ? 9.380  20.817 13.449  1.00 62.57 ? 17  ALA   A O    1 
ATOM   57   C  CB   . ALA   A 1 17  ? 9.484  21.915 16.546  1.00 62.36 ? 17  ALA   A CB   1 
ATOM   58   N  N    . GLU   A 1 18  ? 7.610  22.083 14.021  1.00 62.93 ? 18  GLU   A N    1 
ATOM   59   C  CA   . GLU   A 1 18  ? 7.418  22.611 12.688  1.00 63.51 ? 18  GLU   A CA   1 
ATOM   60   C  C    . GLU   A 1 18  ? 8.181  23.920 12.594  1.00 63.84 ? 18  GLU   A C    1 
ATOM   61   O  O    . GLU   A 1 18  ? 8.085  24.758 13.492  1.00 64.05 ? 18  GLU   A O    1 
ATOM   62   C  CB   . GLU   A 1 18  ? 5.940  22.837 12.411  1.00 66.09 ? 18  GLU   A CB   1 
ATOM   63   C  CG   . GLU   A 1 18  ? 5.637  23.152 10.961  1.00 71.69 ? 18  GLU   A CG   1 
ATOM   64   C  CD   . GLU   A 1 18  ? 4.169  23.448 10.743  1.00 78.98 ? 18  GLU   A CD   1 
ATOM   65   O  OE1  . GLU   A 1 18  ? 3.331  22.681 11.270  1.00 80.85 ? 18  GLU   A OE1  1 
ATOM   66   O  OE2  . GLU   A 1 18  ? 3.856  24.456 10.067  1.00 80.65 ? 18  GLU   A OE2  1 
ATOM   67   N  N    . ILE   A 1 19  ? 8.991  24.066 11.542  1.00 63.80 ? 19  ILE   A N    1 
ATOM   68   C  CA   . ILE   A 1 19  ? 9.769  25.276 11.274  1.00 64.50 ? 19  ILE   A CA   1 
ATOM   69   C  C    . ILE   A 1 19  ? 8.946  26.226 10.361  1.00 66.04 ? 19  ILE   A C    1 
ATOM   70   O  O    . ILE   A 1 19  ? 8.929  27.443 10.572  1.00 65.94 ? 19  ILE   A O    1 
ATOM   71   C  CB   . ILE   A 1 19  ? 11.151 24.904 10.669  1.00 64.19 ? 19  ILE   A CB   1 
ATOM   72   C  CG1  . ILE   A 1 19  ? 12.065 24.255 11.732  1.00 64.99 ? 19  ILE   A CG1  1 
ATOM   73   C  CG2  . ILE   A 1 19  ? 11.833 26.088 10.020  1.00 63.99 ? 19  ILE   A CG2  1 
ATOM   74   C  CD1  . ILE   A 1 19  ? 13.410 23.726 11.170  1.00 65.90 ? 19  ILE   A CD1  1 
ATOM   75   N  N    . GLY   A 1 20  ? 8.250  25.655 9.382   1.00 67.01 ? 20  GLY   A N    1 
ATOM   76   C  CA   . GLY   A 1 20  ? 7.430  26.435 8.474   1.00 68.51 ? 20  GLY   A CA   1 
ATOM   77   C  C    . GLY   A 1 20  ? 6.656  25.625 7.456   1.00 70.28 ? 20  GLY   A C    1 
ATOM   78   O  O    . GLY   A 1 20  ? 6.639  24.385 7.485   1.00 69.79 ? 20  GLY   A O    1 
ATOM   79   N  N    . GLU   A 1 21  ? 5.964  26.334 6.560   1.00 71.94 ? 21  GLU   A N    1 
ATOM   80   C  CA   . GLU   A 1 21  ? 5.189  25.646 5.493   1.00 73.83 ? 21  GLU   A CA   1 
ATOM   81   C  C    . GLU   A 1 21  ? 5.568  26.239 4.134   1.00 75.20 ? 21  GLU   A C    1 
ATOM   82   O  O    . GLU   A 1 21  ? 5.627  27.477 4.029   1.00 75.26 ? 21  GLU   A O    1 
ATOM   83   C  CB   . GLU   A 1 21  ? 3.685  25.765 5.743   1.00 76.50 ? 21  GLU   A CB   1 
ATOM   84   C  CG   . GLU   A 1 21  ? 3.188  24.858 6.851   1.00 82.08 ? 21  GLU   A CG   1 
ATOM   85   C  CD   . GLU   A 1 21  ? 1.679  24.830 7.013   1.00 90.01 ? 21  GLU   A CD   1 
ATOM   86   O  OE1  . GLU   A 1 21  ? 0.992  24.468 6.040   1.00 91.95 ? 21  GLU   A OE1  1 
ATOM   87   O  OE2  . GLU   A 1 21  ? 1.197  25.161 8.113   1.00 92.39 ? 21  GLU   A OE2  1 
ATOM   88   N  N    . GLY   A 1 22  ? 5.814  25.381 3.142   1.00 76.16 ? 22  GLY   A N    1 
ATOM   89   C  CA   . GLY   A 1 22  ? 6.139  25.858 1.785   1.00 77.73 ? 22  GLY   A CA   1 
ATOM   90   C  C    . GLY   A 1 22  ? 5.206  25.261 0.750   1.00 79.27 ? 22  GLY   A C    1 
ATOM   91   O  O    . GLY   A 1 22  ? 4.376  24.414 1.126   1.00 79.65 ? 22  GLY   A O    1 
ATOM   92   N  N    . ALA   A 1 23  ? 5.313  25.704 -0.503  1.00 79.99 ? 23  ALA   A N    1 
ATOM   93   C  CA   . ALA   A 1 23  ? 4.499  25.111 -1.588  1.00 81.03 ? 23  ALA   A CA   1 
ATOM   94   C  C    . ALA   A 1 23  ? 5.047  23.721 -1.924  1.00 81.66 ? 23  ALA   A C    1 
ATOM   95   O  O    . ALA   A 1 23  ? 6.276  23.538 -1.863  1.00 82.57 ? 23  ALA   A O    1 
ATOM   96   C  CB   . ALA   A 1 23  ? 4.524  26.013 -2.794  1.00 81.37 ? 23  ALA   A CB   1 
ATOM   97   N  N    . TYR   A 1 24  ? 4.159  22.782 -2.253  1.00 80.86 ? 24  TYR   A N    1 
ATOM   98   C  CA   . TYR   A 1 24  ? 3.392  22.052 -1.217  1.00 80.54 ? 24  TYR   A CA   1 
ATOM   99   C  C    . TYR   A 1 24  ? 4.354  21.214 -0.372  1.00 79.61 ? 24  TYR   A C    1 
ATOM   100  O  O    . TYR   A 1 24  ? 4.790  20.147 -0.846  1.00 79.83 ? 24  TYR   A O    1 
ATOM   101  C  CB   . TYR   A 1 24  ? 2.327  21.197 -1.857  1.00 80.71 ? 24  TYR   A CB   1 
ATOM   102  N  N    . GLY   A 1 25  ? 4.684  21.693 0.829   1.00 78.10 ? 25  GLY   A N    1 
ATOM   103  C  CA   . GLY   A 1 25  ? 5.550  20.907 1.724   1.00 76.78 ? 25  GLY   A CA   1 
ATOM   104  C  C    . GLY   A 1 25  ? 5.676  21.543 3.092   1.00 74.68 ? 25  GLY   A C    1 
ATOM   105  O  O    . GLY   A 1 25  ? 5.482  22.765 3.195   1.00 74.92 ? 25  GLY   A O    1 
ATOM   106  N  N    . LYS   A 1 26  ? 5.999  20.741 4.107   1.00 72.24 ? 26  LYS   A N    1 
ATOM   107  C  CA   . LYS   A 1 26  ? 6.231  21.308 5.459   1.00 70.12 ? 26  LYS   A CA   1 
ATOM   108  C  C    . LYS   A 1 26  ? 7.722  21.221 5.777   1.00 66.50 ? 26  LYS   A C    1 
ATOM   109  O  O    . LYS   A 1 26  ? 8.400  20.353 5.202   1.00 66.30 ? 26  LYS   A O    1 
ATOM   110  C  CB   . LYS   A 1 26  ? 5.394  20.575 6.511   1.00 73.01 ? 26  LYS   A CB   1 
ATOM   111  C  CG   . LYS   A 1 26  ? 4.016  21.166 6.774   1.00 77.95 ? 26  LYS   A CG   1 
ATOM   112  C  CD   . LYS   A 1 26  ? 3.187  20.329 7.720   1.00 83.42 ? 26  LYS   A CD   1 
ATOM   113  C  CE   . LYS   A 1 26  ? 1.853  20.957 8.063   1.00 88.80 ? 26  LYS   A CE   1 
ATOM   114  N  NZ   . LYS   A 1 26  ? 2.018  22.194 8.861   1.00 91.93 ? 26  LYS   A NZ   1 
ATOM   115  N  N    . VAL   A 1 27  ? 8.202  22.109 6.642   1.00 63.59 ? 27  VAL   A N    1 
ATOM   116  C  CA   . VAL   A 1 27  ? 9.595  22.090 7.045   1.00 60.93 ? 27  VAL   A CA   1 
ATOM   117  C  C    . VAL   A 1 27  ? 9.573  21.720 8.521   1.00 58.24 ? 27  VAL   A C    1 
ATOM   118  O  O    . VAL   A 1 27  ? 8.812  22.319 9.276   1.00 58.28 ? 27  VAL   A O    1 
ATOM   119  C  CB   . VAL   A 1 27  ? 10.290 23.455 6.822   1.00 61.01 ? 27  VAL   A CB   1 
ATOM   120  C  CG1  . VAL   A 1 27  ? 11.782 23.348 7.110   1.00 61.48 ? 27  VAL   A CG1  1 
ATOM   121  C  CG2  . VAL   A 1 27  ? 10.062 23.954 5.405   1.00 61.46 ? 27  VAL   A CG2  1 
ATOM   122  N  N    . PHE   A 1 28  ? 10.415 20.774 8.934   1.00 56.02 ? 28  PHE   A N    1 
ATOM   123  C  CA   . PHE   A 1 28  ? 10.364 20.319 10.347  1.00 54.78 ? 28  PHE   A CA   1 
ATOM   124  C  C    . PHE   A 1 28  ? 11.759 20.273 10.968  1.00 52.57 ? 28  PHE   A C    1 
ATOM   125  O  O    . PHE   A 1 28  ? 12.714 19.907 10.263  1.00 52.49 ? 28  PHE   A O    1 
ATOM   126  C  CB   . PHE   A 1 28  ? 9.741  18.926 10.438  1.00 55.06 ? 28  PHE   A CB   1 
ATOM   127  C  CG   . PHE   A 1 28  ? 8.242  18.881 10.297  1.00 56.51 ? 28  PHE   A CG   1 
ATOM   128  C  CD1  . PHE   A 1 28  ? 7.421  19.459 11.251  1.00 57.64 ? 28  PHE   A CD1  1 
ATOM   129  C  CD2  . PHE   A 1 28  ? 7.653  18.268 9.203   1.00 57.74 ? 28  PHE   A CD2  1 
ATOM   130  C  CE1  . PHE   A 1 28  ? 6.042  19.416 11.119  1.00 58.75 ? 28  PHE   A CE1  1 
ATOM   131  C  CE2  . PHE   A 1 28  ? 6.275  18.227 9.072   1.00 58.72 ? 28  PHE   A CE2  1 
ATOM   132  C  CZ   . PHE   A 1 28  ? 5.472  18.801 10.029  1.00 58.72 ? 28  PHE   A CZ   1 
ATOM   133  N  N    . LYS   A 1 29  ? 11.874 20.655 12.242  1.00 50.53 ? 29  LYS   A N    1 
ATOM   134  C  CA   . LYS   A 1 29  ? 13.167 20.491 12.954  1.00 48.58 ? 29  LYS   A CA   1 
ATOM   135  C  C    . LYS   A 1 29  ? 13.214 19.023 13.373  1.00 48.22 ? 29  LYS   A C    1 
ATOM   136  O  O    . LYS   A 1 29  ? 12.273 18.583 14.054  1.00 48.96 ? 29  LYS   A O    1 
ATOM   137  C  CB   . LYS   A 1 29  ? 13.257 21.428 14.159  1.00 48.03 ? 29  LYS   A CB   1 
ATOM   138  C  CG   . LYS   A 1 29  ? 14.542 21.336 14.970  1.00 49.41 ? 29  LYS   A CG   1 
ATOM   139  C  CD   . LYS   A 1 29  ? 14.567 22.308 16.126  1.00 52.46 ? 29  LYS   A CD   1 
ATOM   140  C  CE   . LYS   A 1 29  ? 15.873 22.301 16.889  1.00 53.70 ? 29  LYS   A CE   1 
ATOM   141  N  NZ   . LYS   A 1 29  ? 15.859 23.274 18.006  1.00 54.15 ? 29  LYS   A NZ   1 
ATOM   142  N  N    . ALA   A 1 30  ? 14.246 18.289 12.961  1.00 47.06 ? 30  ALA   A N    1 
ATOM   143  C  CA   . ALA   A 1 30  ? 14.255 16.837 13.241  1.00 46.94 ? 30  ALA   A CA   1 
ATOM   144  C  C    . ALA   A 1 30  ? 15.534 16.416 13.960  1.00 46.93 ? 30  ALA   A C    1 
ATOM   145  O  O    . ALA   A 1 30  ? 16.510 17.185 13.945  1.00 46.73 ? 30  ALA   A O    1 
ATOM   146  C  CB   . ALA   A 1 30  ? 14.099 16.075 11.952  1.00 47.02 ? 30  ALA   A CB   1 
ATOM   147  N  N    . ARG   A 1 31  ? 15.506 15.233 14.572  1.00 46.63 ? 31  ARG   A N    1 
ATOM   148  C  CA   . ARG   A 1 31  ? 16.721 14.684 15.220  1.00 46.89 ? 31  ARG   A CA   1 
ATOM   149  C  C    . ARG   A 1 31  ? 17.378 13.710 14.242  1.00 46.34 ? 31  ARG   A C    1 
ATOM   150  O  O    . ARG   A 1 31  ? 16.690 12.770 13.810  1.00 45.77 ? 31  ARG   A O    1 
ATOM   151  C  CB   . ARG   A 1 31  ? 16.343 13.962 16.516  1.00 47.88 ? 31  ARG   A CB   1 
ATOM   152  C  CG   . ARG   A 1 31  ? 16.012 14.881 17.681  1.00 50.36 ? 31  ARG   A CG   1 
ATOM   153  C  CD   . ARG   A 1 31  ? 17.271 15.387 18.353  1.00 53.54 ? 31  ARG   A CD   1 
ATOM   154  N  NE   . ARG   A 1 31  ? 17.012 15.843 19.709  1.00 55.91 ? 31  ARG   A NE   1 
ATOM   155  C  CZ   . ARG   A 1 31  ? 17.943 16.289 20.541  1.00 57.21 ? 31  ARG   A CZ   1 
ATOM   156  N  NH1  . ARG   A 1 31  ? 19.195 16.398 20.135  1.00 56.39 ? 31  ARG   A NH1  1 
ATOM   157  N  NH2  . ARG   A 1 31  ? 17.620 16.621 21.778  1.00 58.06 ? 31  ARG   A NH2  1 
ATOM   158  N  N    . ASP   A 1 32  ? 18.645 13.938 13.893  1.00 46.41 ? 32  ASP   A N    1 
ATOM   159  C  CA   . ASP   A 1 32  ? 19.377 12.971 13.032  1.00 47.55 ? 32  ASP   A CA   1 
ATOM   160  C  C    . ASP   A 1 32  ? 19.821 11.820 13.937  1.00 48.79 ? 32  ASP   A C    1 
ATOM   161  O  O    . ASP   A 1 32  ? 20.931 11.900 14.487  1.00 48.77 ? 32  ASP   A O    1 
ATOM   162  C  CB   . ASP   A 1 32  ? 20.522 13.648 12.276  1.00 48.02 ? 32  ASP   A CB   1 
ATOM   163  C  CG   . ASP   A 1 32  ? 21.165 12.774 11.216  1.00 50.37 ? 32  ASP   A CG   1 
ATOM   164  O  OD1  . ASP   A 1 32  ? 20.773 11.597 11.108  1.00 50.69 ? 32  ASP   A OD1  1 
ATOM   165  O  OD2  . ASP   A 1 32  ? 22.038 13.289 10.495  1.00 51.20 ? 32  ASP   A OD2  1 
ATOM   166  N  N    . LEU   A 1 33  ? 18.984 10.793 14.074  1.00 50.10 ? 33  LEU   A N    1 
ATOM   167  C  CA   . LEU   A 1 33  ? 19.266 9.677  15.017  1.00 51.94 ? 33  LEU   A CA   1 
ATOM   168  C  C    . LEU   A 1 33  ? 20.598 8.995  14.693  1.00 52.61 ? 33  LEU   A C    1 
ATOM   169  O  O    . LEU   A 1 33  ? 21.289 8.595  15.645  1.00 52.66 ? 33  LEU   A O    1 
ATOM   170  C  CB   . LEU   A 1 33  ? 18.101 8.686  14.931  1.00 52.59 ? 33  LEU   A CB   1 
ATOM   171  C  CG   . LEU   A 1 33  ? 16.709 9.307  15.041  1.00 54.77 ? 33  LEU   A CG   1 
ATOM   172  C  CD1  . LEU   A 1 33  ? 15.636 8.231  15.086  1.00 55.31 ? 33  LEU   A CD1  1 
ATOM   173  C  CD2  . LEU   A 1 33  ? 16.611 10.205 16.263  1.00 55.54 ? 33  LEU   A CD2  1 
ATOM   174  N  N    . LYS   A 1 34  ? 20.944 8.861  13.410  1.00 52.81 ? 34  LYS   A N    1 
ATOM   175  C  CA   . LYS   A 1 34  ? 22.175 8.108  13.043  1.00 53.67 ? 34  LYS   A CA   1 
ATOM   176  C  C    . LYS   A 1 34  ? 23.409 9.011  13.142  1.00 53.25 ? 34  LYS   A C    1 
ATOM   177  O  O    . LYS   A 1 34  ? 24.518 8.508  12.906  1.00 53.41 ? 34  LYS   A O    1 
ATOM   178  C  CB   . LYS   A 1 34  ? 22.039 7.500  11.644  1.00 57.02 ? 34  LYS   A CB   1 
ATOM   179  C  CG   . LYS   A 1 34  ? 21.062 6.338  11.533  1.00 62.71 ? 34  LYS   A CG   1 
ATOM   180  C  CD   . LYS   A 1 34  ? 21.243 5.527  10.268  1.00 69.08 ? 34  LYS   A CD   1 
ATOM   181  C  CE   . LYS   A 1 34  ? 20.243 4.398  10.138  1.00 74.52 ? 34  LYS   A CE   1 
ATOM   182  N  NZ   . LYS   A 1 34  ? 18.849 4.899  10.105  1.00 77.29 ? 34  LYS   A NZ   1 
ATOM   183  N  N    . ASN   A 1 35  ? 23.222 10.287 13.481  1.00 52.57 ? 35  ASN   A N    1 
ATOM   184  C  CA   . ASN   A 1 35  ? 24.373 11.228 13.523  1.00 51.91 ? 35  ASN   A CA   1 
ATOM   185  C  C    . ASN   A 1 35  ? 24.420 11.946 14.876  1.00 50.45 ? 35  ASN   A C    1 
ATOM   186  O  O    . ASN   A 1 35  ? 24.649 13.169 14.882  1.00 51.25 ? 35  ASN   A O    1 
ATOM   187  C  CB   . ASN   A 1 35  ? 24.364 12.168 12.316  1.00 53.73 ? 35  ASN   A CB   1 
ATOM   188  C  CG   . ASN   A 1 35  ? 24.709 11.449 11.030  1.00 57.31 ? 35  ASN   A CG   1 
ATOM   189  O  OD1  . ASN   A 1 35  ? 23.866 11.300 10.149  1.00 57.76 ? 35  ASN   A OD1  1 
ATOM   190  N  ND2  . ASN   A 1 35  ? 25.937 10.969 10.928  1.00 59.10 ? 35  ASN   A ND2  1 
ATOM   191  N  N    . GLY   A 1 36  ? 24.216 11.214 15.975  1.00 47.57 ? 36  GLY   A N    1 
ATOM   192  C  CA   . GLY   A 1 36  ? 24.350 11.812 17.319  1.00 46.33 ? 36  GLY   A CA   1 
ATOM   193  C  C    . GLY   A 1 36  ? 23.146 12.631 17.739  1.00 44.64 ? 36  GLY   A C    1 
ATOM   194  O  O    . GLY   A 1 36  ? 23.301 13.479 18.633  1.00 44.28 ? 36  GLY   A O    1 
ATOM   195  N  N    . GLY   A 1 37  ? 21.989 12.385 17.124  1.00 43.53 ? 37  GLY   A N    1 
ATOM   196  C  CA   . GLY   A 1 37  ? 20.779 13.165 17.437  1.00 42.61 ? 37  GLY   A CA   1 
ATOM   197  C  C    . GLY   A 1 37  ? 20.984 14.639 17.150  1.00 41.43 ? 37  GLY   A C    1 
ATOM   198  O  O    . GLY   A 1 37  ? 20.358 15.462 17.836  1.00 42.28 ? 37  GLY   A O    1 
ATOM   199  N  N    . ARG   A 1 38  ? 21.837 14.960 16.177  1.00 39.62 ? 38  ARG   A N    1 
ATOM   200  C  CA   . ARG   A 1 38  ? 22.033 16.378 15.781  1.00 39.13 ? 38  ARG   A CA   1 
ATOM   201  C  C    . ARG   A 1 38  ? 20.716 16.904 15.207  1.00 39.28 ? 38  ARG   A C    1 
ATOM   202  O  O    . ARG   A 1 38  ? 19.995 16.119 14.570  1.00 39.70 ? 38  ARG   A O    1 
ATOM   203  C  CB   . ARG   A 1 38  ? 23.160 16.509 14.754  1.00 39.37 ? 38  ARG   A CB   1 
ATOM   204  C  CG   . ARG   A 1 38  ? 22.884 15.808 13.433  1.00 41.12 ? 38  ARG   A CG   1 
ATOM   205  C  CD   . ARG   A 1 38  ? 24.041 15.954 12.466  1.00 43.97 ? 38  ARG   A CD   1 
ATOM   206  N  NE   . ARG   A 1 38  ? 23.826 15.227 11.224  1.00 47.10 ? 38  ARG   A NE   1 
ATOM   207  C  CZ   . ARG   A 1 38  ? 24.709 15.155 10.236  1.00 49.78 ? 38  ARG   A CZ   1 
ATOM   208  N  NH1  . ARG   A 1 38  ? 25.861 15.795 10.333  1.00 49.22 ? 38  ARG   A NH1  1 
ATOM   209  N  NH2  . ARG   A 1 38  ? 24.438 14.442 9.157   1.00 49.95 ? 38  ARG   A NH2  1 
ATOM   210  N  N    . PHE   A 1 39  ? 20.415 18.177 15.452  1.00 38.87 ? 39  PHE   A N    1 
ATOM   211  C  CA   . PHE   A 1 39  ? 19.188 18.784 14.880  1.00 39.21 ? 39  PHE   A CA   1 
ATOM   212  C  C    . PHE   A 1 39  ? 19.388 18.986 13.376  1.00 40.45 ? 39  PHE   A C    1 
ATOM   213  O  O    . PHE   A 1 39  ? 20.485 19.400 12.964  1.00 40.77 ? 39  PHE   A O    1 
ATOM   214  C  CB   . PHE   A 1 39  ? 18.837 20.092 15.590  1.00 38.35 ? 39  PHE   A CB   1 
ATOM   215  C  CG   . PHE   A 1 39  ? 18.231 19.916 16.959  1.00 37.89 ? 39  PHE   A CG   1 
ATOM   216  C  CD1  . PHE   A 1 39  ? 17.118 19.111 17.139  1.00 38.42 ? 39  PHE   A CD1  1 
ATOM   217  C  CD2  . PHE   A 1 39  ? 18.758 20.569 18.060  1.00 38.36 ? 39  PHE   A CD2  1 
ATOM   218  C  CE1  . PHE   A 1 39  ? 16.555 18.951 18.395  1.00 39.05 ? 39  PHE   A CE1  1 
ATOM   219  C  CE2  . PHE   A 1 39  ? 18.193 20.409 19.315  1.00 39.05 ? 39  PHE   A CE2  1 
ATOM   220  C  CZ   . PHE   A 1 39  ? 17.094 19.601 19.480  1.00 38.88 ? 39  PHE   A CZ   1 
ATOM   221  N  N    . VAL   A 1 40  ? 18.354 18.681 12.592  1.00 40.54 ? 40  VAL   A N    1 
ATOM   222  C  CA   . VAL   A 1 40  ? 18.423 18.862 11.115  1.00 40.64 ? 40  VAL   A CA   1 
ATOM   223  C  C    . VAL   A 1 40  ? 17.113 19.502 10.649  1.00 41.39 ? 40  VAL   A C    1 
ATOM   224  O  O    . VAL   A 1 40  ? 16.102 19.342 11.353  1.00 41.89 ? 40  VAL   A O    1 
ATOM   225  C  CB   . VAL   A 1 40  ? 18.678 17.521 10.403  1.00 40.16 ? 40  VAL   A CB   1 
ATOM   226  C  CG1  . VAL   A 1 40  ? 20.111 17.047 10.582  1.00 40.13 ? 40  VAL   A CG1  1 
ATOM   227  C  CG2  . VAL   A 1 40  ? 17.695 16.451 10.847  1.00 40.10 ? 40  VAL   A CG2  1 
ATOM   228  N  N    . ALA   A 1 41  ? 17.139 20.212 9.521   1.00 41.04 ? 41  ALA   A N    1 
ATOM   229  C  CA   . ALA   A 1 41  ? 15.900 20.789 8.957   1.00 41.43 ? 41  ALA   A CA   1 
ATOM   230  C  C    . ALA   A 1 41  ? 15.421 19.880 7.824   1.00 43.68 ? 41  ALA   A C    1 
ATOM   231  O  O    . ALA   A 1 41  ? 16.139 19.770 6.818   1.00 43.53 ? 41  ALA   A O    1 
ATOM   232  C  CB   . ALA   A 1 41  ? 16.156 22.192 8.480   1.00 40.50 ? 41  ALA   A CB   1 
ATOM   233  N  N    . LEU   A 1 42  ? 14.262 19.243 7.998   1.00 45.91 ? 42  LEU   A N    1 
ATOM   234  C  CA   . LEU   A 1 42  ? 13.746 18.293 6.978   1.00 48.56 ? 42  LEU   A CA   1 
ATOM   235  C  C    . LEU   A 1 42  ? 12.658 18.972 6.142   1.00 50.57 ? 42  LEU   A C    1 
ATOM   236  O  O    . LEU   A 1 42  ? 11.645 19.395 6.723   1.00 50.49 ? 42  LEU   A O    1 
ATOM   237  C  CB   . LEU   A 1 42  ? 13.206 17.044 7.680   1.00 49.85 ? 42  LEU   A CB   1 
ATOM   238  C  CG   . LEU   A 1 42  ? 14.065 15.790 7.537   1.00 52.63 ? 42  LEU   A CG   1 
ATOM   239  C  CD1  . LEU   A 1 42  ? 15.312 15.886 8.401   1.00 53.69 ? 42  LEU   A CD1  1 
ATOM   240  C  CD2  . LEU   A 1 42  ? 13.267 14.546 7.889   1.00 53.46 ? 42  LEU   A CD2  1 
ATOM   241  N  N    . LYS   A 1 43  ? 12.873 19.067 4.829   1.00 52.35 ? 43  LYS   A N    1 
ATOM   242  C  CA   . LYS   A 1 43  ? 11.862 19.662 3.918   1.00 54.70 ? 43  LYS   A CA   1 
ATOM   243  C  C    . LYS   A 1 43  ? 11.351 18.567 2.980   1.00 59.12 ? 43  LYS   A C    1 
ATOM   244  O  O    . LYS   A 1 43  ? 12.182 17.931 2.305   1.00 58.76 ? 43  LYS   A O    1 
ATOM   245  C  CB   . LYS   A 1 43  ? 12.458 20.828 3.125   1.00 54.59 ? 43  LYS   A CB   1 
ATOM   246  C  CG   . LYS   A 1 43  ? 11.638 21.271 1.920   1.00 56.59 ? 43  LYS   A CG   1 
ATOM   247  C  CD   . LYS   A 1 43  ? 12.118 22.563 1.299   1.00 58.50 ? 43  LYS   A CD   1 
ATOM   248  C  CE   . LYS   A 1 43  ? 11.809 23.777 2.148   1.00 60.98 ? 43  LYS   A CE   1 
ATOM   249  N  NZ   . LYS   A 1 43  ? 12.213 25.034 1.477   1.00 62.48 ? 43  LYS   A NZ   1 
ATOM   250  N  N    . ARG   A 1 44  ? 10.034 18.361 2.951   1.00 63.04 ? 44  ARG   A N    1 
ATOM   251  C  CA   . ARG   A 1 44  ? 9.441  17.305 2.089   1.00 67.16 ? 44  ARG   A CA   1 
ATOM   252  C  C    . ARG   A 1 44  ? 8.884  17.951 0.818   1.00 70.38 ? 44  ARG   A C    1 
ATOM   253  O  O    . ARG   A 1 44  ? 8.042  18.858 0.940   1.00 71.05 ? 44  ARG   A O    1 
ATOM   254  C  CB   . ARG   A 1 44  ? 8.378  16.533 2.875   1.00 70.11 ? 44  ARG   A CB   1 
ATOM   255  C  CG   . ARG   A 1 44  ? 8.943  15.780 4.070   1.00 75.48 ? 44  ARG   A CG   1 
ATOM   256  C  CD   . ARG   A 1 44  ? 7.892  15.098 4.923   1.00 80.58 ? 44  ARG   A CD   1 
ATOM   257  N  NE   . ARG   A 1 44  ? 8.500  14.397 6.045   1.00 84.41 ? 44  ARG   A NE   1 
ATOM   258  C  CZ   . ARG   A 1 44  ? 7.824  13.721 6.967   1.00 87.40 ? 44  ARG   A CZ   1 
ATOM   259  N  NH1  . ARG   A 1 44  ? 6.505  13.693 6.931   1.00 87.47 ? 44  ARG   A NH1  1 
ATOM   260  N  NH2  . ARG   A 1 44  ? 8.472  13.078 7.922   1.00 87.51 ? 44  ARG   A NH2  1 
ATOM   261  N  N    . VAL   A 1 45  ? 9.355  17.505 -0.349  1.00 72.31 ? 45  VAL   A N    1 
ATOM   262  C  CA   . VAL   A 1 45  ? 8.906  18.081 -1.638  1.00 74.81 ? 45  VAL   A CA   1 
ATOM   263  C  C    . VAL   A 1 45  ? 7.955  17.098 -2.324  1.00 77.39 ? 45  VAL   A C    1 
ATOM   264  O  O    . VAL   A 1 45  ? 8.377  15.953 -2.571  1.00 77.58 ? 45  VAL   A O    1 
ATOM   265  C  CB   . VAL   A 1 45  ? 10.103 18.387 -2.499  1.00 74.85 ? 45  VAL   A CB   1 
ATOM   266  N  N    . ARG   A 1 46  ? 6.727  17.533 -2.626  1.00 79.21 ? 46  ARG   A N    1 
ATOM   267  C  CA   . ARG   A 1 46  ? 5.714  16.625 -3.217  1.00 81.25 ? 46  ARG   A CA   1 
ATOM   268  C  C    . ARG   A 1 46  ? 5.941  16.456 -4.724  1.00 82.73 ? 46  ARG   A C    1 
ATOM   269  O  O    . ARG   A 1 46  ? 6.727  17.237 -5.295  1.00 82.97 ? 46  ARG   A O    1 
ATOM   270  C  CB   . ARG   A 1 46  ? 4.330  17.152 -2.926  1.00 81.57 ? 46  ARG   A CB   1 
ATOM   271  N  N    . VAL   A 1 47  ? 5.273  15.473 -5.336  1.00 83.47 ? 47  VAL   A N    1 
ATOM   272  C  CA   . VAL   A 1 47  ? 5.409  15.225 -6.792  1.00 84.54 ? 47  VAL   A CA   1 
ATOM   273  C  C    . VAL   A 1 47  ? 4.108  15.603 -7.509  1.00 85.09 ? 47  VAL   A C    1 
ATOM   274  O  O    . VAL   A 1 47  ? 4.112  15.564 -8.755  1.00 85.29 ? 47  VAL   A O    1 
ATOM   275  C  CB   . VAL   A 1 47  ? 5.765  13.779 -7.036  1.00 84.82 ? 47  VAL   A CB   1 
ATOM   276  N  N    . PRO   A 1 55  ? 8.063  14.676 -12.287 1.00 79.71 ? 55  PRO   A N    1 
ATOM   277  C  CA   . PRO   A 1 55  ? 8.561  15.875 -13.002 1.00 79.82 ? 55  PRO   A CA   1 
ATOM   278  C  C    . PRO   A 1 55  ? 10.052 15.705 -13.303 1.00 79.61 ? 55  PRO   A C    1 
ATOM   279  O  O    . PRO   A 1 55  ? 10.637 14.713 -12.830 1.00 79.97 ? 55  PRO   A O    1 
ATOM   280  C  CB   . PRO   A 1 55  ? 8.302  17.111 -12.178 1.00 79.87 ? 55  PRO   A CB   1 
ATOM   281  N  N    . LEU   A 1 56  ? 10.636 16.633 -14.067 1.00 78.55 ? 56  LEU   A N    1 
ATOM   282  C  CA   . LEU   A 1 56  ? 12.082 16.573 -14.382 1.00 77.53 ? 56  LEU   A CA   1 
ATOM   283  C  C    . LEU   A 1 56  ? 12.750 17.888 -13.969 1.00 75.80 ? 56  LEU   A C    1 
ATOM   284  O  O    . LEU   A 1 56  ? 13.945 17.859 -13.625 1.00 75.48 ? 56  LEU   A O    1 
ATOM   285  C  CB   . LEU   A 1 56  ? 12.274 16.291 -15.850 1.00 77.76 ? 56  LEU   A CB   1 
ATOM   286  N  N    . SER   A 1 57  ? 12.000 18.993 -14.004 1.00 74.21 ? 57  SER   A N    1 
ATOM   287  C  CA   . SER   A 1 57  ? 12.547 20.314 -13.604 1.00 72.84 ? 57  SER   A CA   1 
ATOM   288  C  C    . SER   A 1 57  ? 12.976 20.260 -12.136 1.00 71.17 ? 57  SER   A C    1 
ATOM   289  O  O    . SER   A 1 57  ? 14.073 20.753 -11.821 1.00 70.86 ? 57  SER   A O    1 
ATOM   290  C  CB   . SER   A 1 57  ? 11.533 21.401 -13.837 1.00 73.87 ? 57  SER   A CB   1 
ATOM   291  O  OG   . SER   A 1 57  ? 10.315 21.104 -13.171 1.00 75.59 ? 57  SER   A OG   1 
ATOM   292  N  N    . THR   A 1 58  ? 12.137 19.675 -11.280 1.00 69.77 ? 58  THR   A N    1 
ATOM   293  C  CA   . THR   A 1 58  ? 12.472 19.547 -9.837  1.00 68.84 ? 58  THR   A CA   1 
ATOM   294  C  C    . THR   A 1 58  ? 13.667 18.598 -9.688  1.00 67.00 ? 58  THR   A C    1 
ATOM   295  O  O    . THR   A 1 58  ? 14.515 18.856 -8.816  1.00 66.95 ? 58  THR   A O    1 
ATOM   296  C  CB   . THR   A 1 58  ? 11.244 19.098 -9.034  1.00 70.35 ? 58  THR   A CB   1 
ATOM   297  O  OG1  . THR   A 1 58  ? 10.230 20.090 -9.196  1.00 71.53 ? 58  THR   A OG1  1 
ATOM   298  C  CG2  . THR   A 1 58  ? 11.540 18.901 -7.564  1.00 70.71 ? 58  THR   A CG2  1 
ATOM   299  N  N    . ILE   A 1 59  ? 13.728 17.551 -10.514 1.00 65.15 ? 59  ILE   A N    1 
ATOM   300  C  CA   . ILE   A 1 59  ? 14.885 16.609 -10.481 1.00 63.58 ? 59  ILE   A CA   1 
ATOM   301  C  C    . ILE   A 1 59  ? 16.155 17.416 -10.753 1.00 60.15 ? 59  ILE   A C    1 
ATOM   302  O  O    . ILE   A 1 59  ? 17.143 17.220 -10.023 1.00 59.75 ? 59  ILE   A O    1 
ATOM   303  C  CB   . ILE   A 1 59  ? 14.699 15.481 -11.513 1.00 65.07 ? 59  ILE   A CB   1 
ATOM   304  C  CG1  . ILE   A 1 59  ? 13.348 14.781 -11.349 1.00 66.70 ? 59  ILE   A CG1  1 
ATOM   305  C  CG2  . ILE   A 1 59  ? 15.856 14.496 -11.452 1.00 65.55 ? 59  ILE   A CG2  1 
ATOM   306  C  CD1  . ILE   A 1 59  ? 13.138 14.169 -9.986  1.00 68.29 ? 59  ILE   A CD1  1 
ATOM   307  N  N    . ARG   A 1 60  ? 16.112 18.293 -11.758 1.00 57.39 ? 60  ARG   A N    1 
ATOM   308  C  CA   . ARG   A 1 60  ? 17.275 19.158 -12.084 1.00 55.36 ? 60  ARG   A CA   1 
ATOM   309  C  C    . ARG   A 1 60  ? 17.576 20.078 -10.897 1.00 51.92 ? 60  ARG   A C    1 
ATOM   310  O  O    . ARG   A 1 60  ? 18.761 20.237 -10.567 1.00 51.20 ? 60  ARG   A O    1 
ATOM   311  C  CB   . ARG   A 1 60  ? 16.961 19.965 -13.345 1.00 58.37 ? 60  ARG   A CB   1 
ATOM   312  C  CG   . ARG   A 1 60  ? 17.580 21.355 -13.374 1.00 66.04 ? 60  ARG   A CG   1 
ATOM   313  C  CD   . ARG   A 1 60  ? 17.050 22.165 -14.541 1.00 72.56 ? 60  ARG   A CD   1 
ATOM   314  N  NE   . ARG   A 1 60  ? 15.597 22.255 -14.525 1.00 78.13 ? 60  ARG   A NE   1 
ATOM   315  C  CZ   . ARG   A 1 60  ? 14.872 22.894 -15.436 1.00 82.77 ? 60  ARG   A CZ   1 
ATOM   316  N  NH1  . ARG   A 1 60  ? 15.462 23.472 -16.466 1.00 82.51 ? 60  ARG   A NH1  1 
ATOM   317  N  NH2  . ARG   A 1 60  ? 13.557 22.953 -15.313 1.00 83.91 ? 60  ARG   A NH2  1 
ATOM   318  N  N    . GLU   A 1 61  ? 16.539 20.662 -10.292 1.00 49.32 ? 61  GLU   A N    1 
ATOM   319  C  CA   . GLU   A 1 61  ? 16.735 21.618 -9.171  1.00 47.65 ? 61  GLU   A CA   1 
ATOM   320  C  C    . GLU   A 1 61  ? 17.497 20.928 -8.037  1.00 45.99 ? 61  GLU   A C    1 
ATOM   321  O  O    . GLU   A 1 61  ? 18.447 21.535 -7.513  1.00 46.26 ? 61  GLU   A O    1 
ATOM   322  C  CB   . GLU   A 1 61  ? 15.385 22.152 -8.691  1.00 50.26 ? 61  GLU   A CB   1 
ATOM   323  C  CG   . GLU   A 1 61  ? 14.679 23.026 -9.710  1.00 56.25 ? 61  GLU   A CG   1 
ATOM   324  C  CD   . GLU   A 1 61  ? 13.474 23.777 -9.170  1.00 64.80 ? 61  GLU   A CD   1 
ATOM   325  O  OE1  . GLU   A 1 61  ? 12.540 23.118 -8.676  1.00 67.15 ? 61  GLU   A OE1  1 
ATOM   326  O  OE2  . GLU   A 1 61  ? 13.472 25.020 -9.248  1.00 67.74 ? 61  GLU   A OE2  1 
ATOM   327  N  N    . VAL   A 1 62  ? 17.092 19.708 -7.686  1.00 44.55 ? 62  VAL   A N    1 
ATOM   328  C  CA   . VAL   A 1 62  ? 17.774 18.942 -6.601  1.00 44.31 ? 62  VAL   A CA   1 
ATOM   329  C  C    . VAL   A 1 62  ? 19.203 18.618 -7.045  1.00 42.84 ? 62  VAL   A C    1 
ATOM   330  O  O    . VAL   A 1 62  ? 20.105 18.671 -6.197  1.00 43.46 ? 62  VAL   A O    1 
ATOM   331  C  CB   . VAL   A 1 62  ? 16.985 17.670 -6.244  1.00 45.65 ? 62  VAL   A CB   1 
ATOM   332  C  CG1  . VAL   A 1 62  ? 17.688 16.850 -5.174  1.00 46.12 ? 62  VAL   A CG1  1 
ATOM   333  C  CG2  . VAL   A 1 62  ? 15.563 18.000 -5.820  1.00 46.29 ? 62  VAL   A CG2  1 
ATOM   334  N  N    . ALA   A 1 63  ? 19.392 18.308 -8.330  1.00 40.61 ? 63  ALA   A N    1 
ATOM   335  C  CA   . ALA   A 1 63  ? 20.737 17.998 -8.864  1.00 39.30 ? 63  ALA   A CA   1 
ATOM   336  C  C    . ALA   A 1 63  ? 21.649 19.218 -8.711  1.00 38.67 ? 63  ALA   A C    1 
ATOM   337  O  O    . ALA   A 1 63  ? 22.823 19.034 -8.348  1.00 40.21 ? 63  ALA   A O    1 
ATOM   338  C  CB   . ALA   A 1 63  ? 20.627 17.574 -10.306 1.00 38.63 ? 63  ALA   A CB   1 
ATOM   339  N  N    . VAL   A 1 64  ? 21.117 20.413 -8.973  1.00 36.43 ? 64  VAL   A N    1 
ATOM   340  C  CA   . VAL   A 1 64  ? 21.914 21.663 -8.819  1.00 35.99 ? 64  VAL   A CA   1 
ATOM   341  C  C    . VAL   A 1 64  ? 22.285 21.822 -7.343  1.00 36.97 ? 64  VAL   A C    1 
ATOM   342  O  O    . VAL   A 1 64  ? 23.443 22.170 -7.066  1.00 37.24 ? 64  VAL   A O    1 
ATOM   343  C  CB   . VAL   A 1 64  ? 21.138 22.888 -9.338  1.00 35.10 ? 64  VAL   A CB   1 
ATOM   344  C  CG1  . VAL   A 1 64  ? 21.883 24.186 -9.072  1.00 34.87 ? 64  VAL   A CG1  1 
ATOM   345  C  CG2  . VAL   A 1 64  ? 20.793 22.755 -10.813 1.00 34.31 ? 64  VAL   A CG2  1 
ATOM   346  N  N    . LEU   A 1 65  ? 21.333 21.568 -6.443  1.00 37.31 ? 65  LEU   A N    1 
ATOM   347  C  CA   . LEU   A 1 65  ? 21.578 21.736 -4.985  1.00 38.67 ? 65  LEU   A CA   1 
ATOM   348  C  C    . LEU   A 1 65  ? 22.662 20.755 -4.523  1.00 38.82 ? 65  LEU   A C    1 
ATOM   349  O  O    . LEU   A 1 65  ? 23.547 21.179 -3.763  1.00 38.78 ? 65  LEU   A O    1 
ATOM   350  C  CB   . LEU   A 1 65  ? 20.258 21.515 -4.238  1.00 39.43 ? 65  LEU   A CB   1 
ATOM   351  C  CG   . LEU   A 1 65  ? 19.603 22.773 -3.671  1.00 42.67 ? 65  LEU   A CG   1 
ATOM   352  C  CD1  . LEU   A 1 65  ? 19.364 23.799 -4.766  1.00 43.69 ? 65  LEU   A CD1  1 
ATOM   353  C  CD2  . LEU   A 1 65  ? 18.293 22.431 -2.979  1.00 44.04 ? 65  LEU   A CD2  1 
ATOM   354  N  N    . ARG   A 1 66  ? 22.597 19.503 -4.980  1.00 38.90 ? 66  ARG   A N    1 
ATOM   355  C  CA   . ARG   A 1 66  ? 23.612 18.482 -4.605  1.00 39.34 ? 66  ARG   A CA   1 
ATOM   356  C  C    . ARG   A 1 66  ? 24.976 18.896 -5.163  1.00 38.74 ? 66  ARG   A C    1 
ATOM   357  O  O    . ARG   A 1 66  ? 25.985 18.668 -4.475  1.00 38.79 ? 66  ARG   A O    1 
ATOM   358  C  CB   . ARG   A 1 66  ? 23.189 17.104 -5.118  1.00 41.60 ? 66  ARG   A CB   1 
ATOM   359  C  CG   . ARG   A 1 66  ? 21.805 16.669 -4.660  1.00 47.09 ? 66  ARG   A CG   1 
ATOM   360  C  CD   . ARG   A 1 66  ? 21.824 15.297 -4.018  1.00 53.57 ? 66  ARG   A CD   1 
ATOM   361  N  NE   . ARG   A 1 66  ? 22.655 15.277 -2.823  1.00 60.02 ? 66  ARG   A NE   1 
ATOM   362  C  CZ   . ARG   A 1 66  ? 22.830 14.214 -2.047  1.00 65.22 ? 66  ARG   A CZ   1 
ATOM   363  N  NH1  . ARG   A 1 66  ? 22.246 13.070 -2.353  1.00 65.69 ? 66  ARG   A NH1  1 
ATOM   364  N  NH2  . ARG   A 1 66  ? 23.587 14.301 -0.967  1.00 66.09 ? 66  ARG   A NH2  1 
ATOM   365  N  N    . HIS   A 1 67  ? 24.994 19.484 -6.362  1.00 38.17 ? 67  HIS   A N    1 
ATOM   366  C  CA   . HIS   A 1 67  ? 26.261 19.945 -6.989  1.00 37.40 ? 67  HIS   A CA   1 
ATOM   367  C  C    . HIS   A 1 67  ? 26.850 21.106 -6.183  1.00 37.44 ? 67  HIS   A C    1 
ATOM   368  O  O    . HIS   A 1 67  ? 28.067 21.113 -5.935  1.00 37.03 ? 67  HIS   A O    1 
ATOM   369  C  CB   . HIS   A 1 67  ? 26.015 20.339 -8.449  1.00 36.98 ? 67  HIS   A CB   1 
ATOM   370  C  CG   . HIS   A 1 67  ? 27.188 20.974 -9.116  1.00 36.88 ? 67  HIS   A CG   1 
ATOM   371  N  ND1  . HIS   A 1 67  ? 28.382 20.317 -9.319  1.00 38.34 ? 67  HIS   A ND1  1 
ATOM   372  C  CD2  . HIS   A 1 67  ? 27.346 22.196 -9.632  1.00 36.53 ? 67  HIS   A CD2  1 
ATOM   373  C  CE1  . HIS   A 1 67  ? 29.227 21.130 -9.933  1.00 37.99 ? 67  HIS   A CE1  1 
ATOM   374  N  NE2  . HIS   A 1 67  ? 28.618 22.277 -10.132 1.00 36.84 ? 67  HIS   A NE2  1 
ATOM   375  N  N    . LEU   A 1 68  ? 26.011 22.069 -5.798  1.00 37.52 ? 68  LEU   A N    1 
ATOM   376  C  CA   . LEU   A 1 68  ? 26.483 23.230 -4.996  1.00 38.18 ? 68  LEU   A CA   1 
ATOM   377  C  C    . LEU   A 1 68  ? 27.043 22.720 -3.664  1.00 37.46 ? 68  LEU   A C    1 
ATOM   378  O  O    . LEU   A 1 68  ? 28.020 23.312 -3.178  1.00 37.12 ? 68  LEU   A O    1 
ATOM   379  C  CB   . LEU   A 1 68  ? 25.311 24.191 -4.781  1.00 39.14 ? 68  LEU   A CB   1 
ATOM   380  C  CG   . LEU   A 1 68  ? 25.211 25.349 -5.773  1.00 41.11 ? 68  LEU   A CG   1 
ATOM   381  C  CD1  . LEU   A 1 68  ? 25.230 24.842 -7.206  1.00 42.08 ? 68  LEU   A CD1  1 
ATOM   382  C  CD2  . LEU   A 1 68  ? 23.952 26.163 -5.518  1.00 41.10 ? 68  LEU   A CD2  1 
ATOM   383  N  N    . GLU   A 1 69  ? 26.449 21.658 -3.117  1.00 37.04 ? 69  GLU   A N    1 
ATOM   384  C  CA   . GLU   A 1 69  ? 26.924 21.063 -1.840  1.00 36.49 ? 69  GLU   A CA   1 
ATOM   385  C  C    . GLU   A 1 69  ? 28.357 20.551 -2.018  1.00 37.44 ? 69  GLU   A C    1 
ATOM   386  O  O    . GLU   A 1 69  ? 29.136 20.659 -1.062  1.00 38.69 ? 69  GLU   A O    1 
ATOM   387  C  CB   . GLU   A 1 69  ? 25.989 19.937 -1.399  1.00 37.21 ? 69  GLU   A CB   1 
ATOM   388  C  CG   . GLU   A 1 69  ? 26.545 19.103 -0.259  1.00 39.69 ? 69  GLU   A CG   1 
ATOM   389  C  CD   . GLU   A 1 69  ? 26.753 19.835 1.056   1.00 43.20 ? 69  GLU   A CD   1 
ATOM   390  O  OE1  . GLU   A 1 69  ? 26.371 21.016 1.146   1.00 42.80 ? 69  GLU   A OE1  1 
ATOM   391  O  OE2  . GLU   A 1 69  ? 27.313 19.224 1.984   1.00 43.80 ? 69  GLU   A OE2  1 
ATOM   392  N  N    . THR   A 1 70  ? 28.685 20.035 -3.204  1.00 36.50 ? 70  THR   A N    1 
ATOM   393  C  CA   . THR   A 1 70  ? 30.043 19.493 -3.470  1.00 36.35 ? 70  THR   A CA   1 
ATOM   394  C  C    . THR   A 1 70  ? 31.092 20.556 -3.131  1.00 37.82 ? 70  THR   A C    1 
ATOM   395  O  O    . THR   A 1 70  ? 32.175 20.177 -2.657  1.00 39.94 ? 70  THR   A O    1 
ATOM   396  C  CB   . THR   A 1 70  ? 30.186 19.005 -4.919  1.00 35.99 ? 70  THR   A CB   1 
ATOM   397  O  OG1  . THR   A 1 70  ? 30.293 20.141 -5.776  1.00 36.53 ? 70  THR   A OG1  1 
ATOM   398  C  CG2  . THR   A 1 70  ? 29.038 18.123 -5.359  1.00 35.74 ? 70  THR   A CG2  1 
ATOM   399  N  N    . PHE   A 1 71  ? 30.777 21.830 -3.367  1.00 36.92 ? 71  PHE   A N    1 
ATOM   400  C  CA   . PHE   A 1 71  ? 31.736 22.927 -3.071  1.00 36.67 ? 71  PHE   A CA   1 
ATOM   401  C  C    . PHE   A 1 71  ? 31.724 23.241 -1.570  1.00 38.09 ? 71  PHE   A C    1 
ATOM   402  O  O    . PHE   A 1 71  ? 32.675 23.883 -1.094  1.00 38.32 ? 71  PHE   A O    1 
ATOM   403  C  CB   . PHE   A 1 71  ? 31.425 24.165 -3.914  1.00 36.00 ? 71  PHE   A CB   1 
ATOM   404  C  CG   . PHE   A 1 71  ? 31.318 23.917 -5.396  1.00 35.88 ? 71  PHE   A CG   1 
ATOM   405  C  CD1  . PHE   A 1 71  ? 30.240 23.229 -5.926  1.00 36.46 ? 71  PHE   A CD1  1 
ATOM   406  C  CD2  . PHE   A 1 71  ? 32.309 24.352 -6.261  1.00 36.30 ? 71  PHE   A CD2  1 
ATOM   407  C  CE1  . PHE   A 1 71  ? 30.145 22.996 -7.288  1.00 37.60 ? 71  PHE   A CE1  1 
ATOM   408  C  CE2  . PHE   A 1 71  ? 32.215 24.115 -7.623  1.00 37.25 ? 71  PHE   A CE2  1 
ATOM   409  C  CZ   . PHE   A 1 71  ? 31.134 23.438 -8.134  1.00 37.30 ? 71  PHE   A CZ   1 
ATOM   410  N  N    . GLU   A 1 72  ? 30.681 22.807 -0.858  1.00 38.81 ? 72  GLU   A N    1 
ATOM   411  C  CA   . GLU   A 1 72  ? 30.570 23.048 0.608   1.00 39.93 ? 72  GLU   A CA   1 
ATOM   412  C  C    . GLU   A 1 72  ? 30.973 24.492 0.927   1.00 39.06 ? 72  GLU   A C    1 
ATOM   413  O  O    . GLU   A 1 72  ? 31.932 24.679 1.697   1.00 39.62 ? 72  GLU   A O    1 
ATOM   414  C  CB   . GLU   A 1 72  ? 31.421 22.045 1.390   1.00 44.64 ? 72  GLU   A CB   1 
ATOM   415  C  CG   . GLU   A 1 72  ? 30.959 20.609 1.239   1.00 52.84 ? 72  GLU   A CG   1 
ATOM   416  C  CD   . GLU   A 1 72  ? 31.701 19.605 2.103   1.00 62.23 ? 72  GLU   A CD   1 
ATOM   417  O  OE1  . GLU   A 1 72  ? 31.042 18.919 2.908   1.00 66.16 ? 72  GLU   A OE1  1 
ATOM   418  O  OE2  . GLU   A 1 72  ? 32.936 19.515 1.972   1.00 63.49 ? 72  GLU   A OE2  1 
ATOM   419  N  N    . HIS   A 1 73  ? 30.261 25.468 0.355   1.00 37.10 ? 73  HIS   A N    1 
ATOM   420  C  CA   . HIS   A 1 73  ? 30.592 26.901 0.584   1.00 35.68 ? 73  HIS   A CA   1 
ATOM   421  C  C    . HIS   A 1 73  ? 30.268 27.267 2.036   1.00 36.30 ? 73  HIS   A C    1 
ATOM   422  O  O    . HIS   A 1 73  ? 29.227 26.835 2.567   1.00 35.88 ? 73  HIS   A O    1 
ATOM   423  C  CB   . HIS   A 1 73  ? 29.888 27.799 -0.440  1.00 34.13 ? 73  HIS   A CB   1 
ATOM   424  C  CG   . HIS   A 1 73  ? 30.334 29.222 -0.398  1.00 33.40 ? 73  HIS   A CG   1 
ATOM   425  N  ND1  . HIS   A 1 73  ? 29.989 30.090 0.614   1.00 33.61 ? 73  HIS   A ND1  1 
ATOM   426  C  CD2  . HIS   A 1 73  ? 31.076 29.931 -1.255  1.00 34.19 ? 73  HIS   A CD2  1 
ATOM   427  C  CE1  . HIS   A 1 73  ? 30.526 31.277 0.373   1.00 34.27 ? 73  HIS   A CE1  1 
ATOM   428  N  NE2  . HIS   A 1 73  ? 31.192 31.201 -0.756  1.00 35.17 ? 73  HIS   A NE2  1 
ATOM   429  N  N    . PRO   A 1 74  ? 31.130 28.060 2.705   1.00 36.89 ? 74  PRO   A N    1 
ATOM   430  C  CA   . PRO   A 1 74  ? 30.925 28.413 4.113   1.00 36.95 ? 74  PRO   A CA   1 
ATOM   431  C  C    . PRO   A 1 74  ? 29.666 29.257 4.348   1.00 37.83 ? 74  PRO   A C    1 
ATOM   432  O  O    . PRO   A 1 74  ? 29.163 29.236 5.453   1.00 38.26 ? 74  PRO   A O    1 
ATOM   433  C  CB   . PRO   A 1 74  ? 32.164 29.261 4.435   1.00 37.30 ? 74  PRO   A CB   1 
ATOM   434  C  CG   . PRO   A 1 74  ? 32.612 29.797 3.098   1.00 38.37 ? 74  PRO   A CG   1 
ATOM   435  C  CD   . PRO   A 1 74  ? 32.343 28.655 2.144   1.00 36.31 ? 74  PRO   A CD   1 
ATOM   436  N  N    . ASN   A 1 75  ? 29.182 29.955 3.318   1.00 36.52 ? 75  ASN   A N    1 
ATOM   437  C  CA   . ASN   A 1 75  ? 28.038 30.886 3.511   1.00 35.20 ? 75  ASN   A CA   1 
ATOM   438  C  C    . ASN   A 1 75  ? 26.751 30.303 2.915   1.00 34.28 ? 75  ASN   A C    1 
ATOM   439  O  O    . ASN   A 1 75  ? 25.829 31.087 2.638   1.00 33.91 ? 75  ASN   A O    1 
ATOM   440  C  CB   . ASN   A 1 75  ? 28.392 32.285 3.000   1.00 36.10 ? 75  ASN   A CB   1 
ATOM   441  C  CG   . ASN   A 1 75  ? 29.535 32.900 3.778   1.00 39.07 ? 75  ASN   A CG   1 
ATOM   442  O  OD1  . ASN   A 1 75  ? 30.571 33.238 3.211   1.00 42.18 ? 75  ASN   A OD1  1 
ATOM   443  N  ND2  . ASN   A 1 75  ? 29.359 33.037 5.081   1.00 35.82 ? 75  ASN   A ND2  1 
ATOM   444  N  N    . VAL   A 1 76  ? 26.691 28.984 2.733   1.00 33.24 ? 76  VAL   A N    1 
ATOM   445  C  CA   . VAL   A 1 76  ? 25.428 28.340 2.265   1.00 33.50 ? 76  VAL   A CA   1 
ATOM   446  C  C    . VAL   A 1 76  ? 25.126 27.157 3.191   1.00 33.89 ? 76  VAL   A C    1 
ATOM   447  O  O    . VAL   A 1 76  ? 26.073 26.461 3.585   1.00 33.93 ? 76  VAL   A O    1 
ATOM   448  C  CB   . VAL   A 1 76  ? 25.494 27.916 0.784   1.00 34.11 ? 76  VAL   A CB   1 
ATOM   449  C  CG1  . VAL   A 1 76  ? 25.562 29.121 -0.141  1.00 34.99 ? 76  VAL   A CG1  1 
ATOM   450  C  CG2  . VAL   A 1 76  ? 26.652 26.972 0.516   1.00 34.39 ? 76  VAL   A CG2  1 
ATOM   451  N  N    . VAL   A 1 77  ? 23.851 26.959 3.526   1.00 34.38 ? 77  VAL   A N    1 
ATOM   452  C  CA   . VAL   A 1 77  ? 23.453 25.857 4.450   1.00 34.66 ? 77  VAL   A CA   1 
ATOM   453  C  C    . VAL   A 1 77  ? 23.881 24.524 3.830   1.00 35.04 ? 77  VAL   A C    1 
ATOM   454  O  O    . VAL   A 1 77  ? 23.776 24.385 2.600   1.00 34.43 ? 77  VAL   A O    1 
ATOM   455  C  CB   . VAL   A 1 77  ? 21.945 25.897 4.762   1.00 35.41 ? 77  VAL   A CB   1 
ATOM   456  C  CG1  . VAL   A 1 77  ? 21.098 25.663 3.521   1.00 35.80 ? 77  VAL   A CG1  1 
ATOM   457  C  CG2  . VAL   A 1 77  ? 21.564 24.918 5.860   1.00 35.88 ? 77  VAL   A CG2  1 
ATOM   458  N  N    . ARG   A 1 78  ? 24.349 23.588 4.658   1.00 35.36 ? 78  ARG   A N    1 
ATOM   459  C  CA   . ARG   A 1 78  ? 24.833 22.276 4.161   1.00 36.71 ? 78  ARG   A CA   1 
ATOM   460  C  C    . ARG   A 1 78  ? 23.656 21.364 3.808   1.00 37.51 ? 78  ARG   A C    1 
ATOM   461  O  O    . ARG   A 1 78  ? 22.674 21.357 4.569   1.00 37.71 ? 78  ARG   A O    1 
ATOM   462  C  CB   . ARG   A 1 78  ? 25.695 21.591 5.227   1.00 38.86 ? 78  ARG   A CB   1 
ATOM   463  C  CG   . ARG   A 1 78  ? 27.068 22.210 5.442   1.00 42.43 ? 78  ARG   A CG   1 
ATOM   464  C  CD   . ARG   A 1 78  ? 28.071 21.816 4.375   1.00 45.97 ? 78  ARG   A CD   1 
ATOM   465  N  NE   . ARG   A 1 78  ? 27.900 22.561 3.138   1.00 48.52 ? 78  ARG   A NE   1 
ATOM   466  C  CZ   . ARG   A 1 78  ? 28.024 23.878 3.032   1.00 51.26 ? 78  ARG   A CZ   1 
ATOM   467  N  NH1  . ARG   A 1 78  ? 28.539 24.579 4.026   1.00 53.89 ? 78  ARG   A NH1  1 
ATOM   468  N  NH2  . ARG   A 1 78  ? 27.637 24.491 1.928   1.00 49.68 ? 78  ARG   A NH2  1 
ATOM   469  N  N    . LEU   A 1 79  ? 23.756 20.635 2.694   1.00 37.26 ? 79  LEU   A N    1 
ATOM   470  C  CA   . LEU   A 1 79  ? 22.716 19.632 2.347   1.00 38.35 ? 79  LEU   A CA   1 
ATOM   471  C  C    . LEU   A 1 79  ? 23.259 18.269 2.781   1.00 41.58 ? 79  LEU   A C    1 
ATOM   472  O  O    . LEU   A 1 79  ? 24.076 17.701 2.036   1.00 43.06 ? 79  LEU   A O    1 
ATOM   473  C  CB   . LEU   A 1 79  ? 22.429 19.679 0.843   1.00 37.05 ? 79  LEU   A CB   1 
ATOM   474  C  CG   . LEU   A 1 79  ? 21.462 18.615 0.326   1.00 37.44 ? 79  LEU   A CG   1 
ATOM   475  C  CD1  . LEU   A 1 79  ? 20.096 18.764 0.976   1.00 37.95 ? 79  LEU   A CD1  1 
ATOM   476  C  CD2  . LEU   A 1 79  ? 21.343 18.686 -1.188  1.00 38.29 ? 79  LEU   A CD2  1 
ATOM   477  N  N    . PHE   A 1 80  ? 22.840 17.782 3.950   1.00 42.53 ? 80  PHE   A N    1 
ATOM   478  C  CA   . PHE   A 1 80  ? 23.381 16.513 4.502   1.00 43.35 ? 80  PHE   A CA   1 
ATOM   479  C  C    . PHE   A 1 80  ? 22.856 15.307 3.720   1.00 47.03 ? 80  PHE   A C    1 
ATOM   480  O  O    . PHE   A 1 80  ? 23.636 14.363 3.509   1.00 48.49 ? 80  PHE   A O    1 
ATOM   481  C  CB   . PHE   A 1 80  ? 23.015 16.387 5.984   1.00 41.10 ? 80  PHE   A CB   1 
ATOM   482  C  CG   . PHE   A 1 80  ? 23.776 17.295 6.915   1.00 39.77 ? 80  PHE   A CG   1 
ATOM   483  C  CD1  . PHE   A 1 80  ? 24.902 17.976 6.484   1.00 39.77 ? 80  PHE   A CD1  1 
ATOM   484  C  CD2  . PHE   A 1 80  ? 23.346 17.491 8.217   1.00 39.72 ? 80  PHE   A CD2  1 
ATOM   485  C  CE1  . PHE   A 1 80  ? 25.596 18.812 7.344   1.00 39.88 ? 80  PHE   A CE1  1 
ATOM   486  C  CE2  . PHE   A 1 80  ? 24.038 18.330 9.074   1.00 39.86 ? 80  PHE   A CE2  1 
ATOM   487  C  CZ   . PHE   A 1 80  ? 25.162 18.989 8.636   1.00 39.42 ? 80  PHE   A CZ   1 
ATOM   488  N  N    . ASP   A 1 81  ? 21.586 15.327 3.313   1.00 48.59 ? 81  ASP   A N    1 
ATOM   489  C  CA   . ASP   A 1 81  ? 21.024 14.115 2.662   1.00 51.20 ? 81  ASP   A CA   1 
ATOM   490  C  C    . ASP   A 1 81  ? 19.848 14.451 1.742   1.00 53.30 ? 81  ASP   A C    1 
ATOM   491  O  O    . ASP   A 1 81  ? 19.225 15.507 1.943   1.00 52.49 ? 81  ASP   A O    1 
ATOM   492  C  CB   . ASP   A 1 81  ? 20.587 13.100 3.721   1.00 54.27 ? 81  ASP   A CB   1 
ATOM   493  C  CG   . ASP   A 1 81  ? 20.287 11.716 3.174   1.00 61.42 ? 81  ASP   A CG   1 
ATOM   494  O  OD1  . ASP   A 1 81  ? 20.482 11.507 1.961   1.00 62.16 ? 81  ASP   A OD1  1 
ATOM   495  O  OD2  . ASP   A 1 81  ? 19.854 10.859 3.968   1.00 64.71 ? 81  ASP   A OD2  1 
ATOM   496  N  N    . VAL   A 1 82  ? 19.572 13.582 0.767   1.00 56.11 ? 82  VAL   A N    1 
ATOM   497  C  CA   . VAL   A 1 82  ? 18.389 13.745 -0.129  1.00 59.37 ? 82  VAL   A CA   1 
ATOM   498  C  C    . VAL   A 1 82  ? 17.751 12.359 -0.242  1.00 63.34 ? 82  VAL   A C    1 
ATOM   499  O  O    . VAL   A 1 82  ? 18.432 11.448 -0.742  1.00 63.66 ? 82  VAL   A O    1 
ATOM   500  C  CB   . VAL   A 1 82  ? 18.781 14.307 -1.509  1.00 59.61 ? 82  VAL   A CB   1 
ATOM   501  C  CG1  . VAL   A 1 82  ? 17.629 14.233 -2.496  1.00 59.99 ? 82  VAL   A CG1  1 
ATOM   502  C  CG2  . VAL   A 1 82  ? 19.317 15.726 -1.412  1.00 59.84 ? 82  VAL   A CG2  1 
ATOM   503  N  N    . CYS   A 1 83  ? 16.508 12.196 0.218   1.00 66.15 ? 83  CYS   A N    1 
ATOM   504  C  CA   . CYS   A 1 83  ? 15.887 10.844 0.243   1.00 68.81 ? 83  CYS   A CA   1 
ATOM   505  C  C    . CYS   A 1 83  ? 14.626 10.801 -0.624  1.00 70.32 ? 83  CYS   A C    1 
ATOM   506  O  O    . CYS   A 1 83  ? 13.941 11.835 -0.720  1.00 70.12 ? 83  CYS   A O    1 
ATOM   507  C  CB   . CYS   A 1 83  ? 15.498 10.456 1.664   1.00 71.02 ? 83  CYS   A CB   1 
ATOM   508  S  SG   . CYS   A 1 83  ? 16.834 10.654 2.871   1.00 78.90 ? 83  CYS   A SG   1 
ATOM   509  N  N    . THR   A 1 84  ? 14.329 9.638  -1.210  1.00 71.55 ? 84  THR   A N    1 
ATOM   510  C  CA   . THR   A 1 84  ? 13.094 9.479  -2.022  1.00 72.98 ? 84  THR   A CA   1 
ATOM   511  C  C    . THR   A 1 84  ? 11.997 8.852  -1.155  1.00 73.29 ? 84  THR   A C    1 
ATOM   512  O  O    . THR   A 1 84  ? 12.348 7.964  -0.357  1.00 73.71 ? 84  THR   A O    1 
ATOM   513  C  CB   . THR   A 1 84  ? 13.361 8.644  -3.280  1.00 75.39 ? 84  THR   A CB   1 
ATOM   514  O  OG1  . THR   A 1 84  ? 12.101 8.341  -3.879  1.00 76.50 ? 84  THR   A OG1  1 
ATOM   515  C  CG2  . THR   A 1 84  ? 14.110 7.362  -2.991  1.00 76.27 ? 84  THR   A CG2  1 
ATOM   516  N  N    . LYS   A 1 93  ? 7.455  12.525 -0.935  1.00 67.54 ? 93  LYS   A N    1 
ATOM   517  C  CA   . LYS   A 1 93  ? 8.078  11.954 -2.158  1.00 67.76 ? 93  LYS   A CA   1 
ATOM   518  C  C    . LYS   A 1 93  ? 9.591  12.179 -2.092  1.00 66.84 ? 93  LYS   A C    1 
ATOM   519  O  O    . LYS   A 1 93  ? 10.341 11.208 -2.307  1.00 66.60 ? 93  LYS   A O    1 
ATOM   520  C  CB   . LYS   A 1 93  ? 7.463  12.593 -3.407  1.00 70.38 ? 93  LYS   A CB   1 
ATOM   521  C  CG   . LYS   A 1 93  ? 8.006  12.086 -4.736  1.00 75.65 ? 93  LYS   A CG   1 
ATOM   522  C  CD   . LYS   A 1 93  ? 7.809  10.599 -4.932  1.00 80.95 ? 93  LYS   A CD   1 
ATOM   523  C  CE   . LYS   A 1 93  ? 8.122  10.143 -6.341  1.00 85.10 ? 93  LYS   A CE   1 
ATOM   524  N  NZ   . LYS   A 1 93  ? 7.245  10.804 -7.337  1.00 86.62 ? 93  LYS   A NZ   1 
ATOM   525  N  N    . LEU   A 1 94  ? 10.014 13.412 -1.799  1.00 65.92 ? 94  LEU   A N    1 
ATOM   526  C  CA   . LEU   A 1 94  ? 11.463 13.716 -1.664  1.00 65.09 ? 94  LEU   A CA   1 
ATOM   527  C  C    . LEU   A 1 94  ? 11.698 14.412 -0.321  1.00 62.34 ? 94  LEU   A C    1 
ATOM   528  O  O    . LEU   A 1 94  ? 10.961 15.368 -0.019  1.00 62.59 ? 94  LEU   A O    1 
ATOM   529  C  CB   . LEU   A 1 94  ? 11.893 14.612 -2.830  1.00 66.23 ? 94  LEU   A CB   1 
ATOM   530  C  CG   . LEU   A 1 94  ? 13.345 14.468 -3.281  1.00 68.61 ? 94  LEU   A CG   1 
ATOM   531  C  CD1  . LEU   A 1 94  ? 13.667 15.469 -4.378  1.00 69.41 ? 94  LEU   A CD1  1 
ATOM   532  C  CD2  . LEU   A 1 94  ? 14.300 14.643 -2.112  1.00 69.53 ? 94  LEU   A CD2  1 
ATOM   533  N  N    . THR   A 1 95  ? 12.687 13.949 0.444   1.00 59.69 ? 95  THR   A N    1 
ATOM   534  C  CA   . THR   A 1 95  ? 13.020 14.606 1.735   1.00 57.90 ? 95  THR   A CA   1 
ATOM   535  C  C    . THR   A 1 95  ? 14.406 15.249 1.631   1.00 54.38 ? 95  THR   A C    1 
ATOM   536  O  O    . THR   A 1 95  ? 15.369 14.522 1.328   1.00 54.14 ? 95  THR   A O    1 
ATOM   537  C  CB   . THR   A 1 95  ? 12.925 13.619 2.904   1.00 60.27 ? 95  THR   A CB   1 
ATOM   538  O  OG1  . THR   A 1 95  ? 11.562 13.216 3.029   1.00 62.18 ? 95  THR   A OG1  1 
ATOM   539  C  CG2  . THR   A 1 95  ? 13.402 14.213 4.210   1.00 61.04 ? 95  THR   A CG2  1 
ATOM   540  N  N    . LEU   A 1 96  ? 14.489 16.560 1.863   1.00 51.24 ? 96  LEU   A N    1 
ATOM   541  C  CA   . LEU   A 1 96  ? 15.797 17.266 1.834   1.00 48.39 ? 96  LEU   A CA   1 
ATOM   542  C  C    . LEU   A 1 96  ? 16.273 17.490 3.272   1.00 45.41 ? 96  LEU   A C    1 
ATOM   543  O  O    . LEU   A 1 96  ? 15.588 18.211 4.013   1.00 44.53 ? 96  LEU   A O    1 
ATOM   544  C  CB   . LEU   A 1 96  ? 15.641 18.593 1.088   1.00 48.02 ? 96  LEU   A CB   1 
ATOM   545  C  CG   . LEU   A 1 96  ? 15.613 18.493 -0.436  1.00 49.16 ? 96  LEU   A CG   1 
ATOM   546  C  CD1  . LEU   A 1 96  ? 14.278 17.950 -0.922  1.00 50.01 ? 96  LEU   A CD1  1 
ATOM   547  C  CD2  . LEU   A 1 96  ? 15.899 19.844 -1.070  1.00 49.23 ? 96  LEU   A CD2  1 
ATOM   548  N  N    . VAL   A 1 97  ? 17.404 16.885 3.637   1.00 43.88 ? 97  VAL   A N    1 
ATOM   549  C  CA   . VAL   A 1 97  ? 17.955 17.031 5.017   1.00 43.16 ? 97  VAL   A CA   1 
ATOM   550  C  C    . VAL   A 1 97  ? 19.054 18.096 4.995   1.00 41.79 ? 97  VAL   A C    1 
ATOM   551  O  O    . VAL   A 1 97  ? 20.057 17.897 4.289   1.00 42.13 ? 97  VAL   A O    1 
ATOM   552  C  CB   . VAL   A 1 97  ? 18.474 15.690 5.567   1.00 43.89 ? 97  VAL   A CB   1 
ATOM   553  C  CG1  . VAL   A 1 97  ? 19.017 15.835 6.979   1.00 44.45 ? 97  VAL   A CG1  1 
ATOM   554  C  CG2  . VAL   A 1 97  ? 17.404 14.612 5.510   1.00 44.62 ? 97  VAL   A CG2  1 
ATOM   555  N  N    . PHE   A 1 98  ? 18.859 19.178 5.747   1.00 39.93 ? 98  PHE   A N    1 
ATOM   556  C  CA   . PHE   A 1 98  ? 19.842 20.286 5.788   1.00 38.93 ? 98  PHE   A CA   1 
ATOM   557  C  C    . PHE   A 1 98  ? 20.377 20.446 7.209   1.00 39.10 ? 98  PHE   A C    1 
ATOM   558  O  O    . PHE   A 1 98  ? 19.736 19.944 8.147   1.00 39.06 ? 98  PHE   A O    1 
ATOM   559  C  CB   . PHE   A 1 98  ? 19.171 21.602 5.400   1.00 38.39 ? 98  PHE   A CB   1 
ATOM   560  C  CG   . PHE   A 1 98  ? 18.740 21.725 3.961   1.00 38.55 ? 98  PHE   A CG   1 
ATOM   561  C  CD1  . PHE   A 1 98  ? 19.671 21.914 2.953   1.00 39.36 ? 98  PHE   A CD1  1 
ATOM   562  C  CD2  . PHE   A 1 98  ? 17.401 21.646 3.615   1.00 39.39 ? 98  PHE   A CD2  1 
ATOM   563  C  CE1  . PHE   A 1 98  ? 19.270 22.034 1.632   1.00 40.11 ? 98  PHE   A CE1  1 
ATOM   564  C  CE2  . PHE   A 1 98  ? 17.002 21.760 2.293   1.00 40.22 ? 98  PHE   A CE2  1 
ATOM   565  C  CZ   . PHE   A 1 98  ? 17.937 21.953 1.305   1.00 40.02 ? 98  PHE   A CZ   1 
ATOM   566  N  N    . GLU   A 1 99  ? 21.498 21.138 7.366   1.00 38.59 ? 99  GLU   A N    1 
ATOM   567  C  CA   . GLU   A 1 99  ? 22.001 21.443 8.723   1.00 38.12 ? 99  GLU   A CA   1 
ATOM   568  C  C    . GLU   A 1 99  ? 20.998 22.385 9.387   1.00 37.95 ? 99  GLU   A C    1 
ATOM   569  O  O    . GLU   A 1 99  ? 20.422 23.209 8.692   1.00 37.95 ? 99  GLU   A O    1 
ATOM   570  C  CB   . GLU   A 1 99  ? 23.398 22.058 8.683   1.00 39.04 ? 99  GLU   A CB   1 
ATOM   571  C  CG   . GLU   A 1 99  ? 23.460 23.452 8.107   1.00 43.41 ? 99  GLU   A CG   1 
ATOM   572  C  CD   . GLU   A 1 99  ? 24.834 24.092 8.158   1.00 46.44 ? 99  GLU   A CD   1 
ATOM   573  O  OE1  . GLU   A 1 99  ? 25.334 24.497 7.100   1.00 43.08 ? 99  GLU   A OE1  1 
ATOM   574  O  OE2  . GLU   A 1 99  ? 25.398 24.177 9.259   1.00 47.83 ? 99  GLU   A OE2  1 
ATOM   575  N  N    . HIS   A 1 100 ? 20.810 22.244 10.689  1.00 37.15 ? 100 HIS   A N    1 
ATOM   576  C  CA   . HIS   A 1 100 ? 19.914 23.161 11.423  1.00 37.76 ? 100 HIS   A CA   1 
ATOM   577  C  C    . HIS   A 1 100 ? 20.708 24.343 11.974  1.00 38.38 ? 100 HIS   A C    1 
ATOM   578  O  O    . HIS   A 1 100 ? 21.763 24.133 12.578  1.00 39.62 ? 100 HIS   A O    1 
ATOM   579  C  CB   . HIS   A 1 100 ? 19.151 22.409 12.516  1.00 38.51 ? 100 HIS   A CB   1 
ATOM   580  C  CG   . HIS   A 1 100 ? 18.233 23.281 13.300  1.00 39.54 ? 100 HIS   A CG   1 
ATOM   581  N  ND1  . HIS   A 1 100 ? 18.664 24.129 14.294  1.00 40.59 ? 100 HIS   A ND1  1 
ATOM   582  C  CD2  . HIS   A 1 100 ? 16.911 23.415 13.247  1.00 40.17 ? 100 HIS   A CD2  1 
ATOM   583  C  CE1  . HIS   A 1 100 ? 17.626 24.764 14.803  1.00 41.06 ? 100 HIS   A CE1  1 
ATOM   584  N  NE2  . HIS   A 1 100 ? 16.554 24.342 14.182  1.00 41.51 ? 100 HIS   A NE2  1 
ATOM   585  N  N    . VAL   A 1 101 ? 20.226 25.553 11.730  1.00 36.80 ? 101 VAL   A N    1 
ATOM   586  C  CA   . VAL   A 1 101 ? 20.843 26.767 12.320  1.00 36.51 ? 101 VAL   A CA   1 
ATOM   587  C  C    . VAL   A 1 101 ? 19.762 27.342 13.235  1.00 37.69 ? 101 VAL   A C    1 
ATOM   588  O  O    . VAL   A 1 101 ? 18.610 27.418 12.807  1.00 37.05 ? 101 VAL   A O    1 
ATOM   589  C  CB   . VAL   A 1 101 ? 21.352 27.768 11.270  1.00 36.03 ? 101 VAL   A CB   1 
ATOM   590  C  CG1  . VAL   A 1 101 ? 21.911 29.026 11.906  1.00 35.40 ? 101 VAL   A CG1  1 
ATOM   591  C  CG2  . VAL   A 1 101 ? 22.355 27.140 10.318  1.00 36.01 ? 101 VAL   A CG2  1 
ATOM   592  N  N    . ASP   A 1 102 ? 20.126 27.691 14.460  1.00 38.58 ? 102 ASP   A N    1 
ATOM   593  C  CA   . ASP   A 1 102 ? 19.130 28.112 15.476  1.00 40.44 ? 102 ASP   A CA   1 
ATOM   594  C  C    . ASP   A 1 102 ? 18.422 29.426 15.134  1.00 40.52 ? 102 ASP   A C    1 
ATOM   595  O  O    . ASP   A 1 102 ? 17.243 29.527 15.457  1.00 41.13 ? 102 ASP   A O    1 
ATOM   596  C  CB   . ASP   A 1 102 ? 19.793 28.176 16.857  1.00 45.14 ? 102 ASP   A CB   1 
ATOM   597  C  CG   . ASP   A 1 102 ? 20.074 26.826 17.485  1.00 52.72 ? 102 ASP   A CG   1 
ATOM   598  O  OD1  . ASP   A 1 102 ? 19.153 25.996 17.522  1.00 54.58 ? 102 ASP   A OD1  1 
ATOM   599  O  OD2  . ASP   A 1 102 ? 21.198 26.639 17.974  1.00 56.53 ? 102 ASP   A OD2  1 
ATOM   600  N  N    . GLN   A 1 103 ? 19.110 30.384 14.525  1.00 40.24 ? 103 GLN   A N    1 
ATOM   601  C  CA   . GLN   A 1 103 ? 18.465 31.702 14.322  1.00 41.64 ? 103 GLN   A CA   1 
ATOM   602  C  C    . GLN   A 1 103 ? 18.578 32.263 12.899  1.00 41.59 ? 103 GLN   A C    1 
ATOM   603  O  O    . GLN   A 1 103 ? 19.513 31.899 12.188  1.00 40.99 ? 103 GLN   A O    1 
ATOM   604  C  CB   . GLN   A 1 103 ? 19.001 32.706 15.348  1.00 44.79 ? 103 GLN   A CB   1 
ATOM   605  C  CG   . GLN   A 1 103 ? 20.263 33.448 14.955  1.00 52.06 ? 103 GLN   A CG   1 
ATOM   606  C  CD   . GLN   A 1 103 ? 20.804 34.201 16.146  1.00 61.62 ? 103 GLN   A CD   1 
ATOM   607  O  OE1  . GLN   A 1 103 ? 20.119 35.025 16.748  1.00 63.80 ? 103 GLN   A OE1  1 
ATOM   608  N  NE2  . GLN   A 1 103 ? 22.038 33.900 16.513  1.00 64.32 ? 103 GLN   A NE2  1 
ATOM   609  N  N    . ASP   A 1 104 ? 17.635 33.131 12.540  1.00 42.25 ? 104 ASP   A N    1 
ATOM   610  C  CA   . ASP   A 1 104 ? 17.653 33.841 11.243  1.00 43.73 ? 104 ASP   A CA   1 
ATOM   611  C  C    . ASP   A 1 104 ? 18.095 35.273 11.536  1.00 45.76 ? 104 ASP   A C    1 
ATOM   612  O  O    . ASP   A 1 104 ? 18.252 35.605 12.709  1.00 46.78 ? 104 ASP   A O    1 
ATOM   613  C  CB   . ASP   A 1 104 ? 16.280 33.742 10.579  1.00 45.12 ? 104 ASP   A CB   1 
ATOM   614  C  CG   . ASP   A 1 104 ? 15.110 34.268 11.389  1.00 49.91 ? 104 ASP   A CG   1 
ATOM   615  O  OD1  . ASP   A 1 104 ? 15.346 34.951 12.389  1.00 51.10 ? 104 ASP   A OD1  1 
ATOM   616  O  OD2  . ASP   A 1 104 ? 13.971 33.959 11.017  1.00 52.28 ? 104 ASP   A OD2  1 
ATOM   617  N  N    . LEU   A 1 105 ? 18.299 36.078 10.507  1.00 46.35 ? 105 LEU   A N    1 
ATOM   618  C  CA   . LEU   A 1 105 ? 18.760 37.476 10.710  1.00 47.18 ? 105 LEU   A CA   1 
ATOM   619  C  C    . LEU   A 1 105 ? 17.682 38.261 11.467  1.00 48.48 ? 105 LEU   A C    1 
ATOM   620  O  O    . LEU   A 1 105 ? 18.051 39.147 12.251  1.00 48.03 ? 105 LEU   A O    1 
ATOM   621  C  CB   . LEU   A 1 105 ? 19.064 38.100 9.345   1.00 46.94 ? 105 LEU   A CB   1 
ATOM   622  C  CG   . LEU   A 1 105 ? 19.715 39.480 9.383   1.00 47.61 ? 105 LEU   A CG   1 
ATOM   623  C  CD1  . LEU   A 1 105 ? 21.117 39.399 9.966   1.00 47.59 ? 105 LEU   A CD1  1 
ATOM   624  C  CD2  . LEU   A 1 105 ? 19.752 40.093 7.992   1.00 47.11 ? 105 LEU   A CD2  1 
ATOM   625  N  N    . THR   A 1 106 ? 16.406 37.937 11.242  1.00 49.81 ? 106 THR   A N    1 
ATOM   626  C  CA   . THR   A 1 106 ? 15.283 38.655 11.902  1.00 50.99 ? 106 THR   A CA   1 
ATOM   627  C  C    . THR   A 1 106 ? 15.376 38.484 13.420  1.00 51.31 ? 106 THR   A C    1 
ATOM   628  O  O    . THR   A 1 106 ? 15.322 39.502 14.130  1.00 51.19 ? 106 THR   A O    1 
ATOM   629  C  CB   . THR   A 1 106 ? 13.929 38.140 11.399  1.00 52.83 ? 106 THR   A CB   1 
ATOM   630  O  OG1  . THR   A 1 106 ? 13.872 38.324 9.984   1.00 54.62 ? 106 THR   A OG1  1 
ATOM   631  C  CG2  . THR   A 1 106 ? 12.756 38.834 12.054  1.00 53.51 ? 106 THR   A CG2  1 
ATOM   632  N  N    . THR   A 1 107 ? 15.507 37.241 13.886  1.00 51.65 ? 107 THR   A N    1 
ATOM   633  C  CA   . THR   A 1 107 ? 15.577 36.965 15.345  1.00 52.35 ? 107 THR   A CA   1 
ATOM   634  C  C    . THR   A 1 107 ? 16.864 37.574 15.907  1.00 51.98 ? 107 THR   A C    1 
ATOM   635  O  O    . THR   A 1 107 ? 16.847 38.002 17.074  1.00 52.30 ? 107 THR   A O    1 
ATOM   636  C  CB   . THR   A 1 107 ? 15.447 35.464 15.623  1.00 55.30 ? 107 THR   A CB   1 
ATOM   637  O  OG1  . THR   A 1 107 ? 16.455 34.793 14.869  1.00 58.98 ? 107 THR   A OG1  1 
ATOM   638  C  CG2  . THR   A 1 107 ? 14.086 34.915 15.257  1.00 55.61 ? 107 THR   A CG2  1 
ATOM   639  N  N    . TYR   A 1 108 ? 17.931 37.611 15.107  1.00 51.18 ? 108 TYR   A N    1 
ATOM   640  C  CA   . TYR   A 1 108 ? 19.194 38.251 15.552  1.00 51.36 ? 108 TYR   A CA   1 
ATOM   641  C  C    . TYR   A 1 108 ? 18.975 39.758 15.695  1.00 51.29 ? 108 TYR   A C    1 
ATOM   642  O  O    . TYR   A 1 108 ? 19.450 40.347 16.682  1.00 51.54 ? 108 TYR   A O    1 
ATOM   643  C  CB   . TYR   A 1 108 ? 20.325 37.975 14.560  1.00 51.39 ? 108 TYR   A CB   1 
ATOM   644  C  CG   . TYR   A 1 108 ? 21.570 38.785 14.816  1.00 52.45 ? 108 TYR   A CG   1 
ATOM   645  C  CD1  . TYR   A 1 108 ? 22.358 38.550 15.928  1.00 53.89 ? 108 TYR   A CD1  1 
ATOM   646  C  CD2  . TYR   A 1 108 ? 21.935 39.819 13.971  1.00 53.51 ? 108 TYR   A CD2  1 
ATOM   647  C  CE1  . TYR   A 1 108 ? 23.496 39.298 16.178  1.00 55.16 ? 108 TYR   A CE1  1 
ATOM   648  C  CE2  . TYR   A 1 108 ? 23.066 40.580 14.208  1.00 54.81 ? 108 TYR   A CE2  1 
ATOM   649  C  CZ   . TYR   A 1 108 ? 23.851 40.318 15.316  1.00 56.31 ? 108 TYR   A CZ   1 
ATOM   650  O  OH   . TYR   A 1 108 ? 24.976 41.066 15.559  1.00 58.62 ? 108 TYR   A OH   1 
ATOM   651  N  N    . LEU   A 1 109 ? 18.276 40.359 14.732  1.00 50.78 ? 109 LEU   A N    1 
ATOM   652  C  CA   . LEU   A 1 109 ? 18.036 41.825 14.755  1.00 51.41 ? 109 LEU   A CA   1 
ATOM   653  C  C    . LEU   A 1 109 ? 17.023 42.166 15.853  1.00 53.39 ? 109 LEU   A C    1 
ATOM   654  O  O    . LEU   A 1 109 ? 17.102 43.280 16.396  1.00 53.53 ? 109 LEU   A O    1 
ATOM   655  C  CB   . LEU   A 1 109 ? 17.530 42.259 13.376  1.00 50.28 ? 109 LEU   A CB   1 
ATOM   656  C  CG   . LEU   A 1 109 ? 18.536 42.124 12.234  1.00 50.10 ? 109 LEU   A CG   1 
ATOM   657  C  CD1  . LEU   A 1 109 ? 18.026 42.810 10.976  1.00 49.47 ? 109 LEU   A CD1  1 
ATOM   658  C  CD2  . LEU   A 1 109 ? 19.890 42.685 12.635  1.00 50.26 ? 109 LEU   A CD2  1 
ATOM   659  N  N    . ASP   A 1 110 ? 16.108 41.243 16.160  1.00 54.77 ? 110 ASP   A N    1 
ATOM   660  C  CA   . ASP   A 1 110 ? 15.134 41.481 17.222  1.00 56.42 ? 110 ASP   A CA   1 
ATOM   661  C  C    . ASP   A 1 110 ? 15.852 41.516 18.565  1.00 58.15 ? 110 ASP   A C    1 
ATOM   662  O  O    . ASP   A 1 110 ? 15.617 42.420 19.354  1.00 58.25 ? 110 ASP   A O    1 
ATOM   663  C  CB   . ASP   A 1 110 ? 14.076 40.354 17.276  1.00 58.10 ? 110 ASP   A CB   1 
ATOM   664  C  CG   . ASP   A 1 110 ? 12.988 40.395 16.224  1.00 62.62 ? 110 ASP   A CG   1 
ATOM   665  O  OD1  . ASP   A 1 110 ? 12.687 41.499 15.723  1.00 63.31 ? 110 ASP   A OD1  1 
ATOM   666  O  OD2  . ASP   A 1 110 ? 12.427 39.321 15.912  1.00 64.75 ? 110 ASP   A OD2  1 
ATOM   667  N  N    . LYS   A 1 111 ? 16.737 40.546 18.823  1.00 59.30 ? 111 LYS   A N    1 
ATOM   668  C  CA   . LYS   A 1 111 ? 17.380 40.424 20.123  1.00 61.20 ? 111 LYS   A CA   1 
ATOM   669  C  C    . LYS   A 1 111 ? 18.656 41.239 20.319  1.00 62.60 ? 111 LYS   A C    1 
ATOM   670  O  O    . LYS   A 1 111 ? 19.153 41.275 21.441  1.00 62.91 ? 111 LYS   A O    1 
ATOM   671  C  CB   . LYS   A 1 111 ? 17.652 38.951 20.435  1.00 63.76 ? 111 LYS   A CB   1 
ATOM   672  C  CG   . LYS   A 1 111 ? 16.395 38.086 20.359  1.00 69.30 ? 111 LYS   A CG   1 
ATOM   673  C  CD   . LYS   A 1 111 ? 16.697 36.629 20.684  1.00 74.33 ? 111 LYS   A CD   1 
ATOM   674  C  CE   . LYS   A 1 111 ? 15.440 35.806 20.681  1.00 78.32 ? 111 LYS   A CE   1 
ATOM   675  N  NZ   . LYS   A 1 111 ? 15.724 34.363 20.895  1.00 80.95 ? 111 LYS   A NZ   1 
ATOM   676  N  N    . VAL   A 1 112 ? 19.205 41.863 19.261  1.00 63.13 ? 112 VAL   A N    1 
ATOM   677  C  CA   . VAL   A 1 112 ? 20.438 42.639 19.414  1.00 64.15 ? 112 VAL   A CA   1 
ATOM   678  C  C    . VAL   A 1 112 ? 20.203 43.877 20.329  1.00 65.18 ? 112 VAL   A C    1 
ATOM   679  O  O    . VAL   A 1 112 ? 19.206 44.596 20.154  1.00 65.69 ? 112 VAL   A O    1 
ATOM   680  C  CB   . VAL   A 1 112 ? 21.087 42.975 18.039  1.00 64.72 ? 112 VAL   A CB   1 
ATOM   681  C  CG1  . VAL   A 1 112 ? 20.402 44.157 17.368  1.00 65.07 ? 112 VAL   A CG1  1 
ATOM   682  C  CG2  . VAL   A 1 112 ? 22.588 43.214 18.176  1.00 65.07 ? 112 VAL   A CG2  1 
ATOM   683  N  N    . PRO   A 1 113 ? 21.051 44.094 21.366  1.00 65.32 ? 113 PRO   A N    1 
ATOM   684  C  CA   . PRO   A 1 113 ? 20.814 45.224 22.287  1.00 66.14 ? 113 PRO   A CA   1 
ATOM   685  C  C    . PRO   A 1 113 ? 21.029 46.621 21.691  1.00 67.42 ? 113 PRO   A C    1 
ATOM   686  O  O    . PRO   A 1 113 ? 21.657 46.770 20.636  1.00 67.58 ? 113 PRO   A O    1 
ATOM   687  C  CB   . PRO   A 1 113 ? 21.792 44.957 23.450  1.00 66.50 ? 113 PRO   A CB   1 
ATOM   688  C  CG   . PRO   A 1 113 ? 22.271 43.548 23.262  1.00 66.60 ? 113 PRO   A CG   1 
ATOM   689  C  CD   . PRO   A 1 113 ? 22.222 43.305 21.784  1.00 64.89 ? 113 PRO   A CD   1 
ATOM   690  N  N    . GLU   A 1 114 ? 20.512 47.655 22.373  1.00 67.68 ? 114 GLU   A N    1 
ATOM   691  C  CA   . GLU   A 1 114 ? 20.693 49.036 21.918  1.00 68.39 ? 114 GLU   A CA   1 
ATOM   692  C  C    . GLU   A 1 114 ? 22.171 49.463 22.041  1.00 67.99 ? 114 GLU   A C    1 
ATOM   693  O  O    . GLU   A 1 114 ? 22.902 48.941 22.898  1.00 68.39 ? 114 GLU   A O    1 
ATOM   694  C  CB   . GLU   A 1 114 ? 19.801 49.990 22.729  1.00 71.74 ? 114 GLU   A CB   1 
ATOM   695  C  CG   . GLU   A 1 114 ? 18.318 49.728 22.558  1.00 77.41 ? 114 GLU   A CG   1 
ATOM   696  C  CD   . GLU   A 1 114 ? 17.840 49.797 21.122  1.00 82.81 ? 114 GLU   A CD   1 
ATOM   697  O  OE1  . GLU   A 1 114 ? 18.232 50.747 20.404  1.00 83.16 ? 114 GLU   A OE1  1 
ATOM   698  O  OE2  . GLU   A 1 114 ? 17.079 48.890 20.713  1.00 84.08 ? 114 GLU   A OE2  1 
ATOM   699  N  N    . PRO   A 1 115 ? 22.651 50.371 21.165  1.00 66.64 ? 115 PRO   A N    1 
ATOM   700  C  CA   . PRO   A 1 115 ? 21.923 51.078 20.100  1.00 65.76 ? 115 PRO   A CA   1 
ATOM   701  C  C    . PRO   A 1 115 ? 21.881 50.339 18.754  1.00 64.87 ? 115 PRO   A C    1 
ATOM   702  O  O    . PRO   A 1 115 ? 21.735 50.972 17.704  1.00 65.18 ? 115 PRO   A O    1 
ATOM   703  C  CB   . PRO   A 1 115 ? 22.681 52.406 20.016  1.00 66.41 ? 115 PRO   A CB   1 
ATOM   704  C  CG   . PRO   A 1 115 ? 24.124 52.002 20.283  1.00 67.01 ? 115 PRO   A CG   1 
ATOM   705  C  CD   . PRO   A 1 115 ? 24.062 50.802 21.223  1.00 65.86 ? 115 PRO   A CD   1 
ATOM   706  N  N    . GLY   A 1 116 ? 21.989 49.015 18.789  1.00 63.38 ? 116 GLY   A N    1 
ATOM   707  C  CA   . GLY   A 1 116 ? 21.917 48.222 17.569  1.00 62.53 ? 116 GLY   A CA   1 
ATOM   708  C  C    . GLY   A 1 116 ? 23.159 47.420 17.248  1.00 60.85 ? 116 GLY   A C    1 
ATOM   709  O  O    . GLY   A 1 116 ? 24.081 47.332 18.060  1.00 60.83 ? 116 GLY   A O    1 
ATOM   710  N  N    . VAL   A 1 117 ? 23.178 46.830 16.040  1.00 59.20 ? 117 VAL   A N    1 
ATOM   711  C  CA   . VAL   A 1 117 ? 24.280 46.008 15.536  1.00 57.66 ? 117 VAL   A CA   1 
ATOM   712  C  C    . VAL   A 1 117 ? 25.553 46.842 15.406  1.00 56.36 ? 117 VAL   A C    1 
ATOM   713  O  O    . VAL   A 1 117 ? 25.544 47.905 14.779  1.00 56.38 ? 117 VAL   A O    1 
ATOM   714  C  CB   . VAL   A 1 117 ? 23.912 45.361 14.164  1.00 57.73 ? 117 VAL   A CB   1 
ATOM   715  C  CG1  . VAL   A 1 117 ? 24.939 44.321 13.750  1.00 57.51 ? 117 VAL   A CG1  1 
ATOM   716  C  CG2  . VAL   A 1 117 ? 22.518 44.740 14.196  1.00 58.17 ? 117 VAL   A CG2  1 
ATOM   717  N  N    . PRO   A 1 118 ? 26.671 46.366 15.965  1.00 55.45 ? 118 PRO   A N    1 
ATOM   718  C  CA   . PRO   A 1 118 ? 27.936 47.100 15.802  1.00 55.42 ? 118 PRO   A CA   1 
ATOM   719  C  C    . PRO   A 1 118 ? 28.329 47.218 14.333  1.00 55.80 ? 118 PRO   A C    1 
ATOM   720  O  O    . PRO   A 1 118 ? 28.132 46.287 13.556  1.00 55.37 ? 118 PRO   A O    1 
ATOM   721  C  CB   . PRO   A 1 118 ? 28.954 46.244 16.567  1.00 56.01 ? 118 PRO   A CB   1 
ATOM   722  C  CG   . PRO   A 1 118 ? 28.136 45.367 17.471  1.00 56.52 ? 118 PRO   A CG   1 
ATOM   723  C  CD   . PRO   A 1 118 ? 26.854 45.120 16.730  1.00 55.01 ? 118 PRO   A CD   1 
ATOM   724  N  N    . THR   A 1 119 ? 28.868 48.373 13.962  1.00 56.42 ? 119 THR   A N    1 
ATOM   725  C  CA   . THR   A 1 119 ? 29.318 48.715 12.611  1.00 57.40 ? 119 THR   A CA   1 
ATOM   726  C  C    . THR   A 1 119 ? 30.125 47.596 11.929  1.00 57.21 ? 119 THR   A C    1 
ATOM   727  O  O    . THR   A 1 119 ? 29.932 47.326 10.746  1.00 57.83 ? 119 THR   A O    1 
ATOM   728  C  CB   . THR   A 1 119 ? 30.109 50.050 12.677  1.00 59.79 ? 119 THR   A CB   1 
ATOM   729  O  OG1  . THR   A 1 119 ? 30.688 50.360 11.410  1.00 61.54 ? 119 THR   A OG1  1 
ATOM   730  C  CG2  . THR   A 1 119 ? 31.215 50.027 13.722  1.00 60.33 ? 119 THR   A CG2  1 
ATOM   731  N  N    . GLU   A 1 120 ? 31.018 46.949 12.673  1.00 56.32 ? 120 GLU   A N    1 
ATOM   732  C  CA   . GLU   A 1 120 ? 31.876 45.916 12.115  1.00 55.81 ? 120 GLU   A CA   1 
ATOM   733  C  C    . GLU   A 1 120 ? 31.204 44.548 12.006  1.00 54.43 ? 120 GLU   A C    1 
ATOM   734  O  O    . GLU   A 1 120 ? 31.668 43.709 11.229  1.00 53.85 ? 120 GLU   A O    1 
ATOM   735  C  CB   . GLU   A 1 120 ? 33.199 45.862 12.881  1.00 57.85 ? 120 GLU   A CB   1 
ATOM   736  C  CG   . GLU   A 1 120 ? 33.976 47.155 12.702  1.00 63.72 ? 120 GLU   A CG   1 
ATOM   737  C  CD   . GLU   A 1 120 ? 34.264 47.538 11.259  1.00 73.45 ? 120 GLU   A CD   1 
ATOM   738  O  OE1  . GLU   A 1 120 ? 35.057 46.823 10.600  1.00 75.38 ? 120 GLU   A OE1  1 
ATOM   739  O  OE2  . GLU   A 1 120 ? 33.676 48.538 10.781  1.00 76.45 ? 120 GLU   A OE2  1 
ATOM   740  N  N    . THR   A 1 121 ? 30.122 44.327 12.779  1.00 53.20 ? 121 THR   A N    1 
ATOM   741  C  CA   . THR   A 1 121 ? 29.312 43.128 12.703  1.00 52.37 ? 121 THR   A CA   1 
ATOM   742  C  C    . THR   A 1 121 ? 28.434 43.245 11.454  1.00 51.88 ? 121 THR   A C    1 
ATOM   743  O  O    . THR   A 1 121 ? 28.299 42.266 10.716  1.00 51.83 ? 121 THR   A O    1 
ATOM   744  C  CB   . THR   A 1 121 ? 28.514 42.952 13.973  1.00 53.79 ? 121 THR   A CB   1 
ATOM   745  O  OG1  . THR   A 1 121 ? 29.426 42.739 15.053  1.00 55.98 ? 121 THR   A OG1  1 
ATOM   746  C  CG2  . THR   A 1 121 ? 27.566 41.790 13.890  1.00 53.64 ? 121 THR   A CG2  1 
ATOM   747  N  N    . ILE   A 1 122 ? 27.892 44.468 11.168  1.00 51.27 ? 122 ILE   A N    1 
ATOM   748  C  CA   . ILE   A 1 122 ? 27.108 44.765 9.965   1.00 51.07 ? 122 ILE   A CA   1 
ATOM   749  C  C    . ILE   A 1 122 ? 28.002 44.501 8.758   1.00 51.67 ? 122 ILE   A C    1 
ATOM   750  O  O    . ILE   A 1 122 ? 27.600 43.769 7.859   1.00 52.57 ? 122 ILE   A O    1 
ATOM   751  C  CB   . ILE   A 1 122 ? 26.580 46.233 9.954   1.00 50.82 ? 122 ILE   A CB   1 
ATOM   752  C  CG1  . ILE   A 1 122 ? 25.486 46.458 11.012  1.00 51.18 ? 122 ILE   A CG1  1 
ATOM   753  C  CG2  . ILE   A 1 122 ? 26.068 46.627 8.550   1.00 51.17 ? 122 ILE   A CG2  1 
ATOM   754  C  CD1  . ILE   A 1 122 ? 24.926 47.903 11.111  1.00 51.89 ? 122 ILE   A CD1  1 
ATOM   755  N  N    . LYS   A 1 123 ? 29.240 45.033 8.784   1.00 51.14 ? 123 LYS   A N    1 
ATOM   756  C  CA   . LYS   A 1 123 ? 30.208 44.856 7.707   1.00 51.39 ? 123 LYS   A CA   1 
ATOM   757  C  C    . LYS   A 1 123 ? 30.522 43.396 7.420   1.00 49.96 ? 123 LYS   A C    1 
ATOM   758  O  O    . LYS   A 1 123 ? 30.431 42.969 6.268   1.00 49.83 ? 123 LYS   A O    1 
ATOM   759  C  CB   . LYS   A 1 123 ? 31.501 45.640 7.979   1.00 54.63 ? 123 LYS   A CB   1 
ATOM   760  C  CG   . LYS   A 1 123 ? 32.359 45.747 6.733   1.00 61.31 ? 123 LYS   A CG   1 
ATOM   761  C  CD   . LYS   A 1 123 ? 33.821 45.995 7.045   1.00 68.41 ? 123 LYS   A CD   1 
ATOM   762  C  CE   . LYS   A 1 123 ? 34.102 47.424 7.414   1.00 74.54 ? 123 LYS   A CE   1 
ATOM   763  N  NZ   . LYS   A 1 123 ? 35.564 47.707 7.356   1.00 78.47 ? 123 LYS   A NZ   1 
ATOM   764  N  N    . ASP   A 1 124 ? 30.859 42.627 8.456   1.00 48.62 ? 124 ASP   A N    1 
ATOM   765  C  CA   . ASP   A 1 124 ? 31.240 41.202 8.265   1.00 47.93 ? 124 ASP   A CA   1 
ATOM   766  C  C    . ASP   A 1 124 ? 30.056 40.403 7.711   1.00 46.93 ? 124 ASP   A C    1 
ATOM   767  O  O    . ASP   A 1 124 ? 30.271 39.604 6.781   1.00 47.58 ? 124 ASP   A O    1 
ATOM   768  C  CB   . ASP   A 1 124 ? 31.753 40.582 9.566   1.00 49.88 ? 124 ASP   A CB   1 
ATOM   769  C  CG   . ASP   A 1 124 ? 32.159 39.126 9.420   1.00 56.48 ? 124 ASP   A CG   1 
ATOM   770  O  OD1  . ASP   A 1 124 ? 33.076 38.853 8.624   1.00 57.94 ? 124 ASP   A OD1  1 
ATOM   771  O  OD2  . ASP   A 1 124 ? 31.552 38.279 10.102  1.00 59.53 ? 124 ASP   A OD2  1 
ATOM   772  N  N    . MET   A 1 125 ? 28.863 40.599 8.269   1.00 45.13 ? 125 MET   A N    1 
ATOM   773  C  CA   . MET   A 1 125 ? 27.679 39.805 7.846   1.00 44.06 ? 125 MET   A CA   1 
ATOM   774  C  C    . MET   A 1 125 ? 27.337 40.119 6.386   1.00 42.56 ? 125 MET   A C    1 
ATOM   775  O  O    . MET   A 1 125 ? 26.876 39.207 5.680   1.00 41.83 ? 125 MET   A O    1 
ATOM   776  C  CB   . MET   A 1 125 ? 26.477 40.126 8.736   1.00 44.54 ? 125 MET   A CB   1 
ATOM   777  C  CG   . MET   A 1 125 ? 26.411 39.264 9.979   1.00 46.54 ? 125 MET   A CG   1 
ATOM   778  S  SD   . MET   A 1 125 ? 25.078 39.743 11.101  1.00 48.46 ? 125 MET   A SD   1 
ATOM   779  C  CE   . MET   A 1 125 ? 25.638 38.965 12.615  1.00 49.20 ? 125 MET   A CE   1 
ATOM   780  N  N    . MET   A 1 126 ? 27.547 41.366 5.968   1.00 41.72 ? 126 MET   A N    1 
ATOM   781  C  CA   . MET   A 1 126 ? 27.250 41.778 4.572   1.00 41.80 ? 126 MET   A CA   1 
ATOM   782  C  C    . MET   A 1 126 ? 28.243 41.106 3.619   1.00 40.56 ? 126 MET   A C    1 
ATOM   783  O  O    . MET   A 1 126 ? 27.817 40.690 2.531   1.00 40.86 ? 126 MET   A O    1 
ATOM   784  C  CB   . MET   A 1 126 ? 27.351 43.298 4.435   1.00 44.21 ? 126 MET   A CB   1 
ATOM   785  C  CG   . MET   A 1 126 ? 26.162 44.025 5.029   1.00 49.92 ? 126 MET   A CG   1 
ATOM   786  S  SD   . MET   A 1 126 ? 24.598 43.549 4.255   1.00 59.51 ? 126 MET   A SD   1 
ATOM   787  C  CE   . MET   A 1 126 ? 25.078 43.534 2.529   1.00 47.47 ? 126 MET   A CE   1 
ATOM   788  N  N    . PHE   A 1 127 ? 29.509 41.004 4.026   1.00 39.70 ? 127 PHE   A N    1 
ATOM   789  C  CA   . PHE   A 1 127 ? 30.541 40.341 3.191   1.00 39.55 ? 127 PHE   A CA   1 
ATOM   790  C  C    . PHE   A 1 127 ? 30.190 38.861 3.033   1.00 39.00 ? 127 PHE   A C    1 
ATOM   791  O  O    . PHE   A 1 127 ? 30.261 38.346 1.905   1.00 38.99 ? 127 PHE   A O    1 
ATOM   792  C  CB   . PHE   A 1 127 ? 31.922 40.497 3.828   1.00 39.89 ? 127 PHE   A CB   1 
ATOM   793  C  CG   . PHE   A 1 127 ? 33.077 40.307 2.880   1.00 40.48 ? 127 PHE   A CG   1 
ATOM   794  C  CD1  . PHE   A 1 127 ? 33.294 41.196 1.841   1.00 41.12 ? 127 PHE   A CD1  1 
ATOM   795  C  CD2  . PHE   A 1 127 ? 33.936 39.229 3.015   1.00 40.61 ? 127 PHE   A CD2  1 
ATOM   796  C  CE1  . PHE   A 1 127 ? 34.356 41.022 0.968   1.00 41.74 ? 127 PHE   A CE1  1 
ATOM   797  C  CE2  . PHE   A 1 127 ? 34.994 39.053 2.139   1.00 41.20 ? 127 PHE   A CE2  1 
ATOM   798  C  CZ   . PHE   A 1 127 ? 35.202 39.949 1.117   1.00 41.35 ? 127 PHE   A CZ   1 
ATOM   799  N  N    . GLN   A 1 128 ? 29.816 38.209 4.135   1.00 37.91 ? 128 GLN   A N    1 
ATOM   800  C  CA   . GLN   A 1 128 ? 29.469 36.765 4.098   1.00 37.42 ? 128 GLN   A CA   1 
ATOM   801  C  C    . GLN   A 1 128 ? 28.251 36.558 3.195   1.00 38.41 ? 128 GLN   A C    1 
ATOM   802  O  O    . GLN   A 1 128 ? 28.253 35.587 2.420   1.00 38.19 ? 128 GLN   A O    1 
ATOM   803  C  CB   . GLN   A 1 128 ? 29.185 36.261 5.513   1.00 37.46 ? 128 GLN   A CB   1 
ATOM   804  C  CG   . GLN   A 1 128 ? 30.432 35.991 6.337   1.00 36.21 ? 128 GLN   A CG   1 
ATOM   805  C  CD   . GLN   A 1 128 ? 30.080 35.638 7.761   1.00 38.62 ? 128 GLN   A CD   1 
ATOM   806  O  OE1  . GLN   A 1 128 ? 29.628 36.477 8.536   1.00 38.94 ? 128 GLN   A OE1  1 
ATOM   807  N  NE2  . GLN   A 1 128 ? 30.307 34.387 8.123   1.00 37.30 ? 128 GLN   A NE2  1 
ATOM   808  N  N    . LEU   A 1 129 ? 27.254 37.436 3.305   1.00 38.60 ? 129 LEU   A N    1 
ATOM   809  C  CA   . LEU   A 1 129 ? 26.039 37.335 2.456   1.00 38.86 ? 129 LEU   A CA   1 
ATOM   810  C  C    . LEU   A 1 129 ? 26.445 37.488 0.988   1.00 38.38 ? 129 LEU   A C    1 
ATOM   811  O  O    . LEU   A 1 129 ? 25.954 36.705 0.160   1.00 38.30 ? 129 LEU   A O    1 
ATOM   812  C  CB   . LEU   A 1 129 ? 25.054 38.428 2.877   1.00 39.70 ? 129 LEU   A CB   1 
ATOM   813  C  CG   . LEU   A 1 129 ? 23.801 38.569 2.015   1.00 42.64 ? 129 LEU   A CG   1 
ATOM   814  C  CD1  . LEU   A 1 129 ? 22.901 37.353 2.166   1.00 43.63 ? 129 LEU   A CD1  1 
ATOM   815  C  CD2  . LEU   A 1 129 ? 23.042 39.835 2.379   1.00 43.11 ? 129 LEU   A CD2  1 
ATOM   816  N  N    . LEU   A 1 130 ? 27.320 38.448 0.695   1.00 37.91 ? 130 LEU   A N    1 
ATOM   817  C  CA   . LEU   A 1 130 ? 27.770 38.697 -0.700  1.00 37.83 ? 130 LEU   A CA   1 
ATOM   818  C  C    . LEU   A 1 130 ? 28.640 37.531 -1.186  1.00 38.63 ? 130 LEU   A C    1 
ATOM   819  O  O    . LEU   A 1 130 ? 28.622 37.260 -2.396  1.00 39.03 ? 130 LEU   A O    1 
ATOM   820  C  CB   . LEU   A 1 130 ? 28.533 40.023 -0.731  1.00 37.51 ? 130 LEU   A CB   1 
ATOM   821  C  CG   . LEU   A 1 130 ? 27.677 41.277 -0.567  1.00 38.78 ? 130 LEU   A CG   1 
ATOM   822  C  CD1  . LEU   A 1 130 ? 28.542 42.527 -0.594  1.00 39.30 ? 130 LEU   A CD1  1 
ATOM   823  C  CD2  . LEU   A 1 130 ? 26.611 41.347 -1.650  1.00 38.40 ? 130 LEU   A CD2  1 
ATOM   824  N  N    . ARG   A 1 131 ? 29.373 36.879 -0.279  1.00 39.01 ? 131 ARG   A N    1 
ATOM   825  C  CA   . ARG   A 1 131 ? 30.205 35.703 -0.654  1.00 40.23 ? 131 ARG   A CA   1 
ATOM   826  C  C    . ARG   A 1 131 ? 29.295 34.533 -1.045  1.00 39.65 ? 131 ARG   A C    1 
ATOM   827  O  O    . ARG   A 1 131 ? 29.557 33.910 -2.089  1.00 40.55 ? 131 ARG   A O    1 
ATOM   828  C  CB   . ARG   A 1 131 ? 31.137 35.291 0.489   1.00 43.11 ? 131 ARG   A CB   1 
ATOM   829  C  CG   . ARG   A 1 131 ? 32.361 36.178 0.659   1.00 49.27 ? 131 ARG   A CG   1 
ATOM   830  C  CD   . ARG   A 1 131 ? 33.466 35.401 1.348   1.00 55.09 ? 131 ARG   A CD   1 
ATOM   831  N  NE   . ARG   A 1 131 ? 32.967 34.689 2.515   1.00 62.33 ? 131 ARG   A NE   1 
ATOM   832  C  CZ   . ARG   A 1 131 ? 33.697 33.889 3.283   1.00 65.59 ? 131 ARG   A CZ   1 
ATOM   833  N  NH1  . ARG   A 1 131 ? 34.919 33.551 2.913   1.00 65.52 ? 131 ARG   A NH1  1 
ATOM   834  N  NH2  . ARG   A 1 131 ? 33.199 33.423 4.415   1.00 65.49 ? 131 ARG   A NH2  1 
ATOM   835  N  N    . GLY   A 1 132 ? 28.272 34.253 -0.237  1.00 37.73 ? 132 GLY   A N    1 
ATOM   836  C  CA   . GLY   A 1 132 ? 27.318 33.181 -0.569  1.00 37.20 ? 132 GLY   A CA   1 
ATOM   837  C  C    . GLY   A 1 132 ? 26.526 33.544 -1.807  1.00 36.85 ? 132 GLY   A C    1 
ATOM   838  O  O    . GLY   A 1 132 ? 26.254 32.643 -2.616  1.00 36.28 ? 132 GLY   A O    1 
ATOM   839  N  N    . LEU   A 1 133 ? 26.168 34.822 -1.943  1.00 36.32 ? 133 LEU   A N    1 
ATOM   840  C  CA   . LEU   A 1 133 ? 25.463 35.265 -3.126  1.00 36.80 ? 133 LEU   A CA   1 
ATOM   841  C  C    . LEU   A 1 133 ? 26.320 35.153 -4.376  1.00 35.34 ? 133 LEU   A C    1 
ATOM   842  O  O    . LEU   A 1 133 ? 25.855 34.643 -5.401  1.00 35.14 ? 133 LEU   A O    1 
ATOM   843  C  CB   . LEU   A 1 133 ? 24.966 36.704 -2.938  1.00 38.64 ? 133 LEU   A CB   1 
ATOM   844  C  CG   . LEU   A 1 133 ? 23.566 36.986 -3.456  1.00 41.98 ? 133 LEU   A CG   1 
ATOM   845  C  CD1  . LEU   A 1 133 ? 22.536 35.999 -2.857  1.00 43.01 ? 133 LEU   A CD1  1 
ATOM   846  C  CD2  . LEU   A 1 133 ? 23.166 38.383 -3.111  1.00 43.17 ? 133 LEU   A CD2  1 
ATOM   847  N  N    . ASP   A 1 134 ? 27.576 35.590 -4.300  1.00 34.37 ? 134 ASP   A N    1 
ATOM   848  C  CA   . ASP   A 1 134 ? 28.495 35.467 -5.463  1.00 35.02 ? 134 ASP   A CA   1 
ATOM   849  C  C    . ASP   A 1 134 ? 28.662 33.990 -5.835  1.00 36.58 ? 134 ASP   A C    1 
ATOM   850  O  O    . ASP   A 1 134 ? 28.693 33.692 -7.040  1.00 36.50 ? 134 ASP   A O    1 
ATOM   851  C  CB   . ASP   A 1 134 ? 29.837 36.152 -5.203  1.00 36.04 ? 134 ASP   A CB   1 
ATOM   852  C  CG   . ASP   A 1 134 ? 30.796 36.048 -6.375  1.00 40.98 ? 134 ASP   A CG   1 
ATOM   853  O  OD1  . ASP   A 1 134 ? 30.419 36.489 -7.477  1.00 40.54 ? 134 ASP   A OD1  1 
ATOM   854  O  OD2  . ASP   A 1 134 ? 31.910 35.531 -6.174  1.00 44.69 ? 134 ASP   A OD2  1 
ATOM   855  N  N    . PHE   A 1 135 ? 28.753 33.106 -4.839  1.00 36.23 ? 135 PHE   A N    1 
ATOM   856  C  CA   . PHE   A 1 135 ? 28.893 31.650 -5.096  1.00 36.55 ? 135 PHE   A CA   1 
ATOM   857  C  C    . PHE   A 1 135 ? 27.701 31.152 -5.917  1.00 38.04 ? 135 PHE   A C    1 
ATOM   858  O  O    . PHE   A 1 135 ? 27.914 30.481 -6.942  1.00 39.22 ? 135 PHE   A O    1 
ATOM   859  C  CB   . PHE   A 1 135 ? 28.982 30.885 -3.775  1.00 34.81 ? 135 PHE   A CB   1 
ATOM   860  C  CG   . PHE   A 1 135 ? 28.881 29.386 -3.892  1.00 34.66 ? 135 PHE   A CG   1 
ATOM   861  C  CD1  . PHE   A 1 135 ? 29.852 28.657 -4.558  1.00 35.10 ? 135 PHE   A CD1  1 
ATOM   862  C  CD2  . PHE   A 1 135 ? 27.810 28.704 -3.340  1.00 34.47 ? 135 PHE   A CD2  1 
ATOM   863  C  CE1  . PHE   A 1 135 ? 29.756 27.279 -4.662  1.00 35.21 ? 135 PHE   A CE1  1 
ATOM   864  C  CE2  . PHE   A 1 135 ? 27.713 27.326 -3.449  1.00 34.95 ? 135 PHE   A CE2  1 
ATOM   865  C  CZ   . PHE   A 1 135 ? 28.687 26.616 -4.110  1.00 35.00 ? 135 PHE   A CZ   1 
ATOM   866  N  N    . LEU   A 1 136 ? 26.486 31.476 -5.476  1.00 37.46 ? 136 LEU   A N    1 
ATOM   867  C  CA   . LEU   A 1 136 ? 25.262 31.008 -6.178  1.00 36.99 ? 136 LEU   A CA   1 
ATOM   868  C  C    . LEU   A 1 136 ? 25.221 31.607 -7.587  1.00 36.16 ? 136 LEU   A C    1 
ATOM   869  O  O    . LEU   A 1 136 ? 24.956 30.852 -8.535  1.00 35.36 ? 136 LEU   A O    1 
ATOM   870  C  CB   . LEU   A 1 136 ? 24.044 31.430 -5.352  1.00 37.22 ? 136 LEU   A CB   1 
ATOM   871  C  CG   . LEU   A 1 136 ? 23.439 30.348 -4.459  1.00 38.14 ? 136 LEU   A CG   1 
ATOM   872  C  CD1  . LEU   A 1 136 ? 24.483 29.777 -3.515  1.00 38.54 ? 136 LEU   A CD1  1 
ATOM   873  C  CD2  . LEU   A 1 136 ? 22.262 30.901 -3.671  1.00 37.60 ? 136 LEU   A CD2  1 
ATOM   874  N  N    . HIS   A 1 137 ? 25.498 32.904 -7.711  1.00 36.19 ? 137 HIS   A N    1 
ATOM   875  C  CA   . HIS   A 1 137 ? 25.429 33.591 -9.030  1.00 36.81 ? 137 HIS   A CA   1 
ATOM   876  C  C    . HIS   A 1 137 ? 26.512 33.023 -9.955  1.00 37.46 ? 137 HIS   A C    1 
ATOM   877  O  O    . HIS   A 1 137 ? 26.255 32.904 -11.169 1.00 36.86 ? 137 HIS   A O    1 
ATOM   878  C  CB   . HIS   A 1 137 ? 25.506 35.110 -8.833  1.00 36.63 ? 137 HIS   A CB   1 
ATOM   879  C  CG   . HIS   A 1 137 ? 24.304 35.683 -8.160  1.00 38.12 ? 137 HIS   A CG   1 
ATOM   880  N  ND1  . HIS   A 1 137 ? 24.179 37.018 -7.842  1.00 39.22 ? 137 HIS   A ND1  1 
ATOM   881  C  CD2  . HIS   A 1 137 ? 23.177 35.097 -7.740  1.00 38.59 ? 137 HIS   A CD2  1 
ATOM   882  C  CE1  . HIS   A 1 137 ? 23.010 37.219 -7.254  1.00 38.98 ? 137 HIS   A CE1  1 
ATOM   883  N  NE2  . HIS   A 1 137 ? 22.384 36.066 -7.183  1.00 38.70 ? 137 HIS   A NE2  1 
ATOM   884  N  N    . SER   A 1 138 ? 27.676 32.681 -9.400  1.00 37.72 ? 138 SER   A N    1 
ATOM   885  C  CA   . SER   A 1 138 ? 28.780 32.087 -10.198 1.00 38.73 ? 138 SER   A CA   1 
ATOM   886  C  C    . SER   A 1 138 ? 28.348 30.725 -10.747 1.00 39.56 ? 138 SER   A C    1 
ATOM   887  O  O    . SER   A 1 138 ? 28.894 30.309 -11.779 1.00 40.84 ? 138 SER   A O    1 
ATOM   888  C  CB   . SER   A 1 138 ? 30.029 31.972 -9.372  1.00 39.90 ? 138 SER   A CB   1 
ATOM   889  O  OG   . SER   A 1 138 ? 29.862 31.022 -8.333  1.00 44.20 ? 138 SER   A OG   1 
ATOM   890  N  N    . HIS   A 1 139 ? 27.403 30.067 -10.076 1.00 39.61 ? 139 HIS   A N    1 
ATOM   891  C  CA   . HIS   A 1 139 ? 26.899 28.742 -10.527 1.00 39.61 ? 139 HIS   A CA   1 
ATOM   892  C  C    . HIS   A 1 139 ? 25.532 28.939 -11.188 1.00 42.20 ? 139 HIS   A C    1 
ATOM   893  O  O    . HIS   A 1 139 ? 24.743 27.976 -11.256 1.00 43.28 ? 139 HIS   A O    1 
ATOM   894  C  CB   . HIS   A 1 139 ? 26.919 27.761 -9.351  1.00 38.18 ? 139 HIS   A CB   1 
ATOM   895  C  CG   . HIS   A 1 139 ? 28.302 27.495 -8.863  1.00 39.63 ? 139 HIS   A CG   1 
ATOM   896  N  ND1  . HIS   A 1 139 ? 29.241 26.835 -9.623  1.00 40.26 ? 139 HIS   A ND1  1 
ATOM   897  C  CD2  . HIS   A 1 139 ? 28.904 27.791 -7.707  1.00 39.72 ? 139 HIS   A CD2  1 
ATOM   898  C  CE1  . HIS   A 1 139 ? 30.371 26.744 -8.940  1.00 40.35 ? 139 HIS   A CE1  1 
ATOM   899  N  NE2  . HIS   A 1 139 ? 30.189 27.321 -7.774  1.00 40.59 ? 139 HIS   A NE2  1 
ATOM   900  N  N    . ARG   A 1 140 ? 25.257 30.160 -11.649 1.00 43.60 ? 140 ARG   A N    1 
ATOM   901  C  CA   . ARG   A 1 140 ? 23.985 30.465 -12.363 1.00 46.07 ? 140 ARG   A CA   1 
ATOM   902  C  C    . ARG   A 1 140 ? 22.773 30.061 -11.516 1.00 45.74 ? 140 ARG   A C    1 
ATOM   903  O  O    . ARG   A 1 140 ? 21.802 29.540 -12.090 1.00 46.55 ? 140 ARG   A O    1 
ATOM   904  C  CB   . ARG   A 1 140 ? 23.986 29.824 -13.755 1.00 49.31 ? 140 ARG   A CB   1 
ATOM   905  C  CG   . ARG   A 1 140 ? 24.847 30.568 -14.765 1.00 55.33 ? 140 ARG   A CG   1 
ATOM   906  C  CD   . ARG   A 1 140 ? 24.665 30.068 -16.185 1.00 61.55 ? 140 ARG   A CD   1 
ATOM   907  N  NE   . ARG   A 1 140 ? 25.116 28.695 -16.356 1.00 67.49 ? 140 ARG   A NE   1 
ATOM   908  C  CZ   . ARG   A 1 140 ? 25.066 28.028 -17.502 1.00 70.55 ? 140 ARG   A CZ   1 
ATOM   909  N  NH1  . ARG   A 1 140 ? 24.469 28.563 -18.552 1.00 69.47 ? 140 ARG   A NH1  1 
ATOM   910  N  NH2  . ARG   A 1 140 ? 25.609 26.826 -17.594 1.00 69.66 ? 140 ARG   A NH2  1 
ATOM   911  N  N    . VAL   A 1 141 ? 22.806 30.348 -10.213 1.00 44.11 ? 141 VAL   A N    1 
ATOM   912  C  CA   . VAL   A 1 141 ? 21.616 30.097 -9.348  1.00 42.49 ? 141 VAL   A CA   1 
ATOM   913  C  C    . VAL   A 1 141 ? 21.144 31.449 -8.807  1.00 40.67 ? 141 VAL   A C    1 
ATOM   914  O  O    . VAL   A 1 141 ? 21.996 32.226 -8.342  1.00 39.77 ? 141 VAL   A O    1 
ATOM   915  C  CB   . VAL   A 1 141 ? 21.924 29.108 -8.208  1.00 42.73 ? 141 VAL   A CB   1 
ATOM   916  C  CG1  . VAL   A 1 141 ? 20.758 28.983 -7.240  1.00 42.62 ? 141 VAL   A CG1  1 
ATOM   917  C  CG2  . VAL   A 1 141 ? 22.337 27.745 -8.736  1.00 43.32 ? 141 VAL   A CG2  1 
ATOM   918  N  N    . VAL   A 1 142 ? 19.842 31.725 -8.893  1.00 40.18 ? 142 VAL   A N    1 
ATOM   919  C  CA   . VAL   A 1 142 ? 19.277 32.992 -8.342  1.00 39.13 ? 142 VAL   A CA   1 
ATOM   920  C  C    . VAL   A 1 142 ? 18.348 32.626 -7.181  1.00 38.13 ? 142 VAL   A C    1 
ATOM   921  O  O    . VAL   A 1 142 ? 17.483 31.756 -7.377  1.00 38.77 ? 142 VAL   A O    1 
ATOM   922  C  CB   . VAL   A 1 142 ? 18.543 33.801 -9.430  1.00 39.15 ? 142 VAL   A CB   1 
ATOM   923  C  CG1  . VAL   A 1 142 ? 18.085 35.156 -8.915  1.00 40.03 ? 142 VAL   A CG1  1 
ATOM   924  C  CG2  . VAL   A 1 142 ? 19.390 33.964 -10.682 1.00 38.54 ? 142 VAL   A CG2  1 
ATOM   925  N  N    . HIS   A 1 143 ? 18.538 33.252 -6.018  1.00 36.94 ? 143 HIS   A N    1 
ATOM   926  C  CA   . HIS   A 1 143 ? 17.680 32.970 -4.834  1.00 36.52 ? 143 HIS   A CA   1 
ATOM   927  C  C    . HIS   A 1 143 ? 16.240 33.379 -5.157  1.00 37.68 ? 143 HIS   A C    1 
ATOM   928  O  O    . HIS   A 1 143 ? 15.350 32.516 -5.016  1.00 38.00 ? 143 HIS   A O    1 
ATOM   929  C  CB   . HIS   A 1 143 ? 18.229 33.688 -3.596  1.00 35.58 ? 143 HIS   A CB   1 
ATOM   930  C  CG   . HIS   A 1 143 ? 17.621 33.248 -2.308  1.00 35.04 ? 143 HIS   A CG   1 
ATOM   931  N  ND1  . HIS   A 1 143 ? 16.263 33.253 -2.076  1.00 36.03 ? 143 HIS   A ND1  1 
ATOM   932  C  CD2  . HIS   A 1 143 ? 18.185 32.776 -1.191  1.00 35.50 ? 143 HIS   A CD2  1 
ATOM   933  C  CE1  . HIS   A 1 143 ? 16.029 32.804 -0.852  1.00 36.01 ? 143 HIS   A CE1  1 
ATOM   934  N  NE2  . HIS   A 1 143 ? 17.183 32.510 -0.297  1.00 36.74 ? 143 HIS   A NE2  1 
ATOM   935  N  N    . ARG   A 1 144 ? 16.021 34.639 -5.548  1.00 38.16 ? 144 ARG   A N    1 
ATOM   936  C  CA   . ARG   A 1 144 ? 14.676 35.128 -5.975  1.00 39.16 ? 144 ARG   A CA   1 
ATOM   937  C  C    . ARG   A 1 144 ? 13.780 35.469 -4.775  1.00 38.66 ? 144 ARG   A C    1 
ATOM   938  O  O    . ARG   A 1 144 ? 12.789 36.187 -4.982  1.00 38.58 ? 144 ARG   A O    1 
ATOM   939  C  CB   . ARG   A 1 144 ? 14.004 34.119 -6.915  1.00 42.66 ? 144 ARG   A CB   1 
ATOM   940  C  CG   . ARG   A 1 144 ? 14.873 33.702 -8.092  1.00 47.77 ? 144 ARG   A CG   1 
ATOM   941  C  CD   . ARG   A 1 144 ? 14.075 33.137 -9.250  1.00 53.51 ? 144 ARG   A CD   1 
ATOM   942  N  NE   . ARG   A 1 144 ? 14.963 32.721 -10.324 1.00 59.05 ? 144 ARG   A NE   1 
ATOM   943  C  CZ   . ARG   A 1 144 ? 15.019 33.301 -11.515 1.00 62.59 ? 144 ARG   A CZ   1 
ATOM   944  N  NH1  . ARG   A 1 144 ? 15.775 32.787 -12.468 1.00 62.05 ? 144 ARG   A NH1  1 
ATOM   945  N  NH2  . ARG   A 1 144 ? 14.324 34.401 -11.745 1.00 62.51 ? 144 ARG   A NH2  1 
ATOM   946  N  N    . ASP   A 1 145 ? 14.113 34.993 -3.574  1.00 38.78 ? 145 ASP   A N    1 
ATOM   947  C  CA   . ASP   A 1 145 ? 13.318 35.367 -2.374  1.00 39.60 ? 145 ASP   A CA   1 
ATOM   948  C  C    . ASP   A 1 145 ? 14.255 35.595 -1.184  1.00 38.53 ? 145 ASP   A C    1 
ATOM   949  O  O    . ASP   A 1 145 ? 14.011 35.000 -0.125  1.00 38.18 ? 145 ASP   A O    1 
ATOM   950  C  CB   . ASP   A 1 145 ? 12.246 34.322 -2.058  1.00 43.91 ? 145 ASP   A CB   1 
ATOM   951  C  CG   . ASP   A 1 145 ? 11.147 34.849 -1.150  1.00 52.39 ? 145 ASP   A CG   1 
ATOM   952  O  OD1  . ASP   A 1 145 ? 11.178 36.053 -0.831  1.00 53.21 ? 145 ASP   A OD1  1 
ATOM   953  O  OD2  . ASP   A 1 145 ? 10.277 34.049 -0.760  1.00 54.70 ? 145 ASP   A OD2  1 
ATOM   954  N  N    . LEU   A 1 146 ? 15.270 36.441 -1.358  1.00 38.23 ? 146 LEU   A N    1 
ATOM   955  C  CA   . LEU   A 1 146 ? 16.243 36.708 -0.269  1.00 38.81 ? 146 LEU   A CA   1 
ATOM   956  C  C    . LEU   A 1 146 ? 15.596 37.632 0.764   1.00 38.43 ? 146 LEU   A C    1 
ATOM   957  O  O    . LEU   A 1 146 ? 15.184 38.742 0.390   1.00 38.84 ? 146 LEU   A O    1 
ATOM   958  C  CB   . LEU   A 1 146 ? 17.512 37.328 -0.856  1.00 39.96 ? 146 LEU   A CB   1 
ATOM   959  C  CG   . LEU   A 1 146 ? 18.682 37.473 0.114   1.00 42.25 ? 146 LEU   A CG   1 
ATOM   960  C  CD1  . LEU   A 1 146 ? 19.200 36.109 0.540   1.00 42.50 ? 146 LEU   A CD1  1 
ATOM   961  C  CD2  . LEU   A 1 146 ? 19.798 38.293 -0.512  1.00 42.53 ? 146 LEU   A CD2  1 
ATOM   962  N  N    . LYS   A 1 147 ? 15.520 37.176 2.013   1.00 37.84 ? 147 LYS   A N    1 
ATOM   963  C  CA   . LYS   A 1 147 ? 14.918 37.984 3.103   1.00 37.85 ? 147 LYS   A CA   1 
ATOM   964  C  C    . LYS   A 1 147 ? 15.551 37.555 4.430   1.00 37.99 ? 147 LYS   A C    1 
ATOM   965  O  O    . LYS   A 1 147 ? 16.033 36.417 4.515   1.00 37.84 ? 147 LYS   A O    1 
ATOM   966  C  CB   . LYS   A 1 147 ? 13.397 37.811 3.105   1.00 39.75 ? 147 LYS   A CB   1 
ATOM   967  C  CG   . LYS   A 1 147 ? 12.895 36.381 3.220   1.00 42.73 ? 147 LYS   A CG   1 
ATOM   968  C  CD   . LYS   A 1 147 ? 11.437 36.240 2.848   1.00 45.72 ? 147 LYS   A CD   1 
ATOM   969  C  CE   . LYS   A 1 147 ? 10.961 34.803 2.854   1.00 48.97 ? 147 LYS   A CE   1 
ATOM   970  N  NZ   . LYS   A 1 147 ? 9.541  34.697 2.443   1.00 51.59 ? 147 LYS   A NZ   1 
ATOM   971  N  N    . PRO   A 1 148 ? 15.581 38.426 5.459   1.00 38.30 ? 148 PRO   A N    1 
ATOM   972  C  CA   . PRO   A 1 148 ? 16.228 38.098 6.733   1.00 38.50 ? 148 PRO   A CA   1 
ATOM   973  C  C    . PRO   A 1 148 ? 15.745 36.762 7.315   1.00 39.19 ? 148 PRO   A C    1 
ATOM   974  O  O    . PRO   A 1 148 ? 16.454 36.194 8.113   1.00 40.07 ? 148 PRO   A O    1 
ATOM   975  C  CB   . PRO   A 1 148 ? 15.795 39.263 7.632   1.00 39.19 ? 148 PRO   A CB   1 
ATOM   976  C  CG   . PRO   A 1 148 ? 15.615 40.416 6.676   1.00 39.68 ? 148 PRO   A CG   1 
ATOM   977  C  CD   . PRO   A 1 148 ? 15.019 39.778 5.441   1.00 37.75 ? 148 PRO   A CD   1 
ATOM   978  N  N    . GLN   A 1 149 ? 14.567 36.298 6.895   1.00 39.28 ? 149 GLN   A N    1 
ATOM   979  C  CA   . GLN   A 1 149 ? 13.996 35.032 7.428   1.00 39.68 ? 149 GLN   A CA   1 
ATOM   980  C  C    . GLN   A 1 149 ? 14.738 33.817 6.854   1.00 38.67 ? 149 GLN   A C    1 
ATOM   981  O  O    . GLN   A 1 149 ? 14.764 32.779 7.536   1.00 38.92 ? 149 GLN   A O    1 
ATOM   982  C  CB   . GLN   A 1 149 ? 12.497 34.961 7.129   1.00 42.52 ? 149 GLN   A CB   1 
ATOM   983  C  CG   . GLN   A 1 149 ? 11.676 36.030 7.834   1.00 46.85 ? 149 GLN   A CG   1 
ATOM   984  C  CD   . GLN   A 1 149 ? 11.843 37.394 7.211   1.00 50.85 ? 149 GLN   A CD   1 
ATOM   985  O  OE1  . GLN   A 1 149 ? 12.269 38.347 7.859   1.00 55.78 ? 149 GLN   A OE1  1 
ATOM   986  N  NE2  . GLN   A 1 149 ? 11.504 37.499 5.938   1.00 47.17 ? 149 GLN   A NE2  1 
ATOM   987  N  N    . ASN   A 1 150 ? 15.300 33.939 5.648   1.00 37.69 ? 150 ASN   A N    1 
ATOM   988  C  CA   . ASN   A 1 150 ? 16.011 32.801 5.002   1.00 36.65 ? 150 ASN   A CA   1 
ATOM   989  C  C    . ASN   A 1 150 ? 17.524 32.995 5.145   1.00 36.25 ? 150 ASN   A C    1 
ATOM   990  O  O    . ASN   A 1 150 ? 18.269 32.096 4.730   1.00 37.05 ? 150 ASN   A O    1 
ATOM   991  C  CB   . ASN   A 1 150 ? 15.581 32.598 3.546   1.00 36.13 ? 150 ASN   A CB   1 
ATOM   992  C  CG   . ASN   A 1 150 ? 15.674 33.853 2.709   1.00 36.48 ? 150 ASN   A CG   1 
ATOM   993  O  OD1  . ASN   A 1 150 ? 16.726 34.481 2.629   1.00 36.62 ? 150 ASN   A OD1  1 
ATOM   994  N  ND2  . ASN   A 1 150 ? 14.571 34.222 2.084   1.00 36.48 ? 150 ASN   A ND2  1 
ATOM   995  N  N    . ILE   A 1 151 ? 17.954 34.133 5.688   1.00 35.61 ? 151 ILE   A N    1 
ATOM   996  C  CA   . ILE   A 1 151 ? 19.404 34.344 5.960   1.00 36.12 ? 151 ILE   A CA   1 
ATOM   997  C  C    . ILE   A 1 151 ? 19.651 33.842 7.382   1.00 36.24 ? 151 ILE   A C    1 
ATOM   998  O  O    . ILE   A 1 151 ? 19.166 34.489 8.324   1.00 36.71 ? 151 ILE   A O    1 
ATOM   999  C  CB   . ILE   A 1 151 ? 19.793 35.822 5.779   1.00 36.96 ? 151 ILE   A CB   1 
ATOM   1000 C  CG1  . ILE   A 1 151 ? 19.432 36.333 4.382   1.00 37.57 ? 151 ILE   A CG1  1 
ATOM   1001 C  CG2  . ILE   A 1 151 ? 21.265 36.033 6.095   1.00 37.86 ? 151 ILE   A CG2  1 
ATOM   1002 C  CD1  . ILE   A 1 151 ? 19.727 37.798 4.172   1.00 39.07 ? 151 ILE   A CD1  1 
ATOM   1003 N  N    . LEU   A 1 152 ? 20.368 32.728 7.526   1.00 35.66 ? 152 LEU   A N    1 
ATOM   1004 C  CA   . LEU   A 1 152 ? 20.529 32.115 8.870   1.00 36.07 ? 152 LEU   A CA   1 
ATOM   1005 C  C    . LEU   A 1 152 ? 21.843 32.554 9.518   1.00 36.84 ? 152 LEU   A C    1 
ATOM   1006 O  O    . LEU   A 1 152 ? 22.840 32.701 8.795   1.00 36.85 ? 152 LEU   A O    1 
ATOM   1007 C  CB   . LEU   A 1 152 ? 20.422 30.595 8.716   1.00 36.25 ? 152 LEU   A CB   1 
ATOM   1008 C  CG   . LEU   A 1 152 ? 19.139 30.120 8.036   1.00 37.10 ? 152 LEU   A CG   1 
ATOM   1009 C  CD1  . LEU   A 1 152 ? 19.019 28.607 8.082   1.00 37.41 ? 152 LEU   A CD1  1 
ATOM   1010 C  CD2  . LEU   A 1 152 ? 17.919 30.768 8.669   1.00 37.72 ? 152 LEU   A CD2  1 
ATOM   1011 N  N    . VAL   A 1 153 ? 21.831 32.773 10.835  1.00 37.54 ? 153 VAL   A N    1 
ATOM   1012 C  CA   . VAL   A 1 153 ? 23.053 33.234 11.560  1.00 39.84 ? 153 VAL   A CA   1 
ATOM   1013 C  C    . VAL   A 1 153 ? 23.462 32.161 12.576  1.00 41.06 ? 153 VAL   A C    1 
ATOM   1014 O  O    . VAL   A 1 153 ? 22.600 31.742 13.368  1.00 41.11 ? 153 VAL   A O    1 
ATOM   1015 C  CB   . VAL   A 1 153 ? 22.831 34.602 12.231  1.00 41.07 ? 153 VAL   A CB   1 
ATOM   1016 C  CG1  . VAL   A 1 153 ? 24.110 35.136 12.854  1.00 41.59 ? 153 VAL   A CG1  1 
ATOM   1017 C  CG2  . VAL   A 1 153 ? 22.243 35.617 11.262  1.00 41.07 ? 153 VAL   A CG2  1 
ATOM   1018 N  N    . THR   A 1 154 ? 24.727 31.735 12.545  1.00 41.37 ? 154 THR   A N    1 
ATOM   1019 C  CA   . THR   A 1 154 ? 25.189 30.641 13.441  1.00 42.70 ? 154 THR   A CA   1 
ATOM   1020 C  C    . THR   A 1 154 ? 25.594 31.195 14.809  1.00 43.20 ? 154 THR   A C    1 
ATOM   1021 O  O    . THR   A 1 154 ? 25.684 32.427 14.941  1.00 42.06 ? 154 THR   A O    1 
ATOM   1022 C  CB   . THR   A 1 154 ? 26.360 29.867 12.822  1.00 45.51 ? 154 THR   A CB   1 
ATOM   1023 O  OG1  . THR   A 1 154 ? 27.512 30.709 12.850  1.00 49.38 ? 154 THR   A OG1  1 
ATOM   1024 C  CG2  . THR   A 1 154 ? 26.080 29.408 11.408  1.00 44.29 ? 154 THR   A CG2  1 
ATOM   1025 N  N    . SER   A 1 155 ? 25.834 30.306 15.775  1.00 44.68 ? 155 SER   A N    1 
ATOM   1026 C  CA   . SER   A 1 155 ? 26.285 30.725 17.128  1.00 46.69 ? 155 SER   A CA   1 
ATOM   1027 C  C    . SER   A 1 155 ? 27.651 31.401 17.013  1.00 48.90 ? 155 SER   A C    1 
ATOM   1028 O  O    . SER   A 1 155 ? 28.004 32.172 17.921  1.00 50.49 ? 155 SER   A O    1 
ATOM   1029 C  CB   . SER   A 1 155 ? 26.338 29.544 18.053  1.00 47.17 ? 155 SER   A CB   1 
ATOM   1030 O  OG   . SER   A 1 155 ? 27.132 28.504 17.503  1.00 48.61 ? 155 SER   A OG   1 
ATOM   1031 N  N    . SER   A 1 156 ? 28.381 31.113 15.934  1.00 48.93 ? 156 SER   A N    1 
ATOM   1032 C  CA   . SER   A 1 156 ? 29.714 31.727 15.706  1.00 49.59 ? 156 SER   A CA   1 
ATOM   1033 C  C    . SER   A 1 156 ? 29.568 33.035 14.921  1.00 48.63 ? 156 SER   A C    1 
ATOM   1034 O  O    . SER   A 1 156 ? 30.594 33.696 14.695  1.00 48.87 ? 156 SER   A O    1 
ATOM   1035 C  CB   . SER   A 1 156 ? 30.608 30.758 14.989  1.00 52.69 ? 156 SER   A CB   1 
ATOM   1036 O  OG   . SER   A 1 156 ? 30.589 29.491 15.626  1.00 57.41 ? 156 SER   A OG   1 
ATOM   1037 N  N    . GLY   A 1 157 ? 28.344 33.382 14.514  1.00 47.16 ? 157 GLY   A N    1 
ATOM   1038 C  CA   . GLY   A 1 157 ? 28.105 34.613 13.735  1.00 46.43 ? 157 GLY   A CA   1 
ATOM   1039 C  C    . GLY   A 1 157 ? 28.306 34.395 12.245  1.00 45.16 ? 157 GLY   A C    1 
ATOM   1040 O  O    . GLY   A 1 157 ? 28.588 35.378 11.542  1.00 45.21 ? 157 GLY   A O    1 
ATOM   1041 N  N    . GLN   A 1 158 ? 28.167 33.151 11.785  1.00 43.62 ? 158 GLN   A N    1 
ATOM   1042 C  CA   . GLN   A 1 158 ? 28.401 32.837 10.350  1.00 43.18 ? 158 GLN   A CA   1 
ATOM   1043 C  C    . GLN   A 1 158 ? 27.081 32.925 9.578   1.00 41.44 ? 158 GLN   A C    1 
ATOM   1044 O  O    . GLN   A 1 158 ? 26.103 32.294 10.005  1.00 40.94 ? 158 GLN   A O    1 
ATOM   1045 C  CB   . GLN   A 1 158 ? 29.063 31.469 10.182  1.00 46.16 ? 158 GLN   A CB   1 
ATOM   1046 C  CG   . GLN   A 1 158 ? 30.336 31.520 9.353   1.00 54.75 ? 158 GLN   A CG   1 
ATOM   1047 C  CD   . GLN   A 1 158 ? 30.541 30.286 8.511   1.00 63.85 ? 158 GLN   A CD   1 
ATOM   1048 O  OE1  . GLN   A 1 158 ? 29.773 29.329 8.577   1.00 66.35 ? 158 GLN   A OE1  1 
ATOM   1049 N  NE2  . GLN   A 1 158 ? 31.592 30.300 7.709   1.00 65.48 ? 158 GLN   A NE2  1 
ATOM   1050 N  N    . ILE   A 1 159 ? 27.076 33.684 8.481   1.00 40.77 ? 159 ILE   A N    1 
ATOM   1051 C  CA   . ILE   A 1 159 ? 25.857 33.843 7.637   1.00 40.47 ? 159 ILE   A CA   1 
ATOM   1052 C  C    . ILE   A 1 159 ? 25.715 32.621 6.731   1.00 40.50 ? 159 ILE   A C    1 
ATOM   1053 O  O    . ILE   A 1 159 ? 26.698 32.274 6.064   1.00 40.52 ? 159 ILE   A O    1 
ATOM   1054 C  CB   . ILE   A 1 159 ? 25.941 35.148 6.821   1.00 40.81 ? 159 ILE   A CB   1 
ATOM   1055 C  CG1  . ILE   A 1 159 ? 25.847 36.380 7.722   1.00 41.77 ? 159 ILE   A CG1  1 
ATOM   1056 C  CG2  . ILE   A 1 159 ? 24.888 35.174 5.725   1.00 41.67 ? 159 ILE   A CG2  1 
ATOM   1057 C  CD1  . ILE   A 1 159 ? 24.554 36.472 8.493   1.00 42.60 ? 159 ILE   A CD1  1 
ATOM   1058 N  N    . LYS   A 1 160 ? 24.540 31.991 6.729   1.00 40.16 ? 160 LYS   A N    1 
ATOM   1059 C  CA   . LYS   A 1 160 ? 24.295 30.859 5.835   1.00 40.07 ? 160 LYS   A CA   1 
ATOM   1060 C  C    . LYS   A 1 160 ? 22.989 31.035 5.095   1.00 38.77 ? 160 LYS   A C    1 
ATOM   1061 O  O    . LYS   A 1 160 ? 21.952 31.255 5.704   1.00 38.91 ? 160 LYS   A O    1 
ATOM   1062 C  CB   . LYS   A 1 160 ? 24.352 29.526 6.595   1.00 43.43 ? 160 LYS   A CB   1 
ATOM   1063 C  CG   . LYS   A 1 160 ? 25.779 29.112 6.950   1.00 46.31 ? 160 LYS   A CG   1 
ATOM   1064 C  CD   . LYS   A 1 160 ? 25.843 27.833 7.697   1.00 50.29 ? 160 LYS   A CD   1 
ATOM   1065 C  CE   . LYS   A 1 160 ? 27.286 27.354 7.828   1.00 54.74 ? 160 LYS   A CE   1 
ATOM   1066 N  NZ   . LYS   A 1 160 ? 27.702 26.442 6.715   1.00 57.30 ? 160 LYS   A NZ   1 
ATOM   1067 N  N    . LEU   A 1 161 ? 23.050 31.006 3.776   1.00 37.63 ? 161 LEU   A N    1 
ATOM   1068 C  CA   . LEU   A 1 161 ? 21.874 31.110 2.926   1.00 36.57 ? 161 LEU   A CA   1 
ATOM   1069 C  C    . LEU   A 1 161 ? 21.136 29.806 2.921   1.00 36.32 ? 161 LEU   A C    1 
ATOM   1070 O  O    . LEU   A 1 161 ? 21.739 28.753 2.783   1.00 36.80 ? 161 LEU   A O    1 
ATOM   1071 C  CB   . LEU   A 1 161 ? 22.262 31.439 1.481   1.00 35.41 ? 161 LEU   A CB   1 
ATOM   1072 C  CG   . LEU   A 1 161 ? 23.075 32.687 1.264   1.00 37.02 ? 161 LEU   A CG   1 
ATOM   1073 C  CD1  . LEU   A 1 161 ? 23.292 32.917 -0.221  1.00 37.40 ? 161 LEU   A CD1  1 
ATOM   1074 C  CD2  . LEU   A 1 161 ? 22.392 33.900 1.858   1.00 38.62 ? 161 LEU   A CD2  1 
ATOM   1075 N  N    . ALA   A 1 162 ? 19.833 29.890 3.031   1.00 36.06 ? 162 ALA   A N    1 
ATOM   1076 C  CA   . ALA   A 1 162 ? 18.908 28.777 3.048   1.00 36.34 ? 162 ALA   A CA   1 
ATOM   1077 C  C    . ALA   A 1 162 ? 17.670 29.135 2.178   1.00 37.27 ? 162 ALA   A C    1 
ATOM   1078 O  O    . ALA   A 1 162 ? 17.505 30.310 1.782   1.00 37.17 ? 162 ALA   A O    1 
ATOM   1079 C  CB   . ALA   A 1 162 ? 18.465 28.538 4.485   1.00 35.84 ? 162 ALA   A CB   1 
ATOM   1080 N  N    . ASP   A 1 163 ? 16.832 28.109 1.871   1.00 37.57 ? 163 ASP   A N    1 
ATOM   1081 C  CA   . ASP   A 1 163 ? 15.545 28.257 1.213   1.00 39.45 ? 163 ASP   A CA   1 
ATOM   1082 C  C    . ASP   A 1 163 ? 15.631 28.839 -0.203  1.00 40.40 ? 163 ASP   A C    1 
ATOM   1083 O  O    . ASP   A 1 163 ? 14.984 29.832 -0.506  1.00 41.33 ? 163 ASP   A O    1 
ATOM   1084 C  CB   . ASP   A 1 163 ? 14.619 29.085 2.116   1.00 40.83 ? 163 ASP   A CB   1 
ATOM   1085 C  CG   . ASP   A 1 163 ? 13.162 29.045 1.739   1.00 46.60 ? 163 ASP   A CG   1 
ATOM   1086 O  OD1  . ASP   A 1 163 ? 12.759 28.096 1.041   1.00 46.63 ? 163 ASP   A OD1  1 
ATOM   1087 O  OD2  . ASP   A 1 163 ? 12.415 29.975 2.150   1.00 50.87 ? 163 ASP   A OD2  1 
ATOM   1088 N  N    . PHE   A 1 164 ? 16.415 28.173 -1.053  1.00 41.03 ? 164 PHE   A N    1 
ATOM   1089 C  CA   . PHE   A 1 164 ? 16.610 28.637 -2.449  1.00 42.43 ? 164 PHE   A CA   1 
ATOM   1090 C  C    . PHE   A 1 164 ? 16.809 27.421 -3.360  1.00 45.42 ? 164 PHE   A C    1 
ATOM   1091 O  O    . PHE   A 1 164 ? 17.025 26.315 -2.833  1.00 44.87 ? 164 PHE   A O    1 
ATOM   1092 C  CB   . PHE   A 1 164 ? 17.823 29.565 -2.508  1.00 41.92 ? 164 PHE   A CB   1 
ATOM   1093 C  CG   . PHE   A 1 164 ? 19.112 28.947 -2.027  1.00 42.12 ? 164 PHE   A CG   1 
ATOM   1094 C  CD1  . PHE   A 1 164 ? 19.762 27.980 -2.776  1.00 42.96 ? 164 PHE   A CD1  1 
ATOM   1095 C  CD2  . PHE   A 1 164 ? 19.659 29.311 -0.807  1.00 42.53 ? 164 PHE   A CD2  1 
ATOM   1096 C  CE1  . PHE   A 1 164 ? 20.941 27.406 -2.327  1.00 43.24 ? 164 PHE   A CE1  1 
ATOM   1097 C  CE2  . PHE   A 1 164 ? 20.836 28.735 -0.358  1.00 42.91 ? 164 PHE   A CE2  1 
ATOM   1098 C  CZ   . PHE   A 1 164 ? 21.475 27.784 -1.118  1.00 42.70 ? 164 PHE   A CZ   1 
ATOM   1099 N  N    . GLY   A 1 165 ? 16.728 27.614 -4.680  1.00 48.18 ? 165 GLY   A N    1 
ATOM   1100 C  CA   . GLY   A 1 165 ? 16.998 26.514 -5.629  1.00 50.48 ? 165 GLY   A CA   1 
ATOM   1101 C  C    . GLY   A 1 165 ? 15.779 25.664 -5.933  1.00 52.69 ? 165 GLY   A C    1 
ATOM   1102 O  O    . GLY   A 1 165 ? 15.907 24.717 -6.727  1.00 52.60 ? 165 GLY   A O    1 
ATOM   1103 N  N    . LEU   A 1 166 ? 14.637 25.985 -5.326  1.00 54.54 ? 166 LEU   A N    1 
ATOM   1104 C  CA   . LEU   A 1 166 ? 13.391 25.210 -5.564  1.00 56.98 ? 166 LEU   A CA   1 
ATOM   1105 C  C    . LEU   A 1 166 ? 12.296 26.150 -6.077  1.00 59.62 ? 166 LEU   A C    1 
ATOM   1106 O  O    . LEU   A 1 166 ? 12.381 27.360 -5.810  1.00 60.01 ? 166 LEU   A O    1 
ATOM   1107 C  CB   . LEU   A 1 166 ? 12.966 24.519 -4.266  1.00 57.11 ? 166 LEU   A CB   1 
ATOM   1108 C  CG   . LEU   A 1 166 ? 13.933 23.460 -3.738  1.00 58.46 ? 166 LEU   A CG   1 
ATOM   1109 C  CD1  . LEU   A 1 166 ? 13.293 22.651 -2.621  1.00 59.14 ? 166 LEU   A CD1  1 
ATOM   1110 C  CD2  . LEU   A 1 166 ? 14.399 22.544 -4.858  1.00 58.87 ? 166 LEU   A CD2  1 
ATOM   1111 N  N    . ALA   A 1 167 ? 11.316 25.602 -6.796  1.00 61.30 ? 167 ALA   A N    1 
ATOM   1112 C  CA   . ALA   A 1 167 ? 10.207 26.422 -7.333  1.00 63.49 ? 167 ALA   A CA   1 
ATOM   1113 C  C    . ALA   A 1 167 ? 8.940  26.171 -6.509  1.00 65.30 ? 167 ALA   A C    1 
ATOM   1114 O  O    . ALA   A 1 167 ? 9.079  25.604 -5.407  1.00 66.20 ? 167 ALA   A O    1 
ATOM   1115 C  CB   . ALA   A 1 167 ? 9.995  26.101 -8.791  1.00 63.77 ? 167 ALA   A CB   1 
ATOM   1116 N  N    . VAL   A 1 181 ? 2.976  36.281 1.837   1.00 59.11 ? 181 VAL   A N    1 
ATOM   1117 C  CA   . VAL   A 1 181 ? 3.806  36.941 0.826   1.00 59.22 ? 181 VAL   A CA   1 
ATOM   1118 C  C    . VAL   A 1 181 ? 4.447  38.234 1.359   1.00 58.70 ? 181 VAL   A C    1 
ATOM   1119 O  O    . VAL   A 1 181 ? 3.792  39.001 2.062   1.00 59.52 ? 181 VAL   A O    1 
ATOM   1120 C  CB   . VAL   A 1 181 ? 2.980  37.246 -0.412  1.00 59.41 ? 181 VAL   A CB   1 
ATOM   1121 N  N    . THR   A 1 182 ? 5.733  38.467 1.025   1.00 56.83 ? 182 THR   A N    1 
ATOM   1122 C  CA   . THR   A 1 182 ? 6.463  39.680 1.401   1.00 54.54 ? 182 THR   A CA   1 
ATOM   1123 C  C    . THR   A 1 182 ? 7.218  40.251 0.190   1.00 51.67 ? 182 THR   A C    1 
ATOM   1124 O  O    . THR   A 1 182 ? 8.227  39.712 -0.314  1.00 52.38 ? 182 THR   A O    1 
ATOM   1125 C  CB   . THR   A 1 182 ? 7.330  39.485 2.649   1.00 55.33 ? 182 THR   A CB   1 
ATOM   1126 O  OG1  . THR   A 1 182 ? 6.446  39.534 3.750   1.00 56.41 ? 182 THR   A OG1  1 
ATOM   1127 C  CG2  . THR   A 1 182 ? 8.378  40.573 2.826   1.00 54.90 ? 182 THR   A CG2  1 
ATOM   1128 N  N    . LEU   A 1 183 ? 6.784  41.443 -0.232  1.00 47.84 ? 183 LEU   A N    1 
ATOM   1129 C  CA   . LEU   A 1 183 ? 7.418  42.114 -1.398  1.00 44.65 ? 183 LEU   A CA   1 
ATOM   1130 C  C    . LEU   A 1 183 ? 8.394  43.189 -0.912  1.00 39.58 ? 183 LEU   A C    1 
ATOM   1131 O  O    . LEU   A 1 183 ? 8.936  43.908 -1.764  1.00 38.19 ? 183 LEU   A O    1 
ATOM   1132 C  CB   . LEU   A 1 183 ? 6.305  42.748 -2.234  1.00 46.30 ? 183 LEU   A CB   1 
ATOM   1133 C  CG   . LEU   A 1 183 ? 5.124  41.836 -2.563  1.00 48.67 ? 183 LEU   A CG   1 
ATOM   1134 C  CD1  . LEU   A 1 183 ? 4.136  42.544 -3.477  1.00 48.96 ? 183 LEU   A CD1  1 
ATOM   1135 C  CD2  . LEU   A 1 183 ? 5.602  40.540 -3.200  1.00 49.20 ? 183 LEU   A CD2  1 
ATOM   1136 N  N    . TRP   A 1 184 ? 8.628  43.272 0.398   1.00 37.06 ? 184 TRP   A N    1 
ATOM   1137 C  CA   . TRP   A 1 184 ? 9.496  44.338 0.973   1.00 36.44 ? 184 TRP   A CA   1 
ATOM   1138 C  C    . TRP   A 1 184 ? 10.919 44.271 0.407   1.00 34.92 ? 184 TRP   A C    1 
ATOM   1139 O  O    . TRP   A 1 184 ? 11.617 45.293 0.473   1.00 34.68 ? 184 TRP   A O    1 
ATOM   1140 C  CB   . TRP   A 1 184 ? 9.503  44.228 2.500   1.00 37.31 ? 184 TRP   A CB   1 
ATOM   1141 C  CG   . TRP   A 1 184 ? 8.140  44.247 3.119   1.00 38.04 ? 184 TRP   A CG   1 
ATOM   1142 C  CD1  . TRP   A 1 184 ? 6.961  44.562 2.509   1.00 38.75 ? 184 TRP   A CD1  1 
ATOM   1143 C  CD2  . TRP   A 1 184 ? 7.808  43.889 4.471   1.00 38.28 ? 184 TRP   A CD2  1 
ATOM   1144 N  NE1  . TRP   A 1 184 ? 5.923  44.447 3.394   1.00 39.31 ? 184 TRP   A NE1  1 
ATOM   1145 C  CE2  . TRP   A 1 184 ? 6.411  44.034 4.604   1.00 38.82 ? 184 TRP   A CE2  1 
ATOM   1146 C  CE3  . TRP   A 1 184 ? 8.551  43.471 5.579   1.00 39.23 ? 184 TRP   A CE3  1 
ATOM   1147 C  CZ2  . TRP   A 1 184 ? 5.749  43.775 5.802   1.00 39.49 ? 184 TRP   A CZ2  1 
ATOM   1148 C  CZ3  . TRP   A 1 184 ? 7.896  43.215 6.763   1.00 39.73 ? 184 TRP   A CZ3  1 
ATOM   1149 C  CH2  . TRP   A 1 184 ? 6.514  43.367 6.870   1.00 39.91 ? 184 TRP   A CH2  1 
ATOM   1150 N  N    . TYR   A 1 185 ? 11.339 43.121 -0.114  1.00 34.07 ? 185 TYR   A N    1 
ATOM   1151 C  CA   . TYR   A 1 185 ? 12.720 42.937 -0.620  1.00 34.04 ? 185 TYR   A CA   1 
ATOM   1152 C  C    . TYR   A 1 185 ? 12.700 42.684 -2.130  1.00 34.93 ? 185 TYR   A C    1 
ATOM   1153 O  O    . TYR   A 1 185 ? 13.763 42.657 -2.735  1.00 35.16 ? 185 TYR   A O    1 
ATOM   1154 C  CB   . TYR   A 1 185 ? 13.383 41.811 0.177   1.00 33.35 ? 185 TYR   A CB   1 
ATOM   1155 C  CG   . TYR   A 1 185 ? 13.290 41.972 1.670   1.00 33.04 ? 185 TYR   A CG   1 
ATOM   1156 C  CD1  . TYR   A 1 185 ? 14.152 42.810 2.354   1.00 33.06 ? 185 TYR   A CD1  1 
ATOM   1157 C  CD2  . TYR   A 1 185 ? 12.302 41.329 2.393   1.00 34.60 ? 185 TYR   A CD2  1 
ATOM   1158 C  CE1  . TYR   A 1 185 ? 14.055 42.978 3.723   1.00 34.39 ? 185 TYR   A CE1  1 
ATOM   1159 C  CE2  . TYR   A 1 185 ? 12.187 41.490 3.762   1.00 35.14 ? 185 TYR   A CE2  1 
ATOM   1160 C  CZ   . TYR   A 1 185 ? 13.067 42.320 4.429   1.00 35.79 ? 185 TYR   A CZ   1 
ATOM   1161 O  OH   . TYR   A 1 185 ? 12.956 42.481 5.786   1.00 38.65 ? 185 TYR   A OH   1 
ATOM   1162 N  N    . ARG   A 1 186 ? 11.499 42.536 -2.695  1.00 36.27 ? 186 ARG   A N    1 
ATOM   1163 C  CA   . ARG   A 1 186 ? 11.343 42.275 -4.150  1.00 37.53 ? 186 ARG   A CA   1 
ATOM   1164 C  C    . ARG   A 1 186 ? 11.926 43.431 -4.961  1.00 38.45 ? 186 ARG   A C    1 
ATOM   1165 O  O    . ARG   A 1 186 ? 11.676 44.596 -4.608  1.00 39.30 ? 186 ARG   A O    1 
ATOM   1166 C  CB   . ARG   A 1 186 ? 9.870  42.080 -4.509  1.00 40.29 ? 186 ARG   A CB   1 
ATOM   1167 C  CG   . ARG   A 1 186 ? 9.220  40.857 -3.881  1.00 45.37 ? 186 ARG   A CG   1 
ATOM   1168 C  CD   . ARG   A 1 186 ? 9.510  39.560 -4.603  1.00 50.34 ? 186 ARG   A CD   1 
ATOM   1169 N  NE   . ARG   A 1 186 ? 8.764  38.478 -3.981  1.00 55.21 ? 186 ARG   A NE   1 
ATOM   1170 C  CZ   . ARG   A 1 186 ? 9.322  37.449 -3.359  1.00 59.54 ? 186 ARG   A CZ   1 
ATOM   1171 N  NH1  . ARG   A 1 186 ? 8.569  36.580 -2.709  1.00 59.55 ? 186 ARG   A NH1  1 
ATOM   1172 N  NH2  . ARG   A 1 186 ? 10.635 37.298 -3.382  1.00 61.05 ? 186 ARG   A NH2  1 
ATOM   1173 N  N    . ALA   A 1 187 ? 12.659 43.102 -6.020  1.00 38.60 ? 187 ALA   A N    1 
ATOM   1174 C  CA   . ALA   A 1 187 ? 13.280 44.129 -6.870  1.00 39.56 ? 187 ALA   A CA   1 
ATOM   1175 C  C    . ALA   A 1 187 ? 12.233 44.778 -7.778  1.00 40.61 ? 187 ALA   A C    1 
ATOM   1176 O  O    . ALA   A 1 187 ? 11.218 44.149 -8.085  1.00 40.17 ? 187 ALA   A O    1 
ATOM   1177 C  CB   . ALA   A 1 187 ? 14.401 43.519 -7.656  1.00 39.46 ? 187 ALA   A CB   1 
ATOM   1178 N  N    . PRO   A 1 188 ? 12.464 46.034 -8.186  1.00 41.81 ? 188 PRO   A N    1 
ATOM   1179 C  CA   . PRO   A 1 188 ? 11.540 46.744 -9.070  1.00 42.77 ? 188 PRO   A CA   1 
ATOM   1180 C  C    . PRO   A 1 188 ? 11.178 46.019 -10.386 1.00 43.50 ? 188 PRO   A C    1 
ATOM   1181 O  O    . PRO   A 1 188 ? 10.041 46.054 -10.745 1.00 43.53 ? 188 PRO   A O    1 
ATOM   1182 C  CB   . PRO   A 1 188 ? 12.313 48.051 -9.291  1.00 43.75 ? 188 PRO   A CB   1 
ATOM   1183 C  CG   . PRO   A 1 188 ? 13.743 47.756 -8.955  1.00 43.71 ? 188 PRO   A CG   1 
ATOM   1184 C  CD   . PRO   A 1 188 ? 13.618 46.826 -7.779  1.00 41.79 ? 188 PRO   A CD   1 
ATOM   1185 N  N    . GLU   A 1 189 ? 12.133 45.341 -11.019 1.00 43.66 ? 189 GLU   A N    1 
ATOM   1186 C  CA   . GLU   A 1 189 ? 11.902 44.605 -12.293 1.00 44.23 ? 189 GLU   A CA   1 
ATOM   1187 C  C    . GLU   A 1 189 ? 11.056 43.355 -12.031 1.00 44.67 ? 189 GLU   A C    1 
ATOM   1188 O  O    . GLU   A 1 189 ? 10.401 42.887 -12.976 1.00 44.72 ? 189 GLU   A O    1 
ATOM   1189 C  CB   . GLU   A 1 189 ? 13.228 44.236 -12.961 1.00 45.07 ? 189 GLU   A CB   1 
ATOM   1190 C  CG   . GLU   A 1 189 ? 14.133 43.354 -12.119 1.00 46.00 ? 189 GLU   A CG   1 
ATOM   1191 C  CD   . GLU   A 1 189 ? 15.079 44.099 -11.194 1.00 43.37 ? 189 GLU   A CD   1 
ATOM   1192 O  OE1  . GLU   A 1 189 ? 14.970 45.337 -11.110 1.00 42.44 ? 189 GLU   A OE1  1 
ATOM   1193 O  OE2  . GLU   A 1 189 ? 15.938 43.441 -10.582 1.00 42.01 ? 189 GLU   A OE2  1 
ATOM   1194 N  N    . VAL   A 1 190 ? 11.070 42.840 -10.799 1.00 44.63 ? 190 VAL   A N    1 
ATOM   1195 C  CA   . VAL   A 1 190 ? 10.224 41.688 -10.466 1.00 44.88 ? 190 VAL   A CA   1 
ATOM   1196 C  C    . VAL   A 1 190 ? 8.787  42.217 -10.236 1.00 45.61 ? 190 VAL   A C    1 
ATOM   1197 O  O    . VAL   A 1 190 ? 7.835  41.658 -10.791 1.00 46.15 ? 190 VAL   A O    1 
ATOM   1198 C  CB   . VAL   A 1 190 ? 10.794 40.851 -9.284  1.00 45.13 ? 190 VAL   A CB   1 
ATOM   1199 C  CG1  . VAL   A 1 190 ? 9.776  39.854 -8.740  1.00 45.09 ? 190 VAL   A CG1  1 
ATOM   1200 C  CG2  . VAL   A 1 190 ? 12.052 40.130 -9.711  1.00 45.34 ? 190 VAL   A CG2  1 
ATOM   1201 N  N    . LEU   A 1 191 ? 8.654  43.373 -9.538  1.00 45.41 ? 191 LEU   A N    1 
ATOM   1202 C  CA   . LEU   A 1 191 ? 7.373  44.034 -9.288  1.00 45.52 ? 191 LEU   A CA   1 
ATOM   1203 C  C    . LEU   A 1 191 ? 6.696  44.444 -10.606 1.00 46.67 ? 191 LEU   A C    1 
ATOM   1204 O  O    . LEU   A 1 191 ? 5.496  44.215 -10.775 1.00 46.41 ? 191 LEU   A O    1 
ATOM   1205 C  CB   . LEU   A 1 191 ? 7.562  45.258 -8.392  1.00 44.20 ? 191 LEU   A CB   1 
ATOM   1206 C  CG   . LEU   A 1 191 ? 8.098  44.986 -6.993  1.00 43.93 ? 191 LEU   A CG   1 
ATOM   1207 C  CD1  . LEU   A 1 191 ? 8.423  46.284 -6.289  1.00 43.11 ? 191 LEU   A CD1  1 
ATOM   1208 C  CD2  . LEU   A 1 191 ? 7.119  44.164 -6.183  1.00 44.03 ? 191 LEU   A CD2  1 
ATOM   1209 N  N    . LEU   A 1 192 ? 7.490  45.007 -11.543 1.00 47.43 ? 192 LEU   A N    1 
ATOM   1210 C  CA   . LEU   A 1 192 ? 7.047  45.443 -12.874 1.00 48.58 ? 192 LEU   A CA   1 
ATOM   1211 C  C    . LEU   A 1 192 ? 6.800  44.288 -13.849 1.00 51.06 ? 192 LEU   A C    1 
ATOM   1212 O  O    . LEU   A 1 192 ? 6.245  44.516 -14.922 1.00 51.08 ? 192 LEU   A O    1 
ATOM   1213 C  CB   . LEU   A 1 192 ? 8.067  46.406 -13.485 1.00 47.77 ? 192 LEU   A CB   1 
ATOM   1214 C  CG   . LEU   A 1 192 ? 8.093  47.775 -12.849 1.00 48.38 ? 192 LEU   A CG   1 
ATOM   1215 C  CD1  . LEU   A 1 192 ? 9.327  48.550 -13.256 1.00 48.19 ? 192 LEU   A CD1  1 
ATOM   1216 C  CD2  . LEU   A 1 192 ? 6.831  48.533 -13.181 1.00 49.07 ? 192 LEU   A CD2  1 
ATOM   1217 N  N    . GLN   A 1 193 ? 7.252  43.070 -13.480 1.00 52.75 ? 193 GLN   A N    1 
ATOM   1218 C  CA   . GLN   A 1 193 ? 7.204  41.823 -14.221 1.00 54.55 ? 193 GLN   A CA   1 
ATOM   1219 C  C    . GLN   A 1 193 ? 7.955  41.922 -15.532 1.00 55.83 ? 193 GLN   A C    1 
ATOM   1220 O  O    . GLN   A 1 193 ? 7.420  41.521 -16.561 1.00 56.16 ? 193 GLN   A O    1 
ATOM   1221 C  CB   . GLN   A 1 193 ? 5.764  41.300 -14.390 1.00 57.32 ? 193 GLN   A CB   1 
ATOM   1222 C  CG   . GLN   A 1 193 ? 5.102  41.009 -13.042 1.00 62.57 ? 193 GLN   A CG   1 
ATOM   1223 C  CD   . GLN   A 1 193 ? 3.780  40.291 -13.143 1.00 69.06 ? 193 GLN   A CD   1 
ATOM   1224 O  OE1  . GLN   A 1 193 ? 3.390  39.791 -14.202 1.00 72.51 ? 193 GLN   A OE1  1 
ATOM   1225 N  NE2  . GLN   A 1 193 ? 3.059  40.214 -12.028 1.00 69.09 ? 193 GLN   A NE2  1 
ATOM   1226 N  N    . SER   A 1 194 ? 9.205  42.436 -15.511 1.00 56.27 ? 194 SER   A N    1 
ATOM   1227 C  CA   . SER   A 1 194 ? 9.983  42.524 -16.750 1.00 57.24 ? 194 SER   A CA   1 
ATOM   1228 C  C    . SER   A 1 194 ? 11.138 41.516 -16.814 1.00 58.25 ? 194 SER   A C    1 
ATOM   1229 O  O    . SER   A 1 194 ? 11.173 40.714 -17.741 1.00 59.25 ? 194 SER   A O    1 
ATOM   1230 C  CB   . SER   A 1 194 ? 10.458 43.948 -17.023 1.00 58.53 ? 194 SER   A CB   1 
ATOM   1231 O  OG   . SER   A 1 194 ? 11.644 44.288 -16.328 1.00 61.79 ? 194 SER   A OG   1 
ATOM   1232 N  N    . SER   A 1 195 ? 12.059 41.518 -15.842 1.00 58.07 ? 195 SER   A N    1 
ATOM   1233 C  CA   . SER   A 1 195 ? 13.205 40.602 -15.864 1.00 58.23 ? 195 SER   A CA   1 
ATOM   1234 C  C    . SER   A 1 195 ? 13.414 39.891 -14.529 1.00 58.63 ? 195 SER   A C    1 
ATOM   1235 O  O    . SER   A 1 195 ? 12.969 40.392 -13.499 1.00 59.52 ? 195 SER   A O    1 
ATOM   1236 C  CB   . SER   A 1 195 ? 14.468 41.355 -16.260 1.00 59.52 ? 195 SER   A CB   1 
ATOM   1237 O  OG   . SER   A 1 195 ? 14.641 42.524 -15.477 1.00 61.13 ? 195 SER   A OG   1 
ATOM   1238 N  N    . TYR   A 1 196 ? 14.071 38.730 -14.547 1.00 57.86 ? 196 TYR   A N    1 
ATOM   1239 C  CA   . TYR   A 1 196 ? 14.235 37.942 -13.296 1.00 57.34 ? 196 TYR   A CA   1 
ATOM   1240 C  C    . TYR   A 1 196 ? 15.660 37.387 -13.233 1.00 54.33 ? 196 TYR   A C    1 
ATOM   1241 O  O    . TYR   A 1 196 ? 15.828 36.180 -13.000 1.00 54.82 ? 196 TYR   A O    1 
ATOM   1242 C  CB   . TYR   A 1 196 ? 13.172 36.843 -13.234 1.00 59.00 ? 196 TYR   A CB   1 
ATOM   1243 C  CG   . TYR   A 1 196 ? 11.770 37.340 -13.476 1.00 62.21 ? 196 TYR   A CG   1 
ATOM   1244 C  CD1  . TYR   A 1 196 ? 11.161 38.220 -12.598 1.00 63.91 ? 196 TYR   A CD1  1 
ATOM   1245 C  CD2  . TYR   A 1 196 ? 11.063 36.961 -14.605 1.00 64.17 ? 196 TYR   A CD2  1 
ATOM   1246 C  CE1  . TYR   A 1 196 ? 9.879  38.694 -12.820 1.00 65.17 ? 196 TYR   A CE1  1 
ATOM   1247 C  CE2  . TYR   A 1 196 ? 9.780  37.425 -14.843 1.00 65.36 ? 196 TYR   A CE2  1 
ATOM   1248 C  CZ   . TYR   A 1 196 ? 9.185  38.295 -13.947 1.00 66.39 ? 196 TYR   A CZ   1 
ATOM   1249 O  OH   . TYR   A 1 196 ? 7.913  38.757 -14.177 1.00 68.11 ? 196 TYR   A OH   1 
ATOM   1250 N  N    . ALA   A 1 197 ? 16.653 38.254 -13.425 1.00 51.03 ? 197 ALA   A N    1 
ATOM   1251 C  CA   . ALA   A 1 197 ? 18.061 37.798 -13.444 1.00 48.19 ? 197 ALA   A CA   1 
ATOM   1252 C  C    . ALA   A 1 197 ? 18.695 37.916 -12.054 1.00 44.79 ? 197 ALA   A C    1 
ATOM   1253 O  O    . ALA   A 1 197 ? 17.959 38.166 -11.087 1.00 43.60 ? 197 ALA   A O    1 
ATOM   1254 C  CB   . ALA   A 1 197 ? 18.834 38.581 -14.471 1.00 48.44 ? 197 ALA   A CB   1 
ATOM   1255 N  N    . THR   A 1 198 ? 20.016 37.751 -11.975 1.00 42.73 ? 198 THR   A N    1 
ATOM   1256 C  CA   . THR   A 1 198 ? 20.742 37.787 -10.676 1.00 40.95 ? 198 THR   A CA   1 
ATOM   1257 C  C    . THR   A 1 198 ? 20.604 39.147 -9.971  1.00 38.63 ? 198 THR   A C    1 
ATOM   1258 O  O    . THR   A 1 198 ? 20.568 39.134 -8.729  1.00 38.27 ? 198 THR   A O    1 
ATOM   1259 C  CB   . THR   A 1 198 ? 22.208 37.382 -10.881 1.00 42.22 ? 198 THR   A CB   1 
ATOM   1260 O  OG1  . THR   A 1 198 ? 22.825 38.321 -11.762 1.00 43.24 ? 198 THR   A OG1  1 
ATOM   1261 C  CG2  . THR   A 1 198 ? 22.354 35.984 -11.440 1.00 42.42 ? 198 THR   A CG2  1 
ATOM   1262 N  N    . PRO   A 1 199 ? 20.557 40.310 -10.664 1.00 36.42 ? 199 PRO   A N    1 
ATOM   1263 C  CA   . PRO   A 1 199 ? 20.502 41.612 -9.985  1.00 35.15 ? 199 PRO   A CA   1 
ATOM   1264 C  C    . PRO   A 1 199 ? 19.336 41.690 -8.993  1.00 34.94 ? 199 PRO   A C    1 
ATOM   1265 O  O    . PRO   A 1 199 ? 19.402 42.483 -8.078  1.00 34.38 ? 199 PRO   A O    1 
ATOM   1266 C  CB   . PRO   A 1 199 ? 20.280 42.597 -11.137 1.00 35.76 ? 199 PRO   A CB   1 
ATOM   1267 C  CG   . PRO   A 1 199 ? 20.933 41.927 -12.317 1.00 36.08 ? 199 PRO   A CG   1 
ATOM   1268 C  CD   . PRO   A 1 199 ? 20.616 40.461 -12.121 1.00 35.22 ? 199 PRO   A CD   1 
ATOM   1269 N  N    . VAL   A 1 200 ? 18.311 40.868 -9.200  1.00 34.73 ? 200 VAL   A N    1 
ATOM   1270 C  CA   . VAL   A 1 200 ? 17.133 40.826 -8.290  1.00 34.62 ? 200 VAL   A CA   1 
ATOM   1271 C  C    . VAL   A 1 200 ? 17.611 40.592 -6.853  1.00 34.89 ? 200 VAL   A C    1 
ATOM   1272 O  O    . VAL   A 1 200 ? 17.104 41.278 -5.945  1.00 35.15 ? 200 VAL   A O    1 
ATOM   1273 C  CB   . VAL   A 1 200 ? 16.184 39.712 -8.771  1.00 35.46 ? 200 VAL   A CB   1 
ATOM   1274 C  CG1  . VAL   A 1 200 ? 15.228 39.232 -7.695  1.00 36.57 ? 200 VAL   A CG1  1 
ATOM   1275 C  CG2  . VAL   A 1 200 ? 15.442 40.099 -10.041 1.00 35.62 ? 200 VAL   A CG2  1 
ATOM   1276 N  N    . ASP   A 1 201 ? 18.564 39.680 -6.661  1.00 34.54 ? 201 ASP   A N    1 
ATOM   1277 C  CA   . ASP   A 1 201 ? 19.060 39.327 -5.303  1.00 33.85 ? 201 ASP   A CA   1 
ATOM   1278 C  C    . ASP   A 1 201 ? 19.875 40.483 -4.711  1.00 33.74 ? 201 ASP   A C    1 
ATOM   1279 O  O    . ASP   A 1 201 ? 19.855 40.640 -3.478  1.00 32.39 ? 201 ASP   A O    1 
ATOM   1280 C  CB   . ASP   A 1 201 ? 19.852 38.019 -5.355  1.00 33.97 ? 201 ASP   A CB   1 
ATOM   1281 C  CG   . ASP   A 1 201 ? 19.010 36.806 -5.706  1.00 37.71 ? 201 ASP   A CG   1 
ATOM   1282 O  OD1  . ASP   A 1 201 ? 17.776 36.947 -5.764  1.00 37.99 ? 201 ASP   A OD1  1 
ATOM   1283 O  OD2  . ASP   A 1 201 ? 19.601 35.737 -5.941  1.00 40.72 ? 201 ASP   A OD2  1 
ATOM   1284 N  N    . LEU   A 1 202 ? 20.579 41.242 -5.556  1.00 34.00 ? 202 LEU   A N    1 
ATOM   1285 C  CA   . LEU   A 1 202 ? 21.422 42.369 -5.075  1.00 35.38 ? 202 LEU   A CA   1 
ATOM   1286 C  C    . LEU   A 1 202 ? 20.526 43.498 -4.554  1.00 36.81 ? 202 LEU   A C    1 
ATOM   1287 O  O    . LEU   A 1 202 ? 20.951 44.197 -3.620  1.00 37.71 ? 202 LEU   A O    1 
ATOM   1288 C  CB   . LEU   A 1 202 ? 22.333 42.841 -6.212  1.00 36.01 ? 202 LEU   A CB   1 
ATOM   1289 C  CG   . LEU   A 1 202 ? 23.710 42.182 -6.264  1.00 37.85 ? 202 LEU   A CG   1 
ATOM   1290 C  CD1  . LEU   A 1 202 ? 24.409 42.289 -4.919  1.00 37.50 ? 202 LEU   A CD1  1 
ATOM   1291 C  CD2  . LEU   A 1 202 ? 23.600 40.727 -6.692  1.00 38.82 ? 202 LEU   A CD2  1 
ATOM   1292 N  N    . TRP   A 1 203 ? 19.340 43.673 -5.140  1.00 36.26 ? 203 TRP   A N    1 
ATOM   1293 C  CA   . TRP   A 1 203 ? 18.386 44.679 -4.608  1.00 35.82 ? 203 TRP   A CA   1 
ATOM   1294 C  C    . TRP   A 1 203 ? 17.957 44.240 -3.208  1.00 34.87 ? 203 TRP   A C    1 
ATOM   1295 O  O    . TRP   A 1 203 ? 17.945 45.086 -2.301  1.00 34.70 ? 203 TRP   A O    1 
ATOM   1296 C  CB   . TRP   A 1 203 ? 17.182 44.837 -5.542  1.00 35.58 ? 203 TRP   A CB   1 
ATOM   1297 C  CG   . TRP   A 1 203 ? 16.152 45.790 -5.023  1.00 36.87 ? 203 TRP   A CG   1 
ATOM   1298 C  CD1  . TRP   A 1 203 ? 15.176 45.531 -4.105  1.00 38.30 ? 203 TRP   A CD1  1 
ATOM   1299 C  CD2  . TRP   A 1 203 ? 16.023 47.181 -5.363  1.00 37.32 ? 203 TRP   A CD2  1 
ATOM   1300 N  NE1  . TRP   A 1 203 ? 14.437 46.657 -3.867  1.00 38.49 ? 203 TRP   A NE1  1 
ATOM   1301 C  CE2  . TRP   A 1 203 ? 14.934 47.686 -4.622  1.00 38.12 ? 203 TRP   A CE2  1 
ATOM   1302 C  CE3  . TRP   A 1 203 ? 16.712 48.042 -6.223  1.00 38.06 ? 203 TRP   A CE3  1 
ATOM   1303 C  CZ2  . TRP   A 1 203 ? 14.523 49.013 -4.719  1.00 38.78 ? 203 TRP   A CZ2  1 
ATOM   1304 C  CZ3  . TRP   A 1 203 ? 16.303 49.352 -6.320  1.00 39.05 ? 203 TRP   A CZ3  1 
ATOM   1305 C  CH2  . TRP   A 1 203 ? 15.225 49.829 -5.576  1.00 38.87 ? 203 TRP   A CH2  1 
ATOM   1306 N  N    . SER   A 1 204 ? 17.635 42.957 -3.052  1.00 34.21 ? 204 SER   A N    1 
ATOM   1307 C  CA   . SER   A 1 204 ? 17.235 42.419 -1.728  1.00 35.11 ? 204 SER   A CA   1 
ATOM   1308 C  C    . SER   A 1 204 ? 18.373 42.635 -0.725  1.00 36.30 ? 204 SER   A C    1 
ATOM   1309 O  O    . SER   A 1 204 ? 18.076 42.965 0.433   1.00 37.24 ? 204 SER   A O    1 
ATOM   1310 C  CB   . SER   A 1 204 ? 16.854 40.969 -1.844  1.00 36.51 ? 204 SER   A CB   1 
ATOM   1311 O  OG   . SER   A 1 204 ? 15.835 40.789 -2.815  1.00 38.49 ? 204 SER   A OG   1 
ATOM   1312 N  N    . VAL   A 1 205 ? 19.623 42.473 -1.165  1.00 36.51 ? 205 VAL   A N    1 
ATOM   1313 C  CA   . VAL   A 1 205 ? 20.805 42.687 -0.279  1.00 37.23 ? 205 VAL   A CA   1 
ATOM   1314 C  C    . VAL   A 1 205 ? 20.849 44.156 0.156   1.00 36.79 ? 205 VAL   A C    1 
ATOM   1315 O  O    . VAL   A 1 205 ? 21.092 44.399 1.348   1.00 36.57 ? 205 VAL   A O    1 
ATOM   1316 C  CB   . VAL   A 1 205 ? 22.109 42.246 -0.973  1.00 38.81 ? 205 VAL   A CB   1 
ATOM   1317 C  CG1  . VAL   A 1 205 ? 23.331 42.941 -0.396  1.00 39.41 ? 205 VAL   A CG1  1 
ATOM   1318 C  CG2  . VAL   A 1 205 ? 22.280 40.737 -0.939  1.00 39.80 ? 205 VAL   A CG2  1 
ATOM   1319 N  N    . GLY   A 1 206 ? 20.625 45.092 -0.770  1.00 36.80 ? 206 GLY   A N    1 
ATOM   1320 C  CA   . GLY   A 1 206 ? 20.576 46.508 -0.421  1.00 36.97 ? 206 GLY   A CA   1 
ATOM   1321 C  C    . GLY   A 1 206 ? 19.494 46.799 0.602   1.00 37.52 ? 206 GLY   A C    1 
ATOM   1322 O  O    . GLY   A 1 206 ? 19.701 47.563 1.541   1.00 38.22 ? 206 GLY   A O    1 
ATOM   1323 N  N    . CYS   A 1 207 ? 18.339 46.151 0.456   1.00 37.16 ? 207 CYS   A N    1 
ATOM   1324 C  CA   . CYS   A 1 207 ? 17.223 46.270 1.396   1.00 36.71 ? 207 CYS   A CA   1 
ATOM   1325 C  C    . CYS   A 1 207 ? 17.597 45.747 2.763   1.00 36.63 ? 207 CYS   A C    1 
ATOM   1326 O  O    . CYS   A 1 207 ? 17.114 46.272 3.768   1.00 36.33 ? 207 CYS   A O    1 
ATOM   1327 C  CB   . CYS   A 1 207 ? 16.002 45.527 0.864   1.00 36.83 ? 207 CYS   A CB   1 
ATOM   1328 S  SG   . CYS   A 1 207 ? 15.226 46.317 -0.560  1.00 37.86 ? 207 CYS   A SG   1 
ATOM   1329 N  N    . ILE   A 1 208 ? 18.348 44.632 2.792   1.00 36.53 ? 208 ILE   A N    1 
ATOM   1330 C  CA   . ILE   A 1 208 ? 18.799 43.933 4.003   1.00 36.28 ? 208 ILE   A CA   1 
ATOM   1331 C  C    . ILE   A 1 208 ? 19.899 44.722 4.713   1.00 36.93 ? 208 ILE   A C    1 
ATOM   1332 O  O    . ILE   A 1 208 ? 19.843 44.886 5.920   1.00 37.61 ? 208 ILE   A O    1 
ATOM   1333 C  CB   . ILE   A 1 208 ? 19.197 42.474 3.634   1.00 35.51 ? 208 ILE   A CB   1 
ATOM   1334 C  CG1  . ILE   A 1 208 ? 17.920 41.663 3.331   1.00 35.59 ? 208 ILE   A CG1  1 
ATOM   1335 C  CG2  . ILE   A 1 208 ? 19.999 41.820 4.764   1.00 36.24 ? 208 ILE   A CG2  1 
ATOM   1336 C  CD1  . ILE   A 1 208 ? 18.078 40.430 2.421   1.00 36.37 ? 208 ILE   A CD1  1 
ATOM   1337 N  N    . PHE   A 1 209 ? 20.856 45.262 3.955   1.00 37.51 ? 209 PHE   A N    1 
ATOM   1338 C  CA   . PHE   A 1 209 ? 21.949 46.125 4.396   1.00 38.44 ? 209 PHE   A CA   1 
ATOM   1339 C  C    . PHE   A 1 209 ? 21.363 47.326 5.142   1.00 39.71 ? 209 PHE   A C    1 
ATOM   1340 O  O    . PHE   A 1 209 ? 21.758 47.578 6.296   1.00 40.55 ? 209 PHE   A O    1 
ATOM   1341 C  CB   . PHE   A 1 209 ? 22.750 46.585 3.163   1.00 38.40 ? 209 PHE   A CB   1 
ATOM   1342 C  CG   . PHE   A 1 209 ? 24.022 47.345 3.444   1.00 39.50 ? 209 PHE   A CG   1 
ATOM   1343 C  CD1  . PHE   A 1 209 ? 24.746 47.114 4.605   1.00 41.15 ? 209 PHE   A CD1  1 
ATOM   1344 C  CD2  . PHE   A 1 209 ? 24.508 48.273 2.540   1.00 39.94 ? 209 PHE   A CD2  1 
ATOM   1345 C  CE1  . PHE   A 1 209 ? 25.937 47.797 4.849   1.00 41.84 ? 209 PHE   A CE1  1 
ATOM   1346 C  CE2  . PHE   A 1 209 ? 25.710 48.928 2.771   1.00 40.81 ? 209 PHE   A CE2  1 
ATOM   1347 C  CZ   . PHE   A 1 209 ? 26.405 48.704 3.936   1.00 41.23 ? 209 PHE   A CZ   1 
ATOM   1348 N  N    . ALA   A 1 210 ? 20.343 47.996 4.537   1.00 39.36 ? 210 ALA   A N    1 
ATOM   1349 C  CA   . ALA   A 1 210 ? 19.658 49.135 5.155   1.00 39.31 ? 210 ALA   A CA   1 
ATOM   1350 C  C    . ALA   A 1 210 ? 19.001 48.731 6.464   1.00 38.81 ? 210 ALA   A C    1 
ATOM   1351 O  O    . ALA   A 1 210 ? 19.153 49.438 7.446   1.00 39.51 ? 210 ALA   A O    1 
ATOM   1352 C  CB   . ALA   A 1 210 ? 18.611 49.715 4.200   1.00 39.85 ? 210 ALA   A CB   1 
ATOM   1353 N  N    . GLU   A 1 211 ? 18.307 47.582 6.486   1.00 37.46 ? 211 GLU   A N    1 
ATOM   1354 C  CA   . GLU   A 1 211 ? 17.614 47.020 7.632   1.00 36.74 ? 211 GLU   A CA   1 
ATOM   1355 C  C    . GLU   A 1 211 ? 18.554 46.585 8.766   1.00 38.88 ? 211 GLU   A C    1 
ATOM   1356 O  O    . GLU   A 1 211 ? 18.125 46.491 9.926   1.00 38.77 ? 211 GLU   A O    1 
ATOM   1357 C  CB   . GLU   A 1 211 ? 16.731 45.860 7.167   1.00 35.06 ? 211 GLU   A CB   1 
ATOM   1358 C  CG   . GLU   A 1 211 ? 15.852 45.261 8.240   1.00 32.51 ? 211 GLU   A CG   1 
ATOM   1359 C  CD   . GLU   A 1 211 ? 14.739 44.373 7.736   1.00 39.37 ? 211 GLU   A CD   1 
ATOM   1360 O  OE1  . GLU   A 1 211 ? 14.485 44.362 6.507   1.00 39.83 ? 211 GLU   A OE1  1 
ATOM   1361 O  OE2  . GLU   A 1 211 ? 14.104 43.693 8.574   1.00 42.43 ? 211 GLU   A OE2  1 
ATOM   1362 N  N    . MET   A 1 212 ? 19.827 46.316 8.457   1.00 40.05 ? 212 MET   A N    1 
ATOM   1363 C  CA   . MET   A 1 212 ? 20.785 45.967 9.503   1.00 41.76 ? 212 MET   A CA   1 
ATOM   1364 C  C    . MET   A 1 212 ? 21.062 47.191 10.405  1.00 43.22 ? 212 MET   A C    1 
ATOM   1365 O  O    . MET   A 1 212 ? 21.276 47.034 11.617  1.00 42.63 ? 212 MET   A O    1 
ATOM   1366 C  CB   . MET   A 1 212 ? 22.062 45.374 8.907   1.00 43.02 ? 212 MET   A CB   1 
ATOM   1367 C  CG   . MET   A 1 212 ? 21.919 43.890 8.551   1.00 46.20 ? 212 MET   A CG   1 
ATOM   1368 S  SD   . MET   A 1 212 ? 23.470 43.296 7.886   1.00 60.43 ? 212 MET   A SD   1 
ATOM   1369 C  CE   . MET   A 1 212 ? 22.965 41.741 7.113   1.00 58.95 ? 212 MET   A CE   1 
ATOM   1370 N  N    . PHE   A 1 213 ? 20.996 48.418 9.823   1.00 43.83 ? 213 PHE   A N    1 
ATOM   1371 C  CA   . PHE   A 1 213 ? 21.183 49.648 10.576  1.00 44.73 ? 213 PHE   A CA   1 
ATOM   1372 C  C    . PHE   A 1 213 ? 19.856 50.035 11.247  1.00 45.66 ? 213 PHE   A C    1 
ATOM   1373 O  O    . PHE   A 1 213 ? 19.811 50.311 12.450  1.00 45.91 ? 213 PHE   A O    1 
ATOM   1374 C  CB   . PHE   A 1 213 ? 21.642 50.779 9.635   1.00 44.93 ? 213 PHE   A CB   1 
ATOM   1375 C  CG   . PHE   A 1 213 ? 23.049 50.672 9.107   1.00 46.18 ? 213 PHE   A CG   1 
ATOM   1376 C  CD1  . PHE   A 1 213 ? 23.314 50.000 7.930   1.00 46.94 ? 213 PHE   A CD1  1 
ATOM   1377 C  CD2  . PHE   A 1 213 ? 24.107 51.256 9.782   1.00 47.42 ? 213 PHE   A CD2  1 
ATOM   1378 C  CE1  . PHE   A 1 213 ? 24.613 49.875 7.461   1.00 47.80 ? 213 PHE   A CE1  1 
ATOM   1379 C  CE2  . PHE   A 1 213 ? 25.406 51.148 9.297   1.00 47.99 ? 213 PHE   A CE2  1 
ATOM   1380 C  CZ   . PHE   A 1 213 ? 25.650 50.452 8.145   1.00 47.75 ? 213 PHE   A CZ   1 
ATOM   1381 N  N    . ARG   A 1 214 ? 18.768 50.061 10.452  1.00 45.96 ? 214 ARG   A N    1 
ATOM   1382 C  CA   . ARG   A 1 214 ? 17.435 50.464 10.890  1.00 45.95 ? 214 ARG   A CA   1 
ATOM   1383 C  C    . ARG   A 1 214 ? 16.782 49.555 11.907  1.00 46.81 ? 214 ARG   A C    1 
ATOM   1384 O  O    . ARG   A 1 214 ? 16.022 50.027 12.763  1.00 47.60 ? 214 ARG   A O    1 
ATOM   1385 C  CB   . ARG   A 1 214 ? 16.505 50.553 9.681   1.00 46.06 ? 214 ARG   A CB   1 
ATOM   1386 C  CG   . ARG   A 1 214 ? 16.886 51.628 8.707   1.00 48.79 ? 214 ARG   A CG   1 
ATOM   1387 C  CD   . ARG   A 1 214 ? 16.169 51.480 7.370   1.00 51.80 ? 214 ARG   A CD   1 
ATOM   1388 N  NE   . ARG   A 1 214 ? 14.722 51.276 7.497   1.00 53.63 ? 214 ARG   A NE   1 
ATOM   1389 C  CZ   . ARG   A 1 214 ? 13.835 52.250 7.664   1.00 54.32 ? 214 ARG   A CZ   1 
ATOM   1390 N  NH1  . ARG   A 1 214 ? 14.233 53.513 7.756   1.00 53.60 ? 214 ARG   A NH1  1 
ATOM   1391 N  NH2  . ARG   A 1 214 ? 12.545 51.969 7.756   1.00 53.86 ? 214 ARG   A NH2  1 
ATOM   1392 N  N    . ARG   A 1 215 ? 16.993 48.256 11.767  1.00 46.64 ? 215 ARG   A N    1 
ATOM   1393 C  CA   . ARG   A 1 215 ? 16.301 47.241 12.564  1.00 47.44 ? 215 ARG   A CA   1 
ATOM   1394 C  C    . ARG   A 1 215 ? 14.771 47.235 12.301  1.00 47.33 ? 215 ARG   A C    1 
ATOM   1395 O  O    . ARG   A 1 215 ? 13.983 46.864 13.162  1.00 47.38 ? 215 ARG   A O    1 
ATOM   1396 C  CB   . ARG   A 1 215 ? 16.631 47.309 14.052  1.00 49.06 ? 215 ARG   A CB   1 
ATOM   1397 C  CG   . ARG   A 1 215 ? 17.886 46.543 14.407  1.00 53.03 ? 215 ARG   A CG   1 
ATOM   1398 C  CD   . ARG   A 1 215 ? 18.082 46.550 15.894  1.00 57.99 ? 215 ARG   A CD   1 
ATOM   1399 N  NE   . ARG   A 1 215 ? 18.180 47.917 16.402  1.00 62.15 ? 215 ARG   A NE   1 
ATOM   1400 C  CZ   . ARG   A 1 215 ? 18.311 48.238 17.681  1.00 64.89 ? 215 ARG   A CZ   1 
ATOM   1401 N  NH1  . ARG   A 1 215 ? 18.372 47.290 18.610  1.00 64.83 ? 215 ARG   A NH1  1 
ATOM   1402 N  NH2  . ARG   A 1 215 ? 18.405 49.509 18.042  1.00 65.19 ? 215 ARG   A NH2  1 
ATOM   1403 N  N    . LYS   A 1 216 ? 14.383 47.659 11.095  1.00 46.86 ? 216 LYS   A N    1 
ATOM   1404 C  CA   . LYS   A 1 216 ? 13.034 47.656 10.545  1.00 46.93 ? 216 LYS   A CA   1 
ATOM   1405 C  C    . LYS   A 1 216 ? 13.183 47.752 9.024   1.00 45.76 ? 216 LYS   A C    1 
ATOM   1406 O  O    . LYS   A 1 216 ? 14.112 48.394 8.532   1.00 45.28 ? 216 LYS   A O    1 
ATOM   1407 C  CB   . LYS   A 1 216 ? 12.146 48.778 11.127  1.00 49.34 ? 216 LYS   A CB   1 
ATOM   1408 C  CG   . LYS   A 1 216 ? 12.584 50.192 10.798  1.00 54.55 ? 216 LYS   A CG   1 
ATOM   1409 C  CD   . LYS   A 1 216 ? 12.174 51.146 11.924  1.00 60.66 ? 216 LYS   A CD   1 
ATOM   1410 C  CE   . LYS   A 1 216 ? 12.637 52.561 11.656  1.00 65.76 ? 216 LYS   A CE   1 
ATOM   1411 N  NZ   . LYS   A 1 216 ? 11.825 53.233 10.597  1.00 68.32 ? 216 LYS   A NZ   1 
ATOM   1412 N  N    . PRO   A 1 217 ? 12.321 47.069 8.259   1.00 45.87 ? 217 PRO   A N    1 
ATOM   1413 C  CA   . PRO   A 1 217 ? 12.440 47.120 6.795   1.00 46.12 ? 217 PRO   A CA   1 
ATOM   1414 C  C    . PRO   A 1 217 ? 12.482 48.522 6.174   1.00 47.43 ? 217 PRO   A C    1 
ATOM   1415 O  O    . PRO   A 1 217 ? 11.879 49.471 6.701   1.00 48.25 ? 217 PRO   A O    1 
ATOM   1416 C  CB   . PRO   A 1 217 ? 11.232 46.318 6.313   1.00 46.56 ? 217 PRO   A CB   1 
ATOM   1417 C  CG   . PRO   A 1 217 ? 10.868 45.458 7.439   1.00 46.93 ? 217 PRO   A CG   1 
ATOM   1418 C  CD   . PRO   A 1 217 ? 11.192 46.216 8.679   1.00 45.51 ? 217 PRO   A CD   1 
ATOM   1419 N  N    . LEU   A 1 218 ? 13.220 48.659 5.064   1.00 47.45 ? 218 LEU   A N    1 
ATOM   1420 C  CA   . LEU   A 1 218 ? 13.342 49.929 4.367   1.00 48.13 ? 218 LEU   A CA   1 
ATOM   1421 C  C    . LEU   A 1 218 ? 12.072 50.280 3.580   1.00 48.48 ? 218 LEU   A C    1 
ATOM   1422 O  O    . LEU   A 1 218 ? 11.557 51.383 3.710   1.00 49.07 ? 218 LEU   A O    1 
ATOM   1423 C  CB   . LEU   A 1 218 ? 14.570 49.921 3.437   1.00 48.30 ? 218 LEU   A CB   1 
ATOM   1424 C  CG   . LEU   A 1 218 ? 14.892 51.262 2.761   1.00 49.63 ? 218 LEU   A CG   1 
ATOM   1425 C  CD1  . LEU   A 1 218 ? 15.132 52.375 3.782   1.00 49.73 ? 218 LEU   A CD1  1 
ATOM   1426 C  CD2  . LEU   A 1 218 ? 16.108 51.148 1.907   1.00 50.53 ? 218 LEU   A CD2  1 
ATOM   1427 N  N    . PHE   A 1 219 ? 11.551 49.338 2.793   1.00 48.18 ? 219 PHE   A N    1 
ATOM   1428 C  CA   . PHE   A 1 219 ? 10.380 49.570 1.959   1.00 48.27 ? 219 PHE   A CA   1 
ATOM   1429 C  C    . PHE   A 1 219 ? 9.253  48.606 2.346   1.00 50.00 ? 219 PHE   A C    1 
ATOM   1430 O  O    . PHE   A 1 219 ? 9.218  47.497 1.837   1.00 50.16 ? 219 PHE   A O    1 
ATOM   1431 C  CB   . PHE   A 1 219 ? 10.766 49.352 0.497   1.00 46.87 ? 219 PHE   A CB   1 
ATOM   1432 C  CG   . PHE   A 1 219 ? 11.942 50.153 -0.004  1.00 46.57 ? 219 PHE   A CG   1 
ATOM   1433 C  CD1  . PHE   A 1 219 ? 11.892 51.537 -0.048  1.00 47.25 ? 219 PHE   A CD1  1 
ATOM   1434 C  CD2  . PHE   A 1 219 ? 13.079 49.524 -0.478  1.00 46.66 ? 219 PHE   A CD2  1 
ATOM   1435 C  CE1  . PHE   A 1 219 ? 12.959 52.273 -0.555  1.00 47.67 ? 219 PHE   A CE1  1 
ATOM   1436 C  CE2  . PHE   A 1 219 ? 14.138 50.261 -0.997  1.00 47.24 ? 219 PHE   A CE2  1 
ATOM   1437 C  CZ   . PHE   A 1 219 ? 14.070 51.632 -1.040  1.00 47.02 ? 219 PHE   A CZ   1 
ATOM   1438 N  N    . ARG   A 1 220 ? 8.327  49.023 3.231   1.00 51.00 ? 220 ARG   A N    1 
ATOM   1439 C  CA   . ARG   A 1 220 ? 7.249  48.152 3.717   1.00 51.95 ? 220 ARG   A CA   1 
ATOM   1440 C  C    . ARG   A 1 220 ? 5.896  48.302 2.951   1.00 52.08 ? 220 ARG   A C    1 
ATOM   1441 O  O    . ARG   A 1 220 ? 4.861  48.608 3.545   1.00 53.53 ? 220 ARG   A O    1 
ATOM   1442 C  CB   . ARG   A 1 220 ? 7.071  48.362 5.240   1.00 54.26 ? 220 ARG   A CB   1 
ATOM   1443 C  CG   . ARG   A 1 220 ? 6.295  47.260 5.963   1.00 59.54 ? 220 ARG   A CG   1 
ATOM   1444 C  CD   . ARG   A 1 220 ? 6.622  47.125 7.455   1.00 65.60 ? 220 ARG   A CD   1 
ATOM   1445 N  NE   . ARG   A 1 220 ? 6.599  48.393 8.198   1.00 71.48 ? 220 ARG   A NE   1 
ATOM   1446 C  CZ   . ARG   A 1 220 ? 5.519  48.902 8.794   1.00 74.96 ? 220 ARG   A CZ   1 
ATOM   1447 N  NH1  . ARG   A 1 220 ? 4.350  48.277 8.714   1.00 74.78 ? 220 ARG   A NH1  1 
ATOM   1448 N  NH2  . ARG   A 1 220 ? 5.599  50.047 9.462   1.00 74.86 ? 220 ARG   A NH2  1 
ATOM   1449 N  N    . GLY   A 1 221 ? 5.905  48.044 1.655   1.00 50.72 ? 221 GLY   A N    1 
ATOM   1450 C  CA   . GLY   A 1 221 ? 4.701  48.096 0.832   1.00 50.31 ? 221 GLY   A CA   1 
ATOM   1451 C  C    . GLY   A 1 221 ? 3.713  46.993 1.155   1.00 50.04 ? 221 GLY   A C    1 
ATOM   1452 O  O    . GLY   A 1 221 ? 4.043  46.041 1.846   1.00 50.57 ? 221 GLY   A O    1 
ATOM   1453 N  N    . SER   A 1 222 ? 2.490  47.112 0.678   1.00 49.54 ? 222 SER   A N    1 
ATOM   1454 C  CA   . SER   A 1 222 ? 1.414  46.146 0.966   1.00 49.08 ? 222 SER   A CA   1 
ATOM   1455 C  C    . SER   A 1 222 ? 0.826  45.470 -0.297  1.00 48.44 ? 222 SER   A C    1 
ATOM   1456 O  O    . SER   A 1 222 ? -0.148 44.727 -0.197  1.00 48.44 ? 222 SER   A O    1 
ATOM   1457 C  CB   . SER   A 1 222 ? 0.277  46.862 1.691   1.00 49.56 ? 222 SER   A CB   1 
ATOM   1458 O  OG   . SER   A 1 222 ? -0.191 47.923 0.875   1.00 51.00 ? 222 SER   A OG   1 
ATOM   1459 N  N    . SER   A 1 223 ? 1.401  45.755 -1.464  1.00 47.79 ? 223 SER   A N    1 
ATOM   1460 C  CA   . SER   A 1 223 ? 1.001  45.270 -2.782  1.00 47.77 ? 223 SER   A CA   1 
ATOM   1461 C  C    . SER   A 1 223 ? 2.159  45.580 -3.739  1.00 47.83 ? 223 SER   A C    1 
ATOM   1462 O  O    . SER   A 1 223 ? 3.062  46.320 -3.360  1.00 47.27 ? 223 SER   A O    1 
ATOM   1463 C  CB   . SER   A 1 223 ? -0.262 45.992 -3.245  1.00 49.27 ? 223 SER   A CB   1 
ATOM   1464 O  OG   . SER   A 1 223 ? 0.000  47.343 -3.598  1.00 51.90 ? 223 SER   A OG   1 
ATOM   1465 N  N    . ASP   A 1 224 ? 2.145  45.038 -4.962  1.00 48.69 ? 224 ASP   A N    1 
ATOM   1466 C  CA   . ASP   A 1 224 ? 3.227  45.305 -5.917  1.00 50.46 ? 224 ASP   A CA   1 
ATOM   1467 C  C    . ASP   A 1 224 ? 3.310  46.793 -6.299  1.00 51.00 ? 224 ASP   A C    1 
ATOM   1468 O  O    . ASP   A 1 224 ? 4.415  47.362 -6.370  1.00 50.65 ? 224 ASP   A O    1 
ATOM   1469 C  CB   . ASP   A 1 224 ? 3.172  44.383 -7.157  1.00 53.58 ? 224 ASP   A CB   1 
ATOM   1470 C  CG   . ASP   A 1 224 ? 1.837  44.279 -7.882  1.00 62.49 ? 224 ASP   A CG   1 
ATOM   1471 O  OD1  . ASP   A 1 224 ? 0.803  44.677 -7.294  1.00 63.90 ? 224 ASP   A OD1  1 
ATOM   1472 O  OD2  . ASP   A 1 224 ? 1.823  43.790 -9.048  1.00 67.05 ? 224 ASP   A OD2  1 
ATOM   1473 N  N    . VAL   A 1 225 ? 2.136  47.435 -6.477  1.00 51.11 ? 225 VAL   A N    1 
ATOM   1474 C  CA   . VAL   A 1 225 ? 2.085  48.841 -6.855  1.00 50.99 ? 225 VAL   A CA   1 
ATOM   1475 C  C    . VAL   A 1 225 ? 2.432  49.731 -5.673  1.00 50.57 ? 225 VAL   A C    1 
ATOM   1476 O  O    . VAL   A 1 225 ? 3.168  50.702 -5.852  1.00 51.50 ? 225 VAL   A O    1 
ATOM   1477 C  CB   . VAL   A 1 225 ? 0.764  49.249 -7.565  1.00 51.56 ? 225 VAL   A CB   1 
ATOM   1478 C  CG1  . VAL   A 1 225 ? 0.722  48.721 -8.980  1.00 51.11 ? 225 VAL   A CG1  1 
ATOM   1479 C  CG2  . VAL   A 1 225 ? -0.466 48.806 -6.778  1.00 52.26 ? 225 VAL   A CG2  1 
ATOM   1480 N  N    . ASP   A 1 226 ? 1.980  49.379 -4.469  1.00 49.60 ? 226 ASP   A N    1 
ATOM   1481 C  CA   . ASP   A 1 226 ? 2.348  50.133 -3.271  1.00 50.05 ? 226 ASP   A CA   1 
ATOM   1482 C  C    . ASP   A 1 226 ? 3.859  50.009 -3.028  1.00 50.11 ? 226 ASP   A C    1 
ATOM   1483 O  O    . ASP   A 1 226 ? 4.524  51.018 -2.790  1.00 50.87 ? 226 ASP   A O    1 
ATOM   1484 C  CB   . ASP   A 1 226 ? 1.590  49.638 -2.038  1.00 51.84 ? 226 ASP   A CB   1 
ATOM   1485 C  CG   . ASP   A 1 226 ? 1.862  50.470 -0.794  1.00 57.95 ? 226 ASP   A CG   1 
ATOM   1486 O  OD1  . ASP   A 1 226 ? 1.997  51.716 -0.927  1.00 60.95 ? 226 ASP   A OD1  1 
ATOM   1487 O  OD2  . ASP   A 1 226 ? 1.911  49.880 0.323   1.00 56.84 ? 226 ASP   A OD2  1 
ATOM   1488 N  N    . GLN   A 1 227 ? 4.405  48.775 -3.150  1.00 48.37 ? 227 GLN   A N    1 
ATOM   1489 C  CA   . GLN   A 1 227 ? 5.812  48.477 -2.942  1.00 46.72 ? 227 GLN   A CA   1 
ATOM   1490 C  C    . GLN   A 1 227 ? 6.698  49.330 -3.829  1.00 46.30 ? 227 GLN   A C    1 
ATOM   1491 O  O    . GLN   A 1 227 ? 7.601  50.002 -3.322  1.00 46.35 ? 227 GLN   A O    1 
ATOM   1492 C  CB   . GLN   A 1 227 ? 6.094  46.970 -3.136  1.00 45.81 ? 227 GLN   A CB   1 
ATOM   1493 C  CG   . GLN   A 1 227 ? 7.508  46.564 -2.794  1.00 43.61 ? 227 GLN   A CG   1 
ATOM   1494 C  CD   . GLN   A 1 227 ? 7.894  46.835 -1.359  1.00 43.27 ? 227 GLN   A CD   1 
ATOM   1495 O  OE1  . GLN   A 1 227 ? 8.974  47.349 -1.079  1.00 43.62 ? 227 GLN   A OE1  1 
ATOM   1496 N  NE2  . GLN   A 1 227 ? 7.045  46.463 -0.410  1.00 41.16 ? 227 GLN   A NE2  1 
ATOM   1497 N  N    . LEU   A 1 228 ? 6.404  49.353 -5.136  1.00 45.73 ? 228 LEU   A N    1 
ATOM   1498 C  CA   . LEU   A 1 228 ? 7.157  50.141 -6.082  1.00 46.73 ? 228 LEU   A CA   1 
ATOM   1499 C  C    . LEU   A 1 228 ? 7.070  51.642 -5.782  1.00 47.29 ? 228 LEU   A C    1 
ATOM   1500 O  O    . LEU   A 1 228 ? 8.078  52.351 -5.916  1.00 47.75 ? 228 LEU   A O    1 
ATOM   1501 C  CB   . LEU   A 1 228 ? 6.683  49.828 -7.509  1.00 47.95 ? 228 LEU   A CB   1 
ATOM   1502 C  CG   . LEU   A 1 228 ? 7.571  50.308 -8.636  1.00 50.05 ? 228 LEU   A CG   1 
ATOM   1503 C  CD1  . LEU   A 1 228 ? 8.952  49.738 -8.525  1.00 50.46 ? 228 LEU   A CD1  1 
ATOM   1504 C  CD2  . LEU   A 1 228 ? 6.979  49.934 -9.962  1.00 51.48 ? 228 LEU   A CD2  1 
ATOM   1505 N  N    . GLY   A 1 229 ? 5.898  52.106 -5.333  1.00 46.49 ? 229 GLY   A N    1 
ATOM   1506 C  CA   . GLY   A 1 229 ? 5.702  53.502 -4.971  1.00 45.59 ? 229 GLY   A CA   1 
ATOM   1507 C  C    . GLY   A 1 229 ? 6.565  53.897 -3.794  1.00 44.80 ? 229 GLY   A C    1 
ATOM   1508 O  O    . GLY   A 1 229 ? 7.300  54.884 -3.872  1.00 45.24 ? 229 GLY   A O    1 
ATOM   1509 N  N    . LYS   A 1 230 ? 6.521  53.098 -2.718  1.00 43.81 ? 230 LYS   A N    1 
ATOM   1510 C  CA   . LYS   A 1 230 ? 7.356  53.258 -1.525  1.00 44.31 ? 230 LYS   A CA   1 
ATOM   1511 C  C    . LYS   A 1 230 ? 8.866  53.249 -1.868  1.00 45.03 ? 230 LYS   A C    1 
ATOM   1512 O  O    . LYS   A 1 230 ? 9.622  53.989 -1.243  1.00 45.41 ? 230 LYS   A O    1 
ATOM   1513 C  CB   . LYS   A 1 230 ? 7.018  52.184 -0.486  1.00 46.06 ? 230 LYS   A CB   1 
ATOM   1514 C  CG   . LYS   A 1 230 ? 5.577  52.321 0.019   1.00 50.45 ? 230 LYS   A CG   1 
ATOM   1515 C  CD   . LYS   A 1 230 ? 5.434  51.953 1.488   1.00 54.51 ? 230 LYS   A CD   1 
ATOM   1516 C  CE   . LYS   A 1 230 ? 4.023  52.119 2.001   1.00 59.56 ? 230 LYS   A CE   1 
ATOM   1517 N  NZ   . LYS   A 1 230 ? 3.502  53.524 1.860   1.00 62.94 ? 230 LYS   A NZ   1 
ATOM   1518 N  N    . ILE   A 1 231 ? 9.287  52.457 -2.902  1.00 44.44 ? 231 ILE   A N    1 
ATOM   1519 C  CA   . ILE   A 1 231 ? 10.662 52.417 -3.397  1.00 44.73 ? 231 ILE   A CA   1 
ATOM   1520 C  C    . ILE   A 1 231 ? 11.031 53.759 -4.064  1.00 45.20 ? 231 ILE   A C    1 
ATOM   1521 O  O    . ILE   A 1 231 ? 12.019 54.398 -3.682  1.00 45.13 ? 231 ILE   A O    1 
ATOM   1522 C  CB   . ILE   A 1 231 ? 10.879 51.208 -4.376  1.00 44.98 ? 231 ILE   A CB   1 
ATOM   1523 C  CG1  . ILE   A 1 231 ? 10.902 49.853 -3.642  1.00 45.50 ? 231 ILE   A CG1  1 
ATOM   1524 C  CG2  . ILE   A 1 231 ? 12.131 51.379 -5.223  1.00 45.19 ? 231 ILE   A CG2  1 
ATOM   1525 C  CD1  . ILE   A 1 231 ? 10.583 48.694 -4.533  1.00 45.87 ? 231 ILE   A CD1  1 
ATOM   1526 N  N    . LEU   A 1 232 ? 10.218 54.192 -5.037  1.00 45.70 ? 232 LEU   A N    1 
ATOM   1527 C  CA   . LEU   A 1 232 ? 10.457 55.404 -5.811  1.00 47.42 ? 232 LEU   A CA   1 
ATOM   1528 C  C    . LEU   A 1 232 ? 10.357 56.700 -4.982  1.00 50.13 ? 232 LEU   A C    1 
ATOM   1529 O  O    . LEU   A 1 232 ? 10.925 57.712 -5.388  1.00 51.45 ? 232 LEU   A O    1 
ATOM   1530 C  CB   . LEU   A 1 232 ? 9.553  55.436 -7.043  1.00 47.04 ? 232 LEU   A CB   1 
ATOM   1531 C  CG   . LEU   A 1 232 ? 9.731  54.232 -8.007  1.00 48.02 ? 232 LEU   A CG   1 
ATOM   1532 C  CD1  . LEU   A 1 232 ? 8.750  54.288 -9.171  1.00 47.28 ? 232 LEU   A CD1  1 
ATOM   1533 C  CD2  . LEU   A 1 232 ? 11.150 54.150 -8.543  1.00 48.97 ? 232 LEU   A CD2  1 
ATOM   1534 N  N    . ASP   A 1 233 ? 9.711  56.664 -3.812  1.00 50.51 ? 233 ASP   A N    1 
ATOM   1535 C  CA   . ASP   A 1 233 ? 9.687  57.809 -2.911  1.00 52.35 ? 233 ASP   A CA   1 
ATOM   1536 C  C    . ASP   A 1 233 ? 11.127 58.114 -2.422  1.00 53.67 ? 233 ASP   A C    1 
ATOM   1537 O  O    . ASP   A 1 233 ? 11.501 59.281 -2.268  1.00 54.14 ? 233 ASP   A O    1 
ATOM   1538 C  CB   . ASP   A 1 233 ? 8.780  57.525 -1.698  1.00 55.27 ? 233 ASP   A CB   1 
ATOM   1539 C  CG   . ASP   A 1 233 ? 7.298  57.480 -2.017  1.00 63.40 ? 233 ASP   A CG   1 
ATOM   1540 O  OD1  . ASP   A 1 233 ? 6.893  58.047 -3.067  1.00 65.95 ? 233 ASP   A OD1  1 
ATOM   1541 O  OD2  . ASP   A 1 233 ? 6.538  56.869 -1.229  1.00 65.79 ? 233 ASP   A OD2  1 
ATOM   1542 N  N    . VAL   A 1 234 ? 11.934 57.058 -2.192  1.00 53.76 ? 234 VAL   A N    1 
ATOM   1543 C  CA   . VAL   A 1 234 ? 13.318 57.170 -1.739  1.00 53.79 ? 234 VAL   A CA   1 
ATOM   1544 C  C    . VAL   A 1 234 ? 14.339 57.348 -2.883  1.00 54.13 ? 234 VAL   A C    1 
ATOM   1545 O  O    . VAL   A 1 234 ? 15.127 58.294 -2.857  1.00 54.00 ? 234 VAL   A O    1 
ATOM   1546 C  CB   . VAL   A 1 234 ? 13.690 55.971 -0.855  1.00 53.91 ? 234 VAL   A CB   1 
ATOM   1547 C  CG1  . VAL   A 1 234 ? 15.131 56.080 -0.387  1.00 54.69 ? 234 VAL   A CG1  1 
ATOM   1548 C  CG2  . VAL   A 1 234 ? 12.726 55.834 0.312   1.00 54.14 ? 234 VAL   A CG2  1 
ATOM   1549 N  N    . ILE   A 1 235 ? 14.345 56.440 -3.866  1.00 54.32 ? 235 ILE   A N    1 
ATOM   1550 C  CA   . ILE   A 1 235 ? 15.333 56.501 -4.949  1.00 55.56 ? 235 ILE   A CA   1 
ATOM   1551 C  C    . ILE   A 1 235 ? 14.993 57.494 -6.064  1.00 56.51 ? 235 ILE   A C    1 
ATOM   1552 O  O    . ILE   A 1 235 ? 15.828 57.733 -6.933  1.00 56.74 ? 235 ILE   A O    1 
ATOM   1553 C  CB   . ILE   A 1 235 ? 15.620 55.088 -5.533  1.00 55.96 ? 235 ILE   A CB   1 
ATOM   1554 C  CG1  . ILE   A 1 235 ? 14.464 54.584 -6.412  1.00 56.57 ? 235 ILE   A CG1  1 
ATOM   1555 C  CG2  . ILE   A 1 235 ? 15.962 54.101 -4.420  1.00 56.49 ? 235 ILE   A CG2  1 
ATOM   1556 C  CD1  . ILE   A 1 235 ? 14.781 53.338 -7.194  1.00 58.03 ? 235 ILE   A CD1  1 
ATOM   1557 N  N    . GLY   A 1 236 ? 13.779 58.031 -6.061  1.00 57.05 ? 236 GLY   A N    1 
ATOM   1558 C  CA   . GLY   A 1 236 ? 13.347 58.950 -7.099  1.00 57.81 ? 236 GLY   A CA   1 
ATOM   1559 C  C    . GLY   A 1 236 ? 12.904 58.211 -8.340  1.00 59.54 ? 236 GLY   A C    1 
ATOM   1560 O  O    . GLY   A 1 236 ? 13.223 57.029 -8.522  1.00 59.93 ? 236 GLY   A O    1 
ATOM   1561 N  N    . LEU   A 1 237 ? 12.149 58.894 -9.203  1.00 60.18 ? 237 LEU   A N    1 
ATOM   1562 C  CA   . LEU   A 1 237 ? 11.705 58.299 -10.457 1.00 60.97 ? 237 LEU   A CA   1 
ATOM   1563 C  C    . LEU   A 1 237 ? 12.918 58.163 -11.364 1.00 61.92 ? 237 LEU   A C    1 
ATOM   1564 O  O    . LEU   A 1 237 ? 13.707 59.102 -11.460 1.00 62.55 ? 237 LEU   A O    1 
ATOM   1565 C  CB   . LEU   A 1 237 ? 10.656 59.188 -11.127 1.00 61.14 ? 237 LEU   A CB   1 
ATOM   1566 C  CG   . LEU   A 1 237 ? 9.341  58.502 -11.427 1.00 62.54 ? 237 LEU   A CG   1 
ATOM   1567 C  CD1  . LEU   A 1 237 ? 8.552  58.313 -10.162 1.00 63.31 ? 237 LEU   A CD1  1 
ATOM   1568 C  CD2  . LEU   A 1 237 ? 8.541  59.283 -12.452 1.00 63.11 ? 237 LEU   A CD2  1 
ATOM   1569 N  N    . PRO   A 1 238 ? 13.144 56.987 -11.977 1.00 61.85 ? 238 PRO   A N    1 
ATOM   1570 C  CA   . PRO   A 1 238 ? 14.314 56.850 -12.858 1.00 62.39 ? 238 PRO   A CA   1 
ATOM   1571 C  C    . PRO   A 1 238 ? 14.087 57.560 -14.189 1.00 63.51 ? 238 PRO   A C    1 
ATOM   1572 O  O    . PRO   A 1 238 ? 12.947 57.862 -14.556 1.00 63.46 ? 238 PRO   A O    1 
ATOM   1573 C  CB   . PRO   A 1 238 ? 14.398 55.335 -13.083 1.00 62.58 ? 238 PRO   A CB   1 
ATOM   1574 C  CG   . PRO   A 1 238 ? 12.997 54.884 -13.009 1.00 62.62 ? 238 PRO   A CG   1 
ATOM   1575 C  CD   . PRO   A 1 238 ? 12.316 55.763 -11.979 1.00 61.02 ? 238 PRO   A CD   1 
ATOM   1576 N  N    . GLY   A 1 239 ? 15.158 57.744 -14.954 1.00 64.05 ? 239 GLY   A N    1 
ATOM   1577 C  CA   . GLY   A 1 239 ? 15.049 58.318 -16.292 1.00 65.06 ? 239 GLY   A CA   1 
ATOM   1578 C  C    . GLY   A 1 239 ? 14.193 57.443 -17.191 1.00 65.50 ? 239 GLY   A C    1 
ATOM   1579 O  O    . GLY   A 1 239 ? 14.056 56.246 -16.922 1.00 66.22 ? 239 GLY   A O    1 
ATOM   1580 N  N    . GLU   A 1 240 ? 13.568 58.018 -18.219 1.00 65.04 ? 240 GLU   A N    1 
ATOM   1581 C  CA   . GLU   A 1 240 ? 12.699 57.254 -19.110 1.00 65.55 ? 240 GLU   A CA   1 
ATOM   1582 C  C    . GLU   A 1 240 ? 13.443 56.078 -19.784 1.00 65.48 ? 240 GLU   A C    1 
ATOM   1583 O  O    . GLU   A 1 240 ? 12.840 55.038 -20.051 1.00 65.43 ? 240 GLU   A O    1 
ATOM   1584 C  CB   . GLU   A 1 240 ? 12.050 58.186 -20.150 1.00 68.21 ? 240 GLU   A CB   1 
ATOM   1585 C  CG   . GLU   A 1 240 ? 10.826 57.587 -20.815 1.00 73.62 ? 240 GLU   A CG   1 
ATOM   1586 C  CD   . GLU   A 1 240 ? 9.555  57.593 -19.985 1.00 80.25 ? 240 GLU   A CD   1 
ATOM   1587 O  OE1  . GLU   A 1 240 ? 9.017  56.492 -19.723 1.00 81.41 ? 240 GLU   A OE1  1 
ATOM   1588 O  OE2  . GLU   A 1 240 ? 9.079  58.698 -19.629 1.00 81.87 ? 240 GLU   A OE2  1 
ATOM   1589 N  N    . GLU   A 1 241 ? 14.758 56.238 -20.018 1.00 65.33 ? 241 GLU   A N    1 
ATOM   1590 C  CA   . GLU   A 1 241 ? 15.612 55.203 -20.618 1.00 65.90 ? 241 GLU   A CA   1 
ATOM   1591 C  C    . GLU   A 1 241 ? 15.835 54.012 -19.685 1.00 65.53 ? 241 GLU   A C    1 
ATOM   1592 O  O    . GLU   A 1 241 ? 16.171 52.924 -20.162 1.00 65.84 ? 241 GLU   A O    1 
ATOM   1593 C  CB   . GLU   A 1 241 ? 16.980 55.787 -21.035 1.00 69.33 ? 241 GLU   A CB   1 
ATOM   1594 C  CG   . GLU   A 1 241 ? 17.858 56.252 -19.876 1.00 74.79 ? 241 GLU   A CG   1 
ATOM   1595 C  CD   . GLU   A 1 241 ? 17.522 57.628 -19.332 1.00 83.44 ? 241 GLU   A CD   1 
ATOM   1596 O  OE1  . GLU   A 1 241 ? 16.859 58.401 -20.061 1.00 85.24 ? 241 GLU   A OE1  1 
ATOM   1597 O  OE2  . GLU   A 1 241 ? 17.917 57.936 -18.181 1.00 85.77 ? 241 GLU   A OE2  1 
ATOM   1598 N  N    . ASP   A 1 242 ? 15.692 54.232 -18.351 1.00 64.35 ? 242 ASP   A N    1 
ATOM   1599 C  CA   . ASP   A 1 242 ? 15.841 53.211 -17.324 1.00 63.80 ? 242 ASP   A CA   1 
ATOM   1600 C  C    . ASP   A 1 242 ? 14.519 52.495 -17.001 1.00 62.85 ? 242 ASP   A C    1 
ATOM   1601 O  O    . ASP   A 1 242 ? 14.526 51.646 -16.126 1.00 63.10 ? 242 ASP   A O    1 
ATOM   1602 C  CB   . ASP   A 1 242 ? 16.426 53.818 -16.032 1.00 65.26 ? 242 ASP   A CB   1 
ATOM   1603 C  CG   . ASP   A 1 242 ? 17.892 54.197 -16.120 1.00 69.43 ? 242 ASP   A CG   1 
ATOM   1604 O  OD1  . ASP   A 1 242 ? 18.622 53.557 -16.902 1.00 69.86 ? 242 ASP   A OD1  1 
ATOM   1605 O  OD2  . ASP   A 1 242 ? 18.311 55.129 -15.393 1.00 71.90 ? 242 ASP   A OD2  1 
ATOM   1606 N  N    . TRP   A 1 243 ? 13.393 52.841 -17.650 1.00 61.83 ? 243 TRP   A N    1 
ATOM   1607 C  CA   . TRP   A 1 243 ? 12.123 52.173 -17.360 1.00 61.65 ? 243 TRP   A CA   1 
ATOM   1608 C  C    . TRP   A 1 243 ? 11.943 50.999 -18.324 1.00 63.92 ? 243 TRP   A C    1 
ATOM   1609 O  O    . TRP   A 1 243 ? 12.225 51.134 -19.517 1.00 64.32 ? 243 TRP   A O    1 
ATOM   1610 C  CB   . TRP   A 1 243 ? 10.930 53.163 -17.364 1.00 59.73 ? 243 TRP   A CB   1 
ATOM   1611 C  CG   . TRP   A 1 243 ? 9.714  52.658 -16.629 1.00 57.50 ? 243 TRP   A CG   1 
ATOM   1612 C  CD1  . TRP   A 1 243 ? 8.712  51.883 -17.135 1.00 57.60 ? 243 TRP   A CD1  1 
ATOM   1613 C  CD2  . TRP   A 1 243 ? 9.384  52.888 -15.256 1.00 56.11 ? 243 TRP   A CD2  1 
ATOM   1614 N  NE1  . TRP   A 1 243 ? 7.801  51.583 -16.149 1.00 57.16 ? 243 TRP   A NE1  1 
ATOM   1615 C  CE2  . TRP   A 1 243 ? 8.184  52.197 -14.989 1.00 56.43 ? 243 TRP   A CE2  1 
ATOM   1616 C  CE3  . TRP   A 1 243 ? 9.994  53.592 -14.219 1.00 55.87 ? 243 TRP   A CE3  1 
ATOM   1617 C  CZ2  . TRP   A 1 243 ? 7.567  52.234 -13.747 1.00 56.29 ? 243 TRP   A CZ2  1 
ATOM   1618 C  CZ3  . TRP   A 1 243 ? 9.389  53.607 -12.984 1.00 56.28 ? 243 TRP   A CZ3  1 
ATOM   1619 C  CH2  . TRP   A 1 243 ? 8.175  52.962 -12.767 1.00 56.34 ? 243 TRP   A CH2  1 
ATOM   1620 N  N    . PRO   A 1 244 ? 11.596 49.803 -17.814 1.00 65.31 ? 244 PRO   A N    1 
ATOM   1621 C  CA   . PRO   A 1 244 ? 11.481 48.637 -18.700 1.00 66.60 ? 244 PRO   A CA   1 
ATOM   1622 C  C    . PRO   A 1 244 ? 10.415 48.793 -19.767 1.00 68.77 ? 244 PRO   A C    1 
ATOM   1623 O  O    . PRO   A 1 244 ? 9.285  49.168 -19.466 1.00 68.46 ? 244 PRO   A O    1 
ATOM   1624 C  CB   . PRO   A 1 244 ? 11.160 47.491 -17.737 1.00 66.82 ? 244 PRO   A CB   1 
ATOM   1625 C  CG   . PRO   A 1 244 ? 10.526 48.151 -16.584 1.00 66.86 ? 244 PRO   A CG   1 
ATOM   1626 C  CD   . PRO   A 1 244 ? 11.259 49.449 -16.424 1.00 64.93 ? 244 PRO   A CD   1 
ATOM   1627 N  N    . ARG   A 1 245 ? 10.787 48.533 -21.026 1.00 70.89 ? 245 ARG   A N    1 
ATOM   1628 C  CA   . ARG   A 1 245 ? 9.839  48.656 -22.125 1.00 73.39 ? 245 ARG   A CA   1 
ATOM   1629 C  C    . ARG   A 1 245 ? 8.899  47.472 -22.169 1.00 74.36 ? 245 ARG   A C    1 
ATOM   1630 O  O    . ARG   A 1 245 ? 9.243  46.382 -21.705 1.00 74.68 ? 245 ARG   A O    1 
ATOM   1631 C  CB   . ARG   A 1 245 ? 10.559 48.839 -23.471 1.00 76.37 ? 245 ARG   A CB   1 
ATOM   1632 C  CG   . ARG   A 1 245 ? 11.075 50.256 -23.683 1.00 82.30 ? 245 ARG   A CG   1 
ATOM   1633 C  CD   . ARG   A 1 245 ? 12.477 50.241 -24.266 1.00 88.25 ? 245 ARG   A CD   1 
ATOM   1634 N  NE   . ARG   A 1 245 ? 13.027 51.590 -24.424 1.00 93.31 ? 245 ARG   A NE   1 
ATOM   1635 C  CZ   . ARG   A 1 245 ? 13.814 52.189 -23.533 1.00 96.93 ? 245 ARG   A CZ   1 
ATOM   1636 N  NH1  . ARG   A 1 245 ? 14.151 51.567 -22.406 1.00 96.81 ? 245 ARG   A NH1  1 
ATOM   1637 N  NH2  . ARG   A 1 245 ? 14.271 53.415 -23.762 1.00 97.24 ? 245 ARG   A NH2  1 
ATOM   1638 N  N    . ASP   A 1 246 ? 7.700  47.699 -22.711 1.00 74.53 ? 246 ASP   A N    1 
ATOM   1639 C  CA   . ASP   A 1 246 ? 6.669  46.680 -22.882 1.00 75.02 ? 246 ASP   A CA   1 
ATOM   1640 C  C    . ASP   A 1 246 ? 6.209  46.032 -21.569 1.00 73.84 ? 246 ASP   A C    1 
ATOM   1641 O  O    . ASP   A 1 246 ? 5.958  44.830 -21.531 1.00 73.96 ? 246 ASP   A O    1 
ATOM   1642 C  CB   . ASP   A 1 246 ? 7.089  45.623 -23.922 1.00 77.95 ? 246 ASP   A CB   1 
ATOM   1643 C  CG   . ASP   A 1 246 ? 7.218  46.198 -25.329 1.00 85.23 ? 246 ASP   A CG   1 
ATOM   1644 O  OD1  . ASP   A 1 246 ? 8.118  47.050 -25.548 1.00 86.40 ? 246 ASP   A OD1  1 
ATOM   1645 O  OD2  . ASP   A 1 246 ? 6.415  45.798 -26.214 1.00 88.25 ? 246 ASP   A OD2  1 
ATOM   1646 N  N    . VAL   A 1 247 ? 6.065  46.843 -20.511 1.00 72.35 ? 247 VAL   A N    1 
ATOM   1647 C  CA   . VAL   A 1 247 ? 5.504  46.397 -19.230 1.00 71.49 ? 247 VAL   A CA   1 
ATOM   1648 C  C    . VAL   A 1 247 ? 4.143  47.094 -19.015 1.00 70.95 ? 247 VAL   A C    1 
ATOM   1649 O  O    . VAL   A 1 247 ? 3.873  48.127 -19.632 1.00 71.30 ? 247 VAL   A O    1 
ATOM   1650 C  CB   . VAL   A 1 247 ? 6.439  46.587 -18.008 1.00 71.56 ? 247 VAL   A CB   1 
ATOM   1651 C  CG1  . VAL   A 1 247 ? 7.761  45.876 -18.210 1.00 71.82 ? 247 VAL   A CG1  1 
ATOM   1652 C  CG2  . VAL   A 1 247 ? 6.652  48.058 -17.697 1.00 71.90 ? 247 VAL   A CG2  1 
ATOM   1653 N  N    . ALA   A 1 248 ? 3.293  46.538 -18.143 1.00 69.74 ? 248 ALA   A N    1 
ATOM   1654 C  CA   . ALA   A 1 248 ? 1.974  47.095 -17.879 1.00 68.98 ? 248 ALA   A CA   1 
ATOM   1655 C  C    . ALA   A 1 248 ? 1.996  48.473 -17.209 1.00 68.01 ? 248 ALA   A C    1 
ATOM   1656 O  O    . ALA   A 1 248 ? 1.292  49.364 -17.672 1.00 68.70 ? 248 ALA   A O    1 
ATOM   1657 C  CB   . ALA   A 1 248 ? 1.153  46.117 -17.057 1.00 69.29 ? 248 ALA   A CB   1 
ATOM   1658 N  N    . LEU   A 1 249 ? 2.796  48.662 -16.138 1.00 66.38 ? 249 LEU   A N    1 
ATOM   1659 C  CA   . LEU   A 1 249 ? 2.881  49.942 -15.426 1.00 65.10 ? 249 LEU   A CA   1 
ATOM   1660 C  C    . LEU   A 1 249 ? 3.845  50.908 -16.082 1.00 63.32 ? 249 LEU   A C    1 
ATOM   1661 O  O    . LEU   A 1 249 ? 5.044  50.655 -16.091 1.00 63.70 ? 249 LEU   A O    1 
ATOM   1662 C  CB   . LEU   A 1 249 ? 3.350  49.729 -13.986 1.00 65.81 ? 249 LEU   A CB   1 
ATOM   1663 C  CG   . LEU   A 1 249 ? 2.471  48.888 -13.095 1.00 68.04 ? 249 LEU   A CG   1 
ATOM   1664 C  CD1  . LEU   A 1 249 ? 3.294  48.246 -11.984 1.00 68.88 ? 249 LEU   A CD1  1 
ATOM   1665 C  CD2  . LEU   A 1 249 ? 1.353  49.713 -12.521 1.00 68.93 ? 249 LEU   A CD2  1 
ATOM   1666 N  N    . PRO   A 1 250 ? 3.372  52.060 -16.563 1.00 61.68 ? 250 PRO   A N    1 
ATOM   1667 C  CA   . PRO   A 1 250 ? 4.305  53.040 -17.138 1.00 60.66 ? 250 PRO   A CA   1 
ATOM   1668 C  C    . PRO   A 1 250 ? 4.991  53.892 -16.060 1.00 59.05 ? 250 PRO   A C    1 
ATOM   1669 O  O    . PRO   A 1 250 ? 4.541  53.949 -14.923 1.00 58.10 ? 250 PRO   A O    1 
ATOM   1670 C  CB   . PRO   A 1 250 ? 3.404  53.894 -18.037 1.00 61.60 ? 250 PRO   A CB   1 
ATOM   1671 C  CG   . PRO   A 1 250 ? 2.061  53.843 -17.371 1.00 62.31 ? 250 PRO   A CG   1 
ATOM   1672 C  CD   . PRO   A 1 250 ? 1.975  52.536 -16.605 1.00 61.05 ? 250 PRO   A CD   1 
ATOM   1673 N  N    . ARG   A 1 251 ? 6.066  54.586 -16.447 1.00 58.49 ? 251 ARG   A N    1 
ATOM   1674 C  CA   . ARG   A 1 251 ? 6.808  55.503 -15.595 1.00 58.61 ? 251 ARG   A CA   1 
ATOM   1675 C  C    . ARG   A 1 251 ? 5.912  56.656 -15.108 1.00 60.23 ? 251 ARG   A C    1 
ATOM   1676 O  O    . ARG   A 1 251 ? 6.055  57.126 -13.978 1.00 60.23 ? 251 ARG   A O    1 
ATOM   1677 C  CB   . ARG   A 1 251 ? 7.991  56.084 -16.378 1.00 58.59 ? 251 ARG   A CB   1 
ATOM   1678 C  CG   . ARG   A 1 251 ? 8.852  56.998 -15.541 1.00 61.23 ? 251 ARG   A CG   1 
ATOM   1679 C  CD   . ARG   A 1 251 ? 9.727  57.903 -16.371 1.00 64.53 ? 251 ARG   A CD   1 
ATOM   1680 N  NE   . ARG   A 1 251 ? 10.489 58.804 -15.509 1.00 68.45 ? 251 ARG   A NE   1 
ATOM   1681 C  CZ   . ARG   A 1 251 ? 10.629 60.109 -15.711 1.00 71.04 ? 251 ARG   A CZ   1 
ATOM   1682 N  NH1  . ARG   A 1 251 ? 10.077 60.686 -16.769 1.00 71.67 ? 251 ARG   A NH1  1 
ATOM   1683 N  NH2  . ARG   A 1 251 ? 11.344 60.842 -14.870 1.00 70.88 ? 251 ARG   A NH2  1 
ATOM   1684 N  N    . GLN   A 1 252 ? 4.947  57.053 -15.932 1.00 61.15 ? 252 GLN   A N    1 
ATOM   1685 C  CA   . GLN   A 1 252 ? 4.074  58.209 -15.615 1.00 62.40 ? 252 GLN   A CA   1 
ATOM   1686 C  C    . GLN   A 1 252 ? 2.975  57.807 -14.625 1.00 63.02 ? 252 GLN   A C    1 
ATOM   1687 O  O    . GLN   A 1 252 ? 2.204  58.673 -14.222 1.00 62.89 ? 252 GLN   A O    1 
ATOM   1688 C  CB   . GLN   A 1 252 ? 3.503  58.746 -16.932 1.00 64.48 ? 252 GLN   A CB   1 
ATOM   1689 C  CG   . GLN   A 1 252 ? 4.543  59.405 -17.828 1.00 68.29 ? 252 GLN   A CG   1 
ATOM   1690 C  CD   . GLN   A 1 252 ? 5.335  58.444 -18.680 1.00 72.09 ? 252 GLN   A CD   1 
ATOM   1691 O  OE1  . GLN   A 1 252 ? 5.039  57.255 -18.758 1.00 72.54 ? 252 GLN   A OE1  1 
ATOM   1692 N  NE2  . GLN   A 1 252 ? 6.347  58.964 -19.353 1.00 73.09 ? 252 GLN   A NE2  1 
ATOM   1693 N  N    . ALA   A 1 253 ? 2.928  56.543 -14.234 1.00 63.73 ? 253 ALA   A N    1 
ATOM   1694 C  CA   . ALA   A 1 253 ? 1.925  56.103 -13.235 1.00 64.57 ? 253 ALA   A CA   1 
ATOM   1695 C  C    . ALA   A 1 253 ? 2.417  56.475 -11.835 1.00 64.92 ? 253 ALA   A C    1 
ATOM   1696 O  O    . ALA   A 1 253 ? 1.687  56.213 -10.861 1.00 64.93 ? 253 ALA   A O    1 
ATOM   1697 C  CB   . ALA   A 1 253 ? 1.680  54.622 -13.359 1.00 64.88 ? 253 ALA   A CB   1 
ATOM   1698 N  N    . PHE   A 1 254 ? 3.613  57.060 -11.748 1.00 65.33 ? 254 PHE   A N    1 
ATOM   1699 C  CA   . PHE   A 1 254 ? 4.190  57.470 -10.443 1.00 66.38 ? 254 PHE   A CA   1 
ATOM   1700 C  C    . PHE   A 1 254 ? 4.677  58.916 -10.561 1.00 69.23 ? 254 PHE   A C    1 
ATOM   1701 O  O    . PHE   A 1 254 ? 5.217  59.280 -11.621 1.00 69.44 ? 254 PHE   A O    1 
ATOM   1702 C  CB   . PHE   A 1 254 ? 5.324  56.521 -10.049 1.00 65.14 ? 254 PHE   A CB   1 
ATOM   1703 C  CG   . PHE   A 1 254 ? 4.943  55.063 -10.015 1.00 64.45 ? 254 PHE   A CG   1 
ATOM   1704 C  CD1  . PHE   A 1 254 ? 4.047  54.584 -9.074  1.00 64.58 ? 254 PHE   A CD1  1 
ATOM   1705 C  CD2  . PHE   A 1 254 ? 5.462  54.174 -10.941 1.00 64.54 ? 254 PHE   A CD2  1 
ATOM   1706 C  CE1  . PHE   A 1 254 ? 3.696  53.244 -9.046  1.00 64.92 ? 254 PHE   A CE1  1 
ATOM   1707 C  CE2  . PHE   A 1 254 ? 5.107  52.835 -10.915 1.00 65.10 ? 254 PHE   A CE2  1 
ATOM   1708 C  CZ   . PHE   A 1 254 ? 4.225  52.372 -9.968  1.00 64.74 ? 254 PHE   A CZ   1 
ATOM   1709 N  N    . HIS   A 1 255 ? 4.532  59.691 -9.484  1.00 71.28 ? 255 HIS   A N    1 
ATOM   1710 C  CA   . HIS   A 1 255 ? 4.991  61.106 -9.470  1.00 73.49 ? 255 HIS   A CA   1 
ATOM   1711 C  C    . HIS   A 1 255 ? 5.848  61.315 -8.219  1.00 74.93 ? 255 HIS   A C    1 
ATOM   1712 O  O    . HIS   A 1 255 ? 5.745  62.383 -7.581  1.00 74.96 ? 255 HIS   A O    1 
ATOM   1713 C  CB   . HIS   A 1 255 ? 3.781  62.042 -9.529  1.00 75.12 ? 255 HIS   A CB   1 
ATOM   1714 C  CG   . HIS   A 1 255 ? 2.648  61.478 -10.318 1.00 78.20 ? 255 HIS   A CG   1 
ATOM   1715 N  ND1  . HIS   A 1 255 ? 1.425  61.181 -9.757  1.00 80.14 ? 255 HIS   A ND1  1 
ATOM   1716 C  CD2  . HIS   A 1 255 ? 2.558  61.131 -11.607 1.00 79.53 ? 255 HIS   A CD2  1 
ATOM   1717 C  CE1  . HIS   A 1 255 ? 0.626  60.684 -10.690 1.00 80.80 ? 255 HIS   A CE1  1 
ATOM   1718 N  NE2  . HIS   A 1 255 ? 1.294  60.646 -11.822 1.00 80.69 ? 255 HIS   A NE2  1 
ATOM   1719 N  N    . SER   A 1 256 ? 6.679  60.322 -7.883  1.00 75.95 ? 256 SER   A N    1 
ATOM   1720 C  CA   . SER   A 1 256 ? 7.553  60.406 -6.683  1.00 77.09 ? 256 SER   A CA   1 
ATOM   1721 C  C    . SER   A 1 256 ? 8.515  61.586 -6.833  1.00 78.46 ? 256 SER   A C    1 
ATOM   1722 O  O    . SER   A 1 256 ? 9.241  61.879 -5.865  1.00 78.21 ? 256 SER   A O    1 
ATOM   1723 C  CB   . SER   A 1 256 ? 8.283  59.114 -6.470  1.00 77.75 ? 256 SER   A CB   1 
ATOM   1724 O  OG   . SER   A 1 256 ? 7.364  58.052 -6.265  1.00 79.66 ? 256 SER   A OG   1 
ATOM   1725 N  N    . LYS   A 1 257 ? 8.538  62.212 -8.008  1.00 79.52 ? 257 LYS   A N    1 
ATOM   1726 C  CA   . LYS   A 1 257 ? 9.369  63.428 -8.222  1.00 80.93 ? 257 LYS   A CA   1 
ATOM   1727 C  C    . LYS   A 1 257 ? 10.835 63.175 -7.856  1.00 81.56 ? 257 LYS   A C    1 
ATOM   1728 O  O    . LYS   A 1 257 ? 11.435 62.252 -8.442  1.00 82.16 ? 257 LYS   A O    1 
ATOM   1729 C  CB   . LYS   A 1 257 ? 8.801  64.606 -7.422  1.00 83.07 ? 257 LYS   A CB   1 
ATOM   1730 N  N    . SER   A 1 258 ? 11.383 63.958 -6.923  1.00 80.66 ? 258 SER   A N    1 
ATOM   1731 C  CA   . SER   A 1 258 ? 12.835 63.873 -6.609  1.00 80.20 ? 258 SER   A CA   1 
ATOM   1732 C  C    . SER   A 1 258 ? 13.199 62.669 -5.739  1.00 78.89 ? 258 SER   A C    1 
ATOM   1733 O  O    . SER   A 1 258 ? 12.287 62.060 -5.148  1.00 79.22 ? 258 SER   A O    1 
ATOM   1734 C  CB   . SER   A 1 258 ? 13.302 65.148 -5.952  1.00 82.13 ? 258 SER   A CB   1 
ATOM   1735 O  OG   . SER   A 1 258 ? 14.671 65.058 -5.588  1.00 84.98 ? 258 SER   A OG   1 
ATOM   1736 N  N    . ALA   A 1 259 ? 14.495 62.351 -5.678  1.00 77.13 ? 259 ALA   A N    1 
ATOM   1737 C  CA   . ALA   A 1 259 ? 14.989 61.264 -4.808  1.00 75.73 ? 259 ALA   A CA   1 
ATOM   1738 C  C    . ALA   A 1 259 ? 15.502 61.892 -3.511  1.00 74.56 ? 259 ALA   A C    1 
ATOM   1739 O  O    . ALA   A 1 259 ? 16.136 62.959 -3.587  1.00 74.78 ? 259 ALA   A O    1 
ATOM   1740 C  CB   . ALA   A 1 259 ? 16.092 60.534 -5.518  1.00 75.66 ? 259 ALA   A CB   1 
ATOM   1741 N  N    . GLN   A 1 260 ? 15.237 61.258 -2.369  1.00 73.27 ? 260 GLN   A N    1 
ATOM   1742 C  CA   . GLN   A 1 260 ? 15.646 61.827 -1.057  1.00 72.16 ? 260 GLN   A CA   1 
ATOM   1743 C  C    . GLN   A 1 260 ? 17.002 61.247 -0.640  1.00 71.20 ? 260 GLN   A C    1 
ATOM   1744 O  O    . GLN   A 1 260 ? 17.362 60.167 -1.138  1.00 71.63 ? 260 GLN   A O    1 
ATOM   1745 C  CB   . GLN   A 1 260 ? 14.582 61.524 -0.002  1.00 72.38 ? 260 GLN   A CB   1 
ATOM   1746 C  CG   . GLN   A 1 260 ? 13.164 61.840 -0.449  1.00 72.88 ? 260 GLN   A CG   1 
ATOM   1747 C  CD   . GLN   A 1 260 ? 12.157 61.442 0.601   1.00 74.84 ? 260 GLN   A CD   1 
ATOM   1748 O  OE1  . GLN   A 1 260 ? 11.273 60.622 0.363   1.00 75.03 ? 260 GLN   A OE1  1 
ATOM   1749 N  NE2  . GLN   A 1 260 ? 12.289 62.021 1.783   1.00 75.07 ? 260 GLN   A NE2  1 
ATOM   1750 N  N    . PRO   A 1 261 ? 17.766 61.916 0.251   1.00 69.74 ? 261 PRO   A N    1 
ATOM   1751 C  CA   . PRO   A 1 261 ? 19.037 61.378 0.732   1.00 68.89 ? 261 PRO   A CA   1 
ATOM   1752 C  C    . PRO   A 1 261 ? 18.794 60.117 1.572   1.00 67.97 ? 261 PRO   A C    1 
ATOM   1753 O  O    . PRO   A 1 261 ? 17.877 60.118 2.371   1.00 67.64 ? 261 PRO   A O    1 
ATOM   1754 C  CB   . PRO   A 1 261 ? 19.608 62.516 1.589   1.00 69.60 ? 261 PRO   A CB   1 
ATOM   1755 C  CG   . PRO   A 1 261 ? 18.389 63.295 2.026   1.00 70.26 ? 261 PRO   A CG   1 
ATOM   1756 C  CD   . PRO   A 1 261 ? 17.444 63.214 0.846   1.00 68.92 ? 261 PRO   A CD   1 
ATOM   1757 N  N    . ILE   A 1 262 ? 19.629 59.089 1.397   1.00 67.02 ? 262 ILE   A N    1 
ATOM   1758 C  CA   . ILE   A 1 262 ? 19.409 57.791 2.106   1.00 66.46 ? 262 ILE   A CA   1 
ATOM   1759 C  C    . ILE   A 1 262 ? 19.733 57.939 3.598   1.00 65.31 ? 262 ILE   A C    1 
ATOM   1760 O  O    . ILE   A 1 262 ? 19.096 57.238 4.402   1.00 64.96 ? 262 ILE   A O    1 
ATOM   1761 C  CB   . ILE   A 1 262 ? 20.234 56.669 1.442   1.00 67.16 ? 262 ILE   A CB   1 
ATOM   1762 C  CG1  . ILE   A 1 262 ? 19.824 55.287 1.956   1.00 68.06 ? 262 ILE   A CG1  1 
ATOM   1763 C  CG2  . ILE   A 1 262 ? 21.725 56.919 1.608   1.00 67.54 ? 262 ILE   A CG2  1 
ATOM   1764 C  CD1  . ILE   A 1 262 ? 18.372 54.951 1.714   1.00 69.16 ? 262 ILE   A CD1  1 
ATOM   1765 N  N    . GLU   A 1 263 ? 20.694 58.799 3.946   1.00 64.65 ? 263 GLU   A N    1 
ATOM   1766 C  CA   . GLU   A 1 263 ? 21.107 58.978 5.366   1.00 64.55 ? 263 GLU   A CA   1 
ATOM   1767 C  C    . GLU   A 1 263 ? 19.876 59.272 6.230   1.00 64.08 ? 263 GLU   A C    1 
ATOM   1768 O  O    . GLU   A 1 263 ? 19.916 58.968 7.435   1.00 64.45 ? 263 GLU   A O    1 
ATOM   1769 C  CB   . GLU   A 1 263 ? 22.146 60.094 5.492   1.00 66.17 ? 263 GLU   A CB   1 
ATOM   1770 C  CG   . GLU   A 1 263 ? 21.849 61.310 4.637   1.00 69.45 ? 263 GLU   A CG   1 
ATOM   1771 C  CD   . GLU   A 1 263 ? 22.540 61.304 3.285   1.00 74.32 ? 263 GLU   A CD   1 
ATOM   1772 O  OE1  . GLU   A 1 263 ? 22.269 60.388 2.486   1.00 74.62 ? 263 GLU   A OE1  1 
ATOM   1773 O  OE2  . GLU   A 1 263 ? 23.355 62.213 3.039   1.00 76.56 ? 263 GLU   A OE2  1 
ATOM   1774 N  N    . LYS   A 1 264 ? 18.829 59.840 5.632   1.00 63.42 ? 264 LYS   A N    1 
ATOM   1775 C  CA   . LYS   A 1 264 ? 17.578 60.141 6.373   1.00 63.05 ? 264 LYS   A CA   1 
ATOM   1776 C  C    . LYS   A 1 264 ? 16.895 58.834 6.778   1.00 61.31 ? 264 LYS   A C    1 
ATOM   1777 O  O    . LYS   A 1 264 ? 16.412 58.754 7.921   1.00 60.92 ? 264 LYS   A O    1 
ATOM   1778 C  CB   . LYS   A 1 264 ? 16.647 60.967 5.483   1.00 65.51 ? 264 LYS   A CB   1 
ATOM   1779 C  CG   . LYS   A 1 264 ? 15.339 61.412 6.122   1.00 70.74 ? 264 LYS   A CG   1 
ATOM   1780 C  CD   . LYS   A 1 264 ? 14.566 62.374 5.248   1.00 76.00 ? 264 LYS   A CD   1 
ATOM   1781 C  CE   . LYS   A 1 264 ? 13.365 62.981 5.941   1.00 79.83 ? 264 LYS   A CE   1 
ATOM   1782 N  NZ   . LYS   A 1 264 ? 12.723 64.025 5.108   1.00 81.73 ? 264 LYS   A NZ   1 
ATOM   1783 N  N    . PHE   A 1 265 ? 16.861 57.854 5.873   1.00 59.98 ? 265 PHE   A N    1 
ATOM   1784 C  CA   . PHE   A 1 265 ? 16.151 56.577 6.141   1.00 58.82 ? 265 PHE   A CA   1 
ATOM   1785 C  C    . PHE   A 1 265 ? 17.105 55.594 6.822   1.00 57.85 ? 265 PHE   A C    1 
ATOM   1786 O  O    . PHE   A 1 265 ? 16.641 54.759 7.616   1.00 57.09 ? 265 PHE   A O    1 
ATOM   1787 C  CB   . PHE   A 1 265 ? 15.605 56.028 4.823   1.00 58.49 ? 265 PHE   A CB   1 
ATOM   1788 C  CG   . PHE   A 1 265 ? 14.955 57.073 3.953   1.00 59.30 ? 265 PHE   A CG   1 
ATOM   1789 C  CD1  . PHE   A 1 265 ? 13.749 57.650 4.316   1.00 60.50 ? 265 PHE   A CD1  1 
ATOM   1790 C  CD2  . PHE   A 1 265 ? 15.572 57.513 2.794   1.00 60.28 ? 265 PHE   A CD2  1 
ATOM   1791 C  CE1  . PHE   A 1 265 ? 13.159 58.619 3.521   1.00 61.59 ? 265 PHE   A CE1  1 
ATOM   1792 C  CE2  . PHE   A 1 265 ? 14.983 58.485 2.002   1.00 61.64 ? 265 PHE   A CE2  1 
ATOM   1793 C  CZ   . PHE   A 1 265 ? 13.777 59.036 2.366   1.00 61.70 ? 265 PHE   A CZ   1 
ATOM   1794 N  N    . VAL   A 1 266 ? 18.399 55.690 6.543   1.00 57.97 ? 266 VAL   A N    1 
ATOM   1795 C  CA   . VAL   A 1 266 ? 19.429 54.836 7.207   1.00 58.96 ? 266 VAL   A CA   1 
ATOM   1796 C  C    . VAL   A 1 266 ? 20.357 55.810 7.930   1.00 60.90 ? 266 VAL   A C    1 
ATOM   1797 O  O    . VAL   A 1 266 ? 21.292 56.306 7.294   1.00 61.48 ? 266 VAL   A O    1 
ATOM   1798 C  CB   . VAL   A 1 266 ? 20.168 53.946 6.193   1.00 58.68 ? 266 VAL   A CB   1 
ATOM   1799 C  CG1  . VAL   A 1 266 ? 20.929 52.825 6.877   1.00 58.97 ? 266 VAL   A CG1  1 
ATOM   1800 C  CG2  . VAL   A 1 266 ? 19.224 53.387 5.143   1.00 58.58 ? 266 VAL   A CG2  1 
ATOM   1801 N  N    . THR   A 1 267 ? 20.139 56.037 9.222   1.00 61.72 ? 267 THR   A N    1 
ATOM   1802 C  CA   . THR   A 1 267 ? 20.845 57.142 9.933   1.00 62.58 ? 267 THR   A CA   1 
ATOM   1803 C  C    . THR   A 1 267 ? 22.338 56.941 10.191  1.00 62.98 ? 267 THR   A C    1 
ATOM   1804 O  O    . THR   A 1 267 ? 23.089 57.888 9.936   1.00 62.84 ? 267 THR   A O    1 
ATOM   1805 C  CB   . THR   A 1 267 ? 20.101 57.495 11.231  1.00 64.18 ? 267 THR   A CB   1 
ATOM   1806 O  OG1  . THR   A 1 267 ? 19.873 56.305 11.984  1.00 65.45 ? 267 THR   A OG1  1 
ATOM   1807 C  CG2  . THR   A 1 267 ? 18.778 58.179 10.969  1.00 64.54 ? 267 THR   A CG2  1 
ATOM   1808 N  N    . ASP   A 1 268 ? 22.770 55.780 10.655  1.00 63.22 ? 268 ASP   A N    1 
ATOM   1809 C  CA   . ASP   A 1 268 ? 24.201 55.696 11.064  1.00 63.81 ? 268 ASP   A CA   1 
ATOM   1810 C  C    . ASP   A 1 268 ? 25.143 55.177 9.972   1.00 63.12 ? 268 ASP   A C    1 
ATOM   1811 O  O    . ASP   A 1 268 ? 26.261 54.798 10.329  1.00 63.21 ? 268 ASP   A O    1 
ATOM   1812 C  CB   . ASP   A 1 268 ? 24.327 54.864 12.339  1.00 66.77 ? 268 ASP   A CB   1 
ATOM   1813 C  CG   . ASP   A 1 268 ? 23.647 55.511 13.530  1.00 73.91 ? 268 ASP   A CG   1 
ATOM   1814 O  OD1  . ASP   A 1 268 ? 24.013 56.656 13.857  1.00 75.46 ? 268 ASP   A OD1  1 
ATOM   1815 O  OD2  . ASP   A 1 268 ? 22.760 54.866 14.119  1.00 76.75 ? 268 ASP   A OD2  1 
ATOM   1816 N  N    . ILE   A 1 269 ? 24.741 55.199 8.704   1.00 62.43 ? 269 ILE   A N    1 
ATOM   1817 C  CA   . ILE   A 1 269 ? 25.587 54.580 7.637   1.00 62.09 ? 269 ILE   A CA   1 
ATOM   1818 C  C    . ILE   A 1 269 ? 26.783 55.481 7.303   1.00 62.07 ? 269 ILE   A C    1 
ATOM   1819 O  O    . ILE   A 1 269 ? 26.614 56.702 7.288   1.00 62.14 ? 269 ILE   A O    1 
ATOM   1820 C  CB   . ILE   A 1 269 ? 24.740 54.202 6.398   1.00 61.89 ? 269 ILE   A CB   1 
ATOM   1821 C  CG1  . ILE   A 1 269 ? 25.489 53.235 5.477   1.00 62.78 ? 269 ILE   A CG1  1 
ATOM   1822 C  CG2  . ILE   A 1 269 ? 24.253 55.435 5.655   1.00 61.77 ? 269 ILE   A CG2  1 
ATOM   1823 C  CD1  . ILE   A 1 269 ? 24.603 52.530 4.482   1.00 64.23 ? 269 ILE   A CD1  1 
ATOM   1824 N  N    . ASP   A 1 270 ? 27.936 54.874 7.023   1.00 61.94 ? 270 ASP   A N    1 
ATOM   1825 C  CA   . ASP   A 1 270 ? 29.165 55.636 6.681   1.00 62.60 ? 270 ASP   A CA   1 
ATOM   1826 C  C    . ASP   A 1 270 ? 29.116 56.102 5.224   1.00 63.34 ? 270 ASP   A C    1 
ATOM   1827 O  O    . ASP   A 1 270 ? 28.206 55.667 4.497   1.00 63.68 ? 270 ASP   A O    1 
ATOM   1828 C  CB   . ASP   A 1 270 ? 30.416 54.790 6.922   1.00 64.51 ? 270 ASP   A CB   1 
ATOM   1829 C  CG   . ASP   A 1 270 ? 30.439 53.511 6.104   1.00 70.77 ? 270 ASP   A CG   1 
ATOM   1830 O  OD1  . ASP   A 1 270 ? 29.516 52.691 6.277   1.00 72.04 ? 270 ASP   A OD1  1 
ATOM   1831 O  OD2  . ASP   A 1 270 ? 31.378 53.347 5.302   1.00 72.71 ? 270 ASP   A OD2  1 
ATOM   1832 N  N    . GLU   A 1 271 ? 30.063 56.954 4.824   1.00 63.13 ? 271 GLU   A N    1 
ATOM   1833 C  CA   . GLU   A 1 271 ? 30.137 57.423 3.438   1.00 63.31 ? 271 GLU   A CA   1 
ATOM   1834 C  C    . GLU   A 1 271 ? 30.313 56.277 2.431   1.00 61.99 ? 271 GLU   A C    1 
ATOM   1835 O  O    . GLU   A 1 271 ? 29.695 56.284 1.366   1.00 61.29 ? 271 GLU   A O    1 
ATOM   1836 C  CB   . GLU   A 1 271 ? 31.275 58.456 3.269   1.00 67.51 ? 271 GLU   A CB   1 
ATOM   1837 C  CG   . GLU   A 1 271 ? 30.952 59.845 3.808   1.00 76.01 ? 271 GLU   A CG   1 
ATOM   1838 C  CD   . GLU   A 1 271 ? 31.976 60.921 3.481   1.00 85.86 ? 271 GLU   A CD   1 
ATOM   1839 O  OE1  . GLU   A 1 271 ? 32.746 60.734 2.510   1.00 88.16 ? 271 GLU   A OE1  1 
ATOM   1840 O  OE2  . GLU   A 1 271 ? 32.004 61.955 4.190   1.00 87.82 ? 271 GLU   A OE2  1 
ATOM   1841 N  N    . LEU   A 1 272 ? 31.159 55.302 2.771   1.00 61.18 ? 272 LEU   A N    1 
ATOM   1842 C  CA   . LEU   A 1 272 ? 31.416 54.167 1.898   1.00 60.45 ? 272 LEU   A CA   1 
ATOM   1843 C  C    . LEU   A 1 272 ? 30.260 53.189 1.854   1.00 59.66 ? 272 LEU   A C    1 
ATOM   1844 O  O    . LEU   A 1 272 ? 29.942 52.668 0.787   1.00 59.80 ? 272 LEU   A O    1 
ATOM   1845 C  CB   . LEU   A 1 272 ? 32.725 53.474 2.270   1.00 60.56 ? 272 LEU   A CB   1 
ATOM   1846 C  CG   . LEU   A 1 272 ? 33.974 54.313 2.036   1.00 61.81 ? 272 LEU   A CG   1 
ATOM   1847 C  CD1  . LEU   A 1 272 ? 35.204 53.566 2.465   1.00 62.42 ? 272 LEU   A CD1  1 
ATOM   1848 C  CD2  . LEU   A 1 272 ? 34.088 54.756 0.571   1.00 62.24 ? 272 LEU   A CD2  1 
ATOM   1849 N  N    . GLY   A 1 273 ? 29.611 52.989 2.993   1.00 58.51 ? 273 GLY   A N    1 
ATOM   1850 C  CA   . GLY   A 1 273 ? 28.436 52.139 3.104   1.00 58.09 ? 273 GLY   A CA   1 
ATOM   1851 C  C    . GLY   A 1 273 ? 27.295 52.704 2.286   1.00 57.81 ? 273 GLY   A C    1 
ATOM   1852 O  O    . GLY   A 1 273 ? 26.616 51.959 1.590   1.00 58.71 ? 273 GLY   A O    1 
ATOM   1853 N  N    . LYS   A 1 274 ? 27.126 54.034 2.302   1.00 56.75 ? 274 LYS   A N    1 
ATOM   1854 C  CA   . LYS   A 1 274 ? 26.114 54.755 1.525   1.00 56.31 ? 274 LYS   A CA   1 
ATOM   1855 C  C    . LYS   A 1 274 ? 26.311 54.483 0.033   1.00 55.57 ? 274 LYS   A C    1 
ATOM   1856 O  O    . LYS   A 1 274 ? 25.339 54.249 -0.678  1.00 55.92 ? 274 LYS   A O    1 
ATOM   1857 C  CB   . LYS   A 1 274 ? 26.234 56.265 1.803   1.00 58.38 ? 274 LYS   A CB   1 
ATOM   1858 C  CG   . LYS   A 1 274 ? 25.414 57.181 0.901   1.00 62.85 ? 274 LYS   A CG   1 
ATOM   1859 C  CD   . LYS   A 1 274 ? 25.707 58.649 1.228   1.00 68.62 ? 274 LYS   A CD   1 
ATOM   1860 C  CE   . LYS   A 1 274 ? 25.179 59.614 0.195   1.00 73.00 ? 274 LYS   A CE   1 
ATOM   1861 N  NZ   . LYS   A 1 274 ? 23.694 59.675 0.204   1.00 75.82 ? 274 LYS   A NZ   1 
ATOM   1862 N  N    . ASP   A 1 275 ? 27.562 54.497 -0.439  1.00 54.42 ? 275 ASP   A N    1 
ATOM   1863 C  CA   . ASP   A 1 275 ? 27.851 54.251 -1.843  1.00 53.80 ? 275 ASP   A CA   1 
ATOM   1864 C  C    . ASP   A 1 275 ? 27.527 52.803 -2.246  1.00 52.67 ? 275 ASP   A C    1 
ATOM   1865 O  O    . ASP   A 1 275 ? 26.910 52.598 -3.283  1.00 52.55 ? 275 ASP   A O    1 
ATOM   1866 C  CB   . ASP   A 1 275 ? 29.292 54.624 -2.186  1.00 55.53 ? 275 ASP   A CB   1 
ATOM   1867 C  CG   . ASP   A 1 275 ? 29.561 54.584 -3.678  1.00 59.99 ? 275 ASP   A CG   1 
ATOM   1868 O  OD1  . ASP   A 1 275 ? 29.130 55.520 -4.382  1.00 60.11 ? 275 ASP   A OD1  1 
ATOM   1869 O  OD2  . ASP   A 1 275 ? 30.197 53.603 -4.143  1.00 62.01 ? 275 ASP   A OD2  1 
ATOM   1870 N  N    . LEU   A 1 276 ? 27.897 51.813 -1.412  1.00 51.30 ? 276 LEU   A N    1 
ATOM   1871 C  CA   . LEU   A 1 276 ? 27.587 50.418 -1.708  1.00 50.30 ? 276 LEU   A CA   1 
ATOM   1872 C  C    . LEU   A 1 276 ? 26.075 50.207 -1.681  1.00 49.56 ? 276 LEU   A C    1 
ATOM   1873 O  O    . LEU   A 1 276 ? 25.532 49.535 -2.562  1.00 50.12 ? 276 LEU   A O    1 
ATOM   1874 C  CB   . LEU   A 1 276 ? 28.283 49.460 -0.717  1.00 49.89 ? 276 LEU   A CB   1 
ATOM   1875 C  CG   . LEU   A 1 276 ? 27.891 47.972 -0.866  1.00 50.18 ? 276 LEU   A CG   1 
ATOM   1876 C  CD1  . LEU   A 1 276 ? 28.177 47.449 -2.266  1.00 49.95 ? 276 LEU   A CD1  1 
ATOM   1877 C  CD2  . LEU   A 1 276 ? 28.496 47.112 0.215   1.00 50.12 ? 276 LEU   A CD2  1 
ATOM   1878 N  N    . LEU   A 1 277 ? 25.397 50.788 -0.694  1.00 48.09 ? 277 LEU   A N    1 
ATOM   1879 C  CA   . LEU   A 1 277 ? 23.955 50.679 -0.585  1.00 47.98 ? 277 LEU   A CA   1 
ATOM   1880 C  C    . LEU   A 1 277 ? 23.241 51.255 -1.826  1.00 48.14 ? 277 LEU   A C    1 
ATOM   1881 O  O    . LEU   A 1 277 ? 22.255 50.686 -2.289  1.00 48.29 ? 277 LEU   A O    1 
ATOM   1882 C  CB   . LEU   A 1 277 ? 23.475 51.389 0.687   1.00 47.88 ? 277 LEU   A CB   1 
ATOM   1883 C  CG   . LEU   A 1 277 ? 21.984 51.397 0.908   1.00 49.09 ? 277 LEU   A CG   1 
ATOM   1884 C  CD1  . LEU   A 1 277 ? 21.508 50.037 1.178   1.00 49.91 ? 277 LEU   A CD1  1 
ATOM   1885 C  CD2  . LEU   A 1 277 ? 21.611 52.263 2.068   1.00 49.75 ? 277 LEU   A CD2  1 
ATOM   1886 N  N    . LEU   A 1 278 ? 23.737 52.367 -2.359  1.00 48.30 ? 278 LEU   A N    1 
ATOM   1887 C  CA   . LEU   A 1 278 ? 23.128 53.002 -3.522  1.00 49.28 ? 278 LEU   A CA   1 
ATOM   1888 C  C    . LEU   A 1 278 ? 23.302 52.185 -4.788  1.00 48.56 ? 278 LEU   A C    1 
ATOM   1889 O  O    . LEU   A 1 278 ? 22.382 52.094 -5.609  1.00 48.17 ? 278 LEU   A O    1 
ATOM   1890 C  CB   . LEU   A 1 278 ? 23.702 54.403 -3.715  1.00 50.79 ? 278 LEU   A CB   1 
ATOM   1891 C  CG   . LEU   A 1 278 ? 23.148 55.460 -2.773  1.00 53.90 ? 278 LEU   A CG   1 
ATOM   1892 C  CD1  . LEU   A 1 278 ? 23.884 56.789 -2.963  1.00 54.92 ? 278 LEU   A CD1  1 
ATOM   1893 C  CD2  . LEU   A 1 278 ? 21.644 55.640 -2.976  1.00 55.15 ? 278 LEU   A CD2  1 
ATOM   1894 N  N    . LYS   A 1 279 ? 24.475 51.565 -4.930  1.00 48.04 ? 279 LYS   A N    1 
ATOM   1895 C  CA   . LYS   A 1 279 ? 24.791 50.716 -6.071  1.00 47.52 ? 279 LYS   A CA   1 
ATOM   1896 C  C    . LYS   A 1 279 ? 23.905 49.450 -6.097  1.00 46.11 ? 279 LYS   A C    1 
ATOM   1897 O  O    . LYS   A 1 279 ? 23.595 48.958 -7.182  1.00 45.71 ? 279 LYS   A O    1 
ATOM   1898 C  CB   . LYS   A 1 279 ? 26.284 50.386 -6.054  1.00 49.73 ? 279 LYS   A CB   1 
ATOM   1899 C  CG   . LYS   A 1 279 ? 27.129 51.606 -6.408  1.00 52.53 ? 279 LYS   A CG   1 
ATOM   1900 C  CD   . LYS   A 1 279 ? 28.618 51.318 -6.541  1.00 55.69 ? 279 LYS   A CD   1 
ATOM   1901 C  CE   . LYS   A 1 279 ? 29.235 52.430 -7.361  1.00 59.45 ? 279 LYS   A CE   1 
ATOM   1902 N  NZ   . LYS   A 1 279 ? 30.486 52.973 -6.764  1.00 61.36 ? 279 LYS   A NZ   1 
ATOM   1903 N  N    . CYS   A 1 280 ? 23.434 48.978 -4.906  1.00 44.27 ? 280 CYS   A N    1 
ATOM   1904 C  CA   . CYS   A 1 280 ? 22.518 47.836 -4.786  1.00 43.66 ? 280 CYS   A CA   1 
ATOM   1905 C  C    . CYS   A 1 280 ? 21.096 48.271 -5.104  1.00 43.62 ? 280 CYS   A C    1 
ATOM   1906 O  O    . CYS   A 1 280 ? 20.337 47.539 -5.729  1.00 43.27 ? 280 CYS   A O    1 
ATOM   1907 C  CB   . CYS   A 1 280 ? 22.580 47.224 -3.386  1.00 43.97 ? 280 CYS   A CB   1 
ATOM   1908 S  SG   . CYS   A 1 280 ? 24.152 46.450 -2.968  1.00 46.23 ? 280 CYS   A SG   1 
ATOM   1909 N  N    . LEU   A 1 281 ? 20.705 49.443 -4.603  1.00 44.13 ? 281 LEU   A N    1 
ATOM   1910 C  CA   . LEU   A 1 281 ? 19.370 49.960 -4.790  1.00 44.14 ? 281 LEU   A CA   1 
ATOM   1911 C  C    . LEU   A 1 281 ? 19.222 50.818 -6.061  1.00 45.74 ? 281 LEU   A C    1 
ATOM   1912 O  O    . LEU   A 1 281 ? 18.518 51.831 -6.057  1.00 47.30 ? 281 LEU   A O    1 
ATOM   1913 C  CB   . LEU   A 1 281 ? 18.907 50.695 -3.537  1.00 43.73 ? 281 LEU   A CB   1 
ATOM   1914 C  CG   . LEU   A 1 281 ? 18.838 49.851 -2.241  1.00 44.77 ? 281 LEU   A CG   1 
ATOM   1915 C  CD1  . LEU   A 1 281 ? 18.364 50.716 -1.050  1.00 46.38 ? 281 LEU   A CD1  1 
ATOM   1916 C  CD2  . LEU   A 1 281 ? 17.930 48.630 -2.401  1.00 44.08 ? 281 LEU   A CD2  1 
ATOM   1917 N  N    . THR   A 1 282 ? 19.837 50.377 -7.156  1.00 45.58 ? 282 THR   A N    1 
ATOM   1918 C  CA   . THR   A 1 282 ? 19.751 50.994 -8.473  1.00 45.98 ? 282 THR   A CA   1 
ATOM   1919 C  C    . THR   A 1 282 ? 18.552 50.376 -9.209  1.00 46.57 ? 282 THR   A C    1 
ATOM   1920 O  O    . THR   A 1 282 ? 18.438 49.146 -9.283  1.00 46.78 ? 282 THR   A O    1 
ATOM   1921 C  CB   . THR   A 1 282 ? 21.046 50.729 -9.213  1.00 47.32 ? 282 THR   A CB   1 
ATOM   1922 O  OG1  . THR   A 1 282 ? 22.097 51.327 -8.479  1.00 48.98 ? 282 THR   A OG1  1 
ATOM   1923 C  CG2  . THR   A 1 282 ? 21.057 51.301 -10.585 1.00 47.54 ? 282 THR   A CG2  1 
ATOM   1924 N  N    . PHE   A 1 283 ? 17.659 51.221 -9.741  1.00 46.34 ? 283 PHE   A N    1 
ATOM   1925 C  CA   . PHE   A 1 283 ? 16.442 50.787 -10.416 1.00 46.14 ? 283 PHE   A CA   1 
ATOM   1926 C  C    . PHE   A 1 283 ? 16.727 49.930 -11.611 1.00 46.08 ? 283 PHE   A C    1 
ATOM   1927 O  O    . PHE   A 1 283 ? 16.081 48.899 -11.788 1.00 46.05 ? 283 PHE   A O    1 
ATOM   1928 C  CB   . PHE   A 1 283 ? 15.560 51.991 -10.818 1.00 46.01 ? 283 PHE   A CB   1 
ATOM   1929 C  CG   . PHE   A 1 283 ? 14.248 51.615 -11.469 1.00 46.34 ? 283 PHE   A CG   1 
ATOM   1930 C  CD1  . PHE   A 1 283 ? 14.153 51.460 -12.841 1.00 47.10 ? 283 PHE   A CD1  1 
ATOM   1931 C  CD2  . PHE   A 1 283 ? 13.109 51.426 -10.709 1.00 47.30 ? 283 PHE   A CD2  1 
ATOM   1932 C  CE1  . PHE   A 1 283 ? 12.948 51.086 -13.438 1.00 47.67 ? 283 PHE   A CE1  1 
ATOM   1933 C  CE2  . PHE   A 1 283 ? 11.903 51.074 -11.313 1.00 48.06 ? 283 PHE   A CE2  1 
ATOM   1934 C  CZ   . PHE   A 1 283 ? 11.834 50.905 -12.674 1.00 47.51 ? 283 PHE   A CZ   1 
ATOM   1935 N  N    . ASN   A 1 284 ? 17.674 50.354 -12.448 1.00 46.37 ? 284 ASN   A N    1 
ATOM   1936 C  CA   . ASN   A 1 284 ? 17.996 49.633 -13.662 1.00 46.78 ? 284 ASN   A CA   1 
ATOM   1937 C  C    . ASN   A 1 284 ? 18.883 48.443 -13.315 1.00 46.49 ? 284 ASN   A C    1 
ATOM   1938 O  O    . ASN   A 1 284 ? 20.012 48.626 -12.870 1.00 47.06 ? 284 ASN   A O    1 
ATOM   1939 C  CB   . ASN   A 1 284 ? 18.651 50.570 -14.671 1.00 49.11 ? 284 ASN   A CB   1 
ATOM   1940 C  CG   . ASN   A 1 284 ? 18.857 49.962 -16.033 1.00 55.05 ? 284 ASN   A CG   1 
ATOM   1941 O  OD1  . ASN   A 1 284 ? 18.815 48.741 -16.224 1.00 57.28 ? 284 ASN   A OD1  1 
ATOM   1942 N  ND2  . ASN   A 1 284 ? 19.092 50.801 -17.030 1.00 57.12 ? 284 ASN   A ND2  1 
ATOM   1943 N  N    . PRO   A 1 285 ? 18.375 47.213 -13.509 1.00 45.24 ? 285 PRO   A N    1 
ATOM   1944 C  CA   . PRO   A 1 285 ? 19.151 46.031 -13.123 1.00 44.83 ? 285 PRO   A CA   1 
ATOM   1945 C  C    . PRO   A 1 285 ? 20.469 45.864 -13.851 1.00 45.49 ? 285 PRO   A C    1 
ATOM   1946 O  O    . PRO   A 1 285 ? 21.387 45.250 -13.294 1.00 45.66 ? 285 PRO   A O    1 
ATOM   1947 C  CB   . PRO   A 1 285 ? 18.203 44.871 -13.407 1.00 45.57 ? 285 PRO   A CB   1 
ATOM   1948 C  CG   . PRO   A 1 285 ? 17.181 45.420 -14.376 1.00 46.08 ? 285 PRO   A CG   1 
ATOM   1949 C  CD   . PRO   A 1 285 ? 17.033 46.849 -14.002 1.00 44.29 ? 285 PRO   A CD   1 
ATOM   1950 N  N    . ALA   A 1 286 ? 20.574 46.385 -15.108 1.00 45.22 ? 286 ALA   A N    1 
ATOM   1951 C  CA   . ALA   A 1 286 ? 21.831 46.295 -15.859 1.00 45.03 ? 286 ALA   A CA   1 
ATOM   1952 C  C    . ALA   A 1 286 ? 22.896 47.224 -15.263 1.00 44.91 ? 286 ALA   A C    1 
ATOM   1953 O  O    . ALA   A 1 286 ? 24.071 46.942 -15.415 1.00 46.22 ? 286 ALA   A O    1 
ATOM   1954 C  CB   . ALA   A 1 286 ? 21.605 46.622 -17.330 1.00 45.04 ? 286 ALA   A CB   1 
ATOM   1955 N  N    . LYS   A 1 287 ? 22.502 48.309 -14.589 1.00 43.54 ? 287 LYS   A N    1 
ATOM   1956 C  CA   . LYS   A 1 287 ? 23.445 49.249 -13.966 1.00 43.90 ? 287 LYS   A CA   1 
ATOM   1957 C  C    . LYS   A 1 287 ? 23.712 48.957 -12.461 1.00 42.58 ? 287 LYS   A C    1 
ATOM   1958 O  O    . LYS   A 1 287 ? 24.521 49.647 -11.838 1.00 42.94 ? 287 LYS   A O    1 
ATOM   1959 C  CB   . LYS   A 1 287 ? 22.924 50.693 -14.093 1.00 46.73 ? 287 LYS   A CB   1 
ATOM   1960 C  CG   . LYS   A 1 287 ? 22.590 51.093 -15.517 1.00 51.45 ? 287 LYS   A CG   1 
ATOM   1961 C  CD   . LYS   A 1 287 ? 22.095 52.524 -15.543 1.00 57.09 ? 287 LYS   A CD   1 
ATOM   1962 C  CE   . LYS   A 1 287 ? 22.081 53.099 -16.948 1.00 61.09 ? 287 LYS   A CE   1 
ATOM   1963 N  NZ   . LYS   A 1 287 ? 21.464 54.450 -16.971 1.00 63.69 ? 287 LYS   A NZ   1 
ATOM   1964 N  N    . ARG   A 1 288 ? 23.021 47.965 -11.893 1.00 40.81 ? 288 ARG   A N    1 
ATOM   1965 C  CA   . ARG   A 1 288 ? 23.143 47.581 -10.500 1.00 40.21 ? 288 ARG   A CA   1 
ATOM   1966 C  C    . ARG   A 1 288 ? 24.444 46.824 -10.263 1.00 41.03 ? 288 ARG   A C    1 
ATOM   1967 O  O    . ARG   A 1 288 ? 24.760 45.916 -11.036 1.00 42.05 ? 288 ARG   A O    1 
ATOM   1968 C  CB   . ARG   A 1 288 ? 21.957 46.673 -10.131 1.00 39.03 ? 288 ARG   A CB   1 
ATOM   1969 C  CG   . ARG   A 1 288 ? 21.768 46.512 -8.626  1.00 37.62 ? 288 ARG   A CG   1 
ATOM   1970 C  CD   . ARG   A 1 288 ? 20.510 45.745 -8.329  1.00 38.18 ? 288 ARG   A CD   1 
ATOM   1971 N  NE   . ARG   A 1 288 ? 19.324 46.446 -8.827  1.00 38.84 ? 288 ARG   A NE   1 
ATOM   1972 C  CZ   . ARG   A 1 288 ? 18.217 45.840 -9.244  1.00 38.01 ? 288 ARG   A CZ   1 
ATOM   1973 N  NH1  . ARG   A 1 288 ? 18.124 44.517 -9.211  1.00 35.69 ? 288 ARG   A NH1  1 
ATOM   1974 N  NH2  . ARG   A 1 288 ? 17.195 46.552 -9.699  1.00 37.17 ? 288 ARG   A NH2  1 
ATOM   1975 N  N    . ILE   A 1 289 ? 25.152 47.107 -9.142  1.00 40.32 ? 289 ILE   A N    1 
ATOM   1976 C  CA   . ILE   A 1 289 ? 26.375 46.377 -8.797  1.00 40.09 ? 289 ILE   A CA   1 
ATOM   1977 C  C    . ILE   A 1 289 ? 26.107 44.864 -8.702  1.00 39.77 ? 289 ILE   A C    1 
ATOM   1978 O  O    . ILE   A 1 289 ? 24.981 44.454 -8.422  1.00 39.67 ? 289 ILE   A O    1 
ATOM   1979 C  CB   . ILE   A 1 289 ? 26.993 46.933 -7.485  1.00 41.11 ? 289 ILE   A CB   1 
ATOM   1980 C  CG1  . ILE   A 1 289 ? 28.465 46.555 -7.339  1.00 41.95 ? 289 ILE   A CG1  1 
ATOM   1981 C  CG2  . ILE   A 1 289 ? 26.179 46.544 -6.236  1.00 41.55 ? 289 ILE   A CG2  1 
ATOM   1982 C  CD1  . ILE   A 1 289 ? 29.164 47.387 -6.379  1.00 43.29 ? 289 ILE   A CD1  1 
ATOM   1983 N  N    . SER   A 1 290 ? 27.108 44.038 -9.036  1.00 39.16 ? 290 SER   A N    1 
ATOM   1984 C  CA   . SER   A 1 290 ? 26.977 42.593 -8.923  1.00 38.23 ? 290 SER   A CA   1 
ATOM   1985 C  C    . SER   A 1 290 ? 27.541 42.155 -7.571  1.00 38.93 ? 290 SER   A C    1 
ATOM   1986 O  O    . SER   A 1 290 ? 28.212 42.951 -6.896  1.00 39.36 ? 290 SER   A O    1 
ATOM   1987 C  CB   . SER   A 1 290 ? 27.739 41.907 -10.039 1.00 37.92 ? 290 SER   A CB   1 
ATOM   1988 O  OG   . SER   A 1 290 ? 29.109 42.229 -9.914  1.00 39.12 ? 290 SER   A OG   1 
ATOM   1989 N  N    . ALA   A 1 291 ? 27.266 40.902 -7.157  1.00 38.71 ? 291 ALA   A N    1 
ATOM   1990 C  CA   . ALA   A 1 291 ? 27.785 40.384 -5.891  1.00 40.08 ? 291 ALA   A CA   1 
ATOM   1991 C  C    . ALA   A 1 291 ? 29.319 40.347 -5.929  1.00 41.66 ? 291 ALA   A C    1 
ATOM   1992 O  O    . ALA   A 1 291 ? 29.964 40.703 -4.953  1.00 41.81 ? 291 ALA   A O    1 
ATOM   1993 C  CB   . ALA   A 1 291 ? 27.237 38.994 -5.634  1.00 39.64 ? 291 ALA   A CB   1 
ATOM   1994 N  N    . TYR   A 1 292 ? 29.888 40.006 -7.097  1.00 42.13 ? 292 TYR   A N    1 
ATOM   1995 C  CA   . TYR   A 1 292 ? 31.312 39.924 -7.302  1.00 43.55 ? 292 TYR   A CA   1 
ATOM   1996 C  C    . TYR   A 1 292 ? 32.011 41.264 -7.175  1.00 44.40 ? 292 TYR   A C    1 
ATOM   1997 O  O    . TYR   A 1 292 ? 33.045 41.336 -6.501  1.00 45.18 ? 292 TYR   A O    1 
ATOM   1998 C  CB   . TYR   A 1 292 ? 31.611 39.262 -8.644  1.00 44.23 ? 292 TYR   A CB   1 
ATOM   1999 C  CG   . TYR   A 1 292 ? 33.086 39.077 -8.869  1.00 45.53 ? 292 TYR   A CG   1 
ATOM   2000 C  CD1  . TYR   A 1 292 ? 33.815 38.183 -8.105  1.00 46.73 ? 292 TYR   A CD1  1 
ATOM   2001 C  CD2  . TYR   A 1 292 ? 33.759 39.805 -9.842  1.00 46.95 ? 292 TYR   A CD2  1 
ATOM   2002 C  CE1  . TYR   A 1 292 ? 35.162 37.965 -8.345  1.00 48.07 ? 292 TYR   A CE1  1 
ATOM   2003 C  CE2  . TYR   A 1 292 ? 35.122 39.654 -10.037 1.00 48.10 ? 292 TYR   A CE2  1 
ATOM   2004 C  CZ   . TYR   A 1 292 ? 35.819 38.721 -9.295  1.00 49.60 ? 292 TYR   A CZ   1 
ATOM   2005 O  OH   . TYR   A 1 292 ? 37.157 38.512 -9.520  1.00 52.56 ? 292 TYR   A OH   1 
ATOM   2006 N  N    . SER   A 1 293 ? 31.468 42.329 -7.793  1.00 44.34 ? 293 SER   A N    1 
ATOM   2007 C  CA   . SER   A 1 293 ? 32.069 43.658 -7.634  1.00 45.33 ? 293 SER   A CA   1 
ATOM   2008 C  C    . SER   A 1 293 ? 31.688 44.318 -6.307  1.00 46.45 ? 293 SER   A C    1 
ATOM   2009 O  O    . SER   A 1 293 ? 32.361 45.256 -5.891  1.00 47.80 ? 293 SER   A O    1 
ATOM   2010 C  CB   . SER   A 1 293 ? 31.789 44.568 -8.823  1.00 47.76 ? 293 SER   A CB   1 
ATOM   2011 O  OG   . SER   A 1 293 ? 30.525 44.330 -9.416  1.00 51.76 ? 293 SER   A OG   1 
ATOM   2012 N  N    . ALA   A 1 294 ? 30.613 43.850 -5.631  1.00 45.74 ? 294 ALA   A N    1 
ATOM   2013 C  CA   . ALA   A 1 294 ? 30.283 44.366 -4.301  1.00 45.17 ? 294 ALA   A CA   1 
ATOM   2014 C  C    . ALA   A 1 294 ? 31.361 43.841 -3.332  1.00 45.38 ? 294 ALA   A C    1 
ATOM   2015 O  O    . ALA   A 1 294 ? 31.840 44.607 -2.501  1.00 45.49 ? 294 ALA   A O    1 
ATOM   2016 C  CB   . ALA   A 1 294 ? 28.897 43.921 -3.868  1.00 44.47 ? 294 ALA   A CB   1 
ATOM   2017 N  N    . LEU   A 1 295 ? 31.817 42.579 -3.503  1.00 45.25 ? 295 LEU   A N    1 
ATOM   2018 C  CA   . LEU   A 1 295 ? 32.870 41.989 -2.685  1.00 46.06 ? 295 LEU   A CA   1 
ATOM   2019 C  C    . LEU   A 1 295 ? 34.187 42.804 -2.660  1.00 48.57 ? 295 LEU   A C    1 
ATOM   2020 O  O    . LEU   A 1 295 ? 34.937 42.743 -1.683  1.00 48.99 ? 295 LEU   A O    1 
ATOM   2021 C  CB   . LEU   A 1 295 ? 33.135 40.537 -3.127  1.00 44.79 ? 295 LEU   A CB   1 
ATOM   2022 C  CG   . LEU   A 1 295 ? 32.148 39.493 -2.603  1.00 44.26 ? 295 LEU   A CG   1 
ATOM   2023 C  CD1  . LEU   A 1 295 ? 32.368 38.135 -3.261  1.00 43.69 ? 295 LEU   A CD1  1 
ATOM   2024 C  CD2  . LEU   A 1 295 ? 32.220 39.371 -1.086  1.00 43.91 ? 295 LEU   A CD2  1 
ATOM   2025 N  N    . SER   A 1 296 ? 34.446 43.578 -3.711  1.00 50.34 ? 296 SER   A N    1 
ATOM   2026 C  CA   . SER   A 1 296 ? 35.645 44.402 -3.841  1.00 52.44 ? 296 SER   A CA   1 
ATOM   2027 C  C    . SER   A 1 296 ? 35.434 45.888 -3.500  1.00 53.91 ? 296 SER   A C    1 
ATOM   2028 O  O    . SER   A 1 296 ? 36.371 46.666 -3.651  1.00 54.79 ? 296 SER   A O    1 
ATOM   2029 C  CB   . SER   A 1 296 ? 36.177 44.309 -5.267  1.00 54.35 ? 296 SER   A CB   1 
ATOM   2030 O  OG   . SER   A 1 296 ? 37.193 43.328 -5.374  1.00 57.48 ? 296 SER   A OG   1 
ATOM   2031 N  N    . HIS   A 1 297 ? 34.220 46.293 -3.107  1.00 54.00 ? 297 HIS   A N    1 
ATOM   2032 C  CA   . HIS   A 1 297 ? 33.892 47.690 -2.821  1.00 54.59 ? 297 HIS   A CA   1 
ATOM   2033 C  C    . HIS   A 1 297 ? 34.746 48.213 -1.655  1.00 55.41 ? 297 HIS   A C    1 
ATOM   2034 O  O    . HIS   A 1 297 ? 35.026 47.459 -0.724  1.00 55.22 ? 297 HIS   A O    1 
ATOM   2035 C  CB   . HIS   A 1 297 ? 32.381 47.824 -2.515  1.00 54.89 ? 297 HIS   A CB   1 
ATOM   2036 C  CG   . HIS   A 1 297 ? 31.870 49.234 -2.478  1.00 56.70 ? 297 HIS   A CG   1 
ATOM   2037 N  ND1  . HIS   A 1 297 ? 31.897 49.982 -1.315  1.00 58.52 ? 297 HIS   A ND1  1 
ATOM   2038 C  CD2  . HIS   A 1 297 ? 31.347 49.993 -3.468  1.00 57.84 ? 297 HIS   A CD2  1 
ATOM   2039 C  CE1  . HIS   A 1 297 ? 31.400 51.167 -1.631  1.00 58.88 ? 297 HIS   A CE1  1 
ATOM   2040 N  NE2  . HIS   A 1 297 ? 31.046 51.222 -2.910  1.00 58.90 ? 297 HIS   A NE2  1 
ATOM   2041 N  N    . PRO   A 1 298 ? 35.202 49.489 -1.712  1.00 56.00 ? 298 PRO   A N    1 
ATOM   2042 C  CA   . PRO   A 1 298 ? 36.053 50.023 -0.631  1.00 56.41 ? 298 PRO   A CA   1 
ATOM   2043 C  C    . PRO   A 1 298 ? 35.479 49.898 0.786   1.00 56.51 ? 298 PRO   A C    1 
ATOM   2044 O  O    . PRO   A 1 298 ? 36.247 49.819 1.743   1.00 56.56 ? 298 PRO   A O    1 
ATOM   2045 C  CB   . PRO   A 1 298 ? 36.279 51.481 -1.041  1.00 57.13 ? 298 PRO   A CB   1 
ATOM   2046 C  CG   . PRO   A 1 298 ? 36.090 51.495 -2.509  1.00 57.45 ? 298 PRO   A CG   1 
ATOM   2047 C  CD   . PRO   A 1 298 ? 35.017 50.483 -2.787  1.00 55.70 ? 298 PRO   A CD   1 
ATOM   2048 N  N    . TYR   A 1 299 ? 34.150 49.786 0.918   1.00 56.39 ? 299 TYR   A N    1 
ATOM   2049 C  CA   . TYR   A 1 299 ? 33.485 49.562 2.197   1.00 56.76 ? 299 TYR   A CA   1 
ATOM   2050 C  C    . TYR   A 1 299 ? 34.052 48.320 2.931   1.00 57.98 ? 299 TYR   A C    1 
ATOM   2051 O  O    . TYR   A 1 299 ? 33.995 48.252 4.162   1.00 58.00 ? 299 TYR   A O    1 
ATOM   2052 C  CB   . TYR   A 1 299 ? 31.973 49.414 1.971   1.00 56.04 ? 299 TYR   A CB   1 
ATOM   2053 C  CG   . TYR   A 1 299 ? 31.211 48.979 3.200   1.00 55.90 ? 299 TYR   A CG   1 
ATOM   2054 C  CD1  . TYR   A 1 299 ? 31.050 49.835 4.283   1.00 56.57 ? 299 TYR   A CD1  1 
ATOM   2055 C  CD2  . TYR   A 1 299 ? 30.674 47.706 3.293   1.00 55.96 ? 299 TYR   A CD2  1 
ATOM   2056 C  CE1  . TYR   A 1 299 ? 30.364 49.436 5.422   1.00 56.96 ? 299 TYR   A CE1  1 
ATOM   2057 C  CE2  . TYR   A 1 299 ? 30.007 47.289 4.435   1.00 56.70 ? 299 TYR   A CE2  1 
ATOM   2058 C  CZ   . TYR   A 1 299 ? 29.851 48.157 5.499   1.00 57.58 ? 299 TYR   A CZ   1 
ATOM   2059 O  OH   . TYR   A 1 299 ? 29.156 47.758 6.617   1.00 58.50 ? 299 TYR   A OH   1 
ATOM   2060 N  N    . PHE   A 1 300 ? 34.597 47.345 2.180   1.00 58.62 ? 300 PHE   A N    1 
ATOM   2061 C  CA   . PHE   A 1 300 ? 35.161 46.143 2.779   1.00 59.78 ? 300 PHE   A CA   1 
ATOM   2062 C  C    . PHE   A 1 300 ? 36.689 46.171 2.932   1.00 62.76 ? 300 PHE   A C    1 
ATOM   2063 O  O    . PHE   A 1 300 ? 37.263 45.194 3.411   1.00 63.26 ? 300 PHE   A O    1 
ATOM   2064 C  CB   . PHE   A 1 300 ? 34.706 44.897 2.022   1.00 58.46 ? 300 PHE   A CB   1 
ATOM   2065 C  CG   . PHE   A 1 300 ? 33.208 44.706 2.006   1.00 57.51 ? 300 PHE   A CG   1 
ATOM   2066 C  CD1  . PHE   A 1 300 ? 32.523 44.366 3.163   1.00 57.50 ? 300 PHE   A CD1  1 
ATOM   2067 C  CD2  . PHE   A 1 300 ? 32.489 44.836 0.829   1.00 57.26 ? 300 PHE   A CD2  1 
ATOM   2068 C  CE1  . PHE   A 1 300 ? 31.152 44.154 3.139   1.00 57.85 ? 300 PHE   A CE1  1 
ATOM   2069 C  CE2  . PHE   A 1 300 ? 31.121 44.624 0.806   1.00 57.63 ? 300 PHE   A CE2  1 
ATOM   2070 C  CZ   . PHE   A 1 300 ? 30.457 44.304 1.963   1.00 57.89 ? 300 PHE   A CZ   1 
ATOM   2071 N  N    . GLN   A 1 301 ? 37.326 47.243 2.481   1.00 64.60 ? 301 GLN   A N    1 
ATOM   2072 C  CA   . GLN   A 1 301 ? 38.806 47.338 2.571   1.00 66.79 ? 301 GLN   A CA   1 
ATOM   2073 C  C    . GLN   A 1 301 ? 39.198 47.620 4.024   1.00 67.70 ? 301 GLN   A C    1 
ATOM   2074 O  O    . GLN   A 1 301 ? 40.288 47.251 4.434   1.00 68.13 ? 301 GLN   A O    1 
ATOM   2075 C  CB   . GLN   A 1 301 ? 39.331 48.396 1.601   1.00 69.72 ? 301 GLN   A CB   1 
ATOM   2076 C  CG   . GLN   A 1 301 ? 39.215 47.980 0.141   1.00 75.51 ? 301 GLN   A CG   1 
ATOM   2077 C  CD   . GLN   A 1 301 ? 39.315 49.148 -0.808  1.00 82.48 ? 301 GLN   A CD   1 
ATOM   2078 O  OE1  . GLN   A 1 301 ? 39.433 50.299 -0.395  1.00 84.05 ? 301 GLN   A OE1  1 
ATOM   2079 N  NE2  . GLN   A 1 301 ? 39.254 48.861 -2.097  1.00 84.35 ? 301 GLN   A NE2  1 
HETATM 2080 C  C12  . A1AZ4 B 2 .   ? 14.284 27.144 6.698   1.00 40.86 ? 401 A1AZ4 A C12  1 
HETATM 2081 C  C10  . A1AZ4 B 2 .   ? 15.137 25.117 5.715   1.00 40.45 ? 401 A1AZ4 A C10  1 
HETATM 2082 C  C28  . A1AZ4 B 2 .   ? 18.332 25.361 8.684   1.00 40.71 ? 401 A1AZ4 A C28  1 
HETATM 2083 C  C11  . A1AZ4 B 2 .   ? 15.216 26.107 6.699   1.00 40.77 ? 401 A1AZ4 A C11  1 
HETATM 2084 C  C7   . A1AZ4 B 2 .   ? 13.191 26.163 4.752   1.00 40.82 ? 401 A1AZ4 A C7   1 
HETATM 2085 C  C13  . A1AZ4 B 2 .   ? 13.289 27.144 5.731   1.00 40.92 ? 401 A1AZ4 A C13  1 
HETATM 2086 C  C8   . A1AZ4 B 2 .   ? 14.152 25.182 4.762   1.00 40.65 ? 401 A1AZ4 A C8   1 
HETATM 2087 C  C29  . A1AZ4 B 2 .   ? 17.524 25.491 7.569   1.00 41.09 ? 401 A1AZ4 A C29  1 
HETATM 2088 C  C14  . A1AZ4 B 2 .   ? 16.272 26.068 7.746   1.00 41.33 ? 401 A1AZ4 A C14  1 
HETATM 2089 C  C5   . A1AZ4 B 2 .   ? 11.478 27.424 4.482   1.00 41.47 ? 401 A1AZ4 A C5   1 
HETATM 2090 C  C16  . A1AZ4 B 2 .   ? 16.761 26.380 9.960   1.00 41.69 ? 401 A1AZ4 A C16  1 
HETATM 2091 C  C20  . A1AZ4 B 2 .   ? 15.352 29.047 11.054  1.00 45.00 ? 401 A1AZ4 A C20  1 
HETATM 2092 C  C21  . A1AZ4 B 2 .   ? 14.148 29.835 11.516  1.00 45.86 ? 401 A1AZ4 A C21  1 
HETATM 2093 C  C23  . A1AZ4 B 2 .   ? 13.640 28.329 13.272  1.00 46.04 ? 401 A1AZ4 A C23  1 
HETATM 2094 C  C18  . A1AZ4 B 2 .   ? 15.202 27.589 11.491  1.00 44.23 ? 401 A1AZ4 A C18  1 
HETATM 2095 C  C24  . A1AZ4 B 2 .   ? 14.880 27.505 12.980  1.00 45.52 ? 401 A1AZ4 A C24  1 
HETATM 2096 C  C1   . A1AZ4 B 2 .   ? 13.044 30.213 6.127   1.00 39.74 ? 401 A1AZ4 A C1   1 
HETATM 2097 C  C3   . A1AZ4 B 2 .   ? 11.548 28.935 7.728   1.00 39.71 ? 401 A1AZ4 A C3   1 
HETATM 2098 C  C32  . A1AZ4 B 2 .   ? 9.069  27.870 4.976   1.00 41.20 ? 401 A1AZ4 A C32  1 
HETATM 2099 C  C33  . A1AZ4 B 2 .   ? 9.693  27.254 2.627   1.00 40.87 ? 401 A1AZ4 A C33  1 
HETATM 2100 C  C2   . A1AZ4 B 2 .   ? 11.903 29.216 6.275   1.00 40.19 ? 401 A1AZ4 A C2   1 
HETATM 2101 C  C31  . A1AZ4 B 2 .   ? 10.152 27.947 3.906   1.00 41.46 ? 401 A1AZ4 A C31  1 
HETATM 2102 N  N27  . A1AZ4 B 2 .   ? 17.966 25.798 9.892   1.00 40.91 ? 401 A1AZ4 A N27  1 
HETATM 2103 N  N6   . A1AZ4 B 2 .   ? 12.051 26.350 3.979   1.00 41.26 ? 401 A1AZ4 A N6   1 
HETATM 2104 N  N15  . A1AZ4 B 2 .   ? 15.891 26.550 8.942   1.00 41.58 ? 401 A1AZ4 A N15  1 
HETATM 2105 N  N4   . A1AZ4 B 2 .   ? 12.181 27.965 5.534   1.00 40.57 ? 401 A1AZ4 A N4   1 
HETATM 2106 N  N17  . A1AZ4 B 2 .   ? 16.389 26.813 11.185  1.00 42.42 ? 401 A1AZ4 A N17  1 
HETATM 2107 O  O22  . A1AZ4 B 2 .   ? 13.941 29.695 12.932  1.00 46.72 ? 401 A1AZ4 A O22  1 
HETATM 2108 O  O26  . A1AZ4 B 2 .   ? 14.667 26.155 13.395  1.00 46.15 ? 401 A1AZ4 A O26  1 
HETATM 2109 O  O34  . A1AZ4 B 2 .   ? 10.311 29.328 3.559   1.00 42.18 ? 401 A1AZ4 A O34  1 
HETATM 2110 F  F9   . A1AZ4 B 2 .   ? 14.151 24.279 3.760   1.00 40.47 ? 401 A1AZ4 A F9   1 
HETATM 2111 CL CL30 . A1AZ4 B 2 .   ? 18.154 25.061 6.014   1.00 41.55 ? 401 A1AZ4 A CL30 1 
HETATM 2112 O  O    . HOH   C 3 .   ? 16.666 64.863 -6.692  1.00 67.92 ? 501 HOH   A O    1 
HETATM 2113 O  O    . HOH   C 3 .   ? 25.514 23.224 0.427   1.00 41.19 ? 502 HOH   A O    1 
HETATM 2114 O  O    . HOH   C 3 .   ? 21.266 48.074 13.928  1.00 48.48 ? 503 HOH   A O    1 
HETATM 2115 O  O    . HOH   C 3 .   ? -1.619 44.861 -8.139  1.00 60.28 ? 504 HOH   A O    1 
HETATM 2116 O  O    . HOH   C 3 .   ? 14.588 46.196 4.285   1.00 37.03 ? 505 HOH   A O    1 
HETATM 2117 O  O    . HOH   C 3 .   ? 27.929 24.673 -0.985  1.00 40.88 ? 506 HOH   A O    1 
HETATM 2118 O  O    . HOH   C 3 .   ? 23.410 42.946 -9.866  1.00 40.91 ? 507 HOH   A O    1 
HETATM 2119 O  O    . HOH   C 3 .   ? 25.837 50.244 -9.659  1.00 51.31 ? 508 HOH   A O    1 
HETATM 2120 O  O    . HOH   C 3 .   ? 20.680 39.088 18.638  1.00 65.47 ? 509 HOH   A O    1 
HETATM 2121 O  O    . HOH   C 3 .   ? 18.338 24.240 -7.657  1.00 45.95 ? 510 HOH   A O    1 
HETATM 2122 O  O    . HOH   C 3 .   ? 23.966 40.335 -10.468 1.00 38.03 ? 511 HOH   A O    1 
HETATM 2123 O  O    . HOH   C 3 .   ? 41.618 49.141 5.750   1.00 68.31 ? 512 HOH   A O    1 
HETATM 2124 O  O    . HOH   C 3 .   ? 30.852 41.768 -11.875 1.00 39.46 ? 513 HOH   A O    1 
HETATM 2125 O  O    . HOH   C 3 .   ? 29.012 45.660 -11.170 1.00 51.65 ? 514 HOH   A O    1 
HETATM 2126 O  O    . HOH   C 3 .   ? 12.380 38.446 -0.941  1.00 35.01 ? 515 HOH   A O    1 
HETATM 2127 O  O    . HOH   C 3 .   ? 12.723 46.626 2.522   1.00 40.19 ? 516 HOH   A O    1 
HETATM 2128 O  O    . HOH   C 3 .   ? 8.499  36.873 -0.030  1.00 66.81 ? 517 HOH   A O    1 
HETATM 2129 O  O    . HOH   C 3 .   ? 25.800 25.971 -15.042 1.00 65.92 ? 518 HOH   A O    1 
HETATM 2130 O  O    . HOH   C 3 .   ? 24.150 45.722 20.233  1.00 65.32 ? 519 HOH   A O    1 
HETATM 2131 O  O    . HOH   C 3 .   ? 4.501  46.598 -15.058 1.00 54.56 ? 520 HOH   A O    1 
HETATM 2132 O  O    . HOH   C 3 .   ? 19.444 54.332 -6.633  1.00 48.00 ? 521 HOH   A O    1 
HETATM 2133 O  O    . HOH   C 3 .   ? 31.856 33.886 -3.575  1.00 48.34 ? 522 HOH   A O    1 
HETATM 2134 O  O    . HOH   C 3 .   ? 15.862 29.758 -6.381  1.00 46.47 ? 523 HOH   A O    1 
HETATM 2135 O  O    . HOH   C 3 .   ? 32.652 20.361 -7.221  1.00 53.30 ? 524 HOH   A O    1 
HETATM 2136 O  O    . HOH   C 3 .   ? 4.158  55.816 -2.235  1.00 47.85 ? 525 HOH   A O    1 
HETATM 2137 O  O    . HOH   C 3 .   ? 11.844 46.164 -2.305  1.00 33.43 ? 526 HOH   A O    1 
HETATM 2138 O  O    . HOH   C 3 .   ? 8.638  23.575 -3.351  1.00 62.24 ? 527 HOH   A O    1 
HETATM 2139 O  O    . HOH   C 3 .   ? 21.959 24.031 0.476   1.00 46.81 ? 528 HOH   A O    1 
HETATM 2140 O  O    . HOH   C 3 .   ? 13.939 30.948 -3.145  1.00 54.71 ? 529 HOH   A O    1 
HETATM 2141 O  O    . HOH   C 3 .   ? 32.351 30.795 -7.016  1.00 42.66 ? 530 HOH   A O    1 
HETATM 2142 O  O    . HOH   C 3 .   ? 15.597 27.656 16.791  1.00 51.37 ? 531 HOH   A O    1 
HETATM 2143 O  O    . HOH   C 3 .   ? 12.798 39.041 -3.938  1.00 40.31 ? 532 HOH   A O    1 
HETATM 2144 O  O    . HOH   C 3 .   ? 24.116 16.561 -8.962  1.00 41.16 ? 533 HOH   A O    1 
HETATM 2145 O  O    . HOH   C 3 .   ? 15.915 37.826 -3.779  1.00 28.53 ? 534 HOH   A O    1 
HETATM 2146 O  O    . HOH   C 3 .   ? 28.826 18.418 4.694   1.00 65.84 ? 535 HOH   A O    1 
HETATM 2147 O  O    . HOH   C 3 .   ? 9.249  49.466 8.663   1.00 67.11 ? 536 HOH   A O    1 
HETATM 2148 O  O    . HOH   C 3 .   ? 14.191 40.679 -5.538  1.00 48.12 ? 537 HOH   A O    1 
HETATM 2149 O  O    . HOH   C 3 .   ? 17.341 25.308 2.480   1.00 42.34 ? 538 HOH   A O    1 
HETATM 2150 O  O    . HOH   C 3 .   ? 22.290 30.800 16.108  1.00 54.86 ? 539 HOH   A O    1 
HETATM 2151 O  O    . HOH   C 3 .   ? 23.569 23.263 -1.698  1.00 44.92 ? 540 HOH   A O    1 
HETATM 2152 O  O    . HOH   C 3 .   ? 18.157 54.048 -9.112  1.00 55.87 ? 541 HOH   A O    1 
HETATM 2153 O  O    . HOH   C 3 .   ? 28.380 17.372 -9.152  1.00 49.80 ? 542 HOH   A O    1 
HETATM 2154 O  O    . HOH   C 3 .   ? 21.123 23.708 15.947  1.00 55.92 ? 543 HOH   A O    1 
HETATM 2155 O  O    . HOH   C 3 .   ? 0.167  36.693 2.795   1.00 57.01 ? 544 HOH   A O    1 
HETATM 2156 O  O    . HOH   C 3 .   ? 4.006  42.690 1.854   1.00 48.21 ? 545 HOH   A O    1 
HETATM 2157 O  O    . HOH   C 3 .   ? 11.093 31.154 -0.443  1.00 66.06 ? 546 HOH   A O    1 
HETATM 2158 O  O    . HOH   C 3 .   ? 12.434 31.933 9.319   1.00 44.19 ? 547 HOH   A O    1 
HETATM 2159 O  O    . HOH   C 3 .   ? 27.594 15.122 7.885   1.00 63.95 ? 548 HOH   A O    1 
HETATM 2160 O  O    . HOH   C 3 .   ? 7.212  63.194 -10.604 1.00 61.07 ? 549 HOH   A O    1 
HETATM 2161 O  O    . HOH   C 3 .   ? 10.118 25.559 -0.728  1.00 53.74 ? 550 HOH   A O    1 
HETATM 2162 O  O    . HOH   C 3 .   ? 32.157 24.730 4.849   1.00 53.06 ? 551 HOH   A O    1 
HETATM 2163 O  O    . HOH   C 3 .   ? 9.887  28.966 13.183  1.00 59.76 ? 552 HOH   A O    1 
HETATM 2164 O  O    . HOH   C 3 .   ? 2.551  44.938 4.426   1.00 51.99 ? 553 HOH   A O    1 
HETATM 2165 O  O    . HOH   C 3 .   ? 14.510 17.444 20.980  1.00 44.44 ? 554 HOH   A O    1 
HETATM 2166 O  O    . HOH   C 3 .   ? 15.920 24.683 -0.258  1.00 63.05 ? 555 HOH   A O    1 
HETATM 2167 O  O    . HOH   C 3 .   ? 10.904 11.972 6.084   1.00 62.39 ? 556 HOH   A O    1 
HETATM 2168 O  O    . HOH   C 3 .   ? 17.351 41.392 -12.663 1.00 42.17 ? 557 HOH   A O    1 
HETATM 2169 O  O    . HOH   C 3 .   ? 8.582  52.559 3.118   1.00 54.19 ? 558 HOH   A O    1 
HETATM 2170 O  O    . HOH   C 3 .   ? -0.199 42.623 -4.954  1.00 57.56 ? 559 HOH   A O    1 
HETATM 2171 O  O    . HOH   C 3 .   ? 17.922 29.304 -10.028 1.00 46.45 ? 560 HOH   A O    1 
HETATM 2172 O  O    . HOH   C 3 .   ? 25.919 49.999 17.366  1.00 56.93 ? 561 HOH   A O    1 
HETATM 2173 O  O    . HOH   C 3 .   ? 14.140 28.696 -8.282  1.00 80.71 ? 562 HOH   A O    1 
HETATM 2174 O  O    . HOH   C 3 .   ? 35.272 21.385 -3.122  1.00 69.43 ? 563 HOH   A O    1 
HETATM 2175 O  O    . HOH   C 3 .   ? 11.609 32.042 13.669  1.00 50.25 ? 564 HOH   A O    1 
HETATM 2176 O  O    . HOH   C 3 .   ? 6.207  27.612 13.460  1.00 66.30 ? 565 HOH   A O    1 
HETATM 2177 O  O    . HOH   C 3 .   ? 6.015  12.335 -10.844 1.00 70.20 ? 566 HOH   A O    1 
HETATM 2178 O  O    . HOH   C 3 .   ? 15.971 55.526 -10.028 1.00 53.01 ? 567 HOH   A O    1 
HETATM 2179 O  O    . HOH   C 3 .   ? 4.266  56.507 -5.820  1.00 53.89 ? 568 HOH   A O    1 
HETATM 2180 O  O    . HOH   C 3 .   ? 19.397 53.592 -12.415 1.00 50.03 ? 569 HOH   A O    1 
HETATM 2181 O  O    . HOH   C 3 .   ? 27.645 48.162 -12.571 1.00 69.12 ? 570 HOH   A O    1 
HETATM 2182 O  O    . HOH   C 3 .   ? 33.935 35.355 8.868   1.00 59.22 ? 571 HOH   A O    1 
HETATM 2183 O  O    . HOH   C 3 .   ? 20.193 34.938 -14.263 1.00 52.26 ? 572 HOH   A O    1 
HETATM 2184 O  O    . HOH   C 3 .   ? 23.761 27.379 15.117  1.00 34.47 ? 573 HOH   A O    1 
HETATM 2185 O  O    . HOH   C 3 .   ? 4.826  52.297 6.636   1.00 74.32 ? 574 HOH   A O    1 
HETATM 2186 O  O    . HOH   C 3 .   ? 26.455 16.301 -7.550  1.00 51.69 ? 575 HOH   A O    1 
HETATM 2187 O  O    . HOH   C 3 .   ? 8.289  8.082  -2.736  1.00 71.79 ? 576 HOH   A O    1 
HETATM 2188 O  O    . HOH   C 3 .   ? 29.227 27.429 12.160  1.00 56.02 ? 577 HOH   A O    1 
HETATM 2189 O  O    . HOH   C 3 .   ? 28.854 16.599 -1.602  1.00 45.42 ? 578 HOH   A O    1 
HETATM 2190 O  O    . HOH   C 3 .   ? 19.161 25.310 0.157   1.00 52.64 ? 579 HOH   A O    1 
HETATM 2191 O  O    . HOH   C 3 .   ? 6.101  18.292 14.727  1.00 62.32 ? 580 HOH   A O    1 
HETATM 2192 O  O    . HOH   C 3 .   ? 20.121 63.425 -2.414  1.00 71.18 ? 581 HOH   A O    1 
HETATM 2193 O  O    . HOH   C 3 .   ? 29.110 59.534 8.237   1.00 62.55 ? 582 HOH   A O    1 
HETATM 2194 O  O    . HOH   C 3 .   ? 32.626 31.777 -4.592  1.00 44.43 ? 583 HOH   A O    1 
HETATM 2195 O  O    . HOH   C 3 .   ? 16.684 38.971 -17.762 1.00 47.00 ? 584 HOH   A O    1 
HETATM 2196 O  O    . HOH   C 3 .   ? 23.060 50.671 26.870  1.00 80.76 ? 585 HOH   A O    1 
HETATM 2197 O  O    . HOH   C 3 .   ? 14.319 7.643  5.874   1.00 68.53 ? 586 HOH   A O    1 
HETATM 2198 O  O    . HOH   C 3 .   ? 35.624 43.779 -9.667  1.00 65.59 ? 587 HOH   A O    1 
HETATM 2199 O  O    . HOH   C 3 .   ? 15.756 5.886  2.476   1.00 64.59 ? 588 HOH   A O    1 
HETATM 2200 O  O    . HOH   C 3 .   ? 3.954  10.402 -11.894 1.00 66.52 ? 589 HOH   A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N    . GLN   A 11  ? 0.9673 0.8453 0.8296 0.0763  0.0218  0.0950  11  GLN   A N    
2    C  CA   . GLN   A 11  ? 0.9674 0.8561 0.8357 0.0811  0.0144  0.0884  11  GLN   A CA   
3    C  C    . GLN   A 11  ? 0.9568 0.8525 0.8153 0.0949  0.0149  0.0864  11  GLN   A C    
4    O  O    . GLN   A 11  ? 0.9661 0.8623 0.8160 0.1003  0.0206  0.0898  11  GLN   A O    
5    C  CB   . GLN   A 11  ? 0.9820 0.8927 0.8750 0.0744  0.0123  0.0851  11  GLN   A CB   
6    C  CG   . GLN   A 11  ? 1.0384 0.9504 0.9383 0.0724  0.0034  0.0794  11  GLN   A CG   
7    C  CD   . GLN   A 11  ? 1.0993 1.0325 1.0104 0.0776  0.0010  0.0742  11  GLN   A CD   
8    O  OE1  . GLN   A 11  ? 1.1263 1.0593 1.0297 0.0857  -0.0022 0.0706  11  GLN   A OE1  
9    N  NE2  . GLN   A 11  ? 1.0914 1.0431 1.0212 0.0730  0.0027  0.0738  11  GLN   A NE2  
10   N  N    . GLN   A 12  ? 0.9320 0.8327 0.7914 0.1003  0.0088  0.0810  12  GLN   A N    
11   C  CA   . GLN   A 12  ? 0.9087 0.8180 0.7621 0.1122  0.0078  0.0782  12  GLN   A CA   
12   C  C    . GLN   A 12  ? 0.8588 0.7927 0.7265 0.1138  0.0086  0.0752  12  GLN   A C    
13   O  O    . GLN   A 12  ? 0.8505 0.7928 0.7136 0.1229  0.0085  0.0736  12  GLN   A O    
14   C  CB   . GLN   A 12  ? 0.9411 0.8447 0.7905 0.1160  0.0017  0.0740  12  GLN   A CB   
15   C  CG   . GLN   A 12  ? 1.0089 0.9101 0.8447 0.1287  0.0015  0.0735  12  GLN   A CG   
16   C  CD   . GLN   A 12  ? 1.0586 0.9759 0.9024 0.1340  -0.0022 0.0679  12  GLN   A CD   
17   O  OE1  . GLN   A 12  ? 1.0720 0.9833 0.9136 0.1355  -0.0056 0.0650  12  GLN   A OE1  
18   N  NE2  . GLN   A 12  ? 1.0545 0.9912 0.9063 0.1373  -0.0012 0.0662  12  GLN   A NE2  
19   N  N    . TYR   A 13  ? 0.8253 0.7704 0.7102 0.1052  0.0088  0.0742  13  TYR   A N    
20   C  CA   . TYR   A 13  ? 0.7960 0.7628 0.6948 0.1059  0.0096  0.0712  13  TYR   A CA   
21   C  C    . TYR   A 13  ? 0.7983 0.7715 0.7066 0.0995  0.0156  0.0748  13  TYR   A C    
22   O  O    . TYR   A 13  ? 0.8038 0.7701 0.7178 0.0906  0.0165  0.0776  13  TYR   A O    
23   C  CB   . TYR   A 13  ? 0.7695 0.7454 0.6811 0.1033  0.0034  0.0654  13  TYR   A CB   
24   C  CG   . TYR   A 13  ? 0.7591 0.7309 0.6623 0.1101  -0.0014 0.0617  13  TYR   A CG   
25   C  CD1  . TYR   A 13  ? 0.7577 0.7403 0.6584 0.1184  -0.0016 0.0589  13  TYR   A CD1  
26   C  CD2  . TYR   A 13  ? 0.7680 0.7245 0.6653 0.1082  -0.0056 0.0610  13  TYR   A CD2  
27   C  CE1  . TYR   A 13  ? 0.7656 0.7457 0.6601 0.1246  -0.0052 0.0559  13  TYR   A CE1  
28   C  CE2  . TYR   A 13  ? 0.7749 0.7275 0.6642 0.1150  -0.0088 0.0579  13  TYR   A CE2  
29   C  CZ   . TYR   A 13  ? 0.7767 0.7420 0.6656 0.1232  -0.0082 0.0555  13  TYR   A CZ   
30   O  OH   . TYR   A 13  ? 0.7771 0.7407 0.6602 0.1298  -0.0107 0.0526  13  TYR   A OH   
31   N  N    . GLU   A 14  ? 0.7969 0.7829 0.7069 0.1038  0.0199  0.0749  14  GLU   A N    
32   C  CA   . GLU   A 14  ? 0.8042 0.7969 0.7224 0.0991  0.0271  0.0785  14  GLU   A CA   
33   C  C    . GLU   A 14  ? 0.8070 0.8199 0.7397 0.0997  0.0273  0.0747  14  GLU   A C    
34   O  O    . GLU   A 14  ? 0.8102 0.8301 0.7369 0.1073  0.0278  0.0725  14  GLU   A O    
35   C  CB   . GLU   A 14  ? 0.8382 0.8223 0.7396 0.1043  0.0340  0.0836  14  GLU   A CB   
36   C  CG   . GLU   A 14  ? 0.8944 0.8824 0.8012 0.0998  0.0432  0.0884  14  GLU   A CG   
37   C  CD   . GLU   A 14  ? 0.9703 0.9576 0.8620 0.1083  0.0489  0.0907  14  GLU   A CD   
38   O  OE1  . GLU   A 14  ? 0.9794 0.9508 0.8527 0.1118  0.0516  0.0949  14  GLU   A OE1  
39   O  OE2  . GLU   A 14  ? 0.9951 0.9967 0.8919 0.1118  0.0503  0.0880  14  GLU   A OE2  
40   N  N    . CYS   A 15  ? 0.8051 0.8267 0.7565 0.0918  0.0266  0.0740  15  CYS   A N    
41   C  CA   . CYS   A 15  ? 0.8050 0.8448 0.7709 0.0922  0.0268  0.0705  15  CYS   A CA   
42   C  C    . CYS   A 15  ? 0.7984 0.8455 0.7625 0.0957  0.0356  0.0733  15  CYS   A C    
43   O  O    . CYS   A 15  ? 0.8042 0.8477 0.7686 0.0920  0.0430  0.0789  15  CYS   A O    
44   C  CB   . CYS   A 15  ? 0.8183 0.8650 0.8043 0.0836  0.0240  0.0698  15  CYS   A CB   
45   S  SG   . CYS   A 15  ? 0.8915 0.9279 0.8781 0.0795  0.0130  0.0662  15  CYS   A SG   
46   N  N    . VAL   A 16  ? 0.7893 0.8456 0.7506 0.1026  0.0351  0.0693  16  VAL   A N    
47   C  CA   . VAL   A 16  ? 0.7896 0.8518 0.7466 0.1071  0.0428  0.0710  16  VAL   A CA   
48   C  C    . VAL   A 16  ? 0.7824 0.8604 0.7552 0.1063  0.0444  0.0684  16  VAL   A C    
49   O  O    . VAL   A 16  ? 0.7911 0.8744 0.7648 0.1078  0.0526  0.0710  16  VAL   A O    
50   C  CB   . VAL   A 16  ? 0.8065 0.8643 0.7438 0.1165  0.0418  0.0694  16  VAL   A CB   
51   C  CG1  . VAL   A 16  ? 0.8213 0.8632 0.7423 0.1183  0.0420  0.0733  16  VAL   A CG1  
52   C  CG2  . VAL   A 16  ? 0.8092 0.8732 0.7471 0.1204  0.0334  0.0624  16  VAL   A CG2  
53   N  N    . ALA   A 17  ? 0.7702 0.8548 0.7543 0.1045  0.0371  0.0633  17  ALA   A N    
54   C  CA   . ALA   A 17  ? 0.7607 0.8593 0.7590 0.1046  0.0376  0.0603  17  ALA   A CA   
55   C  C    . ALA   A 17  ? 0.7567 0.8585 0.7671 0.1008  0.0289  0.0561  17  ALA   A C    
56   O  O    . ALA   A 17  ? 0.7596 0.8527 0.7649 0.0994  0.0224  0.0546  17  ALA   A O    
57   C  CB   . ALA   A 17  ? 0.7594 0.8621 0.7476 0.1126  0.0388  0.0567  17  ALA   A CB   
58   N  N    . GLU   A 18  ? 0.7505 0.8643 0.7761 0.0999  0.0291  0.0543  18  GLU   A N    
59   C  CA   . GLU   A 18  ? 0.7530 0.8704 0.7896 0.0974  0.0210  0.0501  18  GLU   A CA   
60   C  C    . GLU   A 18  ? 0.7587 0.8784 0.7884 0.1036  0.0177  0.0442  18  GLU   A C    
61   O  O    . GLU   A 18  ? 0.7607 0.8859 0.7868 0.1086  0.0228  0.0434  18  GLU   A O    
62   C  CB   . GLU   A 18  ? 0.7747 0.9040 0.8322 0.0931  0.0229  0.0518  18  GLU   A CB   
63   C  CG   . GLU   A 18  ? 0.8419 0.9710 0.9111 0.0877  0.0138  0.0497  18  GLU   A CG   
64   C  CD   . GLU   A 18  ? 0.9221 1.0655 1.0132 0.0848  0.0143  0.0506  18  GLU   A CD   
65   O  OE1  . GLU   A 18  ? 0.9401 1.0885 1.0432 0.0793  0.0190  0.0557  18  GLU   A OE1  
66   O  OE2  . GLU   A 18  ? 0.9393 1.0892 1.0360 0.0881  0.0103  0.0464  18  GLU   A OE2  
67   N  N    . ILE   A 19  ? 0.7612 0.8752 0.7877 0.1031  0.0096  0.0400  19  ILE   A N    
68   C  CA   . ILE   A 19  ? 0.7719 0.8866 0.7923 0.1076  0.0057  0.0342  19  ILE   A CA   
69   C  C    . ILE   A 19  ? 0.7849 0.9059 0.8184 0.1063  0.0018  0.0313  19  ILE   A C    
70   O  O    . ILE   A 19  ? 0.7823 0.9081 0.8152 0.1104  0.0022  0.0278  19  ILE   A O    
71   C  CB   . ILE   A 19  ? 0.7754 0.8798 0.7836 0.1084  0.0003  0.0319  19  ILE   A CB   
72   C  CG1  . ILE   A 19  ? 0.7916 0.8915 0.7864 0.1117  0.0040  0.0344  19  ILE   A CG1  
73   C  CG2  . ILE   A 19  ? 0.7739 0.8787 0.7785 0.1111  -0.0043 0.0260  19  ILE   A CG2  
74   C  CD1  . ILE   A 19  ? 0.8095 0.9005 0.7937 0.1130  -0.0006 0.0329  19  ILE   A CD1  
75   N  N    . GLY   A 20  ? 0.7939 0.9141 0.8382 0.1008  -0.0022 0.0328  20  GLY   A N    
76   C  CA   . GLY   A 20  ? 0.8069 0.9324 0.8639 0.0994  -0.0070 0.0306  20  GLY   A CA   
77   C  C    . GLY   A 20  ? 0.8267 0.9495 0.8939 0.0927  -0.0127 0.0323  20  GLY   A C    
78   O  O    . GLY   A 20  ? 0.8227 0.9398 0.8890 0.0882  -0.0120 0.0359  20  GLY   A O    
79   N  N    . GLU   A 21  ? 0.8437 0.9698 0.9200 0.0923  -0.0189 0.0295  21  GLU   A N    
80   C  CA   . GLU   A 21  ? 0.8649 0.9888 0.9514 0.0863  -0.0262 0.0301  21  GLU   A CA   
81   C  C    . GLU   A 21  ? 0.8880 1.0018 0.9675 0.0870  -0.0355 0.0254  21  GLU   A C    
82   O  O    . GLU   A 21  ? 0.8875 1.0045 0.9675 0.0913  -0.0376 0.0219  21  GLU   A O    
83   C  CB   . GLU   A 21  ? 0.8862 1.0258 0.9944 0.0845  -0.0252 0.0323  21  GLU   A CB   
84   C  CG   . GLU   A 21  ? 0.9511 1.0984 1.0693 0.0804  -0.0175 0.0382  21  GLU   A CG   
85   C  CD   . GLU   A 21  ? 1.0422 1.1970 1.1807 0.0730  -0.0213 0.0410  21  GLU   A CD   
86   O  OE1  . GLU   A 21  ? 1.0708 1.2154 1.2077 0.0672  -0.0295 0.0405  21  GLU   A OE1  
87   O  OE2  . GLU   A 21  ? 1.0612 1.2321 1.2173 0.0727  -0.0157 0.0439  21  GLU   A OE2  
88   N  N    . GLY   A 22  ? 0.9072 1.0076 0.9789 0.0829  -0.0406 0.0256  22  GLY   A N    
89   C  CA   . GLY   A 22  ? 0.9337 1.0220 0.9976 0.0828  -0.0493 0.0218  22  GLY   A CA   
90   C  C    . GLY   A 22  ? 0.9486 1.0380 1.0254 0.0774  -0.0571 0.0224  22  GLY   A C    
91   O  O    . GLY   A 22  ? 0.9437 1.0453 1.0373 0.0738  -0.0553 0.0257  22  GLY   A O    
92   N  N    . ALA   A 23  ? 0.9646 1.0411 1.0336 0.0766  -0.0659 0.0194  23  ALA   A N    
93   C  CA   . ALA   A 23  ? 0.9743 1.0505 1.0541 0.0715  -0.0752 0.0195  23  ALA   A CA   
94   C  C    . ALA   A 23  ? 0.9934 1.0492 1.0600 0.0672  -0.0826 0.0187  23  ALA   A C    
95   O  O    . ALA   A 23  ? 1.0143 1.0566 1.0664 0.0702  -0.0874 0.0151  23  ALA   A O    
96   C  CB   . ALA   A 23  ? 0.9746 1.0567 1.0604 0.0758  -0.0806 0.0161  23  ALA   A CB   
97   N  N    . TYR   A 24  ? 0.9835 1.0355 1.0535 0.0602  -0.0832 0.0222  24  TYR   A N    
98   C  CA   . TYR   A 24  ? 0.9694 1.0352 1.0554 0.0556  -0.0770 0.0270  24  TYR   A CA   
99   C  C    . TYR   A 24  ? 0.9640 1.0226 1.0384 0.0555  -0.0685 0.0300  24  TYR   A C    
100  O  O    . TYR   A 24  ? 0.9785 1.0188 1.0360 0.0547  -0.0705 0.0296  24  TYR   A O    
101  C  CB   . TYR   A 24  ? 0.9661 1.0337 1.0669 0.0467  -0.0845 0.0288  24  TYR   A CB   
102  N  N    . GLY   A 25  ? 0.9372 1.0100 1.0202 0.0568  -0.0590 0.0331  25  GLY   A N    
103  C  CA   . GLY   A 25  ? 0.9252 0.9938 0.9984 0.0576  -0.0503 0.0364  25  GLY   A CA   
104  C  C    . GLY   A 25  ? 0.8948 0.9752 0.9675 0.0648  -0.0415 0.0363  25  GLY   A C    
105  O  O    . GLY   A 25  ? 0.8953 0.9822 0.9691 0.0700  -0.0427 0.0327  25  GLY   A O    
106  N  N    . LYS   A 26  ? 0.8644 0.9464 0.9341 0.0650  -0.0329 0.0402  26  LYS   A N    
107  C  CA   . LYS   A 26  ? 0.8352 0.9268 0.9022 0.0716  -0.0245 0.0404  26  LYS   A CA   
108  C  C    . LYS   A 26  ? 0.7996 0.8805 0.8466 0.0772  -0.0230 0.0388  26  LYS   A C    
109  O  O    . LYS   A 26  ? 0.8057 0.8722 0.8413 0.0762  -0.0272 0.0380  26  LYS   A O    
110  C  CB   . LYS   A 26  ? 0.8659 0.9663 0.9417 0.0692  -0.0156 0.0459  26  LYS   A CB   
111  C  CG   . LYS   A 26  ? 0.9154 1.0331 1.0131 0.0668  -0.0141 0.0472  26  LYS   A CG   
112  C  CD   . LYS   A 26  ? 0.9797 1.1052 1.0845 0.0648  -0.0037 0.0529  26  LYS   A CD   
113  C  CE   . LYS   A 26  ? 1.0338 1.1773 1.1629 0.0615  -0.0017 0.0549  26  LYS   A CE   
114  N  NZ   . LYS   A 26  ? 1.0673 1.2242 1.2013 0.0694  0.0018  0.0525  26  LYS   A NZ   
115  N  N    . VAL   A 27  ? 0.7617 0.8500 0.8045 0.0833  -0.0171 0.0381  27  VAL   A N    
116  C  CA   . VAL   A 27  ? 0.7356 0.8176 0.7619 0.0889  -0.0151 0.0367  27  VAL   A CA   
117  C  C    . VAL   A 27  ? 0.7009 0.7875 0.7245 0.0910  -0.0065 0.0407  27  VAL   A C    
118  O  O    . VAL   A 27  ? 0.6948 0.7929 0.7267 0.0922  -0.0018 0.0414  27  VAL   A O    
119  C  CB   . VAL   A 27  ? 0.7371 0.8221 0.7588 0.0943  -0.0174 0.0312  27  VAL   A CB   
120  C  CG1  . VAL   A 27  ? 0.7504 0.8289 0.7567 0.0989  -0.0165 0.0298  27  VAL   A CG1  
121  C  CG2  . VAL   A 27  ? 0.7430 0.8239 0.7682 0.0922  -0.0251 0.0276  27  VAL   A CG2  
122  N  N    . PHE   A 28  ? 0.6802 0.7570 0.6914 0.0919  -0.0044 0.0433  28  PHE   A N    
123  C  CA   . PHE   A 28  ? 0.6658 0.7443 0.6713 0.0945  0.0034  0.0472  28  PHE   A CA   
124  C  C    . PHE   A 28  ? 0.6447 0.7189 0.6339 0.1014  0.0040  0.0458  28  PHE   A C    
125  O  O    . PHE   A 28  ? 0.6487 0.7154 0.6304 0.1030  -0.0010 0.0434  28  PHE   A O    
126  C  CB   . PHE   A 28  ? 0.6723 0.7423 0.6773 0.0891  0.0063  0.0530  28  PHE   A CB   
127  C  CG   . PHE   A 28  ? 0.6827 0.7591 0.7053 0.0816  0.0074  0.0557  28  PHE   A CG   
128  C  CD1  . PHE   A 28  ? 0.6904 0.7777 0.7220 0.0811  0.0154  0.0590  28  PHE   A CD1  
129  C  CD2  . PHE   A 28  ? 0.6974 0.7688 0.7276 0.0749  0.0006  0.0550  28  PHE   A CD2  
130  C  CE1  . PHE   A 28  ? 0.6954 0.7909 0.7459 0.0740  0.0168  0.0617  28  PHE   A CE1  
131  C  CE2  . PHE   A 28  ? 0.7013 0.7800 0.7496 0.0675  0.0008  0.0575  28  PHE   A CE2  
132  C  CZ   . PHE   A 28  ? 0.6933 0.7850 0.7527 0.0669  0.0091  0.0609  28  PHE   A CZ   
133  N  N    . LYS   A 29  ? 0.6191 0.6979 0.6028 0.1058  0.0100  0.0474  29  LYS   A N    
134  C  CA   . LYS   A 29  ? 0.6007 0.6760 0.5690 0.1124  0.0107  0.0469  29  LYS   A CA   
135  C  C    . LYS   A 29  ? 0.6028 0.6667 0.5628 0.1112  0.0138  0.0525  29  LYS   A C    
136  O  O    . LYS   A 29  ? 0.6108 0.6745 0.5749 0.1077  0.0196  0.0571  29  LYS   A O    
137  C  CB   . LYS   A 29  ? 0.5921 0.6757 0.5572 0.1172  0.0154  0.0462  29  LYS   A CB   
138  C  CG   . LYS   A 29  ? 0.6152 0.6969 0.5655 0.1240  0.0139  0.0443  29  LYS   A CG   
139  C  CD   . LYS   A 29  ? 0.6540 0.7407 0.5984 0.1284  0.0190  0.0446  29  LYS   A CD   
140  C  CE   . LYS   A 29  ? 0.6749 0.7603 0.6050 0.1349  0.0163  0.0424  29  LYS   A CE   
141  N  NZ   . LYS   A 29  ? 0.6808 0.7713 0.6053 0.1388  0.0192  0.0406  29  LYS   A NZ   
142  N  N    . ALA   A 30  ? 0.5948 0.6487 0.5445 0.1135  0.0101  0.0523  30  ALA   A N    
143  C  CA   . ALA   A 30  ? 0.6010 0.6417 0.5407 0.1130  0.0127  0.0576  30  ALA   A CA   
144  C  C    . ALA   A 30  ? 0.6080 0.6439 0.5313 0.1212  0.0130  0.0582  30  ALA   A C    
145  O  O    . ALA   A 30  ? 0.6043 0.6463 0.5249 0.1265  0.0094  0.0540  30  ALA   A O    
146  C  CB   . ALA   A 30  ? 0.6053 0.6350 0.5463 0.1082  0.0081  0.0577  30  ALA   A CB   
147  N  N    . ARG   A 31  ? 0.6115 0.6362 0.5241 0.1219  0.0173  0.0636  31  ARG   A N    
148  C  CA   . ARG   A 31  ? 0.6231 0.6399 0.5185 0.1297  0.0175  0.0655  31  ARG   A CA   
149  C  C    . ARG   A 31  ? 0.6223 0.6265 0.5121 0.1300  0.0132  0.0656  31  ARG   A C    
150  O  O    . ARG   A 31  ? 0.6181 0.6115 0.5093 0.1237  0.0141  0.0685  31  ARG   A O    
151  C  CB   . ARG   A 31  ? 0.6415 0.6501 0.5277 0.1294  0.0251  0.0719  31  ARG   A CB   
152  C  CG   . ARG   A 31  ? 0.6774 0.6868 0.5494 0.1380  0.0276  0.0729  31  ARG   A CG   
153  C  CD   . ARG   A 31  ? 0.7109 0.7352 0.5882 0.1400  0.0283  0.0694  31  ARG   A CD   
154  N  NE   . ARG   A 31  ? 0.7432 0.7708 0.6104 0.1486  0.0234  0.0661  31  ARG   A NE   
155  C  CZ   . ARG   A 31  ? 0.7639 0.7914 0.6182 0.1551  0.0251  0.0670  31  ARG   A CZ   
156  N  NH1  . ARG   A 31  ? 0.7560 0.7808 0.6057 0.1543  0.0327  0.0707  31  ARG   A NH1  
157  N  NH2  . ARG   A 31  ? 0.7762 0.8071 0.6227 0.1625  0.0191  0.0638  31  ARG   A NH2  
158  N  N    . ASP   A 32  ? 0.6243 0.6302 0.5088 0.1368  0.0085  0.0624  32  ASP   A N    
159  C  CA   . ASP   A 32  ? 0.6449 0.6390 0.5226 0.1390  0.0050  0.0624  32  ASP   A CA   
160  C  C    . ASP   A 32  ? 0.6709 0.6518 0.5309 0.1455  0.0075  0.0674  32  ASP   A C    
161  O  O    . ASP   A 32  ? 0.6727 0.6561 0.5244 0.1545  0.0055  0.0666  32  ASP   A O    
162  C  CB   . ASP   A 32  ? 0.6464 0.6499 0.5282 0.1435  -0.0003 0.0568  32  ASP   A CB   
163  C  CG   . ASP   A 32  ? 0.6820 0.6749 0.5571 0.1471  -0.0032 0.0564  32  ASP   A CG   
164  O  OD1  . ASP   A 32  ? 0.6948 0.6708 0.5604 0.1463  -0.0018 0.0604  32  ASP   A OD1  
165  O  OD2  . ASP   A 32  ? 0.6884 0.6892 0.5676 0.1504  -0.0066 0.0521  32  ASP   A OD2  
166  N  N    . LEU   A 33  ? 0.6940 0.6609 0.5485 0.1408  0.0117  0.0725  33  LEU   A N    
167  C  CA   . LEU   A 33  ? 0.7288 0.6796 0.5652 0.1453  0.0153  0.0782  33  LEU   A CA   
168  C  C    . LEU   A 33  ? 0.7448 0.6865 0.5676 0.1550  0.0119  0.0781  33  LEU   A C    
169  O  O    . LEU   A 33  ? 0.7519 0.6884 0.5605 0.1630  0.0133  0.0811  33  LEU   A O    
170  C  CB   . LEU   A 33  ? 0.7426 0.6779 0.5776 0.1362  0.0197  0.0831  33  LEU   A CB   
171  C  CG   . LEU   A 33  ? 0.7679 0.7060 0.6071 0.1302  0.0268  0.0870  33  LEU   A CG   
172  C  CD1  . LEU   A 33  ? 0.7625 0.7221 0.6171 0.1287  0.0270  0.0832  33  LEU   A CD1  
173  C  CD2  . LEU   A 33  ? 0.7792 0.7067 0.6244 0.1185  0.0292  0.0901  33  LEU   A CD2  
174  N  N    . LYS   A 34  ? 0.7468 0.6865 0.5734 0.1548  0.0075  0.0749  34  LYS   A N    
175  C  CA   . LYS   A 34  ? 0.7643 0.6956 0.5792 0.1642  0.0048  0.0749  34  LYS   A CA   
176  C  C    . LYS   A 34  ? 0.7518 0.7006 0.5708 0.1730  0.0011  0.0708  34  LYS   A C    
177  O  O    . LYS   A 34  ? 0.7584 0.7031 0.5678 0.1827  -0.0005 0.0714  34  LYS   A O    
178  C  CB   . LYS   A 34  ? 0.8112 0.7295 0.6258 0.1606  0.0027  0.0737  34  LYS   A CB   
179  C  CG   . LYS   A 34  ? 0.8971 0.7897 0.6959 0.1590  0.0052  0.0789  34  LYS   A CG   
180  C  CD   . LYS   A 34  ? 0.9847 0.8628 0.7770 0.1606  0.0023  0.0774  34  LYS   A CD   
181  C  CE   . LYS   A 34  ? 1.0678 0.9184 0.8451 0.1566  0.0042  0.0818  34  LYS   A CE   
182  N  NZ   . LYS   A 34  ? 1.1010 0.9480 0.8879 0.1423  0.0042  0.0821  34  LYS   A NZ   
183  N  N    . ASN   A 35  ? 0.7320 0.7001 0.5653 0.1699  -0.0003 0.0666  35  ASN   A N    
184  C  CA   . ASN   A 35  ? 0.7165 0.7013 0.5546 0.1770  -0.0041 0.0624  35  ASN   A CA   
185  C  C    . ASN   A 35  ? 0.6938 0.6910 0.5321 0.1793  -0.0039 0.0620  35  ASN   A C    
186  O  O    . ASN   A 35  ? 0.6947 0.7087 0.5439 0.1781  -0.0064 0.0574  35  ASN   A O    
187  C  CB   . ASN   A 35  ? 0.7314 0.7262 0.5838 0.1730  -0.0071 0.0570  35  ASN   A CB   
188  C  CG   . ASN   A 35  ? 0.7827 0.7638 0.6311 0.1734  -0.0076 0.0573  35  ASN   A CG   
189  O  OD1  . ASN   A 35  ? 0.7940 0.7607 0.6399 0.1668  -0.0062 0.0592  35  ASN   A OD1  
190  N  ND2  . ASN   A 35  ? 0.8049 0.7894 0.6514 0.1816  -0.0096 0.0558  35  ASN   A ND2  
191  N  N    . GLY   A 36  ? 0.6654 0.6525 0.4894 0.1834  -0.0011 0.0670  36  GLY   A N    
192  C  CA   . GLY   A 36  ? 0.6492 0.6434 0.4678 0.1873  -0.0007 0.0675  36  GLY   A CA   
193  C  C    . GLY   A 36  ? 0.6231 0.6239 0.4491 0.1797  0.0028  0.0668  36  GLY   A C    
194  O  O    . GLY   A 36  ? 0.6157 0.6263 0.4406 0.1825  0.0019  0.0650  36  GLY   A O    
195  N  N    . GLY   A 37  ? 0.6088 0.6035 0.4415 0.1706  0.0066  0.0682  37  GLY   A N    
196  C  CA   . GLY   A 37  ? 0.5920 0.5931 0.4340 0.1630  0.0106  0.0679  37  GLY   A CA   
197  C  C    . GLY   A 37  ? 0.5664 0.5856 0.4222 0.1613  0.0071  0.0617  37  GLY   A C    
198  O  O    . GLY   A 37  ? 0.5736 0.5999 0.4330 0.1590  0.0100  0.0611  37  GLY   A O    
199  N  N    . ARG   A 38  ? 0.5389 0.5649 0.4017 0.1627  0.0016  0.0571  38  ARG   A N    
200  C  CA   . ARG   A 38  ? 0.5233 0.5647 0.3986 0.1604  -0.0017 0.0511  38  ARG   A CA   
201  C  C    . ARG   A 38  ? 0.5208 0.5634 0.4082 0.1514  0.0008  0.0505  38  ARG   A C    
202  O  O    . ARG   A 38  ? 0.5291 0.5617 0.4177 0.1467  0.0029  0.0535  38  ARG   A O    
203  C  CB   . ARG   A 38  ? 0.5230 0.5699 0.4032 0.1632  -0.0071 0.0470  38  ARG   A CB   
204  C  CG   . ARG   A 38  ? 0.5472 0.5846 0.4307 0.1596  -0.0073 0.0475  38  ARG   A CG   
205  C  CD   . ARG   A 38  ? 0.5794 0.6229 0.4683 0.1620  -0.0113 0.0434  38  ARG   A CD   
206  N  NE   . ARG   A 38  ? 0.6238 0.6546 0.5112 0.1602  -0.0112 0.0446  38  ARG   A NE   
207  C  CZ   . ARG   A 38  ? 0.6580 0.6881 0.5453 0.1640  -0.0132 0.0429  38  ARG   A CZ   
208  N  NH1  . ARG   A 38  ? 0.6453 0.6886 0.5364 0.1692  -0.0155 0.0398  38  ARG   A NH1  
209  N  NH2  . ARG   A 38  ? 0.6663 0.6821 0.5497 0.1625  -0.0127 0.0441  38  ARG   A NH2  
210  N  N    . PHE   A 39  ? 0.5090 0.5632 0.4047 0.1491  0.0005  0.0467  39  PHE   A N    
211  C  CA   . PHE   A 39  ? 0.5084 0.5651 0.4163 0.1416  0.0023  0.0458  39  PHE   A CA   
212  C  C    . PHE   A 39  ? 0.5212 0.5784 0.4375 0.1386  -0.0022 0.0422  39  PHE   A C    
213  O  O    . PHE   A 39  ? 0.5239 0.5855 0.4397 0.1421  -0.0062 0.0386  39  PHE   A O    
214  C  CB   . PHE   A 39  ? 0.4921 0.5600 0.4050 0.1411  0.0036  0.0428  39  PHE   A CB   
215  C  CG   . PHE   A 39  ? 0.4892 0.5565 0.3940 0.1437  0.0089  0.0460  39  PHE   A CG   
216  C  CD1  . PHE   A 39  ? 0.4987 0.5588 0.4022 0.1408  0.0152  0.0517  39  PHE   A CD1  
217  C  CD2  . PHE   A 39  ? 0.4949 0.5688 0.3938 0.1483  0.0081  0.0431  39  PHE   A CD2  
218  C  CE1  . PHE   A 39  ? 0.5098 0.5688 0.4051 0.1433  0.0212  0.0549  39  PHE   A CE1  
219  C  CE2  . PHE   A 39  ? 0.5074 0.5794 0.3970 0.1511  0.0133  0.0460  39  PHE   A CE2  
220  C  CZ   . PHE   A 39  ? 0.5085 0.5728 0.3960 0.1489  0.0203  0.0520  39  PHE   A CZ   
221  N  N    . VAL   A 40  ? 0.5213 0.5739 0.4452 0.1321  -0.0016 0.0433  40  VAL   A N    
222  C  CA   . VAL   A 40  ? 0.5207 0.5716 0.4517 0.1284  -0.0056 0.0402  40  VAL   A CA   
223  C  C    . VAL   A 40  ? 0.5245 0.5801 0.4680 0.1219  -0.0050 0.0393  40  VAL   A C    
224  O  O    . VAL   A 40  ? 0.5288 0.5875 0.4752 0.1201  -0.0008 0.0420  40  VAL   A O    
225  C  CB   . VAL   A 40  ? 0.5216 0.5579 0.4462 0.1280  -0.0070 0.0427  40  VAL   A CB   
226  C  CG1  . VAL   A 40  ? 0.5259 0.5592 0.4396 0.1357  -0.0080 0.0429  40  VAL   A CG1  
227  C  CG2  . VAL   A 40  ? 0.5247 0.5511 0.4476 0.1235  -0.0037 0.0480  40  VAL   A CG2  
228  N  N    . ALA   A 41  ? 0.5176 0.5740 0.4679 0.1190  -0.0091 0.0355  41  ALA   A N    
229  C  CA   . ALA   A 41  ? 0.5172 0.5774 0.4794 0.1134  -0.0098 0.0345  41  ALA   A CA   
230  C  C    . ALA   A 41  ? 0.5495 0.5980 0.5122 0.1089  -0.0130 0.0358  41  ALA   A C    
231  O  O    . ALA   A 41  ? 0.5517 0.5932 0.5089 0.1103  -0.0165 0.0337  41  ALA   A O    
232  C  CB   . ALA   A 41  ? 0.5013 0.5692 0.4682 0.1143  -0.0126 0.0291  41  ALA   A CB   
233  N  N    . LEU   A 42  ? 0.5769 0.6224 0.5450 0.1036  -0.0114 0.0397  42  LEU   A N    
234  C  CA   . LEU   A 42  ? 0.6142 0.6477 0.5830 0.0978  -0.0147 0.0415  42  LEU   A CA   
235  C  C    . LEU   A 42  ? 0.6336 0.6721 0.6156 0.0927  -0.0190 0.0390  42  LEU   A C    
236  O  O    . LEU   A 42  ? 0.6248 0.6750 0.6185 0.0908  -0.0168 0.0395  42  LEU   A O    
237  C  CB   . LEU   A 42  ? 0.6321 0.6612 0.6007 0.0942  -0.0101 0.0473  42  LEU   A CB   
238  C  CG   . LEU   A 42  ? 0.6775 0.6909 0.6314 0.0957  -0.0087 0.0509  42  LEU   A CG   
239  C  CD1  . LEU   A 42  ? 0.6962 0.6947 0.6489 0.0893  -0.0128 0.0521  42  LEU   A CD1  
240  C  CD2  . LEU   A 42  ? 0.6930 0.7040 0.6341 0.1042  -0.0090 0.0491  42  LEU   A CD2  
241  N  N    . LYS   A 43  ? 0.6602 0.6894 0.6395 0.0911  -0.0251 0.0363  43  LYS   A N    
242  C  CA   . LYS   A 43  ? 0.6857 0.7174 0.6754 0.0868  -0.0305 0.0338  43  LYS   A CA   
243  C  C    . LYS   A 43  ? 0.7465 0.7645 0.7352 0.0805  -0.0354 0.0354  43  LYS   A C    
244  O  O    . LYS   A 43  ? 0.7515 0.7540 0.7270 0.0816  -0.0378 0.0349  43  LYS   A O    
245  C  CB   . LYS   A 43  ? 0.6849 0.7177 0.6717 0.0906  -0.0338 0.0285  43  LYS   A CB   
246  C  CG   . LYS   A 43  ? 0.7073 0.7404 0.7026 0.0870  -0.0402 0.0259  43  LYS   A CG   
247  C  CD   . LYS   A 43  ? 0.7318 0.7667 0.7244 0.0909  -0.0422 0.0210  43  LYS   A CD   
248  C  CE   . LYS   A 43  ? 0.7544 0.8033 0.7595 0.0910  -0.0419 0.0197  43  LYS   A CE   
249  N  NZ   . LYS   A 43  ? 0.7744 0.8245 0.7751 0.0951  -0.0427 0.0151  43  LYS   A NZ   
250  N  N    . ARG   A 44  ? 0.7897 0.8132 0.7923 0.0740  -0.0369 0.0373  44  ARG   A N    
251  C  CA   . ARG   A 44  ? 0.8454 0.8572 0.8493 0.0666  -0.0425 0.0387  44  ARG   A CA   
252  C  C    . ARG   A 44  ? 0.8847 0.8955 0.8939 0.0644  -0.0512 0.0347  44  ARG   A C    
253  O  O    . ARG   A 44  ? 0.8835 0.9088 0.9073 0.0638  -0.0524 0.0335  44  ARG   A O    
254  C  CB   . ARG   A 44  ? 0.8771 0.8943 0.8925 0.0599  -0.0388 0.0438  44  ARG   A CB   
255  C  CG   . ARG   A 44  ? 0.9520 0.9606 0.9554 0.0612  -0.0320 0.0480  44  ARG   A CG   
256  C  CD   . ARG   A 44  ? 1.0105 1.0265 1.0245 0.0560  -0.0255 0.0533  44  ARG   A CD   
257  N  NE   . ARG   A 44  ? 1.0669 1.0736 1.0667 0.0589  -0.0188 0.0572  44  ARG   A NE   
258  C  CZ   . ARG   A 44  ? 1.1031 1.1116 1.1062 0.0554  -0.0116 0.0625  44  ARG   A CZ   
259  N  NH1  . ARG   A 44  ? 1.0934 1.1144 1.1156 0.0485  -0.0098 0.0647  44  ARG   A NH1  
260  N  NH2  . ARG   A 44  ? 1.1133 1.1112 1.1007 0.0591  -0.0061 0.0658  44  ARG   A NH2  
261  N  N    . VAL   A 45  ? 0.9198 0.9125 0.9152 0.0645  -0.0571 0.0325  45  VAL   A N    
262  C  CA   . VAL   A 45  ? 0.9533 0.9404 0.9486 0.0633  -0.0659 0.0285  45  VAL   A CA   
263  C  C    . VAL   A 45  ? 0.9889 0.9649 0.9866 0.0550  -0.0736 0.0296  45  VAL   A C    
264  O  O    . VAL   A 45  ? 1.0014 0.9600 0.9863 0.0527  -0.0742 0.0312  45  VAL   A O    
265  C  CB   . VAL   A 45  ? 0.9643 0.9381 0.9414 0.0696  -0.0668 0.0251  45  VAL   A CB   
266  N  N    . ARG   A 46  ? 1.0032 0.9893 1.0173 0.0505  -0.0796 0.0287  46  ARG   A N    
267  C  CA   . ARG   A 46  ? 1.0287 1.0086 1.0497 0.0415  -0.0883 0.0295  46  ARG   A CA   
268  C  C    . ARG   A 46  ? 1.0611 1.0175 1.0648 0.0406  -0.0980 0.0262  46  ARG   A C    
269  O  O    . ARG   A 46  ? 1.0732 1.0190 1.0602 0.0475  -0.0977 0.0232  46  ARG   A O    
270  C  CB   . ARG   A 46  ? 1.0178 1.0185 1.0629 0.0385  -0.0918 0.0292  46  ARG   A CB   
271  N  N    . VAL   A 47  ? 1.0720 1.0199 1.0796 0.0319  -0.1065 0.0268  47  VAL   A N    
272  C  CA   . VAL   A 47  ? 1.0989 1.0230 1.0901 0.0297  -0.1170 0.0238  47  VAL   A CA   
273  C  C    . VAL   A 47  ? 1.0997 1.0299 1.1032 0.0264  -0.1287 0.0209  47  VAL   A C    
274  O  O    . VAL   A 47  ? 1.1129 1.0259 1.1019 0.0276  -0.1376 0.0173  47  VAL   A O    
275  C  CB   . VAL   A 47  ? 1.1109 1.0175 1.0943 0.0219  -0.1188 0.0266  47  VAL   A CB   
276  N  N    . PRO   A 55  ? 1.1021 0.9272 0.9991 0.0426  -0.1402 0.0102  55  PRO   A N    
277  C  CA   . PRO   A 55  ? 1.1083 0.9299 0.9947 0.0507  -0.1403 0.0066  55  PRO   A CA   
278  C  C    . PRO   A 55  ? 1.1217 0.9219 0.9812 0.0583  -0.1337 0.0057  55  PRO   A C    
279  O  O    . PRO   A 55  ? 1.1346 0.9211 0.9827 0.0576  -0.1303 0.0078  55  PRO   A O    
280  C  CB   . PRO   A 55  ? 1.0932 0.9428 0.9988 0.0546  -0.1339 0.0067  55  PRO   A CB   
281  N  N    . LEU   A 56  ? 1.1131 0.9095 0.9621 0.0657  -0.1319 0.0028  56  LEU   A N    
282  C  CA   . LEU   A 56  ? 1.1138 0.8926 0.9394 0.0736  -0.1249 0.0018  56  LEU   A CA   
283  C  C    . LEU   A 56  ? 1.0856 0.8792 0.9152 0.0808  -0.1164 0.0006  56  LEU   A C    
284  O  O    . LEU   A 56  ? 1.0858 0.8763 0.9057 0.0869  -0.1070 0.0012  56  LEU   A O    
285  C  CB   . LEU   A 56  ? 1.1349 0.8836 0.9360 0.0743  -0.1334 -0.0012 56  LEU   A CB   
286  N  N    . SER   A 57  ? 1.0552 0.8649 0.8995 0.0800  -0.1199 -0.0009 57  SER   A N    
287  C  CA   . SER   A 57  ? 1.0312 0.8553 0.8808 0.0854  -0.1131 -0.0022 57  SER   A CA   
288  C  C    . SER   A 57  ? 0.9968 0.8443 0.8630 0.0861  -0.1033 0.0005  57  SER   A C    
289  O  O    . SER   A 57  ? 0.9910 0.8455 0.8558 0.0913  -0.0947 0.0001  57  SER   A O    
290  C  CB   . SER   A 57  ? 1.0377 0.8709 0.8981 0.0840  -0.1207 -0.0044 57  SER   A CB   
291  O  OG   . SER   A 57  ? 1.0468 0.8966 0.9287 0.0778  -0.1259 -0.0027 57  SER   A OG   
292  N  N    . THR   A 58  ? 0.9701 0.8291 0.8516 0.0806  -0.1048 0.0033  58  THR   A N    
293  C  CA   . THR   A 58  ? 0.9471 0.8259 0.8427 0.0808  -0.0964 0.0063  58  THR   A CA   
294  C  C    . THR   A 58  ? 0.9320 0.7998 0.8137 0.0842  -0.0894 0.0081  58  THR   A C    
295  O  O    . THR   A 58  ? 0.9262 0.8062 0.8115 0.0885  -0.0809 0.0092  58  THR   A O    
296  C  CB   . THR   A 58  ? 0.9543 0.8481 0.8705 0.0737  -0.1002 0.0086  58  THR   A CB   
297  O  OG1  . THR   A 58  ? 0.9609 0.8669 0.8901 0.0729  -0.1053 0.0066  58  THR   A OG1  
298  C  CG2  . THR   A 58  ? 0.9488 0.8604 0.8774 0.0737  -0.0914 0.0121  58  THR   A CG2  
299  N  N    . ILE   A 59  ? 0.9223 0.7661 0.7868 0.0831  -0.0934 0.0083  59  ILE   A N    
300  C  CA   . ILE   A 59  ? 0.9126 0.7421 0.7610 0.0873  -0.0874 0.0100  59  ILE   A CA   
301  C  C    . ILE   A 59  ? 0.8714 0.7024 0.7118 0.0956  -0.0798 0.0083  59  ILE   A C    
302  O  O    . ILE   A 59  ? 0.8643 0.7016 0.7044 0.1003  -0.0716 0.0101  59  ILE   A O    
303  C  CB   . ILE   A 59  ? 0.9479 0.7481 0.7765 0.0849  -0.0941 0.0097  59  ILE   A CB   
304  C  CG1  . ILE   A 59  ? 0.9658 0.7649 0.8036 0.0754  -0.1016 0.0116  59  ILE   A CG1  
305  C  CG2  . ILE   A 59  ? 0.9664 0.7490 0.7750 0.0914  -0.0874 0.0109  59  ILE   A CG2  
306  C  CD1  . ILE   A 59  ? 0.9795 0.7882 0.8268 0.0727  -0.0959 0.0161  59  ILE   A CD1  
307  N  N    . ARG   A 60  ? 0.8399 0.6658 0.6748 0.0972  -0.0827 0.0049  60  ARG   A N    
308  C  CA   . ARG   A 60  ? 0.8161 0.6429 0.6444 0.1036  -0.0761 0.0030  60  ARG   A CA   
309  C  C    . ARG   A 60  ? 0.7578 0.6111 0.6038 0.1050  -0.0697 0.0032  60  ARG   A C    
310  O  O    . ARG   A 60  ? 0.7479 0.6061 0.5916 0.1101  -0.0618 0.0032  60  ARG   A O    
311  C  CB   . ARG   A 60  ? 0.8628 0.6752 0.6799 0.1038  -0.0818 -0.0005 60  ARG   A CB   
312  C  CG   . ARG   A 60  ? 0.9784 0.7613 0.7695 0.1073  -0.0826 -0.0015 60  ARG   A CG   
313  C  CD   . ARG   A 60  ? 1.0712 0.8342 0.8514 0.1036  -0.0899 -0.0005 60  ARG   A CD   
314  N  NE   . ARG   A 60  ? 1.1421 0.9050 0.9215 0.1048  -0.0844 0.0027  60  ARG   A NE   
315  C  CZ   . ARG   A 60  ? 1.2145 0.9564 0.9738 0.1094  -0.0809 0.0034  60  ARG   A CZ   
316  N  NH1  . ARG   A 60  ? 1.2263 0.9449 0.9638 0.1132  -0.0819 0.0012  60  ARG   A NH1  
317  N  NH2  . ARG   A 60  ? 1.2285 0.9715 0.9881 0.1109  -0.0762 0.0065  60  ARG   A NH2  
318  N  N    . GLU   A 61  ? 0.7134 0.5836 0.5770 0.1006  -0.0734 0.0032  61  GLU   A N    
319  C  CA   . GLU   A 61  ? 0.6788 0.5729 0.5586 0.1014  -0.0684 0.0032  61  GLU   A CA   
320  C  C    . GLU   A 61  ? 0.6529 0.5574 0.5371 0.1036  -0.0612 0.0060  61  GLU   A C    
321  O  O    . GLU   A 61  ? 0.6510 0.5676 0.5390 0.1073  -0.0550 0.0054  61  GLU   A O    
322  C  CB   . GLU   A 61  ? 0.7019 0.6096 0.5983 0.0966  -0.0737 0.0032  61  GLU   A CB   
323  C  CG   . GLU   A 61  ? 0.7793 0.6836 0.6742 0.0967  -0.0789 -0.0002 61  GLU   A CG   
324  C  CD   . GLU   A 61  ? 0.8767 0.7968 0.7887 0.0939  -0.0830 -0.0006 61  GLU   A CD   
325  O  OE1  . GLU   A 61  ? 0.8992 0.8282 0.8240 0.0897  -0.0855 0.0018  61  GLU   A OE1  
326  O  OE2  . GLU   A 61  ? 0.9131 0.8356 0.8251 0.0961  -0.0835 -0.0032 61  GLU   A OE2  
327  N  N    . VAL   A 62  ? 0.6372 0.5357 0.5198 0.1015  -0.0624 0.0091  62  VAL   A N    
328  C  CA   . VAL   A 62  ? 0.6316 0.5364 0.5156 0.1040  -0.0564 0.0122  62  VAL   A CA   
329  C  C    . VAL   A 62  ? 0.6209 0.5161 0.4908 0.1109  -0.0509 0.0120  62  VAL   A C    
330  O  O    . VAL   A 62  ? 0.6237 0.5305 0.4972 0.1151  -0.0449 0.0132  62  VAL   A O    
331  C  CB   . VAL   A 62  ? 0.6504 0.5488 0.5353 0.0992  -0.0595 0.0156  62  VAL   A CB   
332  C  CG1  . VAL   A 62  ? 0.6561 0.5573 0.5389 0.1026  -0.0533 0.0191  62  VAL   A CG1  
333  C  CG2  . VAL   A 62  ? 0.6483 0.5603 0.5504 0.0927  -0.0634 0.0161  62  VAL   A CG2  
334  N  N    . ALA   A 63  ? 0.6050 0.4794 0.4588 0.1124  -0.0530 0.0105  63  ALA   A N    
335  C  CA   . ALA   A 63  ? 0.5964 0.4604 0.4363 0.1194  -0.0473 0.0104  63  ALA   A CA   
336  C  C    . ALA   A 63  ? 0.5814 0.4603 0.4277 0.1230  -0.0415 0.0083  63  ALA   A C    
337  O  O    . ALA   A 63  ? 0.5993 0.4838 0.4446 0.1287  -0.0348 0.0091  63  ALA   A O    
338  C  CB   . ALA   A 63  ? 0.6033 0.4405 0.4239 0.1197  -0.0511 0.0089  63  ALA   A CB   
339  N  N    . VAL   A 64  ? 0.5482 0.4342 0.4017 0.1197  -0.0443 0.0056  64  VAL   A N    
340  C  CA   . VAL   A 64  ? 0.5361 0.4354 0.3959 0.1215  -0.0396 0.0034  64  VAL   A CA   
341  C  C    . VAL   A 64  ? 0.5357 0.4582 0.4107 0.1222  -0.0358 0.0047  64  VAL   A C    
342  O  O    . VAL   A 64  ? 0.5353 0.4670 0.4125 0.1260  -0.0300 0.0043  64  VAL   A O    
343  C  CB   . VAL   A 64  ? 0.5243 0.4228 0.3864 0.1177  -0.0444 0.0004  64  VAL   A CB   
344  C  CG1  . VAL   A 64  ? 0.5137 0.4273 0.3839 0.1186  -0.0397 -0.0017 64  VAL   A CG1  
345  C  CG2  . VAL   A 64  ? 0.5284 0.4025 0.3728 0.1182  -0.0479 -0.0011 64  VAL   A CG2  
346  N  N    . LEU   A 65  ? 0.5337 0.4652 0.4186 0.1186  -0.0390 0.0065  65  LEU   A N    
347  C  CA   . LEU   A 65  ? 0.5402 0.4917 0.4374 0.1193  -0.0358 0.0079  65  LEU   A CA   
348  C  C    . LEU   A 65  ? 0.5432 0.4957 0.4362 0.1249  -0.0309 0.0103  65  LEU   A C    
349  O  O    . LEU   A 65  ? 0.5358 0.5029 0.4349 0.1281  -0.0269 0.0098  65  LEU   A O    
350  C  CB   . LEU   A 65  ? 0.5447 0.5022 0.4511 0.1147  -0.0395 0.0099  65  LEU   A CB   
351  C  CG   . LEU   A 65  ? 0.5764 0.5487 0.4959 0.1113  -0.0411 0.0083  65  LEU   A CG   
352  C  CD1  . LEU   A 65  ? 0.5839 0.5686 0.5075 0.1135  -0.0375 0.0055  65  LEU   A CD1  
353  C  CD2  . LEU   A 65  ? 0.5964 0.5607 0.5164 0.1070  -0.0473 0.0070  65  LEU   A CD2  
354  N  N    . ARG   A 66  ? 0.5534 0.4894 0.4352 0.1264  -0.0317 0.0126  66  ARG   A N    
355  C  CA   . ARG   A 66  ? 0.5622 0.4953 0.4373 0.1327  -0.0275 0.0152  66  ARG   A CA   
356  C  C    . ARG   A 66  ? 0.5551 0.4901 0.4268 0.1386  -0.0222 0.0135  66  ARG   A C    
357  O  O    . ARG   A 66  ? 0.5509 0.4968 0.4260 0.1440  -0.0181 0.0147  66  ARG   A O    
358  C  CB   . ARG   A 66  ? 0.6027 0.5137 0.4640 0.1326  -0.0298 0.0175  66  ARG   A CB   
359  C  CG   . ARG   A 66  ? 0.6713 0.5811 0.5368 0.1265  -0.0340 0.0199  66  ARG   A CG   
360  C  CD   . ARG   A 66  ? 0.7598 0.6593 0.6165 0.1293  -0.0325 0.0239  66  ARG   A CD   
361  N  NE   . ARG   A 66  ? 0.8340 0.7496 0.6970 0.1341  -0.0280 0.0259  66  ARG   A NE   
362  C  CZ   . ARG   A 66  ? 0.9032 0.8142 0.7609 0.1366  -0.0263 0.0297  66  ARG   A CZ   
363  N  NH1  . ARG   A 66  ? 0.9196 0.8102 0.7660 0.1341  -0.0285 0.0319  66  ARG   A NH1  
364  N  NH2  . ARG   A 66  ? 0.9075 0.8333 0.7703 0.1415  -0.0229 0.0312  66  ARG   A NH2  
365  N  N    . HIS   A 67  ? 0.5530 0.4784 0.4188 0.1376  -0.0224 0.0108  67  HIS   A N    
366  C  CA   . HIS   A 67  ? 0.5438 0.4703 0.4069 0.1421  -0.0168 0.0091  67  HIS   A CA   
367  C  C    . HIS   A 67  ? 0.5313 0.4813 0.4097 0.1412  -0.0142 0.0073  67  HIS   A C    
368  O  O    . HIS   A 67  ? 0.5213 0.4818 0.4037 0.1459  -0.0090 0.0075  67  HIS   A O    
369  C  CB   . HIS   A 67  ? 0.5493 0.4563 0.3996 0.1408  -0.0178 0.0069  67  HIS   A CB   
370  C  CG   . HIS   A 67  ? 0.5483 0.4567 0.3964 0.1445  -0.0111 0.0052  67  HIS   A CG   
371  N  ND1  . HIS   A 67  ? 0.5702 0.4747 0.4118 0.1516  -0.0047 0.0067  67  HIS   A ND1  
372  C  CD2  . HIS   A 67  ? 0.5403 0.4549 0.3930 0.1418  -0.0093 0.0024  67  HIS   A CD2  
373  C  CE1  . HIS   A 67  ? 0.5632 0.4731 0.4072 0.1527  0.0010  0.0049  67  HIS   A CE1  
374  N  NE2  . HIS   A 67  ? 0.5451 0.4599 0.3948 0.1466  -0.0016 0.0023  67  HIS   A NE2  
375  N  N    . LEU   A 68  ? 0.5265 0.4852 0.4138 0.1354  -0.0179 0.0055  68  LEU   A N    
376  C  CA   . LEU   A 68  ? 0.5237 0.5029 0.4242 0.1339  -0.0162 0.0035  68  LEU   A CA   
377  C  C    . LEU   A 68  ? 0.5065 0.5019 0.4150 0.1373  -0.0146 0.0055  68  LEU   A C    
378  O  O    . LEU   A 68  ? 0.4946 0.5048 0.4109 0.1390  -0.0116 0.0043  68  LEU   A O    
379  C  CB   . LEU   A 68  ? 0.5324 0.5157 0.4391 0.1280  -0.0209 0.0019  68  LEU   A CB   
380  C  CG   . LEU   A 68  ? 0.5584 0.5390 0.4647 0.1246  -0.0214 -0.0016 68  LEU   A CG   
381  C  CD1  . LEU   A 68  ? 0.5802 0.5444 0.4744 0.1263  -0.0191 -0.0026 68  LEU   A CD1  
382  C  CD2  . LEU   A 68  ? 0.5582 0.5364 0.4669 0.1203  -0.0271 -0.0021 68  LEU   A CD2  
383  N  N    . GLU   A 69  ? 0.5035 0.4946 0.4092 0.1383  -0.0168 0.0087  69  GLU   A N    
384  C  CA   . GLU   A 69  ? 0.4913 0.4938 0.4014 0.1421  -0.0158 0.0112  69  GLU   A CA   
385  C  C    . GLU   A 69  ? 0.5027 0.5088 0.4111 0.1494  -0.0115 0.0121  69  GLU   A C    
386  O  O    . GLU   A 69  ? 0.5105 0.5330 0.4268 0.1524  -0.0106 0.0124  69  GLU   A O    
387  C  CB   . GLU   A 69  ? 0.5054 0.4981 0.4101 0.1413  -0.0185 0.0147  69  GLU   A CB   
388  C  CG   . GLU   A 69  ? 0.5336 0.5346 0.4398 0.1456  -0.0175 0.0178  69  GLU   A CG   
389  C  CD   . GLU   A 69  ? 0.5676 0.5896 0.4844 0.1464  -0.0171 0.0168  69  GLU   A CD   
390  O  OE1  . GLU   A 69  ? 0.5570 0.5876 0.4815 0.1416  -0.0184 0.0140  69  GLU   A OE1  
391  O  OE2  . GLU   A 69  ? 0.5727 0.6019 0.4895 0.1522  -0.0158 0.0185  69  GLU   A OE2  
392  N  N    . THR   A 70  ? 0.4992 0.4904 0.3974 0.1527  -0.0089 0.0124  70  THR   A N    
393  C  CA   . THR   A 70  ? 0.4969 0.4907 0.3935 0.1604  -0.0040 0.0135  70  THR   A CA   
394  C  C    . THR   A 70  ? 0.5041 0.5188 0.4140 0.1608  -0.0010 0.0110  70  THR   A C    
395  O  O    . THR   A 70  ? 0.5255 0.5516 0.4403 0.1670  0.0017  0.0122  70  THR   A O    
396  C  CB   . THR   A 70  ? 0.5046 0.4765 0.3862 0.1637  -0.0011 0.0140  70  THR   A CB   
397  O  OG1  . THR   A 70  ? 0.5131 0.4809 0.3939 0.1600  0.0004  0.0109  70  THR   A OG1  
398  C  CG2  . THR   A 70  ? 0.5132 0.4633 0.3813 0.1623  -0.0048 0.0160  70  THR   A CG2  
399  N  N    . PHE   A 71  ? 0.4889 0.5090 0.4050 0.1543  -0.0018 0.0077  71  PHE   A N    
400  C  CA   . PHE   A 71  ? 0.4750 0.5142 0.4039 0.1531  0.0006  0.0052  71  PHE   A CA   
401  C  C    . PHE   A 71  ? 0.4831 0.5411 0.4229 0.1518  -0.0030 0.0048  71  PHE   A C    
402  O  O    . PHE   A 71  ? 0.4766 0.5518 0.4274 0.1514  -0.0019 0.0029  71  PHE   A O    
403  C  CB   . PHE   A 71  ? 0.4683 0.5027 0.3969 0.1467  0.0013  0.0018  71  PHE   A CB   
404  C  CG   . PHE   A 71  ? 0.4775 0.4923 0.3937 0.1477  0.0048  0.0018  71  PHE   A CG   
405  C  CD1  . PHE   A 71  ? 0.4961 0.4901 0.3991 0.1467  0.0015  0.0027  71  PHE   A CD1  
406  C  CD2  . PHE   A 71  ? 0.4816 0.4985 0.3991 0.1497  0.0114  0.0009  71  PHE   A CD2  
407  C  CE1  . PHE   A 71  ? 0.5218 0.4958 0.4111 0.1483  0.0042  0.0026  71  PHE   A CE1  
408  C  CE2  . PHE   A 71  ? 0.5049 0.5018 0.4087 0.1514  0.0153  0.0011  71  PHE   A CE2  
409  C  CZ   . PHE   A 71  ? 0.5179 0.4928 0.4067 0.1509  0.0113  0.0018  71  PHE   A CZ   
410  N  N    . GLU   A 72  ? 0.4945 0.5489 0.4311 0.1508  -0.0073 0.0065  72  GLU   A N    
411  C  CA   . GLU   A 72  ? 0.5015 0.5703 0.4452 0.1499  -0.0106 0.0065  72  GLU   A CA   
412  C  C    . GLU   A 72  ? 0.4819 0.5660 0.4361 0.1454  -0.0109 0.0025  72  GLU   A C    
413  O  O    . GLU   A 72  ? 0.4810 0.5812 0.4433 0.1477  -0.0112 0.0018  72  GLU   A O    
414  C  CB   . GLU   A 72  ? 0.5587 0.6349 0.5027 0.1574  -0.0106 0.0096  72  GLU   A CB   
415  C  CG   . GLU   A 72  ? 0.6716 0.7320 0.6040 0.1613  -0.0108 0.0137  72  GLU   A CG   
416  C  CD   . GLU   A 72  ? 0.7898 0.8546 0.7201 0.1697  -0.0105 0.0169  72  GLU   A CD   
417  O  OE1  . GLU   A 72  ? 0.8426 0.9035 0.7677 0.1707  -0.0126 0.0197  72  GLU   A OE1  
418  O  OE2  . GLU   A 72  ? 0.8025 0.8740 0.7359 0.1756  -0.0080 0.0169  72  GLU   A OE2  
419  N  N    . HIS   A 73  ? 0.4595 0.5372 0.4129 0.1393  -0.0110 -0.0002 73  HIS   A N    
420  C  CA   . HIS   A 73  ? 0.4355 0.5236 0.3965 0.1344  -0.0111 -0.0041 73  HIS   A CA   
421  C  C    . HIS   A 73  ? 0.4377 0.5379 0.4035 0.1332  -0.0148 -0.0048 73  HIS   A C    
422  O  O    . HIS   A 73  ? 0.4355 0.5307 0.3972 0.1334  -0.0171 -0.0029 73  HIS   A O    
423  C  CB   . HIS   A 73  ? 0.4214 0.4974 0.3779 0.1289  -0.0108 -0.0064 73  HIS   A CB   
424  C  CG   . HIS   A 73  ? 0.4077 0.4915 0.3700 0.1243  -0.0096 -0.0103 73  HIS   A CG   
425  N  ND1  . HIS   A 73  ? 0.4060 0.4982 0.3727 0.1207  -0.0125 -0.0127 73  HIS   A ND1  
426  C  CD2  . HIS   A 73  ? 0.4171 0.5009 0.3811 0.1228  -0.0053 -0.0121 73  HIS   A CD2  
427  C  CE1  . HIS   A 73  ? 0.4116 0.5082 0.3822 0.1167  -0.0106 -0.0159 73  HIS   A CE1  
428  N  NE2  . HIS   A 73  ? 0.4249 0.5169 0.3946 0.1175  -0.0060 -0.0156 73  HIS   A NE2  
429  N  N    . PRO   A 74  ? 0.4374 0.5529 0.4114 0.1320  -0.0156 -0.0074 74  PRO   A N    
430  C  CA   . PRO   A 74  ? 0.4343 0.5593 0.4103 0.1316  -0.0195 -0.0080 74  PRO   A CA   
431  C  C    . PRO   A 74  ? 0.4491 0.5673 0.4212 0.1272  -0.0210 -0.0094 74  PRO   A C    
432  O  O    . PRO   A 74  ? 0.4542 0.5751 0.4245 0.1283  -0.0233 -0.0084 74  PRO   A O    
433  C  CB   . PRO   A 74  ? 0.4304 0.5711 0.4155 0.1297  -0.0204 -0.0114 74  PRO   A CB   
434  C  CG   . PRO   A 74  ? 0.4437 0.5820 0.4320 0.1269  -0.0163 -0.0131 74  PRO   A CG   
435  C  CD   . PRO   A 74  ? 0.4242 0.5493 0.4060 0.1308  -0.0130 -0.0097 74  PRO   A CD   
436  N  N    . ASN   A 75  ? 0.4362 0.5449 0.4064 0.1229  -0.0195 -0.0114 75  ASN   A N    
437  C  CA   . ASN   A 75  ? 0.4222 0.5256 0.3897 0.1192  -0.0210 -0.0131 75  ASN   A CA   
438  C  C    . ASN   A 75  ? 0.4166 0.5069 0.3790 0.1193  -0.0212 -0.0107 75  ASN   A C    
439  O  O    . ASN   A 75  ? 0.4144 0.4986 0.3752 0.1164  -0.0220 -0.0122 75  ASN   A O    
440  C  CB   . ASN   A 75  ? 0.4332 0.5363 0.4022 0.1143  -0.0200 -0.0174 75  ASN   A CB   
441  C  CG   . ASN   A 75  ? 0.4642 0.5813 0.4391 0.1128  -0.0211 -0.0201 75  ASN   A CG   
442  O  OD1  . ASN   A 75  ? 0.5001 0.6227 0.4799 0.1112  -0.0192 -0.0216 75  ASN   A OD1  
443  N  ND2  . ASN   A 75  ? 0.4210 0.5446 0.3956 0.1135  -0.0240 -0.0206 75  ASN   A ND2  
444  N  N    . VAL   A 76  ? 0.4056 0.4916 0.3656 0.1228  -0.0209 -0.0069 76  VAL   A N    
445  C  CA   . VAL   A 76  ? 0.4141 0.4886 0.3701 0.1222  -0.0219 -0.0046 76  VAL   A CA   
446  C  C    . VAL   A 76  ? 0.4189 0.4950 0.3738 0.1254  -0.0223 -0.0005 76  VAL   A C    
447  O  O    . VAL   A 76  ? 0.4179 0.4988 0.3724 0.1293  -0.0215 0.0010  76  VAL   A O    
448  C  CB   . VAL   A 76  ? 0.4287 0.4882 0.3793 0.1212  -0.0217 -0.0044 76  VAL   A CB   
449  C  CG1  . VAL   A 76  ? 0.4407 0.4983 0.3905 0.1195  -0.0197 -0.0078 76  VAL   A CG1  
450  C  CG2  . VAL   A 76  ? 0.4365 0.4880 0.3820 0.1245  -0.0210 -0.0010 76  VAL   A CG2  
451  N  N    . VAL   A 77  ? 0.4262 0.4991 0.3811 0.1238  -0.0234 0.0012  77  VAL   A N    
452  C  CA   . VAL   A 77  ? 0.4300 0.5033 0.3835 0.1259  -0.0231 0.0052  77  VAL   A CA   
453  C  C    . VAL   A 77  ? 0.4399 0.5037 0.3878 0.1286  -0.0226 0.0083  77  VAL   A C    
454  O  O    . VAL   A 77  ? 0.4367 0.4898 0.3815 0.1274  -0.0231 0.0079  77  VAL   A O    
455  C  CB   . VAL   A 77  ? 0.4391 0.5110 0.3954 0.1227  -0.0237 0.0062  77  VAL   A CB   
456  C  CG1  . VAL   A 77  ? 0.4483 0.5082 0.4038 0.1199  -0.0253 0.0076  77  VAL   A CG1  
457  C  CG2  . VAL   A 77  ? 0.4433 0.5206 0.3994 0.1245  -0.0222 0.0093  77  VAL   A CG2  
458  N  N    . ARG   A 78  ? 0.4439 0.5106 0.3889 0.1330  -0.0216 0.0112  78  ARG   A N    
459  C  CA   . ARG   A 78  ? 0.4665 0.5235 0.4047 0.1367  -0.0208 0.0143  78  ARG   A CA   
460  C  C    . ARG   A 78  ? 0.4823 0.5262 0.4167 0.1337  -0.0214 0.0174  78  ARG   A C    
461  O  O    . ARG   A 78  ? 0.4833 0.5294 0.4199 0.1314  -0.0214 0.0192  78  ARG   A O    
462  C  CB   . ARG   A 78  ? 0.4927 0.5558 0.4280 0.1428  -0.0200 0.0169  78  ARG   A CB   
463  C  CG   . ARG   A 78  ? 0.5325 0.6084 0.4713 0.1472  -0.0201 0.0148  78  ARG   A CG   
464  C  CD   . ARG   A 78  ? 0.5785 0.6514 0.5168 0.1500  -0.0186 0.0139  78  ARG   A CD   
465  N  NE   . ARG   A 78  ? 0.6110 0.6805 0.5522 0.1450  -0.0182 0.0105  78  ARG   A NE   
466  C  CZ   . ARG   A 78  ? 0.6400 0.7194 0.5883 0.1415  -0.0186 0.0066  78  ARG   A CZ   
467  N  NH1  . ARG   A 78  ? 0.6666 0.7607 0.6204 0.1424  -0.0198 0.0052  78  ARG   A NH1  
468  N  NH2  . ARG   A 78  ? 0.6219 0.6951 0.5704 0.1372  -0.0181 0.0041  78  ARG   A NH2  
469  N  N    . LEU   A 79  ? 0.4859 0.5158 0.4140 0.1339  -0.0218 0.0181  79  LEU   A N    
470  C  CA   . LEU   A 79  ? 0.5063 0.5215 0.4293 0.1309  -0.0231 0.0210  79  LEU   A CA   
471  C  C    . LEU   A 79  ? 0.5526 0.5609 0.4666 0.1364  -0.0212 0.0248  79  LEU   A C    
472  O  O    . LEU   A 79  ? 0.5750 0.5781 0.4830 0.1412  -0.0202 0.0245  79  LEU   A O    
473  C  CB   . LEU   A 79  ? 0.4958 0.4973 0.4145 0.1282  -0.0253 0.0191  79  LEU   A CB   
474  C  CG   . LEU   A 79  ? 0.5083 0.4933 0.4211 0.1246  -0.0277 0.0217  79  LEU   A CG   
475  C  CD1  . LEU   A 79  ? 0.5100 0.5006 0.4314 0.1188  -0.0292 0.0232  79  LEU   A CD1  
476  C  CD2  . LEU   A 79  ? 0.5258 0.4964 0.4325 0.1226  -0.0306 0.0195  79  LEU   A CD2  
477  N  N    . PHE   A 80  ? 0.5649 0.5735 0.4777 0.1362  -0.0203 0.0284  80  PHE   A N    
478  C  CA   . PHE   A 80  ? 0.5809 0.5823 0.4840 0.1418  -0.0185 0.0323  80  PHE   A CA   
479  C  C    . PHE   A 80  ? 0.6377 0.6184 0.5309 0.1399  -0.0191 0.0351  80  PHE   A C    
480  O  O    . PHE   A 80  ? 0.6632 0.6334 0.5457 0.1457  -0.0180 0.0369  80  PHE   A O    
481  C  CB   . PHE   A 80  ? 0.5495 0.5585 0.4537 0.1424  -0.0169 0.0352  80  PHE   A CB   
482  C  CG   . PHE   A 80  ? 0.5251 0.5517 0.4345 0.1463  -0.0166 0.0332  80  PHE   A CG   
483  C  CD1  . PHE   A 80  ? 0.5217 0.5566 0.4329 0.1512  -0.0173 0.0303  80  PHE   A CD1  
484  C  CD2  . PHE   A 80  ? 0.5211 0.5554 0.4326 0.1454  -0.0154 0.0346  80  PHE   A CD2  
485  C  CE1  . PHE   A 80  ? 0.5159 0.5670 0.4322 0.1540  -0.0179 0.0282  80  PHE   A CE1  
486  C  CE2  . PHE   A 80  ? 0.5171 0.5659 0.4313 0.1491  -0.0158 0.0325  80  PHE   A CE2  
487  C  CZ   . PHE   A 80  ? 0.5078 0.5651 0.4248 0.1530  -0.0176 0.0292  80  PHE   A CZ   
488  N  N    . ASP   A 81  ? 0.6584 0.6330 0.5548 0.1320  -0.0210 0.0355  81  ASP   A N    
489  C  CA   . ASP   A 81  ? 0.7012 0.6557 0.5886 0.1288  -0.0224 0.0380  81  ASP   A CA   
490  C  C    . ASP   A 81  ? 0.7275 0.6772 0.6205 0.1204  -0.0265 0.0361  81  ASP   A C    
491  O  O    . ASP   A 81  ? 0.7088 0.6719 0.6139 0.1169  -0.0276 0.0337  81  ASP   A O    
492  C  CB   . ASP   A 81  ? 0.7425 0.6932 0.6264 0.1278  -0.0199 0.0430  81  ASP   A CB   
493  C  CG   . ASP   A 81  ? 0.8450 0.7732 0.7156 0.1265  -0.0202 0.0465  81  ASP   A CG   
494  O  OD1  . ASP   A 81  ? 0.8623 0.7761 0.7235 0.1284  -0.0220 0.0452  81  ASP   A OD1  
495  O  OD2  . ASP   A 81  ? 0.8890 0.8127 0.7572 0.1240  -0.0180 0.0507  81  ASP   A OD2  
496  N  N    . VAL   A 82  ? 0.7729 0.7026 0.6563 0.1175  -0.0291 0.0371  82  VAL   A N    
497  C  CA   . VAL   A 82  ? 0.8160 0.7374 0.7025 0.1095  -0.0343 0.0357  82  VAL   A CA   
498  C  C    . VAL   A 82  ? 0.8759 0.7779 0.7530 0.1052  -0.0356 0.0394  82  VAL   A C    
499  O  O    . VAL   A 82  ? 0.8909 0.7755 0.7523 0.1095  -0.0350 0.0403  82  VAL   A O    
500  C  CB   . VAL   A 82  ? 0.8233 0.7371 0.7045 0.1109  -0.0376 0.0314  82  VAL   A CB   
501  C  CG1  . VAL   A 82  ? 0.8313 0.7344 0.7136 0.1029  -0.0442 0.0302  82  VAL   A CG1  
502  C  CG2  . VAL   A 82  ? 0.8175 0.7489 0.7075 0.1141  -0.0361 0.0279  82  VAL   A CG2  
503  N  N    . CYS   A 83  ? 0.9072 0.8124 0.7938 0.0970  -0.0367 0.0417  83  CYS   A N    
504  C  CA   . CYS   A 83  ? 0.9488 0.8370 0.8289 0.0910  -0.0377 0.0454  83  CYS   A CA   
505  C  C    . CYS   A 83  ? 0.9686 0.8493 0.8540 0.0814  -0.0449 0.0440  83  CYS   A C    
506  O  O    . CYS   A 83  ? 0.9558 0.8515 0.8569 0.0774  -0.0477 0.0418  83  CYS   A O    
507  C  CB   . CYS   A 83  ? 0.9718 0.8684 0.8581 0.0889  -0.0325 0.0500  83  CYS   A CB   
508  S  SG   . CYS   A 83  ? 1.0712 0.9762 0.9506 0.1002  -0.0252 0.0521  83  CYS   A SG   
509  N  N    . THR   A 84  ? 0.9963 0.8537 0.8687 0.0775  -0.0480 0.0454  84  THR   A N    
510  C  CA   . THR   A 84  ? 1.0166 0.8641 0.8923 0.0676  -0.0559 0.0443  84  THR   A CA   
511  C  C    . THR   A 84  ? 1.0133 0.8680 0.9035 0.0576  -0.0554 0.0480  84  THR   A C    
512  O  O    . THR   A 84  ? 1.0195 0.8735 0.9075 0.0578  -0.0491 0.0524  84  THR   A O    
513  C  CB   . THR   A 84  ? 1.0645 0.8821 0.9180 0.0681  -0.0601 0.0434  84  THR   A CB   
514  O  OG1  . THR   A 84  ? 1.0805 0.8887 0.9374 0.0579  -0.0689 0.0420  84  THR   A OG1  
515  C  CG2  . THR   A 84  ? 1.0871 0.8868 0.9240 0.0706  -0.0553 0.0476  84  THR   A CG2  
516  N  N    . LYS   A 93  ? 0.8809 0.8196 0.8659 0.0339  -0.0666 0.0448  93  LYS   A N    
517  C  CA   . LYS   A 93  ? 0.8984 0.8129 0.8630 0.0355  -0.0730 0.0420  93  LYS   A CA   
518  C  C    . LYS   A 93  ? 0.8946 0.8035 0.8416 0.0468  -0.0678 0.0404  93  LYS   A C    
519  O  O    . LYS   A 93  ? 0.9045 0.7936 0.8323 0.0495  -0.0665 0.0414  93  LYS   A O    
520  C  CB   . LYS   A 93  ? 0.9303 0.8437 0.9000 0.0324  -0.0841 0.0376  93  LYS   A CB   
521  C  CG   . LYS   A 93  ? 1.0136 0.9000 0.9610 0.0335  -0.0913 0.0345  93  LYS   A CG   
522  C  CD   . LYS   A 93  ? 1.0891 0.9560 1.0309 0.0238  -0.0975 0.0362  93  LYS   A CD   
523  C  CE   . LYS   A 93  ? 1.1582 0.9979 1.0775 0.0250  -0.1056 0.0326  93  LYS   A CE   
524  N  NZ   . LYS   A 93  ? 1.1746 1.0171 1.0995 0.0238  -0.1159 0.0282  93  LYS   A NZ   
525  N  N    . LEU   A 94  ? 0.8748 0.8012 0.8287 0.0534  -0.0648 0.0381  94  LEU   A N    
526  C  CA   . LEU   A 94  ? 0.8688 0.7942 0.8101 0.0635  -0.0601 0.0364  94  LEU   A CA   
527  C  C    . LEU   A 94  ? 0.8248 0.7695 0.7744 0.0679  -0.0518 0.0382  94  LEU   A C    
528  O  O    . LEU   A 94  ? 0.8163 0.7793 0.7825 0.0660  -0.0510 0.0379  94  LEU   A O    
529  C  CB   . LEU   A 94  ? 0.8834 0.8099 0.8232 0.0672  -0.0648 0.0312  94  LEU   A CB   
530  C  CG   . LEU   A 94  ? 0.9263 0.8348 0.8458 0.0733  -0.0656 0.0287  94  LEU   A CG   
531  C  CD1  . LEU   A 94  ? 0.9351 0.8468 0.8552 0.0761  -0.0692 0.0242  94  LEU   A CD1  
532  C  CD2  . LEU   A 94  ? 0.9405 0.8503 0.8512 0.0811  -0.0576 0.0302  94  LEU   A CD2  
533  N  N    . THR   A 95  ? 0.7966 0.7370 0.7341 0.0744  -0.0459 0.0397  95  THR   A N    
534  C  CA   . THR   A 95  ? 0.7669 0.7237 0.7095 0.0793  -0.0387 0.0412  95  THR   A CA   
535  C  C    . THR   A 95  ? 0.7243 0.6836 0.6584 0.0884  -0.0369 0.0382  95  THR   A C    
536  O  O    . THR   A 95  ? 0.7307 0.6765 0.6501 0.0929  -0.0365 0.0382  95  THR   A O    
537  C  CB   . THR   A 95  ? 0.7994 0.7519 0.7387 0.0774  -0.0333 0.0467  95  THR   A CB   
538  O  OG1  . THR   A 95  ? 0.8134 0.7797 0.7696 0.0713  -0.0315 0.0489  95  THR   A OG1  
539  C  CG2  . THR   A 95  ? 0.8111 0.7669 0.7414 0.0860  -0.0270 0.0482  95  THR   A CG2  
540  N  N    . LEU   A 96  ? 0.6755 0.6521 0.6191 0.0909  -0.0357 0.0354  96  LEU   A N    
541  C  CA   . LEU   A 96  ? 0.6392 0.6214 0.5781 0.0983  -0.0340 0.0323  96  LEU   A CA   
542  C  C    . LEU   A 96  ? 0.5961 0.5919 0.5373 0.1026  -0.0283 0.0338  96  LEU   A C    
543  O  O    . LEU   A 96  ? 0.5772 0.5858 0.5289 0.1007  -0.0264 0.0342  96  LEU   A O    
544  C  CB   . LEU   A 96  ? 0.6297 0.6190 0.5758 0.0975  -0.0375 0.0277  96  LEU   A CB   
545  C  CG   . LEU   A 96  ? 0.6516 0.6276 0.5885 0.0985  -0.0417 0.0245  96  LEU   A CG   
546  C  CD1  . LEU   A 96  ? 0.6698 0.6287 0.6016 0.0933  -0.0468 0.0257  96  LEU   A CD1  
547  C  CD2  . LEU   A 96  ? 0.6479 0.6314 0.5912 0.0983  -0.0442 0.0203  96  LEU   A CD2  
548  N  N    . VAL   A 97  ? 0.5813 0.5739 0.5121 0.1090  -0.0256 0.0346  97  VAL   A N    
549  C  CA   . VAL   A 97  ? 0.5688 0.5720 0.4990 0.1140  -0.0211 0.0361  97  VAL   A CA   
550  C  C    . VAL   A 97  ? 0.5479 0.5614 0.4786 0.1193  -0.0211 0.0321  97  VAL   A C    
551  O  O    . VAL   A 97  ? 0.5563 0.5643 0.4800 0.1235  -0.0218 0.0308  97  VAL   A O    
552  C  CB   . VAL   A 97  ? 0.5856 0.5780 0.5038 0.1174  -0.0184 0.0405  97  VAL   A CB   
553  C  CG1  . VAL   A 97  ? 0.5898 0.5923 0.5068 0.1221  -0.0144 0.0425  97  VAL   A CG1  
554  C  CG2  . VAL   A 97  ? 0.6000 0.5788 0.5164 0.1109  -0.0188 0.0443  97  VAL   A CG2  
555  N  N    . PHE   A 98  ? 0.5168 0.5449 0.4555 0.1193  -0.0200 0.0303  98  PHE   A N    
556  C  CA   . PHE   A 98  ? 0.5002 0.5388 0.4403 0.1232  -0.0201 0.0264  98  PHE   A CA   
557  C  C    . PHE   A 98  ? 0.4999 0.5478 0.4380 0.1276  -0.0174 0.0276  98  PHE   A C    
558  O  O    . PHE   A 98  ? 0.4999 0.5473 0.4368 0.1270  -0.0149 0.0312  98  PHE   A O    
559  C  CB   . PHE   A 98  ? 0.4876 0.5341 0.4370 0.1196  -0.0216 0.0227  98  PHE   A CB   
560  C  CG   . PHE   A 98  ? 0.4919 0.5299 0.4430 0.1156  -0.0251 0.0209  98  PHE   A CG   
561  C  CD1  . PHE   A 98  ? 0.5048 0.5385 0.4521 0.1171  -0.0268 0.0176  98  PHE   A CD1  
562  C  CD2  . PHE   A 98  ? 0.5019 0.5362 0.4585 0.1103  -0.0268 0.0224  98  PHE   A CD2  
563  C  CE1  . PHE   A 98  ? 0.5178 0.5418 0.4644 0.1139  -0.0302 0.0159  98  PHE   A CE1  
564  C  CE2  . PHE   A 98  ? 0.5150 0.5410 0.4724 0.1070  -0.0312 0.0206  98  PHE   A CE2  
565  C  CZ   . PHE   A 98  ? 0.5165 0.5364 0.4677 0.1090  -0.0329 0.0173  98  PHE   A CZ   
566  N  N    . GLU   A 99  ? 0.4906 0.5473 0.4285 0.1316  -0.0180 0.0245  99  GLU   A N    
567  C  CA   . GLU   A 99  ? 0.4820 0.5482 0.4181 0.1356  -0.0168 0.0249  99  GLU   A CA   
568  C  C    . GLU   A 99  ? 0.4756 0.5489 0.4175 0.1322  -0.0156 0.0238  99  GLU   A C    
569  O  O    . GLU   A 99  ? 0.4729 0.5475 0.4214 0.1283  -0.0166 0.0211  99  GLU   A O    
570  C  CB   . GLU   A 99  ? 0.4906 0.5657 0.4270 0.1396  -0.0185 0.0213  99  GLU   A CB   
571  C  CG   . GLU   A 99  ? 0.5421 0.6218 0.4854 0.1362  -0.0201 0.0164  99  GLU   A CG   
572  C  CD   . GLU   A 99  ? 0.5762 0.6665 0.5216 0.1386  -0.0215 0.0127  99  GLU   A CD   
573  O  OE1  . GLU   A 99  ? 0.5323 0.6231 0.4813 0.1368  -0.0221 0.0095  99  GLU   A OE1  
574  O  OE2  . GLU   A 99  ? 0.5920 0.6899 0.5353 0.1422  -0.0221 0.0129  99  GLU   A OE2  
575  N  N    . HIS   A 100 ? 0.4653 0.5426 0.4037 0.1346  -0.0133 0.0258  100 HIS   A N    
576  C  CA   . HIS   A 100 ? 0.4695 0.5532 0.4120 0.1326  -0.0113 0.0249  100 HIS   A CA   
577  C  C    . HIS   A 100 ? 0.4745 0.5676 0.4160 0.1351  -0.0130 0.0203  100 HIS   A C    
578  O  O    . HIS   A 100 ? 0.4912 0.5871 0.4268 0.1396  -0.0145 0.0200  100 HIS   A O    
579  C  CB   . HIS   A 100 ? 0.4814 0.5625 0.4192 0.1335  -0.0068 0.0299  100 HIS   A CB   
580  C  CG   . HIS   A 100 ? 0.4912 0.5785 0.4327 0.1323  -0.0036 0.0294  100 HIS   A CG   
581  N  ND1  . HIS   A 100 ? 0.5047 0.5975 0.4399 0.1363  -0.0027 0.0279  100 HIS   A ND1  
582  C  CD2  . HIS   A 100 ? 0.4957 0.5845 0.4463 0.1279  -0.0012 0.0302  100 HIS   A CD2  
583  C  CE1  . HIS   A 100 ? 0.5080 0.6044 0.4477 0.1346  0.0007  0.0277  100 HIS   A CE1  
584  N  NE2  . HIS   A 100 ? 0.5107 0.6059 0.4606 0.1297  0.0019  0.0292  100 HIS   A NE2  
585  N  N    . VAL   A 101 ? 0.4511 0.5488 0.3984 0.1324  -0.0133 0.0168  101 VAL   A N    
586  C  CA   . VAL   A 101 ? 0.4457 0.5506 0.3908 0.1341  -0.0148 0.0125  101 VAL   A CA   
587  C  C    . VAL   A 101 ? 0.4600 0.5668 0.4051 0.1337  -0.0114 0.0128  101 VAL   A C    
588  O  O    . VAL   A 101 ? 0.4504 0.5555 0.4020 0.1308  -0.0092 0.0142  101 VAL   A O    
589  C  CB   . VAL   A 101 ? 0.4374 0.5456 0.3859 0.1325  -0.0184 0.0073  101 VAL   A CB   
590  C  CG1  . VAL   A 101 ? 0.4299 0.5326 0.3826 0.1303  -0.0196 0.0074  101 VAL   A CG1  
591  C  CG2  . VAL   A 101 ? 0.4356 0.5469 0.3858 0.1306  -0.0185 0.0031  101 VAL   A CG2  
592  N  N    . ASP   A 102 ? 0.4729 0.5828 0.4102 0.1372  -0.0107 0.0122  102 ASP   A N    
593  C  CA   . ASP   A 102 ? 0.4973 0.6079 0.4315 0.1384  -0.0064 0.0131  102 ASP   A CA   
594  C  C    . ASP   A 102 ? 0.4958 0.6084 0.4355 0.1362  -0.0057 0.0096  102 ASP   A C    
595  O  O    . ASP   A 102 ? 0.5025 0.6151 0.4452 0.1360  -0.0011 0.0119  102 ASP   A O    
596  C  CB   . ASP   A 102 ? 0.5607 0.6722 0.4823 0.1432  -0.0068 0.0125  102 ASP   A CB   
597  C  CG   . ASP   A 102 ? 0.6605 0.7683 0.5742 0.1469  -0.0056 0.0174  102 ASP   A CG   
598  O  OD1  . ASP   A 102 ? 0.6851 0.7885 0.6000 0.1461  -0.0007 0.0225  102 ASP   A OD1  
599  O  OD2  . ASP   A 102 ? 0.7109 0.8201 0.6168 0.1506  -0.0095 0.0162  102 ASP   A OD2  
600  N  N    . GLN   A 103 ? 0.4914 0.6057 0.4320 0.1348  -0.0097 0.0043  103 GLN   A N    
601  C  CA   . GLN   A 103 ? 0.5080 0.6224 0.4517 0.1334  -0.0091 0.0009  103 GLN   A CA   
602  C  C    . GLN   A 103 ? 0.5055 0.6184 0.4563 0.1296  -0.0124 -0.0021 103 GLN   A C    
603  O  O    . GLN   A 103 ? 0.4978 0.6102 0.4493 0.1282  -0.0157 -0.0032 103 GLN   A O    
604  C  CB   . GLN   A 103 ? 0.5511 0.6660 0.4849 0.1358  -0.0096 -0.0031 103 GLN   A CB   
605  C  CG   . GLN   A 103 ? 0.6439 0.7602 0.5739 0.1347  -0.0152 -0.0077 103 GLN   A CG   
606  C  CD   . GLN   A 103 ? 0.7688 0.8851 0.6873 0.1372  -0.0164 -0.0106 103 GLN   A CD   
607  O  OE1  . GLN   A 103 ? 0.7993 0.9125 0.7124 0.1385  -0.0140 -0.0124 103 GLN   A OE1  
608  N  NE2  . GLN   A 103 ? 0.8035 0.9229 0.7175 0.1384  -0.0205 -0.0113 103 GLN   A NE2  
609  N  N    . ASP   A 104 ? 0.5130 0.6246 0.4679 0.1287  -0.0113 -0.0036 104 ASP   A N    
610  C  CA   . ASP   A 104 ? 0.5314 0.6398 0.4905 0.1258  -0.0142 -0.0068 104 ASP   A CA   
611  C  C    . ASP   A 104 ? 0.5597 0.6667 0.5123 0.1261  -0.0153 -0.0122 104 ASP   A C    
612  O  O    . ASP   A 104 ? 0.5746 0.6831 0.5199 0.1284  -0.0141 -0.0132 104 ASP   A O    
613  C  CB   . ASP   A 104 ? 0.5464 0.6537 0.5142 0.1249  -0.0131 -0.0048 104 ASP   A CB   
614  C  CG   . ASP   A 104 ? 0.6051 0.7158 0.5754 0.1275  -0.0089 -0.0032 104 ASP   A CG   
615  O  OD1  . ASP   A 104 ? 0.6224 0.7336 0.5854 0.1303  -0.0068 -0.0053 104 ASP   A OD1  
616  O  OD2  . ASP   A 104 ? 0.6314 0.7441 0.6111 0.1268  -0.0076 -0.0001 104 ASP   A OD2  
617  N  N    . LEU   A 105 ? 0.5683 0.6708 0.5219 0.1236  -0.0176 -0.0156 105 LEU   A N    
618  C  CA   . LEU   A 105 ? 0.5823 0.6815 0.5290 0.1230  -0.0186 -0.0207 105 LEU   A CA   
619  C  C    . LEU   A 105 ? 0.6004 0.6982 0.5434 0.1264  -0.0156 -0.0214 105 LEU   A C    
620  O  O    . LEU   A 105 ? 0.5985 0.6936 0.5328 0.1271  -0.0159 -0.0250 105 LEU   A O    
621  C  CB   . LEU   A 105 ? 0.5809 0.6737 0.5290 0.1198  -0.0208 -0.0235 105 LEU   A CB   
622  C  CG   . LEU   A 105 ? 0.5917 0.6819 0.5353 0.1162  -0.0231 -0.0279 105 LEU   A CG   
623  C  CD1  . LEU   A 105 ? 0.5950 0.6760 0.5372 0.1142  -0.0237 -0.0305 105 LEU   A CD1  
624  C  CD2  . LEU   A 105 ? 0.5875 0.6791 0.5234 0.1163  -0.0236 -0.0312 105 LEU   A CD2  
625  N  N    . THR   A 106 ? 0.6143 0.7138 0.5643 0.1286  -0.0129 -0.0179 106 THR   A N    
626  C  CA   . THR   A 106 ? 0.6295 0.7293 0.5788 0.1327  -0.0091 -0.0175 106 THR   A CA   
627  C  C    . THR   A 106 ? 0.6353 0.7375 0.5766 0.1359  -0.0056 -0.0167 106 THR   A C    
628  O  O    . THR   A 106 ? 0.6384 0.7364 0.5700 0.1384  -0.0044 -0.0199 106 THR   A O    
629  C  CB   . THR   A 106 ? 0.6470 0.7513 0.6091 0.1335  -0.0072 -0.0131 106 THR   A CB   
630  O  OG1  . THR   A 106 ? 0.6689 0.7698 0.6367 0.1306  -0.0114 -0.0139 106 THR   A OG1  
631  C  CG2  . THR   A 106 ? 0.6543 0.7606 0.6182 0.1382  -0.0028 -0.0125 106 THR   A CG2  
632  N  N    . THR   A 107 ? 0.6372 0.7443 0.5809 0.1361  -0.0040 -0.0123 107 THR   A N    
633  C  CA   . THR   A 107 ? 0.6487 0.7570 0.5835 0.1395  -0.0007 -0.0108 107 THR   A CA   
634  C  C    . THR   A 107 ? 0.6491 0.7541 0.5717 0.1391  -0.0046 -0.0153 107 THR   A C    
635  O  O    . THR   A 107 ? 0.6577 0.7604 0.5690 0.1424  -0.0029 -0.0163 107 THR   A O    
636  C  CB   . THR   A 107 ? 0.6829 0.7955 0.6225 0.1398  0.0021  -0.0049 107 THR   A CB   
637  O  OG1  . THR   A 107 ? 0.7282 0.8413 0.6717 0.1362  -0.0023 -0.0043 107 THR   A OG1  
638  C  CG2  . THR   A 107 ? 0.6817 0.7982 0.6329 0.1402  0.0068  -0.0006 107 THR   A CG2  
639  N  N    . TYR   A 108 ? 0.6385 0.7431 0.5632 0.1349  -0.0099 -0.0181 108 TYR   A N    
640  C  CA   . TYR   A 108 ? 0.6442 0.7471 0.5601 0.1333  -0.0144 -0.0227 108 TYR   A CA   
641  C  C    . TYR   A 108 ? 0.6485 0.7442 0.5562 0.1334  -0.0145 -0.0279 108 TYR   A C    
642  O  O    . TYR   A 108 ? 0.6566 0.7491 0.5526 0.1345  -0.0158 -0.0310 108 TYR   A O    
643  C  CB   . TYR   A 108 ? 0.6415 0.7473 0.5638 0.1288  -0.0189 -0.0238 108 TYR   A CB   
644  C  CG   . TYR   A 108 ? 0.6571 0.7626 0.5732 0.1262  -0.0235 -0.0289 108 TYR   A CG   
645  C  CD1  . TYR   A 108 ? 0.6757 0.7855 0.5863 0.1274  -0.0264 -0.0291 108 TYR   A CD1  
646  C  CD2  . TYR   A 108 ? 0.6727 0.7729 0.5875 0.1224  -0.0252 -0.0337 108 TYR   A CD2  
647  C  CE1  . TYR   A 108 ? 0.6932 0.8037 0.5990 0.1245  -0.0314 -0.0340 108 TYR   A CE1  
648  C  CE2  . TYR   A 108 ? 0.6912 0.7910 0.6006 0.1190  -0.0294 -0.0385 108 TYR   A CE2  
649  C  CZ   . TYR   A 108 ? 0.7093 0.8150 0.6150 0.1198  -0.0327 -0.0388 108 TYR   A CZ   
650  O  OH   . TYR   A 108 ? 0.7395 0.8461 0.6417 0.1158  -0.0377 -0.0436 108 TYR   A OH   
651  N  N    . LEU   A 109 ? 0.6416 0.7336 0.5543 0.1324  -0.0136 -0.0289 109 LEU   A N    
652  C  CA   . LEU   A 109 ? 0.6552 0.7386 0.5596 0.1330  -0.0134 -0.0334 109 LEU   A CA   
653  C  C    . LEU   A 109 ? 0.6840 0.7645 0.5801 0.1391  -0.0086 -0.0328 109 LEU   A C    
654  O  O    . LEU   A 109 ? 0.6926 0.7647 0.5765 0.1402  -0.0089 -0.0371 109 LEU   A O    
655  C  CB   . LEU   A 109 ? 0.6401 0.7193 0.5510 0.1313  -0.0138 -0.0342 109 LEU   A CB   
656  C  CG   . LEU   A 109 ? 0.6367 0.7148 0.5520 0.1254  -0.0179 -0.0360 109 LEU   A CG   
657  C  CD1  . LEU   A 109 ? 0.6299 0.7014 0.5485 0.1249  -0.0179 -0.0367 109 LEU   A CD1  
658  C  CD2  . LEU   A 109 ? 0.6426 0.7175 0.5496 0.1212  -0.0213 -0.0409 109 LEU   A CD2  
659  N  N    . ASP   A 110 ? 0.6974 0.7840 0.5998 0.1429  -0.0038 -0.0275 110 ASP   A N    
660  C  CA   . ASP   A 110 ? 0.7208 0.8061 0.6168 0.1491  0.0024  -0.0258 110 ASP   A CA   
661  C  C    . ASP   A 110 ? 0.7490 0.8308 0.6295 0.1508  0.0018  -0.0274 110 ASP   A C    
662  O  O    . ASP   A 110 ? 0.7577 0.8313 0.6244 0.1539  0.0030  -0.0307 110 ASP   A O    
663  C  CB   . ASP   A 110 ? 0.7350 0.8292 0.6433 0.1512  0.0077  -0.0191 110 ASP   A CB   
664  C  CG   . ASP   A 110 ? 0.7858 0.8841 0.7093 0.1511  0.0092  -0.0170 110 ASP   A CG   
665  O  OD1  . ASP   A 110 ? 0.7966 0.8900 0.7190 0.1524  0.0084  -0.0202 110 ASP   A OD1  
666  O  OD2  . ASP   A 110 ? 0.8062 0.9120 0.7422 0.1501  0.0110  -0.0120 110 ASP   A OD2  
667  N  N    . LYS   A 111 ? 0.7615 0.8485 0.6432 0.1489  -0.0006 -0.0252 111 LYS   A N    
668  C  CA   . LYS   A 111 ? 0.7910 0.8757 0.6586 0.1510  -0.0020 -0.0258 111 LYS   A CA   
669  C  C    . LYS   A 111 ? 0.8140 0.8936 0.6710 0.1477  -0.0093 -0.0322 111 LYS   A C    
670  O  O    . LYS   A 111 ? 0.8240 0.8996 0.6667 0.1501  -0.0108 -0.0337 111 LYS   A O    
671  C  CB   . LYS   A 111 ? 0.8193 0.9112 0.6922 0.1508  -0.0020 -0.0207 111 LYS   A CB   
672  C  CG   . LYS   A 111 ? 0.8861 0.9813 0.7657 0.1542  0.0060  -0.0143 111 LYS   A CG   
673  C  CD   . LYS   A 111 ? 0.9472 1.0470 0.8300 0.1539  0.0062  -0.0092 111 LYS   A CD   
674  C  CE   . LYS   A 111 ? 0.9938 1.0968 0.8851 0.1557  0.0142  -0.0029 111 LYS   A CE   
675  N  NZ   . LYS   A 111 ? 1.0250 1.1308 0.9201 0.1546  0.0145  0.0022  111 LYS   A NZ   
676  N  N    . VAL   A 112 ? 0.8189 0.8978 0.6819 0.1422  -0.0137 -0.0360 112 VAL   A N    
677  C  CA   . VAL   A 112 ? 0.8359 0.9109 0.6907 0.1379  -0.0205 -0.0420 112 VAL   A CA   
678  C  C    . VAL   A 112 ? 0.8593 0.9218 0.6954 0.1406  -0.0200 -0.0465 112 VAL   A C    
679  O  O    . VAL   A 112 ? 0.8689 0.9246 0.7025 0.1434  -0.0153 -0.0469 112 VAL   A O    
680  C  CB   . VAL   A 112 ? 0.8389 0.9157 0.7043 0.1309  -0.0243 -0.0446 112 VAL   A CB   
681  C  CG1  . VAL   A 112 ? 0.8468 0.9146 0.7110 0.1304  -0.0219 -0.0470 112 VAL   A CG1  
682  C  CG2  . VAL   A 112 ? 0.8441 0.9222 0.7062 0.1255  -0.0316 -0.0491 112 VAL   A CG2  
683  N  N    . PRO   A 113 ? 0.8668 0.9258 0.6891 0.1404  -0.0248 -0.0497 113 PRO   A N    
684  C  CA   . PRO   A 113 ? 0.8885 0.9336 0.6908 0.1432  -0.0244 -0.0541 113 PRO   A CA   
685  C  C    . PRO   A 113 ? 0.9095 0.9447 0.7076 0.1384  -0.0270 -0.0600 113 PRO   A C    
686  O  O    . PRO   A 113 ? 0.9063 0.9458 0.7156 0.1315  -0.0308 -0.0617 113 PRO   A O    
687  C  CB   . PRO   A 113 ? 0.8975 0.9422 0.6872 0.1434  -0.0305 -0.0559 113 PRO   A CB   
688  C  CG   . PRO   A 113 ? 0.8895 0.9483 0.6925 0.1432  -0.0319 -0.0510 113 PRO   A CG   
689  C  CD   . PRO   A 113 ? 0.8585 0.9253 0.6816 0.1384  -0.0311 -0.0495 113 PRO   A CD   
690  N  N    . GLU   A 114 ? 0.9234 0.9441 0.7040 0.1423  -0.0245 -0.0631 114 GLU   A N    
691  C  CA   . GLU   A 114 ? 0.9396 0.9471 0.7119 0.1384  -0.0266 -0.0690 114 GLU   A CA   
692  C  C    . GLU   A 114 ? 0.9365 0.9423 0.7045 0.1295  -0.0361 -0.0747 114 GLU   A C    
693  O  O    . GLU   A 114 ? 0.9409 0.9521 0.7055 0.1289  -0.0411 -0.0749 114 GLU   A O    
694  C  CB   . GLU   A 114 ? 0.9942 0.9853 0.7462 0.1457  -0.0216 -0.0709 114 GLU   A CB   
695  C  CG   . GLU   A 114 ? 1.0634 1.0560 0.8216 0.1537  -0.0121 -0.0661 114 GLU   A CG   
696  C  CD   . GLU   A 114 ? 1.1252 1.1215 0.8996 0.1513  -0.0107 -0.0650 114 GLU   A CD   
697  O  OE1  . GLU   A 114 ? 1.1343 1.1210 0.9045 0.1462  -0.0142 -0.0697 114 GLU   A OE1  
698  O  OE2  . GLU   A 114 ? 1.1318 1.1401 0.9228 0.1541  -0.0063 -0.0594 114 GLU   A OE2  
699  N  N    . PRO   A 115 ? 0.9213 0.9205 0.6904 0.1223  -0.0390 -0.0791 115 PRO   A N    
700  C  CA   . PRO   A 115 ? 0.9121 0.9030 0.6837 0.1223  -0.0344 -0.0794 115 PRO   A CA   
701  C  C    . PRO   A 115 ? 0.8892 0.8927 0.6828 0.1201  -0.0324 -0.0752 115 PRO   A C    
702  O  O    . PRO   A 115 ? 0.8943 0.8914 0.6907 0.1184  -0.0305 -0.0760 115 PRO   A O    
703  C  CB   . PRO   A 115 ? 0.9292 0.9058 0.6885 0.1147  -0.0396 -0.0865 115 PRO   A CB   
704  C  CG   . PRO   A 115 ? 0.9310 0.9184 0.6965 0.1067  -0.0477 -0.0884 115 PRO   A CG   
705  C  CD   . PRO   A 115 ? 0.9119 0.9112 0.6794 0.1129  -0.0478 -0.0843 115 PRO   A CD   
706  N  N    . GLY   A 116 ? 0.8603 0.8801 0.6677 0.1204  -0.0330 -0.0707 116 GLY   A N    
707  C  CA   . GLY   A 116 ? 0.8393 0.8704 0.6662 0.1187  -0.0314 -0.0666 116 GLY   A CA   
708  C  C    . GLY   A 116 ? 0.8094 0.8539 0.6487 0.1128  -0.0362 -0.0658 116 GLY   A C    
709  O  O    . GLY   A 116 ? 0.8091 0.8578 0.6443 0.1112  -0.0411 -0.0675 116 GLY   A O    
710  N  N    . VAL   A 117 ? 0.7812 0.8324 0.6356 0.1103  -0.0349 -0.0631 117 VAL   A N    
711  C  CA   . VAL   A 117 ? 0.7530 0.8170 0.6208 0.1056  -0.0382 -0.0618 117 VAL   A CA   
712  C  C    . VAL   A 117 ? 0.7375 0.8002 0.6039 0.0971  -0.0434 -0.0672 117 VAL   A C    
713  O  O    . VAL   A 117 ? 0.7427 0.7946 0.6047 0.0928  -0.0428 -0.0706 117 VAL   A O    
714  C  CB   . VAL   A 117 ? 0.7478 0.8161 0.6296 0.1056  -0.0348 -0.0577 117 VAL   A CB   
715  C  CG1  . VAL   A 117 ? 0.7363 0.8179 0.6308 0.1030  -0.0371 -0.0553 117 VAL   A CG1  
716  C  CG2  . VAL   A 117 ? 0.7530 0.8211 0.6362 0.1128  -0.0300 -0.0530 117 VAL   A CG2  
717  N  N    . PRO   A 118 ? 0.7210 0.7946 0.5914 0.0945  -0.0486 -0.0679 118 PRO   A N    
718  C  CA   . PRO   A 118 ? 0.7194 0.7944 0.5918 0.0856  -0.0537 -0.0729 118 PRO   A CA   
719  C  C    . PRO   A 118 ? 0.7198 0.7962 0.6042 0.0800  -0.0510 -0.0724 118 PRO   A C    
720  O  O    . PRO   A 118 ? 0.7082 0.7919 0.6038 0.0826  -0.0479 -0.0678 118 PRO   A O    
721  C  CB   . PRO   A 118 ? 0.7197 0.8099 0.5984 0.0857  -0.0594 -0.0722 118 PRO   A CB   
722  C  CG   . PRO   A 118 ? 0.7280 0.8192 0.6004 0.0949  -0.0578 -0.0682 118 PRO   A CG   
723  C  CD   . PRO   A 118 ? 0.7102 0.7957 0.5842 0.0994  -0.0503 -0.0642 118 PRO   A CD   
724  N  N    . THR   A 119 ? 0.7319 0.7995 0.6124 0.0724  -0.0520 -0.0771 119 THR   A N    
725  C  CA   . THR   A 119 ? 0.7424 0.8078 0.6309 0.0660  -0.0491 -0.0775 119 THR   A CA   
726  C  C    . THR   A 119 ? 0.7283 0.8104 0.6350 0.0647  -0.0486 -0.0740 119 THR   A C    
727  O  O    . THR   A 119 ? 0.7347 0.8150 0.6476 0.0640  -0.0440 -0.0717 119 THR   A O    
728  C  CB   . THR   A 119 ? 0.7781 0.8340 0.6598 0.0564  -0.0518 -0.0836 119 THR   A CB   
729  O  OG1  . THR   A 119 ? 0.7977 0.8526 0.6877 0.0495  -0.0486 -0.0837 119 THR   A OG1  
730  C  CG2  . THR   A 119 ? 0.7810 0.8469 0.6643 0.0517  -0.0592 -0.0870 119 THR   A CG2  
731  N  N    . GLU   A 120 ? 0.7095 0.8070 0.6235 0.0649  -0.0533 -0.0737 120 GLU   A N    
732  C  CA   . GLU   A 120 ? 0.6919 0.8060 0.6227 0.0642  -0.0533 -0.0708 120 GLU   A CA   
733  C  C    . GLU   A 120 ? 0.6710 0.7911 0.6060 0.0730  -0.0508 -0.0649 120 GLU   A C    
734  O  O    . GLU   A 120 ? 0.6564 0.7860 0.6037 0.0735  -0.0489 -0.0618 120 GLU   A O    
735  C  CB   . GLU   A 120 ? 0.7108 0.8389 0.6483 0.0597  -0.0603 -0.0737 120 GLU   A CB   
736  C  CG   . GLU   A 120 ? 0.7865 0.9103 0.7241 0.0488  -0.0620 -0.0791 120 GLU   A CG   
737  C  CD   . GLU   A 120 ? 0.9076 1.0291 0.8539 0.0430  -0.0558 -0.0785 120 GLU   A CD   
738  O  OE1  . GLU   A 120 ? 0.9221 1.0580 0.8841 0.0428  -0.0541 -0.0757 120 GLU   A OE1  
739  O  OE2  . GLU   A 120 ? 0.9547 1.0590 0.8910 0.0392  -0.0525 -0.0807 120 GLU   A OE2  
740  N  N    . THR   A 121 ? 0.6610 0.7747 0.5857 0.0799  -0.0502 -0.0632 121 THR   A N    
741  C  CA   . THR   A 121 ? 0.6487 0.7652 0.5758 0.0876  -0.0473 -0.0576 121 THR   A CA   
742  C  C    . THR   A 121 ? 0.6454 0.7522 0.5734 0.0878  -0.0416 -0.0557 121 THR   A C    
743  O  O    . THR   A 121 ? 0.6411 0.7516 0.5765 0.0907  -0.0391 -0.0515 121 THR   A O    
744  C  CB   . THR   A 121 ? 0.6714 0.7849 0.5874 0.0938  -0.0483 -0.0568 121 THR   A CB   
745  O  OG1  . THR   A 121 ? 0.6971 0.8188 0.6113 0.0935  -0.0544 -0.0587 121 THR   A OG1  
746  C  CG2  . THR   A 121 ? 0.6680 0.7836 0.5864 0.1009  -0.0447 -0.0509 121 THR   A CG2  
747  N  N    . ILE   A 122 ? 0.6451 0.7384 0.5646 0.0848  -0.0402 -0.0591 122 ILE   A N    
748  C  CA   . ILE   A 122 ? 0.6465 0.7289 0.5650 0.0849  -0.0359 -0.0580 122 ILE   A CA   
749  C  C    . ILE   A 122 ? 0.6497 0.7357 0.5780 0.0803  -0.0343 -0.0574 122 ILE   A C    
750  O  O    . ILE   A 122 ? 0.6599 0.7449 0.5926 0.0830  -0.0315 -0.0538 122 ILE   A O    
751  C  CB   . ILE   A 122 ? 0.6529 0.7192 0.5587 0.0829  -0.0351 -0.0621 122 ILE   A CB   
752  C  CG1  . ILE   A 122 ? 0.6625 0.7238 0.5584 0.0895  -0.0348 -0.0618 122 ILE   A CG1  
753  C  CG2  . ILE   A 122 ? 0.6613 0.7165 0.5665 0.0819  -0.0315 -0.0615 122 ILE   A CG2  
754  C  CD1  . ILE   A 122 ? 0.6817 0.7272 0.5625 0.0886  -0.0347 -0.0664 122 ILE   A CD1  
755  N  N    . LYS   A 123 ? 0.6401 0.7308 0.5720 0.0733  -0.0362 -0.0607 123 LYS   A N    
756  C  CA   . LYS   A 123 ? 0.6384 0.7338 0.5802 0.0684  -0.0339 -0.0604 123 LYS   A CA   
757  C  C    . LYS   A 123 ? 0.6127 0.7202 0.5653 0.0729  -0.0330 -0.0557 123 LYS   A C    
758  O  O    . LYS   A 123 ? 0.6114 0.7151 0.5669 0.0736  -0.0290 -0.0532 123 LYS   A O    
759  C  CB   . LYS   A 123 ? 0.6760 0.7777 0.6219 0.0602  -0.0367 -0.0647 123 LYS   A CB   
760  C  CG   . LYS   A 123 ? 0.7586 0.8595 0.7114 0.0534  -0.0326 -0.0652 123 LYS   A CG   
761  C  CD   . LYS   A 123 ? 0.8398 0.9554 0.8041 0.0462  -0.0353 -0.0678 123 LYS   A CD   
762  C  CE   . LYS   A 123 ? 0.9222 1.0296 0.8804 0.0371  -0.0371 -0.0733 123 LYS   A CE   
763  N  NZ   . LYS   A 123 ? 0.9620 1.0852 0.9344 0.0290  -0.0393 -0.0754 123 LYS   A NZ   
764  N  N    . ASP   A 124 ? 0.5900 0.7104 0.5468 0.0764  -0.0367 -0.0545 124 ASP   A N    
765  C  CA   . ASP   A 124 ? 0.5747 0.7062 0.5402 0.0815  -0.0363 -0.0501 124 ASP   A CA   
766  C  C    . ASP   A 124 ? 0.5656 0.6896 0.5279 0.0875  -0.0333 -0.0457 124 ASP   A C    
767  O  O    . ASP   A 124 ? 0.5713 0.6972 0.5393 0.0894  -0.0307 -0.0425 124 ASP   A O    
768  C  CB   . ASP   A 124 ? 0.5943 0.7389 0.5622 0.0844  -0.0415 -0.0499 124 ASP   A CB   
769  C  CG   . ASP   A 124 ? 0.6707 0.8272 0.6481 0.0892  -0.0413 -0.0457 124 ASP   A CG   
770  O  OD1  . ASP   A 124 ? 0.6830 0.8476 0.6708 0.0866  -0.0400 -0.0457 124 ASP   A OD1  
771  O  OD2  . ASP   A 124 ? 0.7103 0.8672 0.6843 0.0958  -0.0419 -0.0422 124 ASP   A OD2  
772  N  N    . MET   A 125 ? 0.5485 0.6642 0.5020 0.0904  -0.0334 -0.0455 125 MET   A N    
773  C  CA   . MET   A 125 ? 0.5374 0.6473 0.4895 0.0954  -0.0310 -0.0413 125 MET   A CA   
774  C  C    . MET   A 125 ? 0.5221 0.6213 0.4737 0.0936  -0.0279 -0.0410 125 MET   A C    
775  O  O    . MET   A 125 ? 0.5131 0.6096 0.4665 0.0967  -0.0264 -0.0375 125 MET   A O    
776  C  CB   . MET   A 125 ? 0.5475 0.6527 0.4920 0.0991  -0.0314 -0.0410 125 MET   A CB   
777  C  CG   . MET   A 125 ? 0.5702 0.6842 0.5139 0.1028  -0.0336 -0.0396 125 MET   A CG   
778  S  SD   . MET   A 125 ? 0.5995 0.7076 0.5343 0.1076  -0.0323 -0.0385 125 MET   A SD   
779  C  CE   . MET   A 125 ? 0.6062 0.7245 0.5387 0.1117  -0.0351 -0.0368 125 MET   A CE   
780  N  N    . MET   A 126 ? 0.5151 0.6070 0.4629 0.0886  -0.0271 -0.0448 126 MET   A N    
781  C  CA   . MET   A 126 ? 0.5212 0.6011 0.4661 0.0865  -0.0242 -0.0451 126 MET   A CA   
782  C  C    . MET   A 126 ? 0.5022 0.5853 0.4535 0.0849  -0.0218 -0.0435 126 MET   A C    
783  O  O    . MET   A 126 ? 0.5093 0.5843 0.4589 0.0867  -0.0197 -0.0413 126 MET   A O    
784  C  CB   . MET   A 126 ? 0.5577 0.6274 0.4948 0.0817  -0.0239 -0.0496 126 MET   A CB   
785  C  CG   . MET   A 126 ? 0.6361 0.6966 0.5643 0.0849  -0.0249 -0.0505 126 MET   A CG   
786  S  SD   . MET   A 126 ? 0.7600 0.8136 0.6874 0.0914  -0.0240 -0.0464 126 MET   A SD   
787  C  CE   . MET   A 126 ? 0.6125 0.6539 0.5374 0.0881  -0.0214 -0.0465 126 MET   A CE   
788  N  N    . PHE   A 127 ? 0.4846 0.5802 0.4436 0.0822  -0.0223 -0.0445 127 PHE   A N    
789  C  CA   . PHE   A 127 ? 0.4780 0.5798 0.4449 0.0813  -0.0194 -0.0429 127 PHE   A CA   
790  C  C    . PHE   A 127 ? 0.4694 0.5738 0.4387 0.0879  -0.0191 -0.0383 127 PHE   A C    
791  O  O    . PHE   A 127 ? 0.4715 0.5696 0.4404 0.0889  -0.0157 -0.0362 127 PHE   A O    
792  C  CB   . PHE   A 127 ? 0.4739 0.5913 0.4503 0.0776  -0.0210 -0.0450 127 PHE   A CB   
793  C  CG   . PHE   A 127 ? 0.4764 0.5999 0.4618 0.0754  -0.0168 -0.0441 127 PHE   A CG   
794  C  CD1  . PHE   A 127 ? 0.4881 0.6026 0.4716 0.0696  -0.0121 -0.0459 127 PHE   A CD1  
795  C  CD2  . PHE   A 127 ? 0.4701 0.6077 0.4652 0.0796  -0.0169 -0.0414 127 PHE   A CD2  
796  C  CE1  . PHE   A 127 ? 0.4912 0.6116 0.4831 0.0677  -0.0071 -0.0449 127 PHE   A CE1  
797  C  CE2  . PHE   A 127 ? 0.4728 0.6164 0.4765 0.0785  -0.0122 -0.0403 127 PHE   A CE2  
798  C  CZ   . PHE   A 127 ? 0.4778 0.6131 0.4802 0.0724  -0.0070 -0.0420 127 PHE   A CZ   
799  N  N    . GLN   A 128 ? 0.4529 0.5643 0.4231 0.0923  -0.0224 -0.0365 128 GLN   A N    
800  C  CA   . GLN   A 128 ? 0.4457 0.5589 0.4173 0.0981  -0.0223 -0.0320 128 GLN   A CA   
801  C  C    . GLN   A 128 ? 0.4650 0.5641 0.4303 0.1000  -0.0211 -0.0299 128 GLN   A C    
802  O  O    . GLN   A 128 ? 0.4632 0.5590 0.4288 0.1029  -0.0198 -0.0267 128 GLN   A O    
803  C  CB   . GLN   A 128 ? 0.4431 0.5651 0.4152 0.1019  -0.0258 -0.0307 128 GLN   A CB   
804  C  CG   . GLN   A 128 ? 0.4205 0.5570 0.3983 0.1012  -0.0285 -0.0324 128 GLN   A CG   
805  C  CD   . GLN   A 128 ? 0.4506 0.5916 0.4252 0.1059  -0.0316 -0.0306 128 GLN   A CD   
806  O  OE1  . GLN   A 128 ? 0.4552 0.5953 0.4290 0.1108  -0.0309 -0.0264 128 GLN   A OE1  
807  N  NE2  . GLN   A 128 ? 0.4343 0.5778 0.4053 0.1044  -0.0347 -0.0335 128 GLN   A NE2  
808  N  N    . LEU   A 129 ? 0.4720 0.5630 0.4316 0.0986  -0.0220 -0.0317 129 LEU   A N    
809  C  CA   . LEU   A 129 ? 0.4811 0.5596 0.4357 0.1000  -0.0218 -0.0303 129 LEU   A CA   
810  C  C    . LEU   A 129 ? 0.4794 0.5479 0.4312 0.0983  -0.0193 -0.0305 129 LEU   A C    
811  O  O    . LEU   A 129 ? 0.4815 0.5426 0.4311 0.1006  -0.0192 -0.0279 129 LEU   A O    
812  C  CB   . LEU   A 129 ? 0.4956 0.5680 0.4450 0.0990  -0.0229 -0.0330 129 LEU   A CB   
813  C  CG   . LEU   A 129 ? 0.5352 0.6023 0.4827 0.1023  -0.0242 -0.0310 129 LEU   A CG   
814  C  CD1  . LEU   A 129 ? 0.5523 0.6115 0.4938 0.1015  -0.0245 -0.0341 129 LEU   A CD1  
815  C  CD2  . LEU   A 129 ? 0.5439 0.6029 0.4911 0.1037  -0.0245 -0.0283 129 LEU   A CD2  
816  N  N    . LEU   A 130 ? 0.4740 0.5413 0.4250 0.0939  -0.0171 -0.0336 130 LEU   A N    
817  C  CA   . LEU   A 130 ? 0.4777 0.5348 0.4248 0.0918  -0.0135 -0.0341 130 LEU   A CA   
818  C  C    . LEU   A 130 ? 0.4848 0.5465 0.4364 0.0937  -0.0108 -0.0314 130 LEU   A C    
819  O  O    . LEU   A 130 ? 0.4954 0.5458 0.4416 0.0942  -0.0080 -0.0305 130 LEU   A O    
820  C  CB   . LEU   A 130 ? 0.4750 0.5298 0.4203 0.0859  -0.0114 -0.0380 130 LEU   A CB   
821  C  CG   . LEU   A 130 ? 0.4981 0.5410 0.4345 0.0844  -0.0129 -0.0407 130 LEU   A CG   
822  C  CD1  . LEU   A 130 ? 0.5052 0.5475 0.4403 0.0781  -0.0113 -0.0446 130 LEU   A CD1  
823  C  CD2  . LEU   A 130 ? 0.5025 0.5274 0.4291 0.0863  -0.0123 -0.0398 130 LEU   A CD2  
824  N  N    . ARG   A 131 ? 0.4816 0.5588 0.4419 0.0956  -0.0117 -0.0302 131 ARG   A N    
825  C  CA   . ARG   A 131 ? 0.4937 0.5764 0.4586 0.0989  -0.0092 -0.0274 131 ARG   A CA   
826  C  C    . ARG   A 131 ? 0.4910 0.5649 0.4506 0.1038  -0.0104 -0.0238 131 ARG   A C    
827  O  O    . ARG   A 131 ? 0.5063 0.5722 0.4622 0.1059  -0.0076 -0.0219 131 ARG   A O    
828  C  CB   . ARG   A 131 ? 0.5205 0.6220 0.4954 0.1002  -0.0107 -0.0271 131 ARG   A CB   
829  C  CG   . ARG   A 131 ? 0.5922 0.7046 0.5754 0.0957  -0.0086 -0.0298 131 ARG   A CG   
830  C  CD   . ARG   A 131 ? 0.6566 0.7861 0.6503 0.0991  -0.0088 -0.0282 131 ARG   A CD   
831  N  NE   . ARG   A 131 ? 0.7451 0.8832 0.7400 0.1026  -0.0142 -0.0273 131 ARG   A NE   
832  C  CZ   . ARG   A 131 ? 0.7796 0.9312 0.7814 0.1072  -0.0159 -0.0254 131 ARG   A CZ   
833  N  NH1  . ARG   A 131 ? 0.7734 0.9331 0.7830 0.1091  -0.0125 -0.0243 131 ARG   A NH1  
834  N  NH2  . ARG   A 131 ? 0.7771 0.9339 0.7774 0.1104  -0.0206 -0.0246 131 ARG   A NH2  
835  N  N    . GLY   A 132 ? 0.4668 0.5413 0.4255 0.1053  -0.0144 -0.0229 132 GLY   A N    
836  C  CA   . GLY   A 132 ? 0.4640 0.5308 0.4188 0.1087  -0.0162 -0.0196 132 GLY   A CA   
837  C  C    . GLY   A 132 ? 0.4679 0.5178 0.4145 0.1077  -0.0162 -0.0199 132 GLY   A C    
838  O  O    . GLY   A 132 ? 0.4653 0.5059 0.4073 0.1099  -0.0162 -0.0176 132 GLY   A O    
839  N  N    . LEU   A 133 ? 0.4639 0.5087 0.4075 0.1044  -0.0163 -0.0230 133 LEU   A N    
840  C  CA   . LEU   A 133 ? 0.4783 0.5067 0.4131 0.1037  -0.0169 -0.0237 133 LEU   A CA   
841  C  C    . LEU   A 133 ? 0.4652 0.4837 0.3939 0.1035  -0.0127 -0.0237 133 LEU   A C    
842  O  O    . LEU   A 133 ? 0.4699 0.4747 0.3906 0.1053  -0.0136 -0.0223 133 LEU   A O    
843  C  CB   . LEU   A 133 ? 0.5036 0.5286 0.4358 0.1011  -0.0180 -0.0269 133 LEU   A CB   
844  C  CG   . LEU   A 133 ? 0.5512 0.5656 0.4784 0.1025  -0.0220 -0.0266 133 LEU   A CG   
845  C  CD1  . LEU   A 133 ? 0.5598 0.5810 0.4932 0.1050  -0.0255 -0.0237 133 LEU   A CD1  
846  C  CD2  . LEU   A 133 ? 0.5680 0.5798 0.4925 0.1010  -0.0227 -0.0296 133 LEU   A CD2  
847  N  N    . ASP   A 134 ? 0.4492 0.4750 0.3818 0.1014  -0.0082 -0.0251 134 ASP   A N    
848  C  CA   . ASP   A 134 ? 0.4615 0.4798 0.3895 0.1013  -0.0028 -0.0248 134 ASP   A CA   
849  C  C    . ASP   A 134 ? 0.4819 0.4990 0.4091 0.1061  -0.0018 -0.0215 134 ASP   A C    
850  O  O    . ASP   A 134 ? 0.4886 0.4917 0.4065 0.1077  0.0012  -0.0206 134 ASP   A O    
851  C  CB   . ASP   A 134 ? 0.4684 0.4974 0.4035 0.0975  0.0020  -0.0268 134 ASP   A CB   
852  C  CG   . ASP   A 134 ? 0.5350 0.5563 0.4659 0.0977  0.0089  -0.0261 134 ASP   A CG   
853  O  OD1  . ASP   A 134 ? 0.5402 0.5422 0.4580 0.0983  0.0100  -0.0259 134 ASP   A OD1  
854  O  OD2  . ASP   A 134 ? 0.5747 0.6088 0.5147 0.0981  0.0130  -0.0253 134 ASP   A OD2  
855  N  N    . PHE   A 135 ? 0.4706 0.5004 0.4056 0.1087  -0.0042 -0.0196 135 PHE   A N    
856  C  CA   . PHE   A 135 ? 0.4761 0.5036 0.4092 0.1136  -0.0040 -0.0162 135 PHE   A CA   
857  C  C    . PHE   A 135 ? 0.5047 0.5140 0.4268 0.1148  -0.0074 -0.0150 135 PHE   A C    
858  O  O    . PHE   A 135 ? 0.5266 0.5235 0.4401 0.1176  -0.0054 -0.0135 135 PHE   A O    
859  C  CB   . PHE   A 135 ? 0.4460 0.4887 0.3878 0.1161  -0.0065 -0.0144 135 PHE   A CB   
860  C  CG   . PHE   A 135 ? 0.4473 0.4845 0.3850 0.1211  -0.0070 -0.0108 135 PHE   A CG   
861  C  CD1  . PHE   A 135 ? 0.4545 0.4892 0.3898 0.1250  -0.0023 -0.0093 135 PHE   A CD1  
862  C  CD2  . PHE   A 135 ? 0.4468 0.4802 0.3825 0.1218  -0.0115 -0.0088 135 PHE   A CD2  
863  C  CE1  . PHE   A 135 ? 0.4605 0.4876 0.3899 0.1300  -0.0026 -0.0061 135 PHE   A CE1  
864  C  CE2  . PHE   A 135 ? 0.4570 0.4834 0.3877 0.1258  -0.0119 -0.0055 135 PHE   A CE2  
865  C  CZ   . PHE   A 135 ? 0.4603 0.4827 0.3870 0.1301  -0.0076 -0.0043 135 PHE   A CZ   
866  N  N    . LEU   A 136 ? 0.4975 0.5057 0.4201 0.1130  -0.0127 -0.0155 136 LEU   A N    
867  C  CA   . LEU   A 136 ? 0.4991 0.4925 0.4138 0.1134  -0.0172 -0.0145 136 LEU   A CA   
868  C  C    . LEU   A 136 ? 0.4988 0.4739 0.4012 0.1128  -0.0162 -0.0160 136 LEU   A C    
869  O  O    . LEU   A 136 ? 0.4969 0.4572 0.3894 0.1148  -0.0173 -0.0147 136 LEU   A O    
870  C  CB   . LEU   A 136 ? 0.4982 0.4975 0.4187 0.1115  -0.0222 -0.0151 136 LEU   A CB   
871  C  CG   . LEU   A 136 ? 0.5065 0.5106 0.4320 0.1125  -0.0258 -0.0122 136 LEU   A CG   
872  C  CD1  . LEU   A 136 ? 0.5088 0.5192 0.4365 0.1153  -0.0233 -0.0095 136 LEU   A CD1  
873  C  CD2  . LEU   A 136 ? 0.4932 0.5084 0.4269 0.1110  -0.0281 -0.0128 136 LEU   A CD2  
874  N  N    . HIS   A 137 ? 0.4996 0.4745 0.4012 0.1102  -0.0139 -0.0188 137 HIS   A N    
875  C  CA   . HIS   A 137 ? 0.5177 0.4745 0.4064 0.1096  -0.0124 -0.0203 137 HIS   A CA   
876  C  C    . HIS   A 137 ? 0.5319 0.4792 0.4123 0.1116  -0.0063 -0.0193 137 HIS   A C    
877  O  O    . HIS   A 137 ? 0.5356 0.4633 0.4017 0.1129  -0.0065 -0.0194 137 HIS   A O    
878  C  CB   . HIS   A 137 ? 0.5146 0.4731 0.4040 0.1060  -0.0107 -0.0234 137 HIS   A CB   
879  C  CG   . HIS   A 137 ? 0.5315 0.4928 0.4242 0.1051  -0.0168 -0.0245 137 HIS   A CG   
880  N  ND1  . HIS   A 137 ? 0.5438 0.5083 0.4380 0.1024  -0.0160 -0.0272 137 HIS   A ND1  
881  C  CD2  . HIS   A 137 ? 0.5363 0.4983 0.4316 0.1067  -0.0231 -0.0232 137 HIS   A CD2  
882  C  CE1  . HIS   A 137 ? 0.5390 0.5059 0.4362 0.1033  -0.0216 -0.0274 137 HIS   A CE1  
883  N  NE2  . HIS   A 137 ? 0.5350 0.5014 0.4340 0.1057  -0.0258 -0.0249 137 HIS   A NE2  
884  N  N    . SER   A 138 ? 0.5277 0.4888 0.4168 0.1126  -0.0010 -0.0183 138 SER   A N    
885  C  CA   . SER   A 138 ? 0.5441 0.4995 0.4279 0.1154  0.0059  -0.0170 138 SER   A CA   
886  C  C    . SER   A 138 ? 0.5622 0.5047 0.4363 0.1201  0.0037  -0.0145 138 SER   A C    
887  O  O    . SER   A 138 ? 0.5864 0.5157 0.4496 0.1231  0.0085  -0.0136 138 SER   A O    
888  C  CB   . SER   A 138 ? 0.5471 0.5235 0.4453 0.1154  0.0111  -0.0167 138 SER   A CB   
889  O  OG   . SER   A 138 ? 0.5946 0.5835 0.5013 0.1182  0.0076  -0.0147 138 SER   A OG   
890  N  N    . HIS   A 139 ? 0.5609 0.5060 0.4382 0.1205  -0.0033 -0.0133 139 HIS   A N    
891  C  CA   . HIS   A 139 ? 0.5679 0.5006 0.4366 0.1238  -0.0067 -0.0110 139 HIS   A CA   
892  C  C    . HIS   A 139 ? 0.6089 0.5259 0.4686 0.1219  -0.0145 -0.0118 139 HIS   A C    
893  O  O    . HIS   A 139 ? 0.6258 0.5362 0.4823 0.1225  -0.0199 -0.0102 139 HIS   A O    
894  C  CB   . HIS   A 139 ? 0.5414 0.4886 0.4206 0.1254  -0.0084 -0.0087 139 HIS   A CB   
895  C  CG   . HIS   A 139 ? 0.5529 0.5134 0.4393 0.1286  -0.0016 -0.0077 139 HIS   A CG   
896  N  ND1  . HIS   A 139 ? 0.5665 0.5182 0.4448 0.1338  0.0031  -0.0058 139 HIS   A ND1  
897  C  CD2  . HIS   A 139 ? 0.5425 0.5239 0.4429 0.1274  0.0009  -0.0085 139 HIS   A CD2  
898  C  CE1  . HIS   A 139 ? 0.5583 0.5275 0.4476 0.1359  0.0084  -0.0054 139 HIS   A CE1  
899  N  NE2  . HIS   A 139 ? 0.5506 0.5380 0.4535 0.1318  0.0069  -0.0071 139 HIS   A NE2  
900  N  N    . ARG   A 140 ? 0.6300 0.5409 0.4855 0.1195  -0.0151 -0.0142 140 ARG   A N    
901  C  CA   . ARG   A 140 ? 0.6689 0.5657 0.5160 0.1181  -0.0224 -0.0155 140 ARG   A CA   
902  C  C    . ARG   A 140 ? 0.6588 0.5635 0.5155 0.1165  -0.0306 -0.0146 140 ARG   A C    
903  O  O    . ARG   A 140 ? 0.6755 0.5678 0.5255 0.1163  -0.0376 -0.0142 140 ARG   A O    
904  C  CB   . ARG   A 140 ? 0.7254 0.5962 0.5520 0.1206  -0.0230 -0.0154 140 ARG   A CB   
905  C  CG   . ARG   A 140 ? 0.8095 0.6684 0.6243 0.1211  -0.0165 -0.0170 140 ARG   A CG   
906  C  CD   . ARG   A 140 ? 0.9049 0.7364 0.6972 0.1243  -0.0170 -0.0168 140 ARG   A CD   
907  N  NE   . ARG   A 140 ? 0.9831 0.8106 0.7706 0.1280  -0.0120 -0.0147 140 ARG   A NE   
908  C  CZ   . ARG   A 140 ? 1.0354 0.8406 0.8047 0.1312  -0.0139 -0.0140 140 ARG   A CZ   
909  N  NH1  . ARG   A 140 ? 1.0334 0.8183 0.7876 0.1309  -0.0216 -0.0153 140 ARG   A NH1  
910  N  NH2  . ARG   A 140 ? 1.0265 0.8287 0.7916 0.1352  -0.0086 -0.0120 140 ARG   A NH2  
911  N  N    . VAL   A 141 ? 0.6261 0.5515 0.4984 0.1151  -0.0298 -0.0142 141 VAL   A N    
912  C  CA   . VAL   A 141 ? 0.5986 0.5340 0.4816 0.1134  -0.0357 -0.0133 141 VAL   A CA   
913  C  C    . VAL   A 141 ? 0.5708 0.5145 0.4601 0.1115  -0.0365 -0.0157 141 VAL   A C    
914  O  O    . VAL   A 141 ? 0.5560 0.5072 0.4479 0.1110  -0.0312 -0.0172 141 VAL   A O    
915  C  CB   . VAL   A 141 ? 0.5930 0.5437 0.4867 0.1140  -0.0338 -0.0108 141 VAL   A CB   
916  C  CG1  . VAL   A 141 ? 0.5840 0.5462 0.4893 0.1120  -0.0383 -0.0097 141 VAL   A CG1  
917  C  CG2  . VAL   A 141 ? 0.6068 0.5467 0.4923 0.1163  -0.0333 -0.0084 141 VAL   A CG2  
918  N  N    . VAL   A 142 ? 0.5648 0.5060 0.4558 0.1107  -0.0430 -0.0160 142 VAL   A N    
919  C  CA   . VAL   A 142 ? 0.5475 0.4954 0.4438 0.1099  -0.0443 -0.0181 142 VAL   A CA   
920  C  C    . VAL   A 142 ? 0.5246 0.4885 0.4354 0.1092  -0.0469 -0.0164 142 VAL   A C    
921  O  O    . VAL   A 142 ? 0.5323 0.4947 0.4460 0.1087  -0.0516 -0.0144 142 VAL   A O    
922  C  CB   . VAL   A 142 ? 0.5563 0.4884 0.4427 0.1106  -0.0496 -0.0199 142 VAL   A CB   
923  C  CG1  . VAL   A 142 ? 0.5650 0.5018 0.4539 0.1106  -0.0489 -0.0223 142 VAL   A CG1  
924  C  CG2  . VAL   A 142 ? 0.5611 0.4731 0.4302 0.1117  -0.0478 -0.0207 142 VAL   A CG2  
925  N  N    . HIS   A 143 ? 0.5019 0.4805 0.4212 0.1088  -0.0435 -0.0171 143 HIS   A N    
926  C  CA   . HIS   A 143 ? 0.4875 0.4809 0.4194 0.1086  -0.0447 -0.0154 143 HIS   A CA   
927  C  C    . HIS   A 143 ? 0.5010 0.4935 0.4373 0.1088  -0.0506 -0.0153 143 HIS   A C    
928  O  O    . HIS   A 143 ? 0.5014 0.4977 0.4449 0.1079  -0.0538 -0.0128 143 HIS   A O    
929  C  CB   . HIS   A 143 ? 0.4691 0.4762 0.4066 0.1087  -0.0400 -0.0166 143 HIS   A CB   
930  C  CG   . HIS   A 143 ? 0.4539 0.4753 0.4022 0.1089  -0.0398 -0.0144 143 HIS   A CG   
931  N  ND1  . HIS   A 143 ? 0.4631 0.4877 0.4184 0.1090  -0.0433 -0.0129 143 HIS   A ND1  
932  C  CD2  . HIS   A 143 ? 0.4545 0.4873 0.4070 0.1093  -0.0363 -0.0134 143 HIS   A CD2  
933  C  CE1  . HIS   A 143 ? 0.4560 0.4930 0.4190 0.1093  -0.0409 -0.0109 143 HIS   A CE1  
934  N  NE2  . HIS   A 143 ? 0.4645 0.5061 0.4253 0.1096  -0.0370 -0.0111 143 HIS   A NE2  
935  N  N    . ARG   A 144 ? 0.5101 0.4975 0.4424 0.1099  -0.0520 -0.0180 144 ARG   A N    
936  C  CA   . ARG   A 144 ? 0.5221 0.5081 0.4579 0.1112  -0.0579 -0.0184 144 ARG   A CA   
937  C  C    . ARG   A 144 ? 0.5059 0.5081 0.4551 0.1122  -0.0573 -0.0176 144 ARG   A C    
938  O  O    . ARG   A 144 ? 0.5039 0.5061 0.4557 0.1144  -0.0608 -0.0185 144 ARG   A O    
939  C  CB   . ARG   A 144 ? 0.5693 0.5470 0.5045 0.1104  -0.0649 -0.0168 144 ARG   A CB   
940  C  CG   . ARG   A 144 ? 0.6454 0.6045 0.5652 0.1101  -0.0659 -0.0174 144 ARG   A CG   
941  C  CD   . ARG   A 144 ? 0.7226 0.6708 0.6395 0.1096  -0.0745 -0.0166 144 ARG   A CD   
942  N  NE   . ARG   A 144 ? 0.8051 0.7336 0.7049 0.1098  -0.0749 -0.0173 144 ARG   A NE   
943  C  CZ   . ARG   A 144 ? 0.8599 0.7734 0.7448 0.1118  -0.0741 -0.0197 144 ARG   A CZ   
944  N  NH1  . ARG   A 144 ? 0.8525 0.7679 0.7374 0.1136  -0.0732 -0.0217 144 ARG   A NH1  
945  N  NH2  . ARG   A 144 ? 0.8703 0.7657 0.7392 0.1124  -0.0735 -0.0199 144 ARG   A NH2  
946  N  N    . ASP   A 145 ? 0.5006 0.5157 0.4573 0.1114  -0.0528 -0.0159 145 ASP   A N    
947  C  CA   . ASP   A 145 ? 0.5025 0.5317 0.4702 0.1128  -0.0512 -0.0151 145 ASP   A CA   
948  C  C    . ASP   A 145 ? 0.4861 0.5241 0.4537 0.1129  -0.0449 -0.0155 145 ASP   A C    
949  O  O    . ASP   A 145 ? 0.4753 0.5246 0.4509 0.1129  -0.0425 -0.0131 145 ASP   A O    
950  C  CB   . ASP   A 145 ? 0.5503 0.5875 0.5306 0.1117  -0.0542 -0.0115 145 ASP   A CB   
951  C  CG   . ASP   A 145 ? 0.6492 0.7000 0.6415 0.1140  -0.0527 -0.0106 145 ASP   A CG   
952  O  OD1  . ASP   A 145 ? 0.6602 0.7118 0.6496 0.1171  -0.0509 -0.0131 145 ASP   A OD1  
953  O  OD2  . ASP   A 145 ? 0.6713 0.7315 0.6756 0.1126  -0.0531 -0.0073 145 ASP   A OD2  
954  N  N    . LEU   A 146 ? 0.4872 0.5197 0.4456 0.1128  -0.0424 -0.0186 146 LEU   A N    
955  C  CA   . LEU   A 146 ? 0.4926 0.5323 0.4498 0.1126  -0.0377 -0.0198 146 LEU   A CA   
956  C  C    . LEU   A 146 ? 0.4846 0.5309 0.4448 0.1149  -0.0363 -0.0209 146 LEU   A C    
957  O  O    . LEU   A 146 ? 0.4928 0.5333 0.4497 0.1166  -0.0377 -0.0230 146 LEU   A O    
958  C  CB   . LEU   A 146 ? 0.5134 0.5442 0.4606 0.1109  -0.0361 -0.0230 146 LEU   A CB   
959  C  CG   . LEU   A 146 ? 0.5415 0.5765 0.4874 0.1090  -0.0326 -0.0233 146 LEU   A CG   
960  C  CD1  . LEU   A 146 ? 0.5466 0.5807 0.4875 0.1075  -0.0302 -0.0269 146 LEU   A CD1  
961  C  CD2  . LEU   A 146 ? 0.5385 0.5861 0.4915 0.1097  -0.0314 -0.0205 146 LEU   A CD2  
962  N  N    . LYS   A 147 ? 0.4716 0.5291 0.4368 0.1156  -0.0334 -0.0194 147 LYS   A N    
963  C  CA   . LYS   A 147 ? 0.4690 0.5329 0.4361 0.1184  -0.0310 -0.0200 147 LYS   A CA   
964  C  C    . LYS   A 147 ? 0.4679 0.5406 0.4351 0.1184  -0.0275 -0.0191 147 LYS   A C    
965  O  O    . LYS   A 147 ? 0.4643 0.5399 0.4334 0.1168  -0.0273 -0.0168 147 LYS   A O    
966  C  CB   . LYS   A 147 ? 0.4881 0.5570 0.4650 0.1208  -0.0322 -0.0174 147 LYS   A CB   
967  C  CG   . LYS   A 147 ? 0.5204 0.5963 0.5069 0.1193  -0.0325 -0.0128 147 LYS   A CG   
968  C  CD   . LYS   A 147 ? 0.5535 0.6330 0.5506 0.1205  -0.0350 -0.0108 147 LYS   A CD   
969  C  CE   . LYS   A 147 ? 0.5897 0.6747 0.5963 0.1177  -0.0355 -0.0064 147 LYS   A CE   
970  N  NZ   . LYS   A 147 ? 0.6168 0.7073 0.6361 0.1180  -0.0383 -0.0043 147 LYS   A NZ   
971  N  N    . PRO   A 148 ? 0.4719 0.5477 0.4356 0.1205  -0.0249 -0.0209 148 PRO   A N    
972  C  CA   . PRO   A 148 ? 0.4726 0.5556 0.4345 0.1209  -0.0222 -0.0203 148 PRO   A CA   
973  C  C    . PRO   A 148 ? 0.4765 0.5671 0.4453 0.1216  -0.0206 -0.0154 148 PRO   A C    
974  O  O    . PRO   A 148 ? 0.4871 0.5817 0.4535 0.1216  -0.0194 -0.0143 148 PRO   A O    
975  C  CB   . PRO   A 148 ? 0.4833 0.5660 0.4397 0.1239  -0.0200 -0.0228 148 PRO   A CB   
976  C  CG   . PRO   A 148 ? 0.4945 0.5672 0.4461 0.1235  -0.0219 -0.0265 148 PRO   A CG   
977  C  CD   . PRO   A 148 ? 0.4677 0.5393 0.4272 0.1232  -0.0244 -0.0239 148 PRO   A CD   
978  N  N    . GLN   A 149 ? 0.4742 0.5666 0.4517 0.1220  -0.0209 -0.0123 149 GLN   A N    
979  C  CA   . GLN   A 149 ? 0.4748 0.5733 0.4596 0.1218  -0.0191 -0.0074 149 GLN   A CA   
980  C  C    . GLN   A 149 ? 0.4629 0.5588 0.4475 0.1190  -0.0210 -0.0053 149 GLN   A C    
981  O  O    . GLN   A 149 ? 0.4641 0.5638 0.4508 0.1189  -0.0189 -0.0016 149 GLN   A O    
982  C  CB   . GLN   A 149 ? 0.5059 0.6078 0.5017 0.1223  -0.0194 -0.0050 149 GLN   A CB   
983  C  CG   . GLN   A 149 ? 0.5579 0.6657 0.5563 0.1264  -0.0153 -0.0050 149 GLN   A CG   
984  C  CD   . GLN   A 149 ? 0.6124 0.7150 0.6046 0.1291  -0.0164 -0.0096 149 GLN   A CD   
985  O  OE1  . GLN   A 149 ? 0.6760 0.7800 0.6635 0.1327  -0.0128 -0.0111 149 GLN   A OE1  
986  N  NE2  . GLN   A 149 ? 0.5690 0.6638 0.5593 0.1275  -0.0213 -0.0121 149 GLN   A NE2  
987  N  N    . ASN   A 150 ? 0.4540 0.5426 0.4352 0.1170  -0.0245 -0.0075 150 ASN   A N    
988  C  CA   . ASN   A 150 ? 0.4427 0.5276 0.4225 0.1151  -0.0259 -0.0056 150 ASN   A CA   
989  C  C    . ASN   A 150 ? 0.4404 0.5238 0.4130 0.1150  -0.0258 -0.0082 150 ASN   A C    
990  O  O    . ASN   A 150 ? 0.4527 0.5318 0.4232 0.1141  -0.0268 -0.0074 150 ASN   A O    
991  C  CB   . ASN   A 150 ? 0.4376 0.5150 0.4202 0.1130  -0.0296 -0.0048 150 ASN   A CB   
992  C  CG   . ASN   A 150 ? 0.4455 0.5157 0.4249 0.1129  -0.0324 -0.0084 150 ASN   A CG   
993  O  OD1  . ASN   A 150 ? 0.4503 0.5179 0.4232 0.1132  -0.0317 -0.0119 150 ASN   A OD1  
994  N  ND2  . ASN   A 150 ? 0.4453 0.5118 0.4291 0.1122  -0.0359 -0.0077 150 ASN   A ND2  
995  N  N    . ILE   A 151 ? 0.4326 0.5189 0.4015 0.1159  -0.0246 -0.0115 151 ILE   A N    
996  C  CA   . ILE   A 151 ? 0.4403 0.5279 0.4043 0.1153  -0.0246 -0.0140 151 ILE   A CA   
997  C  C    . ILE   A 151 ? 0.4394 0.5351 0.4026 0.1176  -0.0229 -0.0123 151 ILE   A C    
998  O  O    . ILE   A 151 ? 0.4449 0.5436 0.4061 0.1191  -0.0215 -0.0132 151 ILE   A O    
999  C  CB   . ILE   A 151 ? 0.4534 0.5379 0.4131 0.1140  -0.0250 -0.0189 151 ILE   A CB   
1000 C  CG1  . ILE   A 151 ? 0.4648 0.5394 0.4233 0.1122  -0.0265 -0.0204 151 ILE   A CG1  
1001 C  CG2  . ILE   A 151 ? 0.4643 0.5530 0.4211 0.1127  -0.0250 -0.0213 151 ILE   A CG2  
1002 C  CD1  . ILE   A 151 ? 0.4872 0.5565 0.4408 0.1114  -0.0265 -0.0245 151 ILE   A CD1  
1003 N  N    . LEU   A 152 ? 0.4312 0.5291 0.3946 0.1185  -0.0228 -0.0094 152 LEU   A N    
1004 C  CA   . LEU   A 152 ? 0.4353 0.5392 0.3962 0.1212  -0.0214 -0.0073 152 LEU   A CA   
1005 C  C    . LEU   A 152 ? 0.4446 0.5535 0.4016 0.1219  -0.0228 -0.0101 152 LEU   A C    
1006 O  O    . LEU   A 152 ? 0.4444 0.5533 0.4025 0.1202  -0.0244 -0.0124 152 LEU   A O    
1007 C  CB   . LEU   A 152 ? 0.4375 0.5401 0.3997 0.1224  -0.0205 -0.0022 152 LEU   A CB   
1008 C  CG   . LEU   A 152 ? 0.4483 0.5456 0.4156 0.1204  -0.0202 0.0005  152 LEU   A CG   
1009 C  CD1  . LEU   A 152 ? 0.4536 0.5474 0.4204 0.1207  -0.0199 0.0047  152 LEU   A CD1  
1010 C  CD2  . LEU   A 152 ? 0.4540 0.5541 0.4249 0.1206  -0.0179 0.0015  152 LEU   A CD2  
1011 N  N    . VAL   A 153 ? 0.4535 0.5667 0.4060 0.1242  -0.0223 -0.0104 153 VAL   A N    
1012 C  CA   . VAL   A 153 ? 0.4823 0.6008 0.4305 0.1248  -0.0247 -0.0135 153 VAL   A CA   
1013 C  C    . VAL   A 153 ? 0.4977 0.6204 0.4422 0.1289  -0.0250 -0.0101 153 VAL   A C    
1014 O  O    . VAL   A 153 ? 0.5000 0.6211 0.4407 0.1316  -0.0224 -0.0068 153 VAL   A O    
1015 C  CB   . VAL   A 153 ? 0.4999 0.6175 0.4429 0.1239  -0.0251 -0.0178 153 VAL   A CB   
1016 C  CG1  . VAL   A 153 ? 0.5060 0.6285 0.4456 0.1230  -0.0288 -0.0217 153 VAL   A CG1  
1017 C  CG2  . VAL   A 153 ? 0.5012 0.6128 0.4466 0.1208  -0.0244 -0.0204 153 VAL   A CG2  
1018 N  N    . THR   A 154 ? 0.4995 0.6270 0.4453 0.1296  -0.0278 -0.0106 154 THR   A N    
1019 C  CA   . THR   A 154 ? 0.5165 0.6473 0.4585 0.1343  -0.0287 -0.0074 154 THR   A CA   
1020 C  C    . THR   A 154 ? 0.5243 0.6589 0.4583 0.1367  -0.0311 -0.0092 154 THR   A C    
1021 O  O    . THR   A 154 ? 0.5098 0.6456 0.4426 0.1341  -0.0329 -0.0138 154 THR   A O    
1022 C  CB   . THR   A 154 ? 0.5491 0.6836 0.4964 0.1350  -0.0305 -0.0068 154 THR   A CB   
1023 O  OG1  . THR   A 154 ? 0.6001 0.7304 0.5457 0.1384  -0.0287 -0.0017 154 THR   A OG1  
1024 C  CG2  . THR   A 154 ? 0.5302 0.6743 0.4783 0.1361  -0.0348 -0.0097 154 THR   A CG2  
1025 N  N    . SER   A 155 ? 0.5451 0.6802 0.4725 0.1418  -0.0314 -0.0057 155 SER   A N    
1026 C  CA   . SER   A 155 ? 0.5732 0.7105 0.4905 0.1452  -0.0342 -0.0070 155 SER   A CA   
1027 C  C    . SER   A 155 ? 0.5975 0.7432 0.5173 0.1437  -0.0406 -0.0121 155 SER   A C    
1028 O  O    . SER   A 155 ? 0.6198 0.7666 0.5319 0.1444  -0.0440 -0.0151 155 SER   A O    
1029 C  CB   . SER   A 155 ? 0.5827 0.7177 0.4920 0.1513  -0.0336 -0.0019 155 SER   A CB   
1030 O  OG   . SER   A 155 ? 0.5983 0.7370 0.5118 0.1538  -0.0358 0.0002  155 SER   A OG   
1031 N  N    . SER   A 156 ? 0.5923 0.7437 0.5231 0.1413  -0.0420 -0.0131 156 SER   A N    
1032 C  CA   . SER   A 156 ? 0.5952 0.7564 0.5326 0.1386  -0.0472 -0.0176 156 SER   A CA   
1033 C  C    . SER   A 156 ? 0.5815 0.7416 0.5248 0.1314  -0.0463 -0.0222 156 SER   A C    
1034 O  O    . SER   A 156 ? 0.5797 0.7476 0.5296 0.1279  -0.0497 -0.0259 156 SER   A O    
1035 C  CB   . SER   A 156 ? 0.6292 0.7975 0.5751 0.1412  -0.0480 -0.0152 156 SER   A CB   
1036 O  OG   . SER   A 156 ? 0.6924 0.8554 0.6336 0.1468  -0.0453 -0.0096 156 SER   A OG   
1037 N  N    . GLY   A 157 ? 0.5667 0.7173 0.5077 0.1293  -0.0418 -0.0218 157 GLY   A N    
1038 C  CA   . GLY   A 157 ? 0.5577 0.7045 0.5020 0.1233  -0.0407 -0.0258 157 GLY   A CA   
1039 C  C    . GLY   A 157 ? 0.5388 0.6848 0.4923 0.1205  -0.0383 -0.0252 157 GLY   A C    
1040 O  O    . GLY   A 157 ? 0.5392 0.6831 0.4955 0.1154  -0.0379 -0.0287 157 GLY   A O    
1041 N  N    . GLN   A 158 ? 0.5180 0.6644 0.4748 0.1238  -0.0365 -0.0207 158 GLN   A N    
1042 C  CA   . GLN   A 158 ? 0.5114 0.6548 0.4745 0.1221  -0.0340 -0.0197 158 GLN   A CA   
1043 C  C    . GLN   A 158 ? 0.4937 0.6259 0.4548 0.1207  -0.0307 -0.0183 158 GLN   A C    
1044 O  O    . GLN   A 158 ? 0.4900 0.6180 0.4476 0.1233  -0.0293 -0.0150 158 GLN   A O    
1045 C  CB   . GLN   A 158 ? 0.5469 0.6940 0.5130 0.1266  -0.0337 -0.0158 158 GLN   A CB   
1046 C  CG   . GLN   A 158 ? 0.6496 0.8070 0.6236 0.1261  -0.0352 -0.0177 158 GLN   A CG   
1047 C  CD   . GLN   A 158 ? 0.7645 0.9187 0.7427 0.1270  -0.0318 -0.0155 158 GLN   A CD   
1048 O  OE1  . GLN   A 158 ? 0.7932 0.9502 0.7775 0.1237  -0.0304 -0.0178 158 GLN   A OE1  
1049 N  NE2  . GLN   A 158 ? 0.7888 0.9360 0.7629 0.1314  -0.0301 -0.0110 158 GLN   A NE2  
1050 N  N    . ILE   A 159 ? 0.4862 0.6134 0.4497 0.1166  -0.0294 -0.0207 159 ILE   A N    
1051 C  CA   . ILE   A 159 ? 0.4863 0.6030 0.4484 0.1152  -0.0274 -0.0200 159 ILE   A CA   
1052 C  C    . ILE   A 159 ? 0.4879 0.5997 0.4515 0.1170  -0.0260 -0.0161 159 ILE   A C    
1053 O  O    . ILE   A 159 ? 0.4869 0.5999 0.4530 0.1171  -0.0254 -0.0160 159 ILE   A O    
1054 C  CB   . ILE   A 159 ? 0.4924 0.6042 0.4541 0.1104  -0.0270 -0.0243 159 ILE   A CB   
1055 C  CG1  . ILE   A 159 ? 0.5054 0.6185 0.4631 0.1087  -0.0284 -0.0281 159 ILE   A CG1  
1056 C  CG2  . ILE   A 159 ? 0.5076 0.6078 0.4679 0.1095  -0.0255 -0.0235 159 ILE   A CG2  
1057 C  CD1  . ILE   A 159 ? 0.5189 0.6279 0.4718 0.1110  -0.0279 -0.0274 159 ILE   A CD1  
1058 N  N    . LYS   A 160 ? 0.4858 0.5921 0.4480 0.1184  -0.0253 -0.0130 160 LYS   A N    
1059 C  CA   . LYS   A 160 ? 0.4869 0.5863 0.4492 0.1194  -0.0245 -0.0095 160 LYS   A CA   
1060 C  C    . LYS   A 160 ? 0.4735 0.5639 0.4357 0.1174  -0.0246 -0.0090 160 LYS   A C    
1061 O  O    . LYS   A 160 ? 0.4748 0.5659 0.4378 0.1174  -0.0245 -0.0082 160 LYS   A O    
1062 C  CB   . LYS   A 160 ? 0.5291 0.6309 0.4901 0.1233  -0.0242 -0.0052 160 LYS   A CB   
1063 C  CG   . LYS   A 160 ? 0.5632 0.6716 0.5247 0.1262  -0.0246 -0.0051 160 LYS   A CG   
1064 C  CD   . LYS   A 160 ? 0.6140 0.7243 0.5725 0.1307  -0.0246 -0.0011 160 LYS   A CD   
1065 C  CE   . LYS   A 160 ? 0.6678 0.7849 0.6274 0.1345  -0.0254 -0.0010 160 LYS   A CE   
1066 N  NZ   . LYS   A 160 ? 0.7030 0.8127 0.6614 0.1367  -0.0238 0.0015  160 LYS   A NZ   
1067 N  N    . LEU   A 161 ? 0.4624 0.5441 0.4234 0.1160  -0.0248 -0.0095 161 LEU   A N    
1068 C  CA   . LEU   A 161 ? 0.4523 0.5245 0.4127 0.1143  -0.0261 -0.0091 161 LEU   A CA   
1069 C  C    . LEU   A 161 ? 0.4502 0.5187 0.4113 0.1151  -0.0267 -0.0049 161 LEU   A C    
1070 O  O    . LEU   A 161 ? 0.4578 0.5239 0.4166 0.1167  -0.0262 -0.0026 161 LEU   A O    
1071 C  CB   . LEU   A 161 ? 0.4421 0.5045 0.3987 0.1128  -0.0263 -0.0112 161 LEU   A CB   
1072 C  CG   . LEU   A 161 ? 0.4626 0.5261 0.4178 0.1109  -0.0251 -0.0153 161 LEU   A CG   
1073 C  CD1  . LEU   A 161 ? 0.4733 0.5244 0.4231 0.1096  -0.0247 -0.0166 161 LEU   A CD1  
1074 C  CD2  . LEU   A 161 ? 0.4816 0.5480 0.4377 0.1098  -0.0258 -0.0177 161 LEU   A CD2  
1075 N  N    . ALA   A 162 ? 0.4459 0.5137 0.4104 0.1140  -0.0278 -0.0037 162 ALA   A N    
1076 C  CA   . ALA   A 162 ? 0.4499 0.5145 0.4166 0.1134  -0.0287 0.0002  162 ALA   A CA   
1077 C  C    . ALA   A 162 ? 0.4625 0.5213 0.4323 0.1110  -0.0317 -0.0003 162 ALA   A C    
1078 O  O    . ALA   A 162 ? 0.4615 0.5195 0.4312 0.1107  -0.0328 -0.0036 162 ALA   A O    
1079 C  CB   . ALA   A 162 ? 0.4393 0.5128 0.4096 0.1145  -0.0263 0.0028  162 ALA   A CB   
1080 N  N    . ASP   A 163 ? 0.4669 0.5214 0.4393 0.1093  -0.0335 0.0030  163 ASP   A N    
1081 C  CA   . ASP   A 163 ? 0.4901 0.5412 0.4678 0.1067  -0.0373 0.0033  163 ASP   A CA   
1082 C  C    . ASP   A 163 ? 0.5074 0.5477 0.4799 0.1062  -0.0414 0.0002  163 ASP   A C    
1083 O  O    . ASP   A 163 ? 0.5177 0.5593 0.4933 0.1062  -0.0434 -0.0020 163 ASP   A O    
1084 C  CB   . ASP   A 163 ? 0.5006 0.5633 0.4876 0.1070  -0.0357 0.0035  163 ASP   A CB   
1085 C  CG   . ASP   A 163 ? 0.5703 0.6338 0.5665 0.1048  -0.0392 0.0046  163 ASP   A CG   
1086 O  OD1  . ASP   A 163 ? 0.5728 0.6292 0.5698 0.1019  -0.0428 0.0065  163 ASP   A OD1  
1087 O  OD2  . ASP   A 163 ? 0.6197 0.6908 0.6223 0.1061  -0.0386 0.0036  163 ASP   A OD2  
1088 N  N    . PHE   A 164 ? 0.5221 0.5510 0.4858 0.1062  -0.0424 0.0001  164 PHE   A N    
1089 C  CA   . PHE   A 164 ? 0.5469 0.5629 0.5023 0.1061  -0.0453 -0.0026 164 PHE   A CA   
1090 C  C    . PHE   A 164 ? 0.5922 0.5940 0.5395 0.1054  -0.0476 -0.0009 164 PHE   A C    
1091 O  O    . PHE   A 164 ? 0.5849 0.5873 0.5326 0.1052  -0.0462 0.0022  164 PHE   A O    
1092 C  CB   . PHE   A 164 ? 0.5421 0.5588 0.4918 0.1081  -0.0415 -0.0056 164 PHE   A CB   
1093 C  CG   . PHE   A 164 ? 0.5449 0.5642 0.4914 0.1099  -0.0372 -0.0046 164 PHE   A CG   
1094 C  CD1  . PHE   A 164 ? 0.5624 0.5701 0.4999 0.1110  -0.0366 -0.0042 164 PHE   A CD1  
1095 C  CD2  . PHE   A 164 ? 0.5438 0.5766 0.4956 0.1111  -0.0339 -0.0040 164 PHE   A CD2  
1096 C  CE1  . PHE   A 164 ? 0.5653 0.5765 0.5010 0.1136  -0.0327 -0.0030 164 PHE   A CE1  
1097 C  CE2  . PHE   A 164 ? 0.5484 0.5843 0.4979 0.1134  -0.0308 -0.0029 164 PHE   A CE2  
1098 C  CZ   . PHE   A 164 ? 0.5514 0.5773 0.4937 0.1148  -0.0301 -0.0023 164 PHE   A CZ   
1099 N  N    . GLY   A 165 ? 0.6349 0.6224 0.5735 0.1052  -0.0512 -0.0028 165 GLY   A N    
1100 C  CA   . GLY   A 165 ? 0.6730 0.6440 0.6009 0.1049  -0.0537 -0.0018 165 GLY   A CA   
1101 C  C    . GLY   A 165 ? 0.7019 0.6674 0.6327 0.1014  -0.0599 0.0003  165 GLY   A C    
1102 O  O    . GLY   A 165 ? 0.7090 0.6595 0.6301 0.1008  -0.0624 0.0012  165 GLY   A O    
1103 N  N    . LEU   A 166 ? 0.7168 0.6943 0.6612 0.0990  -0.0622 0.0011  166 LEU   A N    
1104 C  CA   . LEU   A 166 ? 0.7461 0.7218 0.6971 0.0947  -0.0682 0.0031  166 LEU   A CA   
1105 C  C    . LEU   A 166 ? 0.7773 0.7539 0.7341 0.0936  -0.0750 0.0011  166 LEU   A C    
1106 O  O    . LEU   A 166 ? 0.7816 0.7610 0.7373 0.0965  -0.0740 -0.0016 166 LEU   A O    
1107 C  CB   . LEU   A 166 ? 0.7387 0.7288 0.7023 0.0927  -0.0645 0.0067  166 LEU   A CB   
1108 C  CG   . LEU   A 166 ? 0.7596 0.7427 0.7188 0.0908  -0.0631 0.0103  166 LEU   A CG   
1109 C  CD1  . LEU   A 166 ? 0.7789 0.7468 0.7212 0.0940  -0.0613 0.0096  166 LEU   A CD1  
1110 C  CD2  . LEU   A 166 ? 0.7573 0.7547 0.7248 0.0912  -0.0566 0.0133  166 LEU   A CD2  
1111 N  N    . ALA   A 167 ? 0.7978 0.7711 0.7600 0.0894  -0.0822 0.0023  167 ALA   A N    
1112 C  CA   . ALA   A 167 ? 0.8227 0.7977 0.7918 0.0886  -0.0899 0.0006  167 ALA   A CA   
1113 C  C    . ALA   A 167 ? 0.8348 0.8234 0.8231 0.0839  -0.0931 0.0034  167 ALA   A C    
1114 O  O    . ALA   A 167 ? 0.8383 0.8401 0.8369 0.0826  -0.0869 0.0062  167 ALA   A O    
1115 C  CB   . ALA   A 167 ? 0.8384 0.7921 0.7923 0.0883  -0.0978 -0.0016 167 ALA   A CB   
1116 N  N    . VAL   A 181 ? 0.6740 0.8087 0.7631 0.1298  -0.0504 0.0010  181 VAL   A N    
1117 C  CA   . VAL   A 181 ? 0.6878 0.8045 0.7578 0.1307  -0.0549 -0.0033 181 VAL   A CA   
1118 C  C    . VAL   A 181 ? 0.6877 0.7987 0.7437 0.1362  -0.0494 -0.0066 181 VAL   A C    
1119 O  O    . VAL   A 181 ? 0.6933 0.8132 0.7549 0.1415  -0.0447 -0.0062 181 VAL   A O    
1120 C  CB   . VAL   A 181 ? 0.6911 0.8026 0.7636 0.1320  -0.0649 -0.0048 181 VAL   A CB   
1121 N  N    . THR   A 182 ? 0.6752 0.7711 0.7130 0.1346  -0.0498 -0.0097 182 THR   A N    
1122 C  CA   . THR   A 182 ? 0.6542 0.7417 0.6766 0.1380  -0.0457 -0.0133 182 THR   A CA   
1123 C  C    . THR   A 182 ? 0.6289 0.6985 0.6359 0.1372  -0.0507 -0.0169 182 THR   A C    
1124 O  O    . THR   A 182 ? 0.6432 0.7045 0.6423 0.1325  -0.0518 -0.0173 182 THR   A O    
1125 C  CB   . THR   A 182 ? 0.6644 0.7556 0.6822 0.1363  -0.0383 -0.0128 182 THR   A CB   
1126 O  OG1  . THR   A 182 ? 0.6697 0.7748 0.6988 0.1394  -0.0330 -0.0101 182 THR   A OG1  
1127 C  CG2  . THR   A 182 ? 0.6681 0.7488 0.6690 0.1378  -0.0356 -0.0169 182 THR   A CG2  
1128 N  N    . LEU   A 183 ? 0.5840 0.6474 0.5862 0.1424  -0.0530 -0.0193 183 LEU   A N    
1129 C  CA   . LEU   A 183 ? 0.5547 0.6003 0.5416 0.1430  -0.0571 -0.0225 183 LEU   A CA   
1130 C  C    . LEU   A 183 ? 0.4989 0.5349 0.4702 0.1435  -0.0519 -0.0259 183 LEU   A C    
1131 O  O    . LEU   A 183 ? 0.4913 0.5115 0.4483 0.1429  -0.0536 -0.0286 183 LEU   A O    
1132 C  CB   . LEU   A 183 ? 0.5751 0.6189 0.5654 0.1489  -0.0631 -0.0229 183 LEU   A CB   
1133 C  CG   . LEU   A 183 ? 0.5950 0.6505 0.6037 0.1484  -0.0694 -0.0197 183 LEU   A CG   
1134 C  CD1  . LEU   A 183 ? 0.5978 0.6525 0.6100 0.1552  -0.0756 -0.0204 183 LEU   A CD1  
1135 C  CD2  . LEU   A 183 ? 0.6052 0.6532 0.6111 0.1420  -0.0748 -0.0189 183 LEU   A CD2  
1136 N  N    . TRP   A 184 ? 0.4633 0.5082 0.4366 0.1440  -0.0454 -0.0256 184 TRP   A N    
1137 C  CA   . TRP   A 184 ? 0.4630 0.4997 0.4220 0.1441  -0.0407 -0.0290 184 TRP   A CA   
1138 C  C    . TRP   A 184 ? 0.4515 0.4769 0.3985 0.1382  -0.0406 -0.0312 184 TRP   A C    
1139 O  O    . TRP   A 184 ? 0.4563 0.4711 0.3902 0.1378  -0.0386 -0.0346 184 TRP   A O    
1140 C  CB   . TRP   A 184 ? 0.4685 0.5172 0.4320 0.1452  -0.0345 -0.0281 184 TRP   A CB   
1141 C  CG   . TRP   A 184 ? 0.4692 0.5307 0.4455 0.1510  -0.0326 -0.0255 184 TRP   A CG   
1142 C  CD1  . TRP   A 184 ? 0.4749 0.5385 0.4588 0.1563  -0.0359 -0.0247 184 TRP   A CD1  
1143 C  CD2  . TRP   A 184 ? 0.4654 0.5400 0.4491 0.1523  -0.0266 -0.0231 184 TRP   A CD2  
1144 N  NE1  . TRP   A 184 ? 0.4725 0.5513 0.4699 0.1605  -0.0320 -0.0218 184 TRP   A NE1  
1145 C  CE2  . TRP   A 184 ? 0.4646 0.5494 0.4611 0.1582  -0.0258 -0.0208 184 TRP   A CE2  
1146 C  CE3  . TRP   A 184 ? 0.4771 0.5558 0.4577 0.1493  -0.0220 -0.0225 184 TRP   A CE3  
1147 C  CZ2  . TRP   A 184 ? 0.4658 0.5637 0.4710 0.1612  -0.0193 -0.0180 184 TRP   A CZ2  
1148 C  CZ3  . TRP   A 184 ? 0.4772 0.5675 0.4647 0.1524  -0.0162 -0.0198 184 TRP   A CZ3  
1149 C  CH2  . TRP   A 184 ? 0.4724 0.5719 0.4719 0.1581  -0.0144 -0.0175 184 TRP   A CH2  
1150 N  N    . TYR   A 185 ? 0.4387 0.4660 0.3899 0.1335  -0.0426 -0.0292 185 TYR   A N    
1151 C  CA   . TYR   A 185 ? 0.4447 0.4627 0.3861 0.1284  -0.0419 -0.0307 185 TYR   A CA   
1152 C  C    . TYR   A 185 ? 0.4620 0.4674 0.3979 0.1274  -0.0467 -0.0308 185 TYR   A C    
1153 O  O    . TYR   A 185 ? 0.4715 0.4668 0.3975 0.1240  -0.0455 -0.0323 185 TYR   A O    
1154 C  CB   . TYR   A 185 ? 0.4304 0.4590 0.3778 0.1244  -0.0391 -0.0287 185 TYR   A CB   
1155 C  CG   . TYR   A 185 ? 0.4213 0.4613 0.3728 0.1259  -0.0349 -0.0284 185 TYR   A CG   
1156 C  CD1  . TYR   A 185 ? 0.4256 0.4627 0.3680 0.1251  -0.0316 -0.0316 185 TYR   A CD1  
1157 C  CD2  . TYR   A 185 ? 0.4330 0.4853 0.3964 0.1284  -0.0341 -0.0251 185 TYR   A CD2  
1158 C  CE1  . TYR   A 185 ? 0.4393 0.4845 0.3829 0.1272  -0.0282 -0.0316 185 TYR   A CE1  
1159 C  CE2  . TYR   A 185 ? 0.4364 0.4972 0.4014 0.1307  -0.0296 -0.0248 185 TYR   A CE2  
1160 C  CZ   . TYR   A 185 ? 0.4497 0.5062 0.4038 0.1305  -0.0269 -0.0282 185 TYR   A CZ   
1161 O  OH   . TYR   A 185 ? 0.4838 0.5472 0.4376 0.1329  -0.0228 -0.0279 185 TYR   A OH   
1162 N  N    . ARG   A 186 ? 0.4770 0.4824 0.4186 0.1305  -0.0520 -0.0294 186 ARG   A N    
1163 C  CA   . ARG   A 186 ? 0.4995 0.4917 0.4347 0.1304  -0.0578 -0.0294 186 ARG   A CA   
1164 C  C    . ARG   A 186 ? 0.5234 0.4966 0.4409 0.1312  -0.0576 -0.0326 186 ARG   A C    
1165 O  O    . ARG   A 186 ? 0.5374 0.5063 0.4494 0.1347  -0.0563 -0.0347 186 ARG   A O    
1166 C  CB   . ARG   A 186 ? 0.5293 0.5266 0.4749 0.1341  -0.0643 -0.0276 186 ARG   A CB   
1167 C  CG   . ARG   A 186 ? 0.5821 0.5965 0.5452 0.1321  -0.0647 -0.0240 186 ARG   A CG   
1168 C  CD   . ARG   A 186 ? 0.6440 0.6564 0.6123 0.1303  -0.0722 -0.0221 186 ARG   A CD   
1169 N  NE   . ARG   A 186 ? 0.6945 0.7233 0.6798 0.1277  -0.0717 -0.0185 186 ARG   A NE   
1170 C  CZ   . ARG   A 186 ? 0.7471 0.7808 0.7344 0.1235  -0.0673 -0.0168 186 ARG   A CZ   
1171 N  NH1  . ARG   A 186 ? 0.7543 0.7793 0.7290 0.1215  -0.0634 -0.0183 186 ARG   A NH1  
1172 N  NH2  . ARG   A 186 ? 0.7568 0.8041 0.7587 0.1213  -0.0665 -0.0134 186 ARG   A NH2  
1173 N  N    . ALA   A 187 ? 0.5329 0.4933 0.4403 0.1280  -0.0582 -0.0330 187 ALA   A N    
1174 C  CA   . ALA   A 187 ? 0.5577 0.4984 0.4472 0.1280  -0.0572 -0.0356 187 ALA   A CA   
1175 C  C    . ALA   A 187 ? 0.5774 0.5059 0.4597 0.1338  -0.0634 -0.0364 187 ALA   A C    
1176 O  O    . ALA   A 187 ? 0.5671 0.5009 0.4581 0.1365  -0.0700 -0.0346 187 ALA   A O    
1177 C  CB   . ALA   A 187 ? 0.5625 0.4932 0.4437 0.1239  -0.0559 -0.0352 187 ALA   A CB   
1178 N  N    . PRO   A 188 ? 0.6032 0.5155 0.4698 0.1357  -0.0617 -0.0390 188 PRO   A N    
1179 C  CA   . PRO   A 188 ? 0.6227 0.5218 0.4806 0.1421  -0.0679 -0.0397 188 PRO   A CA   
1180 C  C    . PRO   A 188 ? 0.6367 0.5260 0.4902 0.1431  -0.0754 -0.0384 188 PRO   A C    
1181 O  O    . PRO   A 188 ? 0.6350 0.5259 0.4932 0.1483  -0.0830 -0.0377 188 PRO   A O    
1182 C  CB   . PRO   A 188 ? 0.6479 0.5280 0.4865 0.1421  -0.0633 -0.0426 188 PRO   A CB   
1183 C  CG   . PRO   A 188 ? 0.6478 0.5288 0.4841 0.1346  -0.0556 -0.0433 188 PRO   A CG   
1184 C  CD   . PRO   A 188 ? 0.6092 0.5137 0.4649 0.1321  -0.0544 -0.0415 188 PRO   A CD   
1185 N  N    . GLU   A 189 ? 0.6444 0.5247 0.4899 0.1383  -0.0735 -0.0380 189 GLU   A N    
1186 C  CA   . GLU   A 189 ? 0.6576 0.5265 0.4964 0.1389  -0.0802 -0.0369 189 GLU   A CA   
1187 C  C    . GLU   A 189 ? 0.6516 0.5370 0.5086 0.1385  -0.0866 -0.0345 189 GLU   A C    
1188 O  O    . GLU   A 189 ? 0.6558 0.5336 0.5098 0.1405  -0.0951 -0.0339 189 GLU   A O    
1189 C  CB   . GLU   A 189 ? 0.6777 0.5323 0.5024 0.1343  -0.0749 -0.0371 189 GLU   A CB   
1190 C  CG   . GLU   A 189 ? 0.6810 0.5503 0.5165 0.1286  -0.0680 -0.0360 189 GLU   A CG   
1191 C  CD   . GLU   A 189 ? 0.6461 0.5202 0.4817 0.1253  -0.0588 -0.0375 189 GLU   A CD   
1192 O  OE1  . GLU   A 189 ? 0.6370 0.5074 0.4682 0.1274  -0.0577 -0.0393 189 GLU   A OE1  
1193 O  OE2  . GLU   A 189 ? 0.6251 0.5061 0.4648 0.1208  -0.0531 -0.0368 189 GLU   A OE2  
1194 N  N    . VAL   A 190 ? 0.6379 0.5449 0.5130 0.1357  -0.0827 -0.0331 190 VAL   A N    
1195 C  CA   . VAL   A 190 ? 0.6296 0.5529 0.5229 0.1346  -0.0877 -0.0305 190 VAL   A CA   
1196 C  C    . VAL   A 190 ? 0.6323 0.5644 0.5363 0.1400  -0.0938 -0.0304 190 VAL   A C    
1197 O  O    . VAL   A 190 ? 0.6359 0.5704 0.5471 0.1411  -0.1024 -0.0291 190 VAL   A O    
1198 C  CB   . VAL   A 190 ? 0.6222 0.5635 0.5290 0.1300  -0.0809 -0.0288 190 VAL   A CB   
1199 C  CG1  . VAL   A 190 ? 0.6098 0.5679 0.5356 0.1288  -0.0852 -0.0259 190 VAL   A CG1  
1200 C  CG2  . VAL   A 190 ? 0.6311 0.5638 0.5279 0.1256  -0.0761 -0.0288 190 VAL   A CG2  
1201 N  N    . LEU   A 191 ? 0.6290 0.5640 0.5325 0.1438  -0.0896 -0.0318 191 LEU   A N    
1202 C  CA   . LEU   A 191 ? 0.6247 0.5676 0.5372 0.1504  -0.0940 -0.0318 191 LEU   A CA   
1203 C  C    . LEU   A 191 ? 0.6478 0.5752 0.5501 0.1553  -0.1036 -0.0327 191 LEU   A C    
1204 O  O    . LEU   A 191 ? 0.6369 0.5741 0.5525 0.1585  -0.1116 -0.0314 191 LEU   A O    
1205 C  CB   . LEU   A 191 ? 0.6085 0.5530 0.5178 0.1537  -0.0870 -0.0335 191 LEU   A CB   
1206 C  CG   . LEU   A 191 ? 0.5966 0.5568 0.5157 0.1502  -0.0784 -0.0328 191 LEU   A CG   
1207 C  CD1  . LEU   A 191 ? 0.5915 0.5459 0.5005 0.1527  -0.0722 -0.0354 191 LEU   A CD1  
1208 C  CD2  . LEU   A 191 ? 0.5822 0.5659 0.5246 0.1509  -0.0794 -0.0299 191 LEU   A CD2  
1209 N  N    . LEU   A 192 ? 0.6732 0.5767 0.5523 0.1553  -0.1028 -0.0346 192 LEU   A N    
1210 C  CA   . LEU   A 192 ? 0.7000 0.5831 0.5629 0.1601  -0.1111 -0.0357 192 LEU   A CA   
1211 C  C    . LEU   A 192 ? 0.7332 0.6112 0.5955 0.1574  -0.1194 -0.0346 192 LEU   A C    
1212 O  O    . LEU   A 192 ? 0.7424 0.6053 0.5932 0.1616  -0.1282 -0.0353 192 LEU   A O    
1213 C  CB   . LEU   A 192 ? 0.7065 0.5649 0.5436 0.1603  -0.1054 -0.0380 192 LEU   A CB   
1214 C  CG   . LEU   A 192 ? 0.7168 0.5728 0.5486 0.1643  -0.0999 -0.0397 192 LEU   A CG   
1215 C  CD1  . LEU   A 192 ? 0.7289 0.5637 0.5385 0.1612  -0.0921 -0.0416 192 LEU   A CD1  
1216 C  CD2  . LEU   A 192 ? 0.7277 0.5792 0.5574 0.1736  -0.1078 -0.0402 192 LEU   A CD2  
1217 N  N    . GLN   A 193 ? 0.7472 0.6366 0.6206 0.1506  -0.1167 -0.0329 193 GLN   A N    
1218 C  CA   . GLN   A 193 ? 0.7714 0.6567 0.6446 0.1467  -0.1229 -0.0317 193 GLN   A CA   
1219 C  C    . GLN   A 193 ? 0.8058 0.6631 0.6525 0.1467  -0.1238 -0.0330 193 GLN   A C    
1220 O  O    . GLN   A 193 ? 0.8159 0.6620 0.6557 0.1475  -0.1333 -0.0330 193 GLN   A O    
1221 C  CB   . GLN   A 193 ? 0.7972 0.6939 0.6867 0.1485  -0.1349 -0.0304 193 GLN   A CB   
1222 C  CG   . GLN   A 193 ? 0.8447 0.7704 0.7624 0.1462  -0.1327 -0.0281 193 GLN   A CG   
1223 C  CD   . GLN   A 193 ? 0.9161 0.8552 0.8527 0.1467  -0.1437 -0.0266 193 GLN   A CD   
1224 O  OE1  . GLN   A 193 ? 0.9652 0.8936 0.8961 0.1458  -0.1540 -0.0269 193 GLN   A OE1  
1225 N  NE2  . GLN   A 193 ? 0.9003 0.8640 0.8607 0.1475  -0.1416 -0.0249 193 GLN   A NE2  
1226 N  N    . SER   A 194 ? 0.8204 0.6658 0.6518 0.1456  -0.1139 -0.0342 194 SER   A N    
1227 C  CA   . SER   A 194 ? 0.8502 0.6686 0.6559 0.1455  -0.1129 -0.0352 194 SER   A CA   
1228 C  C    . SER   A 194 ? 0.8646 0.6812 0.6674 0.1396  -0.1063 -0.0342 194 SER   A C    
1229 O  O    . SER   A 194 ? 0.8832 0.6893 0.6787 0.1388  -0.1116 -0.0336 194 SER   A O    
1230 C  CB   . SER   A 194 ? 0.8784 0.6800 0.6656 0.1486  -0.1074 -0.0371 194 SER   A CB   
1231 O  OG   . SER   A 194 ? 0.9163 0.7249 0.7064 0.1448  -0.0955 -0.0376 194 SER   A OG   
1232 N  N    . SER   A 195 ? 0.8574 0.6836 0.6654 0.1359  -0.0951 -0.0341 195 SER   A N    
1233 C  CA   . SER   A 195 ? 0.8600 0.6862 0.6663 0.1311  -0.0880 -0.0330 195 SER   A CA   
1234 C  C    . SER   A 195 ? 0.8489 0.7008 0.6778 0.1274  -0.0844 -0.0314 195 SER   A C    
1235 O  O    . SER   A 195 ? 0.8495 0.7185 0.6936 0.1282  -0.0849 -0.0314 195 SER   A O    
1236 C  CB   . SER   A 195 ? 0.8861 0.6988 0.6766 0.1299  -0.0778 -0.0342 195 SER   A CB   
1237 O  OG   . SER   A 195 ? 0.9027 0.7225 0.6974 0.1299  -0.0728 -0.0356 195 SER   A OG   
1238 N  N    . TYR   A 196 ? 0.8383 0.6919 0.6683 0.1241  -0.0810 -0.0299 196 TYR   A N    
1239 C  CA   . TYR   A 196 ? 0.8182 0.6936 0.6670 0.1209  -0.0778 -0.0281 196 TYR   A CA   
1240 C  C    . TYR   A 196 ? 0.7815 0.6564 0.6263 0.1182  -0.0685 -0.0275 196 TYR   A C    
1241 O  O    . TYR   A 196 ? 0.7813 0.6664 0.6352 0.1162  -0.0672 -0.0256 196 TYR   A O    
1242 C  CB   . TYR   A 196 ? 0.8337 0.7152 0.6929 0.1202  -0.0863 -0.0261 196 TYR   A CB   
1243 C  CG   . TYR   A 196 ? 0.8720 0.7550 0.7366 0.1229  -0.0960 -0.0266 196 TYR   A CG   
1244 C  CD1  . TYR   A 196 ? 0.8810 0.7837 0.7636 0.1238  -0.0965 -0.0262 196 TYR   A CD1  
1245 C  CD2  . TYR   A 196 ? 0.9077 0.7719 0.7586 0.1252  -0.1048 -0.0275 196 TYR   A CD2  
1246 C  CE1  . TYR   A 196 ? 0.8940 0.7994 0.7828 0.1271  -0.1051 -0.0265 196 TYR   A CE1  
1247 C  CE2  . TYR   A 196 ? 0.9201 0.7866 0.7767 0.1284  -0.1145 -0.0280 196 TYR   A CE2  
1248 C  CZ   . TYR   A 196 ? 0.9193 0.8073 0.7959 0.1294  -0.1144 -0.0274 196 TYR   A CZ   
1249 O  OH   . TYR   A 196 ? 0.9372 0.8294 0.8212 0.1331  -0.1236 -0.0277 196 TYR   A OH   
1250 N  N    . ALA   A 197 ? 0.7477 0.6115 0.5797 0.1182  -0.0618 -0.0291 197 ALA   A N    
1251 C  CA   . ALA   A 197 ? 0.7125 0.5767 0.5417 0.1158  -0.0526 -0.0286 197 ALA   A CA   
1252 C  C    . ALA   A 197 ? 0.6562 0.5433 0.5023 0.1132  -0.0468 -0.0282 197 ALA   A C    
1253 O  O    . ALA   A 197 ? 0.6319 0.5337 0.4911 0.1132  -0.0498 -0.0281 197 ALA   A O    
1254 C  CB   . ALA   A 197 ? 0.7281 0.5735 0.5391 0.1161  -0.0470 -0.0301 197 ALA   A CB   
1255 N  N    . THR   A 198 ? 0.6292 0.5193 0.4750 0.1112  -0.0387 -0.0280 198 THR   A N    
1256 C  CA   . THR   A 198 ? 0.5950 0.5057 0.4553 0.1089  -0.0339 -0.0279 198 THR   A CA   
1257 C  C    . THR   A 198 ? 0.5622 0.4793 0.4262 0.1075  -0.0324 -0.0303 198 THR   A C    
1258 O  O    . THR   A 198 ? 0.5473 0.4823 0.4245 0.1065  -0.0319 -0.0301 198 THR   A O    
1259 C  CB   . THR   A 198 ? 0.6104 0.5235 0.4703 0.1076  -0.0263 -0.0270 198 THR   A CB   
1260 O  OG1  . THR   A 198 ? 0.6313 0.5319 0.4798 0.1064  -0.0206 -0.0286 198 THR   A OG1  
1261 C  CG2  . THR   A 198 ? 0.6158 0.5235 0.4724 0.1097  -0.0275 -0.0246 198 THR   A CG2  
1262 N  N    . PRO   A 199 ? 0.5435 0.4453 0.3950 0.1078  -0.0321 -0.0324 199 PRO   A N    
1263 C  CA   . PRO   A 199 ? 0.5254 0.4314 0.3788 0.1065  -0.0305 -0.0348 199 PRO   A CA   
1264 C  C    . PRO   A 199 ? 0.5147 0.4335 0.3792 0.1086  -0.0357 -0.0347 199 PRO   A C    
1265 O  O    . PRO   A 199 ? 0.5034 0.4304 0.3724 0.1075  -0.0337 -0.0363 199 PRO   A O    
1266 C  CB   . PRO   A 199 ? 0.5466 0.4301 0.3821 0.1076  -0.0304 -0.0364 199 PRO   A CB   
1267 C  CG   . PRO   A 199 ? 0.5586 0.4289 0.3834 0.1073  -0.0273 -0.0352 199 PRO   A CG   
1268 C  CD   . PRO   A 199 ? 0.5422 0.4206 0.3753 0.1092  -0.0320 -0.0328 199 PRO   A CD   
1269 N  N    . VAL   A 200 ? 0.5102 0.4306 0.3790 0.1115  -0.0421 -0.0329 200 VAL   A N    
1270 C  CA   . VAL   A 200 ? 0.5003 0.4335 0.3814 0.1137  -0.0470 -0.0319 200 VAL   A CA   
1271 C  C    . VAL   A 200 ? 0.4928 0.4457 0.3870 0.1118  -0.0431 -0.0315 200 VAL   A C    
1272 O  O    . VAL   A 200 ? 0.4911 0.4528 0.3915 0.1132  -0.0435 -0.0322 200 VAL   A O    
1273 C  CB   . VAL   A 200 ? 0.5111 0.4418 0.3944 0.1151  -0.0533 -0.0295 200 VAL   A CB   
1274 C  CG1  . VAL   A 200 ? 0.5138 0.4621 0.4137 0.1154  -0.0564 -0.0273 200 VAL   A CG1  
1275 C  CG2  . VAL   A 200 ? 0.5230 0.4359 0.3944 0.1181  -0.0595 -0.0304 200 VAL   A CG2  
1276 N  N    . ASP   A 201 ? 0.4854 0.4443 0.3826 0.1092  -0.0391 -0.0304 201 ASP   A N    
1277 C  CA   . ASP   A 201 ? 0.4672 0.4436 0.3753 0.1077  -0.0359 -0.0298 201 ASP   A CA   
1278 C  C    . ASP   A 201 ? 0.4656 0.4446 0.3717 0.1054  -0.0315 -0.0327 201 ASP   A C    
1279 O  O    . ASP   A 201 ? 0.4415 0.4339 0.3554 0.1051  -0.0305 -0.0329 201 ASP   A O    
1280 C  CB   . ASP   A 201 ? 0.4666 0.4469 0.3773 0.1065  -0.0337 -0.0276 201 ASP   A CB   
1281 C  CG   . ASP   A 201 ? 0.5128 0.4929 0.4270 0.1080  -0.0379 -0.0245 201 ASP   A CG   
1282 O  OD1  . ASP   A 201 ? 0.5137 0.4966 0.4330 0.1094  -0.0424 -0.0237 201 ASP   A OD1  
1283 O  OD2  . ASP   A 201 ? 0.5525 0.5299 0.4646 0.1078  -0.0365 -0.0229 201 ASP   A OD2  
1284 N  N    . LEU   A 202 ? 0.4770 0.4426 0.3721 0.1036  -0.0289 -0.0348 202 LEU   A N    
1285 C  CA   . LEU   A 202 ? 0.4954 0.4613 0.3877 0.1003  -0.0248 -0.0378 202 LEU   A CA   
1286 C  C    . LEU   A 202 ? 0.5159 0.4781 0.4047 0.1022  -0.0269 -0.0399 202 LEU   A C    
1287 O  O    . LEU   A 202 ? 0.5257 0.4922 0.4148 0.1001  -0.0248 -0.0422 202 LEU   A O    
1288 C  CB   . LEU   A 202 ? 0.5110 0.4639 0.3933 0.0970  -0.0202 -0.0390 202 LEU   A CB   
1289 C  CG   . LEU   A 202 ? 0.5297 0.4910 0.4176 0.0938  -0.0154 -0.0381 202 LEU   A CG   
1290 C  CD1  . LEU   A 202 ? 0.5165 0.4942 0.4142 0.0904  -0.0136 -0.0396 202 LEU   A CD1  
1291 C  CD2  . LEU   A 202 ? 0.5395 0.5040 0.4314 0.0967  -0.0168 -0.0348 202 LEU   A CD2  
1292 N  N    . TRP   A 203 ? 0.5125 0.4670 0.3980 0.1065  -0.0314 -0.0391 203 TRP   A N    
1293 C  CA   . TRP   A 203 ? 0.5082 0.4608 0.3918 0.1098  -0.0335 -0.0406 203 TRP   A CA   
1294 C  C    . TRP   A 203 ? 0.4856 0.4572 0.3822 0.1107  -0.0335 -0.0396 203 TRP   A C    
1295 O  O    . TRP   A 203 ? 0.4828 0.4575 0.3783 0.1103  -0.0315 -0.0417 203 TRP   A O    
1296 C  CB   . TRP   A 203 ? 0.5096 0.4528 0.3896 0.1149  -0.0390 -0.0397 203 TRP   A CB   
1297 C  CG   . TRP   A 203 ? 0.5263 0.4692 0.4055 0.1193  -0.0407 -0.0410 203 TRP   A CG   
1298 C  CD1  . TRP   A 203 ? 0.5357 0.4928 0.4266 0.1227  -0.0423 -0.0398 203 TRP   A CD1  
1299 C  CD2  . TRP   A 203 ? 0.5418 0.4692 0.4072 0.1207  -0.0397 -0.0439 203 TRP   A CD2  
1300 N  NE1  . TRP   A 203 ? 0.5418 0.4936 0.4273 0.1270  -0.0426 -0.0417 203 TRP   A NE1  
1301 C  CE2  . TRP   A 203 ? 0.5486 0.4817 0.4180 0.1259  -0.0412 -0.0444 203 TRP   A CE2  
1302 C  CE3  . TRP   A 203 ? 0.5629 0.4710 0.4121 0.1184  -0.0373 -0.0460 203 TRP   A CE3  
1303 C  CZ2  . TRP   A 203 ? 0.5655 0.4853 0.4227 0.1291  -0.0407 -0.0470 203 TRP   A CZ2  
1304 C  CZ3  . TRP   A 203 ? 0.5843 0.4782 0.4211 0.1213  -0.0373 -0.0484 203 TRP   A CZ3  
1305 C  CH2  . TRP   A 203 ? 0.5788 0.4787 0.4194 0.1265  -0.0389 -0.0490 203 TRP   A CH2  
1306 N  N    . SER   A 204 ? 0.4699 0.4526 0.3773 0.1118  -0.0355 -0.0364 204 SER   A N    
1307 C  CA   . SER   A 204 ? 0.4720 0.4715 0.3907 0.1128  -0.0349 -0.0348 204 SER   A CA   
1308 C  C    . SER   A 204 ? 0.4843 0.4915 0.4035 0.1096  -0.0310 -0.0364 204 SER   A C    
1309 O  O    . SER   A 204 ? 0.4928 0.5076 0.4146 0.1111  -0.0301 -0.0371 204 SER   A O    
1310 C  CB   . SER   A 204 ? 0.4838 0.4913 0.4121 0.1132  -0.0371 -0.0310 204 SER   A CB   
1311 O  OG   . SER   A 204 ? 0.5115 0.5116 0.4394 0.1154  -0.0417 -0.0298 204 SER   A OG   
1312 N  N    . VAL   A 205 ? 0.4885 0.4937 0.4050 0.1056  -0.0287 -0.0372 205 VAL   A N    
1313 C  CA   . VAL   A 205 ? 0.4947 0.5073 0.4123 0.1019  -0.0258 -0.0390 205 VAL   A CA   
1314 C  C    . VAL   A 205 ? 0.4937 0.5004 0.4037 0.1006  -0.0248 -0.0429 205 VAL   A C    
1315 O  O    . VAL   A 205 ? 0.4875 0.5026 0.3995 0.0999  -0.0243 -0.0442 205 VAL   A O    
1316 C  CB   . VAL   A 205 ? 0.5150 0.5267 0.4327 0.0982  -0.0235 -0.0387 205 VAL   A CB   
1317 C  CG1  . VAL   A 205 ? 0.5232 0.5357 0.4385 0.0932  -0.0205 -0.0420 205 VAL   A CG1  
1318 C  CG2  . VAL   A 205 ? 0.5205 0.5444 0.4472 0.0994  -0.0238 -0.0354 205 VAL   A CG2  
1319 N  N    . GLY   A 206 ? 0.5023 0.4935 0.4024 0.1007  -0.0248 -0.0447 206 GLY   A N    
1320 C  CA   . GLY   A 206 ? 0.5108 0.4928 0.4013 0.1000  -0.0239 -0.0484 206 GLY   A CA   
1321 C  C    . GLY   A 206 ? 0.5158 0.5022 0.4074 0.1050  -0.0253 -0.0485 206 GLY   A C    
1322 O  O    . GLY   A 206 ? 0.5265 0.5125 0.4134 0.1042  -0.0243 -0.0512 206 GLY   A O    
1323 N  N    . CYS   A 207 ? 0.5075 0.4987 0.4057 0.1103  -0.0276 -0.0454 207 CYS   A N    
1324 C  CA   . CYS   A 207 ? 0.4984 0.4962 0.4004 0.1158  -0.0282 -0.0446 207 CYS   A CA   
1325 C  C    . CYS   A 207 ? 0.4905 0.5026 0.3987 0.1150  -0.0265 -0.0440 207 CYS   A C    
1326 O  O    . CYS   A 207 ? 0.4867 0.5010 0.3928 0.1182  -0.0254 -0.0450 207 CYS   A O    
1327 C  CB   . CYS   A 207 ? 0.4960 0.4973 0.4062 0.1202  -0.0310 -0.0411 207 CYS   A CB   
1328 S  SG   . CYS   A 207 ? 0.5178 0.5017 0.4191 0.1236  -0.0343 -0.0421 207 CYS   A SG   
1329 N  N    . ILE   A 208 ? 0.4838 0.5049 0.3991 0.1117  -0.0265 -0.0421 208 ILE   A N    
1330 C  CA   . ILE   A 208 ? 0.4743 0.5088 0.3953 0.1111  -0.0255 -0.0409 208 ILE   A CA   
1331 C  C    . ILE   A 208 ? 0.4851 0.5186 0.3994 0.1073  -0.0246 -0.0448 208 ILE   A C    
1332 O  O    . ILE   A 208 ? 0.4926 0.5312 0.4053 0.1089  -0.0241 -0.0456 208 ILE   A O    
1333 C  CB   . ILE   A 208 ? 0.4589 0.5015 0.3889 0.1098  -0.0261 -0.0373 208 ILE   A CB   
1334 C  CG1  . ILE   A 208 ? 0.4563 0.5022 0.3937 0.1137  -0.0273 -0.0334 208 ILE   A CG1  
1335 C  CG2  . ILE   A 208 ? 0.4630 0.5173 0.3965 0.1087  -0.0253 -0.0366 208 ILE   A CG2  
1336 C  CD1  . ILE   A 208 ? 0.4651 0.5099 0.4070 0.1126  -0.0290 -0.0305 208 ILE   A CD1  
1337 N  N    . PHE   A 209 ? 0.4963 0.5226 0.4063 0.1022  -0.0244 -0.0472 209 PHE   A N    
1338 C  CA   . PHE   A 209 ? 0.5109 0.5346 0.4150 0.0970  -0.0239 -0.0513 209 PHE   A CA   
1339 C  C    . PHE   A 209 ? 0.5331 0.5487 0.4268 0.0991  -0.0239 -0.0545 209 PHE   A C    
1340 O  O    . PHE   A 209 ? 0.5432 0.5633 0.4344 0.0980  -0.0245 -0.0565 209 PHE   A O    
1341 C  CB   . PHE   A 209 ? 0.5149 0.5287 0.4154 0.0918  -0.0226 -0.0529 209 PHE   A CB   
1342 C  CG   . PHE   A 209 ? 0.5303 0.5430 0.4275 0.0847  -0.0220 -0.0567 209 PHE   A CG   
1343 C  CD1  . PHE   A 209 ? 0.5456 0.5706 0.4472 0.0826  -0.0235 -0.0579 209 PHE   A CD1  
1344 C  CD2  . PHE   A 209 ? 0.5429 0.5419 0.4326 0.0799  -0.0200 -0.0591 209 PHE   A CD2  
1345 C  CE1  . PHE   A 209 ? 0.5548 0.5799 0.4550 0.0753  -0.0237 -0.0616 209 PHE   A CE1  
1346 C  CE2  . PHE   A 209 ? 0.5545 0.5532 0.4427 0.0722  -0.0192 -0.0626 209 PHE   A CE2  
1347 C  CZ   . PHE   A 209 ? 0.5533 0.5657 0.4475 0.0698  -0.0214 -0.0639 209 PHE   A CZ   
1348 N  N    . ALA   A 210 ? 0.5349 0.5383 0.4221 0.1029  -0.0235 -0.0547 210 ALA   A N    
1349 C  CA   . ALA   A 210 ? 0.5410 0.5350 0.4175 0.1065  -0.0229 -0.0573 210 ALA   A CA   
1350 C  C    . ALA   A 210 ? 0.5302 0.5346 0.4098 0.1117  -0.0225 -0.0559 210 ALA   A C    
1351 O  O    . ALA   A 210 ? 0.5428 0.5443 0.4140 0.1117  -0.0221 -0.0588 210 ALA   A O    
1352 C  CB   . ALA   A 210 ? 0.5536 0.5354 0.4252 0.1113  -0.0229 -0.0569 210 ALA   A CB   
1353 N  N    . GLU   A 211 ? 0.5055 0.5213 0.3966 0.1157  -0.0224 -0.0514 211 GLU   A N    
1354 C  CA   . GLU   A 211 ? 0.4914 0.5178 0.3870 0.1206  -0.0210 -0.0490 211 GLU   A CA   
1355 C  C    . GLU   A 211 ? 0.5157 0.5506 0.4109 0.1179  -0.0212 -0.0496 211 GLU   A C    
1356 O  O    . GLU   A 211 ? 0.5135 0.5529 0.4067 0.1219  -0.0197 -0.0488 211 GLU   A O    
1357 C  CB   . GLU   A 211 ? 0.4627 0.4981 0.3714 0.1238  -0.0210 -0.0439 211 GLU   A CB   
1358 C  CG   . GLU   A 211 ? 0.4248 0.4710 0.3395 0.1289  -0.0185 -0.0406 211 GLU   A CG   
1359 C  CD   . GLU   A 211 ? 0.5049 0.5586 0.4325 0.1319  -0.0184 -0.0360 211 GLU   A CD   
1360 O  OE1  . GLU   A 211 ? 0.5113 0.5602 0.4419 0.1311  -0.0210 -0.0357 211 GLU   A OE1  
1361 O  OE2  . GLU   A 211 ? 0.5383 0.6017 0.4722 0.1349  -0.0158 -0.0328 211 GLU   A OE2  
1362 N  N    . MET   A 212 ? 0.5293 0.5664 0.4261 0.1116  -0.0231 -0.0509 212 MET   A N    
1363 C  CA   . MET   A 212 ? 0.5482 0.5937 0.4449 0.1093  -0.0245 -0.0517 212 MET   A CA   
1364 C  C    . MET   A 212 ? 0.5738 0.6111 0.4571 0.1082  -0.0252 -0.0566 212 MET   A C    
1365 O  O    . MET   A 212 ? 0.5661 0.6082 0.4456 0.1095  -0.0260 -0.0571 212 MET   A O    
1366 C  CB   . MET   A 212 ? 0.5595 0.6114 0.4636 0.1035  -0.0262 -0.0514 212 MET   A CB   
1367 C  CG   . MET   A 212 ? 0.5925 0.6547 0.5081 0.1057  -0.0258 -0.0463 212 MET   A CG   
1368 S  SD   . MET   A 212 ? 0.7683 0.8366 0.6910 0.0998  -0.0272 -0.0465 212 MET   A SD   
1369 C  CE   . MET   A 212 ? 0.7443 0.8187 0.6768 0.1032  -0.0263 -0.0406 212 MET   A CE   
1370 N  N    . PHE   A 213 ? 0.5892 0.6124 0.4637 0.1062  -0.0249 -0.0601 213 PHE   A N    
1371 C  CA   . PHE   A 213 ? 0.6093 0.6211 0.4691 0.1051  -0.0256 -0.0649 213 PHE   A CA   
1372 C  C    . PHE   A 213 ? 0.6254 0.6319 0.4775 0.1136  -0.0228 -0.0643 213 PHE   A C    
1373 O  O    . PHE   A 213 ? 0.6316 0.6374 0.4751 0.1160  -0.0228 -0.0658 213 PHE   A O    
1374 C  CB   . PHE   A 213 ? 0.6190 0.6163 0.4717 0.0995  -0.0258 -0.0686 213 PHE   A CB   
1375 C  CG   . PHE   A 213 ? 0.6316 0.6329 0.4901 0.0904  -0.0277 -0.0701 213 PHE   A CG   
1376 C  CD1  . PHE   A 213 ? 0.6361 0.6421 0.5052 0.0883  -0.0267 -0.0673 213 PHE   A CD1  
1377 C  CD2  . PHE   A 213 ? 0.6492 0.6499 0.5026 0.0838  -0.0305 -0.0743 213 PHE   A CD2  
1378 C  CE1  . PHE   A 213 ? 0.6433 0.6543 0.5187 0.0805  -0.0275 -0.0683 213 PHE   A CE1  
1379 C  CE2  . PHE   A 213 ? 0.6517 0.6586 0.5130 0.0753  -0.0319 -0.0754 213 PHE   A CE2  
1380 C  CZ   . PHE   A 213 ? 0.6432 0.6555 0.5158 0.0740  -0.0299 -0.0723 213 PHE   A CZ   
1381 N  N    . ARG   A 214 ? 0.6296 0.6323 0.4846 0.1185  -0.0205 -0.0620 214 ARG   A N    
1382 C  CA   . ARG   A 214 ? 0.6322 0.6309 0.4828 0.1272  -0.0173 -0.0609 214 ARG   A CA   
1383 C  C    . ARG   A 214 ? 0.6367 0.6481 0.4937 0.1329  -0.0148 -0.0571 214 ARG   A C    
1384 O  O    . ARG   A 214 ? 0.6505 0.6582 0.4999 0.1395  -0.0116 -0.0573 214 ARG   A O    
1385 C  CB   . ARG   A 214 ? 0.6328 0.6280 0.4891 0.1305  -0.0166 -0.0589 214 ARG   A CB   
1386 C  CG   . ARG   A 214 ? 0.6761 0.6548 0.5228 0.1267  -0.0181 -0.0624 214 ARG   A CG   
1387 C  CD   . ARG   A 214 ? 0.7129 0.6893 0.5659 0.1294  -0.0185 -0.0600 214 ARG   A CD   
1388 N  NE   . ARG   A 214 ? 0.7316 0.7145 0.5916 0.1383  -0.0170 -0.0566 214 ARG   A NE   
1389 C  CZ   . ARG   A 214 ? 0.7459 0.7199 0.5982 0.1457  -0.0153 -0.0576 214 ARG   A CZ   
1390 N  NH1  . ARG   A 214 ? 0.7486 0.7045 0.5835 0.1453  -0.0150 -0.0620 214 ARG   A NH1  
1391 N  NH2  . ARG   A 214 ? 0.7337 0.7169 0.5958 0.1534  -0.0137 -0.0541 214 ARG   A NH2  
1392 N  N    . ARG   A 215 ? 0.6254 0.6509 0.4959 0.1309  -0.0155 -0.0532 215 ARG   A N    
1393 C  CA   . ARG   A 215 ? 0.6289 0.6666 0.5069 0.1355  -0.0127 -0.0487 215 ARG   A CA   
1394 C  C    . ARG   A 215 ? 0.6244 0.6645 0.5095 0.1425  -0.0090 -0.0453 215 ARG   A C    
1395 O  O    . ARG   A 215 ? 0.6212 0.6689 0.5101 0.1475  -0.0051 -0.0419 215 ARG   A O    
1396 C  CB   . ARG   A 215 ? 0.6531 0.6908 0.5202 0.1371  -0.0119 -0.0501 215 ARG   A CB   
1397 C  CG   . ARG   A 215 ? 0.7001 0.7453 0.5694 0.1316  -0.0156 -0.0502 215 ARG   A CG   
1398 C  CD   . ARG   A 215 ? 0.7667 0.8117 0.6248 0.1343  -0.0151 -0.0511 215 ARG   A CD   
1399 N  NE   . ARG   A 215 ? 0.8297 0.8608 0.6708 0.1343  -0.0161 -0.0566 215 ARG   A NE   
1400 C  CZ   . ARG   A 215 ? 0.8712 0.8968 0.6977 0.1379  -0.0153 -0.0584 215 ARG   A CZ   
1401 N  NH1  . ARG   A 215 ? 0.8678 0.9009 0.6945 0.1420  -0.0131 -0.0548 215 ARG   A NH1  
1402 N  NH2  . ARG   A 215 ? 0.8853 0.8962 0.6954 0.1373  -0.0166 -0.0637 215 ARG   A NH2  
1403 N  N    . LYS   A 216 ? 0.6198 0.6536 0.5072 0.1427  -0.0103 -0.0460 216 LYS   A N    
1404 C  CA   . LYS   A 216 ? 0.6169 0.6534 0.5130 0.1486  -0.0086 -0.0431 216 LYS   A CA   
1405 C  C    . LYS   A 216 ? 0.6018 0.6340 0.5028 0.1451  -0.0127 -0.0433 216 LYS   A C    
1406 O  O    . LYS   A 216 ? 0.6024 0.6238 0.4942 0.1403  -0.0151 -0.0469 216 LYS   A O    
1407 C  CB   . LYS   A 216 ? 0.6536 0.6815 0.5395 0.1562  -0.0052 -0.0451 216 LYS   A CB   
1408 C  CG   . LYS   A 216 ? 0.7314 0.7409 0.6001 0.1549  -0.0070 -0.0507 216 LYS   A CG   
1409 C  CD   . LYS   A 216 ? 0.8166 0.8169 0.6712 0.1621  -0.0029 -0.0529 216 LYS   A CD   
1410 C  CE   . LYS   A 216 ? 0.8941 0.8740 0.7303 0.1608  -0.0046 -0.0584 216 LYS   A CE   
1411 N  NZ   . LYS   A 216 ? 0.9297 0.9014 0.7649 0.1671  -0.0043 -0.0584 216 LYS   A NZ   
1412 N  N    . PRO   A 217 ? 0.5963 0.6357 0.5110 0.1471  -0.0137 -0.0395 217 PRO   A N    
1413 C  CA   . PRO   A 217 ? 0.6008 0.6340 0.5176 0.1444  -0.0180 -0.0399 217 PRO   A CA   
1414 C  C    . PRO   A 217 ? 0.6274 0.6438 0.5310 0.1463  -0.0192 -0.0438 217 PRO   A C    
1415 O  O    . PRO   A 217 ? 0.6415 0.6532 0.5386 0.1524  -0.0168 -0.0452 217 PRO   A O    
1416 C  CB   . PRO   A 217 ? 0.5974 0.6414 0.5303 0.1476  -0.0189 -0.0354 217 PRO   A CB   
1417 C  CG   . PRO   A 217 ? 0.5947 0.6526 0.5359 0.1488  -0.0150 -0.0320 217 PRO   A CG   
1418 C  CD   . PRO   A 217 ? 0.5824 0.6357 0.5110 0.1516  -0.0110 -0.0348 217 PRO   A CD   
1419 N  N    . LEU   A 218 ? 0.6329 0.6391 0.5311 0.1412  -0.0222 -0.0457 218 LEU   A N    
1420 C  CA   . LEU   A 218 ? 0.6522 0.6402 0.5364 0.1420  -0.0232 -0.0492 218 LEU   A CA   
1421 C  C    . LEU   A 218 ? 0.6569 0.6415 0.5438 0.1493  -0.0252 -0.0478 218 LEU   A C    
1422 O  O    . LEU   A 218 ? 0.6706 0.6458 0.5481 0.1552  -0.0240 -0.0498 218 LEU   A O    
1423 C  CB   . LEU   A 218 ? 0.6595 0.6380 0.5376 0.1342  -0.0249 -0.0510 218 LEU   A CB   
1424 C  CG   . LEU   A 218 ? 0.6890 0.6467 0.5501 0.1332  -0.0249 -0.0550 218 LEU   A CG   
1425 C  CD1  . LEU   A 218 ? 0.6970 0.6472 0.5455 0.1329  -0.0223 -0.0588 218 LEU   A CD1  
1426 C  CD2  . LEU   A 218 ? 0.7037 0.6547 0.5614 0.1252  -0.0254 -0.0560 218 LEU   A CD2  
1427 N  N    . PHE   A 219 ? 0.6465 0.6384 0.5456 0.1493  -0.0285 -0.0445 219 PHE   A N    
1428 C  CA   . PHE   A 219 ? 0.6468 0.6369 0.5503 0.1555  -0.0321 -0.0431 219 PHE   A CA   
1429 C  C    . PHE   A 219 ? 0.6557 0.6654 0.5788 0.1590  -0.0323 -0.0388 219 PHE   A C    
1430 O  O    . PHE   A 219 ? 0.6513 0.6690 0.5855 0.1554  -0.0352 -0.0360 219 PHE   A O    
1431 C  CB   . PHE   A 219 ? 0.6343 0.6132 0.5333 0.1520  -0.0367 -0.0433 219 PHE   A CB   
1432 C  CG   . PHE   A 219 ? 0.6422 0.6033 0.5240 0.1467  -0.0356 -0.0469 219 PHE   A CG   
1433 C  CD1  . PHE   A 219 ? 0.6620 0.6060 0.5275 0.1496  -0.0344 -0.0502 219 PHE   A CD1  
1434 C  CD2  . PHE   A 219 ? 0.6436 0.6042 0.5253 0.1389  -0.0355 -0.0467 219 PHE   A CD2  
1435 C  CE1  . PHE   A 219 ? 0.6781 0.6051 0.5281 0.1438  -0.0330 -0.0533 219 PHE   A CE1  
1436 C  CE2  . PHE   A 219 ? 0.6608 0.6059 0.5282 0.1337  -0.0339 -0.0497 219 PHE   A CE2  
1437 C  CZ   . PHE   A 219 ? 0.6688 0.5971 0.5206 0.1357  -0.0326 -0.0529 219 PHE   A CZ   
1438 N  N    . ARG   A 220 ? 0.6647 0.6814 0.5917 0.1659  -0.0289 -0.0381 220 ARG   A N    
1439 C  CA   . ARG   A 220 ? 0.6638 0.7000 0.6102 0.1690  -0.0277 -0.0338 220 ARG   A CA   
1440 C  C    . ARG   A 220 ? 0.6603 0.7010 0.6177 0.1756  -0.0319 -0.0320 220 ARG   A C    
1441 O  O    . ARG   A 220 ? 0.6719 0.7231 0.6388 0.1826  -0.0290 -0.0302 220 ARG   A O    
1442 C  CB   . ARG   A 220 ? 0.6912 0.7342 0.6364 0.1725  -0.0204 -0.0336 220 ARG   A CB   
1443 C  CG   . ARG   A 220 ? 0.7451 0.8083 0.7089 0.1732  -0.0171 -0.0289 220 ARG   A CG   
1444 C  CD   . ARG   A 220 ? 0.8223 0.8893 0.7809 0.1730  -0.0102 -0.0288 220 ARG   A CD   
1445 N  NE   . ARG   A 220 ? 0.9053 0.9620 0.8484 0.1790  -0.0061 -0.0321 220 ARG   A NE   
1446 C  CZ   . ARG   A 220 ? 0.9469 1.0084 0.8930 0.1878  -0.0013 -0.0310 220 ARG   A CZ   
1447 N  NH1  . ARG   A 220 ? 0.9324 1.0106 0.8985 0.1912  0.0001  -0.0265 220 ARG   A NH1  
1448 N  NH2  . ARG   A 220 ? 0.9552 1.0045 0.8845 0.1931  0.0022  -0.0344 220 ARG   A NH2  
1449 N  N    . GLY   A 221 ? 0.6456 0.6790 0.6023 0.1735  -0.0388 -0.0322 221 GLY   A N    
1450 C  CA   . GLY   A 221 ? 0.6360 0.6729 0.6028 0.1787  -0.0449 -0.0307 221 GLY   A CA   
1451 C  C    . GLY   A 221 ? 0.6171 0.6762 0.6080 0.1789  -0.0453 -0.0262 221 GLY   A C    
1452 O  O    . GLY   A 221 ? 0.6177 0.6874 0.6162 0.1738  -0.0412 -0.0241 221 GLY   A O    
1453 N  N    . SER   A 222 ? 0.6040 0.6706 0.6076 0.1847  -0.0501 -0.0246 222 SER   A N    
1454 C  CA   . SER   A 222 ? 0.5821 0.6714 0.6111 0.1847  -0.0505 -0.0202 222 SER   A CA   
1455 C  C    . SER   A 222 ? 0.5692 0.6615 0.6097 0.1823  -0.0609 -0.0188 222 SER   A C    
1456 O  O    . SER   A 222 ? 0.5557 0.6664 0.6183 0.1812  -0.0625 -0.0153 222 SER   A O    
1457 C  CB   . SER   A 222 ? 0.5810 0.6822 0.6199 0.1944  -0.0457 -0.0191 222 SER   A CB   
1458 O  OG   . SER   A 222 ? 0.6032 0.6968 0.6378 0.2027  -0.0512 -0.0209 222 SER   A OG   
1459 N  N    . SER   A 223 ? 0.5725 0.6460 0.5973 0.1813  -0.0676 -0.0215 223 SER   A N    
1460 C  CA   . SER   A 223 ? 0.5721 0.6422 0.6008 0.1796  -0.0784 -0.0211 223 SER   A CA   
1461 C  C    . SER   A 223 ? 0.5893 0.6347 0.5935 0.1763  -0.0809 -0.0244 223 SER   A C    
1462 O  O    . SER   A 223 ? 0.5914 0.6254 0.5792 0.1767  -0.0746 -0.0268 223 SER   A O    
1463 C  CB   . SER   A 223 ? 0.5873 0.6613 0.6235 0.1892  -0.0844 -0.0212 223 SER   A CB   
1464 O  OG   . SER   A 223 ? 0.6339 0.6890 0.6492 0.1961  -0.0841 -0.0246 223 SER   A OG   
1465 N  N    . ASP   A 224 ? 0.6042 0.6407 0.6051 0.1731  -0.0896 -0.0245 224 ASP   A N    
1466 C  CA   . ASP   A 224 ? 0.6425 0.6549 0.6199 0.1701  -0.0914 -0.0272 224 ASP   A CA   
1467 C  C    . ASP   A 224 ? 0.6620 0.6559 0.6199 0.1772  -0.0915 -0.0304 224 ASP   A C    
1468 O  O    . ASP   A 224 ? 0.6701 0.6465 0.6081 0.1747  -0.0872 -0.0329 224 ASP   A O    
1469 C  CB   . ASP   A 224 ? 0.6844 0.6902 0.6613 0.1659  -0.1007 -0.0265 224 ASP   A CB   
1470 C  CG   . ASP   A 224 ? 0.7916 0.8029 0.7800 0.1706  -0.1117 -0.0256 224 ASP   A CG   
1471 O  OD1  . ASP   A 224 ? 0.7988 0.8261 0.8031 0.1766  -0.1117 -0.0244 224 ASP   A OD1  
1472 O  OD2  . ASP   A 224 ? 0.8550 0.8553 0.8373 0.1682  -0.1203 -0.0258 224 ASP   A OD2  
1473 N  N    . VAL   A 225 ? 0.6598 0.6580 0.6241 0.1860  -0.0963 -0.0302 225 VAL   A N    
1474 C  CA   . VAL   A 225 ? 0.6701 0.6508 0.6166 0.1942  -0.0972 -0.0329 225 VAL   A CA   
1475 C  C    . VAL   A 225 ? 0.6669 0.6473 0.6072 0.1968  -0.0870 -0.0343 225 VAL   A C    
1476 O  O    . VAL   A 225 ? 0.6931 0.6527 0.6110 0.1975  -0.0839 -0.0372 225 VAL   A O    
1477 C  CB   . VAL   A 225 ? 0.6736 0.6576 0.6278 0.2036  -0.1068 -0.0323 225 VAL   A CB   
1478 C  CG1  . VAL   A 225 ? 0.6734 0.6463 0.6221 0.2013  -0.1178 -0.0323 225 VAL   A CG1  
1479 C  CG2  . VAL   A 225 ? 0.6630 0.6761 0.6466 0.2069  -0.1068 -0.0292 225 VAL   A CG2  
1480 N  N    . ASP   A 226 ? 0.6412 0.6433 0.5999 0.1973  -0.0815 -0.0323 226 ASP   A N    
1481 C  CA   . ASP   A 226 ? 0.6489 0.6511 0.6014 0.1994  -0.0717 -0.0336 226 ASP   A CA   
1482 C  C    . ASP   A 226 ? 0.6587 0.6491 0.5960 0.1903  -0.0664 -0.0355 226 ASP   A C    
1483 O  O    . ASP   A 226 ? 0.6805 0.6539 0.5984 0.1911  -0.0625 -0.0386 226 ASP   A O    
1484 C  CB   . ASP   A 226 ? 0.6558 0.6832 0.6305 0.2011  -0.0665 -0.0306 226 ASP   A CB   
1485 C  CG   . ASP   A 226 ? 0.7361 0.7628 0.7031 0.2044  -0.0567 -0.0320 226 ASP   A CG   
1486 O  OD1  . ASP   A 226 ? 0.7863 0.7952 0.7342 0.2098  -0.0553 -0.0351 226 ASP   A OD1  
1487 O  OD2  . ASP   A 226 ? 0.7125 0.7555 0.6917 0.2020  -0.0505 -0.0299 226 ASP   A OD2  
1488 N  N    . GLN   A 227 ? 0.6310 0.6297 0.5771 0.1816  -0.0669 -0.0337 227 GLN   A N    
1489 C  CA   . GLN   A 227 ? 0.6161 0.6074 0.5517 0.1729  -0.0625 -0.0349 227 GLN   A CA   
1490 C  C    . GLN   A 227 ? 0.6267 0.5934 0.5390 0.1717  -0.0630 -0.0383 227 GLN   A C    
1491 O  O    . GLN   A 227 ? 0.6344 0.5926 0.5342 0.1692  -0.0571 -0.0407 227 GLN   A O    
1492 C  CB   . GLN   A 227 ? 0.5974 0.5985 0.5449 0.1655  -0.0650 -0.0323 227 GLN   A CB   
1493 C  CG   . GLN   A 227 ? 0.5718 0.5715 0.5137 0.1575  -0.0596 -0.0328 227 GLN   A CG   
1494 C  CD   . GLN   A 227 ? 0.5650 0.5721 0.5070 0.1574  -0.0518 -0.0334 227 GLN   A CD   
1495 O  OE1  . GLN   A 227 ? 0.5777 0.5742 0.5056 0.1549  -0.0479 -0.0362 227 GLN   A OE1  
1496 N  NE2  . GLN   A 227 ? 0.5270 0.5522 0.4848 0.1598  -0.0492 -0.0308 227 GLN   A NE2  
1497 N  N    . LEU   A 228 ? 0.6258 0.5802 0.5315 0.1736  -0.0701 -0.0384 228 LEU   A N    
1498 C  CA   . LEU   A 228 ? 0.6545 0.5839 0.5372 0.1729  -0.0707 -0.0412 228 LEU   A CA   
1499 C  C    . LEU   A 228 ? 0.6709 0.5870 0.5388 0.1792  -0.0674 -0.0439 228 LEU   A C    
1500 O  O    . LEU   A 228 ? 0.6889 0.5872 0.5383 0.1757  -0.0632 -0.0465 228 LEU   A O    
1501 C  CB   . LEU   A 228 ? 0.6745 0.5940 0.5534 0.1745  -0.0796 -0.0404 228 LEU   A CB   
1502 C  CG   . LEU   A 228 ? 0.7180 0.6108 0.5728 0.1725  -0.0800 -0.0424 228 LEU   A CG   
1503 C  CD1  . LEU   A 228 ? 0.7266 0.6154 0.5752 0.1630  -0.0733 -0.0431 228 LEU   A CD1  
1504 C  CD2  . LEU   A 228 ? 0.7399 0.6244 0.5917 0.1749  -0.0894 -0.0414 228 LEU   A CD2  
1505 N  N    . GLY   A 229 ? 0.6548 0.5801 0.5315 0.1881  -0.0688 -0.0431 229 GLY   A N    
1506 C  CA   . GLY   A 229 ? 0.6516 0.5653 0.5151 0.1955  -0.0657 -0.0455 229 GLY   A CA   
1507 C  C    . GLY   A 229 ? 0.6440 0.5570 0.5011 0.1911  -0.0569 -0.0474 229 GLY   A C    
1508 O  O    . GLY   A 229 ? 0.6633 0.5558 0.4998 0.1894  -0.0537 -0.0505 229 GLY   A O    
1509 N  N    . LYS   A 230 ? 0.6187 0.5530 0.4928 0.1882  -0.0533 -0.0457 230 LYS   A N    
1510 C  CA   . LYS   A 230 ? 0.6252 0.5624 0.4960 0.1834  -0.0459 -0.0472 230 LYS   A CA   
1511 C  C    . LYS   A 230 ? 0.6434 0.5671 0.5005 0.1733  -0.0440 -0.0494 230 LYS   A C    
1512 O  O    . LYS   A 230 ? 0.6556 0.5697 0.4999 0.1708  -0.0394 -0.0524 230 LYS   A O    
1513 C  CB   . LYS   A 230 ? 0.6319 0.5943 0.5239 0.1818  -0.0435 -0.0442 230 LYS   A CB   
1514 C  CG   . LYS   A 230 ? 0.6779 0.6549 0.5843 0.1916  -0.0437 -0.0418 230 LYS   A CG   
1515 C  CD   . LYS   A 230 ? 0.7214 0.7135 0.6363 0.1924  -0.0367 -0.0407 230 LYS   A CD   
1516 C  CE   . LYS   A 230 ? 0.7757 0.7824 0.7049 0.2023  -0.0353 -0.0383 230 LYS   A CE   
1517 N  NZ   . LYS   A 230 ? 0.8275 0.8205 0.7434 0.2124  -0.0346 -0.0407 230 LYS   A NZ   
1518 N  N    . ILE   A 231 ? 0.6359 0.5576 0.4950 0.1679  -0.0478 -0.0482 231 ILE   A N    
1519 C  CA   . ILE   A 231 ? 0.6476 0.5569 0.4950 0.1590  -0.0458 -0.0499 231 ILE   A CA   
1520 C  C    . ILE   A 231 ? 0.6698 0.5532 0.4944 0.1600  -0.0449 -0.0530 231 ILE   A C    
1521 O  O    . ILE   A 231 ? 0.6760 0.5497 0.4891 0.1544  -0.0402 -0.0557 231 ILE   A O    
1522 C  CB   . ILE   A 231 ? 0.6471 0.5601 0.5016 0.1544  -0.0496 -0.0475 231 ILE   A CB   
1523 C  CG1  . ILE   A 231 ? 0.6398 0.5756 0.5136 0.1504  -0.0486 -0.0448 231 ILE   A CG1  
1524 C  CG2  . ILE   A 231 ? 0.6608 0.5563 0.5000 0.1476  -0.0476 -0.0492 231 ILE   A CG2  
1525 C  CD1  . ILE   A 231 ? 0.6384 0.5812 0.5233 0.1498  -0.0542 -0.0417 231 ILE   A CD1  
1526 N  N    . LEU   A 232 ? 0.6823 0.5541 0.5001 0.1669  -0.0499 -0.0526 232 LEU   A N    
1527 C  CA   . LEU   A 232 ? 0.7209 0.5656 0.5154 0.1686  -0.0496 -0.0550 232 LEU   A CA   
1528 C  C    . LEU   A 232 ? 0.7629 0.5970 0.5448 0.1726  -0.0455 -0.0579 232 LEU   A C    
1529 O  O    . LEU   A 232 ? 0.7944 0.6051 0.5555 0.1708  -0.0433 -0.0604 232 LEU   A O    
1530 C  CB   . LEU   A 232 ? 0.7207 0.5558 0.5109 0.1757  -0.0569 -0.0536 232 LEU   A CB   
1531 C  CG   . LEU   A 232 ? 0.7305 0.5680 0.5261 0.1711  -0.0611 -0.0515 232 LEU   A CG   
1532 C  CD1  . LEU   A 232 ? 0.7248 0.5545 0.5172 0.1790  -0.0698 -0.0502 232 LEU   A CD1  
1533 C  CD2  . LEU   A 232 ? 0.7531 0.5740 0.5335 0.1623  -0.0566 -0.0527 232 LEU   A CD2  
1534 N  N    . ASP   A 233 ? 0.7587 0.6087 0.5518 0.1772  -0.0438 -0.0576 233 ASP   A N    
1535 C  CA   . ASP   A 233 ? 0.7896 0.6296 0.5700 0.1807  -0.0394 -0.0605 233 ASP   A CA   
1536 C  C    . ASP   A 233 ? 0.8124 0.6443 0.5825 0.1698  -0.0341 -0.0635 233 ASP   A C    
1537 O  O    . ASP   A 233 ? 0.8316 0.6430 0.5822 0.1694  -0.0313 -0.0667 233 ASP   A O    
1538 C  CB   . ASP   A 233 ? 0.8148 0.6748 0.6102 0.1878  -0.0380 -0.0592 233 ASP   A CB   
1539 C  CG   . ASP   A 233 ? 0.9102 0.7807 0.7182 0.1989  -0.0428 -0.0563 233 ASP   A CG   
1540 O  OD1  . ASP   A 233 ? 0.9504 0.8064 0.7489 0.2044  -0.0474 -0.0564 233 ASP   A OD1  
1541 O  OD2  . ASP   A 233 ? 0.9264 0.8196 0.7537 0.2023  -0.0419 -0.0539 233 ASP   A OD2  
1542 N  N    . VAL   A 234 ? 0.8040 0.6514 0.5871 0.1609  -0.0332 -0.0624 234 VAL   A N    
1543 C  CA   . VAL   A 234 ? 0.8070 0.6518 0.5851 0.1501  -0.0290 -0.0648 234 VAL   A CA   
1544 C  C    . VAL   A 234 ? 0.8205 0.6488 0.5873 0.1422  -0.0283 -0.0656 234 VAL   A C    
1545 O  O    . VAL   A 234 ? 0.8301 0.6409 0.5809 0.1370  -0.0250 -0.0688 234 VAL   A O    
1546 C  CB   . VAL   A 234 ? 0.7936 0.6636 0.5910 0.1454  -0.0282 -0.0630 234 VAL   A CB   
1547 C  CG1  . VAL   A 234 ? 0.8053 0.6740 0.5986 0.1347  -0.0248 -0.0656 234 VAL   A CG1  
1548 C  CG2  . VAL   A 234 ? 0.7882 0.6734 0.5956 0.1528  -0.0277 -0.0619 234 VAL   A CG2  
1549 N  N    . ILE   A 235 ? 0.8185 0.6520 0.5933 0.1409  -0.0309 -0.0629 235 ILE   A N    
1550 C  CA   . ILE   A 235 ? 0.8422 0.6615 0.6073 0.1335  -0.0292 -0.0632 235 ILE   A CA   
1551 C  C    . ILE   A 235 ? 0.8703 0.6623 0.6144 0.1378  -0.0302 -0.0640 235 ILE   A C    
1552 O  O    . ILE   A 235 ? 0.8829 0.6585 0.6145 0.1317  -0.0273 -0.0648 235 ILE   A O    
1553 C  CB   . ILE   A 235 ? 0.8376 0.6713 0.6172 0.1300  -0.0308 -0.0601 235 ILE   A CB   
1554 C  CG1  . ILE   A 235 ? 0.8433 0.6786 0.6275 0.1380  -0.0371 -0.0573 235 ILE   A CG1  
1555 C  CG2  . ILE   A 235 ? 0.8300 0.6884 0.6280 0.1255  -0.0294 -0.0594 235 ILE   A CG2  
1556 C  CD1  . ILE   A 235 ? 0.8607 0.6962 0.6480 0.1345  -0.0386 -0.0550 235 ILE   A CD1  
1557 N  N    . GLY   A 236 ? 0.8799 0.6674 0.6204 0.1485  -0.0340 -0.0637 236 GLY   A N    
1558 C  CA   . GLY   A 236 ? 0.9047 0.6667 0.6251 0.1547  -0.0360 -0.0642 236 GLY   A CA   
1559 C  C    . GLY   A 236 ? 0.9268 0.6867 0.6487 0.1580  -0.0414 -0.0615 236 GLY   A C    
1560 O  O    . GLY   A 236 ? 0.9223 0.6969 0.6580 0.1534  -0.0424 -0.0595 236 GLY   A O    
1561 N  N    . LEU   A 237 ? 0.9465 0.6870 0.6530 0.1666  -0.0453 -0.0615 237 LEU   A N    
1562 C  CA   . LEU   A 237 ? 0.9593 0.6938 0.6633 0.1705  -0.0514 -0.0592 237 LEU   A CA   
1563 C  C    . LEU   A 237 ? 0.9811 0.6994 0.6720 0.1615  -0.0473 -0.0593 237 LEU   A C    
1564 O  O    . LEU   A 237 ? 1.0018 0.7001 0.6748 0.1569  -0.0412 -0.0613 237 LEU   A O    
1565 C  CB   . LEU   A 237 ? 0.9724 0.6890 0.6616 0.1825  -0.0569 -0.0594 237 LEU   A CB   
1566 C  CG   . LEU   A 237 ? 0.9804 0.7116 0.6844 0.1918  -0.0665 -0.0570 237 LEU   A CG   
1567 C  CD1  . LEU   A 237 ? 0.9746 0.7312 0.6999 0.1968  -0.0672 -0.0565 237 LEU   A CD1  
1568 C  CD2  . LEU   A 237 ? 1.0014 0.7098 0.6865 0.2020  -0.0727 -0.0569 237 LEU   A CD2  
1569 N  N    . PRO   A 238 ? 0.9742 0.7015 0.6744 0.1582  -0.0496 -0.0571 238 PRO   A N    
1570 C  CA   . PRO   A 238 ? 0.9902 0.7024 0.6779 0.1501  -0.0444 -0.0569 238 PRO   A CA   
1571 C  C    . PRO   A 238 ? 1.0232 0.7047 0.6852 0.1551  -0.0466 -0.0568 238 PRO   A C    
1572 O  O    . PRO   A 238 ? 1.0257 0.7019 0.6836 0.1652  -0.0545 -0.0562 238 PRO   A O    
1573 C  CB   . PRO   A 238 ? 0.9801 0.7120 0.6858 0.1470  -0.0468 -0.0546 238 PRO   A CB   
1574 C  CG   . PRO   A 238 ? 0.9716 0.7173 0.6904 0.1557  -0.0561 -0.0531 238 PRO   A CG   
1575 C  CD   . PRO   A 238 ? 0.9493 0.6989 0.6703 0.1617  -0.0566 -0.0546 238 PRO   A CD   
1576 N  N    . GLY   A 239 ? 1.0418 0.7043 0.6876 0.1481  -0.0396 -0.0570 239 GLY   A N    
1577 C  CA   . GLY   A 239 ? 1.0740 0.7051 0.6930 0.1519  -0.0404 -0.0565 239 GLY   A CA   
1578 C  C    . GLY   A 239 ? 1.0784 0.7109 0.6993 0.1588  -0.0497 -0.0544 239 GLY   A C    
1579 O  O    . GLY   A 239 ? 1.0732 0.7284 0.7143 0.1565  -0.0523 -0.0531 239 GLY   A O    
1580 N  N    . GLU   A 240 ? 1.0877 0.6962 0.6875 0.1675  -0.0555 -0.0541 240 GLU   A N    
1581 C  CA   . GLU   A 240 ? 1.0947 0.7020 0.6940 0.1746  -0.0661 -0.0524 240 GLU   A CA   
1582 C  C    . GLU   A 240 ? 1.0930 0.7015 0.6935 0.1682  -0.0640 -0.0508 240 GLU   A C    
1583 O  O    . GLU   A 240 ? 1.0847 0.7051 0.6964 0.1710  -0.0724 -0.0495 240 GLU   A O    
1584 C  CB   . GLU   A 240 ? 1.1478 0.7245 0.7196 0.1845  -0.0718 -0.0526 240 GLU   A CB   
1585 C  CG   . GLU   A 240 ? 1.2137 0.7942 0.7894 0.1943  -0.0858 -0.0515 240 GLU   A CG   
1586 C  CD   . GLU   A 240 ? 1.2849 0.8853 0.8790 0.2031  -0.0944 -0.0518 240 GLU   A CD   
1587 O  OE1  . GLU   A 240 ? 1.2847 0.9079 0.9004 0.2051  -0.1030 -0.0507 240 GLU   A OE1  
1588 O  OE2  . GLU   A 240 ? 1.3114 0.9027 0.8967 0.2086  -0.0929 -0.0530 240 GLU   A OE2  
1589 N  N    . GLU   A 241 ? 1.0985 0.6954 0.6885 0.1595  -0.0526 -0.0509 241 GLU   A N    
1590 C  CA   . GLU   A 241 ? 1.1058 0.7025 0.6955 0.1533  -0.0481 -0.0494 241 GLU   A CA   
1591 C  C    . GLU   A 241 ? 1.0799 0.7103 0.6997 0.1479  -0.0478 -0.0488 241 GLU   A C    
1592 O  O    . GLU   A 241 ? 1.0815 0.7155 0.7046 0.1456  -0.0477 -0.0473 241 GLU   A O    
1593 C  CB   . GLU   A 241 ? 1.1624 0.7381 0.7335 0.1457  -0.0350 -0.0495 241 GLU   A CB   
1594 C  CG   . GLU   A 241 ? 1.2235 0.8118 0.8063 0.1366  -0.0250 -0.0510 241 GLU   A CG   
1595 C  CD   . GLU   A 241 ? 1.3383 0.9182 0.9138 0.1386  -0.0247 -0.0531 241 GLU   A CD   
1596 O  OE1  . GLU   A 241 ? 1.3776 0.9313 0.9298 0.1458  -0.0280 -0.0533 241 GLU   A OE1  
1597 O  OE2  . GLU   A 241 ? 1.3564 0.9544 0.9479 0.1332  -0.0211 -0.0546 241 GLU   A OE2  
1598 N  N    . ASP   A 242 ? 1.0506 0.7039 0.6906 0.1462  -0.0472 -0.0499 242 ASP   A N    
1599 C  CA   . ASP   A 242 ? 1.0235 0.7088 0.6917 0.1418  -0.0469 -0.0493 242 ASP   A CA   
1600 C  C    . ASP   A 242 ? 0.9999 0.7033 0.6849 0.1485  -0.0582 -0.0484 242 ASP   A C    
1601 O  O    . ASP   A 242 ? 0.9870 0.7160 0.6947 0.1456  -0.0587 -0.0477 242 ASP   A O    
1602 C  CB   . ASP   A 242 ? 1.0341 0.7327 0.7129 0.1361  -0.0398 -0.0511 242 ASP   A CB   
1603 C  CG   . ASP   A 242 ? 1.0925 0.7823 0.7633 0.1268  -0.0284 -0.0519 242 ASP   A CG   
1604 O  OD1  . ASP   A 242 ? 1.0997 0.7865 0.7682 0.1226  -0.0240 -0.0505 242 ASP   A OD1  
1605 O  OD2  . ASP   A 242 ? 1.1252 0.8129 0.7938 0.1235  -0.0236 -0.0539 242 ASP   A OD2  
1606 N  N    . TRP   A 243 ? 0.9945 0.6854 0.6694 0.1573  -0.0672 -0.0484 243 TRP   A N    
1607 C  CA   . TRP   A 243 ? 0.9798 0.6895 0.6729 0.1631  -0.0780 -0.0474 243 TRP   A CA   
1608 C  C    . TRP   A 243 ? 1.0100 0.7167 0.7019 0.1632  -0.0846 -0.0458 243 TRP   A C    
1609 O  O    . TRP   A 243 ? 1.0314 0.7124 0.7000 0.1645  -0.0849 -0.0458 243 TRP   A O    
1610 C  CB   . TRP   A 243 ? 0.9594 0.6628 0.6474 0.1730  -0.0853 -0.0482 243 TRP   A CB   
1611 C  CG   . TRP   A 243 ? 0.9137 0.6438 0.6271 0.1777  -0.0933 -0.0474 243 TRP   A CG   
1612 C  CD1  . TRP   A 243 ? 0.9097 0.6468 0.6318 0.1824  -0.1046 -0.0461 243 TRP   A CD1  
1613 C  CD2  . TRP   A 243 ? 0.8820 0.6350 0.6150 0.1779  -0.0903 -0.0477 243 TRP   A CD2  
1614 N  NE1  . TRP   A 243 ? 0.8865 0.6509 0.6344 0.1849  -0.1082 -0.0453 243 TRP   A NE1  
1615 C  CE2  . TRP   A 243 ? 0.8718 0.6460 0.6261 0.1826  -0.0992 -0.0462 243 TRP   A CE2  
1616 C  CE3  . TRP   A 243 ? 0.8769 0.6345 0.6116 0.1743  -0.0810 -0.0491 243 TRP   A CE3  
1617 C  CZ2  . TRP   A 243 ? 0.8547 0.6534 0.6307 0.1845  -0.0981 -0.0458 243 TRP   A CZ2  
1618 C  CZ3  . TRP   A 243 ? 0.8676 0.6484 0.6223 0.1764  -0.0806 -0.0490 243 TRP   A CZ3  
1619 C  CH2  . TRP   A 243 ? 0.8550 0.6558 0.6297 0.1817  -0.0886 -0.0473 243 TRP   A CH2  
1620 N  N    . PRO   A 244 ? 1.0121 0.7427 0.7268 0.1615  -0.0892 -0.0444 244 PRO   A N    
1621 C  CA   . PRO   A 244 ? 1.0311 0.7566 0.7428 0.1610  -0.0954 -0.0431 244 PRO   A CA   
1622 C  C    . PRO   A 244 ? 1.0679 0.7777 0.7672 0.1689  -0.1078 -0.0432 244 PRO   A C    
1623 O  O    . PRO   A 244 ? 1.0575 0.7769 0.7669 0.1749  -0.1157 -0.0434 244 PRO   A O    
1624 C  CB   . PRO   A 244 ? 1.0146 0.7698 0.7544 0.1571  -0.0970 -0.0417 244 PRO   A CB   
1625 C  CG   . PRO   A 244 ? 1.0029 0.7775 0.7599 0.1597  -0.0972 -0.0421 244 PRO   A CG   
1626 C  CD   . PRO   A 244 ? 0.9878 0.7490 0.7301 0.1598  -0.0888 -0.0439 244 PRO   A CD   
1627 N  N    . ARG   A 245 ? 1.1105 0.7957 0.7872 0.1693  -0.1093 -0.0430 245 ARG   A N    
1628 C  CA   . ARG   A 245 ? 1.1536 0.8203 0.8147 0.1768  -0.1217 -0.0433 245 ARG   A CA   
1629 C  C    . ARG   A 245 ? 1.1545 0.8375 0.8334 0.1770  -0.1336 -0.0424 245 ARG   A C    
1630 O  O    . ARG   A 245 ? 1.1482 0.8471 0.8424 0.1706  -0.1306 -0.0413 245 ARG   A O    
1631 C  CB   . ARG   A 245 ? 1.2139 0.8460 0.8417 0.1773  -0.1184 -0.0435 245 ARG   A CB   
1632 C  CG   . ARG   A 245 ? 1.3033 0.9141 0.9096 0.1792  -0.1100 -0.0444 245 ARG   A CG   
1633 C  CD   . ARG   A 245 ? 1.3920 0.9828 0.9784 0.1735  -0.0974 -0.0440 245 ARG   A CD   
1634 N  NE   . ARG   A 245 ? 1.4680 1.0407 1.0366 0.1733  -0.0878 -0.0447 245 ARG   A NE   
1635 C  CZ   . ARG   A 245 ? 1.5063 1.0910 1.0857 0.1671  -0.0767 -0.0453 245 ARG   A CZ   
1636 N  NH1  . ARG   A 245 ? 1.4852 1.1005 1.0927 0.1613  -0.0739 -0.0450 245 ARG   A NH1  
1637 N  NH2  . ARG   A 245 ? 1.5227 1.0880 1.0839 0.1666  -0.0687 -0.0461 245 ARG   A NH2  
1638 N  N    . ASP   A 246 ? 1.1582 0.8377 0.8358 0.1845  -0.1472 -0.0428 246 ASP   A N    
1639 C  CA   . ASP   A 246 ? 1.1546 0.8475 0.8481 0.1853  -0.1609 -0.0421 246 ASP   A CA   
1640 C  C    . ASP   A 246 ? 1.1154 0.8450 0.8450 0.1814  -0.1605 -0.0410 246 ASP   A C    
1641 O  O    . ASP   A 246 ? 1.1076 0.8501 0.8522 0.1778  -0.1673 -0.0400 246 ASP   A O    
1642 C  CB   . ASP   A 246 ? 1.2026 0.8783 0.8808 0.1819  -0.1645 -0.0419 246 ASP   A CB   
1643 C  CG   . ASP   A 246 ? 1.3190 0.9579 0.9613 0.1875  -0.1681 -0.0429 246 ASP   A CG   
1644 O  OD1  . ASP   A 246 ? 1.3475 0.9667 0.9685 0.1864  -0.1562 -0.0431 246 ASP   A OD1  
1645 O  OD2  . ASP   A 246 ? 1.3628 0.9922 0.9979 0.1929  -0.1828 -0.0435 246 ASP   A OD2  
1646 N  N    . VAL   A 247 ? 1.0873 0.8322 0.8295 0.1825  -0.1531 -0.0410 247 VAL   A N    
1647 C  CA   . VAL   A 247 ? 1.0544 0.8328 0.8290 0.1803  -0.1522 -0.0399 247 VAL   A CA   
1648 C  C    . VAL   A 247 ? 1.0405 0.8289 0.8263 0.1889  -0.1616 -0.0400 247 VAL   A C    
1649 O  O    . VAL   A 247 ? 1.0577 0.8268 0.8245 0.1964  -0.1651 -0.0412 247 VAL   A O    
1650 C  CB   . VAL   A 247 ? 1.0477 0.8395 0.8315 0.1752  -0.1377 -0.0397 247 VAL   A CB   
1651 C  CG1  . VAL   A 247 ? 1.0551 0.8414 0.8323 0.1669  -0.1294 -0.0392 247 VAL   A CG1  
1652 C  CG2  . VAL   A 247 ? 1.0604 0.8409 0.8307 0.1796  -0.1310 -0.0413 247 VAL   A CG2  
1653 N  N    . ALA   A 248 ? 1.0053 0.8233 0.8213 0.1882  -0.1650 -0.0386 248 ALA   A N    
1654 C  CA   . ALA   A 248 ? 0.9852 0.8184 0.8174 0.1961  -0.1731 -0.0382 248 ALA   A CA   
1655 C  C    . ALA   A 248 ? 0.9744 0.8069 0.8026 0.2028  -0.1655 -0.0392 248 ALA   A C    
1656 O  O    . ALA   A 248 ? 0.9883 0.8127 0.8092 0.2123  -0.1723 -0.0399 248 ALA   A O    
1657 C  CB   . ALA   A 248 ? 0.9670 0.8327 0.8331 0.1922  -0.1758 -0.0361 248 ALA   A CB   
1658 N  N    . LEU   A 249 ? 0.9503 0.7901 0.7819 0.1981  -0.1520 -0.0392 249 LEU   A N    
1659 C  CA   . LEU   A 249 ? 0.9359 0.7745 0.7630 0.2031  -0.1439 -0.0403 249 LEU   A CA   
1660 C  C    . LEU   A 249 ? 0.9348 0.7417 0.7295 0.2043  -0.1387 -0.0423 249 LEU   A C    
1661 O  O    . LEU   A 249 ? 0.9469 0.7432 0.7300 0.1965  -0.1309 -0.0428 249 LEU   A O    
1662 C  CB   . LEU   A 249 ? 0.9319 0.7921 0.7766 0.1975  -0.1327 -0.0395 249 LEU   A CB   
1663 C  CG   . LEU   A 249 ? 0.9388 0.8309 0.8155 0.1967  -0.1350 -0.0372 249 LEU   A CG   
1664 C  CD1  . LEU   A 249 ? 0.9408 0.8477 0.8288 0.1879  -0.1247 -0.0363 249 LEU   A CD1  
1665 C  CD2  . LEU   A 249 ? 0.9421 0.8467 0.8303 0.2064  -0.1361 -0.0370 249 LEU   A CD2  
1666 N  N    . PRO   A 250 ? 0.9241 0.7155 0.7040 0.2139  -0.1420 -0.0435 250 PRO   A N    
1667 C  CA   . PRO   A 250 ? 0.9324 0.6921 0.6804 0.2144  -0.1361 -0.0453 250 PRO   A CA   
1668 C  C    . PRO   A 250 ? 0.9129 0.6729 0.6580 0.2118  -0.1232 -0.0465 250 PRO   A C    
1669 O  O    . PRO   A 250 ? 0.8866 0.6691 0.6518 0.2129  -0.1202 -0.0461 250 PRO   A O    
1670 C  CB   . PRO   A 250 ? 0.9548 0.6974 0.6880 0.2264  -0.1462 -0.0458 250 PRO   A CB   
1671 C  CG   . PRO   A 250 ? 0.9454 0.7158 0.7062 0.2334  -0.1532 -0.0447 250 PRO   A CG   
1672 C  CD   . PRO   A 250 ? 0.9091 0.7105 0.7000 0.2250  -0.1511 -0.0431 250 PRO   A CD   
1673 N  N    . ARG   A 251 ? 0.9230 0.6569 0.6423 0.2085  -0.1156 -0.0480 251 ARG   A N    
1674 C  CA   . ARG   A 251 ? 0.9288 0.6575 0.6407 0.2052  -0.1041 -0.0496 251 ARG   A CA   
1675 C  C    . ARG   A 251 ? 0.9503 0.6778 0.6603 0.2155  -0.1050 -0.0506 251 ARG   A C    
1676 O  O    . ARG   A 251 ? 0.9470 0.6808 0.6607 0.2137  -0.0970 -0.0517 251 ARG   A O    
1677 C  CB   . ARG   A 251 ? 0.9486 0.6464 0.6314 0.2004  -0.0976 -0.0507 251 ARG   A CB   
1678 C  CG   . ARG   A 251 ? 0.9855 0.6788 0.6621 0.1939  -0.0855 -0.0524 251 ARG   A CG   
1679 C  CD   . ARG   A 251 ? 1.0490 0.7084 0.6946 0.1961  -0.0817 -0.0540 251 ARG   A CD   
1680 N  NE   . ARG   A 251 ? 1.1012 0.7573 0.7422 0.1906  -0.0714 -0.0559 251 ARG   A NE   
1681 C  CZ   . ARG   A 251 ? 1.1516 0.7800 0.7675 0.1918  -0.0667 -0.0576 251 ARG   A CZ   
1682 N  NH1  . ARG   A 251 ? 1.1766 0.7778 0.7687 0.1989  -0.0710 -0.0573 251 ARG   A NH1  
1683 N  NH2  . ARG   A 251 ? 1.1509 0.7778 0.7643 0.1856  -0.0580 -0.0595 251 ARG   A NH2  
1684 N  N    . GLN   A 252 ? 0.9674 0.6857 0.6704 0.2264  -0.1148 -0.0502 252 GLN   A N    
1685 C  CA   . GLN   A 252 ? 0.9857 0.7004 0.6848 0.2379  -0.1163 -0.0510 252 GLN   A CA   
1686 C  C    . GLN   A 252 ? 0.9718 0.7202 0.7026 0.2436  -0.1203 -0.0496 252 GLN   A C    
1687 O  O    . GLN   A 252 ? 0.9696 0.7191 0.7006 0.2535  -0.1204 -0.0501 252 GLN   A O    
1688 C  CB   . GLN   A 252 ? 1.0304 0.7160 0.7036 0.2482  -0.1241 -0.0514 252 GLN   A CB   
1689 C  CG   . GLN   A 252 ? 1.0882 0.7581 0.7484 0.2468  -0.1321 -0.0506 252 GLN   A CG   
1690 C  CD   . GLN   A 252 ? 1.1509 0.7985 0.7899 0.2361  -0.1240 -0.0511 252 GLN   A CD   
1691 O  OE1  . GLN   A 252 ? 1.1523 0.8061 0.7978 0.2286  -0.1252 -0.0502 252 GLN   A OE1  
1692 N  NE2  . GLN   A 252 ? 1.1819 0.8015 0.7939 0.2356  -0.1160 -0.0525 252 GLN   A NE2  
1693 N  N    . ALA   A 253 ? 0.9631 0.7385 0.7200 0.2370  -0.1219 -0.0479 253 ALA   A N    
1694 C  CA   . ALA   A 253 ? 0.9524 0.7607 0.7404 0.2408  -0.1238 -0.0463 253 ALA   A CA   
1695 C  C    . ALA   A 253 ? 0.9508 0.7703 0.7457 0.2378  -0.1120 -0.0470 253 ALA   A C    
1696 O  O    . ALA   A 253 ? 0.9348 0.7795 0.7527 0.2411  -0.1109 -0.0457 253 ALA   A O    
1697 C  CB   . ALA   A 253 ? 0.9412 0.7715 0.7524 0.2342  -0.1295 -0.0441 253 ALA   A CB   
1698 N  N    . PHE   A 254 ? 0.9693 0.7693 0.7436 0.2313  -0.1032 -0.0491 254 PHE   A N    
1699 C  CA   . PHE   A 254 ? 0.9809 0.7855 0.7558 0.2271  -0.0924 -0.0504 254 PHE   A CA   
1700 C  C    . PHE   A 254 ? 1.0370 0.8112 0.7822 0.2299  -0.0875 -0.0532 254 PHE   A C    
1701 O  O    . PHE   A 254 ? 1.0555 0.8042 0.7785 0.2285  -0.0889 -0.0540 254 PHE   A O    
1702 C  CB   . PHE   A 254 ? 0.9593 0.7738 0.7420 0.2134  -0.0865 -0.0501 254 PHE   A CB   
1703 C  CG   . PHE   A 254 ? 0.9334 0.7735 0.7418 0.2095  -0.0912 -0.0474 254 PHE   A CG   
1704 C  CD1  . PHE   A 254 ? 0.9175 0.7855 0.7507 0.2103  -0.0894 -0.0457 254 PHE   A CD1  
1705 C  CD2  . PHE   A 254 ? 0.9373 0.7718 0.7433 0.2051  -0.0970 -0.0464 254 PHE   A CD2  
1706 C  CE1  . PHE   A 254 ? 0.9068 0.7969 0.7628 0.2062  -0.0934 -0.0431 254 PHE   A CE1  
1707 C  CE2  . PHE   A 254 ? 0.9298 0.7858 0.7580 0.2013  -0.1014 -0.0440 254 PHE   A CE2  
1708 C  CZ   . PHE   A 254 ? 0.9076 0.7913 0.7609 0.2016  -0.0996 -0.0423 254 PHE   A CZ   
1709 N  N    . HIS   A 255 ? 1.0629 0.8387 0.8069 0.2346  -0.0818 -0.0545 255 HIS   A N    
1710 C  CA   . HIS   A 255 ? 1.1095 0.8568 0.8258 0.2378  -0.0769 -0.0573 255 HIS   A CA   
1711 C  C    . HIS   A 255 ? 1.1273 0.8772 0.8424 0.2301  -0.0668 -0.0593 255 HIS   A C    
1712 O  O    . HIS   A 255 ? 1.1360 0.8739 0.8380 0.2352  -0.0626 -0.0614 255 HIS   A O    
1713 C  CB   . HIS   A 255 ? 1.1341 0.8752 0.8450 0.2538  -0.0813 -0.0572 255 HIS   A CB   
1714 C  CG   . HIS   A 255 ? 1.1602 0.9200 0.8910 0.2622  -0.0916 -0.0544 255 HIS   A CG   
1715 N  ND1  . HIS   A 255 ? 1.1643 0.9563 0.9245 0.2665  -0.0925 -0.0525 255 HIS   A ND1  
1716 C  CD2  . HIS   A 255 ? 1.1817 0.9326 0.9073 0.2661  -0.1012 -0.0534 255 HIS   A CD2  
1717 C  CE1  . HIS   A 255 ? 1.1648 0.9672 0.9379 0.2724  -0.1028 -0.0503 255 HIS   A CE1  
1718 N  NE2  . HIS   A 255 ? 1.1783 0.9565 0.9310 0.2726  -0.1089 -0.0509 255 HIS   A NE2  
1719 N  N    . SER   A 256 ? 1.1312 0.8956 0.8587 0.2178  -0.0635 -0.0589 256 SER   A N    
1720 C  CA   . SER   A 256 ? 1.1435 0.9133 0.8723 0.2088  -0.0552 -0.0607 256 SER   A CA   
1721 C  C    . SER   A 256 ? 1.1790 0.9203 0.8817 0.2010  -0.0499 -0.0637 256 SER   A C    
1722 O  O    . SER   A 256 ? 1.1745 0.9186 0.8786 0.1894  -0.0450 -0.0648 256 SER   A O    
1723 C  CB   . SER   A 256 ? 1.1354 0.9312 0.8874 0.1999  -0.0548 -0.0588 256 SER   A CB   
1724 O  OG   . SER   A 256 ? 1.1434 0.9641 0.9190 0.2062  -0.0594 -0.0559 256 SER   A OG   
1725 N  N    . LYS   A 257 ? 1.2094 0.9234 0.8887 0.2082  -0.0509 -0.0650 257 LYS   A N    
1726 C  CA   . LYS   A 257 ? 1.2479 0.9290 0.8982 0.2040  -0.0466 -0.0676 257 LYS   A CA   
1727 C  C    . LYS   A 257 ? 1.2576 0.9361 0.9051 0.1882  -0.0398 -0.0693 257 LYS   A C    
1728 O  O    . LYS   A 257 ? 1.2686 0.9406 0.9126 0.1810  -0.0396 -0.0683 257 LYS   A O    
1729 C  CB   . LYS   A 257 ? 1.2868 0.9502 0.9195 0.2129  -0.0443 -0.0700 257 LYS   A CB   
1730 N  N    . SER   A 258 ? 1.2434 0.9279 0.8933 0.1833  -0.0347 -0.0716 258 SER   A N    
1731 C  CA   . SER   A 258 ? 1.2390 0.9217 0.8866 0.1689  -0.0287 -0.0736 258 SER   A CA   
1732 C  C    . SER   A 258 ? 1.2035 0.9174 0.8767 0.1617  -0.0280 -0.0727 258 SER   A C    
1733 O  O    . SER   A 258 ? 1.1941 0.9306 0.8852 0.1676  -0.0303 -0.0712 258 SER   A O    
1734 C  CB   . SER   A 258 ? 1.2766 0.9394 0.9047 0.1674  -0.0241 -0.0775 258 SER   A CB   
1735 O  OG   . SER   A 258 ? 1.3145 0.9743 0.9399 0.1530  -0.0190 -0.0798 258 SER   A OG   
1736 N  N    . ALA   A 259 ? 1.1808 0.8949 0.8548 0.1488  -0.0242 -0.0734 259 ALA   A N    
1737 C  CA   . ALA   A 259 ? 1.1481 0.8871 0.8421 0.1402  -0.0226 -0.0730 259 ALA   A CA   
1738 C  C    . ALA   A 259 ? 1.1344 0.8738 0.8248 0.1362  -0.0193 -0.0765 259 ALA   A C    
1739 O  O    . ALA   A 259 ? 1.1506 0.8683 0.8224 0.1312  -0.0161 -0.0796 259 ALA   A O    
1740 C  CB   . ALA   A 259 ? 1.1486 0.8840 0.8421 0.1290  -0.0198 -0.0726 259 ALA   A CB   
1741 N  N    . GLN   A 260 ? 1.1048 0.8674 0.8117 0.1387  -0.0203 -0.0759 260 GLN   A N    
1742 C  CA   . GLN   A 260 ? 1.0911 0.8555 0.7950 0.1359  -0.0179 -0.0791 260 GLN   A CA   
1743 C  C    . GLN   A 260 ? 1.0722 0.8483 0.7849 0.1226  -0.0159 -0.0803 260 GLN   A C    
1744 O  O    . GLN   A 260 ? 1.0671 0.8592 0.7953 0.1185  -0.0166 -0.0777 260 GLN   A O    
1745 C  CB   . GLN   A 260 ? 1.0838 0.8664 0.7997 0.1458  -0.0193 -0.0777 260 GLN   A CB   
1746 C  CG   . GLN   A 260 ? 1.0963 0.8689 0.8041 0.1595  -0.0208 -0.0770 260 GLN   A CG   
1747 C  CD   . GLN   A 260 ? 1.1100 0.9022 0.8312 0.1684  -0.0208 -0.0755 260 GLN   A CD   
1748 O  OE1  . GLN   A 260 ? 1.1019 0.9100 0.8389 0.1757  -0.0235 -0.0719 260 GLN   A OE1  
1749 N  NE2  . GLN   A 260 ? 1.1154 0.9066 0.8304 0.1679  -0.0177 -0.0781 260 GLN   A NE2  
1750 N  N    . PRO   A 261 ? 1.0595 0.8279 0.7625 0.1157  -0.0138 -0.0843 261 PRO   A N    
1751 C  CA   . PRO   A 261 ? 1.0404 0.8227 0.7543 0.1036  -0.0129 -0.0853 261 PRO   A CA   
1752 C  C    . PRO   A 261 ? 1.0121 0.8234 0.7470 0.1062  -0.0149 -0.0830 261 PRO   A C    
1753 O  O    . PRO   A 261 ? 1.0056 0.8228 0.7416 0.1147  -0.0157 -0.0827 261 PRO   A O    
1754 C  CB   . PRO   A 261 ? 1.0604 0.8264 0.7578 0.0973  -0.0115 -0.0903 261 PRO   A CB   
1755 C  CG   . PRO   A 261 ? 1.0786 0.8299 0.7609 0.1085  -0.0117 -0.0915 261 PRO   A CG   
1756 C  CD   . PRO   A 261 ? 1.0629 0.8104 0.7454 0.1190  -0.0126 -0.0880 261 PRO   A CD   
1757 N  N    . ILE   A 262 ? 0.9888 0.8175 0.7401 0.0997  -0.0151 -0.0809 262 ILE   A N    
1758 C  CA   . ILE   A 262 ? 0.9663 0.8215 0.7372 0.1017  -0.0168 -0.0782 262 ILE   A CA   
1759 C  C    . ILE   A 262 ? 0.9488 0.8125 0.7203 0.0996  -0.0172 -0.0807 262 ILE   A C    
1760 O  O    . ILE   A 262 ? 0.9360 0.8151 0.7170 0.1058  -0.0182 -0.0787 262 ILE   A O    
1761 C  CB   . ILE   A 262 ? 0.9657 0.8345 0.7515 0.0960  -0.0167 -0.0753 262 ILE   A CB   
1762 C  CG1  . ILE   A 262 ? 0.9630 0.8556 0.7675 0.1008  -0.0187 -0.0714 262 ILE   A CG1  
1763 C  CG2  . ILE   A 262 ? 0.9697 0.8397 0.7567 0.0839  -0.0150 -0.0776 262 ILE   A CG2  
1764 C  CD1  . ILE   A 262 ? 0.9749 0.8692 0.7837 0.1104  -0.0205 -0.0680 262 ILE   A CD1  
1765 N  N    . GLU   A 263 ? 0.9480 0.8002 0.7081 0.0914  -0.0167 -0.0851 263 GLU   A N    
1766 C  CA   . GLU   A 263 ? 0.9462 0.8029 0.7033 0.0892  -0.0180 -0.0883 263 GLU   A CA   
1767 C  C    . GLU   A 263 ? 0.9446 0.7970 0.6930 0.1004  -0.0178 -0.0886 263 GLU   A C    
1768 O  O    . GLU   A 263 ? 0.9462 0.8072 0.6953 0.1014  -0.0188 -0.0897 263 GLU   A O    
1769 C  CB   . GLU   A 263 ? 0.9754 0.8181 0.7207 0.0778  -0.0181 -0.0933 263 GLU   A CB   
1770 C  CG   . GLU   A 263 ? 1.0334 0.8473 0.7582 0.0770  -0.0159 -0.0958 263 GLU   A CG   
1771 C  CD   . GLU   A 263 ? 1.0977 0.9036 0.8224 0.0668  -0.0137 -0.0960 263 GLU   A CD   
1772 O  OE1  . GLU   A 263 ? 1.0932 0.9105 0.8314 0.0668  -0.0128 -0.0922 263 GLU   A OE1  
1773 O  OE2  . GLU   A 263 ? 1.1374 0.9242 0.8475 0.0588  -0.0127 -0.0999 263 GLU   A OE2  
1774 N  N    . LYS   A 264 ? 0.9430 0.7830 0.6836 0.1094  -0.0165 -0.0874 264 LYS   A N    
1775 C  CA   . LYS   A 264 ? 0.9413 0.7785 0.6757 0.1214  -0.0155 -0.0870 264 LYS   A CA   
1776 C  C    . LYS   A 264 ? 0.9042 0.7670 0.6582 0.1275  -0.0157 -0.0826 264 LYS   A C    
1777 O  O    . LYS   A 264 ? 0.8977 0.7664 0.6506 0.1324  -0.0147 -0.0828 264 LYS   A O    
1778 C  CB   . LYS   A 264 ? 0.9819 0.8014 0.7057 0.1295  -0.0145 -0.0863 264 LYS   A CB   
1779 C  CG   . LYS   A 264 ? 1.0495 0.8683 0.7699 0.1434  -0.0132 -0.0852 264 LYS   A CG   
1780 C  CD   . LYS   A 264 ? 1.1278 0.9256 0.8341 0.1511  -0.0127 -0.0855 264 LYS   A CD   
1781 C  CE   . LYS   A 264 ? 1.1846 0.9715 0.8771 0.1624  -0.0104 -0.0871 264 LYS   A CE   
1782 N  NZ   . LYS   A 264 ? 1.2232 0.9849 0.8974 0.1689  -0.0102 -0.0883 264 LYS   A NZ   
1783 N  N    . PHE   A 265 ? 0.8772 0.7537 0.6479 0.1268  -0.0167 -0.0785 265 PHE   A N    
1784 C  CA   . PHE   A 265 ? 0.8485 0.7478 0.6385 0.1316  -0.0170 -0.0739 265 PHE   A CA   
1785 C  C    . PHE   A 265 ? 0.8267 0.7433 0.6279 0.1248  -0.0178 -0.0733 265 PHE   A C    
1786 O  O    . PHE   A 265 ? 0.8083 0.7410 0.6198 0.1288  -0.0173 -0.0705 265 PHE   A O    
1787 C  CB   . PHE   A 265 ? 0.8398 0.7426 0.6400 0.1339  -0.0185 -0.0702 265 PHE   A CB   
1788 C  CG   . PHE   A 265 ? 0.8593 0.7453 0.6486 0.1416  -0.0185 -0.0707 265 PHE   A CG   
1789 C  CD1  . PHE   A 265 ? 0.8715 0.7624 0.6647 0.1527  -0.0180 -0.0686 265 PHE   A CD1  
1790 C  CD2  . PHE   A 265 ? 0.8835 0.7486 0.6583 0.1379  -0.0188 -0.0731 265 PHE   A CD2  
1791 C  CE1  . PHE   A 265 ? 0.8937 0.7696 0.6769 0.1607  -0.0185 -0.0691 265 PHE   A CE1  
1792 C  CE2  . PHE   A 265 ? 0.9104 0.7584 0.6733 0.1457  -0.0192 -0.0734 265 PHE   A CE2  
1793 C  CZ   . PHE   A 265 ? 0.9076 0.7616 0.6751 0.1574  -0.0194 -0.0715 265 PHE   A CZ   
1794 N  N    . VAL   A 266 ? 0.8301 0.7435 0.6292 0.1146  -0.0190 -0.0756 266 VAL   A N    
1795 C  CA   . VAL   A 266 ? 0.8338 0.7631 0.6432 0.1078  -0.0203 -0.0754 266 VAL   A CA   
1796 C  C    . VAL   A 266 ? 0.8656 0.7858 0.6624 0.1011  -0.0214 -0.0805 266 VAL   A C    
1797 O  O    . VAL   A 266 ? 0.8771 0.7891 0.6699 0.0922  -0.0219 -0.0832 266 VAL   A O    
1798 C  CB   . VAL   A 266 ? 0.8232 0.7609 0.6454 0.1016  -0.0210 -0.0730 266 VAL   A CB   
1799 C  CG1  . VAL   A 266 ? 0.8159 0.7734 0.6513 0.0978  -0.0224 -0.0716 266 VAL   A CG1  
1800 C  CG2  . VAL   A 266 ? 0.8192 0.7583 0.6484 0.1074  -0.0207 -0.0690 266 VAL   A CG2  
1801 N  N    . THR   A 267 ? 0.8786 0.7985 0.6678 0.1053  -0.0214 -0.0821 267 THR   A N    
1802 C  CA   . THR   A 267 ? 0.8972 0.8075 0.6731 0.0990  -0.0234 -0.0873 267 THR   A CA   
1803 C  C    . THR   A 267 ? 0.8922 0.8204 0.6802 0.0919  -0.0265 -0.0872 267 THR   A C    
1804 O  O    . THR   A 267 ? 0.8799 0.8262 0.6817 0.0956  -0.0265 -0.0831 267 THR   A O    
1805 C  CB   . THR   A 267 ? 0.9270 0.8256 0.6860 0.1065  -0.0222 -0.0897 267 THR   A CB   
1806 O  OG1  . THR   A 267 ? 0.9356 0.8496 0.7015 0.1130  -0.0216 -0.0868 267 THR   A OG1  
1807 C  CG2  . THR   A 267 ? 0.9410 0.8225 0.6888 0.1147  -0.0190 -0.0896 267 THR   A CG2  
1808 N  N    . ASP   A 268 ? 0.8987 0.8217 0.6819 0.0816  -0.0293 -0.0915 268 ASP   A N    
1809 C  CA   . ASP   A 268 ? 0.8974 0.8359 0.6910 0.0737  -0.0332 -0.0923 268 ASP   A CA   
1810 C  C    . ASP   A 268 ? 0.8790 0.8294 0.6897 0.0673  -0.0328 -0.0899 268 ASP   A C    
1811 O  O    . ASP   A 268 ? 0.8725 0.8363 0.6930 0.0606  -0.0359 -0.0907 268 ASP   A O    
1812 C  CB   . ASP   A 268 ? 0.9281 0.8823 0.7267 0.0794  -0.0352 -0.0903 268 ASP   A CB   
1813 C  CG   . ASP   A 268 ? 1.0283 0.9713 0.8088 0.0837  -0.0363 -0.0936 268 ASP   A CG   
1814 O  OD1  . ASP   A 268 ? 1.0582 0.9853 0.8239 0.0781  -0.0385 -0.0989 268 ASP   A OD1  
1815 O  OD2  . ASP   A 268 ? 1.0619 1.0117 0.8424 0.0924  -0.0349 -0.0908 268 ASP   A OD2  
1816 N  N    . ILE   A 269 ? 0.8709 0.8164 0.6847 0.0696  -0.0291 -0.0871 269 ILE   A N    
1817 C  CA   . ILE   A 269 ? 0.8590 0.8134 0.6867 0.0640  -0.0279 -0.0848 269 ILE   A CA   
1818 C  C    . ILE   A 269 ? 0.8633 0.8085 0.6868 0.0523  -0.0279 -0.0889 269 ILE   A C    
1819 O  O    . ILE   A 269 ? 0.8762 0.8010 0.6838 0.0502  -0.0270 -0.0923 269 ILE   A O    
1820 C  CB   . ILE   A 269 ? 0.8557 0.8081 0.6879 0.0700  -0.0246 -0.0804 269 ILE   A CB   
1821 C  CG1  . ILE   A 269 ? 0.8576 0.8226 0.7052 0.0657  -0.0235 -0.0775 269 ILE   A CG1  
1822 C  CG2  . ILE   A 269 ? 0.8669 0.7962 0.6839 0.0716  -0.0222 -0.0819 269 ILE   A CG2  
1823 C  CD1  . ILE   A 269 ? 0.8733 0.8402 0.7270 0.0722  -0.0216 -0.0726 269 ILE   A CD1  
1824 N  N    . ASP   A 270 ? 0.8516 0.8121 0.6896 0.0449  -0.0289 -0.0886 270 ASP   A N    
1825 C  CA   . ASP   A 270 ? 0.8613 0.8175 0.6998 0.0329  -0.0284 -0.0919 270 ASP   A CA   
1826 C  C    . ASP   A 270 ? 0.8767 0.8185 0.7114 0.0306  -0.0227 -0.0905 270 ASP   A C    
1827 O  O    . ASP   A 270 ? 0.8831 0.8204 0.7161 0.0387  -0.0202 -0.0871 270 ASP   A O    
1828 C  CB   . ASP   A 270 ? 0.8713 0.8511 0.7289 0.0270  -0.0309 -0.0913 270 ASP   A CB   
1829 C  CG   . ASP   A 270 ? 0.9400 0.9355 0.8135 0.0315  -0.0282 -0.0859 270 ASP   A CG   
1830 O  OD1  . ASP   A 270 ? 0.9544 0.9542 0.8287 0.0413  -0.0285 -0.0825 270 ASP   A OD1  
1831 O  OD2  . ASP   A 270 ? 0.9580 0.9614 0.8431 0.0251  -0.0258 -0.0850 270 ASP   A OD2  
1832 N  N    . GLU   A 271 ? 0.8772 0.8112 0.7101 0.0196  -0.0208 -0.0933 271 GLU   A N    
1833 C  CA   . GLU   A 271 ? 0.8868 0.8048 0.7138 0.0161  -0.0149 -0.0924 271 GLU   A CA   
1834 C  C    . GLU   A 271 ? 0.8618 0.7912 0.7022 0.0190  -0.0111 -0.0874 271 GLU   A C    
1835 O  O    . GLU   A 271 ? 0.8601 0.7758 0.6927 0.0236  -0.0074 -0.0851 271 GLU   A O    
1836 C  CB   . GLU   A 271 ? 0.9431 0.8539 0.7681 0.0021  -0.0134 -0.0963 271 GLU   A CB   
1837 C  CG   . GLU   A 271 ? 1.0685 0.9493 0.8702 -0.0006 -0.0119 -0.0998 271 GLU   A CG   
1838 C  CD   . GLU   A 271 ? 1.1970 1.0695 0.9957 -0.0153 -0.0111 -0.1041 271 GLU   A CD   
1839 O  OE1  . GLU   A 271 ? 1.2196 1.0995 1.0305 -0.0238 -0.0068 -0.1029 271 GLU   A OE1  
1840 O  OE2  . GLU   A 271 ? 1.2319 1.0893 1.0155 -0.0183 -0.0143 -0.1086 271 GLU   A OE2  
1841 N  N    . LEU   A 272 ? 0.8370 0.7907 0.6967 0.0168  -0.0124 -0.0858 272 LEU   A N    
1842 C  CA   . LEU   A 272 ? 0.8193 0.7851 0.6923 0.0194  -0.0089 -0.0813 272 LEU   A CA   
1843 C  C    . LEU   A 272 ? 0.8078 0.7775 0.6814 0.0314  -0.0105 -0.0774 272 LEU   A C    
1844 O  O    . LEU   A 272 ? 0.8113 0.7763 0.6846 0.0353  -0.0070 -0.0741 272 LEU   A O    
1845 C  CB   . LEU   A 272 ? 0.8061 0.7958 0.6989 0.0133  -0.0097 -0.0810 272 LEU   A CB   
1846 C  CG   . LEU   A 272 ? 0.8213 0.8098 0.7176 0.0002  -0.0072 -0.0842 272 LEU   A CG   
1847 C  CD1  . LEU   A 272 ? 0.8127 0.8278 0.7311 -0.0042 -0.0083 -0.0835 272 LEU   A CD1  
1848 C  CD2  . LEU   A 272 ? 0.8359 0.8055 0.7237 -0.0036 0.0009  -0.0831 272 LEU   A CD2  
1849 N  N    . GLY   A 273 ? 0.7911 0.7678 0.6644 0.0368  -0.0155 -0.0780 273 GLY   A N    
1850 C  CA   . GLY   A 273 ? 0.7843 0.7647 0.6582 0.0476  -0.0170 -0.0745 273 GLY   A CA   
1851 C  C    . GLY   A 273 ? 0.7919 0.7523 0.6524 0.0529  -0.0149 -0.0737 273 GLY   A C    
1852 O  O    . GLY   A 273 ? 0.8021 0.7634 0.6655 0.0590  -0.0141 -0.0701 273 GLY   A O    
1853 N  N    . LYS   A 274 ? 0.7900 0.7313 0.6350 0.0503  -0.0143 -0.0773 274 LYS   A N    
1854 C  CA   . LYS   A 274 ? 0.7968 0.7163 0.6265 0.0550  -0.0126 -0.0773 274 LYS   A CA   
1855 C  C    . LYS   A 274 ? 0.7898 0.7020 0.6195 0.0540  -0.0087 -0.0746 274 LYS   A C    
1856 O  O    . LYS   A 274 ? 0.7980 0.7031 0.6235 0.0615  -0.0089 -0.0721 274 LYS   A O    
1857 C  CB   . LYS   A 274 ? 0.8350 0.7351 0.6480 0.0502  -0.0122 -0.0820 274 LYS   A CB   
1858 C  CG   . LYS   A 274 ? 0.9062 0.7807 0.7010 0.0539  -0.0100 -0.0824 274 LYS   A CG   
1859 C  CD   . LYS   A 274 ? 0.9915 0.8462 0.7695 0.0478  -0.0093 -0.0872 274 LYS   A CD   
1860 C  CE   . LYS   A 274 ? 1.0623 0.8896 0.8215 0.0492  -0.0062 -0.0876 274 LYS   A CE   
1861 N  NZ   . LYS   A 274 ? 1.1040 0.9227 0.8543 0.0621  -0.0080 -0.0862 274 LYS   A NZ   
1862 N  N    . ASP   A 275 ? 0.7730 0.6872 0.6075 0.0449  -0.0052 -0.0751 275 ASP   A N    
1863 C  CA   . ASP   A 275 ? 0.7678 0.6748 0.6015 0.0435  -0.0004 -0.0726 275 ASP   A CA   
1864 C  C    . ASP   A 275 ? 0.7453 0.6657 0.5903 0.0502  -0.0012 -0.0682 275 ASP   A C    
1865 O  O    . ASP   A 275 ? 0.7500 0.6587 0.5880 0.0551  -0.0001 -0.0659 275 ASP   A O    
1866 C  CB   . ASP   A 275 ? 0.7878 0.6961 0.6259 0.0321  0.0043  -0.0741 275 ASP   A CB   
1867 C  CG   . ASP   A 275 ? 0.8503 0.7460 0.6832 0.0305  0.0107  -0.0718 275 ASP   A CG   
1868 O  OD1  . ASP   A 275 ? 0.8657 0.7375 0.6807 0.0323  0.0125  -0.0721 275 ASP   A OD1  
1869 O  OD2  . ASP   A 275 ? 0.8671 0.7762 0.7129 0.0281  0.0140  -0.0695 275 ASP   A OD2  
1870 N  N    . LEU   A 276 ? 0.7150 0.6583 0.5760 0.0509  -0.0037 -0.0670 276 LEU   A N    
1871 C  CA   . LEU   A 276 ? 0.6948 0.6505 0.5660 0.0570  -0.0047 -0.0629 276 LEU   A CA   
1872 C  C    . LEU   A 276 ? 0.6889 0.6394 0.5549 0.0662  -0.0084 -0.0613 276 LEU   A C    
1873 O  O    . LEU   A 276 ? 0.6969 0.6444 0.5629 0.0709  -0.0085 -0.0583 276 LEU   A O    
1874 C  CB   . LEU   A 276 ? 0.6760 0.6560 0.5638 0.0560  -0.0067 -0.0622 276 LEU   A CB   
1875 C  CG   . LEU   A 276 ? 0.6726 0.6643 0.5697 0.0628  -0.0081 -0.0579 276 LEU   A CG   
1876 C  CD1  . LEU   A 276 ? 0.6714 0.6578 0.5686 0.0628  -0.0039 -0.0552 276 LEU   A CD1  
1877 C  CD2  . LEU   A 276 ? 0.6602 0.6734 0.5706 0.0630  -0.0108 -0.0573 276 LEU   A CD2  
1878 N  N    . LEU   A 277 ? 0.6722 0.6214 0.5336 0.0687  -0.0115 -0.0634 277 LEU   A N    
1879 C  CA   . LEU   A 277 ? 0.6731 0.6187 0.5310 0.0774  -0.0145 -0.0619 277 LEU   A CA   
1880 C  C    . LEU   A 277 ? 0.6864 0.6113 0.5313 0.0807  -0.0138 -0.0615 277 LEU   A C    
1881 O  O    . LEU   A 277 ? 0.6880 0.6126 0.5342 0.0876  -0.0163 -0.0589 277 LEU   A O    
1882 C  CB   . LEU   A 277 ? 0.6727 0.6196 0.5268 0.0794  -0.0166 -0.0645 277 LEU   A CB   
1883 C  CG   . LEU   A 277 ? 0.6902 0.6340 0.5410 0.0885  -0.0188 -0.0632 277 LEU   A CG   
1884 C  CD1  . LEU   A 277 ? 0.6904 0.6513 0.5548 0.0932  -0.0207 -0.0594 277 LEU   A CD1  
1885 C  CD2  . LEU   A 277 ? 0.7023 0.6426 0.5454 0.0900  -0.0195 -0.0663 277 LEU   A CD2  
1886 N  N    . LEU   A 278 ? 0.6984 0.6061 0.5308 0.0759  -0.0108 -0.0641 278 LEU   A N    
1887 C  CA   . LEU   A 278 ? 0.7232 0.6088 0.5406 0.0790  -0.0101 -0.0639 278 LEU   A CA   
1888 C  C    . LEU   A 278 ? 0.7145 0.5975 0.5332 0.0797  -0.0088 -0.0608 278 LEU   A C    
1889 O  O    . LEU   A 278 ? 0.7149 0.5880 0.5273 0.0862  -0.0113 -0.0590 278 LEU   A O    
1890 C  CB   . LEU   A 278 ? 0.7536 0.6201 0.5559 0.0729  -0.0066 -0.0674 278 LEU   A CB   
1891 C  CG   . LEU   A 278 ? 0.7988 0.6575 0.5916 0.0749  -0.0084 -0.0706 278 LEU   A CG   
1892 C  CD1  . LEU   A 278 ? 0.8235 0.6622 0.6011 0.0672  -0.0047 -0.0741 278 LEU   A CD1  
1893 C  CD2  . LEU   A 278 ? 0.8197 0.6704 0.6055 0.0859  -0.0119 -0.0695 278 LEU   A CD2  
1894 N  N    . LYS   A 279 ? 0.7015 0.5944 0.5292 0.0734  -0.0052 -0.0600 279 LYS   A N    
1895 C  CA   . LYS   A 279 ? 0.6947 0.5865 0.5241 0.0735  -0.0028 -0.0571 279 LYS   A CA   
1896 C  C    . LYS   A 279 ? 0.6705 0.5729 0.5085 0.0806  -0.0075 -0.0539 279 LYS   A C    
1897 O  O    . LYS   A 279 ? 0.6704 0.5633 0.5030 0.0838  -0.0078 -0.0518 279 LYS   A O    
1898 C  CB   . LYS   A 279 ? 0.7160 0.6186 0.5548 0.0655  0.0024  -0.0573 279 LYS   A CB   
1899 C  CG   . LYS   A 279 ? 0.7603 0.6474 0.5884 0.0579  0.0082  -0.0597 279 LYS   A CG   
1900 C  CD   . LYS   A 279 ? 0.7929 0.6914 0.6318 0.0495  0.0139  -0.0597 279 LYS   A CD   
1901 C  CE   . LYS   A 279 ? 0.8509 0.7307 0.6773 0.0420  0.0200  -0.0618 279 LYS   A CE   
1902 N  NZ   . LYS   A 279 ? 0.8669 0.7593 0.7054 0.0319  0.0248  -0.0630 279 LYS   A NZ   
1903 N  N    . CYS   A 280 ? 0.6377 0.5573 0.4873 0.0833  -0.0113 -0.0536 280 CYS   A N    
1904 C  CA   . CYS   A 280 ? 0.6234 0.5536 0.4819 0.0895  -0.0157 -0.0506 280 CYS   A CA   
1905 C  C    . CYS   A 280 ? 0.6289 0.5484 0.4800 0.0962  -0.0200 -0.0504 280 CYS   A C    
1906 O  O    . CYS   A 280 ? 0.6242 0.5429 0.4771 0.1005  -0.0234 -0.0479 280 CYS   A O    
1907 C  CB   . CYS   A 280 ? 0.6156 0.5670 0.4879 0.0895  -0.0171 -0.0503 280 CYS   A CB   
1908 S  SG   . CYS   A 280 ? 0.6350 0.6028 0.5190 0.0835  -0.0138 -0.0498 280 CYS   A SG   
1909 N  N    . LEU   A 281 ? 0.6404 0.5524 0.4838 0.0972  -0.0203 -0.0530 281 LEU   A N    
1910 C  CA   . LEU   A 281 ? 0.6455 0.5488 0.4828 0.1043  -0.0242 -0.0529 281 LEU   A CA   
1911 C  C    . LEU   A 281 ? 0.6799 0.5587 0.4994 0.1056  -0.0240 -0.0539 281 LEU   A C    
1912 O  O    . LEU   A 281 ? 0.7068 0.5739 0.5163 0.1099  -0.0254 -0.0555 281 LEU   A O    
1913 C  CB   . LEU   A 281 ? 0.6378 0.5471 0.4766 0.1066  -0.0247 -0.0549 281 LEU   A CB   
1914 C  CG   . LEU   A 281 ? 0.6382 0.5702 0.4928 0.1071  -0.0254 -0.0535 281 LEU   A CG   
1915 C  CD1  . LEU   A 281 ? 0.6590 0.5925 0.5108 0.1101  -0.0252 -0.0557 281 LEU   A CD1  
1916 C  CD2  . LEU   A 281 ? 0.6219 0.5649 0.4882 0.1120  -0.0289 -0.0497 281 LEU   A CD2  
1917 N  N    . THR   A 282 ? 0.6822 0.5527 0.4970 0.1030  -0.0222 -0.0527 282 THR   A N    
1918 C  CA   . THR   A 282 ? 0.7012 0.5477 0.4982 0.1043  -0.0217 -0.0529 282 THR   A CA   
1919 C  C    . THR   A 282 ? 0.7098 0.5532 0.5064 0.1121  -0.0286 -0.0506 282 THR   A C    
1920 O  O    . THR   A 282 ? 0.7040 0.5607 0.5127 0.1130  -0.0314 -0.0483 282 THR   A O    
1921 C  CB   . THR   A 282 ? 0.7212 0.5622 0.5144 0.0976  -0.0156 -0.0524 282 THR   A CB   
1922 O  OG1  . THR   A 282 ? 0.7398 0.5856 0.5355 0.0903  -0.0103 -0.0547 282 THR   A OG1  
1923 C  CG2  . THR   A 282 ? 0.7394 0.5544 0.5126 0.0986  -0.0139 -0.0524 282 THR   A CG2  
1924 N  N    . PHE   A 283 ? 0.7173 0.5432 0.5000 0.1177  -0.0318 -0.0514 283 PHE   A N    
1925 C  CA   . PHE   A 283 ? 0.7157 0.5390 0.4985 0.1253  -0.0396 -0.0497 283 PHE   A CA   
1926 C  C    . PHE   A 283 ? 0.7188 0.5347 0.4972 0.1245  -0.0410 -0.0477 283 PHE   A C    
1927 O  O    . PHE   A 283 ? 0.7118 0.5376 0.5003 0.1272  -0.0468 -0.0457 283 PHE   A O    
1928 C  CB   . PHE   A 283 ? 0.7253 0.5302 0.4928 0.1322  -0.0430 -0.0511 283 PHE   A CB   
1929 C  CG   . PHE   A 283 ? 0.7295 0.5329 0.4982 0.1402  -0.0520 -0.0494 283 PHE   A CG   
1930 C  CD1  . PHE   A 283 ? 0.7501 0.5349 0.5045 0.1422  -0.0554 -0.0486 283 PHE   A CD1  
1931 C  CD2  . PHE   A 283 ? 0.7307 0.5515 0.5151 0.1458  -0.0573 -0.0486 283 PHE   A CD2  
1932 C  CE1  . PHE   A 283 ? 0.7570 0.5412 0.5132 0.1492  -0.0650 -0.0472 283 PHE   A CE1  
1933 C  CE2  . PHE   A 283 ? 0.7389 0.5604 0.5268 0.1526  -0.0662 -0.0470 283 PHE   A CE2  
1934 C  CZ   . PHE   A 283 ? 0.7426 0.5460 0.5166 0.1541  -0.0706 -0.0465 283 PHE   A CZ   
1935 N  N    . ASN   A 284 ? 0.7339 0.5315 0.4964 0.1206  -0.0355 -0.0483 284 ASN   A N    
1936 C  CA   . ASN   A 284 ? 0.7456 0.5319 0.4997 0.1203  -0.0356 -0.0466 284 ASN   A CA   
1937 C  C    . ASN   A 284 ? 0.7315 0.5350 0.4998 0.1149  -0.0314 -0.0451 284 ASN   A C    
1938 O  O    . ASN   A 284 ? 0.7365 0.5444 0.5073 0.1087  -0.0237 -0.0459 284 ASN   A O    
1939 C  CB   . ASN   A 284 ? 0.7927 0.5508 0.5226 0.1193  -0.0307 -0.0475 284 ASN   A CB   
1940 C  CG   . ASN   A 284 ? 0.8769 0.6201 0.5945 0.1192  -0.0293 -0.0458 284 ASN   A CG   
1941 O  OD1  . ASN   A 284 ? 0.9009 0.6507 0.6249 0.1212  -0.0340 -0.0440 284 ASN   A OD1  
1942 N  ND2  . ASN   A 284 ? 0.9171 0.6379 0.6152 0.1168  -0.0225 -0.0463 284 ASN   A ND2  
1943 N  N    . PRO   A 285 ? 0.7094 0.5224 0.4871 0.1173  -0.0369 -0.0430 285 PRO   A N    
1944 C  CA   . PRO   A 285 ? 0.6948 0.5232 0.4851 0.1133  -0.0334 -0.0414 285 PRO   A CA   
1945 C  C    . PRO   A 285 ? 0.7093 0.5283 0.4908 0.1089  -0.0250 -0.0410 285 PRO   A C    
1946 O  O    . PRO   A 285 ? 0.7023 0.5367 0.4958 0.1049  -0.0201 -0.0404 285 PRO   A O    
1947 C  CB   . PRO   A 285 ? 0.7012 0.5333 0.4968 0.1172  -0.0414 -0.0393 285 PRO   A CB   
1948 C  CG   . PRO   A 285 ? 0.7187 0.5322 0.5001 0.1227  -0.0485 -0.0398 285 PRO   A CG   
1949 C  CD   . PRO   A 285 ? 0.6984 0.5086 0.4759 0.1237  -0.0469 -0.0420 285 PRO   A CD   
1950 N  N    . ALA   A 286 ? 0.7213 0.5152 0.4818 0.1100  -0.0230 -0.0414 286 ALA   A N    
1951 C  CA   . ALA   A 286 ? 0.7255 0.5089 0.4765 0.1062  -0.0138 -0.0408 286 ALA   A CA   
1952 C  C    . ALA   A 286 ? 0.7213 0.5095 0.4757 0.0996  -0.0052 -0.0424 286 ALA   A C    
1953 O  O    . ALA   A 286 ? 0.7351 0.5280 0.4932 0.0949  0.0029  -0.0418 286 ALA   A O    
1954 C  CB   . ALA   A 286 ? 0.7438 0.4977 0.4700 0.1097  -0.0142 -0.0405 286 ALA   A CB   
1955 N  N    . LYS   A 287 ? 0.7044 0.4919 0.4580 0.0993  -0.0070 -0.0446 287 LYS   A N    
1956 C  CA   . LYS   A 287 ? 0.7072 0.4977 0.4630 0.0926  -0.0001 -0.0467 287 LYS   A CA   
1957 C  C    . LYS   A 287 ? 0.6735 0.4923 0.4519 0.0893  -0.0007 -0.0474 287 LYS   A C    
1958 O  O    . LYS   A 287 ? 0.6745 0.4995 0.4577 0.0829  0.0045  -0.0491 287 LYS   A O    
1959 C  CB   . LYS   A 287 ? 0.7545 0.5263 0.4946 0.0941  -0.0016 -0.0488 287 LYS   A CB   
1960 C  CG   . LYS   A 287 ? 0.8327 0.5742 0.5480 0.0960  0.0009  -0.0484 287 LYS   A CG   
1961 C  CD   . LYS   A 287 ? 0.9153 0.6387 0.6152 0.0988  -0.0014 -0.0504 287 LYS   A CD   
1962 C  CE   . LYS   A 287 ? 0.9856 0.6769 0.6587 0.1005  0.0018  -0.0499 287 LYS   A CE   
1963 N  NZ   . LYS   A 287 ? 1.0299 0.7028 0.6872 0.1034  -0.0003 -0.0519 287 LYS   A NZ   
1964 N  N    . ARG   A 288 ? 0.6414 0.4762 0.4328 0.0935  -0.0072 -0.0460 288 ARG   A N    
1965 C  CA   . ARG   A 288 ? 0.6189 0.4791 0.4299 0.0917  -0.0084 -0.0461 288 ARG   A CA   
1966 C  C    . ARG   A 288 ? 0.6208 0.4952 0.4431 0.0868  -0.0026 -0.0451 288 ARG   A C    
1967 O  O    . ARG   A 288 ? 0.6349 0.5069 0.4560 0.0882  -0.0010 -0.0429 288 ARG   A O    
1968 C  CB   . ARG   A 288 ? 0.5975 0.4681 0.4175 0.0978  -0.0164 -0.0444 288 ARG   A CB   
1969 C  CG   . ARG   A 288 ? 0.5671 0.4593 0.4031 0.0974  -0.0184 -0.0450 288 ARG   A CG   
1970 C  CD   . ARG   A 288 ? 0.5689 0.4692 0.4127 0.1030  -0.0254 -0.0431 288 ARG   A CD   
1971 N  NE   . ARG   A 288 ? 0.5850 0.4716 0.4191 0.1082  -0.0303 -0.0437 288 ARG   A NE   
1972 C  CZ   . ARG   A 288 ? 0.5735 0.4605 0.4103 0.1131  -0.0369 -0.0419 288 ARG   A CZ   
1973 N  NH1  . ARG   A 288 ? 0.5366 0.4351 0.3842 0.1131  -0.0390 -0.0395 288 ARG   A NH1  
1974 N  NH2  . ARG   A 288 ? 0.5693 0.4448 0.3981 0.1182  -0.0418 -0.0426 288 ARG   A NH2  
1975 N  N    . ILE   A 289 ? 0.6025 0.4929 0.4364 0.0818  -0.0002 -0.0467 289 ILE   A N    
1976 C  CA   . ILE   A 289 ? 0.5894 0.4970 0.4368 0.0777  0.0043  -0.0459 289 ILE   A CA   
1977 C  C    . ILE   A 289 ? 0.5781 0.4978 0.4350 0.0824  0.0011  -0.0429 289 ILE   A C    
1978 O  O    . ILE   A 289 ? 0.5760 0.4973 0.4341 0.0872  -0.0053 -0.0420 289 ILE   A O    
1979 C  CB   . ILE   A 289 ? 0.5934 0.5168 0.4516 0.0724  0.0048  -0.0484 289 ILE   A CB   
1980 C  CG1  . ILE   A 289 ? 0.5953 0.5332 0.4654 0.0669  0.0103  -0.0481 289 ILE   A CG1  
1981 C  CG2  . ILE   A 289 ? 0.5911 0.5290 0.4585 0.0762  -0.0019 -0.0485 289 ILE   A CG2  
1982 C  CD1  . ILE   A 289 ? 0.6070 0.5542 0.4837 0.0597  0.0118  -0.0511 289 ILE   A CD1  
1983 N  N    . SER   A 290 ? 0.5661 0.4928 0.4289 0.0810  0.0058  -0.0412 290 SER   A N    
1984 C  CA   . SER   A 290 ? 0.5484 0.4851 0.4189 0.0853  0.0034  -0.0383 290 SER   A CA   
1985 C  C    . SER   A 290 ? 0.5438 0.5042 0.4313 0.0836  0.0028  -0.0384 290 SER   A C    
1986 O  O    . SER   A 290 ? 0.5451 0.5129 0.4375 0.0786  0.0051  -0.0407 290 SER   A O    
1987 C  CB   . SER   A 290 ? 0.5488 0.4778 0.4142 0.0863  0.0089  -0.0362 290 SER   A CB   
1988 O  OG   . SER   A 290 ? 0.5584 0.4967 0.4311 0.0814  0.0163  -0.0368 290 SER   A OG   
1989 N  N    . ALA   A 291 ? 0.5348 0.5059 0.4301 0.0876  -0.0005 -0.0360 291 ALA   A N    
1990 C  CA   . ALA   A 291 ? 0.5400 0.5328 0.4500 0.0873  -0.0015 -0.0356 291 ALA   A CA   
1991 C  C    . ALA   A 291 ? 0.5543 0.5569 0.4717 0.0838  0.0046  -0.0358 291 ALA   A C    
1992 O  O    . ALA   A 291 ? 0.5480 0.5655 0.4752 0.0806  0.0044  -0.0374 291 ALA   A O    
1993 C  CB   . ALA   A 291 ? 0.5314 0.5294 0.4454 0.0925  -0.0051 -0.0324 291 ALA   A CB   
1994 N  N    . TYR   A 292 ? 0.5653 0.5584 0.4771 0.0843  0.0101  -0.0344 292 TYR   A N    
1995 C  CA   . TYR   A 292 ? 0.5778 0.5797 0.4970 0.0815  0.0170  -0.0342 292 TYR   A CA   
1996 C  C    . TYR   A 292 ? 0.5875 0.5908 0.5088 0.0740  0.0207  -0.0373 292 TYR   A C    
1997 O  O    . TYR   A 292 ? 0.5870 0.6079 0.5218 0.0705  0.0226  -0.0380 292 TYR   A O    
1998 C  CB   . TYR   A 292 ? 0.5937 0.5826 0.5043 0.0848  0.0227  -0.0317 292 TYR   A CB   
1999 C  CG   . TYR   A 292 ? 0.6032 0.6033 0.5233 0.0830  0.0307  -0.0309 292 TYR   A CG   
2000 C  CD1  . TYR   A 292 ? 0.6067 0.6274 0.5415 0.0856  0.0304  -0.0294 292 TYR   A CD1  
2001 C  CD2  . TYR   A 292 ? 0.6264 0.6167 0.5409 0.0790  0.0388  -0.0315 292 TYR   A CD2  
2002 C  CE1  . TYR   A 292 ? 0.6164 0.6488 0.5614 0.0849  0.0377  -0.0284 292 TYR   A CE1  
2003 C  CE2  . TYR   A 292 ? 0.6332 0.6356 0.5586 0.0772  0.0468  -0.0306 292 TYR   A CE2  
2004 C  CZ   . TYR   A 292 ? 0.6396 0.6639 0.5810 0.0804  0.0461  -0.0291 292 TYR   A CZ   
2005 O  OH   . TYR   A 292 ? 0.6685 0.7065 0.6221 0.0796  0.0538  -0.0279 292 TYR   A OH   
2006 N  N    . SER   A 293 ? 0.5974 0.5821 0.5053 0.0714  0.0213  -0.0391 293 SER   A N    
2007 C  CA   . SER   A 293 ? 0.6103 0.5938 0.5184 0.0637  0.0245  -0.0422 293 SER   A CA   
2008 C  C    . SER   A 293 ? 0.6201 0.6121 0.5326 0.0614  0.0180  -0.0450 293 SER   A C    
2009 O  O    . SER   A 293 ? 0.6355 0.6302 0.5506 0.0546  0.0195  -0.0478 293 SER   A O    
2010 C  CB   . SER   A 293 ? 0.6553 0.6138 0.5457 0.0618  0.0289  -0.0428 293 SER   A CB   
2011 O  OG   . SER   A 293 ? 0.7162 0.6577 0.5927 0.0683  0.0252  -0.0414 293 SER   A OG   
2012 N  N    . ALA   A 294 ? 0.6095 0.6057 0.5228 0.0670  0.0112  -0.0442 294 ALA   A N    
2013 C  CA   . ALA   A 294 ? 0.5981 0.6029 0.5154 0.0658  0.0057  -0.0466 294 ALA   A CA   
2014 C  C    . ALA   A 294 ? 0.5878 0.6155 0.5210 0.0635  0.0052  -0.0468 294 ALA   A C    
2015 O  O    . ALA   A 294 ? 0.5856 0.6203 0.5227 0.0585  0.0037  -0.0498 294 ALA   A O    
2016 C  CB   . ALA   A 294 ? 0.5910 0.5938 0.5050 0.0724  -0.0002 -0.0453 294 ALA   A CB   
2017 N  N    . LEU   A 295 ? 0.5797 0.6181 0.5214 0.0672  0.0067  -0.0437 295 LEU   A N    
2018 C  CA   . LEU   A 295 ? 0.5775 0.6379 0.5346 0.0665  0.0063  -0.0433 295 LEU   A CA   
2019 C  C    . LEU   A 295 ? 0.6039 0.6723 0.5693 0.0585  0.0103  -0.0457 295 LEU   A C    
2020 O  O    . LEU   A 295 ? 0.5989 0.6858 0.5767 0.0562  0.0076  -0.0469 295 LEU   A O    
2021 C  CB   . LEU   A 295 ? 0.5578 0.6242 0.5198 0.0729  0.0080  -0.0393 295 LEU   A CB   
2022 C  CG   . LEU   A 295 ? 0.5512 0.6189 0.5117 0.0799  0.0027  -0.0368 295 LEU   A CG   
2023 C  CD1  . LEU   A 295 ? 0.5436 0.6114 0.5051 0.0857  0.0053  -0.0330 295 LEU   A CD1  
2024 C  CD2  . LEU   A 295 ? 0.5382 0.6228 0.5073 0.0805  -0.0026 -0.0376 295 LEU   A CD2  
2025 N  N    . SER   A 296 ? 0.6333 0.6877 0.5916 0.0540  0.0165  -0.0464 296 SER   A N    
2026 C  CA   . SER   A 296 ? 0.6558 0.7153 0.6213 0.0454  0.0216  -0.0484 296 SER   A CA   
2027 C  C    . SER   A 296 ? 0.6803 0.7297 0.6383 0.0376  0.0201  -0.0527 296 SER   A C    
2028 O  O    . SER   A 296 ? 0.6885 0.7411 0.6521 0.0291  0.0241  -0.0546 296 SER   A O    
2029 C  CB   . SER   A 296 ? 0.6846 0.7341 0.6464 0.0450  0.0309  -0.0462 296 SER   A CB   
2030 O  OG   . SER   A 296 ? 0.7137 0.7806 0.6897 0.0480  0.0343  -0.0435 296 SER   A OG   
2031 N  N    . HIS   A 297 ? 0.6898 0.7268 0.6353 0.0404  0.0148  -0.0540 297 HIS   A N    
2032 C  CA   . HIS   A 297 ? 0.7050 0.7291 0.6402 0.0347  0.0132  -0.0579 297 HIS   A CA   
2033 C  C    . HIS   A 297 ? 0.7065 0.7463 0.6525 0.0275  0.0098  -0.0613 297 HIS   A C    
2034 O  O    . HIS   A 297 ? 0.6937 0.7528 0.6516 0.0303  0.0051  -0.0608 297 HIS   A O    
2035 C  CB   . HIS   A 297 ? 0.7174 0.7288 0.6394 0.0412  0.0080  -0.0581 297 HIS   A CB   
2036 C  CG   . HIS   A 297 ? 0.7509 0.7446 0.6589 0.0372  0.0073  -0.0617 297 HIS   A CG   
2037 N  ND1  . HIS   A 297 ? 0.7724 0.7705 0.6807 0.0339  0.0026  -0.0652 297 HIS   A ND1  
2038 C  CD2  . HIS   A 297 ? 0.7783 0.7488 0.6705 0.0365  0.0107  -0.0621 297 HIS   A CD2  
2039 C  CE1  . HIS   A 297 ? 0.7890 0.7666 0.6818 0.0313  0.0036  -0.0677 297 HIS   A CE1  
2040 N  NE2  . HIS   A 297 ? 0.7981 0.7587 0.6810 0.0329  0.0083  -0.0659 297 HIS   A NE2  
2041 N  N    . PRO   A 298 ? 0.7184 0.7493 0.6599 0.0181  0.0118  -0.0649 298 PRO   A N    
2042 C  CA   . PRO   A 298 ? 0.7157 0.7605 0.6670 0.0103  0.0077  -0.0686 298 PRO   A CA   
2043 C  C    . PRO   A 298 ? 0.7142 0.7675 0.6654 0.0144  -0.0014 -0.0703 298 PRO   A C    
2044 O  O    . PRO   A 298 ? 0.7045 0.7764 0.6683 0.0112  -0.0057 -0.0719 298 PRO   A O    
2045 C  CB   . PRO   A 298 ? 0.7351 0.7608 0.6747 0.0009  0.0110  -0.0720 298 PRO   A CB   
2046 C  CG   . PRO   A 298 ? 0.7471 0.7571 0.6789 0.0018  0.0194  -0.0692 298 PRO   A CG   
2047 C  CD   . PRO   A 298 ? 0.7277 0.7346 0.6541 0.0139  0.0178  -0.0656 298 PRO   A CD   
2048 N  N    . TYR   A 299 ? 0.7214 0.7621 0.6592 0.0222  -0.0041 -0.0696 299 TYR   A N    
2049 C  CA   . TYR   A 299 ? 0.7249 0.7713 0.6606 0.0277  -0.0112 -0.0705 299 TYR   A CA   
2050 C  C    . TYR   A 299 ? 0.7270 0.7976 0.6785 0.0313  -0.0147 -0.0684 299 TYR   A C    
2051 O  O    . TYR   A 299 ? 0.7241 0.8030 0.6764 0.0329  -0.0208 -0.0700 299 TYR   A O    
2052 C  CB   . TYR   A 299 ? 0.7251 0.7567 0.6475 0.0365  -0.0115 -0.0686 299 TYR   A CB   
2053 C  CG   . TYR   A 299 ? 0.7213 0.7598 0.6427 0.0432  -0.0173 -0.0685 299 TYR   A CG   
2054 C  CD1  . TYR   A 299 ? 0.7332 0.7689 0.6475 0.0411  -0.0215 -0.0724 299 TYR   A CD1  
2055 C  CD2  . TYR   A 299 ? 0.7174 0.7646 0.6441 0.0515  -0.0182 -0.0643 299 TYR   A CD2  
2056 C  CE1  . TYR   A 299 ? 0.7366 0.7783 0.6492 0.0475  -0.0260 -0.0720 299 TYR   A CE1  
2057 C  CE2  . TYR   A 299 ? 0.7249 0.7786 0.6509 0.0572  -0.0226 -0.0638 299 TYR   A CE2  
2058 C  CZ   . TYR   A 299 ? 0.7393 0.7903 0.6581 0.0555  -0.0262 -0.0676 299 TYR   A CZ   
2059 O  OH   . TYR   A 299 ? 0.7500 0.8061 0.6665 0.0616  -0.0297 -0.0669 299 TYR   A OH   
2060 N  N    . PHE   A 300 ? 0.7278 0.8086 0.6908 0.0330  -0.0107 -0.0649 300 PHE   A N    
2061 C  CA   . PHE   A 300 ? 0.7305 0.8329 0.7078 0.0374  -0.0134 -0.0625 300 PHE   A CA   
2062 C  C    . PHE   A 300 ? 0.7564 0.8778 0.7506 0.0307  -0.0132 -0.0637 300 PHE   A C    
2063 O  O    . PHE   A 300 ? 0.7522 0.8924 0.7588 0.0346  -0.0159 -0.0619 300 PHE   A O    
2064 C  CB   . PHE   A 300 ? 0.7140 0.8153 0.6918 0.0458  -0.0101 -0.0575 300 PHE   A CB   
2065 C  CG   . PHE   A 300 ? 0.7108 0.7985 0.6758 0.0528  -0.0118 -0.0560 300 PHE   A CG   
2066 C  CD1  . PHE   A 300 ? 0.7096 0.8025 0.6728 0.0576  -0.0174 -0.0560 300 PHE   A CD1  
2067 C  CD2  . PHE   A 300 ? 0.7167 0.7869 0.6718 0.0548  -0.0077 -0.0545 300 PHE   A CD2  
2068 C  CE1  . PHE   A 300 ? 0.7207 0.8030 0.6745 0.0639  -0.0183 -0.0542 300 PHE   A CE1  
2069 C  CE2  . PHE   A 300 ? 0.7280 0.7879 0.6738 0.0612  -0.0098 -0.0530 300 PHE   A CE2  
2070 C  CZ   . PHE   A 300 ? 0.7289 0.7956 0.6750 0.0655  -0.0148 -0.0528 300 PHE   A CZ   
2071 N  N    . GLN   A 301 ? 0.7808 0.8976 0.7760 0.0205  -0.0103 -0.0668 301 GLN   A N    
2072 C  CA   . GLN   A 301 ? 0.7965 0.9320 0.8093 0.0126  -0.0102 -0.0684 301 GLN   A CA   
2073 C  C    . GLN   A 301 ? 0.8014 0.9512 0.8196 0.0109  -0.0200 -0.0716 301 GLN   A C    
2074 O  O    . GLN   A 301 ? 0.7936 0.9662 0.8288 0.0117  -0.0230 -0.0708 301 GLN   A O    
2075 C  CB   . GLN   A 301 ? 0.8380 0.9625 0.8487 0.0012  -0.0045 -0.0709 301 GLN   A CB   
2076 C  CG   . GLN   A 301 ? 0.9067 1.0350 0.9274 -0.0006 0.0053  -0.0678 301 GLN   A CG   
2077 C  CD   . GLN   A 301 ? 1.0084 1.1129 1.0126 0.0035  0.0124  -0.0653 301 GLN   A CD   
2078 O  OE1  . GLN   A 301 ? 1.0371 1.1244 1.0320 -0.0032 0.0182  -0.0665 301 GLN   A OE1  
2079 N  NE2  . GLN   A 301 ? 1.0343 1.1367 1.0339 0.0144  0.0121  -0.0617 301 GLN   A NE2  
2080 C  C12  . A1AZ4 B .   ? 0.4913 0.5773 0.4839 0.1102  -0.0206 0.0147  401 A1AZ4 A C12  
2081 C  C10  . A1AZ4 B .   ? 0.4945 0.5646 0.4779 0.1083  -0.0232 0.0181  401 A1AZ4 A C10  
2082 C  C28  . A1AZ4 B .   ? 0.4995 0.5841 0.4633 0.1214  -0.0164 0.0164  401 A1AZ4 A C28  
2083 C  C11  . A1AZ4 B .   ? 0.4948 0.5748 0.4796 0.1110  -0.0204 0.0164  401 A1AZ4 A C11  
2084 C  C7   . A1AZ4 B .   ? 0.4927 0.5664 0.4919 0.1035  -0.0277 0.0165  401 A1AZ4 A C7   
2085 C  C13  . A1AZ4 B .   ? 0.4904 0.5737 0.4907 0.1067  -0.0241 0.0149  401 A1AZ4 A C13  
2086 C  C8   . A1AZ4 B .   ? 0.4960 0.5626 0.4861 0.1044  -0.0269 0.0180  401 A1AZ4 A C8   
2087 C  C29  . A1AZ4 B .   ? 0.5041 0.5838 0.4736 0.1174  -0.0185 0.0160  401 A1AZ4 A C29  
2088 C  C14  . A1AZ4 B .   ? 0.5032 0.5869 0.4805 0.1151  -0.0174 0.0165  401 A1AZ4 A C14  
2089 C  C5   . A1AZ4 B .   ? 0.4927 0.5757 0.5075 0.1020  -0.0303 0.0148  401 A1AZ4 A C5   
2090 C  C16  . A1AZ4 B .   ? 0.5065 0.6002 0.4772 0.1205  -0.0117 0.0176  401 A1AZ4 A C16  
2091 C  C20  . A1AZ4 B .   ? 0.5421 0.6488 0.5191 0.1224  -0.0083 0.0121  401 A1AZ4 A C20  
2092 C  C21  . A1AZ4 B .   ? 0.5494 0.6611 0.5319 0.1231  -0.0052 0.0118  401 A1AZ4 A C21  
2093 C  C23  . A1AZ4 B .   ? 0.5521 0.6661 0.5310 0.1253  0.0035  0.0196  401 A1AZ4 A C23  
2094 C  C18  . A1AZ4 B .   ? 0.5332 0.6379 0.5095 0.1219  -0.0055 0.0177  401 A1AZ4 A C18  
2095 C  C24  . A1AZ4 B .   ? 0.5498 0.6581 0.5217 0.1251  0.0002  0.0203  401 A1AZ4 A C24  
2096 C  C1   . A1AZ4 B .   ? 0.4712 0.5646 0.4740 0.1117  -0.0241 0.0067  401 A1AZ4 A C1   
2097 C  C3   . A1AZ4 B .   ? 0.4632 0.5684 0.4773 0.1109  -0.0163 0.0145  401 A1AZ4 A C3   
2098 C  C32  . A1AZ4 B .   ? 0.4754 0.5750 0.5151 0.0994  -0.0295 0.0178  401 A1AZ4 A C32  
2099 C  C33  . A1AZ4 B .   ? 0.4828 0.5598 0.5104 0.0957  -0.0411 0.0147  401 A1AZ4 A C33  
2100 C  C2   . A1AZ4 B .   ? 0.4726 0.5695 0.4849 0.1091  -0.0228 0.0115  401 A1AZ4 A C2   
2101 C  C31  . A1AZ4 B .   ? 0.4872 0.5741 0.5140 0.1000  -0.0341 0.0143  401 A1AZ4 A C31  
2102 N  N27  . A1AZ4 B .   ? 0.4999 0.5909 0.4635 0.1229  -0.0134 0.0171  401 A1AZ4 A N27  
2103 N  N6   . A1AZ4 B .   ? 0.4955 0.5688 0.5036 0.1002  -0.0318 0.0162  401 A1AZ4 A N6   
2104 N  N15  . A1AZ4 B .   ? 0.5033 0.5946 0.4818 0.1168  -0.0137 0.0174  401 A1AZ4 A N15  
2105 N  N4   . A1AZ4 B .   ? 0.4811 0.5696 0.4908 0.1059  -0.0255 0.0137  401 A1AZ4 A N4   
2106 N  N17  . A1AZ4 B .   ? 0.5142 0.6137 0.4838 0.1227  -0.0079 0.0183  401 A1AZ4 A N17  
2107 O  O22  . A1AZ4 B .   ? 0.5608 0.6758 0.5386 0.1263  0.0002  0.0140  401 A1AZ4 A O22  
2108 O  O26  . A1AZ4 B .   ? 0.5590 0.6641 0.5306 0.1240  0.0034  0.0259  401 A1AZ4 A O26  
2109 O  O34  . A1AZ4 B .   ? 0.4968 0.5843 0.5214 0.1033  -0.0358 0.0100  401 A1AZ4 A O34  
2110 F  F9   . A1AZ4 B .   ? 0.4984 0.5537 0.4854 0.1016  -0.0302 0.0194  401 A1AZ4 A F9   
2111 CL CL30 . A1AZ4 B .   ? 0.5146 0.5835 0.4807 0.1163  -0.0222 0.0148  401 A1AZ4 A CL30 
# 
