data_9KSJ
# 
_entry.id   9KSJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9KSJ         pdb_00009ksj 10.2210/pdb9ksj/pdb 
WWPDB D_1300054170 ?            ?                   
# 
_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       2025-04-02 
_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                        9KSJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 zhang_wei2@gzlab.ac.cn wei Zhang ? 'principal investigator/group leader' 0000-0001-8693-6747 
4 peng_wei@gzlab.ac.cn   Wei Peng  ? 'principal investigator/group leader' 0000-0002-0949-4487 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhong, Y.' 1 0009-0009-0876-4148 
'Zhao, L.'  2 0009-0006-1001-3261 
'Zhang, W.' 3 0000-0001-8693-6747 
'Peng, W.'  4 0000-0002-0949-4487 
# 
_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                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            289 
_citation.language                  ? 
_citation.page_first                117497 
_citation.page_last                 117497 
_citation.title                     
;Expanding the utilization of binding pockets proves to be effective for noncovalent small molecule inhibitors against SARS-CoV-2 M pro.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2025.117497 
_citation.pdbx_database_id_PubMed   40090296 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, Q.'  1  ? 
primary 'Huang, X.' 2  ? 
primary 'Zhang, H.' 3  ? 
primary 'Sun, J.'   4  ? 
primary 'Tang, J.'  5  ? 
primary 'Chen, Z.'  6  ? 
primary 'Liu, L.'   7  ? 
primary 'Liu, M.'   8  ? 
primary 'Sun, Z.'   9  ? 
primary 'Tang, Z.'  10 ? 
primary 'Wei, D.'   11 ? 
primary 'Wang, D.'  12 ? 
primary 'Wang, Y.'  13 ? 
primary 'Yan, M.'   14 ? 
primary 'Zhao, L.'  15 ? 
primary 'Zhu, A.'   16 ? 
primary 'Zhong, Y.' 17 ? 
primary 'Yang, H.'  18 ? 
primary 'Zhao, Y.'  19 ? 
primary 'Dai, J.'   20 ? 
primary 'Shi, Y.'   21 ? 
primary 'Huang, B.' 22 ? 
primary 'Zhang, W.' 23 ? 
primary 'Zhao, J.'  24 ? 
primary 'Chen, X.'  25 ? 
primary 'Rao, Z.'   26 ? 
primary 'Peng, W.'  27 ? 
# 
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 '3C-like proteinase nsp5' 33333.996 1   3.4.22.69 P132H ? ? 
2 non-polymer syn 
;3-[[(6E)-6-(6-chloranyl-2-methyl-indazol-5-yl)imino-3-[5-(2-methoxyethoxy)pyridin-3-yl]-2,4-bis(oxidanylidene)-1,3,5-triazinan-1-yl]methyl]-4-methyl-benzenecarbonitrile
;
573.002   1   ?         ?     ? ? 
3 water       nat water 18.015    211 ?         ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRHNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRHNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
_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 
;3-[[(6E)-6-(6-chloranyl-2-methyl-indazol-5-yl)imino-3-[5-(2-methoxyethoxy)pyridin-3-yl]-2,4-bis(oxidanylidene)-1,3,5-triazinan-1-yl]methyl]-4-methyl-benzenecarbonitrile
;
A1EGR 
3 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 HIS n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER 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                   301 
_entity_src_gen.gene_src_common_name               '2019-nCoV, SARS-CoV-2' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1EGR non-polymer         . 
;3-[[(6E)-6-(6-chloranyl-2-methyl-indazol-5-yl)imino-3-[5-(2-methoxyethoxy)pyridin-3-yl]-2,4-bis(oxidanylidene)-1,3,5-triazinan-1-yl]methyl]-4-methyl-benzenecarbonitrile
;
? 'C28 H25 Cl N8 O4' 573.002 
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   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU 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  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EGR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EGR 
_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 A1EGR 1   401 401 A1EGR 384 A . 
C 3 HOH   1   501 75  HOH   HOH A . 
C 3 HOH   2   502 46  HOH   HOH A . 
C 3 HOH   3   503 79  HOH   HOH A . 
C 3 HOH   4   504 110 HOH   HOH A . 
C 3 HOH   5   505 113 HOH   HOH A . 
C 3 HOH   6   506 35  HOH   HOH A . 
C 3 HOH   7   507 38  HOH   HOH A . 
C 3 HOH   8   508 80  HOH   HOH A . 
C 3 HOH   9   509 98  HOH   HOH A . 
C 3 HOH   10  510 131 HOH   HOH A . 
C 3 HOH   11  511 55  HOH   HOH A . 
C 3 HOH   12  512 181 HOH   HOH A . 
C 3 HOH   13  513 134 HOH   HOH A . 
C 3 HOH   14  514 199 HOH   HOH A . 
C 3 HOH   15  515 171 HOH   HOH A . 
C 3 HOH   16  516 57  HOH   HOH A . 
C 3 HOH   17  517 92  HOH   HOH A . 
C 3 HOH   18  518 30  HOH   HOH A . 
C 3 HOH   19  519 125 HOH   HOH A . 
C 3 HOH   20  520 147 HOH   HOH A . 
C 3 HOH   21  521 24  HOH   HOH A . 
C 3 HOH   22  522 41  HOH   HOH A . 
C 3 HOH   23  523 145 HOH   HOH A . 
C 3 HOH   24  524 123 HOH   HOH A . 
C 3 HOH   25  525 27  HOH   HOH A . 
C 3 HOH   26  526 136 HOH   HOH A . 
C 3 HOH   27  527 124 HOH   HOH A . 
C 3 HOH   28  528 40  HOH   HOH A . 
C 3 HOH   29  529 34  HOH   HOH A . 
C 3 HOH   30  530 211 HOH   HOH A . 
C 3 HOH   31  531 100 HOH   HOH A . 
C 3 HOH   32  532 175 HOH   HOH A . 
C 3 HOH   33  533 119 HOH   HOH A . 
C 3 HOH   34  534 19  HOH   HOH A . 
C 3 HOH   35  535 67  HOH   HOH A . 
C 3 HOH   36  536 44  HOH   HOH A . 
C 3 HOH   37  537 156 HOH   HOH A . 
C 3 HOH   38  538 3   HOH   HOH A . 
C 3 HOH   39  539 63  HOH   HOH A . 
C 3 HOH   40  540 82  HOH   HOH A . 
C 3 HOH   41  541 20  HOH   HOH A . 
C 3 HOH   42  542 32  HOH   HOH A . 
C 3 HOH   43  543 25  HOH   HOH A . 
C 3 HOH   44  544 14  HOH   HOH A . 
C 3 HOH   45  545 13  HOH   HOH A . 
C 3 HOH   46  546 7   HOH   HOH A . 
C 3 HOH   47  547 60  HOH   HOH A . 
C 3 HOH   48  548 21  HOH   HOH A . 
C 3 HOH   49  549 206 HOH   HOH A . 
C 3 HOH   50  550 190 HOH   HOH A . 
C 3 HOH   51  551 2   HOH   HOH A . 
C 3 HOH   52  552 128 HOH   HOH A . 
C 3 HOH   53  553 87  HOH   HOH A . 
C 3 HOH   54  554 62  HOH   HOH A . 
C 3 HOH   55  555 85  HOH   HOH A . 
C 3 HOH   56  556 59  HOH   HOH A . 
C 3 HOH   57  557 114 HOH   HOH A . 
C 3 HOH   58  558 207 HOH   HOH A . 
C 3 HOH   59  559 22  HOH   HOH A . 
C 3 HOH   60  560 5   HOH   HOH A . 
C 3 HOH   61  561 1   HOH   HOH A . 
C 3 HOH   62  562 70  HOH   HOH A . 
C 3 HOH   63  563 28  HOH   HOH A . 
C 3 HOH   64  564 9   HOH   HOH A . 
C 3 HOH   65  565 53  HOH   HOH A . 
C 3 HOH   66  566 198 HOH   HOH A . 
C 3 HOH   67  567 137 HOH   HOH A . 
C 3 HOH   68  568 17  HOH   HOH A . 
C 3 HOH   69  569 81  HOH   HOH A . 
C 3 HOH   70  570 89  HOH   HOH A . 
C 3 HOH   71  571 56  HOH   HOH A . 
C 3 HOH   72  572 49  HOH   HOH A . 
C 3 HOH   73  573 188 HOH   HOH A . 
C 3 HOH   74  574 26  HOH   HOH A . 
C 3 HOH   75  575 116 HOH   HOH A . 
C 3 HOH   76  576 43  HOH   HOH A . 
C 3 HOH   77  577 122 HOH   HOH A . 
C 3 HOH   78  578 12  HOH   HOH A . 
C 3 HOH   79  579 10  HOH   HOH A . 
C 3 HOH   80  580 29  HOH   HOH A . 
C 3 HOH   81  581 39  HOH   HOH A . 
C 3 HOH   82  582 219 HOH   HOH A . 
C 3 HOH   83  583 201 HOH   HOH A . 
C 3 HOH   84  584 106 HOH   HOH A . 
C 3 HOH   85  585 11  HOH   HOH A . 
C 3 HOH   86  586 31  HOH   HOH A . 
C 3 HOH   87  587 78  HOH   HOH A . 
C 3 HOH   88  588 23  HOH   HOH A . 
C 3 HOH   89  589 135 HOH   HOH A . 
C 3 HOH   90  590 65  HOH   HOH A . 
C 3 HOH   91  591 127 HOH   HOH A . 
C 3 HOH   92  592 158 HOH   HOH A . 
C 3 HOH   93  593 48  HOH   HOH A . 
C 3 HOH   94  594 8   HOH   HOH A . 
C 3 HOH   95  595 112 HOH   HOH A . 
C 3 HOH   96  596 94  HOH   HOH A . 
C 3 HOH   97  597 218 HOH   HOH A . 
C 3 HOH   98  598 37  HOH   HOH A . 
C 3 HOH   99  599 185 HOH   HOH A . 
C 3 HOH   100 600 146 HOH   HOH A . 
C 3 HOH   101 601 72  HOH   HOH A . 
C 3 HOH   102 602 50  HOH   HOH A . 
C 3 HOH   103 603 215 HOH   HOH A . 
C 3 HOH   104 604 77  HOH   HOH A . 
C 3 HOH   105 605 15  HOH   HOH A . 
C 3 HOH   106 606 52  HOH   HOH A . 
C 3 HOH   107 607 104 HOH   HOH A . 
C 3 HOH   108 608 18  HOH   HOH A . 
C 3 HOH   109 609 69  HOH   HOH A . 
C 3 HOH   110 610 141 HOH   HOH A . 
C 3 HOH   111 611 73  HOH   HOH A . 
C 3 HOH   112 612 103 HOH   HOH A . 
C 3 HOH   113 613 126 HOH   HOH A . 
C 3 HOH   114 614 200 HOH   HOH A . 
C 3 HOH   115 615 174 HOH   HOH A . 
C 3 HOH   116 616 6   HOH   HOH A . 
C 3 HOH   117 617 117 HOH   HOH A . 
C 3 HOH   118 618 71  HOH   HOH A . 
C 3 HOH   119 619 138 HOH   HOH A . 
C 3 HOH   120 620 90  HOH   HOH A . 
C 3 HOH   121 621 84  HOH   HOH A . 
C 3 HOH   122 622 214 HOH   HOH A . 
C 3 HOH   123 623 47  HOH   HOH A . 
C 3 HOH   124 624 45  HOH   HOH A . 
C 3 HOH   125 625 139 HOH   HOH A . 
C 3 HOH   126 626 159 HOH   HOH A . 
C 3 HOH   127 627 205 HOH   HOH A . 
C 3 HOH   128 628 129 HOH   HOH A . 
C 3 HOH   129 629 102 HOH   HOH A . 
C 3 HOH   130 630 68  HOH   HOH A . 
C 3 HOH   131 631 197 HOH   HOH A . 
C 3 HOH   132 632 220 HOH   HOH A . 
C 3 HOH   133 633 54  HOH   HOH A . 
C 3 HOH   134 634 105 HOH   HOH A . 
C 3 HOH   135 635 164 HOH   HOH A . 
C 3 HOH   136 636 88  HOH   HOH A . 
C 3 HOH   137 637 66  HOH   HOH A . 
C 3 HOH   138 638 173 HOH   HOH A . 
C 3 HOH   139 639 191 HOH   HOH A . 
C 3 HOH   140 640 143 HOH   HOH A . 
C 3 HOH   141 641 101 HOH   HOH A . 
C 3 HOH   142 642 111 HOH   HOH A . 
C 3 HOH   143 643 166 HOH   HOH A . 
C 3 HOH   144 644 76  HOH   HOH A . 
C 3 HOH   145 645 16  HOH   HOH A . 
C 3 HOH   146 646 144 HOH   HOH A . 
C 3 HOH   147 647 86  HOH   HOH A . 
C 3 HOH   148 648 118 HOH   HOH A . 
C 3 HOH   149 649 96  HOH   HOH A . 
C 3 HOH   150 650 182 HOH   HOH A . 
C 3 HOH   151 651 133 HOH   HOH A . 
C 3 HOH   152 652 4   HOH   HOH A . 
C 3 HOH   153 653 148 HOH   HOH A . 
C 3 HOH   154 654 217 HOH   HOH A . 
C 3 HOH   155 655 108 HOH   HOH A . 
C 3 HOH   156 656 95  HOH   HOH A . 
C 3 HOH   157 657 177 HOH   HOH A . 
C 3 HOH   158 658 107 HOH   HOH A . 
C 3 HOH   159 659 51  HOH   HOH A . 
C 3 HOH   160 660 154 HOH   HOH A . 
C 3 HOH   161 661 58  HOH   HOH A . 
C 3 HOH   162 662 130 HOH   HOH A . 
C 3 HOH   163 663 151 HOH   HOH A . 
C 3 HOH   164 664 161 HOH   HOH A . 
C 3 HOH   165 665 157 HOH   HOH A . 
C 3 HOH   166 666 165 HOH   HOH A . 
C 3 HOH   167 667 184 HOH   HOH A . 
C 3 HOH   168 668 187 HOH   HOH A . 
C 3 HOH   169 669 210 HOH   HOH A . 
C 3 HOH   170 670 202 HOH   HOH A . 
C 3 HOH   171 671 160 HOH   HOH A . 
C 3 HOH   172 672 186 HOH   HOH A . 
C 3 HOH   173 673 149 HOH   HOH A . 
C 3 HOH   174 674 194 HOH   HOH A . 
C 3 HOH   175 675 109 HOH   HOH A . 
C 3 HOH   176 676 121 HOH   HOH A . 
C 3 HOH   177 677 213 HOH   HOH A . 
C 3 HOH   178 678 155 HOH   HOH A . 
C 3 HOH   179 679 150 HOH   HOH A . 
C 3 HOH   180 680 74  HOH   HOH A . 
C 3 HOH   181 681 142 HOH   HOH A . 
C 3 HOH   182 682 115 HOH   HOH A . 
C 3 HOH   183 683 193 HOH   HOH A . 
C 3 HOH   184 684 208 HOH   HOH A . 
C 3 HOH   185 685 178 HOH   HOH A . 
C 3 HOH   186 686 61  HOH   HOH A . 
C 3 HOH   187 687 97  HOH   HOH A . 
C 3 HOH   188 688 93  HOH   HOH A . 
C 3 HOH   189 689 216 HOH   HOH A . 
C 3 HOH   190 690 179 HOH   HOH A . 
C 3 HOH   191 691 212 HOH   HOH A . 
C 3 HOH   192 692 172 HOH   HOH A . 
C 3 HOH   193 693 99  HOH   HOH A . 
C 3 HOH   194 694 162 HOH   HOH A . 
C 3 HOH   195 695 120 HOH   HOH A . 
C 3 HOH   196 696 64  HOH   HOH A . 
C 3 HOH   197 697 167 HOH   HOH A . 
C 3 HOH   198 698 153 HOH   HOH A . 
C 3 HOH   199 699 170 HOH   HOH A . 
C 3 HOH   200 700 192 HOH   HOH A . 
C 3 HOH   201 701 83  HOH   HOH A . 
C 3 HOH   202 702 42  HOH   HOH A . 
C 3 HOH   203 703 163 HOH   HOH A . 
C 3 HOH   204 704 203 HOH   HOH A . 
C 3 HOH   205 705 169 HOH   HOH A . 
C 3 HOH   206 706 36  HOH   HOH A . 
C 3 HOH   207 707 33  HOH   HOH A . 
C 3 HOH   208 708 168 HOH   HOH A . 
C 3 HOH   209 709 91  HOH   HOH A . 
C 3 HOH   210 710 209 HOH   HOH A . 
C 3 HOH   211 711 152 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 ARG 188 ? CZ  ? A ARG 188 CZ  
2 1 Y 1 A ARG 188 ? NH1 ? A ARG 188 NH1 
3 1 Y 1 A ARG 188 ? NH2 ? A ARG 188 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .                    1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .                    2 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .                    3 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(1.20.1_4487: ???)' 4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .                    5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   114.36 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KSJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     97.192 
_cell.length_a_esd                 ? 
_cell.length_b                     81.599 
_cell.length_b_esd                 ? 
_cell.length_c                     51.822 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9KSJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KSJ 
_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             2.81 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.20 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 MES (pH 5.0-5.6) with polyethylene glycol (PEG) 6,000 (9-11% w/v)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            300 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 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         2024-01-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97853 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KSJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.67 
_reflns.d_resolution_low                               50 
_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                                     42659 
_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                           96.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.533 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.58 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_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                                    1.67 
_reflns_shell.d_res_low                                     1.71 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5742 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.69 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9KSJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.67 
_refine.ls_d_res_low                             32.90 
_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                     41358 
_refine.ls_number_reflns_R_free                  2010 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.00 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1753 
_refine.ls_R_factor_R_free                       0.1886 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1746 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.38 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.84 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.67 
_refine_hist.d_res_low                        32.90 
_refine_hist.number_atoms_solvent             211 
_refine_hist.number_atoms_total               2581 
_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        2370 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.079 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.532 ? 330 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.065 ? 366 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 425 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.67 1.71  . . 126 2655 93.00 . . . . 0.3806 . . . . . . . . . . . 0.4172 
'X-RAY DIFFRACTION' 1.71 1.76  . . 136 2787 96.00 . . . . 0.2914 . . . . . . . . . . . 0.2938 
'X-RAY DIFFRACTION' 1.76 1.81  . . 147 2758 96.00 . . . . 0.2302 . . . . . . . . . . . 0.2475 
'X-RAY DIFFRACTION' 1.81 1.87  . . 154 2760 96.00 . . . . 0.1887 . . . . . . . . . . . 0.2247 
'X-RAY DIFFRACTION' 1.87 1.94  . . 140 2806 97.00 . . . . 0.1956 . . . . . . . . . . . 0.2245 
'X-RAY DIFFRACTION' 1.94 2.01  . . 143 2768 97.00 . . . . 0.2038 . . . . . . . . . . . 0.2278 
'X-RAY DIFFRACTION' 2.01 2.11  . . 132 2830 97.00 . . . . 0.1785 . . . . . . . . . . . 0.2076 
'X-RAY DIFFRACTION' 2.11 2.22  . . 151 2801 97.00 . . . . 0.1707 . . . . . . . . . . . 0.2002 
'X-RAY DIFFRACTION' 2.22 2.36  . . 148 2849 97.00 . . . . 0.1718 . . . . . . . . . . . 0.1752 
'X-RAY DIFFRACTION' 2.36 2.54  . . 150 2818 98.00 . . . . 0.1813 . . . . . . . . . . . 0.1942 
'X-RAY DIFFRACTION' 2.54 2.79  . . 126 2850 98.00 . . . . 0.1822 . . . . . . . . . . . 0.2104 
'X-RAY DIFFRACTION' 2.79 3.20  . . 145 2873 98.00 . . . . 0.1787 . . . . . . . . . . . 0.1937 
'X-RAY DIFFRACTION' 3.20 4.02  . . 149 2885 99.00 . . . . 0.1549 . . . . . . . . . . . 0.1758 
'X-RAY DIFFRACTION' 4.03 32.90 . . 163 2908 99.00 . . . . 0.1436 . . . . . . . . . . . 0.1389 
# 
_struct.entry_id                     9KSJ 
_struct.title                        'Crystal structure of SARS-CoV-2 main protease in complex with compound 8' 
_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        9KSJ 
_struct_keywords.text            'Inhibitor, Complex, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
_struct_ref.pdbx_align_begin           3264 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9KSJ 
_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             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3564 
_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 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9KSJ 
_struct_ref_seq_dif.mon_id                       HIS 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      132 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P0DTD1 
_struct_ref_seq_dif.db_mon_id                    PRO 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          3395 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            132 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2710  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  25200 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_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   'fluorescence resonance energy transfer' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_556 -x,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 -21.3749453055 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 47.2083827004 
# 
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 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 THR A 45  ? MET A 49  ? THR A 45  MET A 49  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? SER A 301 ? THR A 292 SER A 301 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 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 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 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 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
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 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
# 
_pdbx_entry_details.entry_id                   9KSJ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33 ? ? 48.89 -132.20 
2 1 ASN A 84 ? ? 51.64 -122.30 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 532 ? C HOH . 
2 1 A HOH 615 ? C HOH . 
3 1 A HOH 638 ? C HOH . 
4 1 A HOH 695 ? C HOH . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -12.9863 41.3321 11.1234 0.1883 ? 0.0345 ? 0.0140  ? 0.1716 ? 0.0218 ? 0.1967 ? 0.2371 ? -0.1242 ? 
-0.3706 ? 0.2406 ? 0.0870  ? 0.5997 ? 0.0420  ? 0.0187  ? 0.0271  ? 0.0843  ? 0.0360  ? 0.0427  ? -0.2067 ? -0.1359 ? -0.0000 ? 
2 'X-RAY DIFFRACTION' ? refined -16.8984 47.4379 -1.1338 0.2411 ? 0.0868 ? -0.0060 ? 0.2138 ? 0.0534 ? 0.2188 ? 0.3159 ? 0.3676  ? 
-0.2370 ? 0.5030 ? -0.5091 ? 0.6332 ? 0.0413  ? 0.1352  ? 0.1754  ? -0.0852 ? 0.0244  ? 0.1138  ? -0.2428 ? -0.2033 ? 0.0015  ? 
3 'X-RAY DIFFRACTION' ? refined -8.6728  33.2745 10.3307 0.1443 ? 0.0181 ? 0.0088  ? 0.1623 ? 0.0066 ? 0.1490 ? 0.2259 ? -0.1568 ? 
-0.3941 ? 0.4354 ? -0.1278 ? 0.9828 ? -0.0269 ? -0.0259 ? -0.0053 ? 0.0130  ? 0.0461  ? 0.0187  ? 0.0036  ? -0.0006 ? -0.0000 ? 
4 'X-RAY DIFFRACTION' ? refined -4.5745  21.4317 9.3834  0.1740 ? 0.0540 ? -0.0292 ? 0.1418 ? 0.0034 ? 0.1688 ? 0.1946 ? -0.0748 ? 
-0.2050 ? 0.4291 ? -0.1643 ? 0.2021 ? 0.0605  ? 0.0999  ? -0.0978 ? -0.1662 ? -0.0081 ? 0.0887  ? 0.2132  ? 0.2099  ? 0.0242  ? 
5 'X-RAY DIFFRACTION' ? refined 8.7000   12.0631 19.2354 0.3396 ? 0.1996 ? 0.0034  ? 0.4106 ? 0.0752 ? 0.3099 ? 0.6372 ? -0.2775 ? 
0.1731  ? 0.7989 ? -0.3856 ? 0.4299 ? 0.2303  ? 0.2032  ? -0.0657 ? -0.2402 ? -0.2701 ? -0.2196 ? 0.4585  ? 0.5236  ? -0.1236 ? 
6 'X-RAY DIFFRACTION' ? refined 0.9741   14.4459 22.9919 0.2450 ? 0.0729 ? -0.0012 ? 0.2301 ? 0.0464 ? 0.2370 ? 0.4212 ? -0.0101 ? 
0.3633  ? 0.2279 ? -0.2609 ? 0.7151 ? 0.0847  ? -0.0855 ? -0.1049 ? -0.1019 ? -0.0850 ? 0.1013  ? 0.1358  ? 0.1076  ? -0.0001 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 43 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 44 through 99 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 100 through 180 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 181 through 213 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 214 through 260 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 261 through 301 )
;
# 
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 
A1EGR C01  C  Y N 1   
A1EGR C02  C  Y N 2   
A1EGR C03  C  Y N 3   
A1EGR C04  C  Y N 4   
A1EGR C05  C  Y N 5   
A1EGR C06  C  Y N 6   
A1EGR C07  C  Y N 7   
A1EGR C10  C  N N 8   
A1EGR C13  C  N N 9   
A1EGR C15  C  N N 10  
A1EGR C17  C  N N 11  
A1EGR C21  C  N N 12  
A1EGR C22  C  Y N 13  
A1EGR C23  C  Y N 14  
A1EGR C24  C  Y N 15  
A1EGR C25  C  Y N 16  
A1EGR C26  C  Y N 17  
A1EGR C27  C  Y N 18  
A1EGR C28  C  N N 19  
A1EGR C29  C  N N 20  
A1EGR C30  C  Y N 21  
A1EGR C31  C  Y N 22  
A1EGR C33  C  Y N 23  
A1EGR C34  C  Y N 24  
A1EGR C35  C  Y N 25  
A1EGR C38  C  N N 26  
A1EGR C39  C  N N 27  
A1EGR C41  C  N N 28  
A1EGR N08  N  Y N 29  
A1EGR N09  N  Y N 30  
A1EGR N12  N  N N 31  
A1EGR N14  N  N N 32  
A1EGR N16  N  N N 33  
A1EGR N19  N  N N 34  
A1EGR N32  N  Y N 35  
A1EGR N37  N  N N 36  
A1EGR O18  O  N N 37  
A1EGR O20  O  N N 38  
A1EGR O36  O  N N 39  
A1EGR O40  O  N N 40  
A1EGR CL11 CL N N 41  
A1EGR H021 H  N N 42  
A1EGR H051 H  N N 43  
A1EGR H071 H  N N 44  
A1EGR H102 H  N N 45  
A1EGR H103 H  N N 46  
A1EGR H101 H  N N 47  
A1EGR H211 H  N N 48  
A1EGR H212 H  N N 49  
A1EGR H241 H  N N 50  
A1EGR H251 H  N N 51  
A1EGR H271 H  N N 52  
A1EGR H291 H  N N 53  
A1EGR H292 H  N N 54  
A1EGR H293 H  N N 55  
A1EGR H311 H  N N 56  
A1EGR H331 H  N N 57  
A1EGR H351 H  N N 58  
A1EGR H381 H  N N 59  
A1EGR H382 H  N N 60  
A1EGR H391 H  N N 61  
A1EGR H392 H  N N 62  
A1EGR H413 H  N N 63  
A1EGR H411 H  N N 64  
A1EGR H412 H  N N 65  
A1EGR H1   H  N N 66  
ALA   N    N  N N 67  
ALA   CA   C  N S 68  
ALA   C    C  N N 69  
ALA   O    O  N N 70  
ALA   CB   C  N N 71  
ALA   OXT  O  N N 72  
ALA   H    H  N N 73  
ALA   H2   H  N N 74  
ALA   HA   H  N N 75  
ALA   HB1  H  N N 76  
ALA   HB2  H  N N 77  
ALA   HB3  H  N N 78  
ALA   HXT  H  N N 79  
ARG   N    N  N N 80  
ARG   CA   C  N S 81  
ARG   C    C  N N 82  
ARG   O    O  N N 83  
ARG   CB   C  N N 84  
ARG   CG   C  N N 85  
ARG   CD   C  N N 86  
ARG   NE   N  N N 87  
ARG   CZ   C  N N 88  
ARG   NH1  N  N N 89  
ARG   NH2  N  N N 90  
ARG   OXT  O  N N 91  
ARG   H    H  N N 92  
ARG   H2   H  N N 93  
ARG   HA   H  N N 94  
ARG   HB2  H  N N 95  
ARG   HB3  H  N N 96  
ARG   HG2  H  N N 97  
ARG   HG3  H  N N 98  
ARG   HD2  H  N N 99  
ARG   HD3  H  N N 100 
ARG   HE   H  N N 101 
ARG   HH11 H  N N 102 
ARG   HH12 H  N N 103 
ARG   HH21 H  N N 104 
ARG   HH22 H  N N 105 
ARG   HXT  H  N N 106 
ASN   N    N  N N 107 
ASN   CA   C  N S 108 
ASN   C    C  N N 109 
ASN   O    O  N N 110 
ASN   CB   C  N N 111 
ASN   CG   C  N N 112 
ASN   OD1  O  N N 113 
ASN   ND2  N  N N 114 
ASN   OXT  O  N N 115 
ASN   H    H  N N 116 
ASN   H2   H  N N 117 
ASN   HA   H  N N 118 
ASN   HB2  H  N N 119 
ASN   HB3  H  N N 120 
ASN   HD21 H  N N 121 
ASN   HD22 H  N N 122 
ASN   HXT  H  N N 123 
ASP   N    N  N N 124 
ASP   CA   C  N S 125 
ASP   C    C  N N 126 
ASP   O    O  N N 127 
ASP   CB   C  N N 128 
ASP   CG   C  N N 129 
ASP   OD1  O  N N 130 
ASP   OD2  O  N N 131 
ASP   OXT  O  N N 132 
ASP   H    H  N N 133 
ASP   H2   H  N N 134 
ASP   HA   H  N N 135 
ASP   HB2  H  N N 136 
ASP   HB3  H  N N 137 
ASP   HD2  H  N N 138 
ASP   HXT  H  N N 139 
CYS   N    N  N N 140 
CYS   CA   C  N R 141 
CYS   C    C  N N 142 
CYS   O    O  N N 143 
CYS   CB   C  N N 144 
CYS   SG   S  N N 145 
CYS   OXT  O  N N 146 
CYS   H    H  N N 147 
CYS   H2   H  N N 148 
CYS   HA   H  N N 149 
CYS   HB2  H  N N 150 
CYS   HB3  H  N N 151 
CYS   HG   H  N N 152 
CYS   HXT  H  N N 153 
GLN   N    N  N N 154 
GLN   CA   C  N S 155 
GLN   C    C  N N 156 
GLN   O    O  N N 157 
GLN   CB   C  N N 158 
GLN   CG   C  N N 159 
GLN   CD   C  N N 160 
GLN   OE1  O  N N 161 
GLN   NE2  N  N N 162 
GLN   OXT  O  N N 163 
GLN   H    H  N N 164 
GLN   H2   H  N N 165 
GLN   HA   H  N N 166 
GLN   HB2  H  N N 167 
GLN   HB3  H  N N 168 
GLN   HG2  H  N N 169 
GLN   HG3  H  N N 170 
GLN   HE21 H  N N 171 
GLN   HE22 H  N N 172 
GLN   HXT  H  N N 173 
GLU   N    N  N N 174 
GLU   CA   C  N S 175 
GLU   C    C  N N 176 
GLU   O    O  N N 177 
GLU   CB   C  N N 178 
GLU   CG   C  N N 179 
GLU   CD   C  N N 180 
GLU   OE1  O  N N 181 
GLU   OE2  O  N N 182 
GLU   OXT  O  N N 183 
GLU   H    H  N N 184 
GLU   H2   H  N N 185 
GLU   HA   H  N N 186 
GLU   HB2  H  N N 187 
GLU   HB3  H  N N 188 
GLU   HG2  H  N N 189 
GLU   HG3  H  N N 190 
GLU   HE2  H  N N 191 
GLU   HXT  H  N N 192 
GLY   N    N  N N 193 
GLY   CA   C  N N 194 
GLY   C    C  N N 195 
GLY   O    O  N N 196 
GLY   OXT  O  N N 197 
GLY   H    H  N N 198 
GLY   H2   H  N N 199 
GLY   HA2  H  N N 200 
GLY   HA3  H  N N 201 
GLY   HXT  H  N N 202 
HIS   N    N  N N 203 
HIS   CA   C  N S 204 
HIS   C    C  N N 205 
HIS   O    O  N N 206 
HIS   CB   C  N N 207 
HIS   CG   C  Y N 208 
HIS   ND1  N  Y N 209 
HIS   CD2  C  Y N 210 
HIS   CE1  C  Y N 211 
HIS   NE2  N  Y N 212 
HIS   OXT  O  N N 213 
HIS   H    H  N N 214 
HIS   H2   H  N N 215 
HIS   HA   H  N N 216 
HIS   HB2  H  N N 217 
HIS   HB3  H  N N 218 
HIS   HD1  H  N N 219 
HIS   HD2  H  N N 220 
HIS   HE1  H  N N 221 
HIS   HE2  H  N N 222 
HIS   HXT  H  N N 223 
HOH   O    O  N N 224 
HOH   H1   H  N N 225 
HOH   H2   H  N N 226 
ILE   N    N  N N 227 
ILE   CA   C  N S 228 
ILE   C    C  N N 229 
ILE   O    O  N N 230 
ILE   CB   C  N S 231 
ILE   CG1  C  N N 232 
ILE   CG2  C  N N 233 
ILE   CD1  C  N N 234 
ILE   OXT  O  N N 235 
ILE   H    H  N N 236 
ILE   H2   H  N N 237 
ILE   HA   H  N N 238 
ILE   HB   H  N N 239 
ILE   HG12 H  N N 240 
ILE   HG13 H  N N 241 
ILE   HG21 H  N N 242 
ILE   HG22 H  N N 243 
ILE   HG23 H  N N 244 
ILE   HD11 H  N N 245 
ILE   HD12 H  N N 246 
ILE   HD13 H  N N 247 
ILE   HXT  H  N N 248 
LEU   N    N  N N 249 
LEU   CA   C  N S 250 
LEU   C    C  N N 251 
LEU   O    O  N N 252 
LEU   CB   C  N N 253 
LEU   CG   C  N N 254 
LEU   CD1  C  N N 255 
LEU   CD2  C  N N 256 
LEU   OXT  O  N N 257 
LEU   H    H  N N 258 
LEU   H2   H  N N 259 
LEU   HA   H  N N 260 
LEU   HB2  H  N N 261 
LEU   HB3  H  N N 262 
LEU   HG   H  N N 263 
LEU   HD11 H  N N 264 
LEU   HD12 H  N N 265 
LEU   HD13 H  N N 266 
LEU   HD21 H  N N 267 
LEU   HD22 H  N N 268 
LEU   HD23 H  N N 269 
LEU   HXT  H  N N 270 
LYS   N    N  N N 271 
LYS   CA   C  N S 272 
LYS   C    C  N N 273 
LYS   O    O  N N 274 
LYS   CB   C  N N 275 
LYS   CG   C  N N 276 
LYS   CD   C  N N 277 
LYS   CE   C  N N 278 
LYS   NZ   N  N N 279 
LYS   OXT  O  N N 280 
LYS   H    H  N N 281 
LYS   H2   H  N N 282 
LYS   HA   H  N N 283 
LYS   HB2  H  N N 284 
LYS   HB3  H  N N 285 
LYS   HG2  H  N N 286 
LYS   HG3  H  N N 287 
LYS   HD2  H  N N 288 
LYS   HD3  H  N N 289 
LYS   HE2  H  N N 290 
LYS   HE3  H  N N 291 
LYS   HZ1  H  N N 292 
LYS   HZ2  H  N N 293 
LYS   HZ3  H  N N 294 
LYS   HXT  H  N N 295 
MET   N    N  N N 296 
MET   CA   C  N S 297 
MET   C    C  N N 298 
MET   O    O  N N 299 
MET   CB   C  N N 300 
MET   CG   C  N N 301 
MET   SD   S  N N 302 
MET   CE   C  N N 303 
MET   OXT  O  N N 304 
MET   H    H  N N 305 
MET   H2   H  N N 306 
MET   HA   H  N N 307 
MET   HB2  H  N N 308 
MET   HB3  H  N N 309 
MET   HG2  H  N N 310 
MET   HG3  H  N N 311 
MET   HE1  H  N N 312 
MET   HE2  H  N N 313 
MET   HE3  H  N N 314 
MET   HXT  H  N N 315 
PHE   N    N  N N 316 
PHE   CA   C  N S 317 
PHE   C    C  N N 318 
PHE   O    O  N N 319 
PHE   CB   C  N N 320 
PHE   CG   C  Y N 321 
PHE   CD1  C  Y N 322 
PHE   CD2  C  Y N 323 
PHE   CE1  C  Y N 324 
PHE   CE2  C  Y N 325 
PHE   CZ   C  Y N 326 
PHE   OXT  O  N N 327 
PHE   H    H  N N 328 
PHE   H2   H  N N 329 
PHE   HA   H  N N 330 
PHE   HB2  H  N N 331 
PHE   HB3  H  N N 332 
PHE   HD1  H  N N 333 
PHE   HD2  H  N N 334 
PHE   HE1  H  N N 335 
PHE   HE2  H  N N 336 
PHE   HZ   H  N N 337 
PHE   HXT  H  N N 338 
PRO   N    N  N N 339 
PRO   CA   C  N S 340 
PRO   C    C  N N 341 
PRO   O    O  N N 342 
PRO   CB   C  N N 343 
PRO   CG   C  N N 344 
PRO   CD   C  N N 345 
PRO   OXT  O  N N 346 
PRO   H    H  N N 347 
PRO   HA   H  N N 348 
PRO   HB2  H  N N 349 
PRO   HB3  H  N N 350 
PRO   HG2  H  N N 351 
PRO   HG3  H  N N 352 
PRO   HD2  H  N N 353 
PRO   HD3  H  N N 354 
PRO   HXT  H  N N 355 
SER   N    N  N N 356 
SER   CA   C  N S 357 
SER   C    C  N N 358 
SER   O    O  N N 359 
SER   CB   C  N N 360 
SER   OG   O  N N 361 
SER   OXT  O  N N 362 
SER   H    H  N N 363 
SER   H2   H  N N 364 
SER   HA   H  N N 365 
SER   HB2  H  N N 366 
SER   HB3  H  N N 367 
SER   HG   H  N N 368 
SER   HXT  H  N N 369 
THR   N    N  N N 370 
THR   CA   C  N S 371 
THR   C    C  N N 372 
THR   O    O  N N 373 
THR   CB   C  N R 374 
THR   OG1  O  N N 375 
THR   CG2  C  N N 376 
THR   OXT  O  N N 377 
THR   H    H  N N 378 
THR   H2   H  N N 379 
THR   HA   H  N N 380 
THR   HB   H  N N 381 
THR   HG1  H  N N 382 
THR   HG21 H  N N 383 
THR   HG22 H  N N 384 
THR   HG23 H  N N 385 
THR   HXT  H  N N 386 
TRP   N    N  N N 387 
TRP   CA   C  N S 388 
TRP   C    C  N N 389 
TRP   O    O  N N 390 
TRP   CB   C  N N 391 
TRP   CG   C  Y N 392 
TRP   CD1  C  Y N 393 
TRP   CD2  C  Y N 394 
TRP   NE1  N  Y N 395 
TRP   CE2  C  Y N 396 
TRP   CE3  C  Y N 397 
TRP   CZ2  C  Y N 398 
TRP   CZ3  C  Y N 399 
TRP   CH2  C  Y N 400 
TRP   OXT  O  N N 401 
TRP   H    H  N N 402 
TRP   H2   H  N N 403 
TRP   HA   H  N N 404 
TRP   HB2  H  N N 405 
TRP   HB3  H  N N 406 
TRP   HD1  H  N N 407 
TRP   HE1  H  N N 408 
TRP   HE3  H  N N 409 
TRP   HZ2  H  N N 410 
TRP   HZ3  H  N N 411 
TRP   HH2  H  N N 412 
TRP   HXT  H  N N 413 
TYR   N    N  N N 414 
TYR   CA   C  N S 415 
TYR   C    C  N N 416 
TYR   O    O  N N 417 
TYR   CB   C  N N 418 
TYR   CG   C  Y N 419 
TYR   CD1  C  Y N 420 
TYR   CD2  C  Y N 421 
TYR   CE1  C  Y N 422 
TYR   CE2  C  Y N 423 
TYR   CZ   C  Y N 424 
TYR   OH   O  N N 425 
TYR   OXT  O  N N 426 
TYR   H    H  N N 427 
TYR   H2   H  N N 428 
TYR   HA   H  N N 429 
TYR   HB2  H  N N 430 
TYR   HB3  H  N N 431 
TYR   HD1  H  N N 432 
TYR   HD2  H  N N 433 
TYR   HE1  H  N N 434 
TYR   HE2  H  N N 435 
TYR   HH   H  N N 436 
TYR   HXT  H  N N 437 
VAL   N    N  N N 438 
VAL   CA   C  N S 439 
VAL   C    C  N N 440 
VAL   O    O  N N 441 
VAL   CB   C  N N 442 
VAL   CG1  C  N N 443 
VAL   CG2  C  N N 444 
VAL   OXT  O  N N 445 
VAL   H    H  N N 446 
VAL   H2   H  N N 447 
VAL   HA   H  N N 448 
VAL   HB   H  N N 449 
VAL   HG11 H  N N 450 
VAL   HG12 H  N N 451 
VAL   HG13 H  N N 452 
VAL   HG21 H  N N 453 
VAL   HG22 H  N N 454 
VAL   HG23 H  N N 455 
VAL   HXT  H  N N 456 
# 
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 
A1EGR C29 C23  sing N N 1   
A1EGR C24 C23  doub Y N 2   
A1EGR C24 C25  sing Y N 3   
A1EGR C23 C22  sing Y N 4   
A1EGR C25 C26  doub Y N 5   
A1EGR C22 C21  sing N N 6   
A1EGR C22 C27  doub Y N 7   
A1EGR C26 C27  sing Y N 8   
A1EGR C26 C28  sing N N 9   
A1EGR C21 N14  sing N N 10  
A1EGR C28 N37  trip N N 11  
A1EGR N19 C01  sing N N 12  
A1EGR N19 C13  doub N N 13  
A1EGR C02 C01  doub Y N 14  
A1EGR C02 C03  sing Y N 15  
A1EGR C01 C06  sing Y N 16  
A1EGR C03 C07  doub Y N 17  
A1EGR C03 C04  sing Y N 18  
A1EGR C07 N08  sing Y N 19  
A1EGR C06 CL11 sing N N 20  
A1EGR C06 C05  doub Y N 21  
A1EGR C04 C05  sing Y N 22  
A1EGR C04 N09  doub Y N 23  
A1EGR N14 C13  sing N N 24  
A1EGR N14 C15  sing N N 25  
A1EGR N08 N09  sing Y N 26  
A1EGR N08 C10  sing N N 27  
A1EGR C13 N12  sing N N 28  
A1EGR O20 C15  doub N N 29  
A1EGR C15 N16  sing N N 30  
A1EGR N12 C17  sing N N 31  
A1EGR N16 C17  sing N N 32  
A1EGR N16 C30  sing N N 33  
A1EGR C17 O18  doub N N 34  
A1EGR C30 C31  doub Y N 35  
A1EGR C30 C35  sing Y N 36  
A1EGR C31 N32  sing Y N 37  
A1EGR C35 C34  doub Y N 38  
A1EGR N32 C33  doub Y N 39  
A1EGR C34 C33  sing Y N 40  
A1EGR C34 O36  sing N N 41  
A1EGR C38 C39  sing N N 42  
A1EGR C38 O36  sing N N 43  
A1EGR C39 O40  sing N N 44  
A1EGR O40 C41  sing N N 45  
A1EGR C02 H021 sing N N 46  
A1EGR C05 H051 sing N N 47  
A1EGR C07 H071 sing N N 48  
A1EGR C10 H102 sing N N 49  
A1EGR C10 H103 sing N N 50  
A1EGR C10 H101 sing N N 51  
A1EGR C21 H211 sing N N 52  
A1EGR C21 H212 sing N N 53  
A1EGR C24 H241 sing N N 54  
A1EGR C25 H251 sing N N 55  
A1EGR C27 H271 sing N N 56  
A1EGR C29 H291 sing N N 57  
A1EGR C29 H292 sing N N 58  
A1EGR C29 H293 sing N N 59  
A1EGR C31 H311 sing N N 60  
A1EGR C33 H331 sing N N 61  
A1EGR C35 H351 sing N N 62  
A1EGR C38 H381 sing N N 63  
A1EGR C38 H382 sing N N 64  
A1EGR C39 H391 sing N N 65  
A1EGR C39 H392 sing N N 66  
A1EGR C41 H413 sing N N 67  
A1EGR C41 H411 sing N N 68  
A1EGR C41 H412 sing N N 69  
A1EGR N12 H1   sing N N 70  
ALA   N   CA   sing N N 71  
ALA   N   H    sing N N 72  
ALA   N   H2   sing N N 73  
ALA   CA  C    sing N N 74  
ALA   CA  CB   sing N N 75  
ALA   CA  HA   sing N N 76  
ALA   C   O    doub N N 77  
ALA   C   OXT  sing N N 78  
ALA   CB  HB1  sing N N 79  
ALA   CB  HB2  sing N N 80  
ALA   CB  HB3  sing N N 81  
ALA   OXT HXT  sing N N 82  
ARG   N   CA   sing N N 83  
ARG   N   H    sing N N 84  
ARG   N   H2   sing N N 85  
ARG   CA  C    sing N N 86  
ARG   CA  CB   sing N N 87  
ARG   CA  HA   sing N N 88  
ARG   C   O    doub N N 89  
ARG   C   OXT  sing N N 90  
ARG   CB  CG   sing N N 91  
ARG   CB  HB2  sing N N 92  
ARG   CB  HB3  sing N N 93  
ARG   CG  CD   sing N N 94  
ARG   CG  HG2  sing N N 95  
ARG   CG  HG3  sing N N 96  
ARG   CD  NE   sing N N 97  
ARG   CD  HD2  sing N N 98  
ARG   CD  HD3  sing N N 99  
ARG   NE  CZ   sing N N 100 
ARG   NE  HE   sing N N 101 
ARG   CZ  NH1  sing N N 102 
ARG   CZ  NH2  doub N N 103 
ARG   NH1 HH11 sing N N 104 
ARG   NH1 HH12 sing N N 105 
ARG   NH2 HH21 sing N N 106 
ARG   NH2 HH22 sing N N 107 
ARG   OXT HXT  sing N N 108 
ASN   N   CA   sing N N 109 
ASN   N   H    sing N N 110 
ASN   N   H2   sing N N 111 
ASN   CA  C    sing N N 112 
ASN   CA  CB   sing N N 113 
ASN   CA  HA   sing N N 114 
ASN   C   O    doub N N 115 
ASN   C   OXT  sing N N 116 
ASN   CB  CG   sing N N 117 
ASN   CB  HB2  sing N N 118 
ASN   CB  HB3  sing N N 119 
ASN   CG  OD1  doub N N 120 
ASN   CG  ND2  sing N N 121 
ASN   ND2 HD21 sing N N 122 
ASN   ND2 HD22 sing N N 123 
ASN   OXT HXT  sing N N 124 
ASP   N   CA   sing N N 125 
ASP   N   H    sing N N 126 
ASP   N   H2   sing N N 127 
ASP   CA  C    sing N N 128 
ASP   CA  CB   sing N N 129 
ASP   CA  HA   sing N N 130 
ASP   C   O    doub N N 131 
ASP   C   OXT  sing N N 132 
ASP   CB  CG   sing N N 133 
ASP   CB  HB2  sing N N 134 
ASP   CB  HB3  sing N N 135 
ASP   CG  OD1  doub N N 136 
ASP   CG  OD2  sing N N 137 
ASP   OD2 HD2  sing N N 138 
ASP   OXT HXT  sing N N 139 
CYS   N   CA   sing N N 140 
CYS   N   H    sing N N 141 
CYS   N   H2   sing N N 142 
CYS   CA  C    sing N N 143 
CYS   CA  CB   sing N N 144 
CYS   CA  HA   sing N N 145 
CYS   C   O    doub N N 146 
CYS   C   OXT  sing N N 147 
CYS   CB  SG   sing N N 148 
CYS   CB  HB2  sing N N 149 
CYS   CB  HB3  sing N N 150 
CYS   SG  HG   sing N N 151 
CYS   OXT HXT  sing N N 152 
GLN   N   CA   sing N N 153 
GLN   N   H    sing N N 154 
GLN   N   H2   sing N N 155 
GLN   CA  C    sing N N 156 
GLN   CA  CB   sing N N 157 
GLN   CA  HA   sing N N 158 
GLN   C   O    doub N N 159 
GLN   C   OXT  sing N N 160 
GLN   CB  CG   sing N N 161 
GLN   CB  HB2  sing N N 162 
GLN   CB  HB3  sing N N 163 
GLN   CG  CD   sing N N 164 
GLN   CG  HG2  sing N N 165 
GLN   CG  HG3  sing N N 166 
GLN   CD  OE1  doub N N 167 
GLN   CD  NE2  sing N N 168 
GLN   NE2 HE21 sing N N 169 
GLN   NE2 HE22 sing N N 170 
GLN   OXT HXT  sing N N 171 
GLU   N   CA   sing N N 172 
GLU   N   H    sing N N 173 
GLU   N   H2   sing N N 174 
GLU   CA  C    sing N N 175 
GLU   CA  CB   sing N N 176 
GLU   CA  HA   sing N N 177 
GLU   C   O    doub N N 178 
GLU   C   OXT  sing N N 179 
GLU   CB  CG   sing N N 180 
GLU   CB  HB2  sing N N 181 
GLU   CB  HB3  sing N N 182 
GLU   CG  CD   sing N N 183 
GLU   CG  HG2  sing N N 184 
GLU   CG  HG3  sing N N 185 
GLU   CD  OE1  doub N N 186 
GLU   CD  OE2  sing N N 187 
GLU   OE2 HE2  sing N N 188 
GLU   OXT HXT  sing N N 189 
GLY   N   CA   sing N N 190 
GLY   N   H    sing N N 191 
GLY   N   H2   sing N N 192 
GLY   CA  C    sing N N 193 
GLY   CA  HA2  sing N N 194 
GLY   CA  HA3  sing N N 195 
GLY   C   O    doub N N 196 
GLY   C   OXT  sing N N 197 
GLY   OXT HXT  sing N N 198 
HIS   N   CA   sing N N 199 
HIS   N   H    sing N N 200 
HIS   N   H2   sing N N 201 
HIS   CA  C    sing N N 202 
HIS   CA  CB   sing N N 203 
HIS   CA  HA   sing N N 204 
HIS   C   O    doub N N 205 
HIS   C   OXT  sing N N 206 
HIS   CB  CG   sing N N 207 
HIS   CB  HB2  sing N N 208 
HIS   CB  HB3  sing N N 209 
HIS   CG  ND1  sing Y N 210 
HIS   CG  CD2  doub Y N 211 
HIS   ND1 CE1  doub Y N 212 
HIS   ND1 HD1  sing N N 213 
HIS   CD2 NE2  sing Y N 214 
HIS   CD2 HD2  sing N N 215 
HIS   CE1 NE2  sing Y N 216 
HIS   CE1 HE1  sing N N 217 
HIS   NE2 HE2  sing N N 218 
HIS   OXT HXT  sing N N 219 
HOH   O   H1   sing N N 220 
HOH   O   H2   sing N N 221 
ILE   N   CA   sing N N 222 
ILE   N   H    sing N N 223 
ILE   N   H2   sing N N 224 
ILE   CA  C    sing N N 225 
ILE   CA  CB   sing N N 226 
ILE   CA  HA   sing N N 227 
ILE   C   O    doub N N 228 
ILE   C   OXT  sing N N 229 
ILE   CB  CG1  sing N N 230 
ILE   CB  CG2  sing N N 231 
ILE   CB  HB   sing N N 232 
ILE   CG1 CD1  sing N N 233 
ILE   CG1 HG12 sing N N 234 
ILE   CG1 HG13 sing N N 235 
ILE   CG2 HG21 sing N N 236 
ILE   CG2 HG22 sing N N 237 
ILE   CG2 HG23 sing N N 238 
ILE   CD1 HD11 sing N N 239 
ILE   CD1 HD12 sing N N 240 
ILE   CD1 HD13 sing N N 241 
ILE   OXT HXT  sing N N 242 
LEU   N   CA   sing N N 243 
LEU   N   H    sing N N 244 
LEU   N   H2   sing N N 245 
LEU   CA  C    sing N N 246 
LEU   CA  CB   sing N N 247 
LEU   CA  HA   sing N N 248 
LEU   C   O    doub N N 249 
LEU   C   OXT  sing N N 250 
LEU   CB  CG   sing N N 251 
LEU   CB  HB2  sing N N 252 
LEU   CB  HB3  sing N N 253 
LEU   CG  CD1  sing N N 254 
LEU   CG  CD2  sing N N 255 
LEU   CG  HG   sing N N 256 
LEU   CD1 HD11 sing N N 257 
LEU   CD1 HD12 sing N N 258 
LEU   CD1 HD13 sing N N 259 
LEU   CD2 HD21 sing N N 260 
LEU   CD2 HD22 sing N N 261 
LEU   CD2 HD23 sing N N 262 
LEU   OXT HXT  sing N N 263 
LYS   N   CA   sing N N 264 
LYS   N   H    sing N N 265 
LYS   N   H2   sing N N 266 
LYS   CA  C    sing N N 267 
LYS   CA  CB   sing N N 268 
LYS   CA  HA   sing N N 269 
LYS   C   O    doub N N 270 
LYS   C   OXT  sing N N 271 
LYS   CB  CG   sing N N 272 
LYS   CB  HB2  sing N N 273 
LYS   CB  HB3  sing N N 274 
LYS   CG  CD   sing N N 275 
LYS   CG  HG2  sing N N 276 
LYS   CG  HG3  sing N N 277 
LYS   CD  CE   sing N N 278 
LYS   CD  HD2  sing N N 279 
LYS   CD  HD3  sing N N 280 
LYS   CE  NZ   sing N N 281 
LYS   CE  HE2  sing N N 282 
LYS   CE  HE3  sing N N 283 
LYS   NZ  HZ1  sing N N 284 
LYS   NZ  HZ2  sing N N 285 
LYS   NZ  HZ3  sing N N 286 
LYS   OXT HXT  sing N N 287 
MET   N   CA   sing N N 288 
MET   N   H    sing N N 289 
MET   N   H2   sing N N 290 
MET   CA  C    sing N N 291 
MET   CA  CB   sing N N 292 
MET   CA  HA   sing N N 293 
MET   C   O    doub N N 294 
MET   C   OXT  sing N N 295 
MET   CB  CG   sing N N 296 
MET   CB  HB2  sing N N 297 
MET   CB  HB3  sing N N 298 
MET   CG  SD   sing N N 299 
MET   CG  HG2  sing N N 300 
MET   CG  HG3  sing N N 301 
MET   SD  CE   sing N N 302 
MET   CE  HE1  sing N N 303 
MET   CE  HE2  sing N N 304 
MET   CE  HE3  sing N N 305 
MET   OXT HXT  sing N N 306 
PHE   N   CA   sing N N 307 
PHE   N   H    sing N N 308 
PHE   N   H2   sing N N 309 
PHE   CA  C    sing N N 310 
PHE   CA  CB   sing N N 311 
PHE   CA  HA   sing N N 312 
PHE   C   O    doub N N 313 
PHE   C   OXT  sing N N 314 
PHE   CB  CG   sing N N 315 
PHE   CB  HB2  sing N N 316 
PHE   CB  HB3  sing N N 317 
PHE   CG  CD1  doub Y N 318 
PHE   CG  CD2  sing Y N 319 
PHE   CD1 CE1  sing Y N 320 
PHE   CD1 HD1  sing N N 321 
PHE   CD2 CE2  doub Y N 322 
PHE   CD2 HD2  sing N N 323 
PHE   CE1 CZ   doub Y N 324 
PHE   CE1 HE1  sing N N 325 
PHE   CE2 CZ   sing Y N 326 
PHE   CE2 HE2  sing N N 327 
PHE   CZ  HZ   sing N N 328 
PHE   OXT HXT  sing N N 329 
PRO   N   CA   sing N N 330 
PRO   N   CD   sing N N 331 
PRO   N   H    sing N N 332 
PRO   CA  C    sing N N 333 
PRO   CA  CB   sing N N 334 
PRO   CA  HA   sing N N 335 
PRO   C   O    doub N N 336 
PRO   C   OXT  sing N N 337 
PRO   CB  CG   sing N N 338 
PRO   CB  HB2  sing N N 339 
PRO   CB  HB3  sing N N 340 
PRO   CG  CD   sing N N 341 
PRO   CG  HG2  sing N N 342 
PRO   CG  HG3  sing N N 343 
PRO   CD  HD2  sing N N 344 
PRO   CD  HD3  sing N N 345 
PRO   OXT HXT  sing N N 346 
SER   N   CA   sing N N 347 
SER   N   H    sing N N 348 
SER   N   H2   sing N N 349 
SER   CA  C    sing N N 350 
SER   CA  CB   sing N N 351 
SER   CA  HA   sing N N 352 
SER   C   O    doub N N 353 
SER   C   OXT  sing N N 354 
SER   CB  OG   sing N N 355 
SER   CB  HB2  sing N N 356 
SER   CB  HB3  sing N N 357 
SER   OG  HG   sing N N 358 
SER   OXT HXT  sing N N 359 
THR   N   CA   sing N N 360 
THR   N   H    sing N N 361 
THR   N   H2   sing N N 362 
THR   CA  C    sing N N 363 
THR   CA  CB   sing N N 364 
THR   CA  HA   sing N N 365 
THR   C   O    doub N N 366 
THR   C   OXT  sing N N 367 
THR   CB  OG1  sing N N 368 
THR   CB  CG2  sing N N 369 
THR   CB  HB   sing N N 370 
THR   OG1 HG1  sing N N 371 
THR   CG2 HG21 sing N N 372 
THR   CG2 HG22 sing N N 373 
THR   CG2 HG23 sing N N 374 
THR   OXT HXT  sing N N 375 
TRP   N   CA   sing N N 376 
TRP   N   H    sing N N 377 
TRP   N   H2   sing N N 378 
TRP   CA  C    sing N N 379 
TRP   CA  CB   sing N N 380 
TRP   CA  HA   sing N N 381 
TRP   C   O    doub N N 382 
TRP   C   OXT  sing N N 383 
TRP   CB  CG   sing N N 384 
TRP   CB  HB2  sing N N 385 
TRP   CB  HB3  sing N N 386 
TRP   CG  CD1  doub Y N 387 
TRP   CG  CD2  sing Y N 388 
TRP   CD1 NE1  sing Y N 389 
TRP   CD1 HD1  sing N N 390 
TRP   CD2 CE2  doub Y N 391 
TRP   CD2 CE3  sing Y N 392 
TRP   NE1 CE2  sing Y N 393 
TRP   NE1 HE1  sing N N 394 
TRP   CE2 CZ2  sing Y N 395 
TRP   CE3 CZ3  doub Y N 396 
TRP   CE3 HE3  sing N N 397 
TRP   CZ2 CH2  doub Y N 398 
TRP   CZ2 HZ2  sing N N 399 
TRP   CZ3 CH2  sing Y N 400 
TRP   CZ3 HZ3  sing N N 401 
TRP   CH2 HH2  sing N N 402 
TRP   OXT HXT  sing N N 403 
TYR   N   CA   sing N N 404 
TYR   N   H    sing N N 405 
TYR   N   H2   sing N N 406 
TYR   CA  C    sing N N 407 
TYR   CA  CB   sing N N 408 
TYR   CA  HA   sing N N 409 
TYR   C   O    doub N N 410 
TYR   C   OXT  sing N N 411 
TYR   CB  CG   sing N N 412 
TYR   CB  HB2  sing N N 413 
TYR   CB  HB3  sing N N 414 
TYR   CG  CD1  doub Y N 415 
TYR   CG  CD2  sing Y N 416 
TYR   CD1 CE1  sing Y N 417 
TYR   CD1 HD1  sing N N 418 
TYR   CD2 CE2  doub Y N 419 
TYR   CD2 HD2  sing N N 420 
TYR   CE1 CZ   doub Y N 421 
TYR   CE1 HE1  sing N N 422 
TYR   CE2 CZ   sing Y N 423 
TYR   CE2 HE2  sing N N 424 
TYR   CZ  OH   sing N N 425 
TYR   OH  HH   sing N N 426 
TYR   OXT HXT  sing N N 427 
VAL   N   CA   sing N N 428 
VAL   N   H    sing N N 429 
VAL   N   H2   sing N N 430 
VAL   CA  C    sing N N 431 
VAL   CA  CB   sing N N 432 
VAL   CA  HA   sing N N 433 
VAL   C   O    doub N N 434 
VAL   C   OXT  sing N N 435 
VAL   CB  CG1  sing N N 436 
VAL   CB  CG2  sing N N 437 
VAL   CB  HB   sing N N 438 
VAL   CG1 HG11 sing N N 439 
VAL   CG1 HG12 sing N N 440 
VAL   CG1 HG13 sing N N 441 
VAL   CG2 HG21 sing N N 442 
VAL   CG2 HG22 sing N N 443 
VAL   CG2 HG23 sing N N 444 
VAL   OXT HXT  sing N N 445 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 32100142     1 
'Other private'                                       ?     2023A04J0163 2 
'Other private'                                       ?     SRPG22-003   3 
'Other private'                                       ?     SRPG22-011   4 
# 
_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   6LU7 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KSJ 
_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]   0.010289 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004659 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012255 
_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]   0.021183 
_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 
H  
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    . SER   A 1 1   ? -0.097  25.892 36.694  1.00 23.99  ? 1   SER   A N    1 
ATOM   2    C  CA   . SER   A 1 1   ? -0.334  24.641 35.964  1.00 26.86  ? 1   SER   A CA   1 
ATOM   3    C  C    . SER   A 1 1   ? -1.613  24.705 35.141  1.00 26.42  ? 1   SER   A C    1 
ATOM   4    O  O    . SER   A 1 1   ? -2.416  25.634 35.272  1.00 23.29  ? 1   SER   A O    1 
ATOM   5    C  CB   . SER   A 1 1   ? -0.429  23.453 36.929  1.00 27.45  ? 1   SER   A CB   1 
ATOM   6    O  OG   . SER   A 1 1   ? 0.725   23.333 37.733  1.00 32.09  ? 1   SER   A OG   1 
ATOM   7    N  N    . GLY   A 1 2   ? -1.811  23.692 34.310  1.00 26.20  ? 2   GLY   A N    1 
ATOM   8    C  CA   . GLY   A 1 2   ? -2.994  23.572 33.485  1.00 23.93  ? 2   GLY   A CA   1 
ATOM   9    C  C    . GLY   A 1 2   ? -2.682  23.853 32.028  1.00 24.86  ? 2   GLY   A C    1 
ATOM   10   O  O    . GLY   A 1 2   ? -1.677  24.475 31.681  1.00 23.72  ? 2   GLY   A O    1 
ATOM   11   N  N    . PHE   A 1 3   ? -3.548  23.357 31.153  1.00 21.07  ? 3   PHE   A N    1 
ATOM   12   C  CA   . PHE   A 1 3   ? -3.298  23.555 29.729  1.00 22.53  ? 3   PHE   A CA   1 
ATOM   13   C  C    . PHE   A 1 3   ? -4.638  23.664 29.025  1.00 28.14  ? 3   PHE   A C    1 
ATOM   14   O  O    . PHE   A 1 3   ? -5.469  22.753 29.115  1.00 26.84  ? 3   PHE   A O    1 
ATOM   15   C  CB   . PHE   A 1 3   ? -2.464  22.411 29.141  1.00 20.51  ? 3   PHE   A CB   1 
ATOM   16   C  CG   . PHE   A 1 3   ? -1.791  22.775 27.841  1.00 22.69  ? 3   PHE   A CG   1 
ATOM   17   C  CD1  . PHE   A 1 3   ? -0.687  23.617 27.842  1.00 28.20  ? 3   PHE   A CD1  1 
ATOM   18   C  CD2  . PHE   A 1 3   ? -2.262  22.299 26.641  1.00 29.92  ? 3   PHE   A CD2  1 
ATOM   19   C  CE1  . PHE   A 1 3   ? -0.067  23.980 26.648  1.00 32.00  ? 3   PHE   A CE1  1 
ATOM   20   C  CE2  . PHE   A 1 3   ? -1.644  22.651 25.455  1.00 25.36  ? 3   PHE   A CE2  1 
ATOM   21   C  CZ   . PHE   A 1 3   ? -0.546  23.490 25.468  1.00 28.55  ? 3   PHE   A CZ   1 
ATOM   22   N  N    . ARG   A 1 4   ? -4.865  24.784 28.348  1.00 21.65  ? 4   ARG   A N    1 
ATOM   23   C  CA   . ARG   A 1 4   ? -6.154  25.025 27.740  1.00 21.62  ? 4   ARG   A CA   1 
ATOM   24   C  C    . ARG   A 1 4   ? -5.938  25.492 26.311  1.00 21.20  ? 4   ARG   A C    1 
ATOM   25   O  O    . ARG   A 1 4   ? -4.876  26.012 25.981  1.00 24.18  ? 4   ARG   A O    1 
ATOM   26   C  CB   . ARG   A 1 4   ? -6.956  26.085 28.506  1.00 24.24  ? 4   ARG   A CB   1 
ATOM   27   C  CG   . ARG   A 1 4   ? -7.538  25.504 29.781  1.00 27.59  ? 4   ARG   A CG   1 
ATOM   28   C  CD   . ARG   A 1 4   ? -9.012  25.339 29.556  1.00 31.28  ? 4   ARG   A CD   1 
ATOM   29   N  NE   . ARG   A 1 4   ? -9.772  24.909 30.718  1.00 32.42  ? 4   ARG   A NE   1 
ATOM   30   C  CZ   . ARG   A 1 4   ? -10.871 24.168 30.628  1.00 33.63  ? 4   ARG   A CZ   1 
ATOM   31   N  NH1  . ARG   A 1 4   ? -11.355 23.791 29.454  1.00 30.88  ? 4   ARG   A NH1  1 
ATOM   32   N  NH2  . ARG   A 1 4   ? -11.500 23.796 31.738  1.00 24.82  ? 4   ARG   A NH2  1 
ATOM   33   N  N    . LYS   A 1 5   ? -6.965  25.345 25.482  1.00 21.51  ? 5   LYS   A N    1 
ATOM   34   C  CA   . LYS   A 1 5   ? -6.927  26.010 24.176  1.00 22.33  ? 5   LYS   A CA   1 
ATOM   35   C  C    . LYS   A 1 5   ? -7.130  27.499 24.397  1.00 20.75  ? 5   LYS   A C    1 
ATOM   36   O  O    . LYS   A 1 5   ? -8.248  27.968 24.597  1.00 28.32  ? 5   LYS   A O    1 
ATOM   37   C  CB   . LYS   A 1 5   ? -7.959  25.431 23.220  1.00 30.69  ? 5   LYS   A CB   1 
ATOM   38   C  CG   . LYS   A 1 5   ? -7.271  24.886 21.974  1.00 38.33  ? 5   LYS   A CG   1 
ATOM   39   C  CD   . LYS   A 1 5   ? -7.898  23.620 21.471  1.00 44.38  ? 5   LYS   A CD   1 
ATOM   40   C  CE   . LYS   A 1 5   ? -6.945  22.958 20.493  1.00 39.75  ? 5   LYS   A CE   1 
ATOM   41   N  NZ   . LYS   A 1 5   ? -7.645  21.923 19.705  1.00 45.54  ? 5   LYS   A NZ   1 
ATOM   42   N  N    . MET   A 1 6   ? -6.036  28.248 24.346  1.00 19.91  ? 6   MET   A N    1 
ATOM   43   C  CA   . MET   A 1 6   ? -6.000  29.647 24.741  1.00 21.36  ? 6   MET   A CA   1 
ATOM   44   C  C    . MET   A 1 6   ? -5.845  30.555 23.530  1.00 20.60  ? 6   MET   A C    1 
ATOM   45   O  O    . MET   A 1 6   ? -4.923  30.379 22.727  1.00 25.19  ? 6   MET   A O    1 
ATOM   46   C  CB   . MET   A 1 6   ? -4.858  29.869 25.737  1.00 23.19  ? 6   MET   A CB   1 
ATOM   47   C  CG   . MET   A 1 6   ? -5.082  31.024 26.652  1.00 37.32  ? 6   MET   A CG   1 
ATOM   48   S  SD   . MET   A 1 6   ? -3.546  31.380 27.508  1.00 36.44  ? 6   MET   A SD   1 
ATOM   49   C  CE   . MET   A 1 6   ? -3.717  30.182 28.826  1.00 35.61  ? 6   MET   A CE   1 
ATOM   50   N  N    . ALA   A 1 7   ? -6.737  31.524 23.407  1.00 16.61  ? 7   ALA   A N    1 
ATOM   51   C  CA   . ALA   A 1 7   ? -6.659  32.485 22.315  1.00 17.61  ? 7   ALA   A CA   1 
ATOM   52   C  C    . ALA   A 1 7   ? -5.956  33.751 22.797  1.00 21.44  ? 7   ALA   A C    1 
ATOM   53   O  O    . ALA   A 1 7   ? -5.793  33.978 23.999  1.00 19.97  ? 7   ALA   A O    1 
ATOM   54   C  CB   . ALA   A 1 7   ? -8.058  32.799 21.777  1.00 17.24  ? 7   ALA   A CB   1 
ATOM   55   N  N    . PHE   A 1 8   ? -5.535  34.592 21.845  1.00 18.54  ? 8   PHE   A N    1 
ATOM   56   C  CA   . PHE   A 1 8   ? -5.018  35.894 22.230  1.00 20.95  ? 8   PHE   A CA   1 
ATOM   57   C  C    . PHE   A 1 8   ? -6.161  36.799 22.688  1.00 19.07  ? 8   PHE   A C    1 
ATOM   58   O  O    . PHE   A 1 8   ? -7.305  36.643 22.252  1.00 20.83  ? 8   PHE   A O    1 
ATOM   59   C  CB   . PHE   A 1 8   ? -4.284  36.555 21.068  1.00 19.48  ? 8   PHE   A CB   1 
ATOM   60   C  CG   . PHE   A 1 8   ? -2.918  35.979 20.826  1.00 20.43  ? 8   PHE   A CG   1 
ATOM   61   C  CD1  . PHE   A 1 8   ? -1.868  36.258 21.680  1.00 22.18  ? 8   PHE   A CD1  1 
ATOM   62   C  CD2  . PHE   A 1 8   ? -2.725  35.055 19.812  1.00 22.15  ? 8   PHE   A CD2  1 
ATOM   63   C  CE1  . PHE   A 1 8   ? -0.621  35.696 21.486  1.00 25.85  ? 8   PHE   A CE1  1 
ATOM   64   C  CE2  . PHE   A 1 8   ? -1.466  34.470 19.624  1.00 25.16  ? 8   PHE   A CE2  1 
ATOM   65   C  CZ   . PHE   A 1 8   ? -0.424  34.803 20.455  1.00 26.78  ? 8   PHE   A CZ   1 
ATOM   66   N  N    . PRO   A 1 9   ? -5.880  37.740 23.585  1.00 17.48  ? 9   PRO   A N    1 
ATOM   67   C  CA   . PRO   A 1 9   ? -6.900  38.723 23.953  1.00 18.39  ? 9   PRO   A CA   1 
ATOM   68   C  C    . PRO   A 1 9   ? -7.335  39.447 22.688  1.00 20.96  ? 9   PRO   A C    1 
ATOM   69   O  O    . PRO   A 1 9   ? -6.494  39.860 21.884  1.00 22.59  ? 9   PRO   A O    1 
ATOM   70   C  CB   . PRO   A 1 9   ? -6.158  39.673 24.898  1.00 19.75  ? 9   PRO   A CB   1 
ATOM   71   C  CG   . PRO   A 1 9   ? -4.978  38.847 25.458  1.00 20.01  ? 9   PRO   A CG   1 
ATOM   72   C  CD   . PRO   A 1 9   ? -4.609  37.915 24.311  1.00 21.85  ? 9   PRO   A CD   1 
ATOM   73   N  N    . SER   A 1 10  ? -8.648  39.620 22.531  1.00 17.87  ? 10  SER   A N    1 
ATOM   74   C  CA   . SER   A 1 10  ? -9.240  39.992 21.236  1.00 18.08  ? 10  SER   A CA   1 
ATOM   75   C  C    . SER   A 1 10  ? -9.522  41.485 21.094  1.00 18.85  ? 10  SER   A C    1 
ATOM   76   O  O    . SER   A 1 10  ? -9.936  41.934 20.010  1.00 18.82  ? 10  SER   A O    1 
ATOM   77   C  CB   . SER   A 1 10  ? -10.527 39.183 21.024  1.00 18.12  ? 10  SER   A CB   1 
ATOM   78   O  OG   . SER   A 1 10  ? -11.495 39.489 22.029  1.00 21.47  ? 10  SER   A OG   1 
ATOM   79   N  N    . GLY   A 1 11  ? -9.279  42.274 22.141  1.00 18.15  ? 11  GLY   A N    1 
ATOM   80   C  CA   . GLY   A 1 11  ? -9.714  43.669 22.129  1.00 18.10  ? 11  GLY   A CA   1 
ATOM   81   C  C    . GLY   A 1 11  ? -9.174  44.476 20.955  1.00 20.39  ? 11  GLY   A C    1 
ATOM   82   O  O    . GLY   A 1 11  ? -9.918  45.248 20.323  1.00 23.16  ? 11  GLY   A O    1 
ATOM   83   N  N    . LYS   A 1 12  ? -7.867  44.317 20.658  1.00 21.12  ? 12  LYS   A N    1 
ATOM   84   C  CA   . LYS   A 1 12  ? -7.251  45.076 19.572  1.00 21.37  ? 12  LYS   A CA   1 
ATOM   85   C  C    . LYS   A 1 12  ? -7.952  44.818 18.253  1.00 23.43  ? 12  LYS   A C    1 
ATOM   86   O  O    . LYS   A 1 12  ? -7.984  45.692 17.381  1.00 23.41  ? 12  LYS   A O    1 
ATOM   87   C  CB   . LYS   A 1 12  ? -5.766  44.731 19.417  1.00 19.24  ? 12  LYS   A CB   1 
ATOM   88   C  CG   . LYS   A 1 12  ? -4.833  45.530 20.343  1.00 25.20  ? 12  LYS   A CG   1 
ATOM   89   C  CD   . LYS   A 1 12  ? -3.459  44.898 20.308  1.00 28.80  ? 12  LYS   A CD   1 
ATOM   90   C  CE   . LYS   A 1 12  ? -2.484  45.613 21.234  1.00 45.09  ? 12  LYS   A CE   1 
ATOM   91   N  NZ   . LYS   A 1 12  ? -2.990  45.731 22.629  1.00 44.40  ? 12  LYS   A NZ   1 
ATOM   92   N  N    . VAL   A 1 13  ? -8.511  43.629 18.084  1.00 19.99  ? 13  VAL   A N    1 
ATOM   93   C  CA   . VAL   A 1 13  ? -9.198  43.303 16.834  1.00 20.09  ? 13  VAL   A CA   1 
ATOM   94   C  C    . VAL   A 1 13  ? -10.663 43.713 16.899  1.00 20.59  ? 13  VAL   A C    1 
ATOM   95   O  O    . VAL   A 1 13  ? -11.223 44.202 15.914  1.00 20.59  ? 13  VAL   A O    1 
ATOM   96   C  CB   . VAL   A 1 13  ? -9.040  41.799 16.551  1.00 18.39  ? 13  VAL   A CB   1 
ATOM   97   C  CG1  . VAL   A 1 13  ? -9.766  41.403 15.224  1.00 17.99  ? 13  VAL   A CG1  1 
ATOM   98   C  CG2  . VAL   A 1 13  ? -7.580  41.457 16.475  1.00 18.14  ? 13  VAL   A CG2  1 
ATOM   99   N  N    . GLU   A 1 14  ? -11.297 43.541 18.079  1.00 19.28  ? 14  GLU   A N    1 
ATOM   100  C  CA   . GLU   A 1 14  ? -12.682 43.993 18.229  1.00 17.32  ? 14  GLU   A CA   1 
ATOM   101  C  C    . GLU   A 1 14  ? -12.830 45.427 17.756  1.00 20.13  ? 14  GLU   A C    1 
ATOM   102  O  O    . GLU   A 1 14  ? -13.857 45.782 17.166  1.00 21.00  ? 14  GLU   A O    1 
ATOM   103  C  CB   . GLU   A 1 14  ? -13.177 43.889 19.691  1.00 17.79  ? 14  GLU   A CB   1 
ATOM   104  C  CG   . GLU   A 1 14  ? -13.201 42.475 20.214  1.00 17.14  ? 14  GLU   A CG   1 
ATOM   105  C  CD   . GLU   A 1 14  ? -13.330 42.407 21.745  1.00 17.63  ? 14  GLU   A CD   1 
ATOM   106  O  OE1  . GLU   A 1 14  ? -14.199 43.141 22.283  1.00 23.14  ? 14  GLU   A OE1  1 
ATOM   107  O  OE2  . GLU   A 1 14  ? -12.554 41.662 22.365  1.00 22.16  ? 14  GLU   A OE2  1 
ATOM   108  N  N    . GLY   A 1 15  ? -11.822 46.268 18.023  1.00 22.44  ? 15  GLY   A N    1 
ATOM   109  C  CA   . GLY   A 1 15  ? -11.938 47.686 17.661  1.00 23.33  ? 15  GLY   A CA   1 
ATOM   110  C  C    . GLY   A 1 15  ? -11.894 47.954 16.175  1.00 23.92  ? 15  GLY   A C    1 
ATOM   111  O  O    . GLY   A 1 15  ? -12.090 49.102 15.744  1.00 24.08  ? 15  GLY   A O    1 
ATOM   112  N  N    . CYS   A 1 16  ? -11.609 46.934 15.387  1.00 21.13  ? 16  CYS   A N    1 
ATOM   113  C  CA   . CYS   A 1 16  ? -11.557 47.114 13.943  1.00 21.15  ? 16  CYS   A CA   1 
ATOM   114  C  C    . CYS   A 1 16  ? -12.672 46.469 13.156  1.00 23.18  ? 16  CYS   A C    1 
ATOM   115  O  O    . CYS   A 1 16  ? -12.679 46.621 11.928  1.00 19.84  ? 16  CYS   A O    1 
ATOM   116  C  CB   . CYS   A 1 16  ? -10.228 46.642 13.356  1.00 22.40  ? 16  CYS   A CB   1 
ATOM   117  S  SG   . CYS   A 1 16  ? -8.726  47.008 14.248  1.00 24.57  ? 16  CYS   A SG   1 
ATOM   118  N  N    . MET   A 1 17  ? -13.604 45.772 13.797  1.00 22.04  ? 17  MET   A N    1 
ATOM   119  C  CA   . MET   A 1 17  ? -14.669 45.093 13.059  1.00 19.45  ? 17  MET   A CA   1 
ATOM   120  C  C    . MET   A 1 17  ? -15.803 46.045 12.708  1.00 24.86  ? 17  MET   A C    1 
ATOM   121  O  O    . MET   A 1 17  ? -16.261 46.826 13.540  1.00 24.43  ? 17  MET   A O    1 
ATOM   122  C  CB   . MET   A 1 17  ? -15.211 43.909 13.864  1.00 19.96  ? 17  MET   A CB   1 
ATOM   123  C  CG   . MET   A 1 17  ? -14.207 42.781 14.202  1.00 22.32  ? 17  MET   A CG   1 
ATOM   124  S  SD   . MET   A 1 17  ? -13.113 42.344 12.796  1.00 21.98  ? 17  MET   A SD   1 
ATOM   125  C  CE   . MET   A 1 17  ? -14.370 41.669 11.705  1.00 23.45  ? 17  MET   A CE   1 
ATOM   126  N  N    . VAL   A 1 18  ? -16.260 45.966 11.459  1.00 18.89  ? 18  VAL   A N    1 
ATOM   127  C  CA   . VAL   A 1 18  ? -17.359 46.777 10.943  1.00 19.58  ? 18  VAL   A CA   1 
ATOM   128  C  C    . VAL   A 1 18  ? -18.282 45.888 10.113  1.00 23.76  ? 18  VAL   A C    1 
ATOM   129  O  O    . VAL   A 1 18  ? -17.982 44.730 9.836   1.00 21.01  ? 18  VAL   A O    1 
ATOM   130  C  CB   . VAL   A 1 18  ? -16.862 47.957 10.079  1.00 23.70  ? 18  VAL   A CB   1 
ATOM   131  C  CG1  . VAL   A 1 18  ? -15.880 48.815 10.843  1.00 26.69  ? 18  VAL   A CG1  1 
ATOM   132  C  CG2  . VAL   A 1 18  ? -16.187 47.423 8.825   1.00 23.19  ? 18  VAL   A CG2  1 
ATOM   133  N  N    . GLN   A 1 19  ? -19.417 46.444 9.709   1.00 24.45  ? 19  GLN   A N    1 
ATOM   134  C  CA   . GLN   A 1 19  ? -20.347 45.759 8.825   1.00 25.18  ? 19  GLN   A CA   1 
ATOM   135  C  C    . GLN   A 1 19  ? -20.285 46.397 7.449   1.00 25.31  ? 19  GLN   A C    1 
ATOM   136  O  O    . GLN   A 1 19  ? -20.239 47.625 7.331   1.00 28.79  ? 19  GLN   A O    1 
ATOM   137  C  CB   . GLN   A 1 19  ? -21.781 45.834 9.357   1.00 29.01  ? 19  GLN   A CB   1 
ATOM   138  C  CG   . GLN   A 1 19  ? -22.751 44.914 8.639   1.00 31.22  ? 19  GLN   A CG   1 
ATOM   139  C  CD   . GLN   A 1 19  ? -24.140 44.920 9.265   1.00 38.81  ? 19  GLN   A CD   1 
ATOM   140  O  OE1  . GLN   A 1 19  ? -24.426 45.718 10.156  1.00 36.31  ? 19  GLN   A OE1  1 
ATOM   141  N  NE2  . GLN   A 1 19  ? -25.014 44.043 8.781   1.00 41.53  ? 19  GLN   A NE2  1 
ATOM   142  N  N    . VAL   A 1 20  ? -20.282 45.571 6.409   1.00 22.00  ? 20  VAL   A N    1 
ATOM   143  C  CA   . VAL   A 1 20  ? -20.265 46.044 5.029   1.00 23.38  ? 20  VAL   A CA   1 
ATOM   144  C  C    . VAL   A 1 20  ? -21.485 45.470 4.333   1.00 24.40  ? 20  VAL   A C    1 
ATOM   145  O  O    . VAL   A 1 20  ? -21.720 44.255 4.387   1.00 25.12  ? 20  VAL   A O    1 
ATOM   146  C  CB   . VAL   A 1 20  ? -18.982 45.631 4.280   1.00 24.17  ? 20  VAL   A CB   1 
ATOM   147  C  CG1  . VAL   A 1 20  ? -19.053 46.115 2.790   1.00 21.08  ? 20  VAL   A CG1  1 
ATOM   148  C  CG2  . VAL   A 1 20  ? -17.756 46.180 4.947   1.00 26.05  ? 20  VAL   A CG2  1 
ATOM   149  N  N    . THR   A 1 21  ? -22.229 46.333 3.629   1.00 26.27  ? 21  THR   A N    1 
ATOM   150  C  CA   . THR   A 1 21  ? -23.447 45.941 2.941   1.00 27.52  ? 21  THR   A CA   1 
ATOM   151  C  C    . THR   A 1 21  ? -23.416 46.499 1.529   1.00 30.69  ? 21  THR   A C    1 
ATOM   152  O  O    . THR   A 1 21  ? -23.128 47.686 1.324   1.00 31.10  ? 21  THR   A O    1 
ATOM   153  C  CB   . THR   A 1 21  ? -24.702 46.452 3.667   1.00 32.70  ? 21  THR   A CB   1 
ATOM   154  O  OG1  . THR   A 1 21  ? -24.727 45.936 5.004   1.00 29.06  ? 21  THR   A OG1  1 
ATOM   155  C  CG2  . THR   A 1 21  ? -25.967 46.000 2.928   1.00 36.88  ? 21  THR   A CG2  1 
ATOM   156  N  N    . CYS   A 1 22  ? -23.726 45.647 0.561   1.00 27.44  ? 22  CYS   A N    1 
ATOM   157  C  CA   . CYS   A 1 22  ? -23.830 46.050 -0.833  1.00 27.88  ? 22  CYS   A CA   1 
ATOM   158  C  C    . CYS   A 1 22  ? -25.157 45.476 -1.330  1.00 31.24  ? 22  CYS   A C    1 
ATOM   159  O  O    . CYS   A 1 22  ? -25.335 44.254 -1.393  1.00 31.08  ? 22  CYS   A O    1 
ATOM   160  C  CB   . CYS   A 1 22  ? -22.609 45.558 -1.632  1.00 25.76  ? 22  CYS   A CB   1 
ATOM   161  S  SG   . CYS   A 1 22  ? -22.643 46.042 -3.358  1.00 39.93  ? 22  CYS   A SG   1 
ATOM   162  N  N    . GLY   A 1 23  ? -26.123 46.354 -1.596  1.00 36.09  ? 23  GLY   A N    1 
ATOM   163  C  CA   . GLY   A 1 23  ? -27.479 45.903 -1.866  1.00 39.21  ? 23  GLY   A CA   1 
ATOM   164  C  C    . GLY   A 1 23  ? -28.116 45.273 -0.644  1.00 34.19  ? 23  GLY   A C    1 
ATOM   165  O  O    . GLY   A 1 23  ? -28.264 45.927 0.393   1.00 38.97  ? 23  GLY   A O    1 
ATOM   166  N  N    . THR   A 1 24  ? -28.511 44.007 -0.745  1.00 31.74  ? 24  THR   A N    1 
ATOM   167  C  CA   . THR   A 1 24  ? -28.973 43.262 0.420   1.00 37.77  ? 24  THR   A CA   1 
ATOM   168  C  C    . THR   A 1 24  ? -27.949 42.246 0.886   1.00 30.88  ? 24  THR   A C    1 
ATOM   169  O  O    . THR   A 1 24  ? -28.238 41.477 1.809   1.00 34.48  ? 24  THR   A O    1 
ATOM   170  C  CB   . THR   A 1 24  ? -30.293 42.541 0.125   1.00 36.22  ? 24  THR   A CB   1 
ATOM   171  O  OG1  . THR   A 1 24  ? -30.176 41.825 -1.105  1.00 46.21  ? 24  THR   A OG1  1 
ATOM   172  C  CG2  . THR   A 1 24  ? -31.428 43.533 0.017   1.00 43.55  ? 24  THR   A CG2  1 
ATOM   173  N  N    . THR   A 1 25  ? -26.767 42.216 0.272   1.00 28.48  ? 25  THR   A N    1 
ATOM   174  C  CA   . THR   A 1 25  ? -25.713 41.290 0.670   1.00 29.22  ? 25  THR   A CA   1 
ATOM   175  C  C    . THR   A 1 25  ? -24.846 41.950 1.735   1.00 30.54  ? 25  THR   A C    1 
ATOM   176  O  O    . THR   A 1 25  ? -24.431 43.104 1.583   1.00 27.88  ? 25  THR   A O    1 
ATOM   177  C  CB   . THR   A 1 25  ? -24.882 40.879 -0.545  1.00 29.75  ? 25  THR   A CB   1 
ATOM   178  O  OG1  . THR   A 1 25  ? -25.779 40.422 -1.568  1.00 30.14  ? 25  THR   A OG1  1 
ATOM   179  C  CG2  . THR   A 1 25  ? -23.904 39.760 -0.195  1.00 29.16  ? 25  THR   A CG2  1 
ATOM   180  N  N    . THR   A 1 26  ? -24.597 41.242 2.833   1.00 28.86  ? 26  THR   A N    1 
ATOM   181  C  CA   . THR   A 1 26  ? -23.896 41.905 3.916   1.00 27.21  ? 26  THR   A CA   1 
ATOM   182  C  C    . THR   A 1 26  ? -22.938 40.906 4.554   1.00 23.81  ? 26  THR   A C    1 
ATOM   183  O  O    . THR   A 1 26  ? -23.138 39.695 4.468   1.00 24.16  ? 26  THR   A O    1 
ATOM   184  C  CB   . THR   A 1 26  ? -24.879 42.461 4.955   1.00 30.29  ? 26  THR   A CB   1 
ATOM   185  O  OG1  . THR   A 1 26  ? -24.149 43.002 6.053   1.00 33.70  ? 26  THR   A OG1  1 
ATOM   186  C  CG2  . THR   A 1 26  ? -25.749 41.326 5.501   1.00 32.41  ? 26  THR   A CG2  1 
ATOM   187  N  N    . LEU   A 1 27  ? -21.891 41.427 5.176   1.00 21.75  ? 27  LEU   A N    1 
ATOM   188  C  CA   . LEU   A 1 27  ? -20.896 40.605 5.876   1.00 22.59  ? 27  LEU   A CA   1 
ATOM   189  C  C    . LEU   A 1 27  ? -20.016 41.530 6.715   1.00 21.42  ? 27  LEU   A C    1 
ATOM   190  O  O    . LEU   A 1 27  ? -20.312 42.725 6.862   1.00 24.32  ? 27  LEU   A O    1 
ATOM   191  C  CB   . LEU   A 1 27  ? -20.075 39.745 4.899   1.00 19.10  ? 27  LEU   A CB   1 
ATOM   192  C  CG   . LEU   A 1 27  ? -19.583 40.364 3.576   1.00 21.86  ? 27  LEU   A CG   1 
ATOM   193  C  CD1  . LEU   A 1 27  ? -18.586 41.493 3.787   1.00 21.55  ? 27  LEU   A CD1  1 
ATOM   194  C  CD2  . LEU   A 1 27  ? -18.937 39.256 2.734   1.00 21.60  ? 27  LEU   A CD2  1 
ATOM   195  N  N    . ASN   A 1 28  ? -18.950 40.964 7.303   1.00 20.09  ? 28  ASN   A N    1 
ATOM   196  C  CA   . ASN   A 1 28  ? -18.057 41.706 8.190   1.00 19.42  ? 28  ASN   A CA   1 
ATOM   197  C  C    . ASN   A 1 28  ? -16.872 42.259 7.417   1.00 19.92  ? 28  ASN   A C    1 
ATOM   198  O  O    . ASN   A 1 28  ? -16.426 41.674 6.426   1.00 19.57  ? 28  ASN   A O    1 
ATOM   199  C  CB   . ASN   A 1 28  ? -17.534 40.809 9.317   1.00 17.83  ? 28  ASN   A CB   1 
ATOM   200  C  CG   . ASN   A 1 28  ? -18.653 40.188 10.118  1.00 24.00  ? 28  ASN   A CG   1 
ATOM   201  O  OD1  . ASN   A 1 28  ? -19.282 40.854 10.951  1.00 23.28  ? 28  ASN   A OD1  1 
ATOM   202  N  ND2  . ASN   A 1 28  ? -18.955 38.927 9.829   1.00 20.60  ? 28  ASN   A ND2  1 
ATOM   203  N  N    . GLY   A 1 29  ? -16.376 43.413 7.868   1.00 17.92  ? 29  GLY   A N    1 
ATOM   204  C  CA   . GLY   A 1 29  ? -15.149 43.971 7.344   1.00 18.26  ? 29  GLY   A CA   1 
ATOM   205  C  C    . GLY   A 1 29  ? -14.195 44.360 8.462   1.00 18.72  ? 29  GLY   A C    1 
ATOM   206  O  O    . GLY   A 1 29  ? -14.569 44.444 9.628   1.00 20.47  ? 29  GLY   A O    1 
ATOM   207  N  N    . LEU   A 1 30  ? -12.949 44.614 8.061   1.00 19.57  ? 30  LEU   A N    1 
ATOM   208  C  CA   . LEU   A 1 30  ? -11.836 44.961 8.938   1.00 22.64  ? 30  LEU   A CA   1 
ATOM   209  C  C    . LEU   A 1 30  ? -11.350 46.367 8.602   1.00 20.96  ? 30  LEU   A C    1 
ATOM   210  O  O    . LEU   A 1 30  ? -10.869 46.616 7.491   1.00 20.37  ? 30  LEU   A O    1 
ATOM   211  C  CB   . LEU   A 1 30  ? -10.709 43.930 8.788   1.00 19.09  ? 30  LEU   A CB   1 
ATOM   212  C  CG   . LEU   A 1 30  ? -9.550  44.052 9.754   1.00 18.81  ? 30  LEU   A CG   1 
ATOM   213  C  CD1  . LEU   A 1 30  ? -9.927  43.520 11.133  1.00 18.61  ? 30  LEU   A CD1  1 
ATOM   214  C  CD2  . LEU   A 1 30  ? -8.365  43.257 9.201   1.00 17.60  ? 30  LEU   A CD2  1 
ATOM   215  N  N    . TRP   A 1 31  ? -11.476 47.281 9.564   1.00 21.59  ? 31  TRP   A N    1 
ATOM   216  C  CA   . TRP   A 1 31  ? -11.197 48.703 9.371   1.00 22.38  ? 31  TRP   A CA   1 
ATOM   217  C  C    . TRP   A 1 31  ? -9.831  49.032 9.965   1.00 22.66  ? 31  TRP   A C    1 
ATOM   218  O  O    . TRP   A 1 31  ? -9.671  49.046 11.186  1.00 21.96  ? 31  TRP   A O    1 
ATOM   219  C  CB   . TRP   A 1 31  ? -12.299 49.512 10.045  1.00 18.25  ? 31  TRP   A CB   1 
ATOM   220  C  CG   . TRP   A 1 31  ? -12.233 50.980 9.917   1.00 22.45  ? 31  TRP   A CG   1 
ATOM   221  C  CD1  . TRP   A 1 31  ? -11.557 51.714 8.981   1.00 21.97  ? 31  TRP   A CD1  1 
ATOM   222  C  CD2  . TRP   A 1 31  ? -12.873 51.921 10.791  1.00 27.08  ? 31  TRP   A CD2  1 
ATOM   223  N  NE1  . TRP   A 1 31  ? -11.756 53.069 9.217   1.00 24.43  ? 31  TRP   A NE1  1 
ATOM   224  C  CE2  . TRP   A 1 31  ? -12.558 53.215 10.322  1.00 27.83  ? 31  TRP   A CE2  1 
ATOM   225  C  CE3  . TRP   A 1 31  ? -13.687 51.789 11.925  1.00 26.09  ? 31  TRP   A CE3  1 
ATOM   226  C  CZ2  . TRP   A 1 31  ? -13.037 54.373 10.947  1.00 27.96  ? 31  TRP   A CZ2  1 
ATOM   227  C  CZ3  . TRP   A 1 31  ? -14.163 52.939 12.543  1.00 27.11  ? 31  TRP   A CZ3  1 
ATOM   228  C  CH2  . TRP   A 1 31  ? -13.828 54.214 12.057  1.00 28.65  ? 31  TRP   A CH2  1 
ATOM   229  N  N    . LEU   A 1 32  ? -8.842  49.293 9.105   1.00 21.70  ? 32  LEU   A N    1 
ATOM   230  C  CA   . LEU   A 1 32  ? -7.499  49.637 9.540   1.00 19.83  ? 32  LEU   A CA   1 
ATOM   231  C  C    . LEU   A 1 32  ? -7.105  50.931 8.848   1.00 24.44  ? 32  LEU   A C    1 
ATOM   232  O  O    . LEU   A 1 32  ? -7.240  51.036 7.625   1.00 23.61  ? 32  LEU   A O    1 
ATOM   233  C  CB   . LEU   A 1 32  ? -6.497  48.520 9.214   1.00 23.38  ? 32  LEU   A CB   1 
ATOM   234  C  CG   . LEU   A 1 32  ? -6.793  47.135 9.789   1.00 20.97  ? 32  LEU   A CG   1 
ATOM   235  C  CD1  . LEU   A 1 32  ? -5.902  46.080 9.133   1.00 19.68  ? 32  LEU   A CD1  1 
ATOM   236  C  CD2  . LEU   A 1 32  ? -6.546  47.165 11.296  1.00 20.08  ? 32  LEU   A CD2  1 
ATOM   237  N  N    . ASP   A 1 33  ? -6.627  51.914 9.623   1.00 25.40  ? 33  ASP   A N    1 
ATOM   238  C  CA   . ASP   A 1 33  ? -6.371  53.269 9.091   1.00 24.00  ? 33  ASP   A CA   1 
ATOM   239  C  C    . ASP   A 1 33  ? -7.625  53.685 8.323   1.00 27.86  ? 33  ASP   A C    1 
ATOM   240  O  O    . ASP   A 1 33  ? -8.735  53.520 8.850   1.00 26.30  ? 33  ASP   A O    1 
ATOM   241  C  CB   . ASP   A 1 33  ? -5.067  53.306 8.306   1.00 26.90  ? 33  ASP   A CB   1 
ATOM   242  C  CG   . ASP   A 1 33  ? -3.891  52.825 9.119   1.00 33.32  ? 33  ASP   A CG   1 
ATOM   243  O  OD1  . ASP   A 1 33  ? -3.770  53.282 10.275  1.00 35.12  ? 33  ASP   A OD1  1 
ATOM   244  O  OD2  . ASP   A 1 33  ? -3.086  52.027 8.610   1.00 37.29  ? 33  ASP   A OD2  1 
ATOM   245  N  N    . ASP   A 1 34  ? -7.517  54.205 7.097   1.00 26.45  ? 34  ASP   A N    1 
ATOM   246  C  CA   . ASP   A 1 34  ? -8.703  54.618 6.358   1.00 28.88  ? 34  ASP   A CA   1 
ATOM   247  C  C    . ASP   A 1 34  ? -9.133  53.591 5.306   1.00 26.20  ? 34  ASP   A C    1 
ATOM   248  O  O    . ASP   A 1 34  ? -9.664  53.973 4.253   1.00 26.17  ? 34  ASP   A O    1 
ATOM   249  C  CB   . ASP   A 1 34  ? -8.470  55.992 5.714   1.00 25.58  ? 34  ASP   A CB   1 
ATOM   250  C  CG   . ASP   A 1 34  ? -7.325  55.992 4.724   1.00 35.21  ? 34  ASP   A CG   1 
ATOM   251  O  OD1  . ASP   A 1 34  ? -6.557  55.006 4.676   1.00 30.53  ? 34  ASP   A OD1  1 
ATOM   252  O  OD2  . ASP   A 1 34  ? -7.191  57.000 3.984   1.00 34.16  ? 34  ASP   A OD2  1 
ATOM   253  N  N    . VAL   A 1 35  ? -8.944  52.297 5.565   1.00 23.36  ? 35  VAL   A N    1 
ATOM   254  C  CA   . VAL   A 1 35  ? -9.307  51.266 4.590   1.00 21.56  ? 35  VAL   A CA   1 
ATOM   255  C  C    . VAL   A 1 35  ? -10.134 50.200 5.295   1.00 23.93  ? 35  VAL   A C    1 
ATOM   256  O  O    . VAL   A 1 35  ? -9.846  49.835 6.440   1.00 21.84  ? 35  VAL   A O    1 
ATOM   257  C  CB   . VAL   A 1 35  ? -8.066  50.622 3.940   1.00 21.97  ? 35  VAL   A CB   1 
ATOM   258  C  CG1  . VAL   A 1 35  ? -8.503  49.495 2.963   1.00 23.40  ? 35  VAL   A CG1  1 
ATOM   259  C  CG2  . VAL   A 1 35  ? -7.240  51.680 3.212   1.00 24.80  ? 35  VAL   A CG2  1 
ATOM   260  N  N    . VAL   A 1 36  ? -11.167 49.710 4.621   1.00 22.09  ? 36  VAL   A N    1 
ATOM   261  C  CA   . VAL   A 1 36  ? -11.969 48.593 5.110   1.00 21.57  ? 36  VAL   A CA   1 
ATOM   262  C  C    . VAL   A 1 36  ? -11.726 47.416 4.175   1.00 22.11  ? 36  VAL   A C    1 
ATOM   263  O  O    . VAL   A 1 36  ? -11.900 47.544 2.965   1.00 23.09  ? 36  VAL   A O    1 
ATOM   264  C  CB   . VAL   A 1 36  ? -13.459 48.945 5.180   1.00 20.90  ? 36  VAL   A CB   1 
ATOM   265  C  CG1  . VAL   A 1 36  ? -14.275 47.683 5.486   1.00 20.42  ? 36  VAL   A CG1  1 
ATOM   266  C  CG2  . VAL   A 1 36  ? -13.690 50.018 6.258   1.00 22.78  ? 36  VAL   A CG2  1 
ATOM   267  N  N    . TYR   A 1 37  ? -11.291 46.288 4.730   1.00 19.40  ? 37  TYR   A N    1 
ATOM   268  C  CA   . TYR   A 1 37  ? -11.029 45.065 3.978   1.00 18.63  ? 37  TYR   A CA   1 
ATOM   269  C  C    . TYR   A 1 37  ? -12.188 44.100 4.171   1.00 19.01  ? 37  TYR   A C    1 
ATOM   270  O  O    . TYR   A 1 37  ? -12.615 43.870 5.306   1.00 21.14  ? 37  TYR   A O    1 
ATOM   271  C  CB   . TYR   A 1 37  ? -9.718  44.400 4.421   1.00 19.86  ? 37  TYR   A CB   1 
ATOM   272  C  CG   . TYR   A 1 37  ? -8.514  45.311 4.351   1.00 21.35  ? 37  TYR   A CG   1 
ATOM   273  C  CD1  . TYR   A 1 37  ? -8.300  46.286 5.310   1.00 19.70  ? 37  TYR   A CD1  1 
ATOM   274  C  CD2  . TYR   A 1 37  ? -7.618  45.229 3.270   1.00 21.22  ? 37  TYR   A CD2  1 
ATOM   275  C  CE1  . TYR   A 1 37  ? -7.222  47.139 5.229   1.00 22.05  ? 37  TYR   A CE1  1 
ATOM   276  C  CE2  . TYR   A 1 37  ? -6.529  46.077 3.190   1.00 22.59  ? 37  TYR   A CE2  1 
ATOM   277  C  CZ   . TYR   A 1 37  ? -6.342  47.030 4.169   1.00 24.98  ? 37  TYR   A CZ   1 
ATOM   278  O  OH   . TYR   A 1 37  ? -5.275  47.898 4.097   1.00 27.96  ? 37  TYR   A OH   1 
ATOM   279  N  N    . CYS   A 1 38  ? -12.695 43.518 3.084   1.00 17.43  ? 38  CYS   A N    1 
ATOM   280  C  CA   . CYS   A 1 38  ? -13.732 42.510 3.276   1.00 14.85  ? 38  CYS   A CA   1 
ATOM   281  C  C    . CYS   A 1 38  ? -13.738 41.550 2.100   1.00 20.50  ? 38  CYS   A C    1 
ATOM   282  O  O    . CYS   A 1 38  ? -13.084 41.794 1.080   1.00 17.94  ? 38  CYS   A O    1 
ATOM   283  C  CB   . CYS   A 1 38  ? -15.102 43.158 3.483   1.00 16.78  ? 38  CYS   A CB   1 
ATOM   284  S  SG   . CYS   A 1 38  ? -15.762 43.880 1.961   1.00 22.51  ? 38  CYS   A SG   1 
ATOM   285  N  N    . PRO   A 1 39  ? -14.425 40.415 2.224   1.00 18.50  ? 39  PRO   A N    1 
ATOM   286  C  CA   . PRO   A 1 39  ? -14.480 39.489 1.077   1.00 17.13  ? 39  PRO   A CA   1 
ATOM   287  C  C    . PRO   A 1 39  ? -15.191 40.144 -0.111  1.00 18.54  ? 39  PRO   A C    1 
ATOM   288  O  O    . PRO   A 1 39  ? -16.208 40.828 0.044   1.00 19.16  ? 39  PRO   A O    1 
ATOM   289  C  CB   . PRO   A 1 39  ? -15.276 38.296 1.615   1.00 15.58  ? 39  PRO   A CB   1 
ATOM   290  C  CG   . PRO   A 1 39  ? -15.050 38.340 3.149   1.00 14.41  ? 39  PRO   A CG   1 
ATOM   291  C  CD   . PRO   A 1 39  ? -14.998 39.823 3.454   1.00 20.32  ? 39  PRO   A CD   1 
ATOM   292  N  N    . ARG   A 1 40  ? -14.660 39.915 -1.315  1.00 18.58  ? 40  ARG   A N    1 
ATOM   293  C  CA   . ARG   A 1 40  ? -15.289 40.536 -2.476  1.00 18.45  ? 40  ARG   A CA   1 
ATOM   294  C  C    . ARG   A 1 40  ? -16.675 39.962 -2.777  1.00 21.25  ? 40  ARG   A C    1 
ATOM   295  O  O    . ARG   A 1 40  ? -17.464 40.599 -3.501  1.00 21.34  ? 40  ARG   A O    1 
ATOM   296  C  CB   . ARG   A 1 40  ? -14.393 40.400 -3.697  1.00 20.17  ? 40  ARG   A CB   1 
ATOM   297  C  CG   . ARG   A 1 40  ? -14.243 38.978 -4.219  1.00 20.18  ? 40  ARG   A CG   1 
ATOM   298  C  CD   . ARG   A 1 40  ? -13.279 38.948 -5.405  1.00 18.44  ? 40  ARG   A CD   1 
ATOM   299  N  NE   . ARG   A 1 40  ? -13.023 37.580 -5.836  1.00 20.89  ? 40  ARG   A NE   1 
ATOM   300  C  CZ   . ARG   A 1 40  ? -12.418 37.266 -6.976  1.00 28.21  ? 40  ARG   A CZ   1 
ATOM   301  N  NH1  . ARG   A 1 40  ? -11.953 38.204 -7.790  1.00 22.90  ? 40  ARG   A NH1  1 
ATOM   302  N  NH2  . ARG   A 1 40  ? -12.288 35.985 -7.309  1.00 20.45  ? 40  ARG   A NH2  1 
ATOM   303  N  N    . HIS   A 1 41  ? -16.993 38.788 -2.215  1.00 18.30  ? 41  HIS   A N    1 
ATOM   304  C  CA   . HIS   A 1 41  ? -18.290 38.168 -2.448  1.00 18.47  ? 41  HIS   A CA   1 
ATOM   305  C  C    . HIS   A 1 41  ? -19.431 39.100 -2.080  1.00 23.39  ? 41  HIS   A C    1 
ATOM   306  O  O    . HIS   A 1 41  ? -20.555 38.891 -2.538  1.00 23.62  ? 41  HIS   A O    1 
ATOM   307  C  CB   . HIS   A 1 41  ? -18.372 36.861 -1.654  1.00 22.20  ? 41  HIS   A CB   1 
ATOM   308  C  CG   . HIS   A 1 41  ? -19.424 35.913 -2.137  1.00 27.12  ? 41  HIS   A CG   1 
ATOM   309  N  ND1  . HIS   A 1 41  ? -19.323 35.255 -3.344  1.00 25.01  ? 41  HIS   A ND1  1 
ATOM   310  C  CD2  . HIS   A 1 41  ? -20.556 35.456 -1.552  1.00 25.14  ? 41  HIS   A CD2  1 
ATOM   311  C  CE1  . HIS   A 1 41  ? -20.363 34.453 -3.492  1.00 28.69  ? 41  HIS   A CE1  1 
ATOM   312  N  NE2  . HIS   A 1 41  ? -21.127 34.557 -2.420  1.00 28.49  ? 41  HIS   A NE2  1 
ATOM   313  N  N    . VAL   A 1 42  ? -19.169 40.134 -1.272  1.00 20.00  ? 42  VAL   A N    1 
ATOM   314  C  CA   . VAL   A 1 42  ? -20.237 41.040 -0.870  1.00 20.87  ? 42  VAL   A CA   1 
ATOM   315  C  C    . VAL   A 1 42  ? -20.860 41.765 -2.061  1.00 23.24  ? 42  VAL   A C    1 
ATOM   316  O  O    . VAL   A 1 42  ? -22.005 42.220 -1.960  1.00 23.27  ? 42  VAL   A O    1 
ATOM   317  C  CB   . VAL   A 1 42  ? -19.733 42.064 0.175   1.00 21.12  ? 42  VAL   A CB   1 
ATOM   318  C  CG1  . VAL   A 1 42  ? -18.764 43.059 -0.457  1.00 21.21  ? 42  VAL   A CG1  1 
ATOM   319  C  CG2  . VAL   A 1 42  ? -20.913 42.770 0.809   1.00 21.79  ? 42  VAL   A CG2  1 
ATOM   320  N  N    . ILE   A 1 43  ? -20.159 41.864 -3.196  1.00 24.26  ? 43  ILE   A N    1 
ATOM   321  C  CA   . ILE   A 1 43  ? -20.738 42.599 -4.330  1.00 26.02  ? 43  ILE   A CA   1 
ATOM   322  C  C    . ILE   A 1 43  ? -21.647 41.712 -5.169  1.00 29.57  ? 43  ILE   A C    1 
ATOM   323  O  O    . ILE   A 1 43  ? -22.151 42.138 -6.214  1.00 33.97  ? 43  ILE   A O    1 
ATOM   324  C  CB   . ILE   A 1 43  ? -19.665 43.251 -5.222  1.00 23.97  ? 43  ILE   A CB   1 
ATOM   325  C  CG1  . ILE   A 1 43  ? -18.942 42.202 -6.073  1.00 25.66  ? 43  ILE   A CG1  1 
ATOM   326  C  CG2  . ILE   A 1 43  ? -18.699 44.122 -4.421  1.00 28.04  ? 43  ILE   A CG2  1 
ATOM   327  C  CD1  . ILE   A 1 43  ? -17.798 42.798 -6.885  1.00 25.13  ? 43  ILE   A CD1  1 
ATOM   328  N  N    . CYS   A 1 44  ? -21.870 40.488 -4.726  1.00 24.89  ? 44  CYS   A N    1 
ATOM   329  C  CA   . CYS   A 1 44  ? -22.708 39.546 -5.447  1.00 24.21  ? 44  CYS   A CA   1 
ATOM   330  C  C    . CYS   A 1 44  ? -24.151 39.674 -4.972  1.00 28.99  ? 44  CYS   A C    1 
ATOM   331  O  O    . CYS   A 1 44  ? -24.413 39.698 -3.766  1.00 30.74  ? 44  CYS   A O    1 
ATOM   332  C  CB   . CYS   A 1 44  ? -22.218 38.123 -5.200  1.00 29.33  ? 44  CYS   A CB   1 
ATOM   333  S  SG   . CYS   A 1 44  ? -20.689 37.711 -6.040  1.00 31.64  ? 44  CYS   A SG   1 
ATOM   334  N  N    . THR   A 1 45  ? -25.088 39.746 -5.917  1.00 37.42  ? 45  THR   A N    1 
ATOM   335  C  CA   . THR   A 1 45  ? -26.473 39.486 -5.550  1.00 32.79  ? 45  THR   A CA   1 
ATOM   336  C  C    . THR   A 1 45  ? -26.710 37.979 -5.499  1.00 38.41  ? 45  THR   A C    1 
ATOM   337  O  O    . THR   A 1 45  ? -25.860 37.176 -5.890  1.00 36.76  ? 45  THR   A O    1 
ATOM   338  C  CB   . THR   A 1 45  ? -27.438 40.150 -6.536  1.00 36.51  ? 45  THR   A CB   1 
ATOM   339  O  OG1  . THR   A 1 45  ? -27.350 39.479 -7.794  1.00 38.20  ? 45  THR   A OG1  1 
ATOM   340  C  CG2  . THR   A 1 45  ? -27.104 41.621 -6.717  1.00 39.35  ? 45  THR   A CG2  1 
ATOM   341  N  N    . SER   A 1 46  ? -27.887 37.592 -5.003  1.00 42.30  ? 46  SER   A N    1 
ATOM   342  C  CA   . SER   A 1 46  ? -28.215 36.172 -4.917  1.00 42.19  ? 46  SER   A CA   1 
ATOM   343  C  C    . SER   A 1 46  ? -27.959 35.452 -6.238  1.00 46.56  ? 46  SER   A C    1 
ATOM   344  O  O    . SER   A 1 46  ? -27.396 34.351 -6.257  1.00 50.89  ? 46  SER   A O    1 
ATOM   345  C  CB   . SER   A 1 46  ? -29.670 36.006 -4.489  1.00 49.47  ? 46  SER   A CB   1 
ATOM   346  O  OG   . SER   A 1 46  ? -29.794 36.243 -3.102  1.00 53.22  ? 46  SER   A OG   1 
ATOM   347  N  N    . GLU   A 1 47  ? -28.345 36.066 -7.360  1.00 47.06  ? 47  GLU   A N    1 
ATOM   348  C  CA   . GLU   A 1 47  ? -28.169 35.411 -8.653  1.00 48.89  ? 47  GLU   A CA   1 
ATOM   349  C  C    . GLU   A 1 47  ? -26.725 35.439 -9.147  1.00 53.43  ? 47  GLU   A C    1 
ATOM   350  O  O    . GLU   A 1 47  ? -26.390 34.685 -10.067 1.00 56.65  ? 47  GLU   A O    1 
ATOM   351  C  CB   . GLU   A 1 47  ? -29.086 36.054 -9.696  1.00 54.38  ? 47  GLU   A CB   1 
ATOM   352  C  CG   . GLU   A 1 47  ? -30.570 35.931 -9.379  1.00 62.50  ? 47  GLU   A CG   1 
ATOM   353  C  CD   . GLU   A 1 47  ? -31.057 36.979 -8.386  1.00 70.58  ? 47  GLU   A CD   1 
ATOM   354  O  OE1  . GLU   A 1 47  ? -30.218 37.708 -7.809  1.00 57.59  ? 47  GLU   A OE1  1 
ATOM   355  O  OE2  . GLU   A 1 47  ? -32.288 37.074 -8.181  1.00 87.00  ? 47  GLU   A OE2  1 
ATOM   356  N  N    . ASP   A 1 48  ? -25.873 36.298 -8.579  1.00 42.74  ? 48  ASP   A N    1 
ATOM   357  C  CA   . ASP   A 1 48  ? -24.474 36.380 -8.991  1.00 43.33  ? 48  ASP   A CA   1 
ATOM   358  C  C    . ASP   A 1 48  ? -23.586 35.342 -8.307  1.00 38.69  ? 48  ASP   A C    1 
ATOM   359  O  O    . ASP   A 1 48  ? -22.472 35.090 -8.781  1.00 41.95  ? 48  ASP   A O    1 
ATOM   360  C  CB   . ASP   A 1 48  ? -23.903 37.762 -8.665  1.00 40.62  ? 48  ASP   A CB   1 
ATOM   361  C  CG   . ASP   A 1 48  ? -24.482 38.864 -9.512  1.00 46.84  ? 48  ASP   A CG   1 
ATOM   362  O  OD1  . ASP   A 1 48  ? -24.663 38.660 -10.738 1.00 45.18  ? 48  ASP   A OD1  1 
ATOM   363  O  OD2  . ASP   A 1 48  ? -24.715 39.956 -8.942  1.00 40.54  ? 48  ASP   A OD2  1 
ATOM   364  N  N    . MET   A 1 49  ? -24.049 34.746 -7.207  1.00 42.36  ? 49  MET   A N    1 
ATOM   365  C  CA   . MET   A 1 49  ? -23.157 34.017 -6.301  1.00 41.00  ? 49  MET   A CA   1 
ATOM   366  C  C    . MET   A 1 49  ? -22.678 32.688 -6.880  1.00 38.64  ? 49  MET   A C    1 
ATOM   367  O  O    . MET   A 1 49  ? -21.585 32.226 -6.534  1.00 37.68  ? 49  MET   A O    1 
ATOM   368  C  CB   . MET   A 1 49  ? -23.869 33.804 -4.961  1.00 39.56  ? 49  MET   A CB   1 
ATOM   369  C  CG   . MET   A 1 49  ? -24.389 35.102 -4.356  1.00 39.94  ? 49  MET   A CG   1 
ATOM   370  S  SD   . MET   A 1 49  ? -25.149 34.853 -2.741  1.00 39.45  ? 49  MET   A SD   1 
ATOM   371  C  CE   . MET   A 1 49  ? -25.422 36.530 -2.163  1.00 40.15  ? 49  MET   A CE   1 
ATOM   372  N  N    . LEU   A 1 50  ? -23.467 32.064 -7.758  1.00 41.33  ? 50  LEU   A N    1 
ATOM   373  C  CA   . LEU   A 1 50  ? -23.106 30.752 -8.290  1.00 42.68  ? 50  LEU   A CA   1 
ATOM   374  C  C    . LEU   A 1 50  ? -21.877 30.831 -9.189  1.00 43.09  ? 50  LEU   A C    1 
ATOM   375  O  O    . LEU   A 1 50  ? -20.964 30.003 -9.086  1.00 40.70  ? 50  LEU   A O    1 
ATOM   376  C  CB   . LEU   A 1 50  ? -24.296 30.154 -9.051  1.00 46.29  ? 50  LEU   A CB   1 
ATOM   377  C  CG   . LEU   A 1 50  ? -24.145 28.832 -9.823  1.00 54.99  ? 50  LEU   A CG   1 
ATOM   378  C  CD1  . LEU   A 1 50  ? -23.288 28.984 -11.079 1.00 60.28  ? 50  LEU   A CD1  1 
ATOM   379  C  CD2  . LEU   A 1 50  ? -23.605 27.715 -8.935  1.00 54.45  ? 50  LEU   A CD2  1 
ATOM   380  N  N    . ASN   A 1 51  ? -21.844 31.804 -10.101 1.00 40.83  ? 51  ASN   A N    1 
ATOM   381  C  CA   . ASN   A 1 51  ? -20.776 31.893 -11.098 1.00 43.68  ? 51  ASN   A CA   1 
ATOM   382  C  C    . ASN   A 1 51  ? -20.493 33.356 -11.411 1.00 42.67  ? 51  ASN   A C    1 
ATOM   383  O  O    . ASN   A 1 51  ? -20.760 33.841 -12.516 1.00 38.93  ? 51  ASN   A O    1 
ATOM   384  C  CB   . ASN   A 1 51  ? -21.160 31.131 -12.363 1.00 47.94  ? 51  ASN   A CB   1 
ATOM   385  C  CG   . ASN   A 1 51  ? -20.072 31.158 -13.393 1.00 51.46  ? 51  ASN   A CG   1 
ATOM   386  O  OD1  . ASN   A 1 51  ? -18.894 31.010 -13.060 1.00 60.18  ? 51  ASN   A OD1  1 
ATOM   387  N  ND2  . ASN   A 1 51  ? -20.446 31.361 -14.651 1.00 60.98  ? 51  ASN   A ND2  1 
ATOM   388  N  N    . PRO   A 1 52  ? -19.925 34.089 -10.461 1.00 37.03  ? 52  PRO   A N    1 
ATOM   389  C  CA   . PRO   A 1 52  ? -19.753 35.531 -10.654 1.00 28.51  ? 52  PRO   A CA   1 
ATOM   390  C  C    . PRO   A 1 52  ? -18.510 35.850 -11.461 1.00 31.95  ? 52  PRO   A C    1 
ATOM   391  O  O    . PRO   A 1 52  ? -17.490 35.163 -11.375 1.00 32.56  ? 52  PRO   A O    1 
ATOM   392  C  CB   . PRO   A 1 52  ? -19.622 36.063 -9.221  1.00 31.78  ? 52  PRO   A CB   1 
ATOM   393  C  CG   . PRO   A 1 52  ? -19.131 34.895 -8.420  1.00 38.06  ? 52  PRO   A CG   1 
ATOM   394  C  CD   . PRO   A 1 52  ? -19.363 33.621 -9.186  1.00 35.42  ? 52  PRO   A CD   1 
ATOM   395  N  N    . ASN   A 1 53  ? -18.606 36.913 -12.260 1.00 28.56  ? 53  ASN   A N    1 
ATOM   396  C  CA   . ASN   A 1 53  ? -17.421 37.531 -12.849 1.00 24.34  ? 53  ASN   A CA   1 
ATOM   397  C  C    . ASN   A 1 53  ? -17.192 38.813 -12.064 1.00 31.00  ? 53  ASN   A C    1 
ATOM   398  O  O    . ASN   A 1 53  ? -17.885 39.822 -12.261 1.00 26.88  ? 53  ASN   A O    1 
ATOM   399  C  CB   . ASN   A 1 53  ? -17.590 37.778 -14.351 1.00 27.65  ? 53  ASN   A CB   1 
ATOM   400  C  CG   . ASN   A 1 53  ? -16.347 38.360 -14.994 1.00 34.78  ? 53  ASN   A CG   1 
ATOM   401  O  OD1  . ASN   A 1 53  ? -15.856 39.421 -14.603 1.00 34.89  ? 53  ASN   A OD1  1 
ATOM   402  N  ND2  . ASN   A 1 53  ? -15.801 37.640 -15.967 1.00 47.66  ? 53  ASN   A ND2  1 
ATOM   403  N  N    . TYR   A 1 54  ? -16.229 38.759 -11.146 1.00 26.85  ? 54  TYR   A N    1 
ATOM   404  C  CA   . TYR   A 1 54  ? -16.096 39.826 -10.168 1.00 24.78  ? 54  TYR   A CA   1 
ATOM   405  C  C    . TYR   A 1 54  ? -15.649 41.141 -10.795 1.00 26.81  ? 54  TYR   A C    1 
ATOM   406  O  O    . TYR   A 1 54  ? -16.029 42.208 -10.308 1.00 24.88  ? 54  TYR   A O    1 
ATOM   407  C  CB   . TYR   A 1 54  ? -15.116 39.400 -9.088  1.00 22.98  ? 54  TYR   A CB   1 
ATOM   408  C  CG   . TYR   A 1 54  ? -15.693 38.433 -8.099  1.00 27.38  ? 54  TYR   A CG   1 
ATOM   409  C  CD1  . TYR   A 1 54  ? -16.578 38.859 -7.123  1.00 27.24  ? 54  TYR   A CD1  1 
ATOM   410  C  CD2  . TYR   A 1 54  ? -15.343 37.075 -8.137  1.00 27.09  ? 54  TYR   A CD2  1 
ATOM   411  C  CE1  . TYR   A 1 54  ? -17.083 37.959 -6.181  1.00 21.79  ? 54  TYR   A CE1  1 
ATOM   412  C  CE2  . TYR   A 1 54  ? -15.856 36.177 -7.229  1.00 22.35  ? 54  TYR   A CE2  1 
ATOM   413  C  CZ   . TYR   A 1 54  ? -16.721 36.631 -6.242  1.00 25.43  ? 54  TYR   A CZ   1 
ATOM   414  O  OH   . TYR   A 1 54  ? -17.223 35.735 -5.327  1.00 27.18  ? 54  TYR   A OH   1 
ATOM   415  N  N    . GLU   A 1 55  ? -14.800 41.093 -11.829 1.00 26.62  ? 55  GLU   A N    1 
ATOM   416  C  CA   . GLU   A 1 55  ? -14.397 42.328 -12.500 1.00 29.30  ? 55  GLU   A CA   1 
ATOM   417  C  C    . GLU   A 1 55  ? -15.603 43.036 -13.097 1.00 28.09  ? 55  GLU   A C    1 
ATOM   418  O  O    . GLU   A 1 55  ? -15.768 44.258 -12.945 1.00 29.79  ? 55  GLU   A O    1 
ATOM   419  C  CB   . GLU   A 1 55  ? -13.359 42.028 -13.585 1.00 34.82  ? 55  GLU   A CB   1 
ATOM   420  C  CG   . GLU   A 1 55  ? -12.089 41.351 -13.076 1.00 47.54  ? 55  GLU   A CG   1 
ATOM   421  C  CD   . GLU   A 1 55  ? -10.959 42.340 -12.845 1.00 61.55  ? 55  GLU   A CD   1 
ATOM   422  O  OE1  . GLU   A 1 55  ? -10.390 42.818 -13.849 1.00 81.96  ? 55  GLU   A OE1  1 
ATOM   423  O  OE2  . GLU   A 1 55  ? -10.629 42.636 -11.677 1.00 55.93  ? 55  GLU   A OE2  1 
ATOM   424  N  N    . ASP   A 1 56  ? -16.479 42.267 -13.738 1.00 27.27  ? 56  ASP   A N    1 
ATOM   425  C  CA   . ASP   A 1 56  ? -17.706 42.825 -14.291 1.00 32.45  ? 56  ASP   A CA   1 
ATOM   426  C  C    . ASP   A 1 56  ? -18.573 43.408 -13.184 1.00 28.45  ? 56  ASP   A C    1 
ATOM   427  O  O    . ASP   A 1 56  ? -19.071 44.536 -13.288 1.00 27.55  ? 56  ASP   A O    1 
ATOM   428  C  CB   . ASP   A 1 56  ? -18.474 41.743 -15.050 1.00 35.38  ? 56  ASP   A CB   1 
ATOM   429  C  CG   . ASP   A 1 56  ? -17.933 41.519 -16.451 1.00 39.25  ? 56  ASP   A CG   1 
ATOM   430  O  OD1  . ASP   A 1 56  ? -17.204 42.397 -16.958 1.00 37.88  ? 56  ASP   A OD1  1 
ATOM   431  O  OD2  . ASP   A 1 56  ? -18.258 40.467 -17.046 1.00 44.81  ? 56  ASP   A OD2  1 
ATOM   432  N  N    . LEU   A 1 57  ? -18.761 42.651 -12.095 1.00 23.97  ? 57  LEU   A N    1 
ATOM   433  C  CA   . LEU   A 1 57  ? -19.616 43.153 -11.028 1.00 28.77  ? 57  LEU   A CA   1 
ATOM   434  C  C    . LEU   A 1 57  ? -19.042 44.415 -10.399 1.00 28.69  ? 57  LEU   A C    1 
ATOM   435  O  O    . LEU   A 1 57  ? -19.797 45.324 -10.037 1.00 32.28  ? 57  LEU   A O    1 
ATOM   436  C  CB   . LEU   A 1 57  ? -19.841 42.070 -9.967  1.00 25.28  ? 57  LEU   A CB   1 
ATOM   437  C  CG   . LEU   A 1 57  ? -20.321 40.713 -10.479 1.00 29.04  ? 57  LEU   A CG   1 
ATOM   438  C  CD1  . LEU   A 1 57  ? -20.406 39.732 -9.332  1.00 30.19  ? 57  LEU   A CD1  1 
ATOM   439  C  CD2  . LEU   A 1 57  ? -21.686 40.848 -11.110 1.00 35.83  ? 57  LEU   A CD2  1 
ATOM   440  N  N    . LEU   A 1 58  ? -17.711 44.490 -10.247 1.00 25.41  ? 58  LEU   A N    1 
ATOM   441  C  CA   . LEU   A 1 58  ? -17.116 45.642 -9.577  1.00 27.92  ? 58  LEU   A CA   1 
ATOM   442  C  C    . LEU   A 1 58  ? -17.209 46.887 -10.440 1.00 25.72  ? 58  LEU   A C    1 
ATOM   443  O  O    . LEU   A 1 58  ? -17.477 47.980 -9.928  1.00 27.20  ? 58  LEU   A O    1 
ATOM   444  C  CB   . LEU   A 1 58  ? -15.647 45.396 -9.217  1.00 28.24  ? 58  LEU   A CB   1 
ATOM   445  C  CG   . LEU   A 1 58  ? -15.104 46.365 -8.151  1.00 30.58  ? 58  LEU   A CG   1 
ATOM   446  C  CD1  . LEU   A 1 58  ? -16.089 46.620 -6.993  1.00 33.25  ? 58  LEU   A CD1  1 
ATOM   447  C  CD2  . LEU   A 1 58  ? -13.705 46.010 -7.652  1.00 31.42  ? 58  LEU   A CD2  1 
ATOM   448  N  N    . ILE   A 1 59  ? -16.967 46.749 -11.746 1.00 24.16  ? 59  ILE   A N    1 
ATOM   449  C  CA   . ILE   A 1 59  ? -16.985 47.944 -12.578 1.00 25.43  ? 59  ILE   A CA   1 
ATOM   450  C  C    . ILE   A 1 59  ? -18.373 48.557 -12.612 1.00 30.48  ? 59  ILE   A C    1 
ATOM   451  O  O    . ILE   A 1 59  ? -18.520 49.743 -12.934 1.00 33.12  ? 59  ILE   A O    1 
ATOM   452  C  CB   . ILE   A 1 59  ? -16.479 47.649 -14.007 1.00 31.98  ? 59  ILE   A CB   1 
ATOM   453  C  CG1  . ILE   A 1 59  ? -16.301 48.962 -14.770 1.00 42.07  ? 59  ILE   A CG1  1 
ATOM   454  C  CG2  . ILE   A 1 59  ? -17.479 46.809 -14.792 1.00 33.88  ? 59  ILE   A CG2  1 
ATOM   455  C  CD1  . ILE   A 1 59  ? -15.018 49.021 -15.576 1.00 50.34  ? 59  ILE   A CD1  1 
ATOM   456  N  N    . ARG   A 1 60  ? -19.405 47.776 -12.299 1.00 26.34  ? 60  ARG   A N    1 
ATOM   457  C  CA   . ARG   A 1 60  ? -20.764 48.295 -12.266 1.00 29.66  ? 60  ARG   A CA   1 
ATOM   458  C  C    . ARG   A 1 60  ? -21.130 48.936 -10.939 1.00 31.56  ? 60  ARG   A C    1 
ATOM   459  O  O    . ARG   A 1 60  ? -22.280 49.359 -10.779 1.00 31.79  ? 60  ARG   A O    1 
ATOM   460  C  CB   . ARG   A 1 60  ? -21.767 47.190 -12.580 1.00 27.02  ? 60  ARG   A CB   1 
ATOM   461  C  CG   . ARG   A 1 60  ? -21.722 46.719 -14.006 1.00 30.50  ? 60  ARG   A CG   1 
ATOM   462  C  CD   . ARG   A 1 60  ? -22.043 45.268 -14.095 1.00 31.09  ? 60  ARG   A CD   1 
ATOM   463  N  NE   . ARG   A 1 60  ? -21.799 44.753 -15.432 1.00 31.73  ? 60  ARG   A NE   1 
ATOM   464  C  CZ   . ARG   A 1 60  ? -22.018 43.497 -15.788 1.00 36.97  ? 60  ARG   A CZ   1 
ATOM   465  N  NH1  . ARG   A 1 60  ? -22.503 42.613 -14.926 1.00 44.06  ? 60  ARG   A NH1  1 
ATOM   466  N  NH2  . ARG   A 1 60  ? -21.735 43.115 -17.033 1.00 39.56  ? 60  ARG   A NH2  1 
ATOM   467  N  N    . LYS   A 1 61  ? -20.204 49.022 -9.994  1.00 31.55  ? 61  LYS   A N    1 
ATOM   468  C  CA   . LYS   A 1 61  ? -20.483 49.621 -8.702  1.00 33.98  ? 61  LYS   A CA   1 
ATOM   469  C  C    . LYS   A 1 61  ? -19.838 50.997 -8.614  1.00 32.36  ? 61  LYS   A C    1 
ATOM   470  O  O    . LYS   A 1 61  ? -18.858 51.293 -9.296  1.00 32.35  ? 61  LYS   A O    1 
ATOM   471  C  CB   . LYS   A 1 61  ? -19.970 48.729 -7.562  1.00 31.98  ? 61  LYS   A CB   1 
ATOM   472  C  CG   . LYS   A 1 61  ? -20.572 47.324 -7.560  1.00 36.78  ? 61  LYS   A CG   1 
ATOM   473  C  CD   . LYS   A 1 61  ? -21.843 47.255 -6.723  1.00 43.38  ? 61  LYS   A CD   1 
ATOM   474  C  CE   . LYS   A 1 61  ? -22.552 45.915 -6.898  1.00 41.76  ? 61  LYS   A CE   1 
ATOM   475  N  NZ   . LYS   A 1 61  ? -22.452 45.438 -8.325  1.00 52.22  ? 61  LYS   A NZ   1 
ATOM   476  N  N    . SER   A 1 62  ? -20.390 51.834 -7.740  1.00 33.80  ? 62  SER   A N    1 
ATOM   477  C  CA   . SER   A 1 62  ? -19.755 53.083 -7.349  1.00 35.27  ? 62  SER   A CA   1 
ATOM   478  C  C    . SER   A 1 62  ? -19.650 53.106 -5.831  1.00 31.07  ? 62  SER   A C    1 
ATOM   479  O  O    . SER   A 1 62  ? -20.182 52.234 -5.142  1.00 33.90  ? 62  SER   A O    1 
ATOM   480  C  CB   . SER   A 1 62  ? -20.529 54.300 -7.865  1.00 44.12  ? 62  SER   A CB   1 
ATOM   481  O  OG   . SER   A 1 62  ? -21.855 54.271 -7.383  1.00 50.96  ? 62  SER   A OG   1 
ATOM   482  N  N    . ASN   A 1 63  ? -18.959 54.124 -5.312  1.00 31.41  ? 63  ASN   A N    1 
ATOM   483  C  CA   . ASN   A 1 63  ? -18.691 54.181 -3.875  1.00 31.83  ? 63  ASN   A CA   1 
ATOM   484  C  C    . ASN   A 1 63  ? -19.989 54.125 -3.073  1.00 32.58  ? 63  ASN   A C    1 
ATOM   485  O  O    . ASN   A 1 63  ? -20.054 53.477 -2.017  1.00 34.87  ? 63  ASN   A O    1 
ATOM   486  C  CB   . ASN   A 1 63  ? -17.939 55.467 -3.538  1.00 33.69  ? 63  ASN   A CB   1 
ATOM   487  C  CG   . ASN   A 1 63  ? -16.505 55.447 -4.023  1.00 34.40  ? 63  ASN   A CG   1 
ATOM   488  O  OD1  . ASN   A 1 63  ? -15.872 54.391 -4.119  1.00 32.77  ? 63  ASN   A OD1  1 
ATOM   489  N  ND2  . ASN   A 1 63  ? -15.986 56.631 -4.362  1.00 32.11  ? 63  ASN   A ND2  1 
ATOM   490  N  N    . HIS   A 1 64  ? -21.033 54.812 -3.552  1.00 35.55  ? 64  HIS   A N    1 
ATOM   491  C  CA   . HIS   A 1 64  ? -22.258 54.917 -2.770  1.00 38.66  ? 64  HIS   A CA   1 
ATOM   492  C  C    . HIS   A 1 64  ? -23.039 53.615 -2.730  1.00 37.50  ? 64  HIS   A C    1 
ATOM   493  O  O    . HIS   A 1 64  ? -24.043 53.536 -2.017  1.00 38.57  ? 64  HIS   A O    1 
ATOM   494  C  CB   . HIS   A 1 64  ? -23.133 56.051 -3.317  1.00 45.83  ? 64  HIS   A CB   1 
ATOM   495  C  CG   . HIS   A 1 64  ? -23.670 55.795 -4.691  1.00 41.98  ? 64  HIS   A CG   1 
ATOM   496  N  ND1  . HIS   A 1 64  ? -24.644 54.853 -4.946  1.00 50.62  ? 64  HIS   A ND1  1 
ATOM   497  C  CD2  . HIS   A 1 64  ? -23.340 56.326 -5.892  1.00 48.95  ? 64  HIS   A CD2  1 
ATOM   498  C  CE1  . HIS   A 1 64  ? -24.910 54.834 -6.240  1.00 43.88  ? 64  HIS   A CE1  1 
ATOM   499  N  NE2  . HIS   A 1 64  ? -24.131 55.717 -6.837  1.00 51.14  ? 64  HIS   A NE2  1 
ATOM   500  N  N    . ASN   A 1 65  ? -22.606 52.589 -3.460  1.00 34.73  ? 65  ASN   A N    1 
ATOM   501  C  CA   . ASN   A 1 65  ? -23.222 51.273 -3.358  1.00 33.35  ? 65  ASN   A CA   1 
ATOM   502  C  C    . ASN   A 1 65  ? -22.750 50.486 -2.143  1.00 36.51  ? 65  ASN   A C    1 
ATOM   503  O  O    . ASN   A 1 65  ? -23.294 49.407 -1.883  1.00 33.10  ? 65  ASN   A O    1 
ATOM   504  C  CB   . ASN   A 1 65  ? -22.943 50.463 -4.629  1.00 34.74  ? 65  ASN   A CB   1 
ATOM   505  C  CG   . ASN   A 1 65  ? -23.596 51.064 -5.859  1.00 39.20  ? 65  ASN   A CG   1 
ATOM   506  O  OD1  . ASN   A 1 65  ? -23.020 51.075 -6.949  1.00 37.23  ? 65  ASN   A OD1  1 
ATOM   507  N  ND2  . ASN   A 1 65  ? -24.825 51.542 -5.698  1.00 43.19  ? 65  ASN   A ND2  1 
ATOM   508  N  N    . PHE   A 1 66  ? -21.764 50.990 -1.404  1.00 30.53  ? 66  PHE   A N    1 
ATOM   509  C  CA   . PHE   A 1 66  ? -21.200 50.306 -0.247  1.00 33.65  ? 66  PHE   A CA   1 
ATOM   510  C  C    . PHE   A 1 66  ? -21.584 51.066 1.013   1.00 39.01  ? 66  PHE   A C    1 
ATOM   511  O  O    . PHE   A 1 66  ? -21.167 52.212 1.198   1.00 36.73  ? 66  PHE   A O    1 
ATOM   512  C  CB   . PHE   A 1 66  ? -19.676 50.216 -0.342  1.00 32.26  ? 66  PHE   A CB   1 
ATOM   513  C  CG   . PHE   A 1 66  ? -19.180 49.447 -1.535  1.00 31.81  ? 66  PHE   A CG   1 
ATOM   514  C  CD1  . PHE   A 1 66  ? -19.136 48.062 -1.518  1.00 29.89  ? 66  PHE   A CD1  1 
ATOM   515  C  CD2  . PHE   A 1 66  ? -18.775 50.116 -2.679  1.00 30.35  ? 66  PHE   A CD2  1 
ATOM   516  C  CE1  . PHE   A 1 66  ? -18.668 47.361 -2.622  1.00 32.67  ? 66  PHE   A CE1  1 
ATOM   517  C  CE2  . PHE   A 1 66  ? -18.321 49.421 -3.788  1.00 34.42  ? 66  PHE   A CE2  1 
ATOM   518  C  CZ   . PHE   A 1 66  ? -18.271 48.047 -3.763  1.00 30.47  ? 66  PHE   A CZ   1 
ATOM   519  N  N    . LEU   A 1 67  ? -22.352 50.423 1.881   1.00 30.78  ? 67  LEU   A N    1 
ATOM   520  C  CA   . LEU   A 1 67  ? -22.707 50.982 3.174   1.00 31.26  ? 67  LEU   A CA   1 
ATOM   521  C  C    . LEU   A 1 67  ? -21.835 50.300 4.221   1.00 34.92  ? 67  LEU   A C    1 
ATOM   522  O  O    . LEU   A 1 67  ? -21.904 49.075 4.386   1.00 31.31  ? 67  LEU   A O    1 
ATOM   523  C  CB   . LEU   A 1 67  ? -24.194 50.758 3.460   1.00 39.03  ? 67  LEU   A CB   1 
ATOM   524  C  CG   . LEU   A 1 67  ? -24.730 51.000 4.875   1.00 48.83  ? 67  LEU   A CG   1 
ATOM   525  C  CD1  . LEU   A 1 67  ? -24.612 52.471 5.247   1.00 48.61  ? 67  LEU   A CD1  1 
ATOM   526  C  CD2  . LEU   A 1 67  ? -26.176 50.526 4.999   1.00 49.49  ? 67  LEU   A CD2  1 
ATOM   527  N  N    . VAL   A 1 68  ? -20.991 51.079 4.897   1.00 28.84  ? 68  VAL   A N    1 
ATOM   528  C  CA   . VAL   A 1 68  ? -20.102 50.568 5.931   1.00 28.54  ? 68  VAL   A CA   1 
ATOM   529  C  C    . VAL   A 1 68  ? -20.559 51.156 7.257   1.00 29.59  ? 68  VAL   A C    1 
ATOM   530  O  O    . VAL   A 1 68  ? -20.735 52.373 7.373   1.00 30.18  ? 68  VAL   A O    1 
ATOM   531  C  CB   . VAL   A 1 68  ? -18.631 50.920 5.637   1.00 27.77  ? 68  VAL   A CB   1 
ATOM   532  C  CG1  . VAL   A 1 68  ? -17.749 50.529 6.807   1.00 29.50  ? 68  VAL   A CG1  1 
ATOM   533  C  CG2  . VAL   A 1 68  ? -18.166 50.236 4.361   1.00 26.94  ? 68  VAL   A CG2  1 
ATOM   534  N  N    . GLN   A 1 69  ? -20.770 50.302 8.248   1.00 28.00  ? 69  GLN   A N    1 
ATOM   535  C  CA   . GLN   A 1 69  ? -21.235 50.754 9.554   1.00 31.01  ? 69  GLN   A CA   1 
ATOM   536  C  C    . GLN   A 1 69  ? -20.254 50.297 10.621  1.00 30.26  ? 69  GLN   A C    1 
ATOM   537  O  O    . GLN   A 1 69  ? -19.971 49.101 10.732  1.00 28.13  ? 69  GLN   A O    1 
ATOM   538  C  CB   . GLN   A 1 69  ? -22.645 50.233 9.833   1.00 31.85  ? 69  GLN   A CB   1 
ATOM   539  C  CG   . GLN   A 1 69  ? -23.605 50.538 8.682   1.00 45.50  ? 69  GLN   A CG   1 
ATOM   540  C  CD   . GLN   A 1 69  ? -24.993 49.973 8.894   1.00 55.23  ? 69  GLN   A CD   1 
ATOM   541  O  OE1  . GLN   A 1 69  ? -25.359 48.943 8.315   1.00 48.14  ? 69  GLN   A OE1  1 
ATOM   542  N  NE2  . GLN   A 1 69  ? -25.785 50.659 9.714   1.00 56.81  ? 69  GLN   A NE2  1 
ATOM   543  N  N    . ALA   A 1 70  ? -19.730 51.252 11.393  1.00 30.36  ? 70  ALA   A N    1 
ATOM   544  C  CA   . ALA   A 1 70  ? -18.861 50.998 12.536  1.00 33.78  ? 70  ALA   A CA   1 
ATOM   545  C  C    . ALA   A 1 70  ? -19.672 51.361 13.776  1.00 41.73  ? 70  ALA   A C    1 
ATOM   546  O  O    . ALA   A 1 70  ? -19.858 52.543 14.077  1.00 36.71  ? 70  ALA   A O    1 
ATOM   547  C  CB   . ALA   A 1 70  ? -17.580 51.822 12.440  1.00 33.14  ? 70  ALA   A CB   1 
ATOM   548  N  N    . GLY   A 1 71  ? -20.167 50.349 14.483  1.00 45.90  ? 71  GLY   A N    1 
ATOM   549  C  CA   . GLY   A 1 71  ? -21.166 50.621 15.509  1.00 45.99  ? 71  GLY   A CA   1 
ATOM   550  C  C    . GLY   A 1 71  ? -22.386 51.219 14.843  1.00 46.96  ? 71  GLY   A C    1 
ATOM   551  O  O    . GLY   A 1 71  ? -22.886 50.692 13.842  1.00 50.97  ? 71  GLY   A O    1 
ATOM   552  N  N    . ASN   A 1 72  ? -22.869 52.343 15.371  1.00 56.91  ? 72  ASN   A N    1 
ATOM   553  C  CA   . ASN   A 1 72  ? -23.941 53.065 14.695  1.00 65.49  ? 72  ASN   A CA   1 
ATOM   554  C  C    . ASN   A 1 72  ? -23.429 54.104 13.704  1.00 60.68  ? 72  ASN   A C    1 
ATOM   555  O  O    . ASN   A 1 72  ? -24.228 54.647 12.933  1.00 67.99  ? 72  ASN   A O    1 
ATOM   556  C  CB   . ASN   A 1 72  ? -24.866 53.754 15.710  1.00 70.50  ? 72  ASN   A CB   1 
ATOM   557  C  CG   . ASN   A 1 72  ? -26.153 54.275 15.069  1.00 75.30  ? 72  ASN   A CG   1 
ATOM   558  O  OD1  . ASN   A 1 72  ? -26.486 53.918 13.937  1.00 76.83  ? 72  ASN   A OD1  1 
ATOM   559  N  ND2  . ASN   A 1 72  ? -26.871 55.134 15.788  1.00 74.34  ? 72  ASN   A ND2  1 
ATOM   560  N  N    . VAL   A 1 73  ? -22.127 54.380 13.685  1.00 53.10  ? 73  VAL   A N    1 
ATOM   561  C  CA   . VAL   A 1 73  ? -21.586 55.423 12.819  1.00 44.66  ? 73  VAL   A CA   1 
ATOM   562  C  C    . VAL   A 1 73  ? -21.440 54.874 11.406  1.00 46.35  ? 73  VAL   A C    1 
ATOM   563  O  O    . VAL   A 1 73  ? -20.745 53.880 11.183  1.00 40.42  ? 73  VAL   A O    1 
ATOM   564  C  CB   . VAL   A 1 73  ? -20.238 55.928 13.348  1.00 47.42  ? 73  VAL   A CB   1 
ATOM   565  C  CG1  . VAL   A 1 73  ? -19.530 56.742 12.282  1.00 49.30  ? 73  VAL   A CG1  1 
ATOM   566  C  CG2  . VAL   A 1 73  ? -20.435 56.733 14.620  1.00 54.21  ? 73  VAL   A CG2  1 
ATOM   567  N  N    . GLN   A 1 74  ? -22.077 55.523 10.441  1.00 45.37  ? 74  GLN   A N    1 
ATOM   568  C  CA   . GLN   A 1 74  ? -21.870 55.146 9.050   1.00 42.81  ? 74  GLN   A CA   1 
ATOM   569  C  C    . GLN   A 1 74  ? -20.574 55.784 8.557   1.00 43.17  ? 74  GLN   A C    1 
ATOM   570  O  O    . GLN   A 1 74  ? -20.336 56.969 8.799   1.00 41.58  ? 74  GLN   A O    1 
ATOM   571  C  CB   . GLN   A 1 74  ? -23.059 55.586 8.198   1.00 50.04  ? 74  GLN   A CB   1 
ATOM   572  C  CG   . GLN   A 1 74  ? -23.010 55.112 6.754   1.00 50.49  ? 74  GLN   A CG   1 
ATOM   573  C  CD   . GLN   A 1 74  ? -24.179 55.633 5.931   1.00 66.16  ? 74  GLN   A CD   1 
ATOM   574  O  OE1  . GLN   A 1 74  ? -24.000 56.199 4.845   1.00 64.29  ? 74  GLN   A OE1  1 
ATOM   575  N  NE2  . GLN   A 1 74  ? -25.385 55.464 6.460   1.00 67.19  ? 74  GLN   A NE2  1 
ATOM   576  N  N    . LEU   A 1 75  ? -19.726 55.001 7.890   1.00 33.21  ? 75  LEU   A N    1 
ATOM   577  C  CA   . LEU   A 1 75  ? -18.474 55.497 7.335   1.00 31.06  ? 75  LEU   A CA   1 
ATOM   578  C  C    . LEU   A 1 75  ? -18.667 55.778 5.856   1.00 37.23  ? 75  LEU   A C    1 
ATOM   579  O  O    . LEU   A 1 75  ? -19.256 54.968 5.134   1.00 40.40  ? 75  LEU   A O    1 
ATOM   580  C  CB   . LEU   A 1 75  ? -17.330 54.492 7.505   1.00 29.73  ? 75  LEU   A CB   1 
ATOM   581  C  CG   . LEU   A 1 75  ? -16.951 54.072 8.924   1.00 30.32  ? 75  LEU   A CG   1 
ATOM   582  C  CD1  . LEU   A 1 75  ? -15.796 53.084 8.859   1.00 29.96  ? 75  LEU   A CD1  1 
ATOM   583  C  CD2  . LEU   A 1 75  ? -16.634 55.277 9.801   1.00 33.66  ? 75  LEU   A CD2  1 
ATOM   584  N  N    . ARG   A 1 76  ? -18.163 56.920 5.401   1.00 32.21  ? 76  ARG   A N    1 
ATOM   585  C  CA   . ARG   A 1 76  ? -18.385 57.341 4.028   1.00 34.14  ? 76  ARG   A CA   1 
ATOM   586  C  C    . ARG   A 1 76  ? -17.298 56.729 3.148   1.00 36.31  ? 76  ARG   A C    1 
ATOM   587  O  O    . ARG   A 1 76  ? -16.102 56.945 3.380   1.00 32.31  ? 76  ARG   A O    1 
ATOM   588  C  CB   . ARG   A 1 76  ? -18.398 58.867 3.931   1.00 33.50  ? 76  ARG   A CB   1 
ATOM   589  C  CG   . ARG   A 1 76  ? -18.114 59.399 2.544   1.00 46.87  ? 76  ARG   A CG   1 
ATOM   590  C  CD   . ARG   A 1 76  ? -18.921 60.658 2.279   1.00 52.45  ? 76  ARG   A CD   1 
ATOM   591  N  NE   . ARG   A 1 76  ? -18.860 61.040 0.872   1.00 64.60  ? 76  ARG   A NE   1 
ATOM   592  C  CZ   . ARG   A 1 76  ? -17.937 61.837 0.351   1.00 68.05  ? 76  ARG   A CZ   1 
ATOM   593  N  NH1  . ARG   A 1 76  ? -17.002 62.397 1.103   1.00 64.13  ? 76  ARG   A NH1  1 
ATOM   594  N  NH2  . ARG   A 1 76  ? -17.950 62.075 -0.957  1.00 67.44  ? 76  ARG   A NH2  1 
ATOM   595  N  N    . VAL   A 1 77  ? -17.721 55.942 2.161   1.00 32.01  ? 77  VAL   A N    1 
ATOM   596  C  CA   . VAL   A 1 77  ? -16.811 55.295 1.219   1.00 33.49  ? 77  VAL   A CA   1 
ATOM   597  C  C    . VAL   A 1 77  ? -16.385 56.293 0.148   1.00 29.48  ? 77  VAL   A C    1 
ATOM   598  O  O    . VAL   A 1 77  ? -17.229 56.892 -0.528  1.00 30.84  ? 77  VAL   A O    1 
ATOM   599  C  CB   . VAL   A 1 77  ? -17.461 54.053 0.596   1.00 27.50  ? 77  VAL   A CB   1 
ATOM   600  C  CG1  . VAL   A 1 77  ? -16.512 53.408 -0.377  1.00 25.39  ? 77  VAL   A CG1  1 
ATOM   601  C  CG2  . VAL   A 1 77  ? -17.819 53.049 1.726   1.00 27.62  ? 77  VAL   A CG2  1 
ATOM   602  N  N    . ILE   A 1 78  ? -15.073 56.473 -0.011  1.00 27.50  ? 78  ILE   A N    1 
ATOM   603  C  CA   . ILE   A 1 78  ? -14.538 57.426 -0.976  1.00 27.21  ? 78  ILE   A CA   1 
ATOM   604  C  C    . ILE   A 1 78  ? -13.678 56.763 -2.037  1.00 29.33  ? 78  ILE   A C    1 
ATOM   605  O  O    . ILE   A 1 78  ? -13.202 57.449 -2.948  1.00 33.09  ? 78  ILE   A O    1 
ATOM   606  C  CB   . ILE   A 1 78  ? -13.754 58.560 -0.285  1.00 35.31  ? 78  ILE   A CB   1 
ATOM   607  C  CG1  . ILE   A 1 78  ? -12.579 57.999 0.526   1.00 34.61  ? 78  ILE   A CG1  1 
ATOM   608  C  CG2  . ILE   A 1 78  ? -14.693 59.388 0.604   1.00 38.84  ? 78  ILE   A CG2  1 
ATOM   609  C  CD1  . ILE   A 1 78  ? -11.671 59.091 1.071   1.00 37.41  ? 78  ILE   A CD1  1 
ATOM   610  N  N    . GLY   A 1 79  ? -13.467 55.453 -1.953  1.00 29.55  ? 79  GLY   A N    1 
ATOM   611  C  CA   . GLY   A 1 79  ? -12.827 54.738 -3.044  1.00 28.83  ? 79  GLY   A CA   1 
ATOM   612  C  C    . GLY   A 1 79  ? -13.068 53.254 -2.897  1.00 28.58  ? 79  GLY   A C    1 
ATOM   613  O  O    . GLY   A 1 79  ? -13.388 52.774 -1.811  1.00 25.93  ? 79  GLY   A O    1 
ATOM   614  N  N    . HIS   A 1 80  ? -12.927 52.525 -4.001  1.00 25.54  ? 80  HIS   A N    1 
ATOM   615  C  CA   . HIS   A 1 80  ? -13.050 51.078 -3.931  1.00 27.88  ? 80  HIS   A CA   1 
ATOM   616  C  C    . HIS   A 1 80  ? -12.101 50.445 -4.933  1.00 28.76  ? 80  HIS   A C    1 
ATOM   617  O  O    . HIS   A 1 80  ? -11.857 50.994 -6.019  1.00 27.08  ? 80  HIS   A O    1 
ATOM   618  C  CB   . HIS   A 1 80  ? -14.481 50.586 -4.202  1.00 27.19  ? 80  HIS   A CB   1 
ATOM   619  C  CG   . HIS   A 1 80  ? -15.032 51.016 -5.526  1.00 28.06  ? 80  HIS   A CG   1 
ATOM   620  N  ND1  . HIS   A 1 80  ? -15.345 52.325 -5.816  1.00 28.33  ? 80  HIS   A ND1  1 
ATOM   621  C  CD2  . HIS   A 1 80  ? -15.262 50.312 -6.660  1.00 27.99  ? 80  HIS   A CD2  1 
ATOM   622  C  CE1  . HIS   A 1 80  ? -15.782 52.406 -7.064  1.00 34.65  ? 80  HIS   A CE1  1 
ATOM   623  N  NE2  . HIS   A 1 80  ? -15.742 51.198 -7.599  1.00 30.19  ? 80  HIS   A NE2  1 
ATOM   624  N  N    . SER   A 1 81  ? -11.581 49.275 -4.566  1.00 24.32  ? 81  SER   A N    1 
ATOM   625  C  CA   . SER   A 1 81  ? -10.771 48.485 -5.492  1.00 26.20  ? 81  SER   A CA   1 
ATOM   626  C  C    . SER   A 1 81  ? -10.825 47.026 -5.074  1.00 31.26  ? 81  SER   A C    1 
ATOM   627  O  O    . SER   A 1 81  ? -11.210 46.697 -3.948  1.00 27.05  ? 81  SER   A O    1 
ATOM   628  C  CB   . SER   A 1 81  ? -9.316  48.966 -5.545  1.00 30.46  ? 81  SER   A CB   1 
ATOM   629  O  OG   . SER   A 1 81  ? -8.679  48.825 -4.291  1.00 31.29  ? 81  SER   A OG   1 
ATOM   630  N  N    . MET   A 1 82  ? -10.392 46.158 -5.987  1.00 25.30  ? 82  MET   A N    1 
ATOM   631  C  CA   . MET   A 1 82  ? -10.322 44.727 -5.731  1.00 26.66  ? 82  MET   A CA   1 
ATOM   632  C  C    . MET   A 1 82  ? -8.862  44.303 -5.685  1.00 25.85  ? 82  MET   A C    1 
ATOM   633  O  O    . MET   A 1 82  ? -8.059  44.724 -6.518  1.00 26.59  ? 82  MET   A O    1 
ATOM   634  C  CB   . MET   A 1 82  ? -11.091 43.980 -6.819  1.00 30.91  ? 82  MET   A CB   1 
ATOM   635  C  CG   . MET   A 1 82  ? -10.912 42.492 -6.920  1.00 31.26  ? 82  MET   A CG   1 
ATOM   636  S  SD   . MET   A 1 82  ? -12.513 41.813 -7.407  1.00 30.41  ? 82  MET   A SD   1 
ATOM   637  C  CE   . MET   A 1 82  ? -12.431 42.256 -9.151  1.00 31.52  ? 82  MET   A CE   1 
ATOM   638  N  N    . GLN   A 1 83  ? -8.516  43.479 -4.700  1.00 21.43  ? 83  GLN   A N    1 
ATOM   639  C  CA   . GLN   A 1 83  ? -7.182  42.897 -4.558  1.00 25.40  ? 83  GLN   A CA   1 
ATOM   640  C  C    . GLN   A 1 83  ? -7.403  41.399 -4.366  1.00 18.98  ? 83  GLN   A C    1 
ATOM   641  O  O    . GLN   A 1 83  ? -7.756  40.961 -3.267  1.00 23.17  ? 83  GLN   A O    1 
ATOM   642  C  CB   . GLN   A 1 83  ? -6.433  43.513 -3.378  1.00 32.38  ? 83  GLN   A CB   1 
ATOM   643  C  CG   . GLN   A 1 83  ? -5.297  42.651 -2.826  1.00 42.27  ? 83  GLN   A CG   1 
ATOM   644  C  CD   . GLN   A 1 83  ? -4.056  43.440 -2.467  1.00 38.06  ? 83  GLN   A CD   1 
ATOM   645  O  OE1  . GLN   A 1 83  ? -4.138  44.612 -2.100  1.00 42.76  ? 83  GLN   A OE1  1 
ATOM   646  N  NE2  . GLN   A 1 83  ? -2.904  42.786 -2.528  1.00 42.50  ? 83  GLN   A NE2  1 
ATOM   647  N  N    . ASN   A 1 84  ? -7.199  40.627 -5.437  1.00 19.19  ? 84  ASN   A N    1 
ATOM   648  C  CA   . ASN   A 1 84  ? -7.467  39.194 -5.426  1.00 18.70  ? 84  ASN   A CA   1 
ATOM   649  C  C    . ASN   A 1 84  ? -8.879  38.957 -4.914  1.00 18.14  ? 84  ASN   A C    1 
ATOM   650  O  O    . ASN   A 1 84  ? -9.820  39.517 -5.495  1.00 18.97  ? 84  ASN   A O    1 
ATOM   651  C  CB   . ASN   A 1 84  ? -6.371  38.440 -4.665  1.00 17.40  ? 84  ASN   A CB   1 
ATOM   652  C  CG   . ASN   A 1 84  ? -4.988  38.836 -5.168  1.00 22.74  ? 84  ASN   A CG   1 
ATOM   653  O  OD1  . ASN   A 1 84  ? -4.687  38.609 -6.347  1.00 24.94  ? 84  ASN   A OD1  1 
ATOM   654  N  ND2  . ASN   A 1 84  ? -4.163  39.425 -4.318  1.00 19.97  ? 84  ASN   A ND2  1 
ATOM   655  N  N    . CYS   A 1 85  ? -9.063  38.183 -3.839  1.00 17.08  ? 85  CYS   A N    1 
ATOM   656  C  CA   . CYS   A 1 85  ? -10.427 37.902 -3.414  1.00 14.83  ? 85  CYS   A CA   1 
ATOM   657  C  C    . CYS   A 1 85  ? -10.918 38.852 -2.317  1.00 21.75  ? 85  CYS   A C    1 
ATOM   658  O  O    . CYS   A 1 85  ? -11.974 38.607 -1.728  1.00 18.68  ? 85  CYS   A O    1 
ATOM   659  C  CB   . CYS   A 1 85  ? -10.551 36.452 -2.961  1.00 18.73  ? 85  CYS   A CB   1 
ATOM   660  S  SG   . CYS   A 1 85  ? -10.188 35.275 -4.319  1.00 20.04  ? 85  CYS   A SG   1 
ATOM   661  N  N    . VAL   A 1 86  ? -10.214 39.946 -2.070  1.00 16.87  ? 86  VAL   A N    1 
ATOM   662  C  CA   . VAL   A 1 86  ? -10.606 40.915 -1.056  1.00 18.10  ? 86  VAL   A CA   1 
ATOM   663  C  C    . VAL   A 1 86  ? -10.954 42.234 -1.735  1.00 22.82  ? 86  VAL   A C    1 
ATOM   664  O  O    . VAL   A 1 86  ? -10.445 42.565 -2.812  1.00 23.76  ? 86  VAL   A O    1 
ATOM   665  C  CB   . VAL   A 1 86  ? -9.480  41.075 -0.010  1.00 21.24  ? 86  VAL   A CB   1 
ATOM   666  C  CG1  . VAL   A 1 86  ? -9.548  42.424 0.667   1.00 31.82  ? 86  VAL   A CG1  1 
ATOM   667  C  CG2  . VAL   A 1 86  ? -9.609  39.947 1.017   1.00 21.59  ? 86  VAL   A CG2  1 
ATOM   668  N  N    . LEU   A 1 87  ? -11.884 42.959 -1.134  1.00 18.67  ? 87  LEU   A N    1 
ATOM   669  C  CA   . LEU   A 1 87  ? -12.250 44.291 -1.573  1.00 17.46  ? 87  LEU   A CA   1 
ATOM   670  C  C    . LEU   A 1 87  ? -11.637 45.259 -0.572  1.00 24.69  ? 87  LEU   A C    1 
ATOM   671  O  O    . LEU   A 1 87  ? -11.571 44.954 0.629   1.00 21.68  ? 87  LEU   A O    1 
ATOM   672  C  CB   . LEU   A 1 87  ? -13.777 44.392 -1.651  1.00 23.13  ? 87  LEU   A CB   1 
ATOM   673  C  CG   . LEU   A 1 87  ? -14.593 45.613 -2.033  1.00 38.15  ? 87  LEU   A CG   1 
ATOM   674  C  CD1  . LEU   A 1 87  ? -14.399 45.899 -3.481  1.00 35.41  ? 87  LEU   A CD1  1 
ATOM   675  C  CD2  . LEU   A 1 87  ? -16.074 45.312 -1.755  1.00 29.07  ? 87  LEU   A CD2  1 
ATOM   676  N  N    . LYS   A 1 88  ? -11.114 46.375 -1.077  1.00 22.79  ? 88  LYS   A N    1 
ATOM   677  C  CA   . LYS   A 1 88  ? -10.565 47.449 -0.256  1.00 22.34  ? 88  LYS   A CA   1 
ATOM   678  C  C    . LYS   A 1 88  ? -11.446 48.672 -0.462  1.00 28.93  ? 88  LYS   A C    1 
ATOM   679  O  O    . LYS   A 1 88  ? -11.552 49.189 -1.586  1.00 23.69  ? 88  LYS   A O    1 
ATOM   680  C  CB   . LYS   A 1 88  ? -9.117  47.760 -0.631  1.00 21.54  ? 88  LYS   A CB   1 
ATOM   681  C  CG   . LYS   A 1 88  ? -8.155  46.598 -0.351  1.00 24.17  ? 88  LYS   A CG   1 
ATOM   682  C  CD   . LYS   A 1 88  ? -6.807  46.771 -1.021  1.00 33.88  ? 88  LYS   A CD   1 
ATOM   683  C  CE   . LYS   A 1 88  ? -5.908  47.662 -0.204  1.00 37.75  ? 88  LYS   A CE   1 
ATOM   684  N  NZ   . LYS   A 1 88  ? -4.517  47.710 -0.749  1.00 47.83  ? 88  LYS   A NZ   1 
ATOM   685  N  N    . LEU   A 1 89  ? -12.094 49.117 0.607   1.00 24.73  ? 89  LEU   A N    1 
ATOM   686  C  CA   . LEU   A 1 89  ? -12.963 50.284 0.550   1.00 23.29  ? 89  LEU   A CA   1 
ATOM   687  C  C    . LEU   A 1 89  ? -12.248 51.418 1.278   1.00 27.18  ? 89  LEU   A C    1 
ATOM   688  O  O    . LEU   A 1 89  ? -12.063 51.360 2.495   1.00 25.02  ? 89  LEU   A O    1 
ATOM   689  C  CB   . LEU   A 1 89  ? -14.316 49.977 1.188   1.00 26.26  ? 89  LEU   A CB   1 
ATOM   690  C  CG   . LEU   A 1 89  ? -15.092 48.826 0.536   1.00 26.68  ? 89  LEU   A CG   1 
ATOM   691  C  CD1  . LEU   A 1 89  ? -16.315 48.449 1.350   1.00 29.69  ? 89  LEU   A CD1  1 
ATOM   692  C  CD2  . LEU   A 1 89  ? -15.493 49.186 -0.897  1.00 29.03  ? 89  LEU   A CD2  1 
ATOM   693  N  N    . LYS   A 1 90  ? -11.816 52.435 0.545   1.00 25.00  ? 90  LYS   A N    1 
ATOM   694  C  CA   . LYS   A 1 90  ? -11.244 53.600 1.206   1.00 27.69  ? 90  LYS   A CA   1 
ATOM   695  C  C    . LYS   A 1 90  ? -12.372 54.439 1.797   1.00 25.42  ? 90  LYS   A C    1 
ATOM   696  O  O    . LYS   A 1 90  ? -13.334 54.767 1.096   1.00 29.40  ? 90  LYS   A O    1 
ATOM   697  C  CB   . LYS   A 1 90  ? -10.412 54.430 0.224   1.00 30.00  ? 90  LYS   A CB   1 
ATOM   698  C  CG   . LYS   A 1 90  ? -9.523  55.454 0.920   1.00 31.65  ? 90  LYS   A CG   1 
ATOM   699  C  CD   . LYS   A 1 90  ? -9.084  56.577 -0.010  1.00 39.03  ? 90  LYS   A CD   1 
ATOM   700  C  CE   . LYS   A 1 90  ? -7.674  57.057 0.347   1.00 48.23  ? 90  LYS   A CE   1 
ATOM   701  N  NZ   . LYS   A 1 90  ? -6.885  57.490 -0.854  1.00 56.53  ? 90  LYS   A NZ   1 
ATOM   702  N  N    . VAL   A 1 91  ? -12.241 54.788 3.081   1.00 26.45  ? 91  VAL   A N    1 
ATOM   703  C  CA   . VAL   A 1 91  ? -13.243 55.561 3.805   1.00 26.60  ? 91  VAL   A CA   1 
ATOM   704  C  C    . VAL   A 1 91  ? -12.634 56.900 4.213   1.00 30.40  ? 91  VAL   A C    1 
ATOM   705  O  O    . VAL   A 1 91  ? -11.413 57.088 4.201   1.00 29.46  ? 91  VAL   A O    1 
ATOM   706  C  CB   . VAL   A 1 91  ? -13.772 54.799 5.038   1.00 28.91  ? 91  VAL   A CB   1 
ATOM   707  C  CG1  . VAL   A 1 91  ? -14.606 53.605 4.591   1.00 29.18  ? 91  VAL   A CG1  1 
ATOM   708  C  CG2  . VAL   A 1 91  ? -12.614 54.364 5.928   1.00 28.20  ? 91  VAL   A CG2  1 
ATOM   709  N  N    . ASP   A 1 92  ? -13.499 57.847 4.570   1.00 32.92  ? 92  ASP   A N    1 
ATOM   710  C  CA   . ASP   A 1 92  ? -13.012 59.198 4.821   1.00 33.85  ? 92  ASP   A CA   1 
ATOM   711  C  C    . ASP   A 1 92  ? -12.525 59.404 6.251   1.00 38.85  ? 92  ASP   A C    1 
ATOM   712  O  O    . ASP   A 1 92  ? -12.116 60.517 6.588   1.00 37.08  ? 92  ASP   A O    1 
ATOM   713  C  CB   . ASP   A 1 92  ? -14.089 60.243 4.481   1.00 44.49  ? 92  ASP   A CB   1 
ATOM   714  C  CG   . ASP   A 1 92  ? -15.293 60.178 5.397   1.00 44.53  ? 92  ASP   A CG   1 
ATOM   715  O  OD1  . ASP   A 1 92  ? -15.251 59.440 6.400   1.00 45.43  ? 92  ASP   A OD1  1 
ATOM   716  O  OD2  . ASP   A 1 92  ? -16.278 60.898 5.121   1.00 52.27  ? 92  ASP   A OD2  1 
ATOM   717  N  N    . THR   A 1 93  ? -12.552 58.371 7.093   1.00 34.87  ? 93  THR   A N    1 
ATOM   718  C  CA   . THR   A 1 93  ? -12.085 58.464 8.473   1.00 34.81  ? 93  THR   A CA   1 
ATOM   719  C  C    . THR   A 1 93  ? -11.129 57.321 8.782   1.00 33.55  ? 93  THR   A C    1 
ATOM   720  O  O    . THR   A 1 93  ? -11.451 56.156 8.534   1.00 31.70  ? 93  THR   A O    1 
ATOM   721  C  CB   . THR   A 1 93  ? -13.250 58.430 9.471   1.00 38.97  ? 93  THR   A CB   1 
ATOM   722  O  OG1  . THR   A 1 93  ? -14.333 59.230 8.982   1.00 40.25  ? 93  THR   A OG1  1 
ATOM   723  C  CG2  . THR   A 1 93  ? -12.802 58.935 10.828  1.00 42.75  ? 93  THR   A CG2  1 
ATOM   724  N  N    . ALA   A 1 94  ? -9.968  57.650 9.343   1.00 33.36  ? 94  ALA   A N    1 
ATOM   725  C  CA   . ALA   A 1 94  ? -9.047  56.628 9.812   1.00 33.02  ? 94  ALA   A CA   1 
ATOM   726  C  C    . ALA   A 1 94  ? -9.524  56.070 11.146  1.00 32.56  ? 94  ALA   A C    1 
ATOM   727  O  O    . ALA   A 1 94  ? -9.943  56.818 12.035  1.00 32.02  ? 94  ALA   A O    1 
ATOM   728  C  CB   . ALA   A 1 94  ? -7.638  57.202 9.943   1.00 34.90  ? 94  ALA   A CB   1 
ATOM   729  N  N    . ASN   A 1 95  ? -9.482  54.751 11.280  1.00 28.02  ? 95  ASN   A N    1 
ATOM   730  C  CA   . ASN   A 1 95  ? -9.975  54.127 12.508  1.00 25.97  ? 95  ASN   A CA   1 
ATOM   731  C  C    . ASN   A 1 95  ? -9.100  54.557 13.681  1.00 25.54  ? 95  ASN   A C    1 
ATOM   732  O  O    . ASN   A 1 95  ? -7.898  54.255 13.694  1.00 27.00  ? 95  ASN   A O    1 
ATOM   733  C  CB   . ASN   A 1 95  ? -10.006 52.604 12.348  1.00 24.61  ? 95  ASN   A CB   1 
ATOM   734  C  CG   . ASN   A 1 95  ? -10.467 51.881 13.614  1.00 28.14  ? 95  ASN   A CG   1 
ATOM   735  O  OD1  . ASN   A 1 95  ? -10.888 52.516 14.594  1.00 25.32  ? 95  ASN   A OD1  1 
ATOM   736  N  ND2  . ASN   A 1 95  ? -10.431 50.546 13.581  1.00 25.12  ? 95  ASN   A ND2  1 
ATOM   737  N  N    . PRO   A 1 96  ? -9.645  55.271 14.671  1.00 27.01  ? 96  PRO   A N    1 
ATOM   738  C  CA   . PRO   A 1 96  ? -8.818  55.717 15.804  1.00 31.08  ? 96  PRO   A CA   1 
ATOM   739  C  C    . PRO   A 1 96  ? -8.272  54.575 16.639  1.00 31.23  ? 96  PRO   A C    1 
ATOM   740  O  O    . PRO   A 1 96  ? -7.308  54.774 17.395  1.00 30.40  ? 96  PRO   A O    1 
ATOM   741  C  CB   . PRO   A 1 96  ? -9.785  56.579 16.637  1.00 31.75  ? 96  PRO   A CB   1 
ATOM   742  C  CG   . PRO   A 1 96  ? -11.048 56.687 15.841  1.00 40.75  ? 96  PRO   A CG   1 
ATOM   743  C  CD   . PRO   A 1 96  ? -11.074 55.558 14.870  1.00 29.27  ? 96  PRO   A CD   1 
ATOM   744  N  N    . LYS   A 1 97  ? -8.874  53.393 16.547  1.00 26.29  ? 97  LYS   A N    1 
ATOM   745  C  CA   . LYS   A 1 97  ? -8.471  52.234 17.323  1.00 24.76  ? 97  LYS   A CA   1 
ATOM   746  C  C    . LYS   A 1 97  ? -7.526  51.311 16.560  1.00 25.79  ? 97  LYS   A C    1 
ATOM   747  O  O    . LYS   A 1 97  ? -7.310  50.174 16.986  1.00 26.30  ? 97  LYS   A O    1 
ATOM   748  C  CB   . LYS   A 1 97  ? -9.712  51.458 17.758  1.00 26.42  ? 97  LYS   A CB   1 
ATOM   749  C  CG   . LYS   A 1 97  ? -10.552 52.185 18.796  1.00 33.21  ? 97  LYS   A CG   1 
ATOM   750  C  CD   . LYS   A 1 97  ? -11.926 51.561 18.869  1.00 32.07  ? 97  LYS   A CD   1 
ATOM   751  C  CE   . LYS   A 1 97  ? -12.891 52.407 19.671  1.00 46.19  ? 97  LYS   A CE   1 
ATOM   752  N  NZ   . LYS   A 1 97  ? -14.182 51.693 19.862  1.00 53.02  ? 97  LYS   A NZ   1 
ATOM   753  N  N    . THR   A 1 98  ? -6.954  51.768 15.454  1.00 24.94  ? 98  THR   A N    1 
ATOM   754  C  CA   . THR   A 1 98  ? -6.095  50.888 14.675  1.00 24.53  ? 98  THR   A CA   1 
ATOM   755  C  C    . THR   A 1 98  ? -4.895  50.469 15.517  1.00 25.50  ? 98  THR   A C    1 
ATOM   756  O  O    . THR   A 1 98  ? -4.163  51.340 16.018  1.00 27.06  ? 98  THR   A O    1 
ATOM   757  C  CB   . THR   A 1 98  ? -5.620  51.598 13.411  1.00 29.98  ? 98  THR   A CB   1 
ATOM   758  O  OG1  . THR   A 1 98  ? -6.764  52.030 12.679  1.00 27.05  ? 98  THR   A OG1  1 
ATOM   759  C  CG2  . THR   A 1 98  ? -4.812  50.634 12.528  1.00 26.48  ? 98  THR   A CG2  1 
ATOM   760  N  N    . PRO   A 1 99  ? -4.653  49.184 15.702  1.00 24.16  ? 99  PRO   A N    1 
ATOM   761  C  CA   . PRO   A 1 99  ? -3.443  48.749 16.398  1.00 20.80  ? 99  PRO   A CA   1 
ATOM   762  C  C    . PRO   A 1 99  ? -2.266  48.735 15.434  1.00 23.70  ? 99  PRO   A C    1 
ATOM   763  O  O    . PRO   A 1 99  ? -2.432  48.857 14.221  1.00 26.25  ? 99  PRO   A O    1 
ATOM   764  C  CB   . PRO   A 1 99  ? -3.807  47.338 16.857  1.00 21.93  ? 99  PRO   A CB   1 
ATOM   765  C  CG   . PRO   A 1 99  ? -4.699  46.821 15.716  1.00 21.44  ? 99  PRO   A CG   1 
ATOM   766  C  CD   . PRO   A 1 99  ? -5.446  48.045 15.194  1.00 24.85  ? 99  PRO   A CD   1 
ATOM   767  N  N    . LYS   A 1 100 ? -1.063  48.577 15.978  1.00 24.74  ? 100 LYS   A N    1 
ATOM   768  C  CA   . LYS   A 1 100 ? 0.050   48.207 15.108  1.00 23.92  ? 100 LYS   A CA   1 
ATOM   769  C  C    . LYS   A 1 100 ? -0.267  46.858 14.482  1.00 22.23  ? 100 LYS   A C    1 
ATOM   770  O  O    . LYS   A 1 100 ? -0.735  45.947 15.162  1.00 21.42  ? 100 LYS   A O    1 
ATOM   771  C  CB   . LYS   A 1 100 ? 1.366   48.142 15.884  1.00 27.56  ? 100 LYS   A CB   1 
ATOM   772  C  CG   . LYS   A 1 100 ? 1.918   49.523 16.244  1.00 38.60  ? 100 LYS   A CG   1 
ATOM   773  C  CD   . LYS   A 1 100 ? 2.978   49.463 17.327  1.00 50.78  ? 100 LYS   A CD   1 
ATOM   774  C  CE   . LYS   A 1 100 ? 3.595   50.837 17.572  1.00 56.95  ? 100 LYS   A CE   1 
ATOM   775  N  NZ   . LYS   A 1 100 ? 5.092   50.796 17.581  1.00 61.01  ? 100 LYS   A NZ   1 
ATOM   776  N  N    . TYR   A 1 101 ? -0.056  46.719 13.173  1.00 23.07  ? 101 TYR   A N    1 
ATOM   777  C  CA   . TYR   A 1 101 ? -0.463  45.456 12.578  1.00 21.40  ? 101 TYR   A CA   1 
ATOM   778  C  C    . TYR   A 1 101 ? 0.434   45.110 11.399  1.00 23.46  ? 101 TYR   A C    1 
ATOM   779  O  O    . TYR   A 1 101 ? 1.174   45.948 10.865  1.00 20.35  ? 101 TYR   A O    1 
ATOM   780  C  CB   . TYR   A 1 101 ? -1.921  45.489 12.092  1.00 19.55  ? 101 TYR   A CB   1 
ATOM   781  C  CG   . TYR   A 1 101 ? -2.138  46.391 10.883  1.00 21.17  ? 101 TYR   A CG   1 
ATOM   782  C  CD1  . TYR   A 1 101 ? -2.406  47.749 11.044  1.00 24.51  ? 101 TYR   A CD1  1 
ATOM   783  C  CD2  . TYR   A 1 101 ? -2.100  45.875 9.597   1.00 20.86  ? 101 TYR   A CD2  1 
ATOM   784  C  CE1  . TYR   A 1 101 ? -2.616  48.583 9.953   1.00 25.78  ? 101 TYR   A CE1  1 
ATOM   785  C  CE2  . TYR   A 1 101 ? -2.308  46.706 8.493   1.00 21.59  ? 101 TYR   A CE2  1 
ATOM   786  C  CZ   . TYR   A 1 101 ? -2.560  48.048 8.685   1.00 25.32  ? 101 TYR   A CZ   1 
ATOM   787  O  OH   . TYR   A 1 101 ? -2.765  48.853 7.588   1.00 32.84  ? 101 TYR   A OH   1 
ATOM   788  N  N    . LYS   A 1 102 ? 0.315   43.848 10.991  1.00 19.54  ? 102 LYS   A N    1 
ATOM   789  C  CA   . LYS   A 1 102 ? 1.014   43.273 9.849   1.00 21.68  ? 102 LYS   A CA   1 
ATOM   790  C  C    . LYS   A 1 102 ? 0.042   42.322 9.175   1.00 19.34  ? 102 LYS   A C    1 
ATOM   791  O  O    . LYS   A 1 102 ? -0.840  41.767 9.832   1.00 17.65  ? 102 LYS   A O    1 
ATOM   792  C  CB   . LYS   A 1 102 ? 2.262   42.506 10.318  1.00 22.00  ? 102 LYS   A CB   1 
ATOM   793  C  CG   . LYS   A 1 102 ? 3.351   43.428 10.842  1.00 28.04  ? 102 LYS   A CG   1 
ATOM   794  C  CD   . LYS   A 1 102 ? 4.716   42.839 10.738  1.00 37.48  ? 102 LYS   A CD   1 
ATOM   795  C  CE   . LYS   A 1 102 ? 4.750   41.504 11.401  1.00 31.81  ? 102 LYS   A CE   1 
ATOM   796  N  NZ   . LYS   A 1 102 ? 5.889   41.452 12.385  1.00 51.09  ? 102 LYS   A NZ   1 
ATOM   797  N  N    . PHE   A 1 103 ? 0.166   42.171 7.854   1.00 17.45  ? 103 PHE   A N    1 
ATOM   798  C  CA   . PHE   A 1 103 ? -0.518  41.108 7.121   1.00 15.78  ? 103 PHE   A CA   1 
ATOM   799  C  C    . PHE   A 1 103 ? 0.515   40.032 6.824   1.00 20.06  ? 103 PHE   A C    1 
ATOM   800  O  O    . PHE   A 1 103 ? 1.479   40.282 6.082   1.00 20.75  ? 103 PHE   A O    1 
ATOM   801  C  CB   . PHE   A 1 103 ? -1.110  41.603 5.791   1.00 13.99  ? 103 PHE   A CB   1 
ATOM   802  C  CG   . PHE   A 1 103 ? -2.303  42.532 5.915   1.00 16.53  ? 103 PHE   A CG   1 
ATOM   803  C  CD1  . PHE   A 1 103 ? -2.926  42.774 7.127   1.00 17.87  ? 103 PHE   A CD1  1 
ATOM   804  C  CD2  . PHE   A 1 103 ? -2.804  43.184 4.772   1.00 20.12  ? 103 PHE   A CD2  1 
ATOM   805  C  CE1  . PHE   A 1 103 ? -4.035  43.635 7.201   1.00 18.50  ? 103 PHE   A CE1  1 
ATOM   806  C  CE2  . PHE   A 1 103 ? -3.902  44.056 4.849   1.00 19.61  ? 103 PHE   A CE2  1 
ATOM   807  C  CZ   . PHE   A 1 103 ? -4.530  44.275 6.055   1.00 20.46  ? 103 PHE   A CZ   1 
ATOM   808  N  N    . VAL   A 1 104 ? 0.316   38.843 7.391   1.00 17.21  ? 104 VAL   A N    1 
ATOM   809  C  CA   . VAL   A 1 104 ? 1.259   37.739 7.278   1.00 16.28  ? 104 VAL   A CA   1 
ATOM   810  C  C    . VAL   A 1 104 ? 0.459   36.552 6.766   1.00 23.51  ? 104 VAL   A C    1 
ATOM   811  O  O    . VAL   A 1 104 ? -0.742  36.431 7.027   1.00 29.91  ? 104 VAL   A O    1 
ATOM   812  C  CB   . VAL   A 1 104 ? 1.959   37.407 8.613   1.00 20.64  ? 104 VAL   A CB   1 
ATOM   813  C  CG1  . VAL   A 1 104 ? 2.555   38.672 9.221   1.00 20.20  ? 104 VAL   A CG1  1 
ATOM   814  C  CG2  . VAL   A 1 104 ? 0.955   36.834 9.581   1.00 25.58  ? 104 VAL   A CG2  1 
ATOM   815  N  N    . ARG   A 1 105 ? 1.113   35.694 6.001   1.00 15.98  ? 105 ARG   A N    1 
ATOM   816  C  CA   . ARG   A 1 105 ? 0.512   34.431 5.618   1.00 12.48  ? 105 ARG   A CA   1 
ATOM   817  C  C    . ARG   A 1 105 ? 1.141   33.323 6.438   1.00 17.80  ? 105 ARG   A C    1 
ATOM   818  O  O    . ARG   A 1 105 ? 2.354   33.309 6.643   1.00 18.05  ? 105 ARG   A O    1 
ATOM   819  C  CB   . ARG   A 1 105 ? 0.728   34.172 4.120   1.00 14.76  ? 105 ARG   A CB   1 
ATOM   820  C  CG   . ARG   A 1 105 ? -0.065  33.014 3.611   1.00 15.68  ? 105 ARG   A CG   1 
ATOM   821  C  CD   . ARG   A 1 105 ? 0.179   32.915 2.084   1.00 12.81  ? 105 ARG   A CD   1 
ATOM   822  N  NE   . ARG   A 1 105 ? -0.451  31.730 1.505   1.00 18.47  ? 105 ARG   A NE   1 
ATOM   823  C  CZ   . ARG   A 1 105 ? -1.684  31.684 1.011   1.00 16.73  ? 105 ARG   A CZ   1 
ATOM   824  N  NH1  . ARG   A 1 105 ? -2.464  32.754 0.987   1.00 15.61  ? 105 ARG   A NH1  1 
ATOM   825  N  NH2  . ARG   A 1 105 ? -2.152  30.530 0.544   1.00 14.56  ? 105 ARG   A NH2  1 
ATOM   826  N  N    . ILE   A 1 106 ? 0.323   32.396 6.917   1.00 18.07  ? 106 ILE   A N    1 
ATOM   827  C  CA   . ILE   A 1 106 ? 0.816   31.341 7.781   1.00 19.76  ? 106 ILE   A CA   1 
ATOM   828  C  C    . ILE   A 1 106 ? 0.927   30.045 6.986   1.00 17.74  ? 106 ILE   A C    1 
ATOM   829  O  O    . ILE   A 1 106 ? 0.421   29.923 5.864   1.00 17.96  ? 106 ILE   A O    1 
ATOM   830  C  CB   . ILE   A 1 106 ? -0.062  31.169 9.027   1.00 21.42  ? 106 ILE   A CB   1 
ATOM   831  C  CG1  . ILE   A 1 106 ? -1.519  30.988 8.649   1.00 20.19  ? 106 ILE   A CG1  1 
ATOM   832  C  CG2  . ILE   A 1 106 ? 0.157   32.331 10.012  1.00 27.74  ? 106 ILE   A CG2  1 
ATOM   833  C  CD1  . ILE   A 1 106 ? -2.243  29.911 9.448   1.00 34.91  ? 106 ILE   A CD1  1 
ATOM   834  N  N    . GLN   A 1 107 ? 1.582   29.088 7.557   1.00 19.19  ? 107 GLN   A N    1 
ATOM   835  C  CA   . GLN   A 1 107 ? 1.876   27.731 7.120   1.00 20.32  ? 107 GLN   A CA   1 
ATOM   836  C  C    . GLN   A 1 107 ? 0.933   26.724 7.772   1.00 20.99  ? 107 GLN   A C    1 
ATOM   837  O  O    . GLN   A 1 107 ? 0.488   26.915 8.915   1.00 19.79  ? 107 GLN   A O    1 
ATOM   838  C  CB   . GLN   A 1 107 ? 3.318   27.357 7.479   1.00 23.11  ? 107 GLN   A CB   1 
ATOM   839  C  CG   . GLN   A 1 107 ? 4.329   28.191 6.751   1.00 23.62  ? 107 GLN   A CG   1 
ATOM   840  C  CD   . GLN   A 1 107 ? 4.453   27.755 5.313   1.00 28.51  ? 107 GLN   A CD   1 
ATOM   841  O  OE1  . GLN   A 1 107 ? 4.287   26.573 5.011   1.00 27.56  ? 107 GLN   A OE1  1 
ATOM   842  N  NE2  . GLN   A 1 107 ? 4.726   28.704 4.410   1.00 22.59  ? 107 GLN   A NE2  1 
ATOM   843  N  N    . PRO   A 1 108 ? 0.633   25.637 7.072   1.00 18.73  ? 108 PRO   A N    1 
ATOM   844  C  CA   . PRO   A 1 108 ? -0.040  24.512 7.716   1.00 17.64  ? 108 PRO   A CA   1 
ATOM   845  C  C    . PRO   A 1 108 ? 0.703   24.123 8.973   1.00 20.30  ? 108 PRO   A C    1 
ATOM   846  O  O    . PRO   A 1 108 ? 1.936   24.120 9.006   1.00 23.70  ? 108 PRO   A O    1 
ATOM   847  C  CB   . PRO   A 1 108 ? 0.019   23.401 6.657   1.00 22.50  ? 108 PRO   A CB   1 
ATOM   848  C  CG   . PRO   A 1 108 ? 0.121   24.110 5.375   1.00 22.39  ? 108 PRO   A CG   1 
ATOM   849  C  CD   . PRO   A 1 108 ? 0.920   25.373 5.647   1.00 22.18  ? 108 PRO   A CD   1 
ATOM   850  N  N    . GLY   A 1 109 ? -0.070  23.808 10.008  1.00 19.16  ? 109 GLY   A N    1 
ATOM   851  C  CA   . GLY   A 1 109 ? 0.451   23.464 11.312  1.00 20.68  ? 109 GLY   A CA   1 
ATOM   852  C  C    . GLY   A 1 109 ? 0.584   24.626 12.269  1.00 25.17  ? 109 GLY   A C    1 
ATOM   853  O  O    . GLY   A 1 109 ? 0.764   24.396 13.481  1.00 25.82  ? 109 GLY   A O    1 
ATOM   854  N  N    . GLN   A 1 110 ? 0.527   25.866 11.770  1.00 17.35  ? 110 GLN   A N    1 
ATOM   855  C  CA   . GLN   A 1 110 ? 0.553   27.039 12.637  1.00 18.76  ? 110 GLN   A CA   1 
ATOM   856  C  C    . GLN   A 1 110 ? -0.852  27.374 13.139  1.00 17.79  ? 110 GLN   A C    1 
ATOM   857  O  O    . GLN   A 1 110 ? -1.862  27.066 12.504  1.00 18.80  ? 110 GLN   A O    1 
ATOM   858  C  CB   . GLN   A 1 110 ? 1.196   28.259 11.933  1.00 19.87  ? 110 GLN   A CB   1 
ATOM   859  C  CG   . GLN   A 1 110 ? 2.612   27.999 11.358  1.00 25.52  ? 110 GLN   A CG   1 
ATOM   860  C  CD   . GLN   A 1 110 ? 3.360   29.287 10.923  1.00 42.24  ? 110 GLN   A CD   1 
ATOM   861  O  OE1  . GLN   A 1 110 ? 3.082   29.905 9.880   1.00 25.19  ? 110 GLN   A OE1  1 
ATOM   862  N  NE2  . GLN   A 1 110 ? 4.307   29.701 11.754  1.00 60.62  ? 110 GLN   A NE2  1 
ATOM   863  N  N    . THR   A 1 111 ? -0.912  27.963 14.334  1.00 18.99  ? 111 THR   A N    1 
ATOM   864  C  CA   . THR   A 1 111 ? -2.169  28.287 14.991  1.00 15.76  ? 111 THR   A CA   1 
ATOM   865  C  C    . THR   A 1 111 ? -2.415  29.786 14.962  1.00 19.11  ? 111 THR   A C    1 
ATOM   866  O  O    . THR   A 1 111 ? -1.505  30.585 14.712  1.00 19.65  ? 111 THR   A O    1 
ATOM   867  C  CB   . THR   A 1 111 ? -2.147  27.836 16.459  1.00 17.52  ? 111 THR   A CB   1 
ATOM   868  O  OG1  . THR   A 1 111 ? -0.960  28.367 17.035  1.00 21.76  ? 111 THR   A OG1  1 
ATOM   869  C  CG2  . THR   A 1 111 ? -2.140  26.341 16.530  1.00 19.46  ? 111 THR   A CG2  1 
ATOM   870  N  N    . PHE   A 1 112 ? -3.669  30.150 15.221  1.00 16.62  ? 112 PHE   A N    1 
ATOM   871  C  CA   . PHE   A 1 112 ? -4.061  31.547 15.289  1.00 16.76  ? 112 PHE   A CA   1 
ATOM   872  C  C    . PHE   A 1 112 ? -5.397  31.647 16.008  1.00 19.84  ? 112 PHE   A C    1 
ATOM   873  O  O    . PHE   A 1 112 ? -6.143  30.670 16.098  1.00 18.97  ? 112 PHE   A O    1 
ATOM   874  C  CB   . PHE   A 1 112 ? -4.161  32.192 13.887  1.00 15.60  ? 112 PHE   A CB   1 
ATOM   875  C  CG   . PHE   A 1 112 ? -5.096  31.494 12.912  1.00 20.63  ? 112 PHE   A CG   1 
ATOM   876  C  CD1  . PHE   A 1 112 ? -4.661  30.421 12.142  1.00 19.44  ? 112 PHE   A CD1  1 
ATOM   877  C  CD2  . PHE   A 1 112 ? -6.397  31.960 12.719  1.00 15.97  ? 112 PHE   A CD2  1 
ATOM   878  C  CE1  . PHE   A 1 112 ? -5.521  29.807 11.228  1.00 20.55  ? 112 PHE   A CE1  1 
ATOM   879  C  CE2  . PHE   A 1 112 ? -7.260  31.348 11.823  1.00 19.80  ? 112 PHE   A CE2  1 
ATOM   880  C  CZ   . PHE   A 1 112 ? -6.816  30.276 11.056  1.00 20.82  ? 112 PHE   A CZ   1 
ATOM   881  N  N    . SER   A 1 113 ? -5.701  32.852 16.493  1.00 15.06  ? 113 SER   A N    1 
ATOM   882  C  CA   . SER   A 1 113 ? -6.971  33.126 17.133  1.00 17.02  ? 113 SER   A CA   1 
ATOM   883  C  C    . SER   A 1 113 ? -7.972  33.611 16.105  1.00 18.59  ? 113 SER   A C    1 
ATOM   884  O  O    . SER   A 1 113 ? -7.624  34.363 15.201  1.00 17.97  ? 113 SER   A O    1 
ATOM   885  C  CB   . SER   A 1 113 ? -6.773  34.206 18.196  1.00 18.13  ? 113 SER   A CB   1 
ATOM   886  O  OG   . SER   A 1 113 ? -5.870  33.707 19.148  1.00 19.45  ? 113 SER   A OG   1 
ATOM   887  N  N    . VAL   A 1 114 ? -9.233  33.230 16.273  1.00 17.00  ? 114 VAL   A N    1 
ATOM   888  C  CA   . VAL   A 1 114 ? -10.301 33.660 15.377  1.00 15.99  ? 114 VAL   A CA   1 
ATOM   889  C  C    . VAL   A 1 114 ? -11.294 34.464 16.188  1.00 18.95  ? 114 VAL   A C    1 
ATOM   890  O  O    . VAL   A 1 114 ? -11.738 34.003 17.252  1.00 18.82  ? 114 VAL   A O    1 
ATOM   891  C  CB   . VAL   A 1 114 ? -11.003 32.464 14.709  1.00 16.44  ? 114 VAL   A CB   1 
ATOM   892  C  CG1  . VAL   A 1 114 ? -12.283 32.942 14.022  1.00 18.02  ? 114 VAL   A CG1  1 
ATOM   893  C  CG2  . VAL   A 1 114 ? -10.036 31.729 13.776  1.00 17.70  ? 114 VAL   A CG2  1 
ATOM   894  N  N    . LEU   A 1 115 ? -11.632 35.672 15.695  1.00 17.51  ? 115 LEU   A N    1 
ATOM   895  C  CA   . LEU   A 1 115 ? -12.685 36.472 16.320  1.00 18.10  ? 115 LEU   A CA   1 
ATOM   896  C  C    . LEU   A 1 115 ? -13.928 36.340 15.438  1.00 18.72  ? 115 LEU   A C    1 
ATOM   897  O  O    . LEU   A 1 115 ? -14.043 37.001 14.398  1.00 18.55  ? 115 LEU   A O    1 
ATOM   898  C  CB   . LEU   A 1 115 ? -12.257 37.924 16.499  1.00 16.59  ? 115 LEU   A CB   1 
ATOM   899  C  CG   . LEU   A 1 115 ? -13.321 38.845 17.134  1.00 17.64  ? 115 LEU   A CG   1 
ATOM   900  C  CD1  . LEU   A 1 115 ? -13.566 38.402 18.613  1.00 17.11  ? 115 LEU   A CD1  1 
ATOM   901  C  CD2  . LEU   A 1 115 ? -12.932 40.318 17.044  1.00 18.46  ? 115 LEU   A CD2  1 
ATOM   902  N  N    . ALA   A 1 116 ? -14.846 35.453 15.840  1.00 18.22  ? 116 ALA   A N    1 
ATOM   903  C  CA   . ALA   A 1 116 ? -16.085 35.260 15.103  1.00 16.97  ? 116 ALA   A CA   1 
ATOM   904  C  C    . ALA   A 1 116 ? -17.002 36.458 15.307  1.00 21.71  ? 116 ALA   A C    1 
ATOM   905  O  O    . ALA   A 1 116 ? -17.291 36.850 16.453  1.00 24.27  ? 116 ALA   A O    1 
ATOM   906  C  CB   . ALA   A 1 116 ? -16.789 33.971 15.543  1.00 20.90  ? 116 ALA   A CB   1 
ATOM   907  N  N    . CYS   A 1 117 ? -17.468 37.001 14.172  1.00 16.60  ? 117 CYS   A N    1 
ATOM   908  C  CA   A CYS   A 1 117 ? -18.263 38.218 14.142  0.63 20.75  ? 117 CYS   A CA   1 
ATOM   909  C  CA   B CYS   A 1 117 ? -18.218 38.244 14.075  0.37 20.80  ? 117 CYS   A CA   1 
ATOM   910  C  C    . CYS   A 1 117 ? -19.499 38.037 13.276  1.00 23.39  ? 117 CYS   A C    1 
ATOM   911  O  O    . CYS   A 1 117 ? -19.514 37.272 12.309  1.00 22.54  ? 117 CYS   A O    1 
ATOM   912  C  CB   A CYS   A 1 117 ? -17.476 39.406 13.603  0.63 22.42  ? 117 CYS   A CB   1 
ATOM   913  C  CB   B CYS   A 1 117 ? -17.366 39.309 13.382  0.37 22.54  ? 117 CYS   A CB   1 
ATOM   914  S  SG   A CYS   A 1 117 ? -16.052 39.842 14.555  0.63 21.26  ? 117 CYS   A SG   1 
ATOM   915  S  SG   B CYS   A 1 117 ? -17.675 40.988 13.866  0.37 24.88  ? 117 CYS   A SG   1 
ATOM   916  N  N    . TYR   A 1 118 ? -20.549 38.773 13.647  1.00 20.42  ? 118 TYR   A N    1 
ATOM   917  C  CA   . TYR   A 1 118 ? -21.814 38.800 12.920  1.00 23.07  ? 118 TYR   A CA   1 
ATOM   918  C  C    . TYR   A 1 118 ? -22.334 40.227 12.896  1.00 24.48  ? 118 TYR   A C    1 
ATOM   919  O  O    . TYR   A 1 118 ? -22.401 40.881 13.941  1.00 25.13  ? 118 TYR   A O    1 
ATOM   920  C  CB   . TYR   A 1 118 ? -22.843 37.853 13.553  1.00 24.15  ? 118 TYR   A CB   1 
ATOM   921  C  CG   . TYR   A 1 118 ? -22.322 36.444 13.568  1.00 24.25  ? 118 TYR   A CG   1 
ATOM   922  C  CD1  . TYR   A 1 118 ? -22.535 35.601 12.494  1.00 20.57  ? 118 TYR   A CD1  1 
ATOM   923  C  CD2  . TYR   A 1 118 ? -21.539 35.982 14.630  1.00 18.42  ? 118 TYR   A CD2  1 
ATOM   924  C  CE1  . TYR   A 1 118 ? -22.021 34.318 12.473  1.00 20.26  ? 118 TYR   A CE1  1 
ATOM   925  C  CE2  . TYR   A 1 118 ? -21.005 34.708 14.617  1.00 20.45  ? 118 TYR   A CE2  1 
ATOM   926  C  CZ   . TYR   A 1 118 ? -21.256 33.878 13.527  1.00 21.53  ? 118 TYR   A CZ   1 
ATOM   927  O  OH   . TYR   A 1 118 ? -20.741 32.605 13.490  1.00 21.23  ? 118 TYR   A OH   1 
ATOM   928  N  N    . ASN   A 1 119 ? -22.674 40.712 11.702  1.00 26.60  ? 119 ASN   A N    1 
ATOM   929  C  CA   . ASN   A 1 119 ? -23.186 42.072 11.528  1.00 30.60  ? 119 ASN   A CA   1 
ATOM   930  C  C    . ASN   A 1 119 ? -22.218 43.106 12.110  1.00 26.97  ? 119 ASN   A C    1 
ATOM   931  O  O    . ASN   A 1 119 ? -22.619 44.114 12.693  1.00 26.41  ? 119 ASN   A O    1 
ATOM   932  C  CB   . ASN   A 1 119 ? -24.570 42.198 12.154  1.00 31.65  ? 119 ASN   A CB   1 
ATOM   933  C  CG   . ASN   A 1 119 ? -25.581 41.290 11.480  1.00 36.08  ? 119 ASN   A CG   1 
ATOM   934  O  OD1  . ASN   A 1 119 ? -25.823 41.391 10.275  1.00 41.13  ? 119 ASN   A OD1  1 
ATOM   935  N  ND2  . ASN   A 1 119 ? -26.148 40.371 12.252  1.00 39.02  ? 119 ASN   A ND2  1 
ATOM   936  N  N    . GLY   A 1 120 ? -20.922 42.857 11.938  1.00 24.85  ? 120 GLY   A N    1 
ATOM   937  C  CA   . GLY   A 1 120 ? -19.893 43.738 12.450  1.00 25.23  ? 120 GLY   A CA   1 
ATOM   938  C  C    . GLY   A 1 120 ? -19.698 43.675 13.947  1.00 28.36  ? 120 GLY   A C    1 
ATOM   939  O  O    . GLY   A 1 120 ? -18.870 44.429 14.481  1.00 29.17  ? 120 GLY   A O    1 
ATOM   940  N  N    . SER   A 1 121 ? -20.412 42.786 14.633  1.00 21.72  ? 121 SER   A N    1 
ATOM   941  C  CA   . SER   A 1 121 ? -20.341 42.678 16.092  1.00 20.13  ? 121 SER   A CA   1 
ATOM   942  C  C    . SER   A 1 121 ? -19.614 41.409 16.520  1.00 24.33  ? 121 SER   A C    1 
ATOM   943  O  O    . SER   A 1 121 ? -20.092 40.297 16.231  1.00 25.59  ? 121 SER   A O    1 
ATOM   944  C  CB   . SER   A 1 121 ? -21.748 42.702 16.684  1.00 32.01  ? 121 SER   A CB   1 
ATOM   945  O  OG   . SER   A 1 121 ? -22.270 44.017 16.690  1.00 45.57  ? 121 SER   A OG   1 
ATOM   946  N  N    . PRO   A 1 122 ? -18.495 41.512 17.237  1.00 25.92  ? 122 PRO   A N    1 
ATOM   947  C  CA   . PRO   A 1 122 ? -17.798 40.295 17.677  1.00 24.74  ? 122 PRO   A CA   1 
ATOM   948  C  C    . PRO   A 1 122 ? -18.649 39.463 18.623  1.00 26.14  ? 122 PRO   A C    1 
ATOM   949  O  O    . PRO   A 1 122 ? -19.297 39.983 19.543  1.00 24.53  ? 122 PRO   A O    1 
ATOM   950  C  CB   . PRO   A 1 122 ? -16.535 40.828 18.363  1.00 24.60  ? 122 PRO   A CB   1 
ATOM   951  C  CG   . PRO   A 1 122 ? -16.357 42.244 17.772  1.00 28.55  ? 122 PRO   A CG   1 
ATOM   952  C  CD   . PRO   A 1 122 ? -17.734 42.743 17.519  1.00 24.49  ? 122 PRO   A CD   1 
ATOM   953  N  N    . SER   A 1 123 ? -18.647 38.153 18.389  1.00 23.93  ? 123 SER   A N    1 
ATOM   954  C  CA   . SER   A 1 123 ? -19.417 37.244 19.225  1.00 25.91  ? 123 SER   A CA   1 
ATOM   955  C  C    . SER   A 1 123 ? -18.578 36.282 20.051  1.00 23.01  ? 123 SER   A C    1 
ATOM   956  O  O    . SER   A 1 123 ? -19.005 35.911 21.156  1.00 22.41  ? 123 SER   A O    1 
ATOM   957  C  CB   . SER   A 1 123 ? -20.382 36.416 18.376  1.00 28.06  ? 123 SER   A CB   1 
ATOM   958  O  OG   . SER   A 1 123 ? -19.636 35.503 17.614  1.00 37.68  ? 123 SER   A OG   1 
ATOM   959  N  N    . GLY   A 1 124 ? -17.420 35.842 19.550  1.00 17.82  ? 124 GLY   A N    1 
ATOM   960  C  CA   . GLY   A 1 124 ? -16.633 34.893 20.327  1.00 20.54  ? 124 GLY   A CA   1 
ATOM   961  C  C    . GLY   A 1 124 ? -15.219 34.786 19.807  1.00 23.04  ? 124 GLY   A C    1 
ATOM   962  O  O    . GLY   A 1 124 ? -14.935 35.210 18.688  1.00 18.69  ? 124 GLY   A O    1 
ATOM   963  N  N    . VAL   A 1 125 ? -14.332 34.204 20.615  1.00 18.83  ? 125 VAL   A N    1 
ATOM   964  C  CA   . VAL   A 1 125 ? -12.933 34.043 20.227  1.00 17.95  ? 125 VAL   A CA   1 
ATOM   965  C  C    . VAL   A 1 125 ? -12.470 32.620 20.530  1.00 20.52  ? 125 VAL   A C    1 
ATOM   966  O  O    . VAL   A 1 125 ? -12.783 32.059 21.586  1.00 20.40  ? 125 VAL   A O    1 
ATOM   967  C  CB   . VAL   A 1 125 ? -12.037 35.097 20.917  1.00 20.70  ? 125 VAL   A CB   1 
ATOM   968  C  CG1  . VAL   A 1 125 ? -12.041 34.904 22.426  1.00 23.38  ? 125 VAL   A CG1  1 
ATOM   969  C  CG2  . VAL   A 1 125 ? -10.633 35.061 20.356  1.00 20.67  ? 125 VAL   A CG2  1 
ATOM   970  N  N    . TYR   A 1 126 ? -11.726 32.027 19.599  1.00 17.98  ? 126 TYR   A N    1 
ATOM   971  C  CA   . TYR   A 1 126 ? -11.221 30.666 19.810  1.00 19.75  ? 126 TYR   A CA   1 
ATOM   972  C  C    . TYR   A 1 126 ? -9.944  30.455 19.017  1.00 20.27  ? 126 TYR   A C    1 
ATOM   973  O  O    . TYR   A 1 126 ? -9.621  31.227 18.114  1.00 20.59  ? 126 TYR   A O    1 
ATOM   974  C  CB   . TYR   A 1 126 ? -12.274 29.609 19.446  1.00 17.09  ? 126 TYR   A CB   1 
ATOM   975  C  CG   . TYR   A 1 126 ? -12.787 29.727 18.021  1.00 18.57  ? 126 TYR   A CG   1 
ATOM   976  C  CD1  . TYR   A 1 126 ? -12.165 29.072 16.995  1.00 21.11  ? 126 TYR   A CD1  1 
ATOM   977  C  CD2  . TYR   A 1 126 ? -13.930 30.473 17.745  1.00 19.60  ? 126 TYR   A CD2  1 
ATOM   978  C  CE1  . TYR   A 1 126 ? -12.662 29.186 15.684  1.00 19.13  ? 126 TYR   A CE1  1 
ATOM   979  C  CE2  . TYR   A 1 126 ? -14.435 30.584 16.464  1.00 22.70  ? 126 TYR   A CE2  1 
ATOM   980  C  CZ   . TYR   A 1 126 ? -13.804 29.942 15.452  1.00 20.52  ? 126 TYR   A CZ   1 
ATOM   981  O  OH   . TYR   A 1 126 ? -14.336 30.072 14.186  1.00 25.37  ? 126 TYR   A OH   1 
ATOM   982  N  N    . GLN   A 1 127 ? -9.235  29.372 19.330  1.00 19.91  ? 127 GLN   A N    1 
ATOM   983  C  CA   . GLN   A 1 127 ? -8.006  28.991 18.632  1.00 20.17  ? 127 GLN   A CA   1 
ATOM   984  C  C    . GLN   A 1 127 ? -8.292  27.990 17.528  1.00 26.02  ? 127 GLN   A C    1 
ATOM   985  O  O    . GLN   A 1 127 ? -9.086  27.061 17.718  1.00 24.49  ? 127 GLN   A O    1 
ATOM   986  C  CB   . GLN   A 1 127 ? -6.986  28.339 19.569  1.00 28.06  ? 127 GLN   A CB   1 
ATOM   987  C  CG   . GLN   A 1 127 ? -6.206  29.242 20.403  1.00 28.04  ? 127 GLN   A CG   1 
ATOM   988  C  CD   . GLN   A 1 127 ? -5.297  30.140 19.591  1.00 22.46  ? 127 GLN   A CD   1 
ATOM   989  O  OE1  . GLN   A 1 127 ? -5.663  31.266 19.315  1.00 28.03  ? 127 GLN   A OE1  1 
ATOM   990  N  NE2  . GLN   A 1 127 ? -4.102  29.662 19.237  1.00 23.50  ? 127 GLN   A NE2  1 
ATOM   991  N  N    . CYS   A 1 128 ? -7.579  28.158 16.404  1.00 22.72  ? 128 CYS   A N    1 
ATOM   992  C  CA   . CYS   A 1 128 ? -7.651  27.353 15.191  1.00 22.73  ? 128 CYS   A CA   1 
ATOM   993  C  C    . CYS   A 1 128 ? -6.227  27.007 14.781  1.00 23.14  ? 128 CYS   A C    1 
ATOM   994  O  O    . CYS   A 1 128 ? -5.275  27.675 15.182  1.00 22.44  ? 128 CYS   A O    1 
ATOM   995  C  CB   . CYS   A 1 128 ? -8.335  28.108 14.003  1.00 20.87  ? 128 CYS   A CB   1 
ATOM   996  S  SG   . CYS   A 1 128 ? -10.056 27.713 13.938  1.00 39.74  ? 128 CYS   A SG   1 
ATOM   997  N  N    . ALA   A 1 129 ? -6.087  25.964 13.964  1.00 25.44  ? 129 ALA   A N    1 
ATOM   998  C  CA   . ALA   A 1 129 ? -4.826  25.673 13.300  1.00 18.41  ? 129 ALA   A CA   1 
ATOM   999  C  C    . ALA   A 1 129 ? -5.091  25.574 11.808  1.00 19.54  ? 129 ALA   A C    1 
ATOM   1000 O  O    . ALA   A 1 129 ? -6.164  25.130 11.382  1.00 19.65  ? 129 ALA   A O    1 
ATOM   1001 C  CB   . ALA   A 1 129 ? -4.181  24.359 13.777  1.00 22.69  ? 129 ALA   A CB   1 
ATOM   1002 N  N    . MET   A 1 130 ? -4.100  25.948 11.019  1.00 17.00  ? 130 MET   A N    1 
ATOM   1003 C  CA   . MET   A 1 130 ? -4.254  25.796 9.579   1.00 16.57  ? 130 MET   A CA   1 
ATOM   1004 C  C    . MET   A 1 130 ? -3.905  24.333 9.289   1.00 18.57  ? 130 MET   A C    1 
ATOM   1005 O  O    . MET   A 1 130 ? -2.824  23.862 9.681   1.00 21.27  ? 130 MET   A O    1 
ATOM   1006 C  CB   . MET   A 1 130 ? -3.319  26.753 8.829   1.00 16.45  ? 130 MET   A CB   1 
ATOM   1007 C  CG   . MET   A 1 130 ? -3.194  26.380 7.341   1.00 23.72  ? 130 MET   A CG   1 
ATOM   1008 S  SD   . MET   A 1 130 ? -4.674  26.989 6.474   1.00 23.20  ? 130 MET   A SD   1 
ATOM   1009 C  CE   . MET   A 1 130 ? -5.104  28.613 7.134   1.00 18.43  ? 130 MET   A CE   1 
ATOM   1010 N  N    . ARG   A 1 131 ? -4.810  23.591 8.657   1.00 18.17  ? 131 ARG   A N    1 
ATOM   1011 C  CA   . ARG   A 1 131 ? -4.526  22.187 8.393   1.00 19.16  ? 131 ARG   A CA   1 
ATOM   1012 C  C    . ARG   A 1 131 ? -3.598  22.039 7.174   1.00 20.45  ? 131 ARG   A C    1 
ATOM   1013 O  O    . ARG   A 1 131 ? -3.404  22.963 6.373   1.00 20.34  ? 131 ARG   A O    1 
ATOM   1014 C  CB   . ARG   A 1 131 ? -5.823  21.424 8.128   1.00 20.27  ? 131 ARG   A CB   1 
ATOM   1015 C  CG   . ARG   A 1 131 ? -6.899  21.495 9.207   1.00 20.43  ? 131 ARG   A CG   1 
ATOM   1016 C  CD   . ARG   A 1 131 ? -6.508  21.016 10.598  1.00 22.10  ? 131 ARG   A CD   1 
ATOM   1017 N  NE   . ARG   A 1 131 ? -5.836  19.726 10.566  1.00 20.98  ? 131 ARG   A NE   1 
ATOM   1018 C  CZ   . ARG   A 1 131 ? -5.227  19.197 11.618  1.00 24.24  ? 131 ARG   A CZ   1 
ATOM   1019 N  NH1  . ARG   A 1 131 ? -5.246  19.806 12.800  1.00 22.47  ? 131 ARG   A NH1  1 
ATOM   1020 N  NH2  . ARG   A 1 131 ? -4.630  18.014 11.495  1.00 23.73  ? 131 ARG   A NH2  1 
ATOM   1021 N  N    . HIS   A 1 132 ? -3.042  20.824 7.037   1.00 21.31  ? 132 HIS   A N    1 
ATOM   1022 C  CA   . HIS   A 1 132 ? -2.212  20.458 5.884   1.00 20.56  ? 132 HIS   A CA   1 
ATOM   1023 C  C    . HIS   A 1 132 ? -2.940  20.666 4.565   1.00 21.19  ? 132 HIS   A C    1 
ATOM   1024 O  O    . HIS   A 1 132 ? -2.301  20.954 3.552   1.00 21.62  ? 132 HIS   A O    1 
ATOM   1025 C  CB   . HIS   A 1 132 ? -1.769  18.995 6.018   1.00 24.61  ? 132 HIS   A CB   1 
ATOM   1026 C  CG   . HIS   A 1 132 ? -1.047  18.463 4.816   1.00 37.94  ? 132 HIS   A CG   1 
ATOM   1027 N  ND1  . HIS   A 1 132 ? 0.224   18.867 4.469   1.00 39.59  ? 132 HIS   A ND1  1 
ATOM   1028 C  CD2  . HIS   A 1 132 ? -1.432  17.575 3.865   1.00 41.96  ? 132 HIS   A CD2  1 
ATOM   1029 C  CE1  . HIS   A 1 132 ? 0.599   18.244 3.365   1.00 42.16  ? 132 HIS   A CE1  1 
ATOM   1030 N  NE2  . HIS   A 1 132 ? -0.391  17.459 2.974   1.00 43.15  ? 132 HIS   A NE2  1 
ATOM   1031 N  N    . ASN   A 1 133 ? -4.259  20.485 4.546   1.00 19.12  ? 133 ASN   A N    1 
ATOM   1032 C  CA   . ASN   A 1 133 ? -5.044  20.695 3.336   1.00 20.90  ? 133 ASN   A CA   1 
ATOM   1033 C  C    . ASN   A 1 133 ? -5.570  22.123 3.222   1.00 22.09  ? 133 ASN   A C    1 
ATOM   1034 O  O    . ASN   A 1 133 ? -6.462  22.385 2.403   1.00 20.90  ? 133 ASN   A O    1 
ATOM   1035 C  CB   . ASN   A 1 133 ? -6.171  19.664 3.287   1.00 18.50  ? 133 ASN   A CB   1 
ATOM   1036 C  CG   . ASN   A 1 133 ? -7.245  19.896 4.338   1.00 21.88  ? 133 ASN   A CG   1 
ATOM   1037 O  OD1  . ASN   A 1 133 ? -7.177  20.833 5.140   1.00 19.93  ? 133 ASN   A OD1  1 
ATOM   1038 N  ND2  . ASN   A 1 133 ? -8.211  18.993 4.378   1.00 22.37  ? 133 ASN   A ND2  1 
ATOM   1039 N  N    . PHE   A 1 134 ? -5.039  23.044 4.036   1.00 17.02  ? 134 PHE   A N    1 
ATOM   1040 C  CA   . PHE   A 1 134 ? -5.319  24.474 3.945   1.00 17.44  ? 134 PHE   A CA   1 
ATOM   1041 C  C    . PHE   A 1 134 ? -6.749  24.828 4.312   1.00 20.59  ? 134 PHE   A C    1 
ATOM   1042 O  O    . PHE   A 1 134 ? -7.243  25.887 3.914   1.00 24.42  ? 134 PHE   A O    1 
ATOM   1043 C  CB   . PHE   A 1 134 ? -5.011  24.990 2.533   1.00 17.87  ? 134 PHE   A CB   1 
ATOM   1044 C  CG   . PHE   A 1 134 ? -3.550  25.084 2.242   1.00 18.55  ? 134 PHE   A CG   1 
ATOM   1045 C  CD1  . PHE   A 1 134 ? -2.779  26.048 2.876   1.00 18.53  ? 134 PHE   A CD1  1 
ATOM   1046 C  CD2  . PHE   A 1 134 ? -2.926  24.146 1.420   1.00 22.80  ? 134 PHE   A CD2  1 
ATOM   1047 C  CE1  . PHE   A 1 134 ? -1.390  26.144 2.636   1.00 23.48  ? 134 PHE   A CE1  1 
ATOM   1048 C  CE2  . PHE   A 1 134 ? -1.533  24.211 1.187   1.00 23.50  ? 134 PHE   A CE2  1 
ATOM   1049 C  CZ   . PHE   A 1 134 ? -0.770  25.220 1.799   1.00 23.50  ? 134 PHE   A CZ   1 
ATOM   1050 N  N    . THR   A 1 135 ? -7.446  23.962 5.037   1.00 19.02  ? 135 THR   A N    1 
ATOM   1051 C  CA   . THR   A 1 135 ? -8.703  24.336 5.660   1.00 14.83  ? 135 THR   A CA   1 
ATOM   1052 C  C    . THR   A 1 135 ? -8.462  24.592 7.136   1.00 16.68  ? 135 THR   A C    1 
ATOM   1053 O  O    . THR   A 1 135 ? -7.402  24.274 7.676   1.00 18.98  ? 135 THR   A O    1 
ATOM   1054 C  CB   . THR   A 1 135 ? -9.753  23.236 5.498   1.00 16.50  ? 135 THR   A CB   1 
ATOM   1055 O  OG1  . THR   A 1 135 ? -9.332  22.070 6.220   1.00 20.69  ? 135 THR   A OG1  1 
ATOM   1056 C  CG2  . THR   A 1 135 ? -9.937  22.886 4.040   1.00 19.83  ? 135 THR   A CG2  1 
ATOM   1057 N  N    . ILE   A 1 136 ? -9.460  25.164 7.786   1.00 15.31  ? 136 ILE   A N    1 
ATOM   1058 C  CA   . ILE   A 1 136 ? -9.434  25.248 9.247   1.00 13.67  ? 136 ILE   A CA   1 
ATOM   1059 C  C    . ILE   A 1 136 ? -10.725 24.650 9.786   1.00 18.98  ? 136 ILE   A C    1 
ATOM   1060 O  O    . ILE   A 1 136 ? -11.772 24.703 9.144   1.00 19.92  ? 136 ILE   A O    1 
ATOM   1061 C  CB   . ILE   A 1 136 ? -9.207  26.704 9.734   1.00 18.54  ? 136 ILE   A CB   1 
ATOM   1062 C  CG1  . ILE   A 1 136 ? -10.346 27.640 9.355   1.00 21.05  ? 136 ILE   A CG1  1 
ATOM   1063 C  CG2  . ILE   A 1 136 ? -7.925  27.268 9.150   1.00 23.06  ? 136 ILE   A CG2  1 
ATOM   1064 C  CD1  . ILE   A 1 136 ? -10.530 28.826 10.289  1.00 20.48  ? 136 ILE   A CD1  1 
ATOM   1065 N  N    . LYS   A 1 137 ? -10.641 24.031 10.966  1.00 18.30  ? 137 LYS   A N    1 
ATOM   1066 C  CA   . LYS   A 1 137 ? -11.848 23.504 11.600  1.00 22.10  ? 137 LYS   A CA   1 
ATOM   1067 C  C    . LYS   A 1 137 ? -12.353 24.559 12.565  1.00 21.33  ? 137 LYS   A C    1 
ATOM   1068 O  O    . LYS   A 1 137 ? -12.057 24.543 13.761  1.00 23.22  ? 137 LYS   A O    1 
ATOM   1069 C  CB   . LYS   A 1 137 ? -11.589 22.161 12.270  1.00 21.50  ? 137 LYS   A CB   1 
ATOM   1070 C  CG   . LYS   A 1 137 ? -10.591 21.280 11.536  1.00 30.62  ? 137 LYS   A CG   1 
ATOM   1071 C  CD   . LYS   A 1 137 ? -10.097 20.116 12.406  1.00 35.01  ? 137 LYS   A CD   1 
ATOM   1072 C  CE   . LYS   A 1 137 ? -9.824  18.854 11.578  1.00 43.47  ? 137 LYS   A CE   1 
ATOM   1073 N  NZ   . LYS   A 1 137 ? -9.144  17.787 12.402  1.00 44.79  ? 137 LYS   A NZ   1 
ATOM   1074 N  N    . GLY   A 1 138 ? -13.130 25.494 12.032  1.00 20.40  ? 138 GLY   A N    1 
ATOM   1075 C  CA   . GLY   A 1 138 ? -13.598 26.625 12.800  1.00 19.20  ? 138 GLY   A CA   1 
ATOM   1076 C  C    . GLY   A 1 138 ? -14.982 26.396 13.370  1.00 20.32  ? 138 GLY   A C    1 
ATOM   1077 O  O    . GLY   A 1 138 ? -15.532 25.291 13.353  1.00 20.33  ? 138 GLY   A O    1 
ATOM   1078 N  N    . SER   A 1 139 ? -15.552 27.482 13.880  1.00 16.02  ? 139 SER   A N    1 
ATOM   1079 C  CA   . SER   A 1 139 ? -16.944 27.494 14.328  1.00 16.36  ? 139 SER   A CA   1 
ATOM   1080 C  C    . SER   A 1 139 ? -17.533 28.782 13.779  1.00 21.10  ? 139 SER   A C    1 
ATOM   1081 O  O    . SER   A 1 139 ? -17.265 29.873 14.293  1.00 20.05  ? 139 SER   A O    1 
ATOM   1082 C  CB   . SER   A 1 139 ? -17.061 27.405 15.851  1.00 20.04  ? 139 SER   A CB   1 
ATOM   1083 O  OG   . SER   A 1 139 ? -18.426 27.456 16.257  1.00 23.35  ? 139 SER   A OG   1 
ATOM   1084 N  N    . PHE   A 1 140 ? -18.293 28.640 12.699  1.00 19.79  ? 140 PHE   A N    1 
ATOM   1085 C  CA   . PHE   A 1 140 ? -18.830 29.766 11.965  1.00 20.41  ? 140 PHE   A CA   1 
ATOM   1086 C  C    . PHE   A 1 140 ? -20.254 29.462 11.534  1.00 25.01  ? 140 PHE   A C    1 
ATOM   1087 O  O    . PHE   A 1 140 ? -20.530 28.363 11.056  1.00 25.03  ? 140 PHE   A O    1 
ATOM   1088 C  CB   . PHE   A 1 140 ? -18.012 30.052 10.701  1.00 19.68  ? 140 PHE   A CB   1 
ATOM   1089 C  CG   . PHE   A 1 140 ? -16.611 30.525 10.948  1.00 18.40  ? 140 PHE   A CG   1 
ATOM   1090 C  CD1  . PHE   A 1 140 ? -16.373 31.796 11.455  1.00 20.16  ? 140 PHE   A CD1  1 
ATOM   1091 C  CD2  . PHE   A 1 140 ? -15.535 29.763 10.531  1.00 17.77  ? 140 PHE   A CD2  1 
ATOM   1092 C  CE1  . PHE   A 1 140 ? -15.055 32.283 11.601  1.00 18.58  ? 140 PHE   A CE1  1 
ATOM   1093 C  CE2  . PHE   A 1 140 ? -14.236 30.232 10.673  1.00 19.54  ? 140 PHE   A CE2  1 
ATOM   1094 C  CZ   . PHE   A 1 140 ? -14.003 31.514 11.206  1.00 17.24  ? 140 PHE   A CZ   1 
ATOM   1095 N  N    . LEU   A 1 141 ? -21.145 30.432 11.686  1.00 24.12  ? 141 LEU   A N    1 
ATOM   1096 C  CA   . LEU   A 1 141 ? -22.505 30.324 11.174  1.00 24.96  ? 141 LEU   A CA   1 
ATOM   1097 C  C    . LEU   A 1 141 ? -22.700 31.295 10.023  1.00 23.68  ? 141 LEU   A C    1 
ATOM   1098 O  O    . LEU   A 1 141 ? -21.802 32.057 9.661   1.00 21.09  ? 141 LEU   A O    1 
ATOM   1099 C  CB   . LEU   A 1 141 ? -23.530 30.595 12.273  1.00 24.77  ? 141 LEU   A CB   1 
ATOM   1100 C  CG   . LEU   A 1 141 ? -23.398 29.798 13.558  1.00 28.45  ? 141 LEU   A CG   1 
ATOM   1101 C  CD1  . LEU   A 1 141 ? -24.401 30.292 14.585  1.00 34.39  ? 141 LEU   A CD1  1 
ATOM   1102 C  CD2  . LEU   A 1 141 ? -23.687 28.341 13.224  1.00 29.26  ? 141 LEU   A CD2  1 
ATOM   1103 N  N    . ASN   A 1 142 ? -23.912 31.286 9.467   1.00 25.33  ? 142 ASN   A N    1 
ATOM   1104 C  CA   . ASN   A 1 142 ? -24.219 32.225 8.405   1.00 24.89  ? 142 ASN   A CA   1 
ATOM   1105 C  C    . ASN   A 1 142 ? -24.024 33.646 8.916   1.00 22.35  ? 142 ASN   A C    1 
ATOM   1106 O  O    . ASN   A 1 142 ? -24.394 33.975 10.051  1.00 24.58  ? 142 ASN   A O    1 
ATOM   1107 C  CB   . ASN   A 1 142 ? -25.653 32.015 7.907   1.00 26.94  ? 142 ASN   A CB   1 
ATOM   1108 C  CG   . ASN   A 1 142 ? -25.744 30.878 6.913   1.00 38.08  ? 142 ASN   A CG   1 
ATOM   1109 O  OD1  . ASN   A 1 142 ? -25.247 30.978 5.791   1.00 39.16  ? 142 ASN   A OD1  1 
ATOM   1110 N  ND2  . ASN   A 1 142 ? -26.395 29.791 7.314   1.00 47.14  ? 142 ASN   A ND2  1 
ATOM   1111 N  N    . GLY   A 1 143 ? -23.399 34.479 8.090   1.00 25.87  ? 143 GLY   A N    1 
ATOM   1112 C  CA   . GLY   A 1 143 ? -23.105 35.847 8.459   1.00 23.04  ? 143 GLY   A CA   1 
ATOM   1113 C  C    . GLY   A 1 143 ? -21.714 36.067 9.004   1.00 22.64  ? 143 GLY   A C    1 
ATOM   1114 O  O    . GLY   A 1 143 ? -21.365 37.212 9.312   1.00 22.63  ? 143 GLY   A O    1 
ATOM   1115 N  N    . SER   A 1 144 ? -20.906 35.010 9.122   1.00 19.46  ? 144 SER   A N    1 
ATOM   1116 C  CA   . SER   A 1 144 ? -19.580 35.108 9.723   1.00 21.16  ? 144 SER   A CA   1 
ATOM   1117 C  C    . SER   A 1 144 ? -18.511 35.530 8.728   1.00 18.88  ? 144 SER   A C    1 
ATOM   1118 O  O    . SER   A 1 144 ? -17.368 35.781 9.135   1.00 18.42  ? 144 SER   A O    1 
ATOM   1119 C  CB   . SER   A 1 144 ? -19.171 33.759 10.342  1.00 19.38  ? 144 SER   A CB   1 
ATOM   1120 O  OG   . SER   A 1 144 ? -19.145 32.747 9.344   1.00 24.08  ? 144 SER   A OG   1 
ATOM   1121 N  N    . CYS   A 1 145 ? -18.856 35.635 7.438   1.00 19.24  ? 145 CYS   A N    1 
ATOM   1122 C  CA   . CYS   A 1 145 ? -17.866 35.958 6.431   1.00 18.46  ? 145 CYS   A CA   1 
ATOM   1123 C  C    . CYS   A 1 145 ? -17.203 37.293 6.752   1.00 17.17  ? 145 CYS   A C    1 
ATOM   1124 O  O    . CYS   A 1 145 ? -17.854 38.246 7.184   1.00 19.21  ? 145 CYS   A O    1 
ATOM   1125 C  CB   . CYS   A 1 145 ? -18.550 36.003 5.061   1.00 18.88  ? 145 CYS   A CB   1 
ATOM   1126 S  SG   . CYS   A 1 145 ? -19.249 34.387 4.659   1.00 21.23  ? 145 CYS   A SG   1 
ATOM   1127 N  N    . GLY   A 1 146 ? -15.900 37.375 6.523   1.00 16.33  ? 146 GLY   A N    1 
ATOM   1128 C  CA   . GLY   A 1 146 ? -15.149 38.554 6.894   1.00 16.30  ? 146 GLY   A CA   1 
ATOM   1129 C  C    . GLY   A 1 146 ? -14.582 38.528 8.303   1.00 16.56  ? 146 GLY   A C    1 
ATOM   1130 O  O    . GLY   A 1 146 ? -13.762 39.391 8.635   1.00 18.75  ? 146 GLY   A O    1 
ATOM   1131 N  N    . SER   A 1 147 ? -14.965 37.561 9.127   1.00 18.21  ? 147 SER   A N    1 
ATOM   1132 C  CA   . SER   A 1 147 ? -14.289 37.396 10.418  1.00 16.05  ? 147 SER   A CA   1 
ATOM   1133 C  C    . SER   A 1 147 ? -12.805 37.120 10.168  1.00 18.32  ? 147 SER   A C    1 
ATOM   1134 O  O    . SER   A 1 147 ? -12.435 36.536 9.144   1.00 18.86  ? 147 SER   A O    1 
ATOM   1135 C  CB   . SER   A 1 147 ? -14.893 36.227 11.200  1.00 17.07  ? 147 SER   A CB   1 
ATOM   1136 O  OG   . SER   A 1 147 ? -16.266 36.460 11.506  1.00 19.91  ? 147 SER   A OG   1 
ATOM   1137 N  N    . VAL   A 1 148 ? -11.940 37.548 11.084  1.00 15.93  ? 148 VAL   A N    1 
ATOM   1138 C  CA   . VAL   A 1 148 ? -10.503 37.401 10.855  1.00 14.09  ? 148 VAL   A CA   1 
ATOM   1139 C  C    . VAL   A 1 148 ? -9.813  36.527 11.906  1.00 15.79  ? 148 VAL   A C    1 
ATOM   1140 O  O    . VAL   A 1 148 ? -10.251 36.391 13.061  1.00 18.01  ? 148 VAL   A O    1 
ATOM   1141 C  CB   . VAL   A 1 148 ? -9.777  38.762 10.746  1.00 16.73  ? 148 VAL   A CB   1 
ATOM   1142 C  CG1  . VAL   A 1 148 ? -10.279 39.549 9.523   1.00 18.87  ? 148 VAL   A CG1  1 
ATOM   1143 C  CG2  . VAL   A 1 148 ? -9.886  39.565 12.023  1.00 16.87  ? 148 VAL   A CG2  1 
ATOM   1144 N  N    . GLY   A 1 149 ? -8.678  35.964 11.473  1.00 16.10  ? 149 GLY   A N    1 
ATOM   1145 C  CA   . GLY   A 1 149 ? -7.772  35.213 12.327  1.00 15.92  ? 149 GLY   A CA   1 
ATOM   1146 C  C    . GLY   A 1 149 ? -6.463  35.971 12.477  1.00 18.58  ? 149 GLY   A C    1 
ATOM   1147 O  O    . GLY   A 1 149 ? -6.025  36.672 11.566  1.00 19.09  ? 149 GLY   A O    1 
ATOM   1148 N  N    . PHE   A 1 150 ? -5.840  35.851 13.650  1.00 13.14  ? 150 PHE   A N    1 
ATOM   1149 C  CA   . PHE   A 1 150 ? -4.687  36.698 13.933  1.00 15.22  ? 150 PHE   A CA   1 
ATOM   1150 C  C    . PHE   A 1 150 ? -3.828  36.082 15.029  1.00 19.70  ? 150 PHE   A C    1 
ATOM   1151 O  O    . PHE   A 1 150 ? -4.262  35.191 15.752  1.00 17.96  ? 150 PHE   A O    1 
ATOM   1152 C  CB   . PHE   A 1 150 ? -5.161  38.089 14.376  1.00 18.69  ? 150 PHE   A CB   1 
ATOM   1153 C  CG   . PHE   A 1 150 ? -6.027  38.041 15.584  1.00 19.13  ? 150 PHE   A CG   1 
ATOM   1154 C  CD1  . PHE   A 1 150 ? -7.385  37.730 15.470  1.00 24.35  ? 150 PHE   A CD1  1 
ATOM   1155 C  CD2  . PHE   A 1 150 ? -5.494  38.256 16.850  1.00 18.20  ? 150 PHE   A CD2  1 
ATOM   1156 C  CE1  . PHE   A 1 150 ? -8.200  37.639 16.616  1.00 22.95  ? 150 PHE   A CE1  1 
ATOM   1157 C  CE2  . PHE   A 1 150 ? -6.304  38.187 17.996  1.00 22.37  ? 150 PHE   A CE2  1 
ATOM   1158 C  CZ   . PHE   A 1 150 ? -7.665  37.877 17.874  1.00 25.15  ? 150 PHE   A CZ   1 
ATOM   1159 N  N    . ASN   A 1 151 ? -2.600  36.580 15.131  1.00 16.59  ? 151 ASN   A N    1 
ATOM   1160 C  CA   . ASN   A 1 151 ? -1.728  36.345 16.282  1.00 17.10  ? 151 ASN   A CA   1 
ATOM   1161 C  C    . ASN   A 1 151 ? -1.291  37.701 16.810  1.00 21.62  ? 151 ASN   A C    1 
ATOM   1162 O  O    . ASN   A 1 151 ? -1.367  38.703 16.103  1.00 21.05  ? 151 ASN   A O    1 
ATOM   1163 C  CB   . ASN   A 1 151 ? -0.512  35.485 15.912  1.00 19.09  ? 151 ASN   A CB   1 
ATOM   1164 C  CG   . ASN   A 1 151 ? -0.862  34.020 15.763  1.00 23.51  ? 151 ASN   A CG   1 
ATOM   1165 O  OD1  . ASN   A 1 151 ? -1.074  33.320 16.747  1.00 26.07  ? 151 ASN   A OD1  1 
ATOM   1166 N  ND2  . ASN   A 1 151 ? -1.007  33.564 14.522  1.00 18.97  ? 151 ASN   A ND2  1 
ATOM   1167 N  N    . ILE   A 1 152 ? -0.880  37.726 18.071  1.00 17.86  ? 152 ILE   A N    1 
ATOM   1168 C  CA   . ILE   A 1 152 ? -0.426  39.007 18.675  1.00 22.80  ? 152 ILE   A CA   1 
ATOM   1169 C  C    . ILE   A 1 152 ? 0.972   38.833 19.269  1.00 27.54  ? 152 ILE   A C    1 
ATOM   1170 O  O    . ILE   A 1 152 ? 1.201   37.864 19.973  1.00 26.46  ? 152 ILE   A O    1 
ATOM   1171 C  CB   . ILE   A 1 152 ? -1.428  39.564 19.706  1.00 23.01  ? 152 ILE   A CB   1 
ATOM   1172 C  CG1  . ILE   A 1 152 ? -2.828  39.722 19.115  1.00 25.02  ? 152 ILE   A CG1  1 
ATOM   1173 C  CG2  . ILE   A 1 152 ? -0.915  40.879 20.267  1.00 29.32  ? 152 ILE   A CG2  1 
ATOM   1174 C  CD1  . ILE   A 1 152 ? -3.744  40.570 19.956  1.00 27.28  ? 152 ILE   A CD1  1 
ATOM   1175 N  N    . ASP   A 1 153 ? 1.861   39.753 18.918  1.00 28.90  ? 153 ASP   A N    1 
ATOM   1176 C  CA   . ASP   A 1 153 ? 3.248   39.713 19.432  1.00 35.69  ? 153 ASP   A CA   1 
ATOM   1177 C  C    . ASP   A 1 153 ? 3.636   41.138 19.806  1.00 38.40  ? 153 ASP   A C    1 
ATOM   1178 O  O    . ASP   A 1 153 ? 3.713   41.977 18.914  1.00 38.69  ? 153 ASP   A O    1 
ATOM   1179 C  CB   . ASP   A 1 153 ? 4.192   39.107 18.402  1.00 45.29  ? 153 ASP   A CB   1 
ATOM   1180 C  CG   . ASP   A 1 153 ? 5.639   39.085 18.857  1.00 63.56  ? 153 ASP   A CG   1 
ATOM   1181 O  OD1  . ASP   A 1 153 ? 5.898   38.545 19.946  1.00 60.18  ? 153 ASP   A OD1  1 
ATOM   1182 O  OD2  . ASP   A 1 153 ? 6.493   39.611 18.116  1.00 70.08  ? 153 ASP   A OD2  1 
ATOM   1183 N  N    . TYR   A 1 154 ? 3.780   41.394 21.099  1.00 43.81  ? 154 TYR   A N    1 
ATOM   1184 C  CA   . TYR   A 1 154 ? 4.225   42.733 21.545  1.00 48.95  ? 154 TYR   A CA   1 
ATOM   1185 C  C    . TYR   A 1 154 ? 3.329   43.820 20.949  1.00 41.16  ? 154 TYR   A C    1 
ATOM   1186 O  O    . TYR   A 1 154 ? 3.847   44.695 20.257  1.00 43.64  ? 154 TYR   A O    1 
ATOM   1187 C  CB   . TYR   A 1 154 ? 5.691   42.905 21.164  1.00 58.14  ? 154 TYR   A CB   1 
ATOM   1188 C  CG   . TYR   A 1 154 ? 6.604   41.897 21.807  1.00 74.92  ? 154 TYR   A CG   1 
ATOM   1189 C  CD1  . TYR   A 1 154 ? 6.627   41.735 23.181  1.00 79.53  ? 154 TYR   A CD1  1 
ATOM   1190 C  CD2  . TYR   A 1 154 ? 7.436   41.098 21.044  1.00 82.19  ? 154 TYR   A CD2  1 
ATOM   1191 C  CE1  . TYR   A 1 154 ? 7.461   40.809 23.785  1.00 82.80  ? 154 TYR   A CE1  1 
ATOM   1192 C  CE2  . TYR   A 1 154 ? 8.273   40.165 21.630  1.00 87.94  ? 154 TYR   A CE2  1 
ATOM   1193 C  CZ   . TYR   A 1 154 ? 8.286   40.021 23.005  1.00 90.01  ? 154 TYR   A CZ   1 
ATOM   1194 O  OH   . TYR   A 1 154 ? 9.111   39.105 23.588  1.00 97.79  ? 154 TYR   A OH   1 
ATOM   1195 N  N    . ASP   A 1 155 ? 2.029   43.733 21.200  1.00 37.30  ? 155 ASP   A N    1 
ATOM   1196 C  CA   . ASP   A 1 155 ? 1.075   44.789 20.757  1.00 43.34  ? 155 ASP   A CA   1 
ATOM   1197 C  C    . ASP   A 1 155 ? 0.949   44.876 19.230  1.00 30.83  ? 155 ASP   A C    1 
ATOM   1198 O  O    . ASP   A 1 155 ? 0.191   45.722 18.780  1.00 33.96  ? 155 ASP   A O    1 
ATOM   1199 C  CB   . ASP   A 1 155 ? 1.414   46.129 21.416  1.00 44.94  ? 155 ASP   A CB   1 
ATOM   1200 C  CG   . ASP   A 1 155 ? 1.059   46.159 22.892  1.00 54.73  ? 155 ASP   A CG   1 
ATOM   1201 O  OD1  . ASP   A 1 155 ? 0.182   45.376 23.299  1.00 55.99  ? 155 ASP   A OD1  1 
ATOM   1202 O  OD2  . ASP   A 1 155 ? 1.670   46.954 23.622  1.00 63.72  ? 155 ASP   A OD2  1 
ATOM   1203 N  N    . CYS   A 1 156 ? 1.664   44.036 18.490  1.00 25.94  ? 156 CYS   A N    1 
ATOM   1204 C  CA   . CYS   A 1 156 ? 1.479   44.005 17.035  1.00 22.89  ? 156 CYS   A CA   1 
ATOM   1205 C  C    . CYS   A 1 156 ? 0.561   42.856 16.657  1.00 24.20  ? 156 CYS   A C    1 
ATOM   1206 O  O    . CYS   A 1 156 ? 0.874   41.694 16.946  1.00 22.74  ? 156 CYS   A O    1 
ATOM   1207 C  CB   . CYS   A 1 156 ? 2.801   43.826 16.304  1.00 23.12  ? 156 CYS   A CB   1 
ATOM   1208 S  SG   . CYS   A 1 156 ? 2.588   43.901 14.498  1.00 28.77  ? 156 CYS   A SG   1 
ATOM   1209 N  N    . VAL   A 1 157 ? -0.545  43.177 15.985  1.00 23.09  ? 157 VAL   A N    1 
ATOM   1210 C  CA   . VAL   A 1 157 ? -1.491  42.166 15.525  1.00 18.82  ? 157 VAL   A CA   1 
ATOM   1211 C  C    . VAL   A 1 157 ? -1.048  41.724 14.132  1.00 21.85  ? 157 VAL   A C    1 
ATOM   1212 O  O    . VAL   A 1 157 ? -1.046  42.529 13.201  1.00 20.87  ? 157 VAL   A O    1 
ATOM   1213 C  CB   . VAL   A 1 157 ? -2.922  42.724 15.479  1.00 19.30  ? 157 VAL   A CB   1 
ATOM   1214 C  CG1  . VAL   A 1 157 ? -3.912  41.668 14.985  1.00 19.39  ? 157 VAL   A CG1  1 
ATOM   1215 C  CG2  . VAL   A 1 157 ? -3.330  43.324 16.845  1.00 23.19  ? 157 VAL   A CG2  1 
ATOM   1216 N  N    . SER   A 1 158 ? -0.659  40.460 13.983  1.00 19.17  ? 158 SER   A N    1 
ATOM   1217 C  CA   . SER   A 1 158 ? -0.403  39.895 12.658  1.00 18.78  ? 158 SER   A CA   1 
ATOM   1218 C  C    . SER   A 1 158 ? -1.670  39.205 12.190  1.00 20.03  ? 158 SER   A C    1 
ATOM   1219 O  O    . SER   A 1 158 ? -2.013  38.123 12.668  1.00 17.29  ? 158 SER   A O    1 
ATOM   1220 C  CB   . SER   A 1 158 ? 0.778   38.939 12.670  1.00 19.86  ? 158 SER   A CB   1 
ATOM   1221 O  OG   . SER   A 1 158 ? 1.955   39.620 13.055  1.00 25.54  ? 158 SER   A OG   1 
ATOM   1222 N  N    . PHE   A 1 159 ? -2.384  39.854 11.270  1.00 17.56  ? 159 PHE   A N    1 
ATOM   1223 C  CA   . PHE   A 1 159 ? -3.575  39.256 10.674  1.00 16.46  ? 159 PHE   A CA   1 
ATOM   1224 C  C    . PHE   A 1 159 ? -3.157  38.198 9.669   1.00 16.52  ? 159 PHE   A C    1 
ATOM   1225 O  O    . PHE   A 1 159 ? -2.326  38.468 8.792   1.00 17.93  ? 159 PHE   A O    1 
ATOM   1226 C  CB   . PHE   A 1 159 ? -4.436  40.318 9.982   1.00 18.87  ? 159 PHE   A CB   1 
ATOM   1227 C  CG   . PHE   A 1 159 ? -5.036  41.325 10.927  1.00 16.47  ? 159 PHE   A CG   1 
ATOM   1228 C  CD1  . PHE   A 1 159 ? -6.182  41.001 11.665  1.00 18.30  ? 159 PHE   A CD1  1 
ATOM   1229 C  CD2  . PHE   A 1 159 ? -4.471  42.590 11.070  1.00 17.73  ? 159 PHE   A CD2  1 
ATOM   1230 C  CE1  . PHE   A 1 159 ? -6.755  41.922 12.569  1.00 16.92  ? 159 PHE   A CE1  1 
ATOM   1231 C  CE2  . PHE   A 1 159 ? -5.046  43.526 11.957  1.00 17.66  ? 159 PHE   A CE2  1 
ATOM   1232 C  CZ   . PHE   A 1 159 ? -6.183  43.190 12.688  1.00 19.20  ? 159 PHE   A CZ   1 
ATOM   1233 N  N    . CYS   A 1 160 ? -3.732  36.992 9.774   1.00 15.92  ? 160 CYS   A N    1 
ATOM   1234 C  CA   . CYS   A 1 160 ? -3.363  35.936 8.831   1.00 17.37  ? 160 CYS   A CA   1 
ATOM   1235 C  C    . CYS   A 1 160 ? -4.509  35.271 8.078   1.00 18.73  ? 160 CYS   A C    1 
ATOM   1236 O  O    . CYS   A 1 160 ? -4.226  34.513 7.145   1.00 18.01  ? 160 CYS   A O    1 
ATOM   1237 C  CB   . CYS   A 1 160 ? -2.535  34.845 9.529   1.00 16.33  ? 160 CYS   A CB   1 
ATOM   1238 S  SG   . CYS   A 1 160 ? -3.421  34.092 10.951  1.00 19.90  ? 160 CYS   A SG   1 
ATOM   1239 N  N    . TYR   A 1 161 ? -5.768  35.537 8.417   1.00 15.82  ? 161 TYR   A N    1 
ATOM   1240 C  CA   . TYR   A 1 161 ? -6.890  34.790 7.862   1.00 14.71  ? 161 TYR   A CA   1 
ATOM   1241 C  C    . TYR   A 1 161 ? -8.090  35.721 7.773   1.00 16.66  ? 161 TYR   A C    1 
ATOM   1242 O  O    . TYR   A 1 161 ? -8.335  36.494 8.714   1.00 17.08  ? 161 TYR   A O    1 
ATOM   1243 C  CB   . TYR   A 1 161 ? -7.252  33.580 8.730   1.00 16.19  ? 161 TYR   A CB   1 
ATOM   1244 C  CG   . TYR   A 1 161 ? -8.425  32.738 8.217   1.00 15.01  ? 161 TYR   A CG   1 
ATOM   1245 C  CD1  . TYR   A 1 161 ? -8.253  31.814 7.192   1.00 13.44  ? 161 TYR   A CD1  1 
ATOM   1246 C  CD2  . TYR   A 1 161 ? -9.709  32.881 8.769   1.00 16.10  ? 161 TYR   A CD2  1 
ATOM   1247 C  CE1  . TYR   A 1 161 ? -9.319  31.044 6.716   1.00 13.74  ? 161 TYR   A CE1  1 
ATOM   1248 C  CE2  . TYR   A 1 161 ? -10.781 32.123 8.301   1.00 16.02  ? 161 TYR   A CE2  1 
ATOM   1249 C  CZ   . TYR   A 1 161 ? -10.573 31.206 7.261   1.00 14.91  ? 161 TYR   A CZ   1 
ATOM   1250 O  OH   . TYR   A 1 161 ? -11.615 30.445 6.799   1.00 19.26  ? 161 TYR   A OH   1 
ATOM   1251 N  N    . MET   A 1 162 ? -8.817  35.684 6.643   1.00 14.94  ? 162 MET   A N    1 
ATOM   1252 C  CA   . MET   A 1 162 ? -10.156 36.255 6.663   1.00 14.25  ? 162 MET   A CA   1 
ATOM   1253 C  C    . MET   A 1 162 ? -11.095 35.181 6.102   1.00 15.80  ? 162 MET   A C    1 
ATOM   1254 O  O    . MET   A 1 162 ? -10.800 34.515 5.088   1.00 14.95  ? 162 MET   A O    1 
ATOM   1255 C  CB   . MET   A 1 162 ? -10.260 37.633 5.930   1.00 20.19  ? 162 MET   A CB   1 
ATOM   1256 C  CG   . MET   A 1 162 ? -11.625 38.004 5.456   1.00 14.62  ? 162 MET   A CG   1 
ATOM   1257 S  SD   . MET   A 1 162 ? -11.653 39.692 4.696   1.00 22.86  ? 162 MET   A SD   1 
ATOM   1258 C  CE   . MET   A 1 162 ? -11.557 40.735 6.167   1.00 24.75  ? 162 MET   A CE   1 
ATOM   1259 N  N    . HIS   A 1 163 ? -12.207 34.979 6.804   1.00 14.96  ? 163 HIS   A N    1 
ATOM   1260 C  CA   . HIS   A 1 163 ? -13.068 33.832 6.551   1.00 15.24  ? 163 HIS   A CA   1 
ATOM   1261 C  C    . HIS   A 1 163 ? -13.938 34.078 5.320   1.00 15.41  ? 163 HIS   A C    1 
ATOM   1262 O  O    . HIS   A 1 163 ? -14.535 35.153 5.198   1.00 16.89  ? 163 HIS   A O    1 
ATOM   1263 C  CB   . HIS   A 1 163 ? -13.966 33.564 7.756   1.00 17.49  ? 163 HIS   A CB   1 
ATOM   1264 C  CG   . HIS   A 1 163 ? -14.842 32.368 7.563   1.00 17.45  ? 163 HIS   A CG   1 
ATOM   1265 N  ND1  . HIS   A 1 163 ? -14.346 31.161 7.116   1.00 14.97  ? 163 HIS   A ND1  1 
ATOM   1266 C  CD2  . HIS   A 1 163 ? -16.180 32.202 7.703   1.00 17.83  ? 163 HIS   A CD2  1 
ATOM   1267 C  CE1  . HIS   A 1 163 ? -15.344 30.301 6.986   1.00 13.54  ? 163 HIS   A CE1  1 
ATOM   1268 N  NE2  . HIS   A 1 163 ? -16.468 30.911 7.326   1.00 17.96  ? 163 HIS   A NE2  1 
ATOM   1269 N  N    . HIS   A 1 164 ? -14.038 33.076 4.418   1.00 17.74  ? 164 HIS   A N    1 
ATOM   1270 C  CA   . HIS   A 1 164 ? -14.904 33.227 3.258   1.00 18.07  ? 164 HIS   A CA   1 
ATOM   1271 C  C    . HIS   A 1 164 ? -16.049 32.226 3.253   1.00 19.14  ? 164 HIS   A C    1 
ATOM   1272 O  O    . HIS   A 1 164 ? -17.208 32.619 3.081   1.00 22.87  ? 164 HIS   A O    1 
ATOM   1273 C  CB   . HIS   A 1 164 ? -14.071 33.071 1.969   1.00 15.91  ? 164 HIS   A CB   1 
ATOM   1274 C  CG   . HIS   A 1 164 ? -13.297 34.300 1.644   1.00 16.52  ? 164 HIS   A CG   1 
ATOM   1275 N  ND1  . HIS   A 1 164 ? -13.516 35.085 0.528   1.00 17.60  ? 164 HIS   A ND1  1 
ATOM   1276 C  CD2  . HIS   A 1 164 ? -12.293 34.893 2.337   1.00 15.60  ? 164 HIS   A CD2  1 
ATOM   1277 C  CE1  . HIS   A 1 164 ? -12.644 36.079 0.528   1.00 16.54  ? 164 HIS   A CE1  1 
ATOM   1278 N  NE2  . HIS   A 1 164 ? -11.895 35.991 1.614   1.00 16.63  ? 164 HIS   A NE2  1 
ATOM   1279 N  N    . MET   A 1 165 ? -15.778 30.934 3.419   1.00 17.45  ? 165 MET   A N    1 
ATOM   1280 C  CA   . MET   A 1 165 ? -16.859 29.991 3.165   1.00 19.00  ? 165 MET   A CA   1 
ATOM   1281 C  C    . MET   A 1 165 ? -16.694 28.694 3.928   1.00 19.95  ? 165 MET   A C    1 
ATOM   1282 O  O    . MET   A 1 165 ? -15.613 28.350 4.413   1.00 18.45  ? 165 MET   A O    1 
ATOM   1283 C  CB   . MET   A 1 165 ? -16.985 29.642 1.677   1.00 25.60  ? 165 MET   A CB   1 
ATOM   1284 C  CG   . MET   A 1 165 ? -15.695 29.369 1.009   1.00 22.61  ? 165 MET   A CG   1 
ATOM   1285 S  SD   . MET   A 1 165 ? -15.808 29.342 -0.814  1.00 27.35  ? 165 MET   A SD   1 
ATOM   1286 C  CE   . MET   A 1 165 ? -14.469 28.174 -1.067  1.00 27.69  ? 165 MET   A CE   1 
ATOM   1287 N  N    . GLU   A 1 166 ? -17.794 27.951 3.983   1.00 19.34  ? 166 GLU   A N    1 
ATOM   1288 C  CA   . GLU   A 1 166 ? -17.799 26.617 4.563   1.00 20.75  ? 166 GLU   A CA   1 
ATOM   1289 C  C    . GLU   A 1 166 ? -17.907 25.591 3.440   1.00 26.34  ? 166 GLU   A C    1 
ATOM   1290 O  O    . GLU   A 1 166 ? -18.731 25.749 2.529   1.00 26.30  ? 166 GLU   A O    1 
ATOM   1291 C  CB   . GLU   A 1 166 ? -18.943 26.447 5.555   1.00 22.83  ? 166 GLU   A CB   1 
ATOM   1292 C  CG   . GLU   A 1 166 ? -19.054 25.012 6.088   1.00 24.64  ? 166 GLU   A CG   1 
ATOM   1293 C  CD   . GLU   A 1 166 ? -19.914 24.922 7.326   1.00 24.86  ? 166 GLU   A CD   1 
ATOM   1294 O  OE1  . GLU   A 1 166 ? -19.748 25.753 8.252   1.00 23.66  ? 166 GLU   A OE1  1 
ATOM   1295 O  OE2  . GLU   A 1 166 ? -20.835 24.067 7.323   1.00 27.43  ? 166 GLU   A OE2  1 
ATOM   1296 N  N    . LEU   A 1 167 ? -17.058 24.564 3.498   1.00 22.16  ? 167 LEU   A N    1 
ATOM   1297 C  CA   . LEU   A 1 167 ? -17.097 23.472 2.528   1.00 25.75  ? 167 LEU   A CA   1 
ATOM   1298 C  C    . LEU   A 1 167 ? -18.100 22.409 2.945   1.00 26.52  ? 167 LEU   A C    1 
ATOM   1299 O  O    . LEU   A 1 167 ? -18.621 22.422 4.058   1.00 27.01  ? 167 LEU   A O    1 
ATOM   1300 C  CB   . LEU   A 1 167 ? -15.703 22.877 2.341   1.00 23.40  ? 167 LEU   A CB   1 
ATOM   1301 C  CG   . LEU   A 1 167 ? -14.643 23.943 2.046   1.00 27.04  ? 167 LEU   A CG   1 
ATOM   1302 C  CD1  . LEU   A 1 167 ? -13.217 23.394 2.148   1.00 30.04  ? 167 LEU   A CD1  1 
ATOM   1303 C  CD2  . LEU   A 1 167 ? -14.886 24.555 0.671   1.00 30.36  ? 167 LEU   A CD2  1 
ATOM   1304 N  N    . PRO   A 1 168 ? -18.415 21.476 2.046   1.00 27.96  ? 168 PRO   A N    1 
ATOM   1305 C  CA   . PRO   A 1 168 ? -19.463 20.492 2.361   1.00 25.65  ? 168 PRO   A CA   1 
ATOM   1306 C  C    . PRO   A 1 168 ? -19.173 19.642 3.585   1.00 29.25  ? 168 PRO   A C    1 
ATOM   1307 O  O    . PRO   A 1 168 ? -20.125 19.201 4.239   1.00 32.44  ? 168 PRO   A O    1 
ATOM   1308 C  CB   . PRO   A 1 168 ? -19.527 19.642 1.080   1.00 25.91  ? 168 PRO   A CB   1 
ATOM   1309 C  CG   . PRO   A 1 168 ? -19.135 20.583 0.010   1.00 29.51  ? 168 PRO   A CG   1 
ATOM   1310 C  CD   . PRO   A 1 168 ? -18.051 21.452 0.617   1.00 32.51  ? 168 PRO   A CD   1 
ATOM   1311 N  N    . THR   A 1 169 ? -17.901 19.381 3.912   1.00 28.92  ? 169 THR   A N    1 
ATOM   1312 C  CA   . THR   A 1 169 ? -17.554 18.623 5.108   1.00 28.02  ? 169 THR   A CA   1 
ATOM   1313 C  C    . THR   A 1 169 ? -17.665 19.451 6.383   1.00 28.21  ? 169 THR   A C    1 
ATOM   1314 O  O    . THR   A 1 169 ? -17.397 18.930 7.474   1.00 31.21  ? 169 THR   A O    1 
ATOM   1315 C  CB   . THR   A 1 169 ? -16.137 18.037 4.984   1.00 31.49  ? 169 THR   A CB   1 
ATOM   1316 O  OG1  . THR   A 1 169 ? -15.202 19.079 4.657   1.00 31.01  ? 169 THR   A OG1  1 
ATOM   1317 C  CG2  . THR   A 1 169 ? -16.092 16.945 3.902   1.00 32.74  ? 169 THR   A CG2  1 
ATOM   1318 N  N    . GLY   A 1 170 ? -18.060 20.716 6.282   1.00 25.29  ? 170 GLY   A N    1 
ATOM   1319 C  CA   . GLY   A 1 170 ? -18.216 21.533 7.469   1.00 25.06  ? 170 GLY   A CA   1 
ATOM   1320 C  C    . GLY   A 1 170 ? -16.945 22.184 7.968   1.00 26.32  ? 170 GLY   A C    1 
ATOM   1321 O  O    . GLY   A 1 170 ? -16.941 22.738 9.077   1.00 28.09  ? 170 GLY   A O    1 
ATOM   1322 N  N    . VAL   A 1 171 ? -15.861 22.123 7.199   1.00 25.40  ? 171 VAL   A N    1 
ATOM   1323 C  CA   . VAL   A 1 171 ? -14.645 22.847 7.548   1.00 20.93  ? 171 VAL   A CA   1 
ATOM   1324 C  C    . VAL   A 1 171 ? -14.629 24.126 6.715   1.00 21.20  ? 171 VAL   A C    1 
ATOM   1325 O  O    . VAL   A 1 171 ? -15.493 24.345 5.856   1.00 21.77  ? 171 VAL   A O    1 
ATOM   1326 C  CB   . VAL   A 1 171 ? -13.375 22.004 7.314   1.00 19.83  ? 171 VAL   A CB   1 
ATOM   1327 C  CG1  . VAL   A 1 171 ? -13.472 20.677 8.058   1.00 26.27  ? 171 VAL   A CG1  1 
ATOM   1328 C  CG2  . VAL   A 1 171 ? -13.181 21.748 5.822   1.00 21.71  ? 171 VAL   A CG2  1 
ATOM   1329 N  N    . HIS   A 1 172 ? -13.642 24.970 6.946   1.00 18.53  ? 172 HIS   A N    1 
ATOM   1330 C  CA   . HIS   A 1 172 ? -13.700 26.362 6.531   1.00 16.83  ? 172 HIS   A CA   1 
ATOM   1331 C  C    . HIS   A 1 172 ? -12.521 26.765 5.662   1.00 17.20  ? 172 HIS   A C    1 
ATOM   1332 O  O    . HIS   A 1 172 ? -11.399 26.266 5.829   1.00 15.98  ? 172 HIS   A O    1 
ATOM   1333 C  CB   . HIS   A 1 172 ? -13.819 27.235 7.794   1.00 17.01  ? 172 HIS   A CB   1 
ATOM   1334 C  CG   . HIS   A 1 172 ? -15.038 26.893 8.590   1.00 18.43  ? 172 HIS   A CG   1 
ATOM   1335 N  ND1  . HIS   A 1 172 ? -15.012 26.167 9.772   1.00 19.29  ? 172 HIS   A ND1  1 
ATOM   1336 C  CD2  . HIS   A 1 172 ? -16.346 27.087 8.295   1.00 18.15  ? 172 HIS   A CD2  1 
ATOM   1337 C  CE1  . HIS   A 1 172 ? -16.253 25.987 10.196  1.00 20.10  ? 172 HIS   A CE1  1 
ATOM   1338 N  NE2  . HIS   A 1 172 ? -17.082 26.520 9.313   1.00 21.01  ? 172 HIS   A NE2  1 
ATOM   1339 N  N    . ALA   A 1 173 ? -12.806 27.646 4.693   1.00 15.85  ? 173 ALA   A N    1 
ATOM   1340 C  CA   . ALA   A 1 173 ? -11.810 28.143 3.760   1.00 14.98  ? 173 ALA   A CA   1 
ATOM   1341 C  C    . ALA   A 1 173 ? -11.816 29.663 3.705   1.00 13.30  ? 173 ALA   A C    1 
ATOM   1342 O  O    . ALA   A 1 173 ? -12.856 30.323 3.828   1.00 16.32  ? 173 ALA   A O    1 
ATOM   1343 C  CB   . ALA   A 1 173 ? -12.066 27.616 2.314   1.00 15.57  ? 173 ALA   A CB   1 
ATOM   1344 N  N    . GLY   A 1 174 ? -10.641 30.221 3.532   1.00 14.19  ? 174 GLY   A N    1 
ATOM   1345 C  CA   . GLY   A 1 174 ? -10.549 31.655 3.450   1.00 16.33  ? 174 GLY   A CA   1 
ATOM   1346 C  C    . GLY   A 1 174 ? -9.237  32.075 2.880   1.00 15.30  ? 174 GLY   A C    1 
ATOM   1347 O  O    . GLY   A 1 174 ? -8.478  31.252 2.366   1.00 15.99  ? 174 GLY   A O    1 
ATOM   1348 N  N    . THR   A 1 175 ? -8.948  33.362 3.024   1.00 14.69  ? 175 THR   A N    1 
ATOM   1349 C  CA   . THR   A 1 175 ? -7.789  33.969 2.369   1.00 14.76  ? 175 THR   A CA   1 
ATOM   1350 C  C    . THR   A 1 175 ? -6.845  34.587 3.383   1.00 16.26  ? 175 THR   A C    1 
ATOM   1351 O  O    . THR   A 1 175 ? -7.177  34.745 4.567   1.00 17.03  ? 175 THR   A O    1 
ATOM   1352 C  CB   . THR   A 1 175 ? -8.230  35.072 1.380   1.00 14.18  ? 175 THR   A CB   1 
ATOM   1353 O  OG1  . THR   A 1 175 ? -8.795  36.172 2.124   1.00 15.93  ? 175 THR   A OG1  1 
ATOM   1354 C  CG2  . THR   A 1 175 ? -9.252  34.527 0.380   1.00 16.02  ? 175 THR   A CG2  1 
ATOM   1355 N  N    . ASP   A 1 176 ? -5.644  34.946 2.918   1.00 14.89  ? 176 ASP   A N    1 
ATOM   1356 C  CA   . ASP   A 1 176 ? -4.841  35.852 3.722   1.00 17.36  ? 176 ASP   A CA   1 
ATOM   1357 C  C    . ASP   A 1 176 ? -5.429  37.250 3.507   1.00 18.85  ? 176 ASP   A C    1 
ATOM   1358 O  O    . ASP   A 1 176 ? -6.396  37.424 2.759   1.00 17.70  ? 176 ASP   A O    1 
ATOM   1359 C  CB   . ASP   A 1 176 ? -3.343  35.772 3.372   1.00 16.06  ? 176 ASP   A CB   1 
ATOM   1360 C  CG   . ASP   A 1 176 ? -3.016  36.083 1.924   1.00 19.38  ? 176 ASP   A CG   1 
ATOM   1361 O  OD1  . ASP   A 1 176 ? -3.751  36.846 1.269   1.00 17.21  ? 176 ASP   A OD1  1 
ATOM   1362 O  OD2  . ASP   A 1 176 ? -1.943  35.602 1.466   1.00 21.67  ? 176 ASP   A OD2  1 
ATOM   1363 N  N    . LEU   A 1 177 ? -4.868  38.258 4.166   1.00 16.19  ? 177 LEU   A N    1 
ATOM   1364 C  CA   . LEU   A 1 177 ? -5.442  39.596 4.066   1.00 15.67  ? 177 LEU   A CA   1 
ATOM   1365 C  C    . LEU   A 1 177 ? -5.042  40.304 2.783   1.00 17.14  ? 177 LEU   A C    1 
ATOM   1366 O  O    . LEU   A 1 177 ? -5.483  41.437 2.558   1.00 19.50  ? 177 LEU   A O    1 
ATOM   1367 C  CB   . LEU   A 1 177 ? -5.035  40.443 5.285   1.00 17.86  ? 177 LEU   A CB   1 
ATOM   1368 C  CG   . LEU   A 1 177 ? -6.023  40.348 6.461   1.00 18.15  ? 177 LEU   A CG   1 
ATOM   1369 C  CD1  . LEU   A 1 177 ? -7.368  40.974 6.113   1.00 18.32  ? 177 LEU   A CD1  1 
ATOM   1370 C  CD2  . LEU   A 1 177 ? -6.228  38.876 6.963   1.00 19.23  ? 177 LEU   A CD2  1 
ATOM   1371 N  N    . GLU   A 1 178 ? -4.183  39.682 1.973   1.00 17.31  ? 178 GLU   A N    1 
ATOM   1372 C  CA   . GLU   A 1 178 ? -3.942  40.135 0.610   1.00 20.35  ? 178 GLU   A CA   1 
ATOM   1373 C  C    . GLU   A 1 178 ? -4.985  39.583 -0.351  1.00 21.16  ? 178 GLU   A C    1 
ATOM   1374 O  O    . GLU   A 1 178 ? -4.894  39.857 -1.551  1.00 19.09  ? 178 GLU   A O    1 
ATOM   1375 C  CB   . GLU   A 1 178 ? -2.567  39.664 0.111   1.00 19.96  ? 178 GLU   A CB   1 
ATOM   1376 C  CG   . GLU   A 1 178 ? -1.304  40.064 0.912   1.00 26.50  ? 178 GLU   A CG   1 
ATOM   1377 C  CD   . GLU   A 1 178 ? -1.179  41.520 1.260   1.00 28.98  ? 178 GLU   A CD   1 
ATOM   1378 O  OE1  . GLU   A 1 178 ? -1.787  42.359 0.568   1.00 31.33  ? 178 GLU   A OE1  1 
ATOM   1379 O  OE2  . GLU   A 1 178 ? -0.370  41.842 2.170   1.00 30.76  ? 178 GLU   A OE2  1 
ATOM   1380 N  N    . GLY   A 1 179 ? -5.925  38.761 0.121   1.00 18.28  ? 179 GLY   A N    1 
ATOM   1381 C  CA   . GLY   A 1 179 ? -6.980  38.221 -0.723  1.00 19.78  ? 179 GLY   A CA   1 
ATOM   1382 C  C    . GLY   A 1 179 ? -6.655  36.909 -1.404  1.00 18.99  ? 179 GLY   A C    1 
ATOM   1383 O  O    . GLY   A 1 179 ? -7.438  36.459 -2.263  1.00 18.30  ? 179 GLY   A O    1 
ATOM   1384 N  N    . ASN   A 1 180 ? -5.529  36.276 -1.057  1.00 17.84  ? 180 ASN   A N    1 
ATOM   1385 C  CA   . ASN   A 1 180 ? -5.102  35.055 -1.733  1.00 14.06  ? 180 ASN   A CA   1 
ATOM   1386 C  C    . ASN   A 1 180 ? -5.564  33.861 -0.911  1.00 15.69  ? 180 ASN   A C    1 
ATOM   1387 O  O    . ASN   A 1 180 ? -5.227  33.757 0.284   1.00 16.03  ? 180 ASN   A O    1 
ATOM   1388 C  CB   . ASN   A 1 180 ? -3.585  35.035 -1.922  1.00 15.55  ? 180 ASN   A CB   1 
ATOM   1389 C  CG   . ASN   A 1 180 ? -3.084  36.253 -2.688  1.00 18.34  ? 180 ASN   A CG   1 
ATOM   1390 O  OD1  . ASN   A 1 180 ? -2.380  37.122 -2.144  1.00 22.00  ? 180 ASN   A OD1  1 
ATOM   1391 N  ND2  . ASN   A 1 180 ? -3.441  36.318 -3.943  1.00 17.00  ? 180 ASN   A ND2  1 
ATOM   1392 N  N    . PHE   A 1 181 ? -6.341  32.970 -1.535  1.00 17.09  ? 181 PHE   A N    1 
ATOM   1393 C  CA   . PHE   A 1 181 ? -6.885  31.832 -0.786  1.00 16.80  ? 181 PHE   A CA   1 
ATOM   1394 C  C    . PHE   A 1 181 ? -5.791  30.950 -0.200  1.00 16.68  ? 181 PHE   A C    1 
ATOM   1395 O  O    . PHE   A 1 181 ? -4.728  30.726 -0.796  1.00 15.45  ? 181 PHE   A O    1 
ATOM   1396 C  CB   . PHE   A 1 181 ? -7.798  30.975 -1.685  1.00 15.45  ? 181 PHE   A CB   1 
ATOM   1397 C  CG   . PHE   A 1 181 ? -9.269  31.249 -1.488  1.00 16.15  ? 181 PHE   A CG   1 
ATOM   1398 C  CD1  . PHE   A 1 181 ? -9.969  30.620 -0.441  1.00 18.19  ? 181 PHE   A CD1  1 
ATOM   1399 C  CD2  . PHE   A 1 181 ? -9.920  32.192 -2.262  1.00 15.93  ? 181 PHE   A CD2  1 
ATOM   1400 C  CE1  . PHE   A 1 181 ? -11.316 30.884 -0.231  1.00 16.88  ? 181 PHE   A CE1  1 
ATOM   1401 C  CE2  . PHE   A 1 181 ? -11.275 32.478 -2.051  1.00 17.51  ? 181 PHE   A CE2  1 
ATOM   1402 C  CZ   . PHE   A 1 181 ? -11.974 31.827 -1.028  1.00 20.61  ? 181 PHE   A CZ   1 
ATOM   1403 N  N    . TYR   A 1 182 ? -6.045  30.447 1.008   1.00 13.99  ? 182 TYR   A N    1 
ATOM   1404 C  CA   . TYR   A 1 182 ? -5.334  29.274 1.475   1.00 12.72  ? 182 TYR   A CA   1 
ATOM   1405 C  C    . TYR   A 1 182 ? -5.913  28.049 0.804   1.00 15.53  ? 182 TYR   A C    1 
ATOM   1406 O  O    . TYR   A 1 182 ? -7.111  27.785 0.945   1.00 18.10  ? 182 TYR   A O    1 
ATOM   1407 C  CB   . TYR   A 1 182 ? -5.455  29.127 2.986   1.00 12.84  ? 182 TYR   A CB   1 
ATOM   1408 C  CG   . TYR   A 1 182 ? -4.708  30.179 3.750   1.00 15.11  ? 182 TYR   A CG   1 
ATOM   1409 C  CD1  . TYR   A 1 182 ? -3.342  30.021 3.980   1.00 17.60  ? 182 TYR   A CD1  1 
ATOM   1410 C  CD2  . TYR   A 1 182 ? -5.353  31.296 4.276   1.00 15.52  ? 182 TYR   A CD2  1 
ATOM   1411 C  CE1  . TYR   A 1 182 ? -2.610  30.965 4.720   1.00 14.67  ? 182 TYR   A CE1  1 
ATOM   1412 C  CE2  . TYR   A 1 182 ? -4.629  32.254 5.015   1.00 13.51  ? 182 TYR   A CE2  1 
ATOM   1413 C  CZ   . TYR   A 1 182 ? -3.270  32.074 5.210   1.00 14.35  ? 182 TYR   A CZ   1 
ATOM   1414 O  OH   . TYR   A 1 182 ? -2.554  32.981 5.947   1.00 15.98  ? 182 TYR   A OH   1 
ATOM   1415 N  N    . GLY   A 1 183 ? -5.073  27.308 0.075   1.00 16.47  ? 183 GLY   A N    1 
ATOM   1416 C  CA   . GLY   A 1 183 ? -5.526  26.109 -0.621  1.00 17.44  ? 183 GLY   A CA   1 
ATOM   1417 C  C    . GLY   A 1 183 ? -6.215  26.345 -1.955  1.00 17.99  ? 183 GLY   A C    1 
ATOM   1418 O  O    . GLY   A 1 183 ? -6.422  27.472 -2.414  1.00 17.58  ? 183 GLY   A O    1 
ATOM   1419 N  N    . PRO   A 1 184 ? -6.596  25.249 -2.594  1.00 19.30  ? 184 PRO   A N    1 
ATOM   1420 C  CA   . PRO   A 1 184 ? -7.113  25.298 -3.968  1.00 19.28  ? 184 PRO   A CA   1 
ATOM   1421 C  C    . PRO   A 1 184 ? -8.618  25.547 -3.992  1.00 23.28  ? 184 PRO   A C    1 
ATOM   1422 O  O    . PRO   A 1 184 ? -9.401  24.729 -4.498  1.00 27.41  ? 184 PRO   A O    1 
ATOM   1423 C  CB   . PRO   A 1 184 ? -6.754  23.905 -4.496  1.00 22.44  ? 184 PRO   A CB   1 
ATOM   1424 C  CG   . PRO   A 1 184 ? -6.880  23.024 -3.302  1.00 22.66  ? 184 PRO   A CG   1 
ATOM   1425 C  CD   . PRO   A 1 184 ? -6.481  23.866 -2.095  1.00 22.45  ? 184 PRO   A CD   1 
ATOM   1426 N  N    . PHE   A 1 185 ? -9.032  26.680 -3.438  1.00 20.48  ? 185 PHE   A N    1 
ATOM   1427 C  CA   . PHE   A 1 185 ? -10.441 27.023 -3.303  1.00 21.05  ? 185 PHE   A CA   1 
ATOM   1428 C  C    . PHE   A 1 185 ? -10.708 28.330 -4.024  1.00 20.19  ? 185 PHE   A C    1 
ATOM   1429 O  O    . PHE   A 1 185 ? -9.797  29.147 -4.206  1.00 21.53  ? 185 PHE   A O    1 
ATOM   1430 C  CB   . PHE   A 1 185 ? -10.825 27.120 -1.819  1.00 19.59  ? 185 PHE   A CB   1 
ATOM   1431 C  CG   . PHE   A 1 185 ? -10.487 25.877 -1.065  1.00 19.39  ? 185 PHE   A CG   1 
ATOM   1432 C  CD1  . PHE   A 1 185 ? -11.091 24.669 -1.408  1.00 21.96  ? 185 PHE   A CD1  1 
ATOM   1433 C  CD2  . PHE   A 1 185 ? -9.526  25.884 -0.066  1.00 19.47  ? 185 PHE   A CD2  1 
ATOM   1434 C  CE1  . PHE   A 1 185 ? -10.762 23.497 -0.748  1.00 22.01  ? 185 PHE   A CE1  1 
ATOM   1435 C  CE2  . PHE   A 1 185 ? -9.192  24.715 0.600   1.00 21.65  ? 185 PHE   A CE2  1 
ATOM   1436 C  CZ   . PHE   A 1 185 ? -9.806  23.519 0.269   1.00 21.23  ? 185 PHE   A CZ   1 
ATOM   1437 N  N    . VAL   A 1 186 ? -11.962 28.519 -4.448  1.00 21.85  ? 186 VAL   A N    1 
ATOM   1438 C  CA   . VAL   A 1 186 ? -12.392 29.717 -5.153  1.00 19.31  ? 186 VAL   A CA   1 
ATOM   1439 C  C    . VAL   A 1 186 ? -13.688 30.206 -4.516  1.00 19.89  ? 186 VAL   A C    1 
ATOM   1440 O  O    . VAL   A 1 186 ? -14.482 29.410 -4.006  1.00 22.71  ? 186 VAL   A O    1 
ATOM   1441 C  CB   . VAL   A 1 186 ? -12.593 29.466 -6.670  1.00 22.44  ? 186 VAL   A CB   1 
ATOM   1442 C  CG1  . VAL   A 1 186 ? -11.250 29.124 -7.311  1.00 24.22  ? 186 VAL   A CG1  1 
ATOM   1443 C  CG2  . VAL   A 1 186 ? -13.595 28.335 -6.898  1.00 26.49  ? 186 VAL   A CG2  1 
ATOM   1444 N  N    . ASP   A 1 187 ? -13.900 31.524 -4.569  1.00 19.08  ? 187 ASP   A N    1 
ATOM   1445 C  CA   . ASP   A 1 187 ? -15.052 32.154 -3.918  1.00 21.81  ? 187 ASP   A CA   1 
ATOM   1446 C  C    . ASP   A 1 187 ? -16.248 32.161 -4.881  1.00 24.91  ? 187 ASP   A C    1 
ATOM   1447 O  O    . ASP   A 1 187 ? -16.705 33.185 -5.392  1.00 25.97  ? 187 ASP   A O    1 
ATOM   1448 C  CB   . ASP   A 1 187 ? -14.665 33.531 -3.383  1.00 20.34  ? 187 ASP   A CB   1 
ATOM   1449 C  CG   . ASP   A 1 187 ? -14.036 34.456 -4.414  1.00 24.21  ? 187 ASP   A CG   1 
ATOM   1450 O  OD1  . ASP   A 1 187 ? -13.577 34.028 -5.507  1.00 22.57  ? 187 ASP   A OD1  1 
ATOM   1451 O  OD2  . ASP   A 1 187 ? -13.877 35.641 -4.051  1.00 19.29  ? 187 ASP   A OD2  1 
ATOM   1452 N  N    . ARG   A 1 188 ? -16.713 30.951 -5.100  1.00 25.12  ? 188 ARG   A N    1 
ATOM   1453 C  CA   . ARG   A 1 188 ? -17.868 30.766 -5.984  1.00 34.11  ? 188 ARG   A CA   1 
ATOM   1454 C  C    . ARG   A 1 188 ? -18.605 29.588 -5.391  1.00 42.25  ? 188 ARG   A C    1 
ATOM   1455 O  O    . ARG   A 1 188 ? -17.993 28.769 -4.692  1.00 35.74  ? 188 ARG   A O    1 
ATOM   1456 C  CB   . ARG   A 1 188 ? -17.415 30.350 -7.378  1.00 32.66  ? 188 ARG   A CB   1 
ATOM   1457 C  CG   . ARG   A 1 188 ? -17.017 31.507 -8.277  1.00 46.47  ? 188 ARG   A CG   1 
ATOM   1458 C  CD   . ARG   A 1 188 ? -16.726 31.004 -9.676  1.00 49.85  ? 188 ARG   A CD   1 
ATOM   1459 N  NE   . ARG   A 1 188 ? -16.662 29.552 -9.717  1.00 53.60  ? 188 ARG   A NE   1 
ATOM   1460 N  N    . GLN   A 1 189 ? -19.879 29.518 -5.692  1.00 43.40  ? 189 GLN   A N    1 
ATOM   1461 C  CA   . GLN   A 1 189 ? -20.640 28.431 -5.083  1.00 49.24  ? 189 GLN   A CA   1 
ATOM   1462 C  C    . GLN   A 1 189 ? -20.558 27.173 -5.861  1.00 53.43  ? 189 GLN   A C    1 
ATOM   1463 O  O    . GLN   A 1 189 ? -21.532 26.781 -6.519  1.00 51.47  ? 189 GLN   A O    1 
ATOM   1464 C  CB   . GLN   A 1 189 ? -22.109 28.827 -4.913  1.00 52.66  ? 189 GLN   A CB   1 
ATOM   1465 C  CG   . GLN   A 1 189 ? -22.350 30.001 -3.981  1.00 51.60  ? 189 GLN   A CG   1 
ATOM   1466 C  CD   . GLN   A 1 189 ? -23.313 29.644 -2.876  1.00 65.84  ? 189 GLN   A CD   1 
ATOM   1467 O  OE1  . GLN   A 1 189 ? -23.238 28.571 -2.282  1.00 63.45  ? 189 GLN   A OE1  1 
ATOM   1468 N  NE2  . GLN   A 1 189 ? -24.229 30.552 -2.584  1.00 59.07  ? 189 GLN   A NE2  1 
ATOM   1469 N  N    . THR   A 1 190 ? -19.436 26.534 -5.709  1.00 46.62  ? 190 THR   A N    1 
ATOM   1470 C  CA   . THR   A 1 190 ? -19.254 25.255 -6.381  1.00 50.80  ? 190 THR   A CA   1 
ATOM   1471 C  C    . THR   A 1 190 ? -19.066 24.280 -5.232  1.00 55.44  ? 190 THR   A C    1 
ATOM   1472 O  O    . THR   A 1 190 ? -18.658 24.745 -4.142  1.00 48.81  ? 190 THR   A O    1 
ATOM   1473 C  CB   . THR   A 1 190 ? -18.081 25.380 -7.345  1.00 43.50  ? 190 THR   A CB   1 
ATOM   1474 O  OG1  . THR   A 1 190 ? -18.587 26.127 -8.451  1.00 60.38  ? 190 THR   A OG1  1 
ATOM   1475 C  CG2  . THR   A 1 190 ? -17.532 24.045 -7.795  1.00 51.95  ? 190 THR   A CG2  1 
ATOM   1476 N  N    . ALA   A 1 191 ? -19.384 23.017 -5.459  1.00 48.66  ? 191 ALA   A N    1 
ATOM   1477 C  CA   . ALA   A 1 191 ? -19.115 22.007 -4.423  1.00 61.36  ? 191 ALA   A CA   1 
ATOM   1478 C  C    . ALA   A 1 191 ? -17.626 21.742 -4.512  1.00 56.43  ? 191 ALA   A C    1 
ATOM   1479 O  O    . ALA   A 1 191 ? -17.173 21.130 -5.488  1.00 59.57  ? 191 ALA   A O    1 
ATOM   1480 C  CB   . ALA   A 1 191 ? -19.927 20.760 -4.641  1.00 61.81  ? 191 ALA   A CB   1 
ATOM   1481 N  N    . GLN   A 1 192 ? -16.893 22.271 -3.549  1.00 55.20  ? 192 GLN   A N    1 
ATOM   1482 C  CA   . GLN   A 1 192 ? -15.429 22.131 -3.640  1.00 38.25  ? 192 GLN   A CA   1 
ATOM   1483 C  C    . GLN   A 1 192 ? -15.039 21.235 -2.489  1.00 39.40  ? 192 GLN   A C    1 
ATOM   1484 O  O    . GLN   A 1 192 ? -15.667 21.337 -1.438  1.00 48.02  ? 192 GLN   A O    1 
ATOM   1485 C  CB   . GLN   A 1 192 ? -14.780 23.514 -3.550  1.00 37.27  ? 192 GLN   A CB   1 
ATOM   1486 C  CG   . GLN   A 1 192 ? -15.434 24.573 -4.412  1.00 39.04  ? 192 GLN   A CG   1 
ATOM   1487 C  CD   . GLN   A 1 192 ? -14.786 25.910 -4.167  1.00 28.75  ? 192 GLN   A CD   1 
ATOM   1488 O  OE1  . GLN   A 1 192 ? -13.571 26.017 -4.027  1.00 25.56  ? 192 GLN   A OE1  1 
ATOM   1489 N  NE2  . GLN   A 1 192 ? -15.606 26.942 -4.111  1.00 28.51  ? 192 GLN   A NE2  1 
ATOM   1490 N  N    . ALA   A 1 193 ? -14.014 20.421 -2.666  1.00 37.47  ? 193 ALA   A N    1 
ATOM   1491 C  CA   . ALA   A 1 193 ? -13.745 19.499 -1.550  1.00 31.67  ? 193 ALA   A CA   1 
ATOM   1492 C  C    . ALA   A 1 193 ? -12.346 19.713 -0.998  1.00 29.36  ? 193 ALA   A C    1 
ATOM   1493 O  O    . ALA   A 1 193 ? -11.425 19.963 -1.767  1.00 33.77  ? 193 ALA   A O    1 
ATOM   1494 C  CB   . ALA   A 1 193 ? -13.975 18.079 -1.985  1.00 33.51  ? 193 ALA   A CB   1 
ATOM   1495 N  N    . ALA   A 1 194 ? -12.246 19.644 0.318   1.00 33.12  ? 194 ALA   A N    1 
ATOM   1496 C  CA   . ALA   A 1 194 ? -10.927 19.705 0.928   1.00 36.39  ? 194 ALA   A CA   1 
ATOM   1497 C  C    . ALA   A 1 194 ? -10.130 18.457 0.558   1.00 40.06  ? 194 ALA   A C    1 
ATOM   1498 O  O    . ALA   A 1 194 ? -10.672 17.346 0.527   1.00 39.03  ? 194 ALA   A O    1 
ATOM   1499 C  CB   . ALA   A 1 194 ? -11.071 19.830 2.444   1.00 39.02  ? 194 ALA   A CB   1 
ATOM   1500 N  N    . GLY   A 1 195 ? -8.853  18.647 0.229   1.00 34.40  ? 195 GLY   A N    1 
ATOM   1501 C  CA   . GLY   A 1 195 ? -7.965  17.530 -0.024  1.00 33.13  ? 195 GLY   A CA   1 
ATOM   1502 C  C    . GLY   A 1 195 ? -7.693  16.709 1.227   1.00 33.05  ? 195 GLY   A C    1 
ATOM   1503 O  O    . GLY   A 1 195 ? -8.211  17.010 2.312   1.00 32.28  ? 195 GLY   A O    1 
ATOM   1504 N  N    . THR   A 1 196 ? -6.889  15.660 1.097   1.00 29.83  ? 196 THR   A N    1 
ATOM   1505 C  CA   . THR   A 1 196 ? -6.611  14.829 2.262   1.00 27.67  ? 196 THR   A CA   1 
ATOM   1506 C  C    . THR   A 1 196 ? -5.800  15.609 3.286   1.00 29.47  ? 196 THR   A C    1 
ATOM   1507 O  O    . THR   A 1 196 ? -4.984  16.469 2.946   1.00 31.45  ? 196 THR   A O    1 
ATOM   1508 C  CB   . THR   A 1 196 ? -5.851  13.568 1.868   1.00 33.96  ? 196 THR   A CB   1 
ATOM   1509 O  OG1  . THR   A 1 196 ? -4.646  13.942 1.194   1.00 41.31  ? 196 THR   A OG1  1 
ATOM   1510 C  CG2  . THR   A 1 196 ? -6.698  12.684 0.953   1.00 36.22  ? 196 THR   A CG2  1 
ATOM   1511 N  N    . ASP   A 1 197 ? -6.006  15.269 4.548   1.00 28.70  ? 197 ASP   A N    1 
ATOM   1512 C  CA   . ASP   A 1 197 ? -5.325  15.912 5.662   1.00 23.57  ? 197 ASP   A CA   1 
ATOM   1513 C  C    . ASP   A 1 197 ? -4.437  14.901 6.376   1.00 29.36  ? 197 ASP   A C    1 
ATOM   1514 O  O    . ASP   A 1 197 ? -4.581  13.689 6.212   1.00 30.78  ? 197 ASP   A O    1 
ATOM   1515 C  CB   . ASP   A 1 197 ? -6.341  16.542 6.616   1.00 24.97  ? 197 ASP   A CB   1 
ATOM   1516 C  CG   . ASP   A 1 197 ? -5.720  17.604 7.540   1.00 29.67  ? 197 ASP   A CG   1 
ATOM   1517 O  OD1  . ASP   A 1 197 ? -4.608  18.109 7.280   1.00 27.54  ? 197 ASP   A OD1  1 
ATOM   1518 O  OD2  . ASP   A 1 197 ? -6.371  17.931 8.545   1.00 27.80  ? 197 ASP   A OD2  1 
ATOM   1519 N  N    . THR   A 1 198 ? -3.514  15.418 7.183   1.00 25.67  ? 198 THR   A N    1 
ATOM   1520 C  CA   . THR   A 1 198 ? -2.586  14.582 7.927   1.00 24.42  ? 198 THR   A CA   1 
ATOM   1521 C  C    . THR   A 1 198 ? -2.508  15.145 9.338   1.00 24.31  ? 198 THR   A C    1 
ATOM   1522 O  O    . THR   A 1 198 ? -2.936  16.274 9.587   1.00 25.63  ? 198 THR   A O    1 
ATOM   1523 C  CB   . THR   A 1 198 ? -1.209  14.566 7.242   1.00 36.59  ? 198 THR   A CB   1 
ATOM   1524 O  OG1  . THR   A 1 198 ? -0.341  13.639 7.895   1.00 46.73  ? 198 THR   A OG1  1 
ATOM   1525 C  CG2  . THR   A 1 198 ? -0.584  15.950 7.311   1.00 28.23  ? 198 THR   A CG2  1 
ATOM   1526 N  N    . THR   A 1 199 ? -2.002  14.335 10.274  1.00 25.95  ? 199 THR   A N    1 
ATOM   1527 C  CA   . THR   A 1 199 ? -1.804  14.817 11.638  1.00 23.56  ? 199 THR   A CA   1 
ATOM   1528 C  C    . THR   A 1 199 ? -0.462  15.531 11.766  1.00 25.31  ? 199 THR   A C    1 
ATOM   1529 O  O    . THR   A 1 199 ? 0.557   15.091 11.223  1.00 27.29  ? 199 THR   A O    1 
ATOM   1530 C  CB   . THR   A 1 199 ? -1.907  13.662 12.636  1.00 29.02  ? 199 THR   A CB   1 
ATOM   1531 O  OG1  . THR   A 1 199 ? -3.223  13.095 12.567  1.00 27.26  ? 199 THR   A OG1  1 
ATOM   1532 C  CG2  . THR   A 1 199 ? -1.640  14.165 14.042  1.00 25.12  ? 199 THR   A CG2  1 
ATOM   1533 N  N    . ILE   A 1 200 ? -0.461  16.658 12.480  1.00 22.18  ? 200 ILE   A N    1 
ATOM   1534 C  CA   . ILE   A 1 200 ? 0.719   17.511 12.557  1.00 22.22  ? 200 ILE   A CA   1 
ATOM   1535 C  C    . ILE   A 1 200 ? 1.612   16.971 13.676  1.00 27.18  ? 200 ILE   A C    1 
ATOM   1536 O  O    . ILE   A 1 200 ? 1.418   17.281 14.848  1.00 23.89  ? 200 ILE   A O    1 
ATOM   1537 C  CB   . ILE   A 1 200 ? 0.333   18.971 12.780  1.00 22.52  ? 200 ILE   A CB   1 
ATOM   1538 C  CG1  . ILE   A 1 200 ? -0.752  19.386 11.775  1.00 23.77  ? 200 ILE   A CG1  1 
ATOM   1539 C  CG2  . ILE   A 1 200 ? 1.589   19.852 12.722  1.00 23.41  ? 200 ILE   A CG2  1 
ATOM   1540 C  CD1  . ILE   A 1 200 ? -1.687  20.462 12.288  1.00 28.09  ? 200 ILE   A CD1  1 
ATOM   1541 N  N    . THR   A 1 201 ? 2.630   16.192 13.296  1.00 23.12  ? 201 THR   A N    1 
ATOM   1542 C  CA   . THR   A 1 201 ? 3.413   15.406 14.257  1.00 25.26  ? 201 THR   A CA   1 
ATOM   1543 C  C    . THR   A 1 201 ? 4.154   16.275 15.270  1.00 24.70  ? 201 THR   A C    1 
ATOM   1544 O  O    . THR   A 1 201 ? 4.175   15.966 16.473  1.00 23.97  ? 201 THR   A O    1 
ATOM   1545 C  CB   . THR   A 1 201 ? 4.398   14.527 13.488  1.00 28.81  ? 201 THR   A CB   1 
ATOM   1546 O  OG1  . THR   A 1 201 ? 3.678   13.838 12.471  1.00 31.06  ? 201 THR   A OG1  1 
ATOM   1547 C  CG2  . THR   A 1 201 ? 5.098   13.509 14.419  1.00 27.76  ? 201 THR   A CG2  1 
ATOM   1548 N  N    . VAL   A 1 202 ? 4.838   17.321 14.795  1.00 23.09  ? 202 VAL   A N    1 
ATOM   1549 C  CA   . VAL   A 1 202 ? 5.603   18.161 15.705  1.00 26.85  ? 202 VAL   A CA   1 
ATOM   1550 C  C    . VAL   A 1 202 ? 4.695   18.756 16.769  1.00 21.36  ? 202 VAL   A C    1 
ATOM   1551 O  O    . VAL   A 1 202 ? 5.108   18.915 17.923  1.00 23.73  ? 202 VAL   A O    1 
ATOM   1552 C  CB   . VAL   A 1 202 ? 6.377   19.248 14.934  1.00 26.39  ? 202 VAL   A CB   1 
ATOM   1553 C  CG1  . VAL   A 1 202 ? 5.414   20.294 14.350  1.00 26.46  ? 202 VAL   A CG1  1 
ATOM   1554 C  CG2  . VAL   A 1 202 ? 7.388   19.935 15.866  1.00 27.86  ? 202 VAL   A CG2  1 
ATOM   1555 N  N    . ASN   A 1 203 ? 3.443   19.062 16.410  1.00 20.59  ? 203 ASN   A N    1 
ATOM   1556 C  CA   . ASN   A 1 203 ? 2.498   19.626 17.376  1.00 20.85  ? 203 ASN   A CA   1 
ATOM   1557 C  C    . ASN   A 1 203 ? 2.092   18.582 18.414  1.00 21.45  ? 203 ASN   A C    1 
ATOM   1558 O  O    . ASN   A 1 203 ? 1.997   18.887 19.608  1.00 20.51  ? 203 ASN   A O    1 
ATOM   1559 C  CB   . ASN   A 1 203 ? 1.257   20.174 16.660  1.00 20.34  ? 203 ASN   A CB   1 
ATOM   1560 C  CG   . ASN   A 1 203 ? 1.522   21.507 15.958  1.00 20.33  ? 203 ASN   A CG   1 
ATOM   1561 O  OD1  . ASN   A 1 203 ? 2.667   21.971 15.902  1.00 23.10  ? 203 ASN   A OD1  1 
ATOM   1562 N  ND2  . ASN   A 1 203 ? 0.470   22.114 15.411  1.00 17.56  ? 203 ASN   A ND2  1 
ATOM   1563 N  N    . VAL   A 1 204 ? 1.833   17.348 17.974  1.00 20.24  ? 204 VAL   A N    1 
ATOM   1564 C  CA   . VAL   A 1 204 ? 1.529   16.282 18.925  1.00 22.84  ? 204 VAL   A CA   1 
ATOM   1565 C  C    . VAL   A 1 204 ? 2.673   16.114 19.914  1.00 24.27  ? 204 VAL   A C    1 
ATOM   1566 O  O    . VAL   A 1 204 ? 2.448   15.939 21.120  1.00 21.45  ? 204 VAL   A O    1 
ATOM   1567 C  CB   . VAL   A 1 204 ? 1.217   14.968 18.182  1.00 20.94  ? 204 VAL   A CB   1 
ATOM   1568 C  CG1  . VAL   A 1 204 ? 1.011   13.834 19.182  1.00 25.80  ? 204 VAL   A CG1  1 
ATOM   1569 C  CG2  . VAL   A 1 204 ? -0.044  15.132 17.303  1.00 23.60  ? 204 VAL   A CG2  1 
ATOM   1570 N  N    . LEU   A 1 205 ? 3.925   16.144 19.429  1.00 21.54  ? 205 LEU   A N    1 
ATOM   1571 C  CA   . LEU   A 1 205 ? 5.038   15.981 20.364  1.00 22.54  ? 205 LEU   A CA   1 
ATOM   1572 C  C    . LEU   A 1 205 ? 5.127   17.173 21.301  1.00 22.00  ? 205 LEU   A C    1 
ATOM   1573 O  O    . LEU   A 1 205 ? 5.405   17.015 22.498  1.00 23.35  ? 205 LEU   A O    1 
ATOM   1574 C  CB   . LEU   A 1 205 ? 6.358   15.784 19.601  1.00 23.93  ? 205 LEU   A CB   1 
ATOM   1575 C  CG   . LEU   A 1 205 ? 6.453   14.514 18.756  1.00 25.02  ? 205 LEU   A CG   1 
ATOM   1576 C  CD1  . LEU   A 1 205 ? 7.578   14.640 17.728  1.00 31.35  ? 205 LEU   A CD1  1 
ATOM   1577 C  CD2  . LEU   A 1 205 ? 6.654   13.293 19.669  1.00 25.52  ? 205 LEU   A CD2  1 
ATOM   1578 N  N    . ALA   A 1 206 ? 4.855   18.379 20.785  1.00 21.86  ? 206 ALA   A N    1 
ATOM   1579 C  CA   . ALA   A 1 206 ? 4.872   19.547 21.659  1.00 19.84  ? 206 ALA   A CA   1 
ATOM   1580 C  C    . ALA   A 1 206 ? 3.847   19.395 22.771  1.00 20.90  ? 206 ALA   A C    1 
ATOM   1581 O  O    . ALA   A 1 206 ? 4.114   19.737 23.933  1.00 19.90  ? 206 ALA   A O    1 
ATOM   1582 C  CB   . ALA   A 1 206 ? 4.611   20.817 20.847  1.00 21.56  ? 206 ALA   A CB   1 
ATOM   1583 N  N    . TRP   A 1 207 ? 2.683   18.854 22.428  1.00 18.19  ? 207 TRP   A N    1 
ATOM   1584 C  CA   . TRP   A 1 207 ? 1.604   18.678 23.386  1.00 21.47  ? 207 TRP   A CA   1 
ATOM   1585 C  C    . TRP   A 1 207 ? 1.952   17.600 24.406  1.00 20.50  ? 207 TRP   A C    1 
ATOM   1586 O  O    . TRP   A 1 207 ? 1.589   17.715 25.584  1.00 22.16  ? 207 TRP   A O    1 
ATOM   1587 C  CB   . TRP   A 1 207 ? 0.350   18.305 22.626  1.00 22.00  ? 207 TRP   A CB   1 
ATOM   1588 C  CG   . TRP   A 1 207 ? -0.871  17.974 23.402  1.00 19.04  ? 207 TRP   A CG   1 
ATOM   1589 C  CD1  . TRP   A 1 207 ? -1.682  18.824 24.113  1.00 20.32  ? 207 TRP   A CD1  1 
ATOM   1590 C  CD2  . TRP   A 1 207 ? -1.418  16.667 23.552  1.00 19.15  ? 207 TRP   A CD2  1 
ATOM   1591 N  NE1  . TRP   A 1 207 ? -2.739  18.108 24.662  1.00 22.08  ? 207 TRP   A NE1  1 
ATOM   1592 C  CE2  . TRP   A 1 207 ? -2.579  16.782 24.348  1.00 21.34  ? 207 TRP   A CE2  1 
ATOM   1593 C  CE3  . TRP   A 1 207 ? -1.027  15.403 23.101  1.00 24.36  ? 207 TRP   A CE3  1 
ATOM   1594 C  CZ2  . TRP   A 1 207 ? -3.359  15.677 24.685  1.00 25.87  ? 207 TRP   A CZ2  1 
ATOM   1595 C  CZ3  . TRP   A 1 207 ? -1.805  14.305 23.441  1.00 25.64  ? 207 TRP   A CZ3  1 
ATOM   1596 C  CH2  . TRP   A 1 207 ? -2.958  14.455 24.213  1.00 23.31  ? 207 TRP   A CH2  1 
ATOM   1597 N  N    . LEU   A 1 208 ? 2.637   16.536 23.967  1.00 19.70  ? 208 LEU   A N    1 
ATOM   1598 C  CA   . LEU   A 1 208 ? 3.126   15.541 24.925  1.00 21.15  ? 208 LEU   A CA   1 
ATOM   1599 C  C    . LEU   A 1 208 ? 4.105   16.175 25.907  1.00 21.93  ? 208 LEU   A C    1 
ATOM   1600 O  O    . LEU   A 1 208 ? 4.087   15.864 27.106  1.00 22.19  ? 208 LEU   A O    1 
ATOM   1601 C  CB   . LEU   A 1 208 ? 3.775   14.345 24.210  1.00 20.69  ? 208 LEU   A CB   1 
ATOM   1602 C  CG   . LEU   A 1 208 ? 2.767   13.434 23.474  1.00 22.32  ? 208 LEU   A CG   1 
ATOM   1603 C  CD1  . LEU   A 1 208 ? 3.496   12.373 22.629  1.00 24.27  ? 208 LEU   A CD1  1 
ATOM   1604 C  CD2  . LEU   A 1 208 ? 1.720   12.782 24.391  1.00 24.43  ? 208 LEU   A CD2  1 
ATOM   1605 N  N    . TYR   A 1 209 ? 4.969   17.074 25.424  1.00 23.48  ? 209 TYR   A N    1 
ATOM   1606 C  CA   . TYR   A 1 209 ? 5.848   17.790 26.359  1.00 24.42  ? 209 TYR   A CA   1 
ATOM   1607 C  C    . TYR   A 1 209 ? 5.052   18.656 27.331  1.00 24.19  ? 209 TYR   A C    1 
ATOM   1608 O  O    . TYR   A 1 209 ? 5.388   18.738 28.523  1.00 22.45  ? 209 TYR   A O    1 
ATOM   1609 C  CB   . TYR   A 1 209 ? 6.854   18.656 25.600  1.00 24.15  ? 209 TYR   A CB   1 
ATOM   1610 C  CG   . TYR   A 1 209 ? 8.051   17.878 25.127  1.00 24.19  ? 209 TYR   A CG   1 
ATOM   1611 C  CD1  . TYR   A 1 209 ? 8.984   17.384 26.034  1.00 30.37  ? 209 TYR   A CD1  1 
ATOM   1612 C  CD2  . TYR   A 1 209 ? 8.239   17.609 23.779  1.00 24.80  ? 209 TYR   A CD2  1 
ATOM   1613 C  CE1  . TYR   A 1 209 ? 10.087  16.657 25.598  1.00 32.05  ? 209 TYR   A CE1  1 
ATOM   1614 C  CE2  . TYR   A 1 209 ? 9.329   16.881 23.331  1.00 29.17  ? 209 TYR   A CE2  1 
ATOM   1615 C  CZ   . TYR   A 1 209 ? 10.250  16.405 24.247  1.00 35.49  ? 209 TYR   A CZ   1 
ATOM   1616 O  OH   . TYR   A 1 209 ? 11.334  15.684 23.790  1.00 31.66  ? 209 TYR   A OH   1 
ATOM   1617 N  N    . ALA   A 1 210 ? 4.033   19.356 26.830  1.00 20.98  ? 210 ALA   A N    1 
ATOM   1618 C  CA   . ALA   A 1 210 ? 3.122   20.083 27.706  1.00 20.02  ? 210 ALA   A CA   1 
ATOM   1619 C  C    . ALA   A 1 210 ? 2.555   19.160 28.774  1.00 23.20  ? 210 ALA   A C    1 
ATOM   1620 O  O    . ALA   A 1 210 ? 2.431   19.550 29.934  1.00 23.20  ? 210 ALA   A O    1 
ATOM   1621 C  CB   . ALA   A 1 210 ? 1.981   20.718 26.904  1.00 23.41  ? 210 ALA   A CB   1 
ATOM   1622 N  N    . ALA   A 1 211 ? 2.192   17.934 28.387  1.00 20.19  ? 211 ALA   A N    1 
ATOM   1623 C  CA   . ALA   A 1 211 ? 1.615   17.001 29.347  1.00 22.38  ? 211 ALA   A CA   1 
ATOM   1624 C  C    . ALA   A 1 211 ? 2.626   16.681 30.439  1.00 25.66  ? 211 ALA   A C    1 
ATOM   1625 O  O    . ALA   A 1 211 ? 2.296   16.688 31.638  1.00 23.69  ? 211 ALA   A O    1 
ATOM   1626 C  CB   . ALA   A 1 211 ? 1.167   15.721 28.640  1.00 21.41  ? 211 ALA   A CB   1 
ATOM   1627 N  N    . VAL   A 1 212 ? 3.875   16.403 30.037  1.00 21.56  ? 212 VAL   A N    1 
ATOM   1628 C  CA   . VAL   A 1 212 ? 4.921   16.108 31.028  1.00 25.12  ? 212 VAL   A CA   1 
ATOM   1629 C  C    . VAL   A 1 212 ? 5.132   17.290 31.966  1.00 27.93  ? 212 VAL   A C    1 
ATOM   1630 O  O    . VAL   A 1 212 ? 5.255   17.121 33.188  1.00 26.37  ? 212 VAL   A O    1 
ATOM   1631 C  CB   . VAL   A 1 212 ? 6.239   15.698 30.343  1.00 25.42  ? 212 VAL   A CB   1 
ATOM   1632 C  CG1  . VAL   A 1 212 ? 7.255   15.298 31.396  1.00 28.78  ? 212 VAL   A CG1  1 
ATOM   1633 C  CG2  . VAL   A 1 212 ? 6.008   14.509 29.442  1.00 25.42  ? 212 VAL   A CG2  1 
ATOM   1634 N  N    . ILE   A 1 213 ? 5.205   18.503 31.410  1.00 27.00  ? 213 ILE   A N    1 
ATOM   1635 C  CA   . ILE   A 1 213 ? 5.408   19.685 32.250  1.00 26.99  ? 213 ILE   A CA   1 
ATOM   1636 C  C    . ILE   A 1 213 ? 4.311   19.794 33.293  1.00 30.89  ? 213 ILE   A C    1 
ATOM   1637 O  O    . ILE   A 1 213 ? 4.558   20.227 34.436  1.00 27.76  ? 213 ILE   A O    1 
ATOM   1638 C  CB   . ILE   A 1 213 ? 5.494   20.956 31.373  1.00 30.47  ? 213 ILE   A CB   1 
ATOM   1639 C  CG1  . ILE   A 1 213 ? 6.765   20.929 30.523  1.00 26.75  ? 213 ILE   A CG1  1 
ATOM   1640 C  CG2  . ILE   A 1 213 ? 5.412   22.214 32.233  1.00 32.32  ? 213 ILE   A CG2  1 
ATOM   1641 C  CD1  . ILE   A 1 213 ? 6.722   21.880 29.325  1.00 29.18  ? 213 ILE   A CD1  1 
ATOM   1642 N  N    . ASN   A 1 214 ? 3.104   19.360 32.944  1.00 25.88  ? 214 ASN   A N    1 
ATOM   1643 C  CA   . ASN   A 1 214 ? 1.930   19.424 33.801  1.00 26.40  ? 214 ASN   A CA   1 
ATOM   1644 C  C    . ASN   A 1 214 ? 1.692   18.141 34.585  1.00 30.83  ? 214 ASN   A C    1 
ATOM   1645 O  O    . ASN   A 1 214 ? 0.628   17.991 35.194  1.00 31.87  ? 214 ASN   A O    1 
ATOM   1646 C  CB   . ASN   A 1 214 ? 0.690   19.768 32.978  1.00 27.63  ? 214 ASN   A CB   1 
ATOM   1647 C  CG   . ASN   A 1 214 ? 0.587   21.240 32.704  1.00 32.53  ? 214 ASN   A CG   1 
ATOM   1648 O  OD1  . ASN   A 1 214 ? 0.055   21.996 33.518  1.00 32.96  ? 214 ASN   A OD1  1 
ATOM   1649 N  ND2  . ASN   A 1 214 ? 1.112   21.670 31.564  1.00 33.12  ? 214 ASN   A ND2  1 
ATOM   1650 N  N    . GLY   A 1 215 ? 2.640   17.214 34.570  1.00 31.52  ? 215 GLY   A N    1 
ATOM   1651 C  CA   . GLY   A 1 215 ? 2.588   16.057 35.439  1.00 31.34  ? 215 GLY   A CA   1 
ATOM   1652 C  C    . GLY   A 1 215 ? 1.933   14.800 34.898  1.00 34.97  ? 215 GLY   A C    1 
ATOM   1653 O  O    . GLY   A 1 215 ? 1.831   13.825 35.643  1.00 32.40  ? 215 GLY   A O    1 
ATOM   1654 N  N    . ASP   A 1 216 ? 1.477   14.767 33.645  1.00 28.09  ? 216 ASP   A N    1 
ATOM   1655 C  CA   . ASP   A 1 216 ? 1.080   13.493 33.044  1.00 30.67  ? 216 ASP   A CA   1 
ATOM   1656 C  C    . ASP   A 1 216 ? 2.311   12.821 32.465  1.00 39.41  ? 216 ASP   A C    1 
ATOM   1657 O  O    . ASP   A 1 216 ? 2.927   13.342 31.526  1.00 31.29  ? 216 ASP   A O    1 
ATOM   1658 C  CB   . ASP   A 1 216 ? 0.001   13.595 31.958  1.00 33.78  ? 216 ASP   A CB   1 
ATOM   1659 C  CG   . ASP   A 1 216 ? -1.236  14.295 32.427  1.00 43.97  ? 216 ASP   A CG   1 
ATOM   1660 O  OD1  . ASP   A 1 216 ? -1.769  13.860 33.469  1.00 43.94  ? 216 ASP   A OD1  1 
ATOM   1661 O  OD2  . ASP   A 1 216 ? -1.767  15.150 31.684  1.00 40.37  ? 216 ASP   A OD2  1 
ATOM   1662 N  N    . ARG   A 1 217 ? 2.634   11.648 33.002  1.00 29.46  ? 217 ARG   A N    1 
ATOM   1663 C  CA   . ARG   A 1 217 ? 3.856   10.952 32.652  1.00 30.09  ? 217 ARG   A CA   1 
ATOM   1664 C  C    . ARG   A 1 217 ? 3.645   9.508  32.231  1.00 27.36  ? 217 ARG   A C    1 
ATOM   1665 O  O    . ARG   A 1 217 ? 4.625   8.840  31.875  1.00 26.83  ? 217 ARG   A O    1 
ATOM   1666 C  CB   . ARG   A 1 217 ? 4.819   10.972 33.840  1.00 31.72  ? 217 ARG   A CB   1 
ATOM   1667 C  CG   . ARG   A 1 217 ? 5.493   12.292 34.024  1.00 33.67  ? 217 ARG   A CG   1 
ATOM   1668 C  CD   . ARG   A 1 217 ? 6.398   12.263 35.230  1.00 29.80  ? 217 ARG   A CD   1 
ATOM   1669 N  NE   . ARG   A 1 217 ? 7.646   11.645 34.809  1.00 26.18  ? 217 ARG   A NE   1 
ATOM   1670 C  CZ   . ARG   A 1 217 ? 8.701   12.309 34.366  1.00 31.52  ? 217 ARG   A CZ   1 
ATOM   1671 N  NH1  . ARG   A 1 217 ? 8.673   13.626 34.208  1.00 34.31  ? 217 ARG   A NH1  1 
ATOM   1672 N  NH2  . ARG   A 1 217 ? 9.781   11.631 33.999  1.00 28.99  ? 217 ARG   A NH2  1 
ATOM   1673 N  N    . TRP   A 1 218 ? 2.406   9.013  32.261  1.00 24.62  ? 218 TRP   A N    1 
ATOM   1674 C  CA   . TRP   A 1 218 ? 2.162   7.578  32.175  1.00 25.76  ? 218 TRP   A CA   1 
ATOM   1675 C  C    . TRP   A 1 218 ? 2.605   6.987  30.843  1.00 29.57  ? 218 TRP   A C    1 
ATOM   1676 O  O    . TRP   A 1 218 ? 2.945   5.797  30.777  1.00 29.55  ? 218 TRP   A O    1 
ATOM   1677 C  CB   . TRP   A 1 218 ? 0.679   7.288  32.430  1.00 30.70  ? 218 TRP   A CB   1 
ATOM   1678 C  CG   . TRP   A 1 218 ? -0.292  7.897  31.447  1.00 30.28  ? 218 TRP   A CG   1 
ATOM   1679 C  CD1  . TRP   A 1 218 ? -1.011  9.049  31.600  1.00 26.30  ? 218 TRP   A CD1  1 
ATOM   1680 C  CD2  . TRP   A 1 218 ? -0.638  7.368  30.172  1.00 29.32  ? 218 TRP   A CD2  1 
ATOM   1681 N  NE1  . TRP   A 1 218 ? -1.801  9.265  30.480  1.00 28.90  ? 218 TRP   A NE1  1 
ATOM   1682 C  CE2  . TRP   A 1 218 ? -1.581  8.247  29.591  1.00 28.36  ? 218 TRP   A CE2  1 
ATOM   1683 C  CE3  . TRP   A 1 218 ? -0.239  6.237  29.456  1.00 32.07  ? 218 TRP   A CE3  1 
ATOM   1684 C  CZ2  . TRP   A 1 218 ? -2.130  8.021  28.331  1.00 33.77  ? 218 TRP   A CZ2  1 
ATOM   1685 C  CZ3  . TRP   A 1 218 ? -0.788  6.016  28.206  1.00 35.63  ? 218 TRP   A CZ3  1 
ATOM   1686 C  CH2  . TRP   A 1 218 ? -1.721  6.906  27.657  1.00 34.56  ? 218 TRP   A CH2  1 
ATOM   1687 N  N    . PHE   A 1 219 ? 2.590   7.790  29.770  1.00 29.81  ? 219 PHE   A N    1 
ATOM   1688 C  CA   . PHE   A 1 219 ? 2.939   7.347  28.427  1.00 31.52  ? 219 PHE   A CA   1 
ATOM   1689 C  C    . PHE   A 1 219 ? 4.443   7.306  28.187  1.00 28.55  ? 219 PHE   A C    1 
ATOM   1690 O  O    . PHE   A 1 219 ? 4.871   6.870  27.113  1.00 31.62  ? 219 PHE   A O    1 
ATOM   1691 C  CB   . PHE   A 1 219 ? 2.285   8.274  27.389  1.00 27.93  ? 219 PHE   A CB   1 
ATOM   1692 C  CG   . PHE   A 1 219 ? 2.524   9.727  27.662  1.00 27.63  ? 219 PHE   A CG   1 
ATOM   1693 C  CD1  . PHE   A 1 219 ? 3.668   10.352 27.173  1.00 25.49  ? 219 PHE   A CD1  1 
ATOM   1694 C  CD2  . PHE   A 1 219 ? 1.616   10.468 28.418  1.00 24.92  ? 219 PHE   A CD2  1 
ATOM   1695 C  CE1  . PHE   A 1 219 ? 3.924   11.688 27.441  1.00 25.21  ? 219 PHE   A CE1  1 
ATOM   1696 C  CE2  . PHE   A 1 219 ? 1.848   11.808 28.687  1.00 27.05  ? 219 PHE   A CE2  1 
ATOM   1697 C  CZ   . PHE   A 1 219 ? 3.009   12.428 28.196  1.00 26.47  ? 219 PHE   A CZ   1 
ATOM   1698 N  N    . LEU   A 1 220 ? 5.253   7.766  29.138  1.00 28.12  ? 220 LEU   A N    1 
ATOM   1699 C  CA   . LEU   A 1 220 ? 6.696   7.742  28.958  1.00 29.67  ? 220 LEU   A CA   1 
ATOM   1700 C  C    . LEU   A 1 220 ? 7.214   6.311  29.078  1.00 36.00  ? 220 LEU   A C    1 
ATOM   1701 O  O    . LEU   A 1 220 ? 6.599   5.450  29.713  1.00 34.00  ? 220 LEU   A O    1 
ATOM   1702 C  CB   . LEU   A 1 220 ? 7.383   8.628  30.000  1.00 31.32  ? 220 LEU   A CB   1 
ATOM   1703 C  CG   . LEU   A 1 220 ? 7.148   10.137 29.919  1.00 24.72  ? 220 LEU   A CG   1 
ATOM   1704 C  CD1  . LEU   A 1 220 ? 7.975   10.833 30.990  1.00 26.02  ? 220 LEU   A CD1  1 
ATOM   1705 C  CD2  . LEU   A 1 220 ? 7.525   10.653 28.533  1.00 25.72  ? 220 LEU   A CD2  1 
ATOM   1706 N  N    . ASN   A 1 221 ? 8.377   6.072  28.480  1.00 36.63  ? 221 ASN   A N    1 
ATOM   1707 C  CA   . ASN   A 1 221 ? 8.987   4.750  28.526  1.00 38.09  ? 221 ASN   A CA   1 
ATOM   1708 C  C    . ASN   A 1 221 ? 10.493  4.891  28.371  1.00 49.74  ? 221 ASN   A C    1 
ATOM   1709 O  O    . ASN   A 1 221 ? 10.997  5.930  27.935  1.00 38.59  ? 221 ASN   A O    1 
ATOM   1710 C  CB   . ASN   A 1 221 ? 8.380   3.831  27.454  1.00 41.17  ? 221 ASN   A CB   1 
ATOM   1711 C  CG   . ASN   A 1 221 ? 8.629   4.329  26.032  1.00 50.66  ? 221 ASN   A CG   1 
ATOM   1712 O  OD1  . ASN   A 1 221 ? 9.687   4.879  25.719  1.00 54.05  ? 221 ASN   A OD1  1 
ATOM   1713 N  ND2  . ASN   A 1 221 ? 7.625   4.176  25.176  1.00 47.59  ? 221 ASN   A ND2  1 
ATOM   1714 N  N    . ARG   A 1 222 ? 11.213  3.835  28.768  1.00 42.90  ? 222 ARG   A N    1 
ATOM   1715 C  CA   . ARG   A 1 222 ? 12.657  3.788  28.577  1.00 50.83  ? 222 ARG   A CA   1 
ATOM   1716 C  C    . ARG   A 1 222 ? 13.053  3.516  27.131  1.00 58.12  ? 222 ARG   A C    1 
ATOM   1717 O  O    . ARG   A 1 222 ? 14.231  3.668  26.791  1.00 63.75  ? 222 ARG   A O    1 
ATOM   1718 C  CB   . ARG   A 1 222 ? 13.294  2.724  29.482  1.00 51.41  ? 222 ARG   A CB   1 
ATOM   1719 C  CG   . ARG   A 1 222 ? 14.805  2.671  29.318  1.00 71.13  ? 222 ARG   A CG   1 
ATOM   1720 C  CD   . ARG   A 1 222 ? 15.523  1.683  30.228  1.00 78.08  ? 222 ARG   A CD   1 
ATOM   1721 N  NE   . ARG   A 1 222 ? 16.961  1.752  29.983  1.00 86.96  ? 222 ARG   A NE   1 
ATOM   1722 C  CZ   . ARG   A 1 222 ? 17.892  1.164  30.722  1.00 82.66  ? 222 ARG   A CZ   1 
ATOM   1723 N  NH1  . ARG   A 1 222 ? 17.576  0.398  31.753  1.00 84.55  ? 222 ARG   A NH1  1 
ATOM   1724 N  NH2  . ARG   A 1 222 ? 19.174  1.343  30.413  1.00 87.46  ? 222 ARG   A NH2  1 
ATOM   1725 N  N    . PHE   A 1 223 ? 12.110  3.124  26.276  1.00 57.75  ? 223 PHE   A N    1 
ATOM   1726 C  CA   . PHE   A 1 223 ? 12.417  2.899  24.871  1.00 54.41  ? 223 PHE   A CA   1 
ATOM   1727 C  C    . PHE   A 1 223 ? 12.955  4.167  24.213  1.00 58.52  ? 223 PHE   A C    1 
ATOM   1728 O  O    . PHE   A 1 223 ? 12.720  5.294  24.665  1.00 53.67  ? 223 PHE   A O    1 
ATOM   1729 C  CB   . PHE   A 1 223 ? 11.175  2.446  24.097  1.00 63.96  ? 223 PHE   A CB   1 
ATOM   1730 C  CG   . PHE   A 1 223 ? 10.797  1.004  24.303  1.00 75.82  ? 223 PHE   A CG   1 
ATOM   1731 C  CD1  . PHE   A 1 223 ? 11.552  0.166  25.108  1.00 77.80  ? 223 PHE   A CD1  1 
ATOM   1732 C  CD2  . PHE   A 1 223 ? 9.682   0.484  23.658  1.00 79.52  ? 223 PHE   A CD2  1 
ATOM   1733 C  CE1  . PHE   A 1 223 ? 11.191  -1.165 25.277  1.00 84.55  ? 223 PHE   A CE1  1 
ATOM   1734 C  CE2  . PHE   A 1 223 ? 9.317   -0.839 23.820  1.00 87.50  ? 223 PHE   A CE2  1 
ATOM   1735 C  CZ   . PHE   A 1 223 ? 10.071  -1.667 24.631  1.00 87.81  ? 223 PHE   A CZ   1 
ATOM   1736 N  N    . THR   A 1 224 ? 13.678  3.966  23.116  1.00 47.86  ? 224 THR   A N    1 
ATOM   1737 C  CA   . THR   A 1 224 ? 13.980  5.034  22.179  1.00 56.80  ? 224 THR   A CA   1 
ATOM   1738 C  C    . THR   A 1 224 ? 13.815  4.496  20.767  1.00 54.86  ? 224 THR   A C    1 
ATOM   1739 O  O    . THR   A 1 224 ? 13.562  3.307  20.552  1.00 55.09  ? 224 THR   A O    1 
ATOM   1740 C  CB   . THR   A 1 224 ? 15.392  5.596  22.359  1.00 59.89  ? 224 THR   A CB   1 
ATOM   1741 O  OG1  . THR   A 1 224 ? 15.437  6.932  21.828  1.00 48.43  ? 224 THR   A OG1  1 
ATOM   1742 C  CG2  . THR   A 1 224 ? 16.407  4.718  21.617  1.00 54.66  ? 224 THR   A CG2  1 
ATOM   1743 N  N    . THR   A 1 225 ? 13.955  5.394  19.799  1.00 56.82  ? 225 THR   A N    1 
ATOM   1744 C  CA   . THR   A 1 225 ? 13.814  5.030  18.401  1.00 55.72  ? 225 THR   A CA   1 
ATOM   1745 C  C    . THR   A 1 225 ? 14.703  5.946  17.580  1.00 60.67  ? 225 THR   A C    1 
ATOM   1746 O  O    . THR   A 1 225 ? 15.267  6.920  18.085  1.00 54.98  ? 225 THR   A O    1 
ATOM   1747 C  CB   . THR   A 1 225 ? 12.361  5.141  17.928  1.00 57.48  ? 225 THR   A CB   1 
ATOM   1748 O  OG1  . THR   A 1 225 ? 12.281  4.766  16.548  1.00 57.40  ? 225 THR   A OG1  1 
ATOM   1749 C  CG2  . THR   A 1 225 ? 11.862  6.575  18.074  1.00 47.58  ? 225 THR   A CG2  1 
ATOM   1750 N  N    . THR   A 1 226 ? 14.825  5.618  16.303  1.00 59.50  ? 226 THR   A N    1 
ATOM   1751 C  CA   . THR   A 1 226 ? 15.467  6.500  15.346  1.00 61.52  ? 226 THR   A CA   1 
ATOM   1752 C  C    . THR   A 1 226 ? 14.407  7.300  14.607  1.00 56.11  ? 226 THR   A C    1 
ATOM   1753 O  O    . THR   A 1 226 ? 13.238  6.911  14.534  1.00 53.03  ? 226 THR   A O    1 
ATOM   1754 C  CB   . THR   A 1 226 ? 16.296  5.715  14.336  1.00 64.74  ? 226 THR   A CB   1 
ATOM   1755 O  OG1  . THR   A 1 226 ? 16.818  6.621  13.358  1.00 71.56  ? 226 THR   A OG1  1 
ATOM   1756 C  CG2  . THR   A 1 226 ? 15.410  4.719  13.632  1.00 62.37  ? 226 THR   A CG2  1 
ATOM   1757 N  N    . LEU   A 1 227 ? 14.841  8.421  14.035  1.00 56.44  ? 227 LEU   A N    1 
ATOM   1758 C  CA   . LEU   A 1 227 ? 13.928  9.259  13.268  1.00 56.83  ? 227 LEU   A CA   1 
ATOM   1759 C  C    . LEU   A 1 227 ? 13.273  8.479  12.132  1.00 59.30  ? 227 LEU   A C    1 
ATOM   1760 O  O    . LEU   A 1 227 ? 12.074  8.638  11.874  1.00 51.11  ? 227 LEU   A O    1 
ATOM   1761 C  CB   . LEU   A 1 227 ? 14.677  10.478 12.737  1.00 57.10  ? 227 LEU   A CB   1 
ATOM   1762 C  CG   . LEU   A 1 227 ? 13.849  11.610 12.135  1.00 61.69  ? 227 LEU   A CG   1 
ATOM   1763 C  CD1  . LEU   A 1 227 ? 14.673  12.886 12.099  1.00 56.01  ? 227 LEU   A CD1  1 
ATOM   1764 C  CD2  . LEU   A 1 227 ? 13.388  11.233 10.732  1.00 62.35  ? 227 LEU   A CD2  1 
ATOM   1765 N  N    . ASN   A 1 228 ? 14.034  7.613  11.453  1.00 61.62  ? 228 ASN   A N    1 
ATOM   1766 C  CA   . ASN   A 1 228 ? 13.485  6.937  10.281  1.00 61.86  ? 228 ASN   A CA   1 
ATOM   1767 C  C    . ASN   A 1 228 ? 12.516  5.818  10.660  1.00 57.56  ? 228 ASN   A C    1 
ATOM   1768 O  O    . ASN   A 1 228 ? 11.506  5.620  9.979   1.00 55.93  ? 228 ASN   A O    1 
ATOM   1769 C  CB   . ASN   A 1 228 ? 14.613  6.414  9.388   1.00 79.70  ? 228 ASN   A CB   1 
ATOM   1770 C  CG   . ASN   A 1 228 ? 15.512  7.527  8.877   1.00 82.92  ? 228 ASN   A CG   1 
ATOM   1771 O  OD1  . ASN   A 1 228 ? 16.709  7.551  9.159   1.00 88.67  ? 228 ASN   A OD1  1 
ATOM   1772 N  ND2  . ASN   A 1 228 ? 14.934  8.461  8.125   1.00 79.76  ? 228 ASN   A ND2  1 
ATOM   1773 N  N    . ASP   A 1 229 ? 12.780  5.077  11.741  1.00 62.04  ? 229 ASP   A N    1 
ATOM   1774 C  CA   . ASP   A 1 229 ? 11.796  4.078  12.160  1.00 61.97  ? 229 ASP   A CA   1 
ATOM   1775 C  C    . ASP   A 1 229 ? 10.528  4.746  12.690  1.00 50.83  ? 229 ASP   A C    1 
ATOM   1776 O  O    . ASP   A 1 229 ? 9.398   4.304  12.399  1.00 54.65  ? 229 ASP   A O    1 
ATOM   1777 C  CB   . ASP   A 1 229 ? 12.411  3.131  13.192  1.00 58.69  ? 229 ASP   A CB   1 
ATOM   1778 C  CG   . ASP   A 1 229 ? 13.403  2.160  12.564  1.00 79.39  ? 229 ASP   A CG   1 
ATOM   1779 O  OD1  . ASP   A 1 229 ? 12.952  1.201  11.900  1.00 81.44  ? 229 ASP   A OD1  1 
ATOM   1780 O  OD2  . ASP   A 1 229 ? 14.627  2.362  12.698  1.00 82.28  ? 229 ASP   A OD2  1 
ATOM   1781 N  N    . PHE   A 1 230 ? 10.688  5.843  13.429  1.00 51.63  ? 230 PHE   A N    1 
ATOM   1782 C  CA   . PHE   A 1 230 ? 9.517   6.629  13.794  1.00 52.12  ? 230 PHE   A CA   1 
ATOM   1783 C  C    . PHE   A 1 230 ? 8.722   7.021  12.560  1.00 48.32  ? 230 PHE   A C    1 
ATOM   1784 O  O    . PHE   A 1 230 ? 7.508   6.821  12.512  1.00 46.94  ? 230 PHE   A O    1 
ATOM   1785 C  CB   . PHE   A 1 230 ? 9.892   7.888  14.567  1.00 51.87  ? 230 PHE   A CB   1 
ATOM   1786 C  CG   . PHE   A 1 230 ? 8.696   8.729  14.896  1.00 45.52  ? 230 PHE   A CG   1 
ATOM   1787 C  CD1  . PHE   A 1 230 ? 7.835   8.351  15.907  1.00 39.69  ? 230 PHE   A CD1  1 
ATOM   1788 C  CD2  . PHE   A 1 230 ? 8.379   9.840  14.130  1.00 43.18  ? 230 PHE   A CD2  1 
ATOM   1789 C  CE1  . PHE   A 1 230 ? 6.712   9.098  16.194  1.00 37.83  ? 230 PHE   A CE1  1 
ATOM   1790 C  CE2  . PHE   A 1 230 ? 7.245   10.597 14.412  1.00 44.50  ? 230 PHE   A CE2  1 
ATOM   1791 C  CZ   . PHE   A 1 230 ? 6.417   10.223 15.447  1.00 39.88  ? 230 PHE   A CZ   1 
ATOM   1792 N  N    . ASN   A 1 231 ? 9.392   7.601  11.561  1.00 51.51  ? 231 ASN   A N    1 
ATOM   1793 C  CA   . ASN   A 1 231 ? 8.685   8.054  10.366  1.00 54.54  ? 231 ASN   A CA   1 
ATOM   1794 C  C    . ASN   A 1 231 ? 8.028   6.893  9.634   1.00 53.28  ? 231 ASN   A C    1 
ATOM   1795 O  O    . ASN   A 1 231 ? 6.960   7.060  9.035   1.00 52.73  ? 231 ASN   A O    1 
ATOM   1796 C  CB   . ASN   A 1 231 ? 9.652   8.805  9.453   1.00 50.81  ? 231 ASN   A CB   1 
ATOM   1797 C  CG   . ASN   A 1 231 ? 9.803   10.265 9.840   1.00 50.46  ? 231 ASN   A CG   1 
ATOM   1798 O  OD1  . ASN   A 1 231 ? 9.049   10.781 10.663  1.00 55.52  ? 231 ASN   A OD1  1 
ATOM   1799 N  ND2  . ASN   A 1 231 ? 10.800  10.928 9.276   1.00 58.97  ? 231 ASN   A ND2  1 
ATOM   1800 N  N    . LEU   A 1 232 ? 8.639   5.710  9.675   1.00 52.27  ? 232 LEU   A N    1 
ATOM   1801 C  CA   . LEU   A 1 232 ? 7.991   4.538  9.103   1.00 56.63  ? 232 LEU   A CA   1 
ATOM   1802 C  C    . LEU   A 1 232 ? 6.662   4.264  9.788   1.00 56.44  ? 232 LEU   A C    1 
ATOM   1803 O  O    . LEU   A 1 232 ? 5.699   3.832  9.145   1.00 57.37  ? 232 LEU   A O    1 
ATOM   1804 C  CB   . LEU   A 1 232 ? 8.912   3.321  9.206   1.00 60.75  ? 232 LEU   A CB   1 
ATOM   1805 C  CG   . LEU   A 1 232 ? 9.631   2.881  7.924   1.00 70.07  ? 232 LEU   A CG   1 
ATOM   1806 C  CD1  . LEU   A 1 232 ? 8.637   2.383  6.872   1.00 58.58  ? 232 LEU   A CD1  1 
ATOM   1807 C  CD2  . LEU   A 1 232 ? 10.496  4.003  7.361   1.00 72.95  ? 232 LEU   A CD2  1 
ATOM   1808 N  N    . VAL   A 1 233 ? 6.589   4.499  11.098  1.00 51.92  ? 233 VAL   A N    1 
ATOM   1809 C  CA   . VAL   A 1 233 ? 5.304   4.305  11.777  1.00 54.69  ? 233 VAL   A CA   1 
ATOM   1810 C  C    . VAL   A 1 233 ? 4.350   5.479  11.521  1.00 55.33  ? 233 VAL   A C    1 
ATOM   1811 O  O    . VAL   A 1 233 ? 3.137   5.290  11.303  1.00 59.57  ? 233 VAL   A O    1 
ATOM   1812 C  CB   . VAL   A 1 233 ? 5.544   4.064  13.277  1.00 60.02  ? 233 VAL   A CB   1 
ATOM   1813 C  CG1  . VAL   A 1 233 ? 4.232   4.103  14.044  1.00 54.94  ? 233 VAL   A CG1  1 
ATOM   1814 C  CG2  . VAL   A 1 233 ? 6.204   2.715  13.456  1.00 58.50  ? 233 VAL   A CG2  1 
ATOM   1815 N  N    . ALA   A 1 234 ? 4.880   6.702  11.539  1.00 56.11  ? 234 ALA   A N    1 
ATOM   1816 C  CA   . ALA   A 1 234 ? 4.074   7.887  11.263  1.00 53.30  ? 234 ALA   A CA   1 
ATOM   1817 C  C    . ALA   A 1 234 ? 3.336   7.736  9.941   1.00 54.39  ? 234 ALA   A C    1 
ATOM   1818 O  O    . ALA   A 1 234 ? 2.111   7.886  9.875   1.00 55.47  ? 234 ALA   A O    1 
ATOM   1819 C  CB   . ALA   A 1 234 ? 4.961   9.135  11.251  1.00 52.10  ? 234 ALA   A CB   1 
ATOM   1820 N  N    . MET   A 1 235 ? 4.079   7.424  8.873   1.00 56.80  ? 235 MET   A N    1 
ATOM   1821 C  CA   . MET   A 1 235 ? 3.460   7.195  7.571   1.00 57.15  ? 235 MET   A CA   1 
ATOM   1822 C  C    . MET   A 1 235 ? 2.275   6.249  7.689   1.00 53.81  ? 235 MET   A C    1 
ATOM   1823 O  O    . MET   A 1 235 ? 1.200   6.513  7.138   1.00 52.08  ? 235 MET   A O    1 
ATOM   1824 C  CB   . MET   A 1 235 ? 4.495   6.641  6.591   1.00 66.80  ? 235 MET   A CB   1 
ATOM   1825 C  CG   . MET   A 1 235 ? 5.520   7.664  6.120   1.00 76.20  ? 235 MET   A CG   1 
ATOM   1826 S  SD   . MET   A 1 235 ? 5.138   8.367  4.500   1.00 103.97 ? 235 MET   A SD   1 
ATOM   1827 C  CE   . MET   A 1 235 ? 5.330   6.930  3.455   1.00 76.83  ? 235 MET   A CE   1 
ATOM   1828 N  N    . LYS   A 1 236 ? 2.444   5.150  8.428   1.00 53.97  ? 236 LYS   A N    1 
ATOM   1829 C  CA   . LYS   A 1 236 ? 1.362   4.182  8.541   1.00 50.45  ? 236 LYS   A CA   1 
ATOM   1830 C  C    . LYS   A 1 236 ? 0.154   4.767  9.249   1.00 52.48  ? 236 LYS   A C    1 
ATOM   1831 O  O    . LYS   A 1 236 ? -0.976  4.330  9.002   1.00 54.99  ? 236 LYS   A O    1 
ATOM   1832 C  CB   . LYS   A 1 236 ? 1.834   2.925  9.271   1.00 53.81  ? 236 LYS   A CB   1 
ATOM   1833 C  CG   . LYS   A 1 236 ? 0.684   2.078  9.809   1.00 55.40  ? 236 LYS   A CG   1 
ATOM   1834 C  CD   . LYS   A 1 236 ? 1.152   0.671  10.178  1.00 60.56  ? 236 LYS   A CD   1 
ATOM   1835 C  CE   . LYS   A 1 236 ? 0.321   0.098  11.316  1.00 58.47  ? 236 LYS   A CE   1 
ATOM   1836 N  NZ   . LYS   A 1 236 ? 0.792   -1.253 11.722  1.00 63.48  ? 236 LYS   A NZ   1 
ATOM   1837 N  N    . TYR   A 1 237 ? 0.354   5.744  10.134  1.00 50.41  ? 237 TYR   A N    1 
ATOM   1838 C  CA   . TYR   A 1 237 ? -0.788  6.356  10.806  1.00 41.60  ? 237 TYR   A CA   1 
ATOM   1839 C  C    . TYR   A 1 237 ? -1.191  7.717  10.234  1.00 47.20  ? 237 TYR   A C    1 
ATOM   1840 O  O    . TYR   A 1 237 ? -1.974  8.432  10.870  1.00 37.87  ? 237 TYR   A O    1 
ATOM   1841 C  CB   . TYR   A 1 237 ? -0.524  6.456  12.310  1.00 39.01  ? 237 TYR   A CB   1 
ATOM   1842 C  CG   . TYR   A 1 237 ? -0.623  5.099  12.971  1.00 46.25  ? 237 TYR   A CG   1 
ATOM   1843 C  CD1  . TYR   A 1 237 ? 0.453   4.225  12.969  1.00 41.95  ? 237 TYR   A CD1  1 
ATOM   1844 C  CD2  . TYR   A 1 237 ? -1.810  4.684  13.570  1.00 40.51  ? 237 TYR   A CD2  1 
ATOM   1845 C  CE1  . TYR   A 1 237 ? 0.357   2.977  13.556  1.00 49.31  ? 237 TYR   A CE1  1 
ATOM   1846 C  CE2  . TYR   A 1 237 ? -1.916  3.445  14.155  1.00 45.85  ? 237 TYR   A CE2  1 
ATOM   1847 C  CZ   . TYR   A 1 237 ? -0.830  2.596  14.150  1.00 48.19  ? 237 TYR   A CZ   1 
ATOM   1848 O  OH   . TYR   A 1 237 ? -0.933  1.357  14.737  1.00 52.94  ? 237 TYR   A OH   1 
ATOM   1849 N  N    . ASN   A 1 238 ? -0.723  8.070  9.034   1.00 40.50  ? 238 ASN   A N    1 
ATOM   1850 C  CA   . ASN   A 1 238 ? -1.109  9.333  8.398   1.00 36.56  ? 238 ASN   A CA   1 
ATOM   1851 C  C    . ASN   A 1 238 ? -0.648  10.538 9.220   1.00 38.88  ? 238 ASN   A C    1 
ATOM   1852 O  O    . ASN   A 1 238 ? -1.374  11.522 9.378   1.00 37.84  ? 238 ASN   A O    1 
ATOM   1853 C  CB   . ASN   A 1 238 ? -2.619  9.398  8.147   1.00 37.98  ? 238 ASN   A CB   1 
ATOM   1854 C  CG   . ASN   A 1 238 ? -3.003  10.531 7.201   1.00 43.84  ? 238 ASN   A CG   1 
ATOM   1855 O  OD1  . ASN   A 1 238 ? -2.200  10.958 6.371   1.00 43.56  ? 238 ASN   A OD1  1 
ATOM   1856 N  ND2  . ASN   A 1 238 ? -4.222  11.035 7.341   1.00 44.94  ? 238 ASN   A ND2  1 
ATOM   1857 N  N    . TYR   A 1 239 ? 0.578   10.472 9.722   1.00 38.98  ? 239 TYR   A N    1 
ATOM   1858 C  CA   . TYR   A 1 239 ? 1.197   11.565 10.453  1.00 37.66  ? 239 TYR   A CA   1 
ATOM   1859 C  C    . TYR   A 1 239 ? 2.232   12.201 9.533   1.00 39.87  ? 239 TYR   A C    1 
ATOM   1860 O  O    . TYR   A 1 239 ? 2.874   11.504 8.743   1.00 40.39  ? 239 TYR   A O    1 
ATOM   1861 C  CB   . TYR   A 1 239 ? 1.867   11.043 11.741  1.00 33.41  ? 239 TYR   A CB   1 
ATOM   1862 C  CG   . TYR   A 1 239 ? 1.041   11.118 13.021  1.00 35.09  ? 239 TYR   A CG   1 
ATOM   1863 C  CD1  . TYR   A 1 239 ? -0.178  10.459 13.124  1.00 36.15  ? 239 TYR   A CD1  1 
ATOM   1864 C  CD2  . TYR   A 1 239 ? 1.511   11.793 14.146  1.00 34.86  ? 239 TYR   A CD2  1 
ATOM   1865 C  CE1  . TYR   A 1 239 ? -0.933  10.505 14.290  1.00 35.89  ? 239 TYR   A CE1  1 
ATOM   1866 C  CE2  . TYR   A 1 239 ? 0.764   11.835 15.331  1.00 33.47  ? 239 TYR   A CE2  1 
ATOM   1867 C  CZ   . TYR   A 1 239 ? -0.452  11.189 15.393  1.00 35.02  ? 239 TYR   A CZ   1 
ATOM   1868 O  OH   . TYR   A 1 239 ? -1.204  11.232 16.546  1.00 33.85  ? 239 TYR   A OH   1 
ATOM   1869 N  N    . GLU   A 1 240 ? 2.384   13.519 9.614   1.00 38.52  ? 240 GLU   A N    1 
ATOM   1870 C  CA   . GLU   A 1 240 ? 3.435   14.186 8.852   1.00 37.87  ? 240 GLU   A CA   1 
ATOM   1871 C  C    . GLU   A 1 240 ? 4.799   13.606 9.223   1.00 41.46  ? 240 GLU   A C    1 
ATOM   1872 O  O    . GLU   A 1 240 ? 5.054   13.324 10.404  1.00 35.98  ? 240 GLU   A O    1 
ATOM   1873 C  CB   . GLU   A 1 240 ? 3.421   15.694 9.128   1.00 41.14  ? 240 GLU   A CB   1 
ATOM   1874 C  CG   . GLU   A 1 240 ? 3.730   16.582 7.933   1.00 55.59  ? 240 GLU   A CG   1 
ATOM   1875 C  CD   . GLU   A 1 240 ? 2.499   16.949 7.131   1.00 60.33  ? 240 GLU   A CD   1 
ATOM   1876 O  OE1  . GLU   A 1 240 ? 2.135   16.186 6.209   1.00 56.31  ? 240 GLU   A OE1  1 
ATOM   1877 O  OE2  . GLU   A 1 240 ? 1.896   18.009 7.423   1.00 69.85  ? 240 GLU   A OE2  1 
ATOM   1878 N  N    . PRO   A 1 241 ? 5.694   13.408 8.252   1.00 40.84  ? 241 PRO   A N    1 
ATOM   1879 C  CA   . PRO   A 1 241 ? 7.043   12.923 8.576   1.00 43.20  ? 241 PRO   A CA   1 
ATOM   1880 C  C    . PRO   A 1 241 ? 7.754   13.937 9.457   1.00 47.73  ? 241 PRO   A C    1 
ATOM   1881 O  O    . PRO   A 1 241 ? 7.713   15.136 9.185   1.00 45.49  ? 241 PRO   A O    1 
ATOM   1882 C  CB   . PRO   A 1 241 ? 7.725   12.841 7.206   1.00 49.46  ? 241 PRO   A CB   1 
ATOM   1883 C  CG   . PRO   A 1 241 ? 6.608   12.624 6.236   1.00 43.59  ? 241 PRO   A CG   1 
ATOM   1884 C  CD   . PRO   A 1 241 ? 5.446   13.428 6.795   1.00 45.87  ? 241 PRO   A CD   1 
ATOM   1885 N  N    . LEU   A 1 242 ? 8.431   13.465 10.502  1.00 47.80  ? 242 LEU   A N    1 
ATOM   1886 C  CA   . LEU   A 1 242 ? 9.195   14.369 11.360  1.00 49.91  ? 242 LEU   A CA   1 
ATOM   1887 C  C    . LEU   A 1 242 ? 10.555  14.669 10.736  1.00 45.78  ? 242 LEU   A C    1 
ATOM   1888 O  O    . LEU   A 1 242 ? 11.253  13.754 10.294  1.00 47.87  ? 242 LEU   A O    1 
ATOM   1889 C  CB   . LEU   A 1 242 ? 9.396   13.761 12.751  1.00 41.04  ? 242 LEU   A CB   1 
ATOM   1890 C  CG   . LEU   A 1 242 ? 9.850   14.705 13.878  1.00 42.69  ? 242 LEU   A CG   1 
ATOM   1891 C  CD1  . LEU   A 1 242 ? 8.857   15.854 14.074  1.00 40.26  ? 242 LEU   A CD1  1 
ATOM   1892 C  CD2  . LEU   A 1 242 ? 10.103  13.960 15.189  1.00 49.72  ? 242 LEU   A CD2  1 
ATOM   1893 N  N    . THR   A 1 243 ? 10.954  15.937 10.739  1.00 45.92  ? 243 THR   A N    1 
ATOM   1894 C  CA   . THR   A 1 243 ? 12.228  16.350 10.164  1.00 53.80  ? 243 THR   A CA   1 
ATOM   1895 C  C    . THR   A 1 243 ? 13.201  16.765 11.259  1.00 53.41  ? 243 THR   A C    1 
ATOM   1896 O  O    . THR   A 1 243 ? 12.825  16.962 12.420  1.00 48.33  ? 243 THR   A O    1 
ATOM   1897 C  CB   . THR   A 1 243 ? 12.034  17.509 9.174   1.00 51.70  ? 243 THR   A CB   1 
ATOM   1898 O  OG1  . THR   A 1 243 ? 11.744  18.710 9.899   1.00 50.30  ? 243 THR   A OG1  1 
ATOM   1899 C  CG2  . THR   A 1 243 ? 10.889  17.212 8.233   1.00 45.59  ? 243 THR   A CG2  1 
ATOM   1900 N  N    . GLN   A 1 244 ? 14.473  16.910 10.872  1.00 47.92  ? 244 GLN   A N    1 
ATOM   1901 C  CA   . GLN   A 1 244 ? 15.476  17.389 11.818  1.00 52.95  ? 244 GLN   A CA   1 
ATOM   1902 C  C    . GLN   A 1 244 ? 15.178  18.807 12.288  1.00 51.11  ? 244 GLN   A C    1 
ATOM   1903 O  O    . GLN   A 1 244 ? 15.521  19.168 13.419  1.00 49.05  ? 244 GLN   A O    1 
ATOM   1904 C  CB   . GLN   A 1 244 ? 16.876  17.319 11.203  1.00 51.93  ? 244 GLN   A CB   1 
ATOM   1905 C  CG   . GLN   A 1 244 ? 17.981  17.689 12.183  1.00 52.65  ? 244 GLN   A CG   1 
ATOM   1906 C  CD   . GLN   A 1 244 ? 18.028  16.763 13.384  1.00 54.63  ? 244 GLN   A CD   1 
ATOM   1907 O  OE1  . GLN   A 1 244 ? 17.881  15.548 13.251  1.00 56.22  ? 244 GLN   A OE1  1 
ATOM   1908 N  NE2  . GLN   A 1 244 ? 18.237  17.334 14.566  1.00 54.69  ? 244 GLN   A NE2  1 
ATOM   1909 N  N    . ASP   A 1 245 ? 14.547  19.632 11.447  1.00 49.83  ? 245 ASP   A N    1 
ATOM   1910 C  CA   . ASP   A 1 245 ? 14.175  20.963 11.918  1.00 50.49  ? 245 ASP   A CA   1 
ATOM   1911 C  C    . ASP   A 1 245 ? 13.114  20.879 13.008  1.00 48.93  ? 245 ASP   A C    1 
ATOM   1912 O  O    . ASP   A 1 245 ? 13.157  21.631 13.987  1.00 45.76  ? 245 ASP   A O    1 
ATOM   1913 C  CB   . ASP   A 1 245 ? 13.687  21.831 10.762  1.00 55.95  ? 245 ASP   A CB   1 
ATOM   1914 C  CG   . ASP   A 1 245 ? 13.368  23.244 11.207  1.00 63.89  ? 245 ASP   A CG   1 
ATOM   1915 O  OD1  . ASP   A 1 245 ? 14.206  23.836 11.924  1.00 53.53  ? 245 ASP   A OD1  1 
ATOM   1916 O  OD2  . ASP   A 1 245 ? 12.277  23.754 10.863  1.00 75.39  ? 245 ASP   A OD2  1 
ATOM   1917 N  N    . HIS   A 1 246 ? 12.158  19.965 12.857  1.00 45.63  ? 246 HIS   A N    1 
ATOM   1918 C  CA   . HIS   A 1 246 ? 11.181  19.728 13.915  1.00 44.05  ? 246 HIS   A CA   1 
ATOM   1919 C  C    . HIS   A 1 246 ? 11.856  19.297 15.210  1.00 45.97  ? 246 HIS   A C    1 
ATOM   1920 O  O    . HIS   A 1 246 ? 11.584  19.852 16.283  1.00 43.24  ? 246 HIS   A O    1 
ATOM   1921 C  CB   . HIS   A 1 246 ? 10.175  18.690 13.437  1.00 41.82  ? 246 HIS   A CB   1 
ATOM   1922 C  CG   . HIS   A 1 246 ? 9.310   19.184 12.323  1.00 44.40  ? 246 HIS   A CG   1 
ATOM   1923 N  ND1  . HIS   A 1 246 ? 8.737   18.351 11.386  1.00 42.99  ? 246 HIS   A ND1  1 
ATOM   1924 C  CD2  . HIS   A 1 246 ? 8.890   20.437 12.022  1.00 41.60  ? 246 HIS   A CD2  1 
ATOM   1925 C  CE1  . HIS   A 1 246 ? 8.007   19.073 10.553  1.00 40.54  ? 246 HIS   A CE1  1 
ATOM   1926 N  NE2  . HIS   A 1 246 ? 8.077   20.340 10.919  1.00 46.27  ? 246 HIS   A NE2  1 
ATOM   1927 N  N    . VAL   A 1 247 ? 12.742  18.302 15.132  1.00 46.04  ? 247 VAL   A N    1 
ATOM   1928 C  CA   . VAL   A 1 247 ? 13.511  17.905 16.308  1.00 40.82  ? 247 VAL   A CA   1 
ATOM   1929 C  C    . VAL   A 1 247 ? 14.190  19.121 16.922  1.00 40.92  ? 247 VAL   A C    1 
ATOM   1930 O  O    . VAL   A 1 247 ? 14.177  19.317 18.143  1.00 40.48  ? 247 VAL   A O    1 
ATOM   1931 C  CB   . VAL   A 1 247 ? 14.527  16.817 15.921  1.00 46.64  ? 247 VAL   A CB   1 
ATOM   1932 C  CG1  . VAL   A 1 247 ? 15.533  16.619 17.025  1.00 47.00  ? 247 VAL   A CG1  1 
ATOM   1933 C  CG2  . VAL   A 1 247 ? 13.804  15.528 15.570  1.00 45.12  ? 247 VAL   A CG2  1 
ATOM   1934 N  N    . ASP   A 1 248 ? 14.774  19.972 16.077  1.00 46.77  ? 248 ASP   A N    1 
ATOM   1935 C  CA   . ASP   A 1 248 ? 15.470  21.155 16.570  1.00 47.26  ? 248 ASP   A CA   1 
ATOM   1936 C  C    . ASP   A 1 248 ? 14.518  22.070 17.329  1.00 39.56  ? 248 ASP   A C    1 
ATOM   1937 O  O    . ASP   A 1 248 ? 14.823  22.529 18.435  1.00 49.25  ? 248 ASP   A O    1 
ATOM   1938 C  CB   . ASP   A 1 248 ? 16.110  21.900 15.396  1.00 52.25  ? 248 ASP   A CB   1 
ATOM   1939 C  CG   . ASP   A 1 248 ? 17.365  21.215 14.880  1.00 56.84  ? 248 ASP   A CG   1 
ATOM   1940 O  OD1  . ASP   A 1 248 ? 17.994  20.454 15.646  1.00 58.71  ? 248 ASP   A OD1  1 
ATOM   1941 O  OD2  . ASP   A 1 248 ? 17.717  21.433 13.701  1.00 55.35  ? 248 ASP   A OD2  1 
ATOM   1942 N  N    . ILE   A 1 249 ? 13.352  22.345 16.742  1.00 45.51  ? 249 ILE   A N    1 
ATOM   1943 C  CA   . ILE   A 1 249 ? 12.386  23.273 17.326  1.00 37.78  ? 249 ILE   A CA   1 
ATOM   1944 C  C    . ILE   A 1 249 ? 11.893  22.762 18.667  1.00 41.63  ? 249 ILE   A C    1 
ATOM   1945 O  O    . ILE   A 1 249 ? 11.503  23.550 19.542  1.00 42.12  ? 249 ILE   A O    1 
ATOM   1946 C  CB   . ILE   A 1 249 ? 11.216  23.495 16.345  1.00 37.84  ? 249 ILE   A CB   1 
ATOM   1947 C  CG1  . ILE   A 1 249 ? 11.647  24.388 15.175  1.00 47.63  ? 249 ILE   A CG1  1 
ATOM   1948 C  CG2  . ILE   A 1 249 ? 10.032  24.088 17.057  1.00 38.25  ? 249 ILE   A CG2  1 
ATOM   1949 C  CD1  . ILE   A 1 249 ? 10.983  24.030 13.854  1.00 46.25  ? 249 ILE   A CD1  1 
ATOM   1950 N  N    . LEU   A 1 250 ? 11.884  21.446 18.849  1.00 37.88  ? 250 LEU   A N    1 
ATOM   1951 C  CA   . LEU   A 1 250 ? 11.476  20.846 20.113  1.00 40.50  ? 250 LEU   A CA   1 
ATOM   1952 C  C    . LEU   A 1 250 ? 12.595  20.834 21.149  1.00 44.49  ? 250 LEU   A C    1 
ATOM   1953 O  O    . LEU   A 1 250 ? 12.363  20.392 22.277  1.00 39.21  ? 250 LEU   A O    1 
ATOM   1954 C  CB   . LEU   A 1 250 ? 10.963  19.424 19.858  1.00 37.58  ? 250 LEU   A CB   1 
ATOM   1955 C  CG   . LEU   A 1 250 ? 9.682   19.352 19.026  1.00 32.94  ? 250 LEU   A CG   1 
ATOM   1956 C  CD1  . LEU   A 1 250 ? 9.367   17.937 18.577  1.00 29.49  ? 250 LEU   A CD1  1 
ATOM   1957 C  CD2  . LEU   A 1 250 ? 8.514   19.927 19.843  1.00 34.46  ? 250 LEU   A CD2  1 
ATOM   1958 N  N    . GLY   A 1 251 ? 13.785  21.325 20.795  1.00 43.83  ? 251 GLY   A N    1 
ATOM   1959 C  CA   . GLY   A 1 251 ? 14.924  21.349 21.681  1.00 41.04  ? 251 GLY   A CA   1 
ATOM   1960 C  C    . GLY   A 1 251 ? 14.613  21.928 23.044  1.00 39.03  ? 251 GLY   A C    1 
ATOM   1961 O  O    . GLY   A 1 251 ? 14.812  21.278 24.069  1.00 43.27  ? 251 GLY   A O    1 
ATOM   1962 N  N    . PRO   A 1 252 ? 14.124  23.169 23.084  1.00 45.12  ? 252 PRO   A N    1 
ATOM   1963 C  CA   . PRO   A 1 252 ? 13.839  23.799 24.387  1.00 44.07  ? 252 PRO   A CA   1 
ATOM   1964 C  C    . PRO   A 1 252 ? 12.940  22.978 25.305  1.00 42.19  ? 252 PRO   A C    1 
ATOM   1965 O  O    . PRO   A 1 252 ? 13.250  22.812 26.495  1.00 45.20  ? 252 PRO   A O    1 
ATOM   1966 C  CB   . PRO   A 1 252 ? 13.182  25.119 23.976  1.00 42.35  ? 252 PRO   A CB   1 
ATOM   1967 C  CG   . PRO   A 1 252 ? 13.831  25.451 22.682  1.00 45.68  ? 252 PRO   A CG   1 
ATOM   1968 C  CD   . PRO   A 1 252 ? 14.059  24.136 21.975  1.00 46.70  ? 252 PRO   A CD   1 
ATOM   1969 N  N    . LEU   A 1 253 ? 11.806  22.496 24.796  1.00 37.82  ? 253 LEU   A N    1 
ATOM   1970 C  CA   . LEU   A 1 253 ? 10.927  21.653 25.607  1.00 35.06  ? 253 LEU   A CA   1 
ATOM   1971 C  C    . LEU   A 1 253 ? 11.636  20.384 26.075  1.00 33.11  ? 253 LEU   A C    1 
ATOM   1972 O  O    . LEU   A 1 253 ? 11.461  19.945 27.223  1.00 34.03  ? 253 LEU   A O    1 
ATOM   1973 C  CB   . LEU   A 1 253 ? 9.674   21.321 24.796  1.00 30.78  ? 253 LEU   A CB   1 
ATOM   1974 C  CG   . LEU   A 1 253 ? 8.771   22.526 24.551  1.00 32.88  ? 253 LEU   A CG   1 
ATOM   1975 C  CD1  . LEU   A 1 253 ? 7.575   22.154 23.669  1.00 28.41  ? 253 LEU   A CD1  1 
ATOM   1976 C  CD2  . LEU   A 1 253 ? 8.288   23.043 25.892  1.00 29.07  ? 253 LEU   A CD2  1 
ATOM   1977 N  N    . SER   A 1 254 ? 12.430  19.777 25.193  1.00 35.44  ? 254 SER   A N    1 
ATOM   1978 C  CA   . SER   A 1 254 ? 13.241  18.624 25.573  1.00 35.43  ? 254 SER   A CA   1 
ATOM   1979 C  C    . SER   A 1 254 ? 14.174  18.957 26.733  1.00 43.79  ? 254 SER   A C    1 
ATOM   1980 O  O    . SER   A 1 254 ? 14.326  18.164 27.675  1.00 44.02  ? 254 SER   A O    1 
ATOM   1981 C  CB   . SER   A 1 254 ? 14.051  18.148 24.365  1.00 35.11  ? 254 SER   A CB   1 
ATOM   1982 O  OG   . SER   A 1 254 ? 14.646  16.886 24.622  1.00 43.33  ? 254 SER   A OG   1 
ATOM   1983 N  N    . ALA   A 1 255 ? 14.808  20.130 26.679  1.00 43.01  ? 255 ALA   A N    1 
ATOM   1984 C  CA   . ALA   A 1 255 ? 15.737  20.528 27.731  1.00 44.29  ? 255 ALA   A CA   1 
ATOM   1985 C  C    . ALA   A 1 255 ? 14.998  20.735 29.040  1.00 44.15  ? 255 ALA   A C    1 
ATOM   1986 O  O    . ALA   A 1 255 ? 15.394  20.205 30.083  1.00 47.34  ? 255 ALA   A O    1 
ATOM   1987 C  CB   . ALA   A 1 255 ? 16.485  21.799 27.318  1.00 43.27  ? 255 ALA   A CB   1 
ATOM   1988 N  N    . GLN   A 1 256 ? 13.884  21.464 28.992  1.00 39.07  ? 256 GLN   A N    1 
ATOM   1989 C  CA   . GLN   A 1 256 ? 13.189  21.795 30.226  1.00 43.57  ? 256 GLN   A CA   1 
ATOM   1990 C  C    . GLN   A 1 256 ? 12.559  20.569 30.871  1.00 43.62  ? 256 GLN   A C    1 
ATOM   1991 O  O    . GLN   A 1 256 ? 12.385  20.551 32.095  1.00 51.26  ? 256 GLN   A O    1 
ATOM   1992 C  CB   . GLN   A 1 256 ? 12.151  22.891 29.977  1.00 43.83  ? 256 GLN   A CB   1 
ATOM   1993 C  CG   . GLN   A 1 256 ? 10.911  22.833 30.862  1.00 41.30  ? 256 GLN   A CG   1 
ATOM   1994 C  CD   . GLN   A 1 256 ? 9.826   23.803 30.423  1.00 49.88  ? 256 GLN   A CD   1 
ATOM   1995 O  OE1  . GLN   A 1 256 ? 9.745   24.179 29.251  1.00 50.56  ? 256 GLN   A OE1  1 
ATOM   1996 N  NE2  . GLN   A 1 256 ? 8.976   24.205 31.367  1.00 48.40  ? 256 GLN   A NE2  1 
ATOM   1997 N  N    . THR   A 1 257 ? 12.242  19.533 30.090  1.00 42.78  ? 257 THR   A N    1 
ATOM   1998 C  CA   . THR   A 1 257 ? 11.722  18.300 30.671  1.00 35.03  ? 257 THR   A CA   1 
ATOM   1999 C  C    . THR   A 1 257 ? 12.777  17.215 30.848  1.00 38.38  ? 257 THR   A C    1 
ATOM   2000 O  O    . THR   A 1 257 ? 12.539  16.268 31.606  1.00 38.53  ? 257 THR   A O    1 
ATOM   2001 C  CB   . THR   A 1 257 ? 10.582  17.733 29.813  1.00 37.55  ? 257 THR   A CB   1 
ATOM   2002 O  OG1  . THR   A 1 257 ? 11.096  17.358 28.524  1.00 35.04  ? 257 THR   A OG1  1 
ATOM   2003 C  CG2  . THR   A 1 257 ? 9.461   18.754 29.669  1.00 31.30  ? 257 THR   A CG2  1 
ATOM   2004 N  N    . GLY   A 1 258 ? 13.911  17.315 30.157  1.00 38.11  ? 258 GLY   A N    1 
ATOM   2005 C  CA   . GLY   A 1 258 ? 14.911  16.270 30.221  1.00 43.10  ? 258 GLY   A CA   1 
ATOM   2006 C  C    . GLY   A 1 258 ? 14.534  14.996 29.504  1.00 44.65  ? 258 GLY   A C    1 
ATOM   2007 O  O    . GLY   A 1 258 ? 15.106  13.943 29.794  1.00 43.40  ? 258 GLY   A O    1 
ATOM   2008 N  N    . ILE   A 1 259 ? 13.566  15.050 28.595  1.00 36.76  ? 259 ILE   A N    1 
ATOM   2009 C  CA   . ILE   A 1 259 ? 13.187  13.910 27.770  1.00 38.35  ? 259 ILE   A CA   1 
ATOM   2010 C  C    . ILE   A 1 259 ? 13.653  14.215 26.355  1.00 36.43  ? 259 ILE   A C    1 
ATOM   2011 O  O    . ILE   A 1 259 ? 13.181  15.176 25.736  1.00 35.80  ? 259 ILE   A O    1 
ATOM   2012 C  CB   . ILE   A 1 259 ? 11.671  13.643 27.802  1.00 38.49  ? 259 ILE   A CB   1 
ATOM   2013 C  CG1  . ILE   A 1 259 ? 11.237  13.105 29.167  1.00 41.39  ? 259 ILE   A CG1  1 
ATOM   2014 C  CG2  . ILE   A 1 259 ? 11.273  12.658 26.713  1.00 32.24  ? 259 ILE   A CG2  1 
ATOM   2015 C  CD1  . ILE   A 1 259 ? 10.129  13.888 29.782  1.00 41.48  ? 259 ILE   A CD1  1 
ATOM   2016 N  N    . ALA   A 1 260 ? 14.593  13.419 25.851  1.00 36.71  ? 260 ALA   A N    1 
ATOM   2017 C  CA   . ALA   A 1 260 ? 15.106  13.648 24.506  1.00 36.76  ? 260 ALA   A CA   1 
ATOM   2018 C  C    . ALA   A 1 260 ? 13.983  13.522 23.480  1.00 36.34  ? 260 ALA   A C    1 
ATOM   2019 O  O    . ALA   A 1 260 ? 13.017  12.780 23.676  1.00 34.72  ? 260 ALA   A O    1 
ATOM   2020 C  CB   . ALA   A 1 260 ? 16.229  12.655 24.194  1.00 37.96  ? 260 ALA   A CB   1 
ATOM   2021 N  N    . VAL   A 1 261 ? 14.113  14.256 22.368  1.00 32.02  ? 261 VAL   A N    1 
ATOM   2022 C  CA   . VAL   A 1 261 ? 13.031  14.282 21.385  1.00 33.94  ? 261 VAL   A CA   1 
ATOM   2023 C  C    . VAL   A 1 261 ? 12.744  12.879 20.862  1.00 34.52  ? 261 VAL   A C    1 
ATOM   2024 O  O    . VAL   A 1 261 ? 11.586  12.464 20.762  1.00 30.46  ? 261 VAL   A O    1 
ATOM   2025 C  CB   . VAL   A 1 261 ? 13.358  15.260 20.241  1.00 35.39  ? 261 VAL   A CB   1 
ATOM   2026 C  CG1  . VAL   A 1 261 ? 12.397  15.034 19.086  1.00 32.58  ? 261 VAL   A CG1  1 
ATOM   2027 C  CG2  . VAL   A 1 261 ? 13.301  16.694 20.731  1.00 36.09  ? 261 VAL   A CG2  1 
ATOM   2028 N  N    . LEU   A 1 262 ? 13.787  12.113 20.535  1.00 37.35  ? 262 LEU   A N    1 
ATOM   2029 C  CA   . LEU   A 1 262 ? 13.553  10.772 20.002  1.00 37.04  ? 262 LEU   A CA   1 
ATOM   2030 C  C    . LEU   A 1 262 ? 12.994  9.815  21.057  1.00 33.57  ? 262 LEU   A C    1 
ATOM   2031 O  O    . LEU   A 1 262 ? 12.279  8.863  20.710  1.00 39.80  ? 262 LEU   A O    1 
ATOM   2032 C  CB   . LEU   A 1 262 ? 14.848  10.233 19.398  1.00 41.95  ? 262 LEU   A CB   1 
ATOM   2033 C  CG   . LEU   A 1 262 ? 15.269  10.980 18.133  1.00 46.86  ? 262 LEU   A CG   1 
ATOM   2034 C  CD1  . LEU   A 1 262 ? 16.690  10.581 17.735  1.00 51.73  ? 262 LEU   A CD1  1 
ATOM   2035 C  CD2  . LEU   A 1 262 ? 14.296  10.750 16.985  1.00 52.34  ? 262 LEU   A CD2  1 
ATOM   2036 N  N    . ASP   A 1 263 ? 13.262  10.065 22.341  1.00 34.22  ? 263 ASP   A N    1 
ATOM   2037 C  CA   . ASP   A 1 263 ? 12.554  9.341  23.399  1.00 38.61  ? 263 ASP   A CA   1 
ATOM   2038 C  C    . ASP   A 1 263 ? 11.055  9.623  23.353  1.00 36.06  ? 263 ASP   A C    1 
ATOM   2039 O  O    . ASP   A 1 263 ? 10.218  8.703  23.443  1.00 34.31  ? 263 ASP   A O    1 
ATOM   2040 C  CB   . ASP   A 1 263 ? 13.116  9.729  24.768  1.00 38.42  ? 263 ASP   A CB   1 
ATOM   2041 C  CG   . ASP   A 1 263 ? 14.426  9.040  25.084  1.00 54.35  ? 263 ASP   A CG   1 
ATOM   2042 O  OD1  . ASP   A 1 263 ? 15.290  8.959  24.188  1.00 53.92  ? 263 ASP   A OD1  1 
ATOM   2043 O  OD2  . ASP   A 1 263 ? 14.581  8.564  26.232  1.00 52.48  ? 263 ASP   A OD2  1 
ATOM   2044 N  N    . MET   A 1 264 ? 10.688  10.900 23.224  1.00 30.76  ? 264 MET   A N    1 
ATOM   2045 C  CA   . MET   A 1 264 ? 9.266   11.191 23.195  1.00 27.81  ? 264 MET   A CA   1 
ATOM   2046 C  C    . MET   A 1 264 ? 8.645   10.597 21.928  1.00 31.51  ? 264 MET   A C    1 
ATOM   2047 O  O    . MET   A 1 264 ? 7.481   10.179 21.935  1.00 33.79  ? 264 MET   A O    1 
ATOM   2048 C  CB   . MET   A 1 264 ? 9.027   12.709 23.267  1.00 25.97  ? 264 MET   A CB   1 
ATOM   2049 C  CG   . MET   A 1 264 ? 7.530   13.033 23.314  1.00 24.66  ? 264 MET   A CG   1 
ATOM   2050 S  SD   . MET   A 1 264 ? 6.989   12.551 25.006  1.00 26.79  ? 264 MET   A SD   1 
ATOM   2051 C  CE   . MET   A 1 264 ? 7.667   13.917 25.930  1.00 25.51  ? 264 MET   A CE   1 
ATOM   2052 N  N    . CYS   A 1 265 ? 9.406   10.554 20.823  1.00 33.95  ? 265 CYS   A N    1 
ATOM   2053 C  CA   . CYS   A 1 265 ? 8.924   9.862  19.628  1.00 29.88  ? 265 CYS   A CA   1 
ATOM   2054 C  C    . CYS   A 1 265 ? 8.670   8.382  19.886  1.00 35.84  ? 265 CYS   A C    1 
ATOM   2055 O  O    . CYS   A 1 265 ? 7.707   7.813  19.354  1.00 30.98  ? 265 CYS   A O    1 
ATOM   2056 C  CB   . CYS   A 1 265 ? 9.896   10.032 18.453  1.00 35.14  ? 265 CYS   A CB   1 
ATOM   2057 S  SG   . CYS   A 1 265 ? 10.126  11.734 17.843  1.00 34.58  ? 265 CYS   A SG   1 
ATOM   2058 N  N    . ALA   A 1 266 ? 9.529   7.730  20.682  1.00 35.57  ? 266 ALA   A N    1 
ATOM   2059 C  CA   . ALA   A 1 266 ? 9.246   6.349  21.069  1.00 36.61  ? 266 ALA   A CA   1 
ATOM   2060 C  C    . ALA   A 1 266 ? 7.919   6.250  21.820  1.00 38.65  ? 266 ALA   A C    1 
ATOM   2061 O  O    . ALA   A 1 266 ? 7.115   5.329  21.583  1.00 37.52  ? 266 ALA   A O    1 
ATOM   2062 C  CB   . ALA   A 1 266 ? 10.391  5.799  21.919  1.00 37.14  ? 266 ALA   A CB   1 
ATOM   2063 N  N    . SER   A 1 267 ? 7.670   7.202  22.727  1.00 30.90  ? 267 SER   A N    1 
ATOM   2064 C  CA   . SER   A 1 267 ? 6.374   7.248  23.407  1.00 31.92  ? 267 SER   A CA   1 
ATOM   2065 C  C    . SER   A 1 267 ? 5.223   7.366  22.412  1.00 31.16  ? 267 SER   A C    1 
ATOM   2066 O  O    . SER   A 1 267 ? 4.201   6.675  22.527  1.00 33.20  ? 267 SER   A O    1 
ATOM   2067 C  CB   . SER   A 1 267 ? 6.327   8.419  24.389  1.00 37.17  ? 267 SER   A CB   1 
ATOM   2068 O  OG   . SER   A 1 267 ? 7.076   8.131  25.537  1.00 35.52  ? 267 SER   A OG   1 
ATOM   2069 N  N    . LEU   A 1 268 ? 5.355   8.284  21.455  1.00 30.22  ? 268 LEU   A N    1 
ATOM   2070 C  CA   . LEU   A 1 268 ? 4.287   8.506  20.487  1.00 30.85  ? 268 LEU   A CA   1 
ATOM   2071 C  C    . LEU   A 1 268 ? 4.047   7.261  19.636  1.00 34.55  ? 268 LEU   A C    1 
ATOM   2072 O  O    . LEU   A 1 268 ? 2.899   6.914  19.338  1.00 31.59  ? 268 LEU   A O    1 
ATOM   2073 C  CB   . LEU   A 1 268 ? 4.624   9.716  19.611  1.00 26.70  ? 268 LEU   A CB   1 
ATOM   2074 C  CG   . LEU   A 1 268 ? 3.607   10.078 18.529  1.00 29.79  ? 268 LEU   A CG   1 
ATOM   2075 C  CD1  . LEU   A 1 268 ? 2.183   10.164 19.089  1.00 26.65  ? 268 LEU   A CD1  1 
ATOM   2076 C  CD2  . LEU   A 1 268 ? 3.976   11.402 17.867  1.00 29.67  ? 268 LEU   A CD2  1 
ATOM   2077 N  N    . LYS   A 1 269 ? 5.118   6.582  19.228  1.00 34.80  ? 269 LYS   A N    1 
ATOM   2078 C  CA   . LYS   A 1 269 ? 4.953   5.335  18.487  1.00 36.80  ? 269 LYS   A CA   1 
ATOM   2079 C  C    . LYS   A 1 269 ? 4.125   4.337  19.284  1.00 35.15  ? 269 LYS   A C    1 
ATOM   2080 O  O    . LYS   A 1 269 ? 3.170   3.744  18.762  1.00 36.00  ? 269 LYS   A O    1 
ATOM   2081 C  CB   . LYS   A 1 269 ? 6.315   4.743  18.131  1.00 46.30  ? 269 LYS   A CB   1 
ATOM   2082 C  CG   . LYS   A 1 269 ? 6.233   3.390  17.432  1.00 52.53  ? 269 LYS   A CG   1 
ATOM   2083 C  CD   . LYS   A 1 269 ? 7.602   2.726  17.324  1.00 58.40  ? 269 LYS   A CD   1 
ATOM   2084 C  CE   . LYS   A 1 269 ? 7.927   2.374  15.875  1.00 67.31  ? 269 LYS   A CE   1 
ATOM   2085 N  NZ   . LYS   A 1 269 ? 8.749   1.138  15.714  1.00 69.23  ? 269 LYS   A NZ   1 
ATOM   2086 N  N    . GLU   A 1 270 ? 4.482   4.131  20.559  1.00 36.26  ? 270 GLU   A N    1 
ATOM   2087 C  CA   . GLU   A 1 270 ? 3.678   3.237  21.392  1.00 41.38  ? 270 GLU   A CA   1 
ATOM   2088 C  C    . GLU   A 1 270 ? 2.227   3.689  21.473  1.00 41.38  ? 270 GLU   A C    1 
ATOM   2089 O  O    . GLU   A 1 270 ? 1.310   2.860  21.470  1.00 38.47  ? 270 GLU   A O    1 
ATOM   2090 C  CB   . GLU   A 1 270 ? 4.280   3.115  22.794  1.00 41.86  ? 270 GLU   A CB   1 
ATOM   2091 C  CG   . GLU   A 1 270 ? 5.596   2.390  22.783  1.00 59.24  ? 270 GLU   A CG   1 
ATOM   2092 C  CD   . GLU   A 1 270 ? 5.495   1.090  22.006  1.00 72.75  ? 270 GLU   A CD   1 
ATOM   2093 O  OE1  . GLU   A 1 270 ? 6.358   0.840  21.134  1.00 69.05  ? 270 GLU   A OE1  1 
ATOM   2094 O  OE2  . GLU   A 1 270 ? 4.546   0.321  22.273  1.00 71.86  ? 270 GLU   A OE2  1 
ATOM   2095 N  N    . LEU   A 1 271 ? 1.994   4.998  21.571  1.00 34.48  ? 271 LEU   A N    1 
ATOM   2096 C  CA   . LEU   A 1 271 ? 0.619   5.470  21.706  1.00 34.23  ? 271 LEU   A CA   1 
ATOM   2097 C  C    . LEU   A 1 271 ? -0.166  5.219  20.425  1.00 38.69  ? 271 LEU   A C    1 
ATOM   2098 O  O    . LEU   A 1 271 ? -1.364  4.912  20.466  1.00 37.09  ? 271 LEU   A O    1 
ATOM   2099 C  CB   . LEU   A 1 271 ? 0.622   6.959  22.058  1.00 33.94  ? 271 LEU   A CB   1 
ATOM   2100 C  CG   . LEU   A 1 271 ? 0.941   7.338  23.509  1.00 34.54  ? 271 LEU   A CG   1 
ATOM   2101 C  CD1  . LEU   A 1 271 ? 0.906   8.852  23.683  1.00 32.40  ? 271 LEU   A CD1  1 
ATOM   2102 C  CD2  . LEU   A 1 271 ? -0.015  6.671  24.505  1.00 35.53  ? 271 LEU   A CD2  1 
ATOM   2103 N  N    . LEU   A 1 272 ? 0.504   5.326  19.283  1.00 35.50  ? 272 LEU   A N    1 
ATOM   2104 C  CA   . LEU   A 1 272 ? -0.165  5.110  18.007  1.00 38.79  ? 272 LEU   A CA   1 
ATOM   2105 C  C    . LEU   A 1 272 ? -0.452  3.635  17.791  1.00 44.03  ? 272 LEU   A C    1 
ATOM   2106 O  O    . LEU   A 1 272 ? -1.454  3.279  17.162  1.00 45.53  ? 272 LEU   A O    1 
ATOM   2107 C  CB   . LEU   A 1 272 ? 0.697   5.653  16.874  1.00 37.82  ? 272 LEU   A CB   1 
ATOM   2108 C  CG   . LEU   A 1 272 ? 0.714   7.177  16.814  1.00 38.62  ? 272 LEU   A CG   1 
ATOM   2109 C  CD1  . LEU   A 1 272 ? 1.873   7.661  15.966  1.00 39.16  ? 272 LEU   A CD1  1 
ATOM   2110 C  CD2  . LEU   A 1 272 ? -0.616  7.719  16.315  1.00 36.37  ? 272 LEU   A CD2  1 
ATOM   2111 N  N    . GLN   A 1 273 ? 0.409   2.771  18.317  1.00 48.13  ? 273 GLN   A N    1 
ATOM   2112 C  CA   . GLN   A 1 273 ? 0.272   1.337  18.106  1.00 50.51  ? 273 GLN   A CA   1 
ATOM   2113 C  C    . GLN   A 1 273 ? -0.669  0.673  19.106  1.00 54.31  ? 273 GLN   A C    1 
ATOM   2114 O  O    . GLN   A 1 273 ? -1.325  -0.315 18.759  1.00 52.67  ? 273 GLN   A O    1 
ATOM   2115 C  CB   . GLN   A 1 273 ? 1.656   0.695  18.169  1.00 45.00  ? 273 GLN   A CB   1 
ATOM   2116 C  CG   . GLN   A 1 273 ? 2.406   0.817  16.864  1.00 48.61  ? 273 GLN   A CG   1 
ATOM   2117 C  CD   . GLN   A 1 273 ? 3.853   0.392  16.974  1.00 55.08  ? 273 GLN   A CD   1 
ATOM   2118 O  OE1  . GLN   A 1 273 ? 4.583   0.396  15.986  1.00 57.29  ? 273 GLN   A OE1  1 
ATOM   2119 N  NE2  . GLN   A 1 273 ? 4.283   0.039  18.182  1.00 56.89  ? 273 GLN   A NE2  1 
ATOM   2120 N  N    . ASN   A 1 274 ? -0.770  1.199  20.331  1.00 49.70  ? 274 ASN   A N    1 
ATOM   2121 C  CA   . ASN   A 1 274 ? -1.576  0.579  21.375  1.00 51.98  ? 274 ASN   A CA   1 
ATOM   2122 C  C    . ASN   A 1 274 ? -2.741  1.428  21.861  1.00 52.02  ? 274 ASN   A C    1 
ATOM   2123 O  O    . ASN   A 1 274 ? -3.545  0.938  22.665  1.00 50.11  ? 274 ASN   A O    1 
ATOM   2124 C  CB   . ASN   A 1 274 ? -0.697  0.227  22.583  1.00 55.81  ? 274 ASN   A CB   1 
ATOM   2125 C  CG   . ASN   A 1 274 ? 0.483   -0.646 22.207  1.00 65.55  ? 274 ASN   A CG   1 
ATOM   2126 O  OD1  . ASN   A 1 274 ? 1.603   -0.424 22.665  1.00 67.55  ? 274 ASN   A OD1  1 
ATOM   2127 N  ND2  . ASN   A 1 274 ? 0.237   -1.647 21.368  1.00 68.88  ? 274 ASN   A ND2  1 
ATOM   2128 N  N    . GLY   A 1 275 ? -2.863  2.670  21.410  1.00 45.66  ? 275 GLY   A N    1 
ATOM   2129 C  CA   . GLY   A 1 275 ? -3.909  3.516  21.936  1.00 46.97  ? 275 GLY   A CA   1 
ATOM   2130 C  C    . GLY   A 1 275 ? -3.612  3.929  23.368  1.00 43.51  ? 275 GLY   A C    1 
ATOM   2131 O  O    . GLY   A 1 275 ? -2.506  3.784  23.876  1.00 47.90  ? 275 GLY   A O    1 
ATOM   2132 N  N    . MET   A 1 276 ? -4.625  4.427  24.087  1.00 48.69  ? 276 MET   A N    1 
ATOM   2133 C  CA   . MET   A 1 276 ? -4.390  4.974  25.455  1.00 53.24  ? 276 MET   A CA   1 
ATOM   2134 C  C    . MET   A 1 276 ? -4.977  4.095  26.570  1.00 63.02  ? 276 MET   A C    1 
ATOM   2135 O  O    . MET   A 1 276 ? -4.732  4.411  27.743  1.00 55.09  ? 276 MET   A O    1 
ATOM   2136 C  CB   . MET   A 1 276 ? -5.003  6.370  25.591  1.00 51.16  ? 276 MET   A CB   1 
ATOM   2137 C  CG   . MET   A 1 276 ? -4.195  7.452  24.921  1.00 46.60  ? 276 MET   A CG   1 
ATOM   2138 S  SD   . MET   A 1 276 ? -4.846  9.082  25.317  1.00 50.43  ? 276 MET   A SD   1 
ATOM   2139 C  CE   . MET   A 1 276 ? -4.424  9.948  23.808  1.00 38.52  ? 276 MET   A CE   1 
ATOM   2140 N  N    . ASN   A 1 277 ? -5.756  3.072  26.223  1.00 67.88  ? 277 ASN   A N    1 
ATOM   2141 C  CA   . ASN   A 1 277 ? -6.277  2.129  27.253  1.00 71.03  ? 277 ASN   A CA   1 
ATOM   2142 C  C    . ASN   A 1 277 ? -7.103  2.857  28.314  1.00 64.24  ? 277 ASN   A C    1 
ATOM   2143 O  O    . ASN   A 1 277 ? -6.816  2.656  29.502  1.00 68.27  ? 277 ASN   A O    1 
ATOM   2144 C  CB   . ASN   A 1 277 ? -5.144  1.337  27.904  1.00 73.49  ? 277 ASN   A CB   1 
ATOM   2145 C  CG   . ASN   A 1 277 ? -5.624  0.151  28.712  1.00 86.99  ? 277 ASN   A CG   1 
ATOM   2146 O  OD1  . ASN   A 1 277 ? -6.163  -0.804 28.160  1.00 87.64  ? 277 ASN   A OD1  1 
ATOM   2147 N  ND2  . ASN   A 1 277 ? -5.430  0.203  30.019  1.00 87.32  ? 277 ASN   A ND2  1 
ATOM   2148 N  N    . GLY   A 1 278 ? -8.071  3.677  27.908  1.00 60.58  ? 278 GLY   A N    1 
ATOM   2149 C  CA   . GLY   A 1 278 ? -8.984  4.313  28.877  1.00 60.99  ? 278 GLY   A CA   1 
ATOM   2150 C  C    . GLY   A 1 278 ? -8.328  5.403  29.694  1.00 56.45  ? 278 GLY   A C    1 
ATOM   2151 O  O    . GLY   A 1 278 ? -8.938  5.867  30.661  1.00 56.23  ? 278 GLY   A O    1 
ATOM   2152 N  N    . ARG   A 1 279 ? -7.131  5.806  29.299  1.00 54.37  ? 279 ARG   A N    1 
ATOM   2153 C  CA   . ARG   A 1 279 ? -6.407  6.844  30.018  1.00 47.97  ? 279 ARG   A CA   1 
ATOM   2154 C  C    . ARG   A 1 279 ? -6.453  8.138  29.205  1.00 41.29  ? 279 ARG   A C    1 
ATOM   2155 O  O    . ARG   A 1 279 ? -6.734  8.129  28.005  1.00 38.95  ? 279 ARG   A O    1 
ATOM   2156 C  CB   . ARG   A 1 279 ? -4.963  6.395  30.245  1.00 44.71  ? 279 ARG   A CB   1 
ATOM   2157 C  CG   . ARG   A 1 279 ? -4.763  5.486  31.451  1.00 47.93  ? 279 ARG   A CG   1 
ATOM   2158 C  CD   . ARG   A 1 279 ? -3.292  5.211  31.630  1.00 45.02  ? 279 ARG   A CD   1 
ATOM   2159 N  NE   . ARG   A 1 279 ? -2.853  4.347  30.538  1.00 51.49  ? 279 ARG   A NE   1 
ATOM   2160 C  CZ   . ARG   A 1 279 ? -1.765  3.590  30.546  1.00 51.36  ? 279 ARG   A CZ   1 
ATOM   2161 N  NH1  . ARG   A 1 279 ? -0.970  3.532  31.602  1.00 48.42  ? 279 ARG   A NH1  1 
ATOM   2162 N  NH2  . ARG   A 1 279 ? -1.459  2.886  29.459  1.00 47.28  ? 279 ARG   A NH2  1 
ATOM   2163 N  N    . THR   A 1 280 ? -6.175  9.258  29.863  1.00 34.71  ? 280 THR   A N    1 
ATOM   2164 C  CA   . THR   A 1 280 ? -6.215  10.548 29.190  1.00 32.58  ? 280 THR   A CA   1 
ATOM   2165 C  C    . THR   A 1 280 ? -4.888  11.284 29.345  1.00 26.86  ? 280 THR   A C    1 
ATOM   2166 O  O    . THR   A 1 280 ? -4.083  10.993 30.233  1.00 26.52  ? 280 THR   A O    1 
ATOM   2167 C  CB   . THR   A 1 280 ? -7.359  11.421 29.720  1.00 33.97  ? 280 THR   A CB   1 
ATOM   2168 O  OG1  . THR   A 1 280 ? -7.190  11.632 31.132  1.00 31.64  ? 280 THR   A OG1  1 
ATOM   2169 C  CG2  . THR   A 1 280 ? -8.716  10.748 29.432  1.00 33.57  ? 280 THR   A CG2  1 
ATOM   2170 N  N    . ILE   A 1 281 ? -4.668  12.240 28.446  1.00 24.45  ? 281 ILE   A N    1 
ATOM   2171 C  CA   . ILE   A 1 281 ? -3.526  13.147 28.483  1.00 25.38  ? 281 ILE   A CA   1 
ATOM   2172 C  C    . ILE   A 1 281 ? -4.059  14.565 28.423  1.00 26.64  ? 281 ILE   A C    1 
ATOM   2173 O  O    . ILE   A 1 281 ? -4.760  14.925 27.474  1.00 24.26  ? 281 ILE   A O    1 
ATOM   2174 C  CB   . ILE   A 1 281 ? -2.541  12.896 27.326  1.00 24.95  ? 281 ILE   A CB   1 
ATOM   2175 C  CG1  . ILE   A 1 281 ? -2.139  11.417 27.260  1.00 24.86  ? 281 ILE   A CG1  1 
ATOM   2176 C  CG2  . ILE   A 1 281 ? -1.366  13.861 27.375  1.00 23.43  ? 281 ILE   A CG2  1 
ATOM   2177 C  CD1  . ILE   A 1 281 ? -1.118  11.092 26.160  1.00 26.53  ? 281 ILE   A CD1  1 
ATOM   2178 N  N    . LEU   A 1 282 ? -3.719  15.370 29.422  1.00 24.90  ? 282 LEU   A N    1 
ATOM   2179 C  CA   . LEU   A 1 282 ? -4.189  16.744 29.498  1.00 25.92  ? 282 LEU   A CA   1 
ATOM   2180 C  C    . LEU   A 1 282 ? -5.685  16.813 29.194  1.00 29.44  ? 282 LEU   A C    1 
ATOM   2181 O  O    . LEU   A 1 282 ? -6.163  17.650 28.418  1.00 26.90  ? 282 LEU   A O    1 
ATOM   2182 C  CB   . LEU   A 1 282 ? -3.393  17.660 28.564  1.00 22.94  ? 282 LEU   A CB   1 
ATOM   2183 C  CG   . LEU   A 1 282 ? -1.974  17.943 29.068  1.00 25.25  ? 282 LEU   A CG   1 
ATOM   2184 C  CD1  . LEU   A 1 282 ? -1.062  18.551 27.998  1.00 24.16  ? 282 LEU   A CD1  1 
ATOM   2185 C  CD2  . LEU   A 1 282 ? -1.985  18.773 30.353  1.00 25.45  ? 282 LEU   A CD2  1 
ATOM   2186 N  N    . GLY   A 1 283 ? -6.431  15.882 29.792  1.00 29.12  ? 283 GLY   A N    1 
ATOM   2187 C  CA   . GLY   A 1 283 ? -7.875  15.910 29.661  1.00 32.13  ? 283 GLY   A CA   1 
ATOM   2188 C  C    . GLY   A 1 283 ? -8.418  15.472 28.322  1.00 36.90  ? 283 GLY   A C    1 
ATOM   2189 O  O    . GLY   A 1 283 ? -9.605  15.694 28.043  1.00 41.06  ? 283 GLY   A O    1 
ATOM   2190 N  N    . SER   A 1 284 ? -7.598  14.875 27.468  1.00 28.17  ? 284 SER   A N    1 
ATOM   2191 C  CA   . SER   A 1 284 ? -8.069  14.437 26.164  1.00 25.28  ? 284 SER   A CA   1 
ATOM   2192 C  C    . SER   A 1 284 ? -7.802  12.946 26.001  1.00 28.45  ? 284 SER   A C    1 
ATOM   2193 O  O    . SER   A 1 284 ? -6.832  12.409 26.542  1.00 28.48  ? 284 SER   A O    1 
ATOM   2194 C  CB   . SER   A 1 284 ? -7.397  15.230 25.045  1.00 27.92  ? 284 SER   A CB   1 
ATOM   2195 O  OG   . SER   A 1 284 ? -7.676  14.639 23.778  1.00 34.86  ? 284 SER   A OG   1 
ATOM   2196 N  N    . ALA   A 1 285 ? -8.681  12.274 25.256  1.00 28.36  ? 285 ALA   A N    1 
ATOM   2197 C  CA   . ALA   A 1 285 ? -8.533  10.851 24.996  1.00 28.15  ? 285 ALA   A CA   1 
ATOM   2198 C  C    . ALA   A 1 285 ? -8.003  10.573 23.600  1.00 30.52  ? 285 ALA   A C    1 
ATOM   2199 O  O    . ALA   A 1 285 ? -7.931  9.410  23.191  1.00 32.28  ? 285 ALA   A O    1 
ATOM   2200 C  CB   . ALA   A 1 285 ? -9.865  10.127 25.216  1.00 29.52  ? 285 ALA   A CB   1 
ATOM   2201 N  N    . LEU   A 1 286 ? -7.632  11.609 22.856  1.00 29.13  ? 286 LEU   A N    1 
ATOM   2202 C  CA   . LEU   A 1 286 ? -6.939  11.429 21.593  1.00 29.73  ? 286 LEU   A CA   1 
ATOM   2203 C  C    . LEU   A 1 286 ? -5.706  12.324 21.575  1.00 30.49  ? 286 LEU   A C    1 
ATOM   2204 O  O    . LEU   A 1 286 ? -5.492  13.160 22.461  1.00 31.93  ? 286 LEU   A O    1 
ATOM   2205 C  CB   . LEU   A 1 286 ? -7.850  11.730 20.395  1.00 33.55  ? 286 LEU   A CB   1 
ATOM   2206 C  CG   . LEU   A 1 286 ? -8.723  12.971 20.450  1.00 35.76  ? 286 LEU   A CG   1 
ATOM   2207 C  CD1  . LEU   A 1 286 ? -7.872  14.233 20.311  1.00 36.24  ? 286 LEU   A CD1  1 
ATOM   2208 C  CD2  . LEU   A 1 286 ? -9.804  12.910 19.344  1.00 33.38  ? 286 LEU   A CD2  1 
ATOM   2209 N  N    . LEU   A 1 287 ? -4.880  12.139 20.559  1.00 27.26  ? 287 LEU   A N    1 
ATOM   2210 C  CA   . LEU   A 1 287 ? -3.620  12.861 20.476  1.00 25.47  ? 287 LEU   A CA   1 
ATOM   2211 C  C    . LEU   A 1 287 ? -3.872  14.205 19.806  1.00 28.38  ? 287 LEU   A C    1 
ATOM   2212 O  O    . LEU   A 1 287 ? -4.339  14.259 18.663  1.00 29.02  ? 287 LEU   A O    1 
ATOM   2213 C  CB   . LEU   A 1 287 ? -2.590  12.029 19.716  1.00 27.59  ? 287 LEU   A CB   1 
ATOM   2214 C  CG   . LEU   A 1 287 ? -2.280  10.694 20.420  1.00 26.03  ? 287 LEU   A CG   1 
ATOM   2215 C  CD1  . LEU   A 1 287 ? -1.618  9.701  19.470  1.00 31.89  ? 287 LEU   A CD1  1 
ATOM   2216 C  CD2  . LEU   A 1 287 ? -1.440  10.928 21.657  1.00 27.51  ? 287 LEU   A CD2  1 
ATOM   2217 N  N    . GLU   A 1 288 ? -3.591  15.289 20.517  1.00 24.67  ? 288 GLU   A N    1 
ATOM   2218 C  CA   . GLU   A 1 288 ? -4.005  16.621 20.090  1.00 22.66  ? 288 GLU   A CA   1 
ATOM   2219 C  C    . GLU   A 1 288 ? -2.900  17.221 19.228  1.00 20.35  ? 288 GLU   A C    1 
ATOM   2220 O  O    . GLU   A 1 288 ? -1.730  17.204 19.626  1.00 22.54  ? 288 GLU   A O    1 
ATOM   2221 C  CB   . GLU   A 1 288 ? -4.218  17.508 21.313  1.00 23.54  ? 288 GLU   A CB   1 
ATOM   2222 C  CG   . GLU   A 1 288 ? -5.410  17.165 22.186  1.00 27.75  ? 288 GLU   A CG   1 
ATOM   2223 C  CD   . GLU   A 1 288 ? -6.760  17.457 21.592  1.00 38.87  ? 288 GLU   A CD   1 
ATOM   2224 O  OE1  . GLU   A 1 288 ? -6.894  18.428 20.802  1.00 33.72  ? 288 GLU   A OE1  1 
ATOM   2225 O  OE2  . GLU   A 1 288 ? -7.701  16.731 21.981  1.00 36.21  ? 288 GLU   A OE2  1 
ATOM   2226 N  N    . ASP   A 1 289 ? -3.259  17.805 18.076  1.00 22.06  ? 289 ASP   A N    1 
ATOM   2227 C  CA   . ASP   A 1 289 ? -2.222  18.294 17.175  1.00 20.59  ? 289 ASP   A CA   1 
ATOM   2228 C  C    . ASP   A 1 289 ? -2.376  19.768 16.813  1.00 21.98  ? 289 ASP   A C    1 
ATOM   2229 O  O    . ASP   A 1 289 ? -1.747  20.230 15.860  1.00 22.07  ? 289 ASP   A O    1 
ATOM   2230 C  CB   . ASP   A 1 289 ? -2.155  17.403 15.922  1.00 23.34  ? 289 ASP   A CB   1 
ATOM   2231 C  CG   . ASP   A 1 289 ? -3.233  17.727 14.878  1.00 24.23  ? 289 ASP   A CG   1 
ATOM   2232 O  OD1  . ASP   A 1 289 ? -4.277  18.340 15.207  1.00 23.41  ? 289 ASP   A OD1  1 
ATOM   2233 O  OD2  . ASP   A 1 289 ? -3.032  17.322 13.702  1.00 25.33  ? 289 ASP   A OD2  1 
ATOM   2234 N  N    . GLU   A 1 290 ? -3.146  20.546 17.581  1.00 20.35  ? 290 GLU   A N    1 
ATOM   2235 C  CA   . GLU   A 1 290 ? -3.344  21.951 17.253  1.00 24.71  ? 290 GLU   A CA   1 
ATOM   2236 C  C    . GLU   A 1 290 ? -2.701  22.876 18.293  1.00 21.62  ? 290 GLU   A C    1 
ATOM   2237 O  O    . GLU   A 1 290 ? -3.148  24.004 18.491  1.00 22.45  ? 290 GLU   A O    1 
ATOM   2238 C  CB   . GLU   A 1 290 ? -4.844  22.216 17.058  1.00 23.88  ? 290 GLU   A CB   1 
ATOM   2239 C  CG   . GLU   A 1 290 ? -5.311  21.626 15.701  1.00 23.19  ? 290 GLU   A CG   1 
ATOM   2240 C  CD   . GLU   A 1 290 ? -6.598  22.243 15.120  1.00 26.97  ? 290 GLU   A CD   1 
ATOM   2241 O  OE1  . GLU   A 1 290 ? -7.133  23.201 15.718  1.00 26.02  ? 290 GLU   A OE1  1 
ATOM   2242 O  OE2  . GLU   A 1 290 ? -7.058  21.788 14.027  1.00 26.43  ? 290 GLU   A OE2  1 
ATOM   2243 N  N    . PHE   A 1 291 ? -1.630  22.417 18.941  1.00 19.68  ? 291 PHE   A N    1 
ATOM   2244 C  CA   . PHE   A 1 291 ? -0.774  23.259 19.769  1.00 17.75  ? 291 PHE   A CA   1 
ATOM   2245 C  C    . PHE   A 1 291 ? 0.637   23.236 19.181  1.00 17.49  ? 291 PHE   A C    1 
ATOM   2246 O  O    . PHE   A 1 291 ? 1.255   22.168 19.086  1.00 19.88  ? 291 PHE   A O    1 
ATOM   2247 C  CB   . PHE   A 1 291 ? -0.727  22.730 21.209  1.00 18.84  ? 291 PHE   A CB   1 
ATOM   2248 C  CG   . PHE   A 1 291 ? -2.013  22.870 21.950  1.00 24.87  ? 291 PHE   A CG   1 
ATOM   2249 C  CD1  . PHE   A 1 291 ? -2.420  24.091 22.470  1.00 29.97  ? 291 PHE   A CD1  1 
ATOM   2250 C  CD2  . PHE   A 1 291 ? -2.850  21.764 22.079  1.00 25.82  ? 291 PHE   A CD2  1 
ATOM   2251 C  CE1  . PHE   A 1 291 ? -3.630  24.195 23.169  1.00 31.92  ? 291 PHE   A CE1  1 
ATOM   2252 C  CE2  . PHE   A 1 291 ? -4.065  21.855 22.763  1.00 33.08  ? 291 PHE   A CE2  1 
ATOM   2253 C  CZ   . PHE   A 1 291 ? -4.456  23.076 23.306  1.00 31.20  ? 291 PHE   A CZ   1 
ATOM   2254 N  N    . THR   A 1 292 ? 1.165   24.410 18.827  1.00 19.26  ? 292 THR   A N    1 
ATOM   2255 C  CA   . THR   A 1 292 ? 2.540   24.464 18.350  1.00 22.42  ? 292 THR   A CA   1 
ATOM   2256 C  C    . THR   A 1 292 ? 3.527   24.437 19.513  1.00 22.64  ? 292 THR   A C    1 
ATOM   2257 O  O    . THR   A 1 292 ? 3.162   24.706 20.660  1.00 20.92  ? 292 THR   A O    1 
ATOM   2258 C  CB   . THR   A 1 292 ? 2.784   25.723 17.523  1.00 23.60  ? 292 THR   A CB   1 
ATOM   2259 O  OG1  . THR   A 1 292 ? 2.776   26.877 18.385  1.00 23.59  ? 292 THR   A OG1  1 
ATOM   2260 C  CG2  . THR   A 1 292 ? 1.750   25.874 16.385  1.00 20.30  ? 292 THR   A CG2  1 
ATOM   2261 N  N    . PRO   A 1 293 ? 4.790   24.117 19.242  1.00 21.92  ? 293 PRO   A N    1 
ATOM   2262 C  CA   . PRO   A 1 293 ? 5.810   24.268 20.289  1.00 23.44  ? 293 PRO   A CA   1 
ATOM   2263 C  C    . PRO   A 1 293 ? 5.785   25.650 20.935  1.00 23.78  ? 293 PRO   A C    1 
ATOM   2264 O  O    . PRO   A 1 293 ? 5.949   25.778 22.157  1.00 25.39  ? 293 PRO   A O    1 
ATOM   2265 C  CB   . PRO   A 1 293 ? 7.120   23.993 19.537  1.00 23.32  ? 293 PRO   A CB   1 
ATOM   2266 C  CG   . PRO   A 1 293 ? 6.716   23.085 18.386  1.00 24.28  ? 293 PRO   A CG   1 
ATOM   2267 C  CD   . PRO   A 1 293 ? 5.326   23.539 17.990  1.00 23.35  ? 293 PRO   A CD   1 
ATOM   2268 N  N    . PHE   A 1 294 ? 5.557   26.696 20.133  1.00 24.80  ? 294 PHE   A N    1 
ATOM   2269 C  CA   . PHE   A 1 294 ? 5.476   28.042 20.681  1.00 26.01  ? 294 PHE   A CA   1 
ATOM   2270 C  C    . PHE   A 1 294 ? 4.286   28.183 21.615  1.00 25.16  ? 294 PHE   A C    1 
ATOM   2271 O  O    . PHE   A 1 294 ? 4.397   28.801 22.680  1.00 26.92  ? 294 PHE   A O    1 
ATOM   2272 C  CB   . PHE   A 1 294 ? 5.373   29.060 19.543  1.00 25.56  ? 294 PHE   A CB   1 
ATOM   2273 C  CG   . PHE   A 1 294 ? 5.109   30.464 20.016  1.00 39.88  ? 294 PHE   A CG   1 
ATOM   2274 C  CD1  . PHE   A 1 294 ? 6.161   31.293 20.380  1.00 45.03  ? 294 PHE   A CD1  1 
ATOM   2275 C  CD2  . PHE   A 1 294 ? 3.811   30.954 20.109  1.00 37.31  ? 294 PHE   A CD2  1 
ATOM   2276 C  CE1  . PHE   A 1 294 ? 5.922   32.595 20.827  1.00 48.14  ? 294 PHE   A CE1  1 
ATOM   2277 C  CE2  . PHE   A 1 294 ? 3.562   32.250 20.552  1.00 45.85  ? 294 PHE   A CE2  1 
ATOM   2278 C  CZ   . PHE   A 1 294 ? 4.624   33.072 20.912  1.00 42.91  ? 294 PHE   A CZ   1 
ATOM   2279 N  N    . ASP   A 1 295 ? 3.132   27.639 21.218  1.00 21.00  ? 295 ASP   A N    1 
ATOM   2280 C  CA   . ASP   A 1 295 ? 1.943   27.685 22.068  1.00 23.62  ? 295 ASP   A CA   1 
ATOM   2281 C  C    . ASP   A 1 295 ? 2.230   27.037 23.421  1.00 24.35  ? 295 ASP   A C    1 
ATOM   2282 O  O    . ASP   A 1 295 ? 1.823   27.551 24.483  1.00 24.68  ? 295 ASP   A O    1 
ATOM   2283 C  CB   . ASP   A 1 295 ? 0.786   26.953 21.403  1.00 24.17  ? 295 ASP   A CB   1 
ATOM   2284 C  CG   . ASP   A 1 295 ? 0.316   27.640 20.134  1.00 24.54  ? 295 ASP   A CG   1 
ATOM   2285 O  OD1  . ASP   A 1 295 ? 0.632   28.835 19.975  1.00 24.41  ? 295 ASP   A OD1  1 
ATOM   2286 O  OD2  . ASP   A 1 295 ? -0.370  26.988 19.314  1.00 23.89  ? 295 ASP   A OD2  1 
ATOM   2287 N  N    . VAL   A 1 296 ? 2.889   25.865 23.390  1.00 20.52  ? 296 VAL   A N    1 
ATOM   2288 C  CA   . VAL   A 1 296 ? 3.204   25.155 24.633  1.00 18.38  ? 296 VAL   A CA   1 
ATOM   2289 C  C    . VAL   A 1 296 ? 4.104   26.013 25.499  1.00 24.97  ? 296 VAL   A C    1 
ATOM   2290 O  O    . VAL   A 1 296 ? 3.858   26.190 26.699  1.00 26.01  ? 296 VAL   A O    1 
ATOM   2291 C  CB   . VAL   A 1 296 ? 3.850   23.787 24.340  1.00 21.70  ? 296 VAL   A CB   1 
ATOM   2292 C  CG1  . VAL   A 1 296 ? 4.344   23.136 25.654  1.00 23.82  ? 296 VAL   A CG1  1 
ATOM   2293 C  CG2  . VAL   A 1 296 ? 2.851   22.875 23.636  1.00 20.23  ? 296 VAL   A CG2  1 
ATOM   2294 N  N    . VAL   A 1 297 ? 5.164   26.559 24.907  1.00 24.12  ? 297 VAL   A N    1 
ATOM   2295 C  CA   . VAL   A 1 297 ? 6.096   27.355 25.702  1.00 29.15  ? 297 VAL   A CA   1 
ATOM   2296 C  C    . VAL   A 1 297 ? 5.375   28.554 26.318  1.00 32.01  ? 297 VAL   A C    1 
ATOM   2297 O  O    . VAL   A 1 297 ? 5.614   28.911 27.479  1.00 34.12  ? 297 VAL   A O    1 
ATOM   2298 C  CB   . VAL   A 1 297 ? 7.297   27.786 24.834  1.00 28.73  ? 297 VAL   A CB   1 
ATOM   2299 C  CG1  . VAL   A 1 297 ? 8.033   28.955 25.465  1.00 40.24  ? 297 VAL   A CG1  1 
ATOM   2300 C  CG2  . VAL   A 1 297 ? 8.229   26.619 24.594  1.00 29.92  ? 297 VAL   A CG2  1 
ATOM   2301 N  N    . ARG   A 1 298 ? 4.470   29.184 25.559  1.00 31.19  ? 298 ARG   A N    1 
ATOM   2302 C  CA   . ARG   A 1 298 ? 3.752   30.349 26.075  1.00 32.26  ? 298 ARG   A CA   1 
ATOM   2303 C  C    . ARG   A 1 298 ? 2.915   29.983 27.298  1.00 34.43  ? 298 ARG   A C    1 
ATOM   2304 O  O    . ARG   A 1 298 ? 2.894   30.731 28.283  1.00 36.40  ? 298 ARG   A O    1 
ATOM   2305 C  CB   . ARG   A 1 298 ? 2.858   30.971 24.992  1.00 35.10  ? 298 ARG   A CB   1 
ATOM   2306 C  CG   . ARG   A 1 298 ? 2.341   32.381 25.352  1.00 43.97  ? 298 ARG   A CG   1 
ATOM   2307 C  CD   . ARG   A 1 298 ? 1.315   33.007 24.360  1.00 43.32  ? 298 ARG   A CD   1 
ATOM   2308 N  NE   . ARG   A 1 298 ? 0.356   32.049 23.814  1.00 51.46  ? 298 ARG   A NE   1 
ATOM   2309 C  CZ   . ARG   A 1 298 ? -0.942  32.282 23.614  1.00 47.69  ? 298 ARG   A CZ   1 
ATOM   2310 N  NH1  . ARG   A 1 298 ? -1.497  33.461 23.872  1.00 41.11  ? 298 ARG   A NH1  1 
ATOM   2311 N  NH2  . ARG   A 1 298 ? -1.711  31.300 23.163  1.00 42.60  ? 298 ARG   A NH2  1 
ATOM   2312 N  N    . GLN   A 1 299 ? 2.215   28.838 27.267  1.00 31.00  ? 299 GLN   A N    1 
ATOM   2313 C  CA   . GLN   A 1 299 ? 1.360   28.494 28.412  1.00 30.50  ? 299 GLN   A CA   1 
ATOM   2314 C  C    . GLN   A 1 299 ? 2.068   27.786 29.551  1.00 36.69  ? 299 GLN   A C    1 
ATOM   2315 O  O    . GLN   A 1 299 ? 1.522   27.752 30.662  1.00 36.89  ? 299 GLN   A O    1 
ATOM   2316 C  CB   . GLN   A 1 299 ? 0.202   27.572 28.042  1.00 34.36  ? 299 GLN   A CB   1 
ATOM   2317 C  CG   . GLN   A 1 299 ? -1.002  28.224 27.488  1.00 41.46  ? 299 GLN   A CG   1 
ATOM   2318 C  CD   . GLN   A 1 299 ? -2.154  27.258 27.420  1.00 29.71  ? 299 GLN   A CD   1 
ATOM   2319 O  OE1  . GLN   A 1 299 ? -2.675  26.775 28.433  1.00 24.67  ? 299 GLN   A OE1  1 
ATOM   2320 N  NE2  . GLN   A 1 299 ? -2.474  26.872 26.217  1.00 26.57  ? 299 GLN   A NE2  1 
ATOM   2321 N  N    . CYS   A 1 300 ? 3.173   27.117 29.268  1.00 28.08  ? 300 CYS   A N    1 
ATOM   2322 C  CA   . CYS   A 1 300 ? 3.783   26.253 30.305  1.00 29.54  ? 300 CYS   A CA   1 
ATOM   2323 C  C    . CYS   A 1 300 ? 5.070   26.873 30.841  1.00 44.71  ? 300 CYS   A C    1 
ATOM   2324 O  O    . CYS   A 1 300 ? 5.667   26.263 31.735  1.00 49.73  ? 300 CYS   A O    1 
ATOM   2325 C  CB   . CYS   A 1 300 ? 4.074   24.867 29.733  1.00 28.30  ? 300 CYS   A CB   1 
ATOM   2326 S  SG   . CYS   A 1 300 ? 2.617   23.959 29.167  1.00 34.20  ? 300 CYS   A SG   1 
ATOM   2327 N  N    . SER   A 1 301 ? 5.459   28.036 30.331  1.00 36.02  ? 301 SER   A N    1 
ATOM   2328 C  CA   . SER   A 1 301 ? 6.668   28.737 30.839  1.00 48.09  ? 301 SER   A CA   1 
ATOM   2329 C  C    . SER   A 1 301 ? 6.386   30.230 31.003  1.00 45.31  ? 301 SER   A C    1 
ATOM   2330 O  O    . SER   A 1 301 ? 5.602   30.758 30.200  1.00 50.35  ? 301 SER   A O    1 
ATOM   2331 C  CB   . SER   A 1 301 ? 7.844   28.498 29.932  1.00 30.00  ? 301 SER   A CB   1 
ATOM   2332 O  OG   . SER   A 1 301 ? 7.729   27.255 29.253  1.00 30.00  ? 301 SER   A OG   1 
HETATM 2333 C  C01  . A1EGR B 2 .   ? -23.439 34.870 1.666   1.00 26.81  ? 401 A1EGR A C01  1 
HETATM 2334 C  C02  . A1EGR B 2 .   ? -24.843 34.864 1.629   1.00 29.50  ? 401 A1EGR A C02  1 
HETATM 2335 C  C03  . A1EGR B 2 .   ? -25.537 36.070 1.904   1.00 31.40  ? 401 A1EGR A C03  1 
HETATM 2336 C  C04  . A1EGR B 2 .   ? -24.860 37.236 2.206   1.00 28.97  ? 401 A1EGR A C04  1 
HETATM 2337 C  C05  . A1EGR B 2 .   ? -23.457 37.244 2.238   1.00 28.60  ? 401 A1EGR A C05  1 
HETATM 2338 C  C06  . A1EGR B 2 .   ? -22.778 36.061 1.977   1.00 26.12  ? 401 A1EGR A C06  1 
HETATM 2339 C  C07  . A1EGR B 2 .   ? -26.937 36.455 1.970   1.00 39.69  ? 401 A1EGR A C07  1 
HETATM 2340 C  C10  . A1EGR B 2 .   ? -28.202 38.527 2.448   1.00 43.17  ? 401 A1EGR A C10  1 
HETATM 2341 C  C13  . A1EGR B 2 .   ? -22.144 32.869 2.466   1.00 21.71  ? 401 A1EGR A C13  1 
HETATM 2342 C  C15  . A1EGR B 2 .   ? -20.955 31.060 3.251   1.00 24.48  ? 401 A1EGR A C15  1 
HETATM 2343 C  C17  . A1EGR B 2 .   ? -22.029 32.480 4.671   1.00 21.29  ? 401 A1EGR A C17  1 
HETATM 2344 C  C21  . A1EGR B 2 .   ? -21.018 31.396 0.871   1.00 26.34  ? 401 A1EGR A C21  1 
HETATM 2345 C  C22  . A1EGR B 2 .   ? -19.805 32.162 0.316   1.00 21.55  ? 401 A1EGR A C22  1 
HETATM 2346 C  C23  . A1EGR B 2 .   ? -19.240 31.792 -0.903  1.00 27.98  ? 401 A1EGR A C23  1 
HETATM 2347 C  C24  . A1EGR B 2 .   ? -18.137 32.478 -1.408  1.00 24.96  ? 401 A1EGR A C24  1 
HETATM 2348 C  C25  . A1EGR B 2 .   ? -17.582 33.539 -0.692  1.00 24.61  ? 401 A1EGR A C25  1 
HETATM 2349 C  C26  . A1EGR B 2 .   ? -18.147 33.899 0.530   1.00 20.65  ? 401 A1EGR A C26  1 
HETATM 2350 C  C27  . A1EGR B 2 .   ? -19.247 33.216 1.024   1.00 22.13  ? 401 A1EGR A C27  1 
HETATM 2351 C  C28  . A1EGR B 2 .   ? -17.561 35.055 1.324   1.00 19.26  ? 401 A1EGR A C28  1 
HETATM 2352 C  C29  . A1EGR B 2 .   ? -19.841 30.626 -1.696  1.00 28.63  ? 401 A1EGR A C29  1 
HETATM 2353 C  C30  . A1EGR B 2 .   ? -20.824 30.614 5.618   1.00 21.47  ? 401 A1EGR A C30  1 
HETATM 2354 C  C31  . A1EGR B 2 .   ? -19.517 30.678 6.077   1.00 23.15  ? 401 A1EGR A C31  1 
HETATM 2355 C  C33  . A1EGR B 2 .   ? -19.951 29.155 7.749   1.00 20.78  ? 401 A1EGR A C33  1 
HETATM 2356 C  C34  . A1EGR B 2 .   ? -21.277 29.025 7.339   1.00 22.66  ? 401 A1EGR A C34  1 
HETATM 2357 C  C35  . A1EGR B 2 .   ? -21.729 29.771 6.237   1.00 23.52  ? 401 A1EGR A C35  1 
HETATM 2358 C  C38  . A1EGR B 2 .   ? -23.281 27.704 7.367   1.00 28.49  ? 401 A1EGR A C38  1 
HETATM 2359 C  C39  . A1EGR B 2 .   ? -23.707 26.373 8.012   1.00 36.65  ? 401 A1EGR A C39  1 
HETATM 2360 C  C41  . A1EGR B 2 .   ? -24.342 25.541 10.133  1.00 44.36  ? 401 A1EGR A C41  1 
HETATM 2361 N  N08  . A1EGR B 2 .   ? -26.986 37.734 2.286   1.00 40.06  ? 401 A1EGR A N08  1 
HETATM 2362 N  N09  . A1EGR B 2 .   ? -25.758 38.217 2.430   1.00 36.77  ? 401 A1EGR A N09  1 
HETATM 2363 N  N12  . A1EGR B 2 .   ? -22.464 33.242 3.673   1.00 23.44  ? 401 A1EGR A N12  1 
HETATM 2364 N  N14  . A1EGR B 2 .   ? -21.377 31.798 2.238   1.00 22.16  ? 401 A1EGR A N14  1 
HETATM 2365 N  N16  . A1EGR B 2 .   ? -21.273 31.406 4.464   1.00 23.20  ? 401 A1EGR A N16  1 
HETATM 2366 N  N19  . A1EGR B 2 .   ? -22.627 33.688 1.380   1.00 24.40  ? 401 A1EGR A N19  1 
HETATM 2367 N  N32  . A1EGR B 2 .   ? -19.119 29.969 7.136   1.00 21.90  ? 401 A1EGR A N32  1 
HETATM 2368 N  N37  . A1EGR B 2 .   ? -17.120 35.912 1.924   1.00 22.95  ? 401 A1EGR A N37  1 
HETATM 2369 O  O18  . A1EGR B 2 .   ? -22.358 32.850 5.953   1.00 23.56  ? 401 A1EGR A O18  1 
HETATM 2370 O  O20  . A1EGR B 2 .   ? -20.182 29.942 3.051   1.00 24.00  ? 401 A1EGR A O20  1 
HETATM 2371 O  O36  . A1EGR B 2 .   ? -22.130 28.151 8.026   1.00 26.18  ? 401 A1EGR A O36  1 
HETATM 2372 O  O40  . A1EGR B 2 .   ? -24.006 26.651 9.351   1.00 34.36  ? 401 A1EGR A O40  1 
HETATM 2373 CL CL11 . A1EGR B 2 .   ? -21.019 36.078 2.028   1.00 26.95  ? 401 A1EGR A CL11 1 
HETATM 2374 H  H021 . A1EGR B 2 .   ? -25.386 33.952 1.394   1.00 35.40  ? 401 A1EGR A H021 1 
HETATM 2375 H  H051 . A1EGR B 2 .   ? -22.913 38.156 2.462   1.00 34.32  ? 401 A1EGR A H051 1 
HETATM 2376 H  H071 . A1EGR B 2 .   ? -27.780 35.812 1.792   1.00 47.63  ? 401 A1EGR A H071 1 
HETATM 2377 H  H102 . A1EGR B 2 .   ? -28.997 37.897 2.840   1.00 51.80  ? 401 A1EGR A H102 1 
HETATM 2378 H  H103 . A1EGR B 2 .   ? -28.502 38.932 1.484   1.00 51.80  ? 401 A1EGR A H103 1 
HETATM 2379 H  H101 . A1EGR B 2 .   ? -28.012 39.344 3.141   1.00 51.80  ? 401 A1EGR A H101 1 
HETATM 2380 H  H211 . A1EGR B 2 .   ? -20.787 30.341 0.873   1.00 31.61  ? 401 A1EGR A H211 1 
HETATM 2381 H  H212 . A1EGR B 2 .   ? -21.864 31.578 0.225   1.00 31.61  ? 401 A1EGR A H212 1 
HETATM 2382 H  H241 . A1EGR B 2 .   ? -17.710 32.187 -2.359  1.00 29.96  ? 401 A1EGR A H241 1 
HETATM 2383 H  H251 . A1EGR B 2 .   ? -16.721 34.076 -1.082  1.00 29.53  ? 401 A1EGR A H251 1 
HETATM 2384 H  H271 . A1EGR B 2 .   ? -19.677 33.510 1.975   1.00 26.55  ? 401 A1EGR A H271 1 
HETATM 2385 H  H291 . A1EGR B 2 .   ? -19.851 30.874 -2.753  1.00 34.36  ? 401 A1EGR A H291 1 
HETATM 2386 H  H292 . A1EGR B 2 .   ? -20.856 30.443 -1.357  1.00 34.36  ? 401 A1EGR A H292 1 
HETATM 2387 H  H293 . A1EGR B 2 .   ? -19.240 29.735 -1.539  1.00 34.36  ? 401 A1EGR A H293 1 
HETATM 2388 H  H311 . A1EGR B 2 .   ? -18.808 31.315 5.567   1.00 27.78  ? 401 A1EGR A H311 1 
HETATM 2389 H  H331 . A1EGR B 2 .   ? -19.597 28.571 8.594   1.00 24.94  ? 401 A1EGR A H331 1 
HETATM 2390 H  H351 . A1EGR B 2 .   ? -22.749 29.688 5.885   1.00 28.22  ? 401 A1EGR A H351 1 
HETATM 2391 H  H381 . A1EGR B 2 .   ? -24.074 28.435 7.475   1.00 34.18  ? 401 A1EGR A H381 1 
HETATM 2392 H  H382 . A1EGR B 2 .   ? -23.066 27.550 6.316   1.00 34.18  ? 401 A1EGR A H382 1 
HETATM 2393 H  H391 . A1EGR B 2 .   ? -22.894 25.653 7.953   1.00 43.98  ? 401 A1EGR A H391 1 
HETATM 2394 H  H392 . A1EGR B 2 .   ? -24.585 25.978 7.508   1.00 43.98  ? 401 A1EGR A H392 1 
HETATM 2395 H  H413 . A1EGR B 2 .   ? -24.675 25.875 11.111  1.00 53.23  ? 401 A1EGR A H413 1 
HETATM 2396 H  H411 . A1EGR B 2 .   ? -23.471 24.901 10.246  1.00 53.23  ? 401 A1EGR A H411 1 
HETATM 2397 H  H412 . A1EGR B 2 .   ? -25.139 24.985 9.649   1.00 53.23  ? 401 A1EGR A H412 1 
HETATM 2398 H  H181 . A1EGR B 2 .   ? -21.678 33.076 6.570   1.00 28.27  ? 401 A1EGR A H181 1 
HETATM 2399 H  H191 . A1EGR B 2 .   ? -22.407 33.448 0.434   1.00 29.28  ? 401 A1EGR A H191 1 
HETATM 2400 H  H201 . A1EGR B 2 .   ? -19.523 29.935 2.373   1.00 28.80  ? 401 A1EGR A H201 1 
HETATM 2401 O  O    . HOH   C 3 .   ? -3.618  7.920  12.237  1.00 44.35  ? 501 HOH   A O    1 
HETATM 2402 O  O    . HOH   C 3 .   ? 1.686   19.883 6.065   1.00 41.29  ? 502 HOH   A O    1 
HETATM 2403 O  O    . HOH   C 3 .   ? -3.000  18.781 8.962   1.00 32.73  ? 503 HOH   A O    1 
HETATM 2404 O  O    . HOH   C 3 .   ? -2.973  14.051 2.960   1.00 39.21  ? 504 HOH   A O    1 
HETATM 2405 O  O    . HOH   C 3 .   ? -1.178  30.900 20.815  1.00 51.54  ? 505 HOH   A O    1 
HETATM 2406 O  O    . HOH   C 3 .   ? -21.267 53.873 4.175   1.00 37.19  ? 506 HOH   A O    1 
HETATM 2407 O  O    . HOH   C 3 .   ? -5.673  20.038 19.301  1.00 32.82  ? 507 HOH   A O    1 
HETATM 2408 O  O    . HOH   C 3 .   ? 2.436   40.011 15.502  1.00 30.45  ? 508 HOH   A O    1 
HETATM 2409 O  O    . HOH   C 3 .   ? -23.661 42.898 -8.108  1.00 37.10  ? 509 HOH   A O    1 
HETATM 2410 O  O    . HOH   C 3 .   ? -5.024  25.714 18.604  1.00 43.45  ? 510 HOH   A O    1 
HETATM 2411 O  O    . HOH   C 3 .   ? -3.621  10.421 16.350  1.00 38.68  ? 511 HOH   A O    1 
HETATM 2412 O  O    . HOH   C 3 .   ? -28.096 39.391 -1.223  1.00 42.23  ? 512 HOH   A O    1 
HETATM 2413 O  O    . HOH   C 3 .   ? -21.437 22.329 5.521   1.00 36.19  ? 513 HOH   A O    1 
HETATM 2414 O  O    . HOH   C 3 .   ? -23.569 51.809 -9.360  1.00 45.32  ? 514 HOH   A O    1 
HETATM 2415 O  O    . HOH   C 3 .   ? 18.603  19.953 18.102  1.00 52.43  ? 515 HOH   A O    1 
HETATM 2416 O  O    . HOH   C 3 .   ? -7.390  24.504 17.935  1.00 34.46  ? 516 HOH   A O    1 
HETATM 2417 O  O    . HOH   C 3 .   ? 5.121   25.463 34.135  1.00 38.28  ? 517 HOH   A O    1 
HETATM 2418 O  O    . HOH   C 3 .   ? -4.600  34.750 -5.656  1.00 28.57  ? 518 HOH   A O    1 
HETATM 2419 O  O    . HOH   C 3 .   ? -8.845  6.987  23.409  1.00 46.35  ? 519 HOH   A O    1 
HETATM 2420 O  O    . HOH   C 3 .   ? -24.650 42.939 -3.532  1.00 36.87  ? 520 HOH   A O    1 
HETATM 2421 O  O    . HOH   C 3 .   ? -1.384  31.076 18.037  1.00 25.78  ? 521 HOH   A O    1 
HETATM 2422 O  O    . HOH   C 3 .   ? -0.895  48.098 18.899  1.00 29.37  ? 522 HOH   A O    1 
HETATM 2423 O  O    . HOH   C 3 .   ? 10.621  23.379 21.998  1.00 41.42  ? 523 HOH   A O    1 
HETATM 2424 O  O    . HOH   C 3 .   ? -18.875 42.190 20.886  1.00 37.05  ? 524 HOH   A O    1 
HETATM 2425 O  O    . HOH   C 3 .   ? -23.482 47.672 6.519   1.00 31.06  ? 525 HOH   A O    1 
HETATM 2426 O  O    . HOH   C 3 .   ? 2.614   3.745  29.183  1.00 47.02  ? 526 HOH   A O    1 
HETATM 2427 O  O    . HOH   C 3 .   ? 3.001   36.603 21.403  1.00 46.49  ? 527 HOH   A O    1 
HETATM 2428 O  O    . HOH   C 3 .   ? -22.745 39.442 9.169   1.00 27.60  ? 528 HOH   A O    1 
HETATM 2429 O  O    . HOH   C 3 .   ? 3.828   23.444 14.040  1.00 27.95  ? 529 HOH   A O    1 
HETATM 2430 O  O    . HOH   C 3 .   ? 6.650   32.598 28.612  1.00 56.45  ? 530 HOH   A O    1 
HETATM 2431 O  O    . HOH   C 3 .   ? 9.560   8.247  26.484  1.00 40.03  ? 531 HOH   A O    1 
HETATM 2432 O  O    . HOH   C 3 .   ? 0.000   36.681 0.000   0.50 26.26  ? 532 HOH   A O    1 
HETATM 2433 O  O    . HOH   C 3 .   ? -9.167  58.790 3.913   1.00 39.99  ? 533 HOH   A O    1 
HETATM 2434 O  O    . HOH   C 3 .   ? -15.298 42.653 24.670  1.00 26.29  ? 534 HOH   A O    1 
HETATM 2435 O  O    . HOH   C 3 .   ? -24.091 37.512 5.686   1.00 31.31  ? 535 HOH   A O    1 
HETATM 2436 O  O    . HOH   C 3 .   ? 6.723   15.754 34.963  1.00 29.95  ? 536 HOH   A O    1 
HETATM 2437 O  O    . HOH   C 3 .   ? -4.453  53.940 16.635  1.00 47.89  ? 537 HOH   A O    1 
HETATM 2438 O  O    . HOH   C 3 .   ? -8.726  27.998 3.146   1.00 18.23  ? 538 HOH   A O    1 
HETATM 2439 O  O    . HOH   C 3 .   ? -0.726  28.870 31.633  1.00 30.93  ? 539 HOH   A O    1 
HETATM 2440 O  O    . HOH   C 3 .   ? -17.256 53.420 -9.703  1.00 37.50  ? 540 HOH   A O    1 
HETATM 2441 O  O    . HOH   C 3 .   ? 2.240   29.357 17.473  1.00 26.73  ? 541 HOH   A O    1 
HETATM 2442 O  O    . HOH   C 3 .   ? -19.405 31.597 15.612  1.00 28.55  ? 542 HOH   A O    1 
HETATM 2443 O  O    . HOH   C 3 .   ? -8.681  48.137 18.304  1.00 28.20  ? 543 HOH   A O    1 
HETATM 2444 O  O    . HOH   C 3 .   ? 1.045   39.813 3.273   1.00 25.83  ? 544 HOH   A O    1 
HETATM 2445 O  O    . HOH   C 3 .   ? -13.081 39.183 13.095  1.00 24.24  ? 545 HOH   A O    1 
HETATM 2446 O  O    . HOH   C 3 .   ? -8.284  23.849 12.502  1.00 20.66  ? 546 HOH   A O    1 
HETATM 2447 O  O    . HOH   C 3 .   ? -16.075 50.429 -10.190 1.00 35.06  ? 547 HOH   A O    1 
HETATM 2448 O  O    . HOH   C 3 .   ? -5.075  49.908 5.931   1.00 29.14  ? 548 HOH   A O    1 
HETATM 2449 O  O    . HOH   C 3 .   ? -14.089 30.169 -10.383 1.00 52.89  ? 549 HOH   A O    1 
HETATM 2450 O  O    . HOH   C 3 .   ? 10.765  15.390 33.487  1.00 43.13  ? 550 HOH   A O    1 
HETATM 2451 O  O    . HOH   C 3 .   ? -0.746  19.752 19.674  1.00 17.92  ? 551 HOH   A O    1 
HETATM 2452 O  O    . HOH   C 3 .   ? 3.726   5.463  25.063  1.00 42.79  ? 552 HOH   A O    1 
HETATM 2453 O  O    . HOH   C 3 .   ? -4.817  43.788 1.322   1.00 33.81  ? 553 HOH   A O    1 
HETATM 2454 O  O    . HOH   C 3 .   ? 3.915   37.784 12.519  1.00 38.36  ? 554 HOH   A O    1 
HETATM 2455 O  O    . HOH   C 3 .   ? 15.195  10.972 27.383  1.00 42.02  ? 555 HOH   A O    1 
HETATM 2456 O  O    . HOH   C 3 .   ? -5.702  14.168 31.805  1.00 38.06  ? 556 HOH   A O    1 
HETATM 2457 O  O    . HOH   C 3 .   ? -10.626 57.850 -3.829  1.00 50.31  ? 557 HOH   A O    1 
HETATM 2458 O  O    . HOH   C 3 .   ? 0.905   25.142 32.383  1.00 50.89  ? 558 HOH   A O    1 
HETATM 2459 O  O    . HOH   C 3 .   ? -7.073  21.058 0.062   1.00 26.25  ? 559 HOH   A O    1 
HETATM 2460 O  O    . HOH   C 3 .   ? -23.025 32.820 -1.394  1.00 26.69  ? 560 HOH   A O    1 
HETATM 2461 O  O    . HOH   C 3 .   ? -3.406  31.682 -3.035  1.00 18.01  ? 561 HOH   A O    1 
HETATM 2462 O  O    . HOH   C 3 .   ? -24.178 33.226 -10.876 1.00 43.12  ? 562 HOH   A O    1 
HETATM 2463 O  O    . HOH   C 3 .   ? -10.053 47.093 -8.580  1.00 28.34  ? 563 HOH   A O    1 
HETATM 2464 O  O    . HOH   C 3 .   ? -2.458  38.122 5.638   1.00 25.67  ? 564 HOH   A O    1 
HETATM 2465 O  O    . HOH   C 3 .   ? 0.277   21.420 2.598   1.00 34.06  ? 565 HOH   A O    1 
HETATM 2466 O  O    . HOH   C 3 .   ? 16.444  19.248 19.777  1.00 48.67  ? 566 HOH   A O    1 
HETATM 2467 O  O    . HOH   C 3 .   ? -26.138 33.262 12.126  1.00 41.39  ? 567 HOH   A O    1 
HETATM 2468 O  O    . HOH   C 3 .   ? -11.262 32.646 -6.282  1.00 25.71  ? 568 HOH   A O    1 
HETATM 2469 O  O    . HOH   C 3 .   ? -15.160 19.399 1.867   1.00 36.60  ? 569 HOH   A O    1 
HETATM 2470 O  O    . HOH   C 3 .   ? -22.493 39.200 17.194  1.00 35.92  ? 570 HOH   A O    1 
HETATM 2471 O  O    . HOH   C 3 .   ? -13.257 52.824 16.077  1.00 36.86  ? 571 HOH   A O    1 
HETATM 2472 O  O    . HOH   C 3 .   ? 4.066   24.933 10.678  1.00 33.81  ? 572 HOH   A O    1 
HETATM 2473 O  O    . HOH   C 3 .   ? -11.344 16.402 30.163  1.00 47.47  ? 573 HOH   A O    1 
HETATM 2474 O  O    . HOH   C 3 .   ? -5.277  18.774 25.974  1.00 26.61  ? 574 HOH   A O    1 
HETATM 2475 O  O    . HOH   C 3 .   ? -16.656 43.731 20.994  1.00 33.76  ? 575 HOH   A O    1 
HETATM 2476 O  O    . HOH   C 3 .   ? 2.060   43.780 6.484   1.00 32.91  ? 576 HOH   A O    1 
HETATM 2477 O  O    . HOH   C 3 .   ? -3.954  17.637 0.571   1.00 36.03  ? 577 HOH   A O    1 
HETATM 2478 O  O    . HOH   C 3 .   ? 3.023   25.547 2.681   1.00 23.01  ? 578 HOH   A O    1 
HETATM 2479 O  O    . HOH   C 3 .   ? -8.908  31.491 -5.560  1.00 20.96  ? 579 HOH   A O    1 
HETATM 2480 O  O    . HOH   C 3 .   ? 1.280   30.034 14.981  1.00 31.06  ? 580 HOH   A O    1 
HETATM 2481 O  O    . HOH   C 3 .   ? -9.320  39.998 -8.263  1.00 29.51  ? 581 HOH   A O    1 
HETATM 2482 O  O    . HOH   C 3 .   ? -7.946  7.691  20.913  1.00 55.93  ? 582 HOH   A O    1 
HETATM 2483 O  O    . HOH   C 3 .   ? -15.083 36.481 -1.604  1.00 21.66  ? 583 HOH   A O    1 
HETATM 2484 O  O    . HOH   C 3 .   ? -27.844 42.601 -3.139  1.00 42.01  ? 584 HOH   A O    1 
HETATM 2485 O  O    . HOH   C 3 .   ? -3.114  27.005 20.117  1.00 25.43  ? 585 HOH   A O    1 
HETATM 2486 O  O    . HOH   C 3 .   ? -15.121 22.933 11.277  1.00 26.94  ? 586 HOH   A O    1 
HETATM 2487 O  O    . HOH   C 3 .   ? -5.430  10.132 18.590  1.00 34.74  ? 587 HOH   A O    1 
HETATM 2488 O  O    . HOH   C 3 .   ? 4.751   31.383 5.426   1.00 24.88  ? 588 HOH   A O    1 
HETATM 2489 O  O    . HOH   C 3 .   ? -11.739 24.933 -6.143  1.00 45.50  ? 589 HOH   A O    1 
HETATM 2490 O  O    . HOH   C 3 .   ? -13.457 45.877 -12.426 1.00 38.21  ? 590 HOH   A O    1 
HETATM 2491 O  O    . HOH   C 3 .   ? 17.062  23.551 11.841  1.00 57.41  ? 591 HOH   A O    1 
HETATM 2492 O  O    . HOH   C 3 .   ? -20.838 45.067 18.950  1.00 42.14  ? 592 HOH   A O    1 
HETATM 2493 O  O    . HOH   C 3 .   ? -12.646 18.118 5.558   1.00 36.08  ? 593 HOH   A O    1 
HETATM 2494 O  O    . HOH   C 3 .   ? 1.323   29.802 3.131   1.00 19.32  ? 594 HOH   A O    1 
HETATM 2495 O  O    . HOH   C 3 .   ? -22.059 46.427 14.318  1.00 44.49  ? 595 HOH   A O    1 
HETATM 2496 O  O    . HOH   C 3 .   ? -15.190 33.740 -10.369 1.00 42.48  ? 596 HOH   A O    1 
HETATM 2497 O  O    . HOH   C 3 .   ? 13.432  22.414 34.036  1.00 58.29  ? 597 HOH   A O    1 
HETATM 2498 O  O    . HOH   C 3 .   ? -10.391 19.264 6.254   1.00 29.88  ? 598 HOH   A O    1 
HETATM 2499 O  O    . HOH   C 3 .   ? -5.547  8.811  32.648  1.00 47.27  ? 599 HOH   A O    1 
HETATM 2500 O  O    . HOH   C 3 .   ? -19.844 27.621 0.616   1.00 36.60  ? 600 HOH   A O    1 
HETATM 2501 O  O    . HOH   C 3 .   ? -2.466  19.999 0.812   1.00 33.46  ? 601 HOH   A O    1 
HETATM 2502 O  O    . HOH   C 3 .   ? -24.526 34.932 4.837   1.00 34.47  ? 602 HOH   A O    1 
HETATM 2503 O  O    . HOH   C 3 .   ? 10.976  8.812  28.360  1.00 53.77  ? 603 HOH   A O    1 
HETATM 2504 O  O    . HOH   C 3 .   ? -9.237  17.456 8.286   1.00 40.44  ? 604 HOH   A O    1 
HETATM 2505 O  O    . HOH   C 3 .   ? -0.667  35.545 12.399  1.00 23.15  ? 605 HOH   A O    1 
HETATM 2506 O  O    . HOH   C 3 .   ? 3.872   41.584 7.172   1.00 28.33  ? 606 HOH   A O    1 
HETATM 2507 O  O    . HOH   C 3 .   ? -26.447 29.621 10.244  1.00 39.01  ? 607 HOH   A O    1 
HETATM 2508 O  O    . HOH   C 3 .   ? -0.954  28.415 24.085  1.00 25.88  ? 608 HOH   A O    1 
HETATM 2509 O  O    . HOH   C 3 .   ? 16.667  15.599 21.822  1.00 45.46  ? 609 HOH   A O    1 
HETATM 2510 O  O    . HOH   C 3 .   ? 3.832   46.641 11.915  1.00 40.56  ? 610 HOH   A O    1 
HETATM 2511 O  O    . HOH   C 3 .   ? -6.413  41.503 -8.132  1.00 38.32  ? 611 HOH   A O    1 
HETATM 2512 O  O    . HOH   C 3 .   ? -14.354 32.908 -8.115  1.00 32.02  ? 612 HOH   A O    1 
HETATM 2513 O  O    . HOH   C 3 .   ? -9.924  21.835 -4.724  1.00 36.81  ? 613 HOH   A O    1 
HETATM 2514 O  O    . HOH   C 3 .   ? 3.265   22.405 35.949  1.00 48.72  ? 614 HOH   A O    1 
HETATM 2515 O  O    . HOH   C 3 .   ? -10.687 13.672 23.604  0.50 25.82  ? 615 HOH   A O    1 
HETATM 2516 O  O    . HOH   C 3 .   ? -6.995  33.217 -4.403  1.00 18.49  ? 616 HOH   A O    1 
HETATM 2517 O  O    . HOH   C 3 .   ? 16.535  13.169 20.287  1.00 43.04  ? 617 HOH   A O    1 
HETATM 2518 O  O    . HOH   C 3 .   ? -10.259 27.974 21.724  1.00 31.90  ? 618 HOH   A O    1 
HETATM 2519 O  O    . HOH   C 3 .   ? 1.047   49.162 11.896  1.00 29.61  ? 619 HOH   A O    1 
HETATM 2520 O  O    . HOH   C 3 .   ? -21.328 37.876 -12.972 1.00 37.78  ? 620 HOH   A O    1 
HETATM 2521 O  O    . HOH   C 3 .   ? 4.097   23.866 6.977   1.00 34.74  ? 621 HOH   A O    1 
HETATM 2522 O  O    . HOH   C 3 .   ? -14.619 59.673 -4.327  1.00 52.41  ? 622 HOH   A O    1 
HETATM 2523 O  O    . HOH   C 3 .   ? -12.503 54.082 -6.503  1.00 37.06  ? 623 HOH   A O    1 
HETATM 2524 O  O    . HOH   C 3 .   ? -9.476  51.116 -2.506  1.00 35.03  ? 624 HOH   A O    1 
HETATM 2525 O  O    . HOH   C 3 .   ? -18.786 26.664 -1.861  1.00 44.01  ? 625 HOH   A O    1 
HETATM 2526 O  O    . HOH   C 3 .   ? -6.183  15.255 -1.775  1.00 51.61  ? 626 HOH   A O    1 
HETATM 2527 O  O    . HOH   C 3 .   ? -6.326  17.965 17.351  1.00 44.59  ? 627 HOH   A O    1 
HETATM 2528 O  O    . HOH   C 3 .   ? -9.532  60.540 9.978   1.00 44.74  ? 628 HOH   A O    1 
HETATM 2529 O  O    . HOH   C 3 .   ? -20.948 39.577 -16.081 1.00 46.60  ? 629 HOH   A O    1 
HETATM 2530 O  O    . HOH   C 3 .   ? 0.694   10.186 34.756  1.00 36.31  ? 630 HOH   A O    1 
HETATM 2531 O  O    . HOH   C 3 .   ? -3.981  4.894  17.077  1.00 49.94  ? 631 HOH   A O    1 
HETATM 2532 O  O    . HOH   C 3 .   ? -21.676 35.838 6.044   1.00 30.00  ? 632 HOH   A O    1 
HETATM 2533 O  O    . HOH   C 3 .   ? -17.225 55.606 -7.263  1.00 39.43  ? 633 HOH   A O    1 
HETATM 2534 O  O    . HOH   C 3 .   ? -17.690 53.853 15.689  1.00 51.67  ? 634 HOH   A O    1 
HETATM 2535 O  O    . HOH   C 3 .   ? -29.452 39.636 -3.456  1.00 48.68  ? 635 HOH   A O    1 
HETATM 2536 O  O    . HOH   C 3 .   ? -0.917  51.096 12.878  1.00 38.90  ? 636 HOH   A O    1 
HETATM 2537 O  O    . HOH   C 3 .   ? -19.190 47.481 13.968  1.00 36.29  ? 637 HOH   A O    1 
HETATM 2538 O  O    . HOH   C 3 .   ? 0.000   28.459 0.000   0.50 19.89  ? 638 HOH   A O    1 
HETATM 2539 O  O    . HOH   C 3 .   ? 12.303  13.116 33.185  1.00 49.89  ? 639 HOH   A O    1 
HETATM 2540 O  O    . HOH   C 3 .   ? -20.475 23.712 1.096   1.00 45.48  ? 640 HOH   A O    1 
HETATM 2541 O  O    . HOH   C 3 .   ? -0.532  19.830 37.322  1.00 45.37  ? 641 HOH   A O    1 
HETATM 2542 O  O    . HOH   C 3 .   ? -13.854 56.192 -6.490  1.00 46.47  ? 642 HOH   A O    1 
HETATM 2543 O  O    . HOH   C 3 .   ? 1.601   47.659 8.376   1.00 43.74  ? 643 HOH   A O    1 
HETATM 2544 O  O    . HOH   C 3 .   ? 5.214   17.543 11.776  1.00 35.66  ? 644 HOH   A O    1 
HETATM 2545 O  O    . HOH   C 3 .   ? -3.411  27.727 22.680  1.00 23.65  ? 645 HOH   A O    1 
HETATM 2546 O  O    . HOH   C 3 .   ? 5.003   31.561 8.169   1.00 35.55  ? 646 HOH   A O    1 
HETATM 2547 O  O    . HOH   C 3 .   ? -5.166  21.048 32.388  1.00 37.25  ? 647 HOH   A O    1 
HETATM 2548 O  O    . HOH   C 3 .   ? -25.197 48.533 -11.355 1.00 40.15  ? 648 HOH   A O    1 
HETATM 2549 O  O    . HOH   C 3 .   ? 6.155   26.855 17.108  1.00 30.53  ? 649 HOH   A O    1 
HETATM 2550 O  O    . HOH   C 3 .   ? 19.010  16.124 17.335  1.00 48.89  ? 650 HOH   A O    1 
HETATM 2551 O  O    . HOH   C 3 .   ? -10.667 38.452 -10.622 1.00 48.77  ? 651 HOH   A O    1 
HETATM 2552 O  O    . HOH   C 3 .   ? -2.297  27.728 -1.339  1.00 21.87  ? 652 HOH   A O    1 
HETATM 2553 O  O    . HOH   C 3 .   ? -22.442 39.724 19.741  1.00 47.02  ? 653 HOH   A O    1 
HETATM 2554 O  O    . HOH   C 3 .   ? 5.149   41.072 15.443  1.00 49.11  ? 654 HOH   A O    1 
HETATM 2555 O  O    . HOH   C 3 .   ? 7.198   21.168 35.918  1.00 47.26  ? 655 HOH   A O    1 
HETATM 2556 O  O    . HOH   C 3 .   ? -6.565  21.215 26.505  1.00 43.78  ? 656 HOH   A O    1 
HETATM 2557 O  O    . HOH   C 3 .   ? -3.428  42.539 23.041  1.00 39.56  ? 657 HOH   A O    1 
HETATM 2558 O  O    . HOH   C 3 .   ? 2.710   35.559 18.216  1.00 41.21  ? 658 HOH   A O    1 
HETATM 2559 O  O    . HOH   C 3 .   ? -0.647  37.711 3.683   1.00 31.49  ? 659 HOH   A O    1 
HETATM 2560 O  O    . HOH   C 3 .   ? 6.519   39.576 9.624   1.00 44.65  ? 660 HOH   A O    1 
HETATM 2561 O  O    . HOH   C 3 .   ? 2.165   33.044 17.781  1.00 39.56  ? 661 HOH   A O    1 
HETATM 2562 O  O    . HOH   C 3 .   ? -9.670  53.396 -3.425  1.00 45.40  ? 662 HOH   A O    1 
HETATM 2563 O  O    . HOH   C 3 .   ? 0.163   32.464 29.539  1.00 44.11  ? 663 HOH   A O    1 
HETATM 2564 O  O    . HOH   C 3 .   ? -8.957  48.572 20.661  1.00 39.73  ? 664 HOH   A O    1 
HETATM 2565 O  O    . HOH   C 3 .   ? 7.755   23.630 12.014  1.00 47.95  ? 665 HOH   A O    1 
HETATM 2566 O  O    . HOH   C 3 .   ? -2.656  45.882 1.584   1.00 45.15  ? 666 HOH   A O    1 
HETATM 2567 O  O    . HOH   C 3 .   ? -12.978 34.808 -10.567 1.00 47.00  ? 667 HOH   A O    1 
HETATM 2568 O  O    . HOH   C 3 .   ? -21.522 19.591 7.482   1.00 48.74  ? 668 HOH   A O    1 
HETATM 2569 O  O    . HOH   C 3 .   ? 3.875   19.122 10.171  1.00 46.18  ? 669 HOH   A O    1 
HETATM 2570 O  O    . HOH   C 3 .   ? -24.358 43.509 -11.996 1.00 46.81  ? 670 HOH   A O    1 
HETATM 2571 O  O    . HOH   C 3 .   ? 12.471  12.414 36.240  1.00 46.45  ? 671 HOH   A O    1 
HETATM 2572 O  O    . HOH   C 3 .   ? -23.176 58.630 -8.740  1.00 40.96  ? 672 HOH   A O    1 
HETATM 2573 O  O    . HOH   C 3 .   ? -21.164 56.907 -9.754  1.00 41.15  ? 673 HOH   A O    1 
HETATM 2574 O  O    . HOH   C 3 .   ? -8.630  55.115 20.773  1.00 50.83  ? 674 HOH   A O    1 
HETATM 2575 O  O    . HOH   C 3 .   ? 2.478   37.417 16.183  1.00 38.58  ? 675 HOH   A O    1 
HETATM 2576 O  O    . HOH   C 3 .   ? -12.321 48.835 -8.934  1.00 40.19  ? 676 HOH   A O    1 
HETATM 2577 O  O    . HOH   C 3 .   ? 6.184   27.619 35.166  1.00 50.82  ? 677 HOH   A O    1 
HETATM 2578 O  O    . HOH   C 3 .   ? 3.454   33.396 11.160  1.00 40.05  ? 678 HOH   A O    1 
HETATM 2579 O  O    . HOH   C 3 .   ? 2.898   24.575 33.831  1.00 42.84  ? 679 HOH   A O    1 
HETATM 2580 O  O    . HOH   C 3 .   ? -11.705 32.524 -8.931  1.00 34.95  ? 680 HOH   A O    1 
HETATM 2581 O  O    . HOH   C 3 .   ? 6.006   24.745 7.971   1.00 41.25  ? 681 HOH   A O    1 
HETATM 2582 O  O    . HOH   C 3 .   ? -13.727 48.827 -11.155 1.00 37.57  ? 682 HOH   A O    1 
HETATM 2583 O  O    . HOH   C 3 .   ? -6.483  53.313 20.989  1.00 58.29  ? 683 HOH   A O    1 
HETATM 2584 O  O    . HOH   C 3 .   ? -19.466 40.870 23.407  1.00 51.00  ? 684 HOH   A O    1 
HETATM 2585 O  O    . HOH   C 3 .   ? -6.892  35.250 -6.192  1.00 42.87  ? 685 HOH   A O    1 
HETATM 2586 O  O    . HOH   C 3 .   ? 2.168   35.278 12.732  1.00 40.65  ? 686 HOH   A O    1 
HETATM 2587 O  O    . HOH   C 3 .   ? 4.702   22.696 11.585  1.00 40.98  ? 687 HOH   A O    1 
HETATM 2588 O  O    . HOH   C 3 .   ? 6.334   23.655 35.748  1.00 47.76  ? 688 HOH   A O    1 
HETATM 2589 O  O    . HOH   C 3 .   ? -30.369 54.742 17.936  1.00 56.26  ? 689 HOH   A O    1 
HETATM 2590 O  O    . HOH   C 3 .   ? -3.477  49.019 20.132  1.00 41.60  ? 690 HOH   A O    1 
HETATM 2591 O  O    . HOH   C 3 .   ? -5.392  8.051  19.942  1.00 54.33  ? 691 HOH   A O    1 
HETATM 2592 O  O    . HOH   C 3 .   ? -16.613 17.582 0.207   1.00 46.75  ? 692 HOH   A O    1 
HETATM 2593 O  O    . HOH   C 3 .   ? 6.128   26.446 9.752   1.00 45.44  ? 693 HOH   A O    1 
HETATM 2594 O  O    . HOH   C 3 .   ? 3.722   45.798 7.485   1.00 46.41  ? 694 HOH   A O    1 
HETATM 2595 O  O    . HOH   C 3 .   ? 0.000   20.502 0.000   0.50 39.73  ? 695 HOH   A O    1 
HETATM 2596 O  O    . HOH   C 3 .   ? -7.119  51.187 -1.078  1.00 40.73  ? 696 HOH   A O    1 
HETATM 2597 O  O    . HOH   C 3 .   ? -5.979  53.401 0.098   1.00 47.56  ? 697 HOH   A O    1 
HETATM 2598 O  O    . HOH   C 3 .   ? 1.965   3.777  26.316  1.00 46.86  ? 698 HOH   A O    1 
HETATM 2599 O  O    . HOH   C 3 .   ? -13.646 16.966 8.339   1.00 43.60  ? 699 HOH   A O    1 
HETATM 2600 O  O    . HOH   C 3 .   ? -12.436 15.625 4.322   1.00 50.72  ? 700 HOH   A O    1 
HETATM 2601 O  O    . HOH   C 3 .   ? -7.541  30.439 -7.848  1.00 41.44  ? 701 HOH   A O    1 
HETATM 2602 O  O    . HOH   C 3 .   ? -3.968  21.203 -1.206  1.00 30.92  ? 702 HOH   A O    1 
HETATM 2603 O  O    . HOH   C 3 .   ? 18.205  11.040 20.898  1.00 50.57  ? 703 HOH   A O    1 
HETATM 2604 O  O    . HOH   C 3 .   ? 0.778   53.483 10.793  1.00 63.75  ? 704 HOH   A O    1 
HETATM 2605 O  O    . HOH   C 3 .   ? 1.008   5.205  35.386  1.00 51.78  ? 705 HOH   A O    1 
HETATM 2606 O  O    . HOH   C 3 .   ? -2.671  22.854 -2.793  1.00 28.62  ? 706 HOH   A O    1 
HETATM 2607 O  O    . HOH   C 3 .   ? 3.613   21.903 5.244   1.00 31.28  ? 707 HOH   A O    1 
HETATM 2608 O  O    . HOH   C 3 .   ? -14.336 55.389 15.834  1.00 46.22  ? 708 HOH   A O    1 
HETATM 2609 O  O    . HOH   C 3 .   ? 5.556   20.099 5.153   1.00 41.63  ? 709 HOH   A O    1 
HETATM 2610 O  O    . HOH   C 3 .   ? 6.644   24.507 14.618  1.00 46.72  ? 710 HOH   A O    1 
HETATM 2611 O  O    . HOH   C 3 .   ? 9.230   30.520 10.152  1.00 48.63  ? 711 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   . SER A 1   ? 0.3392 0.3205 0.2519 0.0631  -0.0058 0.0131  1   SER A N   
2    C CA  . SER A 1   ? 0.3735 0.3546 0.2923 0.0637  -0.0026 0.0170  1   SER A CA  
3    C C   . SER A 1   ? 0.3672 0.3432 0.2934 0.0602  0.0016  0.0187  1   SER A C   
4    O O   . SER A 1   ? 0.3292 0.3011 0.2548 0.0586  0.0026  0.0177  1   SER A O   
5    C CB  . SER A 1   ? 0.3843 0.3627 0.2961 0.0710  0.0011  0.0209  1   SER A CB  
6    O OG  . SER A 1   ? 0.4436 0.4275 0.3482 0.0752  -0.0026 0.0197  1   SER A OG  
7    N N   . GLY A 2   ? 0.3620 0.3385 0.2949 0.0593  0.0043  0.0215  2   GLY A N   
8    C CA  . GLY A 2   ? 0.3319 0.3051 0.2723 0.0561  0.0083  0.0231  2   GLY A CA  
9    C C   . GLY A 2   ? 0.3389 0.3167 0.2890 0.0501  0.0055  0.0214  2   GLY A C   
10   O O   . GLY A 2   ? 0.3225 0.3051 0.2735 0.0477  0.0005  0.0184  2   GLY A O   
11   N N   . PHE A 3   ? 0.2887 0.2654 0.2463 0.0476  0.0091  0.0233  3   PHE A N   
12   C CA  . PHE A 3   ? 0.3028 0.2838 0.2695 0.0421  0.0068  0.0219  3   PHE A CA  
13   C C   . PHE A 3   ? 0.3722 0.3514 0.3454 0.0393  0.0104  0.0229  3   PHE A C   
14   O O   . PHE A 3   ? 0.3561 0.3330 0.3309 0.0405  0.0154  0.0255  3   PHE A O   
15   C CB  . PHE A 3   ? 0.2749 0.2594 0.2449 0.0419  0.0064  0.0231  3   PHE A CB  
16   C CG  . PHE A 3   ? 0.2984 0.2880 0.2758 0.0369  0.0025  0.0210  3   PHE A CG  
17   C CD1 . PHE A 3   ? 0.3675 0.3610 0.3432 0.0356  -0.0030 0.0178  3   PHE A CD1 
18   C CD2 . PHE A 3   ? 0.3869 0.3774 0.3726 0.0332  0.0044  0.0219  3   PHE A CD2 
19   C CE1 . PHE A 3   ? 0.4119 0.4096 0.3942 0.0309  -0.0063 0.0158  3   PHE A CE1 
20   C CE2 . PHE A 3   ? 0.3255 0.3204 0.3176 0.0288  0.0008  0.0200  3   PHE A CE2 
21   C CZ  . PHE A 3   ? 0.3654 0.3636 0.3557 0.0278  -0.0043 0.0171  3   PHE A CZ  
22   N N   . ARG A 4   ? 0.2883 0.2688 0.2653 0.0358  0.0081  0.0208  4   ARG A N   
23   C CA  . ARG A 4   ? 0.2863 0.2661 0.2689 0.0338  0.0112  0.0216  4   ARG A CA  
24   C C   . ARG A 4   ? 0.2771 0.2611 0.2674 0.0290  0.0084  0.0200  4   ARG A C   
25   O O   . ARG A 4   ? 0.3143 0.3004 0.3042 0.0273  0.0040  0.0177  4   ARG A O   
26   C CB  . ARG A 4   ? 0.3226 0.2983 0.3003 0.0357  0.0123  0.0211  4   ARG A CB  
27   C CG  . ARG A 4   ? 0.3686 0.3398 0.3400 0.0403  0.0164  0.0233  4   ARG A CG  
28   C CD  . ARG A 4   ? 0.4141 0.3844 0.3901 0.0400  0.0214  0.0252  4   ARG A CD  
29   N NE  . ARG A 4   ? 0.4319 0.3974 0.4026 0.0441  0.0261  0.0273  4   ARG A NE  
30   C CZ  . ARG A 4   ? 0.4459 0.4111 0.4207 0.0440  0.0314  0.0293  4   ARG A CZ  
31   N NH1 . ARG A 4   ? 0.4064 0.3763 0.3907 0.0401  0.0325  0.0294  4   ARG A NH1 
32   N NH2 . ARG A 4   ? 0.3378 0.2981 0.3072 0.0479  0.0359  0.0311  4   ARG A NH2 
33   N N   . LYS A 5   ? 0.2781 0.2637 0.2754 0.0270  0.0110  0.0210  5   LYS A N   
34   C CA  . LYS A 5   ? 0.2853 0.2744 0.2889 0.0230  0.0085  0.0195  5   LYS A CA  
35   C C   . LYS A 5   ? 0.2673 0.2539 0.2672 0.0234  0.0070  0.0179  5   LYS A C   
36   O O   . LYS A 5   ? 0.3638 0.3488 0.3635 0.0248  0.0097  0.0187  5   LYS A O   
37   C CB  . LYS A 5   ? 0.3872 0.3798 0.3992 0.0209  0.0115  0.0208  5   LYS A CB  
38   C CG  . LYS A 5   ? 0.4804 0.4773 0.4988 0.0172  0.0095  0.0202  5   LYS A CG  
39   C CD  . LYS A 5   ? 0.5542 0.5535 0.5785 0.0157  0.0132  0.0217  5   LYS A CD  
40   C CE  . LYS A 5   ? 0.4932 0.4954 0.5217 0.0127  0.0111  0.0212  5   LYS A CE  
41   N NZ  . LYS A 5   ? 0.5633 0.5683 0.5986 0.0101  0.0146  0.0220  5   LYS A NZ  
42   N N   . MET A 6   ? 0.2577 0.2439 0.2547 0.0222  0.0029  0.0154  6   MET A N   
43   C CA  . MET A 6   ? 0.2793 0.2617 0.2707 0.0226  0.0017  0.0134  6   MET A CA  
44   C C   . MET A 6   ? 0.2680 0.2514 0.2635 0.0192  -0.0002 0.0118  6   MET A C   
45   O O   . MET A 6   ? 0.3238 0.3104 0.3229 0.0163  -0.0030 0.0105  6   MET A O   
46   C CB  . MET A 6   ? 0.3054 0.2862 0.2893 0.0236  -0.0011 0.0113  6   MET A CB  
47   C CG  . MET A 6   ? 0.4889 0.4643 0.4650 0.0252  -0.0008 0.0098  6   MET A CG  
48   S SD  . MET A 6   ? 0.4800 0.4557 0.4487 0.0250  -0.0050 0.0061  6   MET A SD  
49   C CE  . MET A 6   ? 0.4713 0.4467 0.4350 0.0301  -0.0031 0.0087  6   MET A CE  
50   N N   . ALA A 7   ? 0.2186 0.1992 0.2132 0.0200  0.0016  0.0120  7   ALA A N   
51   C CA  . ALA A 7   ? 0.2305 0.2111 0.2276 0.0175  0.0004  0.0107  7   ALA A CA  
52   C C   . ALA A 7   ? 0.2834 0.2584 0.2731 0.0170  -0.0011 0.0078  7   ALA A C   
53   O O   . ALA A 7   ? 0.2684 0.2396 0.2509 0.0188  -0.0009 0.0069  7   ALA A O   
54   C CB  . ALA A 7   ? 0.2243 0.2056 0.2250 0.0190  0.0035  0.0128  7   ALA A CB  
55   N N   . PHE A 8   ? 0.2465 0.2206 0.2375 0.0143  -0.0024 0.0060  8   PHE A N   
56   C CA  . PHE A 8   ? 0.2815 0.2492 0.2653 0.0134  -0.0029 0.0031  8   PHE A CA  
57   C C   . PHE A 8   ? 0.2614 0.2231 0.2402 0.0166  0.0008  0.0043  8   PHE A C   
58   O O   . PHE A 8   ? 0.2818 0.2453 0.2645 0.0188  0.0032  0.0072  8   PHE A O   
59   C CB  . PHE A 8   ? 0.2622 0.2296 0.2485 0.0097  -0.0045 0.0010  8   PHE A CB  
60   C CG  . PHE A 8   ? 0.2718 0.2436 0.2608 0.0063  -0.0082 -0.0012 8   PHE A CG  
61   C CD1 . PHE A 8   ? 0.2962 0.2669 0.2798 0.0049  -0.0103 -0.0045 8   PHE A CD1 
62   C CD2 . PHE A 8   ? 0.2889 0.2669 0.2859 0.0048  -0.0095 0.0002  8   PHE A CD2 
63   C CE1 . PHE A 8   ? 0.3400 0.3160 0.3263 0.0022  -0.0137 -0.0064 8   PHE A CE1 
64   C CE2 . PHE A 8   ? 0.3247 0.3070 0.3241 0.0021  -0.0127 -0.0015 8   PHE A CE2 
65   C CZ  . PHE A 8   ? 0.3473 0.3288 0.3415 0.0010  -0.0149 -0.0048 8   PHE A CZ  
66   N N   . PRO A 9   ? 0.2462 0.2013 0.2165 0.0170  0.0013  0.0020  9   PRO A N   
67   C CA  . PRO A 9   ? 0.2618 0.2102 0.2267 0.0200  0.0050  0.0030  9   PRO A CA  
68   C C   . PRO A 9   ? 0.2937 0.2409 0.2616 0.0196  0.0065  0.0039  9   PRO A C   
69   O O   . PRO A 9   ? 0.3142 0.2608 0.2832 0.0162  0.0048  0.0017  9   PRO A O   
70   C CB  . PRO A 9   ? 0.2846 0.2259 0.2399 0.0188  0.0047  -0.0008 9   PRO A CB  
71   C CG  . PRO A 9   ? 0.2862 0.2323 0.2416 0.0167  0.0008  -0.0030 9   PRO A CG  
72   C CD  . PRO A 9   ? 0.3038 0.2577 0.2689 0.0146  -0.0015 -0.0018 9   PRO A CD  
73   N N   . SER A 10  ? 0.2543 0.2014 0.2234 0.0234  0.0098  0.0070  10  SER A N   
74   C CA  . SER A 10  ? 0.2548 0.2036 0.2285 0.0241  0.0110  0.0088  10  SER A CA  
75   C C   . SER A 10  ? 0.2699 0.2099 0.2366 0.0257  0.0141  0.0084  10  SER A C   
76   O O   . SER A 10  ? 0.2684 0.2090 0.2376 0.0268  0.0153  0.0098  10  SER A O   
77   C CB  . SER A 10  ? 0.2507 0.2068 0.2310 0.0272  0.0127  0.0125  10  SER A CB  
78   O OG  . SER A 10  ? 0.2959 0.2486 0.2714 0.0313  0.0159  0.0141  10  SER A OG  
79   N N   . GLY A 11  ? 0.2669 0.1983 0.2243 0.0261  0.0155  0.0064  11  GLY A N   
80   C CA  . GLY A 11  ? 0.2721 0.1938 0.2218 0.0283  0.0195  0.0064  11  GLY A CA  
81   C C   . GLY A 11  ? 0.3023 0.2204 0.2518 0.0261  0.0198  0.0052  11  GLY A C   
82   O O   . GLY A 11  ? 0.3392 0.2538 0.2870 0.0294  0.0232  0.0073  11  GLY A O   
83   N N   . LYS A 12  ? 0.3109 0.2298 0.2619 0.0208  0.0166  0.0017  12  LYS A N   
84   C CA  . LYS A 12  ? 0.3156 0.2303 0.2660 0.0183  0.0171  0.0002  12  LYS A CA  
85   C C   . LYS A 12  ? 0.3374 0.2579 0.2949 0.0207  0.0175  0.0037  12  LYS A C   
86   O O   . LYS A 12  ? 0.3397 0.2550 0.2949 0.0214  0.0198  0.0040  12  LYS A O   
87   C CB  . LYS A 12  ? 0.2871 0.2042 0.2399 0.0122  0.0132  -0.0039 12  LYS A CB  
88   C CG  . LYS A 12  ? 0.3681 0.2772 0.3123 0.0087  0.0136  -0.0087 12  LYS A CG  
89   C CD  . LYS A 12  ? 0.4104 0.3255 0.3586 0.0032  0.0090  -0.0123 12  LYS A CD  
90   C CE  . LYS A 12  ? 0.6212 0.5305 0.5616 -0.0007 0.0089  -0.0177 12  LYS A CE  
91   N NZ  . LYS A 12  ? 0.6158 0.5219 0.5494 0.0020  0.0101  -0.0178 12  LYS A NZ  
92   N N   . VAL A 13  ? 0.2875 0.2186 0.2533 0.0220  0.0154  0.0063  13  VAL A N   
93   C CA  . VAL A 13  ? 0.2841 0.2221 0.2571 0.0241  0.0154  0.0093  13  VAL A CA  
94   C C   . VAL A 13  ? 0.2910 0.2290 0.2624 0.0302  0.0191  0.0129  13  VAL A C   
95   O O   . VAL A 13  ? 0.2904 0.2291 0.2628 0.0331  0.0209  0.0150  13  VAL A O   
96   C CB  . VAL A 13  ? 0.2555 0.2050 0.2383 0.0219  0.0116  0.0099  13  VAL A CB  
97   C CG1 . VAL A 13  ? 0.2450 0.2028 0.2357 0.0235  0.0115  0.0126  13  VAL A CG1 
98   C CG2 . VAL A 13  ? 0.2519 0.2014 0.2359 0.0164  0.0082  0.0065  13  VAL A CG2 
99   N N   . GLU A 14  ? 0.2755 0.2129 0.2443 0.0326  0.0205  0.0138  14  GLU A N   
100  C CA  . GLU A 14  ? 0.2513 0.1886 0.2183 0.0387  0.0244  0.0171  14  GLU A CA  
101  C C   . GLU A 14  ? 0.2925 0.2203 0.2519 0.0415  0.0281  0.0176  14  GLU A C   
102  O O   . GLU A 14  ? 0.3024 0.2327 0.2627 0.0465  0.0306  0.0208  14  GLU A O   
103  C CB  . GLU A 14  ? 0.2596 0.1942 0.2221 0.0407  0.0260  0.0175  14  GLU A CB  
104  C CG  . GLU A 14  ? 0.2463 0.1896 0.2155 0.0390  0.0234  0.0176  14  GLU A CG  
105  C CD  . GLU A 14  ? 0.2561 0.1946 0.2192 0.0401  0.0246  0.0171  14  GLU A CD  
106  O OE1 . GLU A 14  ? 0.3294 0.2629 0.2870 0.0445  0.0284  0.0187  14  GLU A OE1 
107  O OE2 . GLU A 14  ? 0.3129 0.2525 0.2764 0.0370  0.0219  0.0152  14  GLU A OE2 
108  N N   . GLY A 15  ? 0.3281 0.2449 0.2797 0.0384  0.0288  0.0143  15  GLY A N   
109  C CA  . GLY A 15  ? 0.3459 0.2515 0.2889 0.0410  0.0333  0.0146  15  GLY A CA  
110  C C   . GLY A 15  ? 0.3518 0.2593 0.2979 0.0417  0.0335  0.0159  15  GLY A C   
111  O O   . GLY A 15  ? 0.3592 0.2576 0.2982 0.0448  0.0377  0.0168  15  GLY A O   
112  N N   . CYS A 16  ? 0.3096 0.2278 0.2655 0.0391  0.0293  0.0160  16  CYS A N   
113  C CA  . CYS A 16  ? 0.3080 0.2287 0.2671 0.0398  0.0292  0.0172  16  CYS A CA  
114  C C   . CYS A 16  ? 0.3267 0.2601 0.2940 0.0440  0.0284  0.0209  16  CYS A C   
115  O O   . CYS A 16  ? 0.2827 0.2187 0.2523 0.0451  0.0282  0.0220  16  CYS A O   
116  C CB  . CYS A 16  ? 0.3218 0.2440 0.2851 0.0332  0.0254  0.0140  16  CYS A CB  
117  S SG  . CYS A 16  ? 0.3547 0.2670 0.3118 0.0266  0.0246  0.0087  16  CYS A SG  
118  N N   . MET A 17  ? 0.3083 0.2496 0.2796 0.0464  0.0280  0.0227  17  MET A N   
119  C CA  . MET A 17  ? 0.2681 0.2229 0.2480 0.0497  0.0272  0.0257  17  MET A CA  
120  C C   . MET A 17  ? 0.3384 0.2922 0.3141 0.0572  0.0314  0.0291  17  MET A C   
121  O O   . MET A 17  ? 0.3380 0.2839 0.3061 0.0609  0.0351  0.0300  17  MET A O   
122  C CB  . MET A 17  ? 0.2693 0.2334 0.2558 0.0487  0.0255  0.0260  17  MET A CB  
123  C CG  . MET A 17  ? 0.2966 0.2635 0.2880 0.0421  0.0214  0.0232  17  MET A CG  
124  S SD  . MET A 17  ? 0.2892 0.2597 0.2863 0.0371  0.0176  0.0215  17  MET A SD  
125  C CE  . MET A 17  ? 0.2995 0.2851 0.3063 0.0403  0.0172  0.0244  17  MET A CE  
126  N N   . VAL A 18  ? 0.2584 0.2205 0.2390 0.0598  0.0308  0.0310  18  VAL A N   
127  C CA  . VAL A 18  ? 0.2675 0.2312 0.2451 0.0677  0.0344  0.0345  18  VAL A CA  
128  C C   . VAL A 18  ? 0.3110 0.2925 0.2993 0.0696  0.0321  0.0364  18  VAL A C   
129  O O   . VAL A 18  ? 0.2701 0.2609 0.2674 0.0645  0.0281  0.0347  18  VAL A O   
130  C CB  . VAL A 18  ? 0.3259 0.2789 0.2955 0.0699  0.0370  0.0350  18  VAL A CB  
131  C CG1 . VAL A 18  ? 0.3732 0.3086 0.3325 0.0669  0.0395  0.0324  18  VAL A CG1 
132  C CG2 . VAL A 18  ? 0.3155 0.2744 0.2913 0.0663  0.0334  0.0339  18  VAL A CG2 
133  N N   . GLN A 19  ? 0.3184 0.3049 0.3056 0.0771  0.0348  0.0397  19  GLN A N   
134  C CA  . GLN A 19  ? 0.3186 0.3228 0.3154 0.0795  0.0329  0.0413  19  GLN A CA  
135  C C   . GLN A 19  ? 0.3208 0.3256 0.3155 0.0833  0.0333  0.0428  19  GLN A C   
136  O O   . GLN A 19  ? 0.3720 0.3653 0.3566 0.0883  0.0372  0.0445  19  GLN A O   
137  C CB  . GLN A 19  ? 0.3639 0.3763 0.3622 0.0858  0.0355  0.0440  19  GLN A CB  
138  C CG  . GLN A 19  ? 0.3812 0.4141 0.3910 0.0868  0.0331  0.0447  19  GLN A CG  
139  C CD  . GLN A 19  ? 0.4736 0.5154 0.4857 0.0922  0.0357  0.0469  19  GLN A CD  
140  O OE1 . GLN A 19  ? 0.4478 0.4799 0.4520 0.0963  0.0395  0.0485  19  GLN A OE1 
141  N NE2 . GLN A 19  ? 0.4983 0.5587 0.5211 0.0922  0.0338  0.0469  19  GLN A NE2 
142  N N   . VAL A 20  ? 0.2717 0.2891 0.2751 0.0810  0.0295  0.0421  20  VAL A N   
143  C CA  . VAL A 20  ? 0.2887 0.3086 0.2910 0.0847  0.0295  0.0435  20  VAL A CA  
144  C C   . VAL A 20  ? 0.2921 0.3319 0.3031 0.0886  0.0280  0.0451  20  VAL A C   
145  O O   . VAL A 20  ? 0.2935 0.3460 0.3148 0.0838  0.0247  0.0433  20  VAL A O   
146  C CB  . VAL A 20  ? 0.2993 0.3155 0.3035 0.0779  0.0262  0.0409  20  VAL A CB  
147  C CG1 . VAL A 20  ? 0.2596 0.2790 0.2624 0.0824  0.0264  0.0426  20  VAL A CG1 
148  C CG2 . VAL A 20  ? 0.3317 0.3299 0.3280 0.0737  0.0276  0.0388  20  VAL A CG2 
149  N N   . THR A 21  ? 0.3163 0.3589 0.3230 0.0971  0.0304  0.0484  21  THR A N   
150  C CA  . THR A 21  ? 0.3229 0.3855 0.3372 0.1019  0.0292  0.0500  21  THR A CA  
151  C C   . THR A 21  ? 0.3633 0.4282 0.3747 0.1070  0.0292  0.0517  21  THR A C   
152  O O   . THR A 21  ? 0.3766 0.4279 0.3770 0.1123  0.0329  0.0539  21  THR A O   
153  C CB  . THR A 21  ? 0.3879 0.4546 0.4001 0.1094  0.0328  0.0529  21  THR A CB  
154  O OG1 . THR A 21  ? 0.3420 0.4058 0.3565 0.1048  0.0331  0.0513  21  THR A OG1 
155  C CG2 . THR A 21  ? 0.4303 0.5198 0.4513 0.1140  0.0313  0.0541  21  THR A CG2 
156  N N   . CYS A 22  ? 0.3134 0.3953 0.3341 0.1054  0.0253  0.0507  22  CYS A N   
157  C CA  . CYS A 22  ? 0.3177 0.4050 0.3367 0.1106  0.0247  0.0524  22  CYS A CA  
158  C C   . CYS A 22  ? 0.3492 0.4604 0.3774 0.1145  0.0228  0.0530  22  CYS A C   
159  O O   . CYS A 22  ? 0.3389 0.4638 0.3783 0.1080  0.0190  0.0500  22  CYS A O   
160  C CB  . CYS A 22  ? 0.2918 0.3745 0.3125 0.1035  0.0215  0.0497  22  CYS A CB  
161  S SG  . CYS A 22  ? 0.4704 0.5584 0.4883 0.1097  0.0209  0.0517  22  CYS A SG  
162  N N   . GLY A 23  ? 0.4105 0.5268 0.4341 0.1249  0.0257  0.0567  23  GLY A N   
163  C CA  . GLY A 23  ? 0.4394 0.5790 0.4715 0.1292  0.0243  0.0573  23  GLY A CA  
164  C C   . GLY A 23  ? 0.3715 0.5171 0.4104 0.1257  0.0246  0.0560  23  GLY A C   
165  O O   . GLY A 23  ? 0.4380 0.5723 0.4703 0.1287  0.0285  0.0578  23  GLY A O   
166  N N   . THR A 24  ? 0.3306 0.4935 0.3821 0.1195  0.0210  0.0528  24  THR A N   
167  C CA  . THR A 24  ? 0.4033 0.5705 0.4614 0.1147  0.0214  0.0510  24  THR A CA  
168  C C   . THR A 24  ? 0.3173 0.4765 0.3795 0.1033  0.0192  0.0472  24  THR A C   
169  O O   . THR A 24  ? 0.3598 0.5224 0.4279 0.0985  0.0194  0.0454  24  THR A O   
170  C CB  . THR A 24  ? 0.3713 0.5642 0.4409 0.1159  0.0200  0.0500  24  THR A CB  
171  O OG1 . THR A 24  ? 0.4909 0.6972 0.5676 0.1124  0.0159  0.0475  24  THR A OG1 
172  C CG2 . THR A 24  ? 0.4627 0.6636 0.5284 0.1277  0.0229  0.0540  24  THR A CG2 
173  N N   . THR A 25  ? 0.2914 0.4404 0.3505 0.0992  0.0172  0.0460  25  THR A N   
174  C CA  . THR A 25  ? 0.3023 0.4434 0.3646 0.0889  0.0151  0.0426  25  THR A CA  
175  C C   . THR A 25  ? 0.3295 0.4488 0.3823 0.0880  0.0177  0.0433  25  THR A C   
176  O O   . THR A 25  ? 0.3035 0.4097 0.3461 0.0929  0.0199  0.0455  25  THR A O   
177  C CB  . THR A 25  ? 0.3079 0.4503 0.3723 0.0848  0.0117  0.0408  25  THR A CB  
178  O OG1 . THR A 25  ? 0.3034 0.4665 0.3755 0.0868  0.0095  0.0403  25  THR A OG1 
179  C CG2 . THR A 25  ? 0.3005 0.4377 0.3697 0.0743  0.0094  0.0373  25  THR A CG2 
180  N N   . THR A 26  ? 0.3085 0.4238 0.3642 0.0819  0.0177  0.0414  26  THR A N   
181  C CA  . THR A 26  ? 0.2971 0.3931 0.3435 0.0816  0.0202  0.0419  26  THR A CA  
182  C C   . THR A 26  ? 0.2549 0.3451 0.3047 0.0724  0.0181  0.0388  26  THR A C   
183  O O   . THR A 26  ? 0.2524 0.3538 0.3116 0.0671  0.0159  0.0366  26  THR A O   
184  C CB  . THR A 26  ? 0.3373 0.4329 0.3805 0.0874  0.0240  0.0442  26  THR A CB  
185  O OG1 . THR A 26  ? 0.3896 0.4666 0.4242 0.0861  0.0261  0.0442  26  THR A OG1 
186  C CG2 . THR A 26  ? 0.3559 0.4660 0.4095 0.0842  0.0233  0.0428  26  THR A CG2 
187  N N   . LEU A 27  ? 0.2373 0.3100 0.2790 0.0704  0.0190  0.0384  27  LEU A N   
188  C CA  . LEU A 27  ? 0.2497 0.3155 0.2930 0.0625  0.0172  0.0356  27  LEU A CA  
189  C C   . LEU A 27  ? 0.2447 0.2918 0.2774 0.0627  0.0192  0.0356  27  LEU A C   
190  O O   . LEU A 27  ? 0.2867 0.3263 0.3112 0.0687  0.0224  0.0378  27  LEU A O   
191  C CB  . LEU A 27  ? 0.2021 0.2721 0.2513 0.0564  0.0134  0.0333  27  LEU A CB  
192  C CG  . LEU A 27  ? 0.2388 0.3069 0.2851 0.0583  0.0124  0.0339  27  LEU A CG  
193  C CD1 . LEU A 27  ? 0.2444 0.2945 0.2800 0.0593  0.0141  0.0342  27  LEU A CD1 
194  C CD2 . LEU A 27  ? 0.2308 0.3053 0.2846 0.0517  0.0087  0.0314  27  LEU A CD2 
195  N N   . ASN A 28  ? 0.2303 0.2700 0.2629 0.0561  0.0175  0.0332  28  ASN A N   
196  C CA  . ASN A 28  ? 0.2305 0.2537 0.2538 0.0552  0.0190  0.0324  28  ASN A CA  
197  C C   . ASN A 28  ? 0.2412 0.2553 0.2601 0.0531  0.0180  0.0313  28  ASN A C   
198  O O   . ASN A 28  ? 0.2331 0.2529 0.2574 0.0499  0.0151  0.0303  28  ASN A O   
199  C CB  . ASN A 28  ? 0.2104 0.2313 0.2357 0.0497  0.0177  0.0303  28  ASN A CB  
200  C CG  . ASN A 28  ? 0.2844 0.3135 0.3141 0.0512  0.0191  0.0313  28  ASN A CG  
201  O OD1 . ASN A 28  ? 0.2785 0.3032 0.3029 0.0556  0.0222  0.0328  28  ASN A OD1 
202  N ND2 . ASN A 28  ? 0.2341 0.2752 0.2734 0.0478  0.0171  0.0304  28  ASN A ND2 
203  N N   . GLY A 29  ? 0.2242 0.2238 0.2329 0.0548  0.0207  0.0313  29  GLY A N   
204  C CA  . GLY A 29  ? 0.2336 0.2227 0.2374 0.0519  0.0203  0.0296  29  GLY A CA  
205  C C   . GLY A 29  ? 0.2461 0.2219 0.2431 0.0482  0.0211  0.0272  29  GLY A C   
206  O O   . GLY A 29  ? 0.2704 0.2431 0.2643 0.0493  0.0227  0.0274  29  GLY A O   
207  N N   . LEU A 30  ? 0.2604 0.2284 0.2548 0.0439  0.0201  0.0249  30  LEU A N   
208  C CA  . LEU A 30  ? 0.3051 0.2615 0.2936 0.0394  0.0204  0.0219  30  LEU A CA  
209  C C   . LEU A 30  ? 0.2918 0.2343 0.2705 0.0409  0.0241  0.0214  30  LEU A C   
210  O O   . LEU A 30  ? 0.2847 0.2259 0.2636 0.0402  0.0240  0.0213  30  LEU A O   
211  C CB  . LEU A 30  ? 0.2567 0.2171 0.2517 0.0324  0.0159  0.0190  30  LEU A CB  
212  C CG  . LEU A 30  ? 0.2573 0.2092 0.2480 0.0274  0.0152  0.0155  30  LEU A CG  
213  C CD1 . LEU A 30  ? 0.2541 0.2080 0.2449 0.0274  0.0148  0.0154  30  LEU A CD1 
214  C CD2 . LEU A 30  ? 0.2389 0.1944 0.2354 0.0213  0.0112  0.0131  30  LEU A CD2 
215  N N   . TRP A 31  ? 0.3063 0.2381 0.2760 0.0428  0.0278  0.0211  31  TRP A N   
216  C CA  . TRP A 31  ? 0.3247 0.2420 0.2837 0.0448  0.0327  0.0209  31  TRP A CA  
217  C C   . TRP A 31  ? 0.3333 0.2400 0.2876 0.0380  0.0326  0.0163  31  TRP A C   
218  O O   . TRP A 31  ? 0.3267 0.2297 0.2778 0.0361  0.0327  0.0144  31  TRP A O   
219  C CB  . TRP A 31  ? 0.2764 0.1886 0.2282 0.0515  0.0374  0.0236  31  TRP A CB  
220  C CG  . TRP A 31  ? 0.3387 0.2355 0.2787 0.0548  0.0434  0.0240  31  TRP A CG  
221  C CD1 . TRP A 31  ? 0.3370 0.2252 0.2724 0.0541  0.0457  0.0233  31  TRP A CD1 
222  C CD2 . TRP A 31  ? 0.4039 0.2908 0.3342 0.0594  0.0486  0.0253  31  TRP A CD2 
223  N NE1 . TRP A 31  ? 0.3774 0.2504 0.3005 0.0581  0.0523  0.0241  31  TRP A NE1 
224  C CE2 . TRP A 31  ? 0.4219 0.2940 0.3417 0.0614  0.0541  0.0253  31  TRP A CE2 
225  C CE3 . TRP A 31  ? 0.3911 0.2799 0.3204 0.0621  0.0494  0.0264  31  TRP A CE3 
226  C CZ2 . TRP A 31  ? 0.4317 0.2906 0.3400 0.0660  0.0605  0.0264  31  TRP A CZ2 
227  C CZ3 . TRP A 31  ? 0.4120 0.2882 0.3301 0.0668  0.0554  0.0276  31  TRP A CZ3 
228  C CH2 . TRP A 31  ? 0.4399 0.3012 0.3475 0.0686  0.0610  0.0276  31  TRP A CH2 
229  N N   . LEU A 32  ? 0.3228 0.2251 0.2766 0.0344  0.0323  0.0144  32  LEU A N   
230  C CA  . LEU A 32  ? 0.3034 0.1967 0.2534 0.0276  0.0323  0.0096  32  LEU A CA  
231  C C   . LEU A 32  ? 0.3692 0.2489 0.3105 0.0283  0.0375  0.0091  32  LEU A C   
232  O O   . LEU A 32  ? 0.3577 0.2389 0.3006 0.0307  0.0381  0.0112  32  LEU A O   
233  C CB  . LEU A 32  ? 0.3422 0.2445 0.3014 0.0212  0.0266  0.0072  32  LEU A CB  
234  C CG  . LEU A 32  ? 0.3044 0.2199 0.2724 0.0202  0.0217  0.0078  32  LEU A CG  
235  C CD1 . LEU A 32  ? 0.2823 0.2063 0.2592 0.0151  0.0169  0.0062  32  LEU A CD1 
236  C CD2 . LEU A 32  ? 0.2957 0.2075 0.2597 0.0181  0.0216  0.0053  32  LEU A CD2 
237  N N   . ASP A 33  ? 0.3891 0.2553 0.3208 0.0261  0.0414  0.0061  33  ASP A N   
238  C CA  . ASP A 33  ? 0.3798 0.2307 0.3014 0.0273  0.0478  0.0056  33  ASP A CA  
239  C C   . ASP A 33  ? 0.4295 0.2805 0.3486 0.0364  0.0513  0.0113  33  ASP A C   
240  O O   . ASP A 33  ? 0.4081 0.2640 0.3274 0.0419  0.0515  0.0144  33  ASP A O   
241  C CB  . ASP A 33  ? 0.4170 0.2649 0.3404 0.0208  0.0469  0.0022  33  ASP A CB  
242  C CG  . ASP A 33  ? 0.4965 0.3466 0.4231 0.0123  0.0431  -0.0033 33  ASP A CG  
243  O OD1 . ASP A 33  ? 0.5235 0.3671 0.4439 0.0105  0.0448  -0.0059 33  ASP A OD1 
244  O OD2 . ASP A 33  ? 0.5413 0.3996 0.4760 0.0077  0.0385  -0.0049 33  ASP A OD2 
245  N N   . ASP A 34  ? 0.4139 0.2604 0.3306 0.0387  0.0541  0.0128  34  ASP A N   
246  C CA  . ASP A 34  ? 0.4453 0.2928 0.3592 0.0481  0.0573  0.0183  34  ASP A CA  
247  C C   . ASP A 34  ? 0.4023 0.2663 0.3271 0.0504  0.0522  0.0211  34  ASP A C   
248  O O   . ASP A 34  ? 0.4025 0.2666 0.3252 0.0565  0.0546  0.0246  34  ASP A O   
249  C CB  . ASP A 34  ? 0.4132 0.2436 0.3153 0.0508  0.0648  0.0188  34  ASP A CB  
250  C CG  . ASP A 34  ? 0.5357 0.3628 0.4395 0.0455  0.0643  0.0162  34  ASP A CG  
251  O OD1 . ASP A 34  ? 0.4700 0.3067 0.3834 0.0388  0.0582  0.0134  34  ASP A OD1 
252  O OD2 . ASP A 34  ? 0.5294 0.3439 0.4245 0.0484  0.0704  0.0172  34  ASP A OD2 
253  N N   . VAL A 35  ? 0.3580 0.2358 0.2938 0.0459  0.0456  0.0197  35  VAL A N   
254  C CA  . VAL A 35  ? 0.3265 0.2198 0.2727 0.0471  0.0408  0.0219  35  VAL A CA  
255  C C   . VAL A 35  ? 0.3491 0.2565 0.3034 0.0479  0.0368  0.0230  35  VAL A C   
256  O O   . VAL A 35  ? 0.3225 0.2296 0.2778 0.0439  0.0352  0.0207  35  VAL A O   
257  C CB  . VAL A 35  ? 0.3288 0.2248 0.2812 0.0397  0.0369  0.0188  35  VAL A CB  
258  C CG1 . VAL A 35  ? 0.3379 0.2501 0.3010 0.0409  0.0321  0.0209  35  VAL A CG1 
259  C CG2 . VAL A 35  ? 0.3720 0.2537 0.3164 0.0387  0.0414  0.0175  35  VAL A CG2 
260  N N   . VAL A 36  ? 0.3199 0.2397 0.2799 0.0531  0.0353  0.0265  36  VAL A N   
261  C CA  . VAL A 36  ? 0.3053 0.2399 0.2742 0.0535  0.0315  0.0275  36  VAL A CA  
262  C C   . VAL A 36  ? 0.3042 0.2520 0.2839 0.0501  0.0263  0.0270  36  VAL A C   
263  O O   . VAL A 36  ? 0.3151 0.2663 0.2958 0.0529  0.0264  0.0287  36  VAL A O   
264  C CB  . VAL A 36  ? 0.2957 0.2355 0.2630 0.0621  0.0342  0.0316  36  VAL A CB  
265  C CG1 . VAL A 36  ? 0.2805 0.2371 0.2584 0.0617  0.0302  0.0323  36  VAL A CG1 
266  C CG2 . VAL A 36  ? 0.3275 0.2539 0.2841 0.0650  0.0393  0.0319  36  VAL A CG2 
267  N N   . TYR A 37  ? 0.2651 0.2196 0.2522 0.0441  0.0221  0.0247  37  TYR A N   
268  C CA  . TYR A 37  ? 0.2481 0.2145 0.2454 0.0403  0.0174  0.0240  37  TYR A CA  
269  C C   . TYR A 37  ? 0.2454 0.2264 0.2506 0.0424  0.0155  0.0257  37  TYR A C   
270  O O   . TYR A 37  ? 0.2720 0.2538 0.2772 0.0425  0.0159  0.0256  37  TYR A O   
271  C CB  . TYR A 37  ? 0.2635 0.2275 0.2637 0.0323  0.0143  0.0203  37  TYR A CB  
272  C CG  . TYR A 37  ? 0.2893 0.2395 0.2823 0.0292  0.0162  0.0179  37  TYR A CG  
273  C CD1 . TYR A 37  ? 0.2755 0.2136 0.2596 0.0295  0.0196  0.0167  37  TYR A CD1 
274  C CD2 . TYR A 37  ? 0.2873 0.2367 0.2823 0.0260  0.0149  0.0167  37  TYR A CD2 
275  C CE1 . TYR A 37  ? 0.3114 0.2372 0.2891 0.0263  0.0218  0.0141  37  TYR A CE1 
276  C CE2 . TYR A 37  ? 0.3109 0.2479 0.2996 0.0230  0.0171  0.0143  37  TYR A CE2 
277  C CZ  . TYR A 37  ? 0.3479 0.2732 0.3280 0.0229  0.0205  0.0129  37  TYR A CZ  
278  O OH  . TYR A 37  ? 0.3918 0.3048 0.3656 0.0194  0.0231  0.0100  37  TYR A OH  
279  N N   . CYS A 38  ? 0.2192 0.2119 0.2310 0.0437  0.0136  0.0270  38  CYS A N   
280  C CA  . CYS A 38  ? 0.1789 0.1862 0.1990 0.0445  0.0118  0.0279  38  CYS A CA  
281  C C   . CYS A 38  ? 0.2437 0.2629 0.2724 0.0422  0.0084  0.0275  38  CYS A C   
282  O O   . CYS A 38  ? 0.2125 0.2290 0.2401 0.0414  0.0078  0.0272  38  CYS A O   
283  C CB  . CYS A 38  ? 0.2032 0.2139 0.2204 0.0522  0.0149  0.0309  38  CYS A CB  
284  S SG  . CYS A 38  ? 0.2746 0.2904 0.2901 0.0593  0.0162  0.0338  38  CYS A SG  
285  N N   . PRO A 39  ? 0.2111 0.2434 0.2484 0.0406  0.0064  0.0273  39  PRO A N   
286  C CA  . PRO A 39  ? 0.1872 0.2311 0.2325 0.0382  0.0035  0.0266  39  PRO A CA  
287  C C   . PRO A 39  ? 0.2036 0.2532 0.2476 0.0443  0.0043  0.0288  39  PRO A C   
288  O O   . PRO A 39  ? 0.2116 0.2638 0.2527 0.0508  0.0067  0.0310  39  PRO A O   
289  C CB  . PRO A 39  ? 0.1607 0.2167 0.2144 0.0360  0.0025  0.0260  39  PRO A CB  
290  C CG  . PRO A 39  ? 0.1499 0.1974 0.2000 0.0347  0.0039  0.0255  39  PRO A CG  
291  C CD  . PRO A 39  ? 0.2322 0.2679 0.2722 0.0398  0.0069  0.0270  39  PRO A CD  
292  N N   . ARG A 40  ? 0.2026 0.2545 0.2488 0.0425  0.0023  0.0281  40  ARG A N   
293  C CA  . ARG A 40  ? 0.1998 0.2570 0.2441 0.0486  0.0030  0.0302  40  ARG A CA  
294  C C   . ARG A 40  ? 0.2269 0.3022 0.2784 0.0516  0.0021  0.0310  40  ARG A C   
295  O O   . ARG A 40  ? 0.2267 0.3079 0.2760 0.0585  0.0031  0.0332  40  ARG A O   
296  C CB  . ARG A 40  ? 0.2221 0.2776 0.2668 0.0460  0.0012  0.0293  40  ARG A CB  
297  C CG  . ARG A 40  ? 0.2152 0.2820 0.2698 0.0399  -0.0026 0.0270  40  ARG A CG  
298  C CD  . ARG A 40  ? 0.1945 0.2577 0.2484 0.0375  -0.0041 0.0263  40  ARG A CD  
299  N NE  . ARG A 40  ? 0.2196 0.2919 0.2823 0.0312  -0.0073 0.0240  40  ARG A NE  
300  C CZ  . ARG A 40  ? 0.3114 0.3847 0.3756 0.0289  -0.0091 0.0232  40  ARG A CZ  
301  N NH1 . ARG A 40  ? 0.2488 0.3146 0.3066 0.0323  -0.0079 0.0244  40  ARG A NH1 
302  N NH2 . ARG A 40  ? 0.2077 0.2895 0.2798 0.0233  -0.0116 0.0211  40  ARG A NH2 
303  N N   . HIS A 41  ? 0.1838 0.2679 0.2434 0.0468  0.0004  0.0292  41  HIS A N   
304  C CA  . HIS A 41  ? 0.1776 0.2795 0.2448 0.0485  -0.0003 0.0292  41  HIS A CA  
305  C C   . HIS A 41  ? 0.2402 0.3450 0.3035 0.0567  0.0026  0.0320  41  HIS A C   
306  O O   . HIS A 41  ? 0.2362 0.3566 0.3045 0.0601  0.0022  0.0326  41  HIS A O   
307  C CB  . HIS A 41  ? 0.2205 0.3277 0.2954 0.0418  -0.0013 0.0268  41  HIS A CB  
308  C CG  . HIS A 41  ? 0.2734 0.3992 0.3578 0.0407  -0.0025 0.0256  41  HIS A CG  
309  N ND1 . HIS A 41  ? 0.2419 0.3769 0.3315 0.0379  -0.0050 0.0240  41  HIS A ND1 
310  C CD2 . HIS A 41  ? 0.2429 0.3798 0.3327 0.0413  -0.0014 0.0254  41  HIS A CD2 
311  C CE1 . HIS A 41  ? 0.2803 0.4316 0.3781 0.0366  -0.0055 0.0226  41  HIS A CE1 
312  N NE2 . HIS A 41  ? 0.2771 0.4300 0.3754 0.0386  -0.0032 0.0234  41  HIS A NE2 
313  N N   . VAL A 42  ? 0.2050 0.2956 0.2594 0.0601  0.0055  0.0337  42  VAL A N   
314  C CA  . VAL A 42  ? 0.2170 0.3092 0.2670 0.0682  0.0087  0.0366  42  VAL A CA  
315  C C   . VAL A 42  ? 0.2455 0.3447 0.2929 0.0759  0.0092  0.0390  42  VAL A C   
316  O O   . VAL A 42  ? 0.2433 0.3506 0.2902 0.0829  0.0111  0.0413  42  VAL A O   
317  C CB  . VAL A 42  ? 0.2297 0.3035 0.2695 0.0700  0.0121  0.0377  42  VAL A CB  
318  C CG1 . VAL A 42  ? 0.2385 0.2979 0.2693 0.0716  0.0134  0.0385  42  VAL A CG1 
319  C CG2 . VAL A 42  ? 0.2384 0.3147 0.2749 0.0775  0.0155  0.0405  42  VAL A CG2 
320  N N   . ILE A 43  ? 0.2596 0.3566 0.3055 0.0752  0.0077  0.0387  43  ILE A N   
321  C CA  . ILE A 43  ? 0.2811 0.3841 0.3236 0.0833  0.0084  0.0413  43  ILE A CA  
322  C C   . ILE A 43  ? 0.3153 0.4405 0.3676 0.0834  0.0052  0.0403  43  ILE A C   
323  O O   . ILE A 43  ? 0.3688 0.5022 0.4196 0.0898  0.0050  0.0421  43  ILE A O   
324  C CB  . ILE A 43  ? 0.2618 0.3520 0.2969 0.0837  0.0089  0.0418  43  ILE A CB  
325  C CG1 . ILE A 43  ? 0.2791 0.3746 0.3212 0.0764  0.0048  0.0389  43  ILE A CG1 
326  C CG2 . ILE A 43  ? 0.3238 0.3921 0.3493 0.0827  0.0123  0.0421  43  ILE A CG2 
327  C CD1 . ILE A 43  ? 0.2792 0.3613 0.3144 0.0761  0.0054  0.0391  43  ILE A CD1 
328  N N   . CYS A 44  ? 0.2994 0.3620 0.2841 0.0716  -0.0354 0.0568  44  CYS A N   
329  C CA  . CYS A 44  ? 0.2877 0.3624 0.2696 0.0675  -0.0406 0.0586  44  CYS A CA  
330  C C   . CYS A 44  ? 0.3404 0.4294 0.3318 0.0722  -0.0443 0.0626  44  CYS A C   
331  O O   . CYS A 44  ? 0.3587 0.4504 0.3591 0.0755  -0.0424 0.0599  44  CYS A O   
332  C CB  . CYS A 44  ? 0.3532 0.4288 0.3324 0.0600  -0.0399 0.0519  44  CYS A CB  
333  S SG  . CYS A 44  ? 0.3911 0.4526 0.3584 0.0537  -0.0360 0.0485  44  CYS A SG  
334  N N   . THR A 45  ? 0.4445 0.5433 0.4341 0.0722  -0.0495 0.0695  45  THR A N   
335  C CA  . THR A 45  ? 0.3775 0.4928 0.3757 0.0746  -0.0537 0.0734  45  THR A CA  
336  C C   . THR A 45  ? 0.4467 0.5704 0.4422 0.0665  -0.0568 0.0690  45  THR A C   
337  O O   . THR A 45  ? 0.4314 0.5478 0.4176 0.0594  -0.0557 0.0638  45  THR A O   
338  C CB  . THR A 45  ? 0.4214 0.5456 0.4200 0.0775  -0.0585 0.0837  45  THR A CB  
339  O OG1 . THR A 45  ? 0.4463 0.5721 0.4331 0.0692  -0.0627 0.0852  45  THR A OG1 
340  C CG2 . THR A 45  ? 0.4604 0.5744 0.4602 0.0850  -0.0550 0.0880  45  THR A CG2 
341  N N   . SER A 46  ? 0.4882 0.6271 0.4920 0.0677  -0.0605 0.0714  46  SER A N   
342  C CA  . SER A 46  ? 0.4848 0.6322 0.4860 0.0600  -0.0638 0.0676  46  SER A CA  
343  C C   . SER A 46  ? 0.5457 0.6909 0.5325 0.0510  -0.0670 0.0680  46  SER A C   
344  O O   . SER A 46  ? 0.6045 0.7451 0.5841 0.0438  -0.0660 0.0615  46  SER A O   
345  C CB  . SER A 46  ? 0.5685 0.7314 0.5797 0.0615  -0.0676 0.0715  46  SER A CB  
346  O OG  . SER A 46  ? 0.6122 0.7751 0.6347 0.0670  -0.0635 0.0678  46  SER A OG  
347  N N   . GLU A 47  ? 0.5529 0.7005 0.5348 0.0512  -0.0705 0.0758  47  GLU A N   
348  C CA  . GLU A 47  ? 0.5818 0.7271 0.5486 0.0420  -0.0736 0.0765  47  GLU A CA  
349  C C   . GLU A 47  ? 0.6491 0.7759 0.6050 0.0392  -0.0682 0.0712  47  GLU A C   
350  O O   . GLU A 47  ? 0.6961 0.8181 0.6383 0.0308  -0.0690 0.0694  47  GLU A O   
351  C CB  . GLU A 47  ? 0.6489 0.8031 0.6140 0.0423  -0.0795 0.0870  47  GLU A CB  
352  C CG  . GLU A 47  ? 0.7442 0.9102 0.7202 0.0422  -0.0823 0.0896  47  GLU A CG  
353  C CD  . GLU A 47  ? 0.8402 1.0091 0.8326 0.0530  -0.0793 0.0921  47  GLU A CD  
354  O OE1 . GLU A 47  ? 0.6772 0.8383 0.6728 0.0602  -0.0747 0.0905  47  GLU A OE1 
355  O OE2 . GLU A 47  ? 1.0419 1.2202 1.0434 0.0540  -0.0809 0.0955  47  GLU A OE2 
356  N N   . ASP A 48  ? 0.5156 0.6316 0.4766 0.0457  -0.0625 0.0689  48  ASP A N   
357  C CA  . ASP A 48  ? 0.5316 0.6311 0.4838 0.0435  -0.0571 0.0645  48  ASP A CA  
358  C C   . ASP A 48  ? 0.4755 0.5681 0.4266 0.0393  -0.0525 0.0555  48  ASP A C   
359  O O   . ASP A 48  ? 0.5237 0.6040 0.4662 0.0357  -0.0482 0.0520  48  ASP A O   
360  C CB  . ASP A 48  ? 0.4983 0.5890 0.4561 0.0516  -0.0532 0.0663  48  ASP A CB  
361  C CG  . ASP A 48  ? 0.5764 0.6699 0.5335 0.0556  -0.0564 0.0752  48  ASP A CG  
362  O OD1 . ASP A 48  ? 0.5583 0.6533 0.5051 0.0503  -0.0601 0.0790  48  ASP A OD1 
363  O OD2 . ASP A 48  ? 0.4936 0.5869 0.4600 0.0639  -0.0550 0.0785  48  ASP A OD2 
364  N N   . MET A 49  ? 0.5162 0.6168 0.4764 0.0400  -0.0529 0.0522  49  MET A N   
365  C CA  . MET A 49  ? 0.5002 0.5945 0.4631 0.0381  -0.0479 0.0444  49  MET A CA  
366  C C   . MET A 49  ? 0.4755 0.5653 0.4273 0.0293  -0.0467 0.0399  49  MET A C   
367  O O   . MET A 49  ? 0.4668 0.5472 0.4178 0.0275  -0.0412 0.0347  49  MET A O   
368  C CB  . MET A 49  ? 0.4743 0.5789 0.4500 0.0413  -0.0491 0.0426  49  MET A CB  
369  C CG  . MET A 49  ? 0.4745 0.5825 0.4606 0.0502  -0.0492 0.0469  49  MET A CG  
370  S SD  . MET A 49  ? 0.4599 0.5786 0.4603 0.0538  -0.0495 0.0443  49  MET A SD  
371  C CE  . MET A 49  ? 0.4667 0.5829 0.4759 0.0643  -0.0471 0.0487  49  MET A CE  
372  N N   . LEU A 50  ? 0.5104 0.6064 0.4534 0.0236  -0.0516 0.0423  50  LEU A N   
373  C CA  . LEU A 50  ? 0.5332 0.6240 0.4644 0.0148  -0.0501 0.0377  50  LEU A CA  
374  C C   . LEU A 50  ? 0.5475 0.6224 0.4672 0.0123  -0.0446 0.0363  50  LEU A C   
375  O O   . LEU A 50  ? 0.5216 0.5873 0.4373 0.0088  -0.0389 0.0308  50  LEU A O   
376  C CB  . LEU A 50  ? 0.5783 0.6791 0.5012 0.0086  -0.0570 0.0412  50  LEU A CB  
377  C CG  . LEU A 50  ? 0.6957 0.7907 0.6028 -0.0018 -0.0563 0.0375  50  LEU A CG  
378  C CD1 . LEU A 50  ? 0.7727 0.8533 0.6644 -0.0055 -0.0527 0.0377  50  LEU A CD1 
379  C CD2 . LEU A 50  ? 0.6893 0.7803 0.5994 -0.0040 -0.0516 0.0298  50  LEU A CD2 
380  N N   . ASN A 51  ? 0.5217 0.5935 0.4361 0.0141  -0.0459 0.0415  51  ASN A N   
381  C CA  . ASN A 51  ? 0.5667 0.6241 0.4688 0.0111  -0.0411 0.0408  51  ASN A CA  
382  C C   . ASN A 51  ? 0.5542 0.6083 0.4590 0.0174  -0.0411 0.0459  51  ASN A C   
383  O O   . ASN A 51  ? 0.5099 0.5633 0.4059 0.0157  -0.0440 0.0509  51  ASN A O   
384  C CB  . ASN A 51  ? 0.6270 0.6828 0.5119 0.0022  -0.0436 0.0416  51  ASN A CB  
385  C CG  . ASN A 51  ? 0.6811 0.7216 0.5526 -0.0011 -0.0380 0.0406  51  ASN A CG  
386  O OD1 . ASN A 51  ? 0.7943 0.8244 0.6677 0.0004  -0.0307 0.0364  51  ASN A OD1 
387  N ND2 . ASN A 51  ? 0.8065 0.8459 0.6647 -0.0058 -0.0414 0.0448  51  ASN A ND2 
388  N N   . PRO A 52  ? 0.4797 0.5312 0.3962 0.0242  -0.0378 0.0450  52  PRO A N   
389  C CA  . PRO A 52  ? 0.3718 0.4200 0.2913 0.0304  -0.0380 0.0499  52  PRO A CA  
390  C C   . PRO A 52  ? 0.4231 0.4572 0.3335 0.0288  -0.0330 0.0497  52  PRO A C   
391  O O   . PRO A 52  ? 0.4348 0.4604 0.3420 0.0257  -0.0273 0.0449  52  PRO A O   
392  C CB  . PRO A 52  ? 0.4077 0.4576 0.3420 0.0371  -0.0359 0.0482  52  PRO A CB  
393  C CG  . PRO A 52  ? 0.4866 0.5357 0.4237 0.0335  -0.0325 0.0415  52  PRO A CG  
394  C CD  . PRO A 52  ? 0.4564 0.5067 0.3827 0.0257  -0.0336 0.0394  52  PRO A CD  
395  N N   . ASN A 53  ? 0.3823 0.4142 0.2888 0.0313  -0.0349 0.0554  53  ASN A N   
396  C CA  . ASN A 53  ? 0.3351 0.3541 0.2357 0.0317  -0.0303 0.0560  53  ASN A CA  
397  C C   . ASN A 53  ? 0.4165 0.4335 0.3278 0.0395  -0.0293 0.0581  53  ASN A C   
398  O O   . ASN A 53  ? 0.3621 0.3830 0.2761 0.0441  -0.0330 0.0638  53  ASN A O   
399  C CB  . ASN A 53  ? 0.3824 0.3988 0.2694 0.0279  -0.0328 0.0605  53  ASN A CB  
400  C CG  . ASN A 53  ? 0.4794 0.4824 0.3597 0.0279  -0.0277 0.0610  53  ASN A CG  
401  O OD1 . ASN A 53  ? 0.4801 0.4787 0.3669 0.0336  -0.0260 0.0629  53  ASN A OD1 
402  N ND2 . ASN A 53  ? 0.6495 0.6450 0.5162 0.0213  -0.0248 0.0592  53  ASN A ND2 
403  N N   . TYR A 54  ? 0.3640 0.3749 0.2814 0.0408  -0.0241 0.0540  54  TYR A N   
404  C CA  . TYR A 54  ? 0.3349 0.3441 0.2625 0.0473  -0.0231 0.0550  54  TYR A CA  
405  C C   . TYR A 54  ? 0.3647 0.3654 0.2885 0.0506  -0.0224 0.0598  54  TYR A C   
406  O O   . TYR A 54  ? 0.3382 0.3390 0.2681 0.0565  -0.0235 0.0628  54  TYR A O   
407  C CB  . TYR A 54  ? 0.3116 0.3163 0.2453 0.0464  -0.0180 0.0498  54  TYR A CB  
408  C CG  . TYR A 54  ? 0.3617 0.3755 0.3030 0.0453  -0.0191 0.0457  54  TYR A CG  
409  C CD1 . TYR A 54  ? 0.3543 0.3754 0.3052 0.0499  -0.0217 0.0461  54  TYR A CD1 
410  C CD2 . TYR A 54  ? 0.3588 0.3733 0.2974 0.0396  -0.0170 0.0413  54  TYR A CD2 
411  C CE1 . TYR A 54  ? 0.2801 0.3098 0.2380 0.0487  -0.0226 0.0422  54  TYR A CE1 
412  C CE2 . TYR A 54  ? 0.2937 0.3164 0.2391 0.0384  -0.0180 0.0376  54  TYR A CE2 
413  C CZ  . TYR A 54  ? 0.3268 0.3574 0.2820 0.0429  -0.0211 0.0380  54  TYR A CZ  
414  O OH  . TYR A 54  ? 0.3440 0.3830 0.3060 0.0415  -0.0221 0.0344  54  TYR A OH  
415  N N   . GLU A 55  ? 0.3684 0.3609 0.2821 0.0469  -0.0200 0.0605  55  GLU A N   
416  C CA  . GLU A 55  ? 0.4064 0.3911 0.3158 0.0497  -0.0197 0.0654  55  GLU A CA  
417  C C   . GLU A 55  ? 0.3890 0.3805 0.2977 0.0529  -0.0255 0.0715  55  GLU A C   
418  O O   . GLU A 55  ? 0.4102 0.3991 0.3227 0.0587  -0.0262 0.0757  55  GLU A O   
419  C CB  . GLU A 55  ? 0.4831 0.4589 0.3811 0.0446  -0.0162 0.0651  55  GLU A CB  
420  C CG  . GLU A 55  ? 0.6459 0.6151 0.5453 0.0417  -0.0098 0.0604  55  GLU A CG  
421  C CD  . GLU A 55  ? 0.8259 0.7854 0.7272 0.0440  -0.0061 0.0620  55  GLU A CD  
422  O OE1 . GLU A 55  ? 1.0895 1.0420 0.9825 0.0429  -0.0048 0.0651  55  GLU A OE1 
423  O OE2 . GLU A 55  ? 0.7519 0.7107 0.6624 0.0463  -0.0045 0.0605  55  GLU A OE2 
424  N N   . ASP A 56  ? 0.3773 0.3776 0.2813 0.0492  -0.0297 0.0725  56  ASP A N   
425  C CA  . ASP A 56  ? 0.4397 0.4490 0.3441 0.0516  -0.0359 0.0793  56  ASP A CA  
426  C C   . ASP A 56  ? 0.3822 0.3988 0.3001 0.0590  -0.0375 0.0810  56  ASP A C   
427  O O   . ASP A 56  ? 0.3690 0.3866 0.2909 0.0649  -0.0393 0.0871  56  ASP A O   
428  C CB  . ASP A 56  ? 0.4764 0.4945 0.3733 0.0449  -0.0402 0.0797  56  ASP A CB  
429  C CG  . ASP A 56  ? 0.5329 0.5441 0.4144 0.0383  -0.0398 0.0808  56  ASP A CG  
430  O OD1 . ASP A 56  ? 0.5199 0.5218 0.3976 0.0401  -0.0376 0.0833  56  ASP A OD1 
431  O OD2 . ASP A 56  ? 0.6053 0.6197 0.4777 0.0310  -0.0415 0.0792  56  ASP A OD2 
432  N N   . LEU A 57  ? 0.3213 0.3429 0.2466 0.0589  -0.0365 0.0758  57  LEU A N   
433  C CA  . LEU A 57  ? 0.3757 0.4042 0.3134 0.0656  -0.0376 0.0771  57  LEU A CA  
434  C C   . LEU A 57  ? 0.3765 0.3946 0.3188 0.0720  -0.0335 0.0778  57  LEU A C   
435  O O   . LEU A 57  ? 0.4188 0.4396 0.3679 0.0788  -0.0345 0.0822  57  LEU A O   
436  C CB  . LEU A 57  ? 0.3271 0.3622 0.2711 0.0636  -0.0370 0.0710  57  LEU A CB  
437  C CG  . LEU A 57  ? 0.3737 0.4176 0.3123 0.0565  -0.0404 0.0693  57  LEU A CG  
438  C CD1 . LEU A 57  ? 0.3842 0.4330 0.3297 0.0550  -0.0392 0.0630  57  LEU A CD1 
439  C CD2 . LEU A 57  ? 0.4552 0.5120 0.3943 0.0573  -0.0470 0.0763  57  LEU A CD2 
440  N N   . LEU A 58  ? 0.3405 0.3462 0.2789 0.0697  -0.0287 0.0738  58  LEU A N   
441  C CA  . LEU A 58  ? 0.3747 0.3697 0.3163 0.0744  -0.0249 0.0741  58  LEU A CA  
442  C C   . LEU A 58  ? 0.3500 0.3396 0.2876 0.0784  -0.0259 0.0810  58  LEU A C   
443  O O   . LEU A 58  ? 0.3687 0.3540 0.3109 0.0848  -0.0246 0.0837  58  LEU A O   
444  C CB  . LEU A 58  ? 0.3834 0.3677 0.3221 0.0702  -0.0199 0.0691  58  LEU A CB  
445  C CG  . LEU A 58  ? 0.4147 0.3894 0.3578 0.0738  -0.0162 0.0681  58  LEU A CG  
446  C CD1 . LEU A 58  ? 0.4437 0.4237 0.3961 0.0789  -0.0166 0.0673  58  LEU A CD1 
447  C CD2 . LEU A 58  ? 0.4284 0.3951 0.3703 0.0688  -0.0118 0.0637  58  LEU A CD2 
448  N N   . ILE A 59  ? 0.3336 0.3224 0.2620 0.0746  -0.0278 0.0838  59  ILE A N   
449  C CA  . ILE A 59  ? 0.3529 0.3362 0.2773 0.0780  -0.0287 0.0905  59  ILE A CA  
450  C C   . ILE A 59  ? 0.4115 0.4042 0.3426 0.0843  -0.0326 0.0971  59  ILE A C   
451  O O   . ILE A 59  ? 0.4464 0.4343 0.3778 0.0895  -0.0326 0.1030  59  ILE A O   
452  C CB  . ILE A 59  ? 0.4404 0.4214 0.3531 0.0721  -0.0301 0.0924  59  ILE A CB  
453  C CG1 . ILE A 59  ? 0.5721 0.5456 0.4808 0.0755  -0.0304 0.0989  59  ILE A CG1 
454  C CG2 . ILE A 59  ? 0.4614 0.4551 0.3709 0.0683  -0.0355 0.0948  59  ILE A CG2 
455  C CD1 . ILE A 59  ? 0.6840 0.6466 0.5823 0.0707  -0.0276 0.0979  59  ILE A CD1 
456  N N   . ARG A 60  ? 0.3526 0.3589 0.2894 0.0841  -0.0359 0.0969  60  ARG A N   
457  C CA  . ARG A 60  ? 0.3884 0.4055 0.3332 0.0903  -0.0394 0.1039  60  ARG A CA  
458  C C   . ARG A 60  ? 0.4095 0.4246 0.3650 0.0981  -0.0359 0.1030  60  ARG A C   
459  O O   . ARG A 60  ? 0.4067 0.4309 0.3704 0.1042  -0.0378 0.1088  60  ARG A O   
460  C CB  . ARG A 60  ? 0.3490 0.3825 0.2950 0.0862  -0.0449 0.1051  60  ARG A CB  
461  C CG  . ARG A 60  ? 0.3960 0.4324 0.3307 0.0790  -0.0491 0.1082  60  ARG A CG  
462  C CD  . ARG A 60  ? 0.4014 0.4471 0.3327 0.0714  -0.0519 0.1042  60  ARG A CD  
463  N NE  . ARG A 60  ? 0.4143 0.4592 0.3320 0.0632  -0.0547 0.1055  60  ARG A NE  
464  C CZ  . ARG A 60  ? 0.4811 0.5318 0.3919 0.0551  -0.0572 0.1025  60  ARG A CZ  
465  N NH1 . ARG A 60  ? 0.5662 0.6248 0.4831 0.0542  -0.0577 0.0983  60  ARG A NH1 
466  N NH2 . ARG A 60  ? 0.5196 0.5672 0.4164 0.0475  -0.0589 0.1037  60  ARG A NH2 
467  N N   . LYS A 61  ? 0.4131 0.4169 0.3687 0.0978  -0.0307 0.0962  61  LYS A N   
468  C CA  . LYS A 61  ? 0.4423 0.4424 0.4062 0.1041  -0.0268 0.0946  61  LYS A CA  
469  C C   . LYS A 61  ? 0.4284 0.4122 0.3892 0.1084  -0.0224 0.0965  61  LYS A C   
470  O O   . LYS A 61  ? 0.4341 0.4083 0.3866 0.1050  -0.0217 0.0966  61  LYS A O   
471  C CB  . LYS A 61  ? 0.4166 0.4158 0.3827 0.1000  -0.0242 0.0858  61  LYS A CB  
472  C CG  . LYS A 61  ? 0.4714 0.4857 0.4402 0.0955  -0.0281 0.0833  61  LYS A CG  
473  C CD  . LYS A 61  ? 0.5477 0.5733 0.5272 0.1008  -0.0291 0.0846  61  LYS A CD  
474  C CE  . LYS A 61  ? 0.5212 0.5627 0.5027 0.0960  -0.0339 0.0835  61  LYS A CE  
475  N NZ  . LYS A 61  ? 0.6555 0.7006 0.6280 0.0902  -0.0383 0.0866  61  LYS A NZ  
476  N N   . SER A 62  ? 0.4456 0.4257 0.4129 0.1158  -0.0191 0.0979  62  SER A N   
477  C CA  . SER A 62  ? 0.4712 0.4338 0.4352 0.1194  -0.0139 0.0981  62  SER A CA  
478  C C   . SER A 62  ? 0.4188 0.3752 0.3865 0.1205  -0.0091 0.0918  62  SER A C   
479  O O   . SER A 62  ? 0.4491 0.4159 0.4230 0.1195  -0.0100 0.0883  62  SER A O   
480  C CB  . SER A 62  ? 0.5832 0.5439 0.5495 0.1278  -0.0136 0.1070  62  SER A CB  
481  O OG  . SER A 62  ? 0.6625 0.6345 0.6392 0.1344  -0.0139 0.1103  62  SER A OG  
482  N N   . ASN A 63  ? 0.4304 0.3694 0.3935 0.1219  -0.0040 0.0906  63  ASN A N   
483  C CA  . ASN A 63  ? 0.4382 0.3690 0.4023 0.1212  0.0008  0.0843  63  ASN A CA  
484  C C   . ASN A 63  ? 0.4417 0.3809 0.4153 0.1278  0.0021  0.0849  63  ASN A C   
485  O O   . ASN A 63  ? 0.4685 0.4108 0.4456 0.1254  0.0034  0.0791  63  ASN A O   
486  C CB  . ASN A 63  ? 0.4712 0.3812 0.4278 0.1224  0.0061  0.0843  63  ASN A CB  
487  C CG  . ASN A 63  ? 0.4861 0.3873 0.4338 0.1147  0.0055  0.0825  63  ASN A CG  
488  O OD1 . ASN A 63  ? 0.4632 0.3712 0.4105 0.1076  0.0031  0.0787  63  ASN A OD1 
489  N ND2 . ASN A 63  ? 0.4645 0.3504 0.4050 0.1163  0.0080  0.0856  63  ASN A ND2 
490  N N   . HIS A 64  ? 0.4765 0.4196 0.4548 0.1362  0.0019  0.0924  64  HIS A N   
491  C CA  . HIS A 64  ? 0.5105 0.4603 0.4983 0.1435  0.0043  0.0940  64  HIS A CA  
492  C C   . HIS A 64  ? 0.4860 0.4568 0.4820 0.1415  -0.0008 0.0932  64  HIS A C   
493  O O   . HIS A 64  ? 0.4942 0.4726 0.4988 0.1467  0.0009  0.0941  64  HIS A O   
494  C CB  . HIS A 64  ? 0.6000 0.5494 0.5918 0.1503  0.0057  0.1014  64  HIS A CB  
495  C CG  . HIS A 64  ? 0.5454 0.5097 0.5402 0.1497  -0.0010 0.1083  64  HIS A CG  
496  N ND1 . HIS A 64  ? 0.6451 0.6300 0.6481 0.1490  -0.0062 0.1105  64  HIS A ND1 
497  C CD2 . HIS A 64  ? 0.6362 0.5976 0.6261 0.1487  -0.0035 0.1133  64  HIS A CD2 
498  C CE1 . HIS A 64  ? 0.5570 0.5506 0.5595 0.1474  -0.0116 0.1168  64  HIS A CE1 
499  N NE2 . HIS A 64  ? 0.6562 0.6360 0.6510 0.1474  -0.0101 0.1186  64  HIS A NE2 
500  N N   . ASN A 65  ? 0.4488 0.4289 0.4420 0.1339  -0.0064 0.0915  65  ASN A N   
501  C CA  . ASN A 65  ? 0.4233 0.4214 0.4224 0.1305  -0.0110 0.0896  65  ASN A CA  
502  C C   . ASN A 65  ? 0.4636 0.4602 0.4634 0.1254  -0.0089 0.0805  65  ASN A C   
503  O O   . ASN A 65  ? 0.4138 0.4247 0.4190 0.1229  -0.0120 0.0784  65  ASN A O   
504  C CB  . ASN A 65  ? 0.4395 0.4464 0.4339 0.1239  -0.0172 0.0912  65  ASN A CB  
505  C CG  . ASN A 65  ? 0.4942 0.5066 0.4888 0.1280  -0.0207 0.1009  65  ASN A CG  
506  O OD1 . ASN A 65  ? 0.4727 0.4825 0.4596 0.1239  -0.0233 0.1029  65  ASN A OD1 
507  N ND2 . ASN A 65  ? 0.5389 0.5596 0.5427 0.1360  -0.0206 0.1075  65  ASN A ND2 
508  N N   . PHE A 66  ? 0.3952 0.3753 0.3895 0.1233  -0.0039 0.0755  66  PHE A N   
509  C CA  . PHE A 66  ? 0.4354 0.4133 0.4299 0.1177  -0.0019 0.0674  66  PHE A CA  
510  C C   . PHE A 66  ? 0.5054 0.4744 0.5023 0.1227  0.0040  0.0656  66  PHE A C   
511  O O   . PHE A 66  ? 0.4841 0.4364 0.4752 0.1252  0.0087  0.0664  66  PHE A O   
512  C CB  . PHE A 66  ? 0.4244 0.3908 0.4103 0.1098  -0.0011 0.0632  66  PHE A CB  
513  C CG  . PHE A 66  ? 0.4177 0.3908 0.4002 0.1045  -0.0057 0.0643  66  PHE A CG  
514  C CD1 . PHE A 66  ? 0.3886 0.3735 0.3736 0.0988  -0.0089 0.0606  66  PHE A CD1 
515  C CD2 . PHE A 66  ? 0.4034 0.3702 0.3795 0.1053  -0.0065 0.0691  66  PHE A CD2 
516  C CE1 . PHE A 66  ? 0.4239 0.4131 0.4044 0.0938  -0.0122 0.0614  66  PHE A CE1 
517  C CE2 . PHE A 66  ? 0.4546 0.4266 0.4264 0.1002  -0.0102 0.0699  66  PHE A CE2 
518  C CZ  . PHE A 66  ? 0.4004 0.3831 0.3741 0.0945  -0.0127 0.0660  66  PHE A CZ  
519  N N   . LEU A 67  ? 0.3953 0.3744 0.3997 0.1237  0.0041  0.0629  67  LEU A N   
520  C CA  . LEU A 67  ? 0.4036 0.3745 0.4097 0.1274  0.0101  0.0602  67  LEU A CA  
521  C C   . LEU A 67  ? 0.4522 0.4192 0.4556 0.1188  0.0112  0.0519  67  LEU A C   
522  O O   . LEU A 67  ? 0.4004 0.3809 0.4085 0.1140  0.0073  0.0488  67  LEU A O   
523  C CB  . LEU A 67  ? 0.4935 0.4791 0.5105 0.1346  0.0098  0.0635  67  LEU A CB  
524  C CG  . LEU A 67  ? 0.6178 0.5992 0.6383 0.1380  0.0158  0.0600  67  LEU A CG  
525  C CD1 . LEU A 67  ? 0.6239 0.5847 0.6385 0.1437  0.0236  0.0613  67  LEU A CD1 
526  C CD2 . LEU A 67  ? 0.6159 0.6160 0.6484 0.1441  0.0141  0.0638  67  LEU A CD2 
527  N N   . VAL A 68  ? 0.3839 0.3325 0.3794 0.1164  0.0162  0.0488  68  VAL A N   
528  C CA  . VAL A 68  ? 0.3828 0.3264 0.3752 0.1077  0.0173  0.0419  68  VAL A CA  
529  C C   . VAL A 68  ? 0.3995 0.3337 0.3912 0.1103  0.0234  0.0389  68  VAL A C   
530  O O   . VAL A 68  ? 0.4135 0.3330 0.4001 0.1157  0.0288  0.0410  68  VAL A O   
531  C CB  . VAL A 68  ? 0.3807 0.3109 0.3635 0.1007  0.0176  0.0410  68  VAL A CB  
532  C CG1 . VAL A 68  ? 0.4054 0.3302 0.3853 0.0918  0.0191  0.0349  68  VAL A CG1 
533  C CG2 . VAL A 68  ? 0.3669 0.3065 0.3502 0.0978  0.0121  0.0435  68  VAL A CG2 
534  N N   . GLN A 69  ? 0.3751 0.3173 0.3715 0.1066  0.0231  0.0340  69  GLN A N   
535  C CA  . GLN A 69  ? 0.4163 0.3503 0.4117 0.1084  0.0290  0.0307  69  GLN A CA  
536  C C   . GLN A 69  ? 0.4102 0.3385 0.4009 0.0978  0.0295  0.0243  69  GLN A C   
537  O O   . GLN A 69  ? 0.3771 0.3186 0.3730 0.0917  0.0249  0.0217  69  GLN A O   
538  C CB  . GLN A 69  ? 0.4179 0.3679 0.4243 0.1151  0.0286  0.0318  69  GLN A CB  
539  C CG  . GLN A 69  ? 0.5856 0.5448 0.5982 0.1246  0.0267  0.0394  69  GLN A CG  
540  C CD  . GLN A 69  ? 0.6990 0.6761 0.7233 0.1306  0.0255  0.0416  69  GLN A CD  
541  O OE1 . GLN A 69  ? 0.6007 0.5965 0.6320 0.1291  0.0189  0.0431  69  GLN A OE1 
542  N NE2 . GLN A 69  ? 0.7204 0.6916 0.7466 0.1375  0.0322  0.0420  69  GLN A NE2 
543  N N   . ALA A 70  ? 0.4216 0.3300 0.4021 0.0952  0.0353  0.0220  70  ALA A N   
544  C CA  . ALA A 70  ? 0.4692 0.3704 0.4441 0.0848  0.0364  0.0165  70  ALA A CA  
545  C C   . ALA A 70  ? 0.5724 0.4671 0.5460 0.0875  0.0425  0.0131  70  ALA A C   
546  O O   . ALA A 70  ? 0.5175 0.3943 0.4828 0.0914  0.0491  0.0135  70  ALA A O   
547  C CB  . ALA A 70  ? 0.4713 0.3540 0.4339 0.0784  0.0380  0.0168  70  ALA A CB  
548  N N   . GLY A 71  ? 0.6178 0.5267 0.5995 0.0856  0.0406  0.0099  71  GLY A N   
549  C CA  . GLY A 71  ? 0.6197 0.5256 0.6022 0.0901  0.0463  0.0075  71  GLY A CA  
550  C C   . GLY A 71  ? 0.6292 0.5379 0.6173 0.1035  0.0490  0.0126  71  GLY A C   
551  O O   . GLY A 71  ? 0.6712 0.5967 0.6689 0.1084  0.0439  0.0169  71  GLY A O   
552  N N   . ASN A 72  ? 0.7629 0.6549 0.7446 0.1093  0.0575  0.0127  72  ASN A N   
553  C CA  . ASN A 72  ? 0.8695 0.7623 0.8564 0.1224  0.0609  0.0188  72  ASN A CA  
554  C C   . ASN A 72  ? 0.8156 0.6947 0.7952 0.1254  0.0621  0.0234  72  ASN A C   
555  O O   . ASN A 72  ? 0.9055 0.7873 0.8904 0.1360  0.0636  0.0298  72  ASN A O   
556  C CB  . ASN A 72  ? 0.9371 0.8194 0.9223 0.1291  0.0705  0.0175  72  ASN A CB  
557  C CG  . ASN A 72  ? 0.9926 0.8812 0.9872 0.1436  0.0737  0.0249  72  ASN A CG  
558  O OD1 . ASN A 72  ? 1.0033 0.9083 1.0075 0.1479  0.0675  0.0308  72  ASN A OD1 
559  N ND2 . ASN A 72  ? 0.9855 0.8618 0.9774 0.1498  0.0831  0.0249  72  ASN A ND2 
560  N N   . VAL A 73  ? 0.7279 0.5934 0.6962 0.1163  0.0611  0.0210  73  VAL A N   
561  C CA  . VAL A 73  ? 0.6287 0.4794 0.5888 0.1184  0.0625  0.0250  73  VAL A CA  
562  C C   . VAL A 73  ? 0.6420 0.5092 0.6098 0.1198  0.0544  0.0300  73  VAL A C   
563  O O   . VAL A 73  ? 0.5622 0.4408 0.5326 0.1118  0.0477  0.0281  73  VAL A O   
564  C CB  . VAL A 73  ? 0.6755 0.5058 0.6203 0.1074  0.0644  0.0209  73  VAL A CB  
565  C CG1 . VAL A 73  ? 0.7052 0.5248 0.6432 0.1081  0.0635  0.0253  73  VAL A CG1 
566  C CG2 . VAL A 73  ? 0.7720 0.5816 0.7061 0.1068  0.0736  0.0167  73  VAL A CG2 
567  N N   . GLN A 74  ? 0.6282 0.4961 0.5994 0.1297  0.0552  0.0367  74  GLN A N   
568  C CA  . GLN A 74  ? 0.5900 0.4706 0.5660 0.1302  0.0480  0.0416  74  GLN A CA  
569  C C   . GLN A 74  ? 0.6038 0.4685 0.5680 0.1243  0.0476  0.0418  74  GLN A C   
570  O O   . GLN A 74  ? 0.5940 0.4377 0.5483 0.1260  0.0539  0.0422  74  GLN A O   
571  C CB  . GLN A 74  ? 0.6761 0.5647 0.6605 0.1425  0.0485  0.0495  74  GLN A CB  
572  C CG  . GLN A 74  ? 0.6750 0.5788 0.6646 0.1428  0.0406  0.0550  74  GLN A CG  
573  C CD  . GLN A 74  ? 0.8682 0.7797 0.8659 0.1544  0.0410  0.0638  74  GLN A CD  
574  O OE1 . GLN A 74  ? 0.8459 0.7555 0.8414 0.1557  0.0389  0.0689  74  GLN A OE1 
575  N NE2 . GLN A 74  ? 0.8743 0.7972 0.8815 0.1585  0.0426  0.0644  74  GLN A NE2 
576  N N   . LEU A 75  ? 0.4744 0.3483 0.4392 0.1170  0.0408  0.0415  75  LEU A N   
577  C CA  . LEU A 75  ? 0.4546 0.3161 0.4095 0.1112  0.0399  0.0422  75  LEU A CA  
578  C C   . LEU A 75  ? 0.5301 0.3969 0.4874 0.1169  0.0365  0.0491  75  LEU A C   
579  O O   . LEU A 75  ? 0.5608 0.4466 0.5275 0.1196  0.0314  0.0517  75  LEU A O   
580  C CB  . LEU A 75  ? 0.4360 0.3036 0.3900 0.0996  0.0351  0.0383  75  LEU A CB  
581  C CG  . LEU A 75  ? 0.4454 0.3096 0.3972 0.0916  0.0370  0.0319  75  LEU A CG  
582  C CD1 . LEU A 75  ? 0.4379 0.3099 0.3905 0.0811  0.0320  0.0300  75  LEU A CD1 
583  C CD2 . LEU A 75  ? 0.4997 0.3401 0.4391 0.0899  0.0440  0.0300  75  LEU A CD2 
584  N N   . ARG A 76  ? 0.4752 0.3251 0.4234 0.1183  0.0393  0.0520  76  ARG A N   
585  C CA  . ARG A 76  ? 0.4981 0.3513 0.4479 0.1241  0.0368  0.0590  76  ARG A CA  
586  C C   . ARG A 76  ? 0.5244 0.3834 0.4719 0.1163  0.0308  0.0592  76  ARG A C   
587  O O   . ARG A 76  ? 0.4806 0.3278 0.4193 0.1085  0.0315  0.0566  76  ARG A O   
588  C CB  . ARG A 76  ? 0.4997 0.3320 0.4411 0.1297  0.0429  0.0624  76  ARG A CB  
589  C CG  . ARG A 76  ? 0.6702 0.5013 0.6094 0.1321  0.0400  0.0689  76  ARG A CG  
590  C CD  . ARG A 76  ? 0.7438 0.5661 0.6831 0.1415  0.0449  0.0740  76  ARG A CD  
591  N NE  . ARG A 76  ? 0.8957 0.7229 0.8359 0.1431  0.0408  0.0802  76  ARG A NE  
592  C CZ  . ARG A 76  ? 0.9473 0.7606 0.8778 0.1397  0.0412  0.0815  76  ARG A CZ  
593  N NH1 . ARG A 76  ? 0.9082 0.7015 0.8269 0.1341  0.0455  0.0772  76  ARG A NH1 
594  N NH2 . ARG A 76  ? 0.9368 0.7566 0.8691 0.1412  0.0370  0.0872  76  ARG A NH2 
595  N N   . VAL A 77  ? 0.4613 0.3384 0.4163 0.1181  0.0250  0.0623  77  VAL A N   
596  C CA  . VAL A 77  ? 0.4787 0.3620 0.4318 0.1115  0.0198  0.0628  77  VAL A CA  
597  C C   . VAL A 77  ? 0.4336 0.3067 0.3799 0.1137  0.0200  0.0683  77  VAL A C   
598  O O   . VAL A 77  ? 0.4494 0.3241 0.3981 0.1218  0.0200  0.0741  77  VAL A O   
599  C CB  . VAL A 77  ? 0.3925 0.2978 0.3546 0.1119  0.0141  0.0637  77  VAL A CB  
600  C CG1 . VAL A 77  ? 0.3654 0.2751 0.3243 0.1053  0.0099  0.0641  77  VAL A CG1 
601  C CG2 . VAL A 77  ? 0.3887 0.3036 0.3573 0.1091  0.0140  0.0580  77  VAL A CG2 
602  N N   . ILE A 78  ? 0.4146 0.2777 0.3526 0.1065  0.0200  0.0670  78  ILE A N   
603  C CA  . ILE A 78  ? 0.4170 0.2693 0.3476 0.1075  0.0201  0.0719  78  ILE A CA  
604  C C   . ILE A 78  ? 0.4419 0.3016 0.3711 0.1017  0.0155  0.0731  78  ILE A C   
605  O O   . ILE A 78  ? 0.4938 0.3463 0.4171 0.1021  0.0151  0.0772  78  ILE A O   
606  C CB  . ILE A 78  ? 0.5305 0.3605 0.4507 0.1048  0.0253  0.0705  78  ILE A CB  
607  C CG1 . ILE A 78  ? 0.5238 0.3509 0.4404 0.0940  0.0253  0.0652  78  ILE A CG1 
608  C CG2 . ILE A 78  ? 0.5785 0.3985 0.4986 0.1119  0.0310  0.0701  78  ILE A CG2 
609  C CD1 . ILE A 78  ? 0.5704 0.3758 0.4751 0.0894  0.0294  0.0646  78  ILE A CD1 
610  N N   . GLY A 79  ? 0.4385 0.3118 0.3726 0.0965  0.0125  0.0696  79  GLY A N   
611  C CA  . GLY A 79  ? 0.4271 0.3082 0.3602 0.0921  0.0087  0.0710  79  GLY A CA  
612  C C   . GLY A 79  ? 0.4160 0.3136 0.3562 0.0889  0.0059  0.0674  79  GLY A C   
613  O O   . GLY A 79  ? 0.3797 0.2810 0.3248 0.0881  0.0069  0.0632  79  GLY A O   
614  N N   . HIS A 80  ? 0.3746 0.2813 0.3146 0.0869  0.0025  0.0691  80  HIS A N   
615  C CA  . HIS A 80  ? 0.3977 0.3185 0.3430 0.0831  0.0002  0.0656  80  HIS A CA  
616  C C   . HIS A 80  ? 0.4097 0.3322 0.3507 0.0775  -0.0009 0.0662  80  HIS A C   
617  O O   . HIS A 80  ? 0.3919 0.3101 0.3270 0.0785  -0.0016 0.0704  80  HIS A O   
618  C CB  . HIS A 80  ? 0.3824 0.3171 0.3337 0.0880  -0.0031 0.0669  80  HIS A CB  
619  C CG  . HIS A 80  ? 0.3934 0.3310 0.3419 0.0919  -0.0059 0.0730  80  HIS A CG  
620  N ND1 . HIS A 80  ? 0.4004 0.3295 0.3466 0.0978  -0.0048 0.0781  80  HIS A ND1 
621  C CD2 . HIS A 80  ? 0.3899 0.3370 0.3366 0.0899  -0.0097 0.0752  80  HIS A CD2 
622  C CE1 . HIS A 80  ? 0.4792 0.4138 0.4234 0.0996  -0.0082 0.0834  80  HIS A CE1 
623  N NE2 . HIS A 80  ? 0.4192 0.3647 0.3632 0.0946  -0.0114 0.0817  80  HIS A NE2 
624  N N   . SER A 81  ? 0.3505 0.2792 0.2944 0.0719  -0.0007 0.0622  81  SER A N   
625  C CA  . SER A 81  ? 0.3745 0.3058 0.3150 0.0670  -0.0010 0.0624  81  SER A CA  
626  C C   . SER A 81  ? 0.4331 0.3753 0.3792 0.0631  -0.0014 0.0580  81  SER A C   
627  O O   . SER A 81  ? 0.3763 0.3225 0.3287 0.0632  -0.0012 0.0547  81  SER A O   
628  C CB  . SER A 81  ? 0.4336 0.3540 0.3695 0.0627  0.0021  0.0636  81  SER A CB  
629  O OG  . SER A 81  ? 0.4438 0.3615 0.3836 0.0589  0.0044  0.0606  81  SER A OG  
630  N N   . MET A 82  ? 0.3575 0.3033 0.3005 0.0596  -0.0014 0.0581  82  MET A N   
631  C CA  . MET A 82  ? 0.3705 0.3250 0.3175 0.0556  -0.0011 0.0542  82  MET A CA  
632  C C   . MET A 82  ? 0.3620 0.3118 0.3085 0.0502  0.0028  0.0537  82  MET A C   
633  O O   . MET A 82  ? 0.3757 0.3186 0.3162 0.0490  0.0045  0.0567  82  MET A O   
634  C CB  . MET A 82  ? 0.4231 0.3852 0.3663 0.0556  -0.0039 0.0546  82  MET A CB  
635  C CG  . MET A 82  ? 0.4251 0.3936 0.3691 0.0509  -0.0030 0.0511  82  MET A CG  
636  S SD  . MET A 82  ? 0.4105 0.3911 0.3537 0.0522  -0.0082 0.0508  82  MET A SD  
637  C CE  . MET A 82  ? 0.4302 0.4060 0.3614 0.0517  -0.0093 0.0555  82  MET A CE  
638  N N   . GLN A 83  ? 0.3023 0.2563 0.2557 0.0469  0.0044  0.0504  83  GLN A N   
639  C CA  . GLN A 83  ? 0.3525 0.3046 0.3078 0.0418  0.0083  0.0505  83  GLN A CA  
640  C C   . GLN A 83  ? 0.2666 0.2279 0.2266 0.0394  0.0088  0.0470  83  GLN A C   
641  O O   . GLN A 83  ? 0.3153 0.2824 0.2826 0.0387  0.0080  0.0440  83  GLN A O   
642  C CB  . GLN A 83  ? 0.4411 0.3884 0.4007 0.0396  0.0098  0.0511  83  GLN A CB  
643  C CG  . GLN A 83  ? 0.5635 0.5134 0.5292 0.0340  0.0131  0.0510  83  GLN A CG  
644  C CD  . GLN A 83  ? 0.5128 0.4550 0.4782 0.0306  0.0153  0.0547  83  GLN A CD  
645  O OE1 . GLN A 83  ? 0.5760 0.5109 0.5380 0.0316  0.0141  0.0559  83  GLN A OE1 
646  N NE2 . GLN A 83  ? 0.5673 0.5112 0.5364 0.0263  0.0187  0.0570  83  GLN A NE2 
647  N N   . ASN A 84  ? 0.2707 0.2328 0.2258 0.0379  0.0104  0.0471  84  ASN A N   
648  C CA  . ASN A 84  ? 0.2613 0.2306 0.2188 0.0355  0.0112  0.0438  84  ASN A CA  
649  C C   . ASN A 84  ? 0.2504 0.2280 0.2109 0.0378  0.0065  0.0408  84  ASN A C   
650  O O   . ASN A 84  ? 0.2622 0.2406 0.2179 0.0410  0.0028  0.0420  84  ASN A O   
651  C CB  . ASN A 84  ? 0.2419 0.2121 0.2070 0.0317  0.0156  0.0433  84  ASN A CB  
652  C CG  . ASN A 84  ? 0.3128 0.2754 0.2757 0.0299  0.0201  0.0474  84  ASN A CG  
653  O OD1 . ASN A 84  ? 0.3445 0.3031 0.2999 0.0296  0.0225  0.0487  84  ASN A OD1 
654  N ND2 . ASN A 84  ? 0.2766 0.2369 0.2451 0.0284  0.0211  0.0498  84  ASN A ND2 
655  N N   . CYS A 85  ? 0.2319 0.2162 0.2007 0.0362  0.0064  0.0375  85  CYS A N   
656  C CA  . CYS A 85  ? 0.1996 0.1925 0.1711 0.0383  0.0021  0.0349  85  CYS A CA  
657  C C   . CYS A 85  ? 0.2853 0.2788 0.2624 0.0415  0.0000  0.0349  85  CYS A C   
658  O O   . CYS A 85  ? 0.2424 0.2435 0.2237 0.0432  -0.0030 0.0327  85  CYS A O   
659  C CB  . CYS A 85  ? 0.2450 0.2453 0.2212 0.0349  0.0028  0.0312  85  CYS A CB  
660  S SG  . CYS A 85  ? 0.2652 0.2634 0.2327 0.0313  0.0058  0.0307  85  CYS A SG  
661  N N   . VAL A 86  ? 0.2265 0.2115 0.2028 0.0422  0.0016  0.0373  86  VAL A N   
662  C CA  . VAL A 86  ? 0.2418 0.2246 0.2214 0.0449  0.0006  0.0371  86  VAL A CA  
663  C C   . VAL A 86  ? 0.3060 0.2817 0.2792 0.0496  -0.0005 0.0407  86  VAL A C   
664  O O   . VAL A 86  ? 0.3220 0.2922 0.2886 0.0495  0.0003  0.0437  86  VAL A O   
665  C CB  . VAL A 86  ? 0.2817 0.2599 0.2653 0.0407  0.0035  0.0369  86  VAL A CB  
666  C CG1 . VAL A 86  ? 0.4190 0.3889 0.4010 0.0427  0.0036  0.0379  86  VAL A CG1 
667  C CG2 . VAL A 86  ? 0.2805 0.2676 0.2724 0.0375  0.0034  0.0332  86  VAL A CG2 
668  N N   . LEU A 87  ? 0.2527 0.2287 0.2279 0.0540  -0.0020 0.0405  87  LEU A N   
669  C CA  . LEU A 87  ? 0.2415 0.2101 0.2119 0.0591  -0.0024 0.0441  87  LEU A CA  
670  C C   . LEU A 87  ? 0.3366 0.2946 0.3068 0.0584  0.0004  0.0439  87  LEU A C   
671  O O   . LEU A 87  ? 0.2963 0.2559 0.2714 0.0560  0.0013  0.0406  87  LEU A O   
672  C CB  . LEU A 87  ? 0.3097 0.2863 0.2828 0.0649  -0.0055 0.0448  87  LEU A CB  
673  C CG  . LEU A 87  ? 0.5019 0.4748 0.4728 0.0718  -0.0064 0.0490  87  LEU A CG  
674  C CD1 . LEU A 87  ? 0.4703 0.4408 0.4343 0.0723  -0.0078 0.0533  87  LEU A CD1 
675  C CD2 . LEU A 87  ? 0.3809 0.3655 0.3580 0.0763  -0.0092 0.0491  87  LEU A CD2 
676  N N   . LYS A 88  ? 0.3184 0.2652 0.2822 0.0597  0.0017  0.0473  88  LYS A N   
677  C CA  . LYS A 88  ? 0.3178 0.2523 0.2788 0.0588  0.0043  0.0476  88  LYS A CA  
678  C C   . LYS A 88  ? 0.4045 0.3325 0.3622 0.0659  0.0043  0.0502  88  LYS A C   
679  O O   . LYS A 88  ? 0.3405 0.2659 0.2936 0.0691  0.0033  0.0541  88  LYS A O   
680  C CB  . LYS A 88  ? 0.3121 0.2381 0.2682 0.0537  0.0062  0.0500  88  LYS A CB  
681  C CG  . LYS A 88  ? 0.3419 0.2740 0.3025 0.0469  0.0070  0.0485  88  LYS A CG  
682  C CD  . LYS A 88  ? 0.4681 0.3944 0.4247 0.0428  0.0088  0.0520  88  LYS A CD  
683  C CE  . LYS A 88  ? 0.5215 0.4372 0.4754 0.0386  0.0107  0.0535  88  LYS A CE  
684  N NZ  . LYS A 88  ? 0.6512 0.5633 0.6029 0.0338  0.0124  0.0575  88  LYS A NZ  
685  N N   . LEU A 89  ? 0.3514 0.2767 0.3113 0.0685  0.0057  0.0482  89  LEU A N   
686  C CA  . LEU A 89  ? 0.3363 0.2547 0.2938 0.0759  0.0068  0.0507  89  LEU A CA  
687  C C   . LEU A 89  ? 0.3936 0.2947 0.3443 0.0739  0.0107  0.0505  89  LEU A C   
688  O O   . LEU A 89  ? 0.3672 0.2648 0.3186 0.0703  0.0128  0.0468  89  LEU A O   
689  C CB  . LEU A 89  ? 0.3685 0.2960 0.3331 0.0810  0.0064  0.0489  89  LEU A CB  
690  C CG  . LEU A 89  ? 0.3660 0.3110 0.3368 0.0822  0.0021  0.0492  89  LEU A CG  
691  C CD1 . LEU A 89  ? 0.3984 0.3529 0.3768 0.0860  0.0017  0.0472  89  LEU A CD1 
692  C CD2 . LEU A 89  ? 0.3960 0.3432 0.3640 0.0865  -0.0004 0.0548  89  LEU A CD2 
693  N N   . LYS A 90  ? 0.3722 0.2621 0.3157 0.0754  0.0117  0.0544  90  LYS A N   
694  C CA  . LYS A 90  ? 0.4148 0.2869 0.3505 0.0736  0.0155  0.0544  90  LYS A CA  
695  C C   . LYS A 90  ? 0.3882 0.2538 0.3237 0.0810  0.0185  0.0543  90  LYS A C   
696  O O   . LYS A 90  ? 0.4366 0.3058 0.3745 0.0891  0.0178  0.0577  90  LYS A O   
697  C CB  . LYS A 90  ? 0.4500 0.3119 0.3778 0.0727  0.0156  0.0589  90  LYS A CB  
698  C CG  . LYS A 90  ? 0.4800 0.3237 0.3988 0.0680  0.0190  0.0587  90  LYS A CG  
699  C CD  . LYS A 90  ? 0.5804 0.4118 0.4907 0.0698  0.0197  0.0636  90  LYS A CD  
700  C CE  . LYS A 90  ? 0.7038 0.5228 0.6060 0.0609  0.0210  0.0640  90  LYS A CE  
701  N NZ  . LYS A 90  ? 0.8118 0.6270 0.7090 0.0599  0.0198  0.0689  90  LYS A NZ  
702  N N   . VAL A 91  ? 0.4056 0.2615 0.3381 0.0781  0.0221  0.0507  91  VAL A N   
703  C CA  . VAL A 91  ? 0.4105 0.2583 0.3420 0.0845  0.0263  0.0498  91  VAL A CA  
704  C C   . VAL A 91  ? 0.4702 0.2953 0.3896 0.0826  0.0310  0.0503  91  VAL A C   
705  O O   . VAL A 91  ? 0.4632 0.2803 0.3757 0.0746  0.0306  0.0504  91  VAL A O   
706  C CB  . VAL A 91  ? 0.4353 0.2905 0.3727 0.0829  0.0271  0.0446  91  VAL A CB  
707  C CG1 . VAL A 91  ? 0.4277 0.3045 0.3767 0.0863  0.0228  0.0447  91  VAL A CG1 
708  C CG2 . VAL A 91  ? 0.4285 0.2804 0.3626 0.0716  0.0270  0.0408  91  VAL A CG2 
709  N N   . ASP A 92  ? 0.5067 0.3209 0.4233 0.0899  0.0358  0.0509  92  ASP A N   
710  C CA  . ASP A 92  ? 0.5305 0.3213 0.4343 0.0889  0.0407  0.0517  92  ASP A CA  
711  C C   . ASP A 92  ? 0.6010 0.3785 0.4967 0.0810  0.0447  0.0465  92  ASP A C   
712  O O   . ASP A 92  ? 0.5897 0.3461 0.4731 0.0789  0.0492  0.0466  92  ASP A O   
713  C CB  . ASP A 92  ? 0.6682 0.4507 0.5715 0.1006  0.0451  0.0555  92  ASP A CB  
714  C CG  . ASP A 92  ? 0.6664 0.4507 0.5749 0.1069  0.0494  0.0531  92  ASP A CG  
715  O OD1 . ASP A 92  ? 0.6755 0.4648 0.5860 0.1016  0.0494  0.0478  92  ASP A OD1 
716  O OD2 . ASP A 92  ? 0.7649 0.5454 0.6756 0.1174  0.0531  0.0569  92  ASP A OD2 
717  N N   . THR A 93  ? 0.5449 0.3337 0.4464 0.0760  0.0431  0.0420  93  THR A N   
718  C CA  . THR A 93  ? 0.5503 0.3281 0.4443 0.0673  0.0461  0.0372  93  THR A CA  
719  C C   . THR A 93  ? 0.5287 0.3192 0.4271 0.0566  0.0411  0.0353  93  THR A C   
720  O O   . THR A 93  ? 0.4946 0.3050 0.4049 0.0579  0.0371  0.0348  93  THR A O   
721  C CB  . THR A 93  ? 0.6022 0.3796 0.4990 0.0725  0.0506  0.0334  93  THR A CB  
722  O OG1 . THR A 93  ? 0.6198 0.3920 0.5177 0.0849  0.0546  0.0365  93  THR A OG1 
723  C CG2 . THR A 93  ? 0.6602 0.4195 0.5448 0.0641  0.0554  0.0289  93  THR A CG2 
724  N N   . ALA A 94  ? 0.5333 0.3121 0.4220 0.0457  0.0416  0.0347  94  ALA A N   
725  C CA  . ALA A 94  ? 0.5239 0.3138 0.4169 0.0350  0.0376  0.0335  94  ALA A CA  
726  C C   . ALA A 94  ? 0.5161 0.3095 0.4115 0.0317  0.0390  0.0284  94  ALA A C   
727  O O   . ALA A 94  ? 0.5173 0.2955 0.4038 0.0316  0.0440  0.0255  94  ALA A O   
728  C CB  . ALA A 94  ? 0.5556 0.3328 0.4377 0.0241  0.0372  0.0358  94  ALA A CB  
729  N N   . ASN A 95  ? 0.4482 0.2612 0.3554 0.0291  0.0348  0.0272  95  ASN A N   
730  C CA  . ASN A 95  ? 0.4192 0.2375 0.3300 0.0262  0.0357  0.0224  95  ASN A CA  
731  C C   . ASN A 95  ? 0.4221 0.2266 0.3217 0.0138  0.0374  0.0208  95  ASN A C   
732  O O   . ASN A 95  ? 0.4399 0.2470 0.3390 0.0040  0.0342  0.0233  95  ASN A O   
733  C CB  . ASN A 95  ? 0.3892 0.2311 0.3146 0.0253  0.0306  0.0220  95  ASN A CB  
734  C CG  . ASN A 95  ? 0.4302 0.2790 0.3601 0.0217  0.0309  0.0173  95  ASN A CG  
735  O OD1 . ASN A 95  ? 0.4012 0.2375 0.3233 0.0207  0.0352  0.0141  95  ASN A OD1 
736  N ND2 . ASN A 95  ? 0.3815 0.2496 0.3235 0.0199  0.0267  0.0168  95  ASN A ND2 
737  N N   . PRO A 96  ? 0.4489 0.2384 0.3391 0.0136  0.0427  0.0171  96  PRO A N   
738  C CA  . PRO A 96  ? 0.5096 0.2845 0.3870 0.0006  0.0444  0.0155  96  PRO A CA  
739  C C   . PRO A 96  ? 0.5043 0.2935 0.3887 -0.0098 0.0403  0.0143  96  PRO A C   
740  O O   . PRO A 96  ? 0.4993 0.2807 0.3751 -0.0226 0.0397  0.0149  96  PRO A O   
741  C CB  . PRO A 96  ? 0.5273 0.2845 0.3944 0.0046  0.0517  0.0111  96  PRO A CB  
742  C CG  . PRO A 96  ? 0.6369 0.3994 0.5121 0.0204  0.0538  0.0115  96  PRO A CG  
743  C CD  . PRO A 96  ? 0.4778 0.2647 0.3695 0.0246  0.0473  0.0142  96  PRO A CD  
744  N N   . LYS A 97  ? 0.4298 0.2398 0.3293 -0.0051 0.0373  0.0130  97  LYS A N   
745  C CA  . LYS A 97  ? 0.4027 0.2275 0.3104 -0.0138 0.0336  0.0120  97  LYS A CA  
746  C C   . LYS A 97  ? 0.4067 0.2480 0.3253 -0.0171 0.0280  0.0166  97  LYS A C   
747  O O   . LYS A 97  ? 0.4044 0.2615 0.3333 -0.0218 0.0247  0.0164  97  LYS A O   
748  C CB  . LYS A 97  ? 0.4164 0.2536 0.3339 -0.0070 0.0341  0.0076  97  LYS A CB  
749  C CG  . LYS A 97  ? 0.5106 0.3329 0.4182 -0.0058 0.0400  0.0028  97  LYS A CG  
750  C CD  . LYS A 97  ? 0.4884 0.3233 0.4067 0.0043  0.0408  -0.0004 97  LYS A CD  
751  C CE  . LYS A 97  ? 0.6755 0.4949 0.5846 0.0086  0.0480  -0.0044 97  LYS A CE  
752  N NZ  . LYS A 97  ? 0.7532 0.5872 0.6740 0.0173  0.0484  -0.0070 97  LYS A NZ  
753  N N   . THR A 98  ? 0.3977 0.2355 0.3143 -0.0147 0.0272  0.0210  98  THR A N   
754  C CA  . THR A 98  ? 0.3842 0.2370 0.3110 -0.0170 0.0229  0.0255  98  THR A CA  
755  C C   . THR A 98  ? 0.3951 0.2513 0.3224 -0.0309 0.0206  0.0280  98  THR A C   
756  O O   . THR A 98  ? 0.4238 0.2654 0.3391 -0.0396 0.0217  0.0297  98  THR A O   
757  C CB  . THR A 98  ? 0.4568 0.3029 0.3793 -0.0130 0.0230  0.0298  98  THR A CB  
758  O OG1 . THR A 98  ? 0.4208 0.2640 0.3429 -0.0005 0.0250  0.0282  98  THR A OG1 
759  C CG2 . THR A 98  ? 0.4037 0.2655 0.3370 -0.0142 0.0194  0.0343  98  THR A CG2 
760  N N   . PRO A 99  ? 0.3677 0.2421 0.3080 -0.0338 0.0175  0.0287  99  PRO A N   
761  C CA  . PRO A 99  ? 0.3227 0.2022 0.2654 -0.0468 0.0151  0.0327  99  PRO A CA  
762  C C   . PRO A 99  ? 0.3575 0.2401 0.3029 -0.0490 0.0135  0.0396  99  PRO A C   
763  O O   . PRO A 99  ? 0.3892 0.2722 0.3361 -0.0404 0.0140  0.0407  99  PRO A O   
764  C CB  . PRO A 99  ? 0.3259 0.2243 0.2828 -0.0467 0.0129  0.0307  99  PRO A CB  
765  C CG  . PRO A 99  ? 0.3142 0.2215 0.2791 -0.0335 0.0129  0.0288  99  PRO A CG  
766  C CD  . PRO A 99  ? 0.3663 0.2580 0.3201 -0.0253 0.0160  0.0267  99  PRO A CD  
767  N N   . LYS A 100 ? 0.3396 0.3108 0.2898 -0.0195 0.0207  -0.0282 100 LYS A N   
768  C CA  . LYS A 100 ? 0.3231 0.3040 0.2816 -0.0232 0.0192  -0.0292 100 LYS A CA  
769  C C   . LYS A 100 ? 0.2956 0.2858 0.2632 -0.0175 0.0168  -0.0253 100 LYS A C   
770  O O   . LYS A 100 ? 0.2829 0.2783 0.2526 -0.0130 0.0143  -0.0234 100 LYS A O   
771  C CB  . LYS A 100 ? 0.3650 0.3562 0.3260 -0.0294 0.0158  -0.0334 100 LYS A CB  
772  C CG  . LYS A 100 ? 0.5105 0.4929 0.4630 -0.0374 0.0183  -0.0382 100 LYS A CG  
773  C CD  . LYS A 100 ? 0.6611 0.6539 0.6144 -0.0430 0.0142  -0.0424 100 LYS A CD  
774  C CE  . LYS A 100 ? 0.7449 0.7290 0.6899 -0.0525 0.0169  -0.0477 100 LYS A CE  
775  N NZ  . LYS A 100 ? 0.7891 0.7879 0.7410 -0.0605 0.0139  -0.0514 100 LYS A NZ  
776  N N   . TYR A 101 ? 0.3043 0.2957 0.2765 -0.0175 0.0181  -0.0239 101 TYR A N   
777  C CA  . TYR A 101 ? 0.2786 0.2768 0.2578 -0.0121 0.0162  -0.0202 101 TYR A CA  
778  C C   . TYR A 101 ? 0.3007 0.3047 0.2861 -0.0140 0.0163  -0.0201 101 TYR A C   
779  O O   . TYR A 101 ? 0.2625 0.2638 0.2470 -0.0189 0.0185  -0.0223 101 TYR A O   
780  C CB  . TYR A 101 ? 0.2588 0.2490 0.2351 -0.0067 0.0183  -0.0167 101 TYR A CB  
781  C CG  . TYR A 101 ? 0.2833 0.2647 0.2563 -0.0073 0.0223  -0.0161 101 TYR A CG  
782  C CD1 . TYR A 101 ? 0.3325 0.3019 0.2967 -0.0090 0.0262  -0.0173 101 TYR A CD1 
783  C CD2 . TYR A 101 ? 0.2769 0.2610 0.2546 -0.0058 0.0223  -0.0141 101 TYR A CD2 
784  C CE1 . TYR A 101 ? 0.3529 0.3133 0.3131 -0.0088 0.0304  -0.0165 101 TYR A CE1 
785  C CE2 . TYR A 101 ? 0.2902 0.2660 0.2643 -0.0057 0.0260  -0.0134 101 TYR A CE2 
786  C CZ  . TYR A 101 ? 0.3441 0.3083 0.3096 -0.0071 0.0301  -0.0145 101 TYR A CZ  
787  O OH  . TYR A 101 ? 0.4438 0.3992 0.4048 -0.0063 0.0343  -0.0134 101 TYR A OH  
788  N N   . LYS A 102 ? 0.2467 0.2578 0.2381 -0.0099 0.0142  -0.0174 102 LYS A N   
789  C CA  . LYS A 102 ? 0.2702 0.2865 0.2672 -0.0100 0.0142  -0.0165 102 LYS A CA  
790  C C   . LYS A 102 ? 0.2404 0.2554 0.2388 -0.0046 0.0139  -0.0129 102 LYS A C   
791  O O   . LYS A 102 ? 0.2194 0.2343 0.2169 -0.0012 0.0125  -0.0114 102 LYS A O   
792  C CB  . LYS A 102 ? 0.2679 0.2971 0.2708 -0.0114 0.0114  -0.0175 102 LYS A CB  
793  C CG  . LYS A 102 ? 0.3433 0.3761 0.3460 -0.0178 0.0115  -0.0214 102 LYS A CG  
794  C CD  . LYS A 102 ? 0.4560 0.5024 0.4658 -0.0195 0.0097  -0.0219 102 LYS A CD  
795  C CE  . LYS A 102 ? 0.3800 0.4356 0.3930 -0.0143 0.0065  -0.0199 102 LYS A CE  
796  N NZ  . LYS A 102 ? 0.6188 0.6876 0.6348 -0.0169 0.0037  -0.0222 102 LYS A NZ  
797  N N   . PHE A 103 ? 0.2165 0.2301 0.2166 -0.0042 0.0152  -0.0116 103 PHE A N   
798  C CA  . PHE A 103 ? 0.1946 0.2086 0.1964 0.0000  0.0144  -0.0087 103 PHE A CA  
799  C C   . PHE A 103 ? 0.2444 0.2665 0.2512 0.0004  0.0132  -0.0083 103 PHE A C   
800  O O   . PHE A 103 ? 0.2519 0.2757 0.2606 -0.0018 0.0145  -0.0090 103 PHE A O   
801  C CB  . PHE A 103 ? 0.1752 0.1818 0.1744 0.0009  0.0168  -0.0073 103 PHE A CB  
802  C CG  . PHE A 103 ? 0.2119 0.2106 0.2058 0.0022  0.0184  -0.0066 103 PHE A CG  
803  C CD1 . PHE A 103 ? 0.2298 0.2277 0.2215 0.0030  0.0178  -0.0069 103 PHE A CD1 
804  C CD2 . PHE A 103 ? 0.2606 0.2527 0.2511 0.0034  0.0208  -0.0054 103 PHE A CD2 
805  C CE1 . PHE A 103 ? 0.2420 0.2326 0.2285 0.0050  0.0199  -0.0057 103 PHE A CE1 
806  C CE2 . PHE A 103 ? 0.2582 0.2434 0.2434 0.0057  0.0228  -0.0042 103 PHE A CE2 
807  C CZ  . PHE A 103 ? 0.2698 0.2544 0.2531 0.0066  0.0224  -0.0042 103 PHE A CZ  
808  N N   . VAL A 104 ? 0.2064 0.2329 0.2147 0.0034  0.0111  -0.0069 104 VAL A N   
809  C CA  . VAL A 104 ? 0.1910 0.2247 0.2029 0.0049  0.0103  -0.0061 104 VAL A CA  
810  C C   . VAL A 104 ? 0.2839 0.3146 0.2948 0.0085  0.0102  -0.0036 104 VAL A C   
811  O O   . VAL A 104 ? 0.3671 0.3936 0.3758 0.0097  0.0097  -0.0028 104 VAL A O   
812  C CB  . VAL A 104 ? 0.2428 0.2851 0.2565 0.0052  0.0084  -0.0071 104 VAL A CB  
813  C CG1 . VAL A 104 ? 0.2365 0.2809 0.2502 0.0005  0.0083  -0.0101 104 VAL A CG1 
814  C CG2 . VAL A 104 ? 0.3067 0.3471 0.3181 0.0081  0.0072  -0.0061 104 VAL A CG2 
815  N N   . ARG A 105 ? 0.1875 0.2201 0.1996 0.0099  0.0108  -0.0025 105 ARG A N   
816  C CA  . ARG A 105 ? 0.1449 0.1743 0.1551 0.0129  0.0108  -0.0004 105 ARG A CA  
817  C C   . ARG A 105 ? 0.2103 0.2451 0.2212 0.0158  0.0104  0.0005  105 ARG A C   
818  O O   . ARG A 105 ? 0.2100 0.2520 0.2236 0.0162  0.0105  0.0003  105 ARG A O   
819  C CB  . ARG A 105 ? 0.1755 0.2008 0.1845 0.0130  0.0123  0.0005  105 ARG A CB  
820  C CG  . ARG A 105 ? 0.1900 0.2101 0.1957 0.0149  0.0124  0.0020  105 ARG A CG  
821  C CD  . ARG A 105 ? 0.1559 0.1714 0.1595 0.0148  0.0139  0.0026  105 ARG A CD  
822  N NE  . ARG A 105 ? 0.2308 0.2406 0.2301 0.0161  0.0140  0.0038  105 ARG A NE  
823  C CZ  . ARG A 105 ? 0.2113 0.2163 0.2080 0.0149  0.0131  0.0038  105 ARG A CZ  
824  N NH1 . ARG A 105 ? 0.1968 0.2020 0.1945 0.0134  0.0121  0.0032  105 ARG A NH1 
825  N NH2 . ARG A 105 ? 0.1869 0.1870 0.1794 0.0152  0.0133  0.0045  105 ARG A NH2 
826  N N   . ILE A 106 ? 0.2154 0.2472 0.2239 0.0181  0.0101  0.0018  106 ILE A N   
827  C CA  . ILE A 106 ? 0.2358 0.2715 0.2437 0.0216  0.0102  0.0029  106 ILE A CA  
828  C C   . ILE A 106 ? 0.2128 0.2439 0.2175 0.0242  0.0122  0.0049  106 ILE A C   
829  O O   . ILE A 106 ? 0.2184 0.2430 0.2211 0.0228  0.0130  0.0051  106 ILE A O   
830  C CB  . ILE A 106 ? 0.2575 0.2924 0.2640 0.0226  0.0093  0.0030  106 ILE A CB  
831  C CG1 . ILE A 106 ? 0.2452 0.2724 0.2495 0.0214  0.0096  0.0036  106 ILE A CG1 
832  C CG2 . ILE A 106 ? 0.3351 0.3751 0.3436 0.0208  0.0076  0.0010  106 ILE A CG2 
833  C CD1 . ILE A 106 ? 0.4335 0.4579 0.4351 0.0237  0.0103  0.0049  106 ILE A CD1 
834  N N   . GLN A 107 ? 0.2306 0.2647 0.2340 0.0281  0.0131  0.0063  107 GLN A N   
835  C CA  . GLN A 107 ? 0.2478 0.2774 0.2468 0.0318  0.0157  0.0085  107 GLN A CA  
836  C C   . GLN A 107 ? 0.2601 0.2831 0.2543 0.0335  0.0168  0.0095  107 GLN A C   
837  O O   . GLN A 107 ? 0.2438 0.2693 0.2389 0.0338  0.0156  0.0091  107 GLN A O   
838  C CB  . GLN A 107 ? 0.2798 0.3180 0.2801 0.0361  0.0167  0.0099  107 GLN A CB  
839  C CG  . GLN A 107 ? 0.2825 0.3275 0.2877 0.0343  0.0164  0.0092  107 GLN A CG  
840  C CD  . GLN A 107 ? 0.3478 0.3855 0.3500 0.0346  0.0188  0.0103  107 GLN A CD  
841  O OE1 . GLN A 107 ? 0.3402 0.3705 0.3364 0.0378  0.0213  0.0121  107 GLN A OE1 
842  N NE2 . GLN A 107 ? 0.2715 0.3101 0.2768 0.0312  0.0186  0.0091  107 GLN A NE2 
843  N N   . PRO A 108 ? 0.2364 0.2504 0.2249 0.0344  0.0193  0.0107  108 PRO A N   
844  C CA  . PRO A 108 ? 0.2266 0.2339 0.2097 0.0363  0.0212  0.0119  108 PRO A CA  
845  C C   . PRO A 108 ? 0.2585 0.2716 0.2412 0.0416  0.0220  0.0134  108 PRO A C   
846  O O   . PRO A 108 ? 0.2988 0.3190 0.2829 0.0452  0.0223  0.0144  108 PRO A O   
847  C CB  . PRO A 108 ? 0.2939 0.2910 0.2700 0.0371  0.0245  0.0131  108 PRO A CB  
848  C CG  . PRO A 108 ? 0.2918 0.2887 0.2700 0.0338  0.0233  0.0119  108 PRO A CG  
849  C CD  . PRO A 108 ? 0.2828 0.2913 0.2686 0.0337  0.0208  0.0110  108 PRO A CD  
850  N N   . GLY A 109 ? 0.2453 0.2563 0.2263 0.0422  0.0222  0.0136  109 GLY A N   
851  C CA  . GLY A 109 ? 0.2633 0.2793 0.2432 0.0475  0.0227  0.0149  109 GLY A CA  
852  C C   . GLY A 109 ? 0.3149 0.3411 0.3005 0.0465  0.0190  0.0133  109 GLY A C   
853  O O   . GLY A 109 ? 0.3223 0.3522 0.3065 0.0504  0.0190  0.0141  109 GLY A O   
854  N N   . GLN A 110 ? 0.2126 0.2429 0.2037 0.0417  0.0162  0.0111  110 GLN A N   
855  C CA  . GLN A 110 ? 0.2266 0.2644 0.2219 0.0399  0.0131  0.0093  110 GLN A CA  
856  C C   . GLN A 110 ? 0.2164 0.2487 0.2110 0.0374  0.0126  0.0086  110 GLN A C   
857  O O   . GLN A 110 ? 0.2321 0.2569 0.2255 0.0351  0.0138  0.0089  110 GLN A O   
858  C CB  . GLN A 110 ? 0.2369 0.2807 0.2375 0.0360  0.0110  0.0073  110 GLN A CB  
859  C CG  . GLN A 110 ? 0.3057 0.3562 0.3080 0.0381  0.0117  0.0081  110 GLN A CG  
860  C CD  . GLN A 110 ? 0.5130 0.5710 0.5210 0.0339  0.0098  0.0059  110 GLN A CD  
861  O OE1 . GLN A 110 ? 0.2980 0.3517 0.3072 0.0301  0.0100  0.0049  110 GLN A OE1 
862  N NE2 . GLN A 110 ? 0.7411 0.8103 0.7520 0.0345  0.0080  0.0051  110 GLN A NE2 
863  N N   . THR A 111 ? 0.2299 0.2665 0.2251 0.0381  0.0110  0.0078  111 THR A N   
864  C CA  . THR A 111 ? 0.1907 0.2230 0.1851 0.0367  0.0109  0.0075  111 THR A CA  
865  C C   . THR A 111 ? 0.2314 0.2658 0.2289 0.0327  0.0086  0.0053  111 THR A C   
866  O O   . THR A 111 ? 0.2356 0.2755 0.2355 0.0310  0.0070  0.0036  111 THR A O   
867  C CB  . THR A 111 ? 0.2136 0.2473 0.2047 0.0411  0.0113  0.0085  111 THR A CB  
868  O OG1 . THR A 111 ? 0.2638 0.3068 0.2561 0.0425  0.0090  0.0073  111 THR A OG1 
869  C CG2 . THR A 111 ? 0.2413 0.2701 0.2279 0.0453  0.0145  0.0109  111 THR A CG2 
870  N N   . PHE A 112 ? 0.2015 0.2313 0.1985 0.0313  0.0090  0.0055  112 PHE A N   
871  C CA  . PHE A 112 ? 0.2028 0.2328 0.2011 0.0284  0.0077  0.0038  112 PHE A CA  
872  C C   . PHE A 112 ? 0.2438 0.2696 0.2406 0.0290  0.0087  0.0049  112 PHE A C   
873  O O   . PHE A 112 ? 0.2340 0.2567 0.2301 0.0304  0.0103  0.0068  112 PHE A O   
874  C CB  . PHE A 112 ? 0.1878 0.2163 0.1887 0.0248  0.0075  0.0031  112 PHE A CB  
875  C CG  . PHE A 112 ? 0.2529 0.2768 0.2541 0.0240  0.0087  0.0047  112 PHE A CG  
876  C CD1 . PHE A 112 ? 0.2384 0.2611 0.2390 0.0245  0.0096  0.0055  112 PHE A CD1 
877  C CD2 . PHE A 112 ? 0.1946 0.2158 0.1964 0.0226  0.0090  0.0053  112 PHE A CD2 
878  C CE1 . PHE A 112 ? 0.2541 0.2723 0.2543 0.0230  0.0105  0.0064  112 PHE A CE1 
879  C CE2 . PHE A 112 ? 0.2438 0.2623 0.2461 0.0212  0.0097  0.0065  112 PHE A CE2 
880  C CZ  . PHE A 112 ? 0.2577 0.2744 0.2590 0.0210  0.0103  0.0068  112 PHE A CZ  
881  N N   . SER A 113 ? 0.1835 0.2090 0.1797 0.0279  0.0080  0.0037  113 SER A N   
882  C CA  . SER A 113 ? 0.2100 0.2318 0.2049 0.0288  0.0092  0.0050  113 SER A CA  
883  C C   . SER A 113 ? 0.2299 0.2494 0.2271 0.0266  0.0099  0.0058  113 SER A C   
884  O O   . SER A 113 ? 0.2217 0.2413 0.2199 0.0243  0.0092  0.0046  113 SER A O   
885  C CB  . SER A 113 ? 0.2253 0.2468 0.2168 0.0292  0.0085  0.0034  113 SER A CB  
886  O OG  . SER A 113 ? 0.2416 0.2666 0.2310 0.0314  0.0075  0.0027  113 SER A OG  
887  N N   . VAL A 114 ? 0.2101 0.2278 0.2079 0.0274  0.0114  0.0080  114 VAL A N   
888  C CA  . VAL A 114 ? 0.1966 0.2140 0.1968 0.0259  0.0118  0.0091  114 VAL A CA  
889  C C   . VAL A 114 ? 0.2350 0.2511 0.2340 0.0277  0.0132  0.0105  114 VAL A C   
890  O O   . VAL A 114 ? 0.2339 0.2493 0.2317 0.0299  0.0144  0.0117  114 VAL A O   
891  C CB  . VAL A 114 ? 0.2013 0.2193 0.2041 0.0247  0.0124  0.0107  114 VAL A CB  
892  C CG1 . VAL A 114 ? 0.2198 0.2394 0.2254 0.0235  0.0127  0.0123  114 VAL A CG1 
893  C CG2 . VAL A 114 ? 0.2172 0.2350 0.2201 0.0231  0.0115  0.0095  114 VAL A CG2 
894  N N   . LEU A 115 ? 0.2173 0.2324 0.2158 0.0273  0.0134  0.0104  115 LEU A N   
895  C CA  . LEU A 115 ? 0.2258 0.2392 0.2226 0.0297  0.0153  0.0122  115 LEU A CA  
896  C C   . LEU A 115 ? 0.2311 0.2480 0.2320 0.0295  0.0158  0.0149  115 LEU A C   
897  O O   . LEU A 115 ? 0.2286 0.2461 0.2302 0.0288  0.0155  0.0149  115 LEU A O   
898  C CB  . LEU A 115 ? 0.2098 0.2187 0.2017 0.0300  0.0158  0.0107  115 LEU A CB  
899  C CG  . LEU A 115 ? 0.2254 0.2310 0.2140 0.0331  0.0185  0.0128  115 LEU A CG  
900  C CD1 . LEU A 115 ? 0.2199 0.2243 0.2061 0.0356  0.0194  0.0135  115 LEU A CD1 
901  C CD2 . LEU A 115 ? 0.2399 0.2391 0.2225 0.0330  0.0197  0.0113  115 LEU A CD2 
902  N N   . ALA A 116 ? 0.2229 0.2427 0.2268 0.0301  0.0168  0.0170  116 ALA A N   
903  C CA  . ALA A 116 ? 0.2037 0.2288 0.2122 0.0294  0.0171  0.0195  116 ALA A CA  
904  C C   . ALA A 116 ? 0.2638 0.2896 0.2714 0.0327  0.0189  0.0219  116 ALA A C   
905  O O   . ALA A 116 ? 0.2981 0.3212 0.3028 0.0358  0.0210  0.0229  116 ALA A O   
906  C CB  . ALA A 116 ? 0.2513 0.2794 0.2632 0.0284  0.0180  0.0210  116 ALA A CB  
907  N N   . CYS A 117 ? 0.1974 0.2266 0.2068 0.0326  0.0183  0.0228  117 CYS A N   
908  C CA  A CYS A 117 ? 0.2504 0.2800 0.2581 0.0364  0.0203  0.0253  117 CYS A CA  
909  C CA  B CYS A 117 ? 0.2511 0.2806 0.2586 0.0363  0.0202  0.0252  117 CYS A CA  
910  C C   . CYS A 117 ? 0.2787 0.3179 0.2921 0.0366  0.0199  0.0283  117 CYS A C   
911  O O   . CYS A 117 ? 0.2650 0.3090 0.2823 0.0330  0.0175  0.0275  117 CYS A O   
912  C CB  A CYS A 117 ? 0.2755 0.2987 0.2776 0.0371  0.0205  0.0236  117 CYS A CB  
913  C CB  B CYS A 117 ? 0.2766 0.3003 0.2793 0.0364  0.0200  0.0233  117 CYS A CB  
914  S SG  A CYS A 117 ? 0.2663 0.2798 0.2617 0.0363  0.0209  0.0199  117 CYS A SG  
915  S SG  B CYS A 117 ? 0.3111 0.3278 0.3063 0.0414  0.0238  0.0248  117 CYS A SG  
916  N N   . TYR A 118 ? 0.2402 0.2822 0.2535 0.0410  0.0224  0.0319  118 TYR A N   
917  C CA  . TYR A 118 ? 0.2683 0.3213 0.2870 0.0423  0.0222  0.0354  118 TYR A CA  
918  C C   . TYR A 118 ? 0.2881 0.3396 0.3025 0.0485  0.0251  0.0383  118 TYR A C   
919  O O   . TYR A 118 ? 0.3001 0.3452 0.3096 0.0524  0.0284  0.0395  118 TYR A O   
920  C CB  . TYR A 118 ? 0.2770 0.3384 0.3023 0.0413  0.0229  0.0377  118 TYR A CB  
921  C CG  . TYR A 118 ? 0.2775 0.3384 0.3056 0.0353  0.0208  0.0348  118 TYR A CG  
922  C CD1 . TYR A 118 ? 0.2270 0.2946 0.2599 0.0304  0.0180  0.0339  118 TYR A CD1 
923  C CD2 . TYR A 118 ? 0.2075 0.2601 0.2322 0.0348  0.0218  0.0329  118 TYR A CD2 
924  C CE1 . TYR A 118 ? 0.2237 0.2888 0.2575 0.0252  0.0168  0.0313  118 TYR A CE1 
925  C CE2 . TYR A 118 ? 0.2334 0.2843 0.2593 0.0303  0.0205  0.0305  118 TYR A CE2 
926  C CZ  . TYR A 118 ? 0.2437 0.3004 0.2739 0.0255  0.0182  0.0298  118 TYR A CZ  
927  O OH  . TYR A 118 ? 0.2411 0.2945 0.2712 0.0211  0.0176  0.0276  118 TYR A OH  
928  N N   . ASN A 119 ? 0.3130 0.3695 0.3281 0.0498  0.0242  0.0396  119 ASN A N   
929  C CA  . ASN A 119 ? 0.3659 0.4207 0.3760 0.0565  0.0274  0.0429  119 ASN A CA  
930  C C   . ASN A 119 ? 0.3287 0.3677 0.3285 0.0584  0.0303  0.0408  119 ASN A C   
931  O O   . ASN A 119 ? 0.3254 0.3589 0.3191 0.0640  0.0344  0.0433  119 ASN A O   
932  C CB  . ASN A 119 ? 0.3750 0.4387 0.3888 0.0613  0.0300  0.0479  119 ASN A CB  
933  C CG  . ASN A 119 ? 0.4220 0.5027 0.4461 0.0588  0.0271  0.0500  119 ASN A CG  
934  O OD1 . ASN A 119 ? 0.4829 0.5709 0.5090 0.0587  0.0248  0.0506  119 ASN A OD1 
935  N ND2 . ASN A 119 ? 0.4550 0.5421 0.4854 0.0565  0.0271  0.0509  119 ASN A ND2 
936  N N   . GLY A 120 ? 0.3050 0.3365 0.3025 0.0536  0.0283  0.0362  120 GLY A N   
937  C CA  . GLY A 120 ? 0.3175 0.3352 0.3059 0.0538  0.0305  0.0334  120 GLY A CA  
938  C C   . GLY A 120 ? 0.3601 0.3720 0.3454 0.0541  0.0321  0.0326  120 GLY A C   
939  O O   . GLY A 120 ? 0.3769 0.3774 0.3541 0.0538  0.0338  0.0301  120 GLY A O   
940  N N   . SER A 121 ? 0.2718 0.2908 0.2628 0.0543  0.0316  0.0344  121 SER A N   
941  C CA  . SER A 121 ? 0.2544 0.2683 0.2422 0.0553  0.0333  0.0341  121 SER A CA  
942  C C   . SER A 121 ? 0.3057 0.3212 0.2975 0.0504  0.0302  0.0310  121 SER A C   
943  O O   . SER A 121 ? 0.3161 0.3405 0.3156 0.0483  0.0284  0.0320  121 SER A O   
944  C CB  . SER A 121 ? 0.4021 0.4218 0.3924 0.0603  0.0362  0.0391  121 SER A CB  
945  O OG  . SER A 121 ? 0.5778 0.5925 0.5613 0.0662  0.0403  0.0420  121 SER A OG  
946  N N   . PRO A 122 ? 0.3305 0.3377 0.3168 0.0486  0.0298  0.0275  122 PRO A N   
947  C CA  . PRO A 122 ? 0.3138 0.3229 0.3032 0.0451  0.0272  0.0251  122 PRO A CA  
948  C C   . PRO A 122 ? 0.3293 0.3421 0.3218 0.0469  0.0285  0.0276  122 PRO A C   
949  O O   . PRO A 122 ? 0.3112 0.3210 0.3000 0.0510  0.0316  0.0299  122 PRO A O   
950  C CB  . PRO A 122 ? 0.3175 0.3177 0.2994 0.0439  0.0269  0.0212  122 PRO A CB  
951  C CG  . PRO A 122 ? 0.3716 0.3654 0.3477 0.0446  0.0285  0.0207  122 PRO A CG  
952  C CD  . PRO A 122 ? 0.3192 0.3154 0.2960 0.0493  0.0315  0.0252  122 PRO A CD  
953  N N   . SER A 123 ? 0.2973 0.3159 0.2961 0.0438  0.0266  0.0273  123 SER A N   
954  C CA  . SER A 123 ? 0.3203 0.3421 0.3222 0.0448  0.0282  0.0296  123 SER A CA  
955  C C   . SER A 123 ? 0.2854 0.3036 0.2853 0.0435  0.0275  0.0274  123 SER A C   
956  O O   . SER A 123 ? 0.2786 0.2954 0.2773 0.0459  0.0297  0.0290  123 SER A O   
957  C CB  . SER A 123 ? 0.3414 0.3730 0.3518 0.0423  0.0276  0.0317  123 SER A CB  
958  O OG  . SER A 123 ? 0.4622 0.4947 0.4749 0.0377  0.0248  0.0290  123 SER A OG  
959  N N   . GLY A 124 ? 0.2202 0.2371 0.2197 0.0404  0.0247  0.0241  124 GLY A N   
960  C CA  . GLY A 124 ? 0.2562 0.2706 0.2536 0.0401  0.0243  0.0225  124 GLY A CA  
961  C C   . GLY A 124 ? 0.2889 0.3019 0.2847 0.0377  0.0214  0.0191  124 GLY A C   
962  O O   . GLY A 124 ? 0.2327 0.2472 0.2303 0.0354  0.0198  0.0180  124 GLY A O   
963  N N   . VAL A 125 ? 0.2373 0.2481 0.2299 0.0386  0.0209  0.0175  125 VAL A N   
964  C CA  . VAL A 125 ? 0.2265 0.2374 0.2179 0.0368  0.0183  0.0146  125 VAL A CA  
965  C C   . VAL A 125 ? 0.2589 0.2703 0.2503 0.0373  0.0185  0.0147  125 VAL A C   
966  O O   . VAL A 125 ? 0.2589 0.2684 0.2479 0.0401  0.0204  0.0160  125 VAL A O   
967  C CB  . VAL A 125 ? 0.2641 0.2724 0.2500 0.0376  0.0172  0.0121  125 VAL A CB  
968  C CG1 . VAL A 125 ? 0.3006 0.3063 0.2814 0.0411  0.0183  0.0125  125 VAL A CG1 
969  C CG2 . VAL A 125 ? 0.2629 0.2734 0.2490 0.0352  0.0146  0.0092  125 VAL A CG2 
970  N N   . TYR A 126 ? 0.2256 0.2386 0.2189 0.0351  0.0171  0.0135  126 TYR A N   
971  C CA  . TYR A 126 ? 0.2486 0.2609 0.2408 0.0362  0.0178  0.0138  126 TYR A CA  
972  C C   . TYR A 126 ? 0.2545 0.2687 0.2470 0.0349  0.0158  0.0119  126 TYR A C   
973  O O   . TYR A 126 ? 0.2573 0.2732 0.2518 0.0324  0.0140  0.0105  126 TYR A O   
974  C CB  . TYR A 126 ? 0.2146 0.2256 0.2093 0.0347  0.0202  0.0160  126 TYR A CB  
975  C CG  . TYR A 126 ? 0.2311 0.2443 0.2303 0.0305  0.0192  0.0159  126 TYR A CG  
976  C CD1 . TYR A 126 ? 0.2633 0.2760 0.2628 0.0283  0.0183  0.0148  126 TYR A CD1 
977  C CD2 . TYR A 126 ? 0.2421 0.2579 0.2447 0.0294  0.0193  0.0171  126 TYR A CD2 
978  C CE1 . TYR A 126 ? 0.2365 0.2510 0.2394 0.0245  0.0173  0.0146  126 TYR A CE1 
979  C CE2 . TYR A 126 ? 0.2792 0.2979 0.2856 0.0260  0.0182  0.0172  126 TYR A CE2 
980  C CZ  . TYR A 126 ? 0.2518 0.2697 0.2582 0.0234  0.0171  0.0158  126 TYR A CZ  
981  O OH  . TYR A 126 ? 0.3112 0.3319 0.3207 0.0202  0.0158  0.0158  126 TYR A OH  
982  N N   . GLN A 127 ? 0.2510 0.2645 0.2410 0.0371  0.0165  0.0122  127 GLN A N   
983  C CA  . GLN A 127 ? 0.2537 0.2692 0.2437 0.0368  0.0152  0.0111  127 GLN A CA  
984  C C   . GLN A 127 ? 0.3283 0.3409 0.3194 0.0347  0.0167  0.0119  127 GLN A C   
985  O O   . GLN A 127 ? 0.3108 0.3192 0.3005 0.0349  0.0193  0.0135  127 GLN A O   
986  C CB  . GLN A 127 ? 0.3544 0.3714 0.3404 0.0413  0.0155  0.0112  127 GLN A CB  
987  C CG  . GLN A 127 ? 0.3530 0.3746 0.3377 0.0427  0.0131  0.0095  127 GLN A CG  
988  C CD  . GLN A 127 ? 0.2798 0.3063 0.2675 0.0396  0.0103  0.0072  127 GLN A CD  
989  O OE1 . GLN A 127 ? 0.3499 0.3759 0.3392 0.0365  0.0093  0.0059  127 GLN A OE1 
990  N NE2 . GLN A 127 ? 0.2912 0.3222 0.2793 0.0407  0.0095  0.0069  127 GLN A NE2 
991  N N   . CYS A 128 ? 0.2854 0.2997 0.2781 0.0327  0.0152  0.0107  128 CYS A N   
992  C CA  . CYS A 128 ? 0.2866 0.2978 0.2794 0.0305  0.0161  0.0110  128 CYS A CA  
993  C C   . CYS A 128 ? 0.2918 0.3045 0.2831 0.0323  0.0158  0.0105  128 CYS A C   
994  O O   . CYS A 128 ? 0.2808 0.2989 0.2730 0.0339  0.0140  0.0095  128 CYS A O   
995  C CB  . CYS A 128 ? 0.2614 0.2734 0.2580 0.0261  0.0147  0.0103  128 CYS A CB  
996  S SG  . CYS A 128 ? 0.5007 0.5105 0.4987 0.0235  0.0161  0.0118  128 CYS A SG  
997  N N   . ALA A 129 ? 0.3232 0.3314 0.3121 0.0319  0.0176  0.0112  129 ALA A N   
998  C CA  . ALA A 129 ? 0.2340 0.2434 0.2218 0.0335  0.0176  0.0110  129 ALA A CA  
999  C C   . ALA A 129 ? 0.2494 0.2552 0.2376 0.0296  0.0176  0.0104  129 ALA A C   
1000 O O   . ALA A 129 ? 0.2529 0.2536 0.2402 0.0266  0.0185  0.0106  129 ALA A O   
1001 C CB  . ALA A 129 ? 0.2913 0.2973 0.2735 0.0383  0.0206  0.0128  129 ALA A CB  
1002 N N   . MET A 130 ? 0.2160 0.2246 0.2054 0.0297  0.0166  0.0098  130 MET A N   
1003 C CA  . MET A 130 ? 0.2122 0.2167 0.2009 0.0267  0.0167  0.0093  130 MET A CA  
1004 C C   . MET A 130 ? 0.2421 0.2393 0.2244 0.0289  0.0201  0.0107  130 MET A C   
1005 O O   . MET A 130 ? 0.2765 0.2752 0.2566 0.0334  0.0215  0.0118  130 MET A O   
1006 C CB  . MET A 130 ? 0.2079 0.2174 0.1999 0.0261  0.0151  0.0083  130 MET A CB  
1007 C CG  . MET A 130 ? 0.3024 0.3068 0.2920 0.0245  0.0159  0.0082  130 MET A CG  
1008 S SD  . MET A 130 ? 0.2963 0.2981 0.2873 0.0193  0.0141  0.0072  130 MET A SD  
1009 C CE  . MET A 130 ? 0.2316 0.2402 0.2283 0.0183  0.0117  0.0063  130 MET A CE  
1010 N N   . ARG A 131 ? 0.2407 0.2301 0.2194 0.0257  0.0215  0.0106  131 ARG A N   
1011 C CA  . ARG A 131 ? 0.2590 0.2391 0.2299 0.0274  0.0253  0.0118  131 ARG A CA  
1012 C C   . ARG A 131 ? 0.2770 0.2548 0.2453 0.0282  0.0260  0.0117  131 ARG A C   
1013 O O   . ARG A 131 ? 0.2728 0.2549 0.2452 0.0262  0.0234  0.0106  131 ARG A O   
1014 C CB  . ARG A 131 ? 0.2770 0.2490 0.2444 0.0228  0.0268  0.0113  131 ARG A CB  
1015 C CG  . ARG A 131 ? 0.2774 0.2512 0.2475 0.0214  0.0267  0.0116  131 ARG A CG  
1016 C CD  . ARG A 131 ? 0.2995 0.2729 0.2672 0.0268  0.0292  0.0132  131 ARG A CD  
1017 N NE  . ARG A 131 ? 0.2913 0.2555 0.2502 0.0303  0.0337  0.0146  131 ARG A NE  
1018 C CZ  . ARG A 131 ? 0.3342 0.2976 0.2894 0.0364  0.0363  0.0164  131 ARG A CZ  
1019 N NH1 . ARG A 131 ? 0.3079 0.2787 0.2672 0.0391  0.0347  0.0168  131 ARG A NH1 
1020 N NH2 . ARG A 131 ? 0.3337 0.2879 0.2800 0.0402  0.0409  0.0180  131 ARG A NH2 
1021 N N   . HIS A 132 ? 0.2933 0.2629 0.2537 0.0314  0.0300  0.0132  132 HIS A N   
1022 C CA  . HIS A 132 ? 0.2867 0.2517 0.2427 0.0327  0.0317  0.0136  132 HIS A CA  
1023 C C   . HIS A 132 ? 0.2966 0.2568 0.2517 0.0268  0.0301  0.0117  132 HIS A C   
1024 O O   . HIS A 132 ? 0.3022 0.2624 0.2569 0.0271  0.0298  0.0116  132 HIS A O   
1025 C CB  . HIS A 132 ? 0.3451 0.2993 0.2908 0.0371  0.0371  0.0156  132 HIS A CB  
1026 C CG  . HIS A 132 ? 0.5185 0.4654 0.4576 0.0385  0.0397  0.0163  132 HIS A CG  
1027 N ND1 . HIS A 132 ? 0.5363 0.4899 0.4780 0.0429  0.0396  0.0175  132 HIS A ND1 
1028 C CD2 . HIS A 132 ? 0.5772 0.5103 0.5069 0.0358  0.0425  0.0157  132 HIS A CD2 
1029 C CE1 . HIS A 132 ? 0.5746 0.5187 0.5087 0.0436  0.0426  0.0181  132 HIS A CE1 
1030 N NE2 . HIS A 132 ? 0.5940 0.5251 0.5203 0.0393  0.0443  0.0169  132 HIS A NE2 
1031 N N   . ASN A 133 ? 0.2717 0.2283 0.2263 0.0215  0.0293  0.0104  133 ASN A N   
1032 C CA  . ASN A 133 ? 0.2955 0.2492 0.2494 0.0157  0.0273  0.0086  133 ASN A CA  
1033 C C   . ASN A 133 ? 0.3040 0.2683 0.2670 0.0132  0.0227  0.0075  133 ASN A C   
1034 O O   . ASN A 133 ? 0.2888 0.2528 0.2523 0.0085  0.0206  0.0062  133 ASN A O   
1035 C CB  . ASN A 133 ? 0.2701 0.2147 0.2180 0.0109  0.0291  0.0078  133 ASN A CB  
1036 C CG  . ASN A 133 ? 0.3092 0.2593 0.2628 0.0086  0.0279  0.0077  133 ASN A CG  
1037 O OD1 . ASN A 133 ? 0.2788 0.2386 0.2399 0.0109  0.0257  0.0082  133 ASN A OD1 
1038 N ND2 . ASN A 133 ? 0.3193 0.2623 0.2683 0.0040  0.0297  0.0070  133 ASN A ND2 
1039 N N   . PHE A 134 ? 0.2345 0.2079 0.2042 0.0164  0.0213  0.0081  134 PHE A N   
1040 C CA  . PHE A 134 ? 0.2346 0.2166 0.2116 0.0149  0.0178  0.0073  134 PHE A CA  
1041 C C   . PHE A 134 ? 0.2723 0.2572 0.2528 0.0114  0.0159  0.0068  134 PHE A C   
1042 O O   . PHE A 134 ? 0.3178 0.3077 0.3025 0.0097  0.0133  0.0062  134 PHE A O   
1043 C CB  . PHE A 134 ? 0.2406 0.2217 0.2169 0.0136  0.0167  0.0065  134 PHE A CB  
1044 C CG  . PHE A 134 ? 0.2491 0.2309 0.2249 0.0174  0.0181  0.0072  134 PHE A CG  
1045 C CD1 . PHE A 134 ? 0.2441 0.2342 0.2257 0.0195  0.0172  0.0073  134 PHE A CD1 
1046 C CD2 . PHE A 134 ? 0.3079 0.2819 0.2767 0.0187  0.0208  0.0077  134 PHE A CD2 
1047 C CE1 . PHE A 134 ? 0.3058 0.2985 0.2879 0.0226  0.0186  0.0080  134 PHE A CE1 
1048 C CE2 . PHE A 134 ? 0.3161 0.2919 0.2849 0.0228  0.0225  0.0088  134 PHE A CE2 
1049 C CZ  . PHE A 134 ? 0.3101 0.2962 0.2863 0.0245  0.0212  0.0090  134 PHE A CZ  
1050 N N   . THR A 135 ? 0.2542 0.2359 0.2326 0.0104  0.0174  0.0072  135 THR A N   
1051 C CA  . THR A 135 ? 0.1982 0.1844 0.1810 0.0080  0.0161  0.0073  135 THR A CA  
1052 C C   . THR A 135 ? 0.2194 0.2094 0.2049 0.0117  0.0168  0.0083  135 THR A C   
1053 O O   . THR A 135 ? 0.2496 0.2384 0.2330 0.0157  0.0183  0.0089  135 THR A O   
1054 C CB  . THR A 135 ? 0.2223 0.2031 0.2016 0.0036  0.0175  0.0070  135 THR A CB  
1055 O OG1 . THR A 135 ? 0.2797 0.2530 0.2534 0.0057  0.0214  0.0078  135 THR A OG1 
1056 C CG2 . THR A 135 ? 0.2672 0.2436 0.2425 -0.0003 0.0167  0.0057  135 THR A CG2 
1057 N N   . ILE A 136 ? 0.1990 0.1938 0.1890 0.0106  0.0157  0.0086  136 ILE A N   
1058 C CA  . ILE A 136 ? 0.1771 0.1740 0.1683 0.0137  0.0167  0.0096  136 ILE A CA  
1059 C C   . ILE A 136 ? 0.2447 0.2403 0.2362 0.0113  0.0181  0.0104  136 ILE A C   
1060 O O   . ILE A 136 ? 0.2553 0.2526 0.2490 0.0070  0.0171  0.0102  136 ILE A O   
1061 C CB  . ILE A 136 ? 0.2350 0.2388 0.2308 0.0157  0.0144  0.0094  136 ILE A CB  
1062 C CG1 . ILE A 136 ? 0.2639 0.2720 0.2639 0.0132  0.0126  0.0094  136 ILE A CG1 
1063 C CG2 . ILE A 136 ? 0.2917 0.2969 0.2874 0.0172  0.0134  0.0084  136 ILE A CG2 
1064 C CD1 . ILE A 136 ? 0.2543 0.2669 0.2572 0.0154  0.0119  0.0098  136 ILE A CD1 
1065 N N   . LYS A 137 ? 0.2377 0.2306 0.2270 0.0140  0.0207  0.0115  137 LYS A N   
1066 C CA  . LYS A 137 ? 0.2860 0.2777 0.2758 0.0118  0.0226  0.0124  137 LYS A CA  
1067 C C   . LYS A 137 ? 0.2723 0.2708 0.2672 0.0139  0.0214  0.0133  137 LYS A C   
1068 O O   . LYS A 137 ? 0.2969 0.2949 0.2904 0.0179  0.0229  0.0142  137 LYS A O   
1069 C CB  . LYS A 137 ? 0.2835 0.2667 0.2668 0.0135  0.0269  0.0133  137 LYS A CB  
1070 C CG  . LYS A 137 ? 0.4038 0.3794 0.3804 0.0144  0.0286  0.0128  137 LYS A CG  
1071 C CD  . LYS A 137 ? 0.4645 0.4318 0.4338 0.0185  0.0333  0.0142  137 LYS A CD  
1072 C CE  . LYS A 137 ? 0.5783 0.5342 0.5391 0.0168  0.0368  0.0139  137 LYS A CE  
1073 N NZ  . LYS A 137 ? 0.6007 0.5480 0.5531 0.0224  0.0419  0.0157  137 LYS A NZ  
1074 N N   . GLY A 138 ? 0.2568 0.2615 0.2568 0.0115  0.0190  0.0132  138 GLY A N   
1075 C CA  . GLY A 138 ? 0.2384 0.2488 0.2423 0.0138  0.0181  0.0141  138 GLY A CA  
1076 C C   . GLY A 138 ? 0.2508 0.2636 0.2576 0.0122  0.0197  0.0158  138 GLY A C   
1077 O O   . GLY A 138 ? 0.2523 0.2622 0.2581 0.0092  0.0219  0.0162  138 GLY A O   
1078 N N   . SER A 139 ? 0.1934 0.2115 0.2037 0.0142  0.0190  0.0170  139 SER A N   
1079 C CA  . SER A 139 ? 0.1949 0.2175 0.2092 0.0131  0.0204  0.0191  139 SER A CA  
1080 C C   . SER A 139 ? 0.2512 0.2809 0.2696 0.0136  0.0182  0.0198  139 SER A C   
1081 O O   . SER A 139 ? 0.2380 0.2680 0.2556 0.0175  0.0179  0.0202  139 SER A O   
1082 C CB  . SER A 139 ? 0.2428 0.2630 0.2555 0.0169  0.0232  0.0205  139 SER A CB  
1083 O OG  . SER A 139 ? 0.2816 0.3067 0.2987 0.0160  0.0249  0.0229  139 SER A OG  
1084 N N   . PHE A 140 ? 0.2317 0.2667 0.2536 0.0096  0.0168  0.0199  140 PHE A N   
1085 C CA  . PHE A 140 ? 0.2360 0.2780 0.2613 0.0103  0.0147  0.0208  140 PHE A CA  
1086 C C   . PHE A 140 ? 0.2895 0.3405 0.3203 0.0068  0.0144  0.0225  140 PHE A C   
1087 O O   . PHE A 140 ? 0.2895 0.3406 0.3209 0.0016  0.0143  0.0215  140 PHE A O   
1088 C CB  . PHE A 140 ? 0.2281 0.2684 0.2512 0.0092  0.0121  0.0187  140 PHE A CB  
1089 C CG  . PHE A 140 ? 0.2156 0.2493 0.2343 0.0122  0.0120  0.0171  140 PHE A CG  
1090 C CD1 . PHE A 140 ? 0.2382 0.2718 0.2560 0.0162  0.0122  0.0176  140 PHE A CD1 
1091 C CD2 . PHE A 140 ? 0.2107 0.2387 0.2259 0.0108  0.0117  0.0150  140 PHE A CD2 
1092 C CE1 . PHE A 140 ? 0.2211 0.2497 0.2352 0.0179  0.0118  0.0157  140 PHE A CE1 
1093 C CE2 . PHE A 140 ? 0.2354 0.2594 0.2475 0.0133  0.0114  0.0136  140 PHE A CE2 
1094 C CZ  . PHE A 140 ? 0.2062 0.2310 0.2181 0.0164  0.0112  0.0138  140 PHE A CZ  
1095 N N   . LEU A 141 ? 0.2743 0.3331 0.3090 0.0096  0.0145  0.0251  141 LEU A N   
1096 C CA  . LEU A 141 ? 0.2790 0.3493 0.3199 0.0068  0.0137  0.0270  141 LEU A CA  
1097 C C   . LEU A 141 ? 0.2604 0.3370 0.3024 0.0082  0.0109  0.0275  141 LEU A C   
1098 O O   . LEU A 141 ? 0.2309 0.3019 0.2685 0.0112  0.0101  0.0263  141 LEU A O   
1099 C CB  . LEU A 141 ? 0.2734 0.3494 0.3185 0.0096  0.0166  0.0304  141 LEU A CB  
1100 C CG  . LEU A 141 ? 0.3226 0.3921 0.3661 0.0096  0.0200  0.0305  141 LEU A CG  
1101 C CD1 . LEU A 141 ? 0.3949 0.4699 0.4420 0.0134  0.0229  0.0343  141 LEU A CD1 
1102 C CD2 . LEU A 141 ? 0.3325 0.4019 0.3775 0.0024  0.0203  0.0291  141 LEU A CD2 
1103 N N   . ASN A 142 ? 0.2751 0.3642 0.3229 0.0062  0.0097  0.0294  142 ASN A N   
1104 C CA  . ASN A 142 ? 0.2669 0.3631 0.3155 0.0085  0.0073  0.0304  142 ASN A CA  
1105 C C   . ASN A 142 ? 0.2366 0.3300 0.2825 0.0163  0.0092  0.0326  142 ASN A C   
1106 O O   . ASN A 142 ? 0.2647 0.3579 0.3115 0.0199  0.0121  0.0349  142 ASN A O   
1107 C CB  . ASN A 142 ? 0.2851 0.3973 0.3411 0.0058  0.0058  0.0327  142 ASN A CB  
1108 C CG  . ASN A 142 ? 0.4252 0.5398 0.4818 -0.0023 0.0029  0.0299  142 ASN A CG  
1109 O OD1 . ASN A 142 ? 0.4407 0.5533 0.4938 -0.0034 0.0001  0.0279  142 ASN A OD1 
1110 N ND2 . ASN A 142 ? 0.5374 0.6558 0.5981 -0.0083 0.0038  0.0296  142 ASN A ND2 
1111 N N   . GLY A 143 ? 0.2839 0.3736 0.3255 0.0189  0.0079  0.0318  143 GLY A N   
1112 C CA  . GLY A 143 ? 0.2511 0.3359 0.2884 0.0256  0.0100  0.0333  143 GLY A CA  
1113 C C   . GLY A 143 ? 0.2527 0.3236 0.2837 0.0263  0.0112  0.0305  143 GLY A C   
1114 O O   . GLY A 143 ? 0.2561 0.3213 0.2826 0.0310  0.0131  0.0311  143 GLY A O   
1115 N N   . SER A 144 ? 0.2146 0.2800 0.2449 0.0219  0.0103  0.0274  144 SER A N   
1116 C CA  . SER A 144 ? 0.2414 0.2959 0.2666 0.0225  0.0112  0.0249  144 SER A CA  
1117 C C   . SER A 144 ? 0.2157 0.2649 0.2370 0.0220  0.0098  0.0225  144 SER A C   
1118 O O   . SER A 144 ? 0.2137 0.2550 0.2310 0.0226  0.0104  0.0205  144 SER A O   
1119 C CB  . SER A 144 ? 0.2199 0.2711 0.2455 0.0190  0.0114  0.0232  144 SER A CB  
1120 O OG  . SER A 144 ? 0.2784 0.3312 0.3053 0.0141  0.0094  0.0217  144 SER A OG  
1121 N N   . CYS A 145 ? 0.2184 0.2720 0.2405 0.0210  0.0079  0.0228  145 CYS A N   
1122 C CA  . CYS A 145 ? 0.2115 0.2599 0.2299 0.0205  0.0068  0.0207  145 CYS A CA  
1123 C C   . CYS A 145 ? 0.1990 0.2407 0.2128 0.0244  0.0090  0.0206  145 CYS A C   
1124 O O   . CYS A 145 ? 0.2248 0.2676 0.2377 0.0284  0.0109  0.0229  145 CYS A O   
1125 C CB  . CYS A 145 ? 0.2143 0.2693 0.2338 0.0199  0.0047  0.0216  145 CYS A CB  
1126 S SG  . CYS A 145 ? 0.2404 0.3022 0.2642 0.0137  0.0022  0.0209  145 CYS A SG  
1127 N N   . GLY A 146 ? 0.1919 0.2263 0.2023 0.0232  0.0089  0.0179  146 GLY A N   
1128 C CA  . GLY A 146 ? 0.1953 0.2228 0.2013 0.0255  0.0111  0.0172  146 GLY A CA  
1129 C C   . GLY A 146 ? 0.2002 0.2238 0.2051 0.0255  0.0122  0.0160  146 GLY A C   
1130 O O   . GLY A 146 ? 0.2315 0.2488 0.2322 0.0260  0.0137  0.0145  146 GLY A O   
1131 N N   . SER A 147 ? 0.2191 0.2458 0.2270 0.0247  0.0118  0.0165  147 SER A N   
1132 C CA  . SER A 147 ? 0.1936 0.2165 0.1997 0.0248  0.0126  0.0151  147 SER A CA  
1133 C C   . SER A 147 ? 0.2240 0.2434 0.2286 0.0225  0.0115  0.0121  147 SER A C   
1134 O O   . SER A 147 ? 0.2301 0.2505 0.2361 0.0204  0.0102  0.0113  147 SER A O   
1135 C CB  . SER A 147 ? 0.2043 0.2307 0.2137 0.0243  0.0125  0.0162  147 SER A CB  
1136 O OG  . SER A 147 ? 0.2381 0.2689 0.2496 0.0263  0.0137  0.0192  147 SER A OG  
1137 N N   . VAL A 148 ? 0.1958 0.2117 0.1977 0.0228  0.0121  0.0104  148 VAL A N   
1138 C CA  . VAL A 148 ? 0.1733 0.1876 0.1744 0.0207  0.0112  0.0078  148 VAL A CA  
1139 C C   . VAL A 148 ? 0.1944 0.2098 0.1957 0.0207  0.0106  0.0068  148 VAL A C   
1140 O O   . VAL A 148 ? 0.2229 0.2382 0.2232 0.0225  0.0112  0.0075  148 VAL A O   
1141 C CB  . VAL A 148 ? 0.2094 0.2194 0.2068 0.0202  0.0123  0.0060  148 VAL A CB  
1142 C CG1 . VAL A 148 ? 0.2374 0.2456 0.2338 0.0206  0.0133  0.0071  148 VAL A CG1 
1143 C CG2 . VAL A 148 ? 0.2135 0.2202 0.2071 0.0214  0.0136  0.0056  148 VAL A CG2 
1144 N N   . GLY A 149 ? 0.1978 0.2142 0.1998 0.0193  0.0096  0.0052  149 GLY A N   
1145 C CA  . GLY A 149 ? 0.1950 0.2132 0.1968 0.0198  0.0090  0.0043  149 GLY A CA  
1146 C C   . GLY A 149 ? 0.2287 0.2477 0.2294 0.0185  0.0084  0.0019  149 GLY A C   
1147 O O   . GLY A 149 ? 0.2355 0.2535 0.2364 0.0166  0.0086  0.0009  149 GLY A O   
1148 N N   . PHE A 150 ? 0.1596 0.1807 0.1590 0.0195  0.0078  0.0009  150 PHE A N   
1149 C CA  . PHE A 150 ? 0.1857 0.2086 0.1840 0.0174  0.0070  -0.0017 150 PHE A CA  
1150 C C   . PHE A 150 ? 0.2408 0.2689 0.2388 0.0189  0.0057  -0.0025 150 PHE A C   
1151 O O   . PHE A 150 ? 0.2189 0.2474 0.2161 0.0220  0.0058  -0.0009 150 PHE A O   
1152 C CB  . PHE A 150 ? 0.2326 0.2506 0.2271 0.0163  0.0080  -0.0028 150 PHE A CB  
1153 C CG  . PHE A 150 ? 0.2397 0.2556 0.2314 0.0190  0.0085  -0.0017 150 PHE A CG  
1154 C CD1 . PHE A 150 ? 0.3064 0.3200 0.2987 0.0213  0.0098  0.0010  150 PHE A CD1 
1155 C CD2 . PHE A 150 ? 0.2288 0.2457 0.2172 0.0192  0.0076  -0.0034 150 PHE A CD2 
1156 C CE1 . PHE A 150 ? 0.2901 0.3019 0.2799 0.0240  0.0107  0.0024  150 PHE A CE1 
1157 C CE2 . PHE A 150 ? 0.2836 0.2978 0.2686 0.0221  0.0084  -0.0023 150 PHE A CE2 
1158 C CZ  . PHE A 150 ? 0.3194 0.3308 0.3052 0.0247  0.0101  0.0008  150 PHE A CZ  
1159 N N   . ASN A 151 ? 0.1998 0.2323 0.1982 0.0167  0.0045  -0.0049 151 ASN A N   
1160 C CA  . ASN A 151 ? 0.2045 0.2433 0.2020 0.0176  0.0027  -0.0061 151 ASN A CA  
1161 C C   . ASN A 151 ? 0.2628 0.3011 0.2575 0.0138  0.0020  -0.0093 151 ASN A C   
1162 O O   . ASN A 151 ? 0.2572 0.2910 0.2514 0.0103  0.0032  -0.0105 151 ASN A O   
1163 C CB  . ASN A 151 ? 0.2257 0.2728 0.2268 0.0186  0.0018  -0.0058 151 ASN A CB  
1164 C CG  . ASN A 151 ? 0.2818 0.3283 0.2832 0.0230  0.0028  -0.0028 151 ASN A CG  
1165 O OD1 . ASN A 151 ? 0.3148 0.3619 0.3139 0.0267  0.0027  -0.0017 151 ASN A OD1 
1166 N ND2 . ASN A 151 ? 0.2245 0.2683 0.2279 0.0227  0.0040  -0.0015 151 ASN A ND2 
1167 N N   . ILE A 152 ? 0.2148 0.2568 0.2068 0.0143  0.0004  -0.0107 152 ILE A N   
1168 C CA  . ILE A 152 ? 0.2791 0.3201 0.2673 0.0099  -0.0003 -0.0143 152 ILE A CA  
1169 C C   . ILE A 152 ? 0.3347 0.3872 0.3246 0.0086  -0.0033 -0.0164 152 ILE A C   
1170 O O   . ILE A 152 ? 0.3187 0.3777 0.3089 0.0129  -0.0048 -0.0151 152 ILE A O   
1171 C CB  . ILE A 152 ? 0.2868 0.3195 0.2680 0.0112  0.0006  -0.0145 152 ILE A CB  
1172 C CG1 . ILE A 152 ? 0.3156 0.3389 0.2960 0.0132  0.0035  -0.0118 152 ILE A CG1 
1173 C CG2 . ILE A 152 ? 0.3694 0.3992 0.3455 0.0058  0.0003  -0.0185 152 ILE A CG2 
1174 C CD1 . ILE A 152 ? 0.3495 0.3643 0.3228 0.0144  0.0051  -0.0119 152 ILE A CD1 
1175 N N   . ASP A 153 ? 0.3505 0.4061 0.3414 0.0026  -0.0039 -0.0196 153 ASP A N   
1176 C CA  . ASP A 153 ? 0.4312 0.5000 0.4247 0.0004  -0.0069 -0.0218 153 ASP A CA  
1177 C C   . ASP A 153 ? 0.4677 0.5343 0.4572 -0.0070 -0.0073 -0.0264 153 ASP A C   
1178 O O   . ASP A 153 ? 0.4733 0.5340 0.4629 -0.0119 -0.0051 -0.0279 153 ASP A O   
1179 C CB  . ASP A 153 ? 0.5472 0.6253 0.5485 0.0005  -0.0069 -0.0205 153 ASP A CB  
1180 C CG  . ASP A 153 ? 0.7727 0.8648 0.7777 -0.0037 -0.0095 -0.0232 153 ASP A CG  
1181 O OD1 . ASP A 153 ? 0.7264 0.8288 0.7313 -0.0010 -0.0124 -0.0233 153 ASP A OD1 
1182 O OD2 . ASP A 153 ? 0.8537 0.9471 0.8618 -0.0095 -0.0086 -0.0251 153 ASP A OD2 
1183 N N   . TYR A 154 ? 0.5368 0.6065 0.5215 -0.0077 -0.0098 -0.0288 154 TYR A N   
1184 C CA  . TYR A 154 ? 0.6049 0.6710 0.5838 -0.0151 -0.0102 -0.0336 154 TYR A CA  
1185 C C   . TYR A 154 ? 0.5136 0.5630 0.4873 -0.0183 -0.0059 -0.0342 154 TYR A C   
1186 O O   . TYR A 154 ? 0.5459 0.5927 0.5196 -0.0249 -0.0043 -0.0368 154 TYR A O   
1187 C CB  . TYR A 154 ? 0.7149 0.7948 0.6992 -0.0218 -0.0125 -0.0368 154 TYR A CB  
1188 C CG  . TYR A 154 ? 0.9201 1.0182 0.9085 -0.0194 -0.0170 -0.0368 154 TYR A CG  
1189 C CD1 . TYR A 154 ? 0.9797 1.0796 0.9625 -0.0154 -0.0196 -0.0370 154 TYR A CD1 
1190 C CD2 . TYR A 154 ? 1.0038 1.1178 1.0013 -0.0210 -0.0185 -0.0367 154 TYR A CD2 
1191 C CE1 . TYR A 154 ? 1.0142 1.1315 1.0002 -0.0126 -0.0236 -0.0368 154 TYR A CE1 
1192 C CE2 . TYR A 154 ? 1.0694 1.2013 1.0705 -0.0183 -0.0225 -0.0363 154 TYR A CE2 
1193 C CZ  . TYR A 154 ? 1.0971 1.2306 1.0923 -0.0139 -0.0251 -0.0364 154 TYR A CZ  
1194 O OH  . TYR A 154 ? 1.1884 1.3403 1.1868 -0.0104 -0.0291 -0.0358 154 TYR A OH  
1195 N N   . ASP A 155 ? 0.4702 0.5081 0.4389 -0.0132 -0.0037 -0.0316 155 ASP A N   
1196 C CA  . ASP A 155 ? 0.5541 0.5761 0.5165 -0.0144 0.0005  -0.0316 155 ASP A CA  
1197 C C   . ASP A 155 ? 0.3952 0.4139 0.3623 -0.0151 0.0033  -0.0298 155 ASP A C   
1198 O O   . ASP A 155 ? 0.4408 0.4468 0.4027 -0.0157 0.0071  -0.0295 155 ASP A O   
1199 C CB  . ASP A 155 ? 0.5798 0.5943 0.5333 -0.0215 0.0014  -0.0364 155 ASP A CB  
1200 C CG  . ASP A 155 ? 0.7089 0.7176 0.6531 -0.0195 0.0007  -0.0374 155 ASP A CG  
1201 O OD1 . ASP A 155 ? 0.7235 0.7350 0.6688 -0.0126 -0.0005 -0.0343 155 ASP A OD1 
1202 O OD2 . ASP A 155 ? 0.8284 0.8292 0.7635 -0.0250 0.0016  -0.0414 155 ASP A OD2 
1203 N N   . CYS A 156 ? 0.3267 0.3561 0.3028 -0.0147 0.0019  -0.0286 156 CYS A N   
1204 C CA  . CYS A 156 ? 0.2876 0.3140 0.2680 -0.0144 0.0044  -0.0265 156 CYS A CA  
1205 C C   . CYS A 156 ? 0.3030 0.3297 0.2869 -0.0073 0.0045  -0.0220 156 CYS A C   
1206 O O   . CYS A 156 ? 0.2799 0.3159 0.2682 -0.0039 0.0020  -0.0204 156 CYS A O   
1207 C CB  . CYS A 156 ? 0.2846 0.3217 0.2722 -0.0183 0.0033  -0.0277 156 CYS A CB  
1208 S SG  . CYS A 156 ? 0.3566 0.3885 0.3480 -0.0179 0.0068  -0.0254 156 CYS A SG  
1209 N N   . VAL A 157 ? 0.2930 0.3097 0.2745 -0.0052 0.0074  -0.0198 157 VAL A N   
1210 C CA  . VAL A 157 ? 0.2378 0.2546 0.2226 0.0004  0.0076  -0.0158 157 VAL A CA  
1211 C C   . VAL A 157 ? 0.2732 0.2934 0.2637 -0.0001 0.0079  -0.0147 157 VAL A C   
1212 O O   . VAL A 157 ? 0.2629 0.2776 0.2523 -0.0025 0.0102  -0.0151 157 VAL A O   
1213 C CB  . VAL A 157 ? 0.2491 0.2553 0.2288 0.0031  0.0103  -0.0138 157 VAL A CB  
1214 C CG1 . VAL A 157 ? 0.2485 0.2562 0.2322 0.0079  0.0102  -0.0099 157 VAL A CG1 
1215 C CG2 . VAL A 157 ? 0.3026 0.3036 0.2752 0.0035  0.0107  -0.0150 157 VAL A CG2 
1216 N N   . SER A 158 ? 0.2348 0.2631 0.2305 0.0024  0.0061  -0.0131 158 SER A N   
1217 C CA  . SER A 158 ? 0.2277 0.2579 0.2279 0.0029  0.0067  -0.0115 158 SER A CA  
1218 C C   . SER A 158 ? 0.2452 0.2709 0.2452 0.0068  0.0074  -0.0084 158 SER A C   
1219 O O   . SER A 158 ? 0.2093 0.2376 0.2103 0.0101  0.0064  -0.0067 158 SER A O   
1220 C CB  . SER A 158 ? 0.2363 0.2770 0.2413 0.0035  0.0049  -0.0115 158 SER A CB  
1221 O OG  . SER A 158 ? 0.3058 0.3526 0.3118 -0.0008 0.0040  -0.0144 158 SER A OG  
1222 N N   . PHE A 159 ? 0.2166 0.2356 0.2151 0.0064  0.0093  -0.0076 159 PHE A N   
1223 C CA  . PHE A 159 ? 0.2035 0.2197 0.2024 0.0095  0.0098  -0.0048 159 PHE A CA  
1224 C C   . PHE A 159 ? 0.2019 0.2214 0.2043 0.0101  0.0092  -0.0037 159 PHE A C   
1225 O O   . PHE A 159 ? 0.2192 0.2392 0.2228 0.0082  0.0098  -0.0045 159 PHE A O   
1226 C CB  . PHE A 159 ? 0.2374 0.2464 0.2331 0.0094  0.0119  -0.0041 159 PHE A CB  
1227 C CG  . PHE A 159 ? 0.2103 0.2143 0.2011 0.0097  0.0132  -0.0046 159 PHE A CG  
1228 C CD1 . PHE A 159 ? 0.2339 0.2374 0.2239 0.0130  0.0131  -0.0026 159 PHE A CD1 
1229 C CD2 . PHE A 159 ? 0.2294 0.2283 0.2160 0.0067  0.0150  -0.0070 159 PHE A CD2 
1230 C CE1 . PHE A 159 ? 0.2201 0.2181 0.2047 0.0139  0.0148  -0.0027 159 PHE A CE1 
1231 C CE2 . PHE A 159 ? 0.2327 0.2251 0.2131 0.0072  0.0168  -0.0074 159 PHE A CE2 
1232 C CZ  . PHE A 159 ? 0.2527 0.2447 0.2322 0.0112  0.0167  -0.0051 159 PHE A CZ  
1233 N N   . CYS A 160 ? 0.1935 0.2143 0.1970 0.0126  0.0084  -0.0018 160 CYS A N   
1234 C CA  . CYS A 160 ? 0.2108 0.2330 0.2161 0.0132  0.0083  -0.0008 160 CYS A CA  
1235 C C   . CYS A 160 ? 0.2293 0.2482 0.2341 0.0142  0.0085  0.0011  160 CYS A C   
1236 O O   . CYS A 160 ? 0.2203 0.2387 0.2253 0.0142  0.0086  0.0017  160 CYS A O   
1237 C CB  . CYS A 160 ? 0.1956 0.2228 0.2020 0.0149  0.0076  -0.0006 160 CYS A CB  
1238 S SG  . CYS A 160 ? 0.2414 0.2685 0.2462 0.0178  0.0072  0.0006  160 CYS A SG  
1239 N N   . TYR A 161 ? 0.1933 0.2104 0.1973 0.0148  0.0085  0.0022  161 TYR A N   
1240 C CA  . TYR A 161 ? 0.1795 0.1957 0.1838 0.0152  0.0083  0.0039  161 TYR A CA  
1241 C C   . TYR A 161 ? 0.2046 0.2198 0.2084 0.0156  0.0087  0.0049  161 TYR A C   
1242 O O   . TYR A 161 ? 0.2104 0.2252 0.2133 0.0165  0.0093  0.0048  161 TYR A O   
1243 C CB  . TYR A 161 ? 0.1978 0.2150 0.2023 0.0163  0.0083  0.0048  161 TYR A CB  
1244 C CG  . TYR A 161 ? 0.1830 0.1994 0.1878 0.0155  0.0082  0.0063  161 TYR A CG  
1245 C CD1 . TYR A 161 ? 0.1641 0.1786 0.1679 0.0143  0.0081  0.0063  161 TYR A CD1 
1246 C CD2 . TYR A 161 ? 0.1960 0.2137 0.2019 0.0159  0.0084  0.0076  161 TYR A CD2 
1247 C CE1 . TYR A 161 ? 0.1682 0.1820 0.1718 0.0125  0.0079  0.0071  161 TYR A CE1 
1248 C CE2 . TYR A 161 ? 0.1944 0.2129 0.2013 0.0144  0.0082  0.0088  161 TYR A CE2 
1249 C CZ  . TYR A 161 ? 0.1814 0.1980 0.1871 0.0123  0.0078  0.0083  161 TYR A CZ  
1250 O OH  . TYR A 161 ? 0.2362 0.2534 0.2423 0.0099  0.0075  0.0090  161 TYR A OH  
1251 N N   . MET A 162 ? 0.1829 0.1978 0.1868 0.0152  0.0084  0.0059  162 MET A N   
1252 C CA  . MET A 162 ? 0.1738 0.1899 0.1779 0.0164  0.0086  0.0077  162 MET A CA  
1253 C C   . MET A 162 ? 0.1918 0.2108 0.1977 0.0154  0.0074  0.0089  162 MET A C   
1254 O O   . MET A 162 ? 0.1815 0.1997 0.1868 0.0137  0.0065  0.0083  162 MET A O   
1255 C CB  . MET A 162 ? 0.2505 0.2642 0.2523 0.0174  0.0097  0.0079  162 MET A CB  
1256 C CG  . MET A 162 ? 0.1792 0.1953 0.1811 0.0193  0.0097  0.0103  162 MET A CG  
1257 S SD  . MET A 162 ? 0.2866 0.2981 0.2840 0.0217  0.0120  0.0109  162 MET A SD  
1258 C CE  . MET A 162 ? 0.3129 0.3201 0.3073 0.0232  0.0145  0.0106  162 MET A CE  
1259 N N   . HIS A 163 ? 0.1794 0.2017 0.1872 0.0160  0.0075  0.0105  163 HIS A N   
1260 C CA  . HIS A 163 ? 0.1813 0.2067 0.1911 0.0140  0.0065  0.0114  163 HIS A CA  
1261 C C   . HIS A 163 ? 0.1820 0.2111 0.1925 0.0133  0.0052  0.0123  163 HIS A C   
1262 O O   . HIS A 163 ? 0.1998 0.2314 0.2105 0.0157  0.0055  0.0138  163 HIS A O   
1263 C CB  . HIS A 163 ? 0.2080 0.2363 0.2201 0.0148  0.0074  0.0129  163 HIS A CB  
1264 C CG  . HIS A 163 ? 0.2058 0.2371 0.2201 0.0119  0.0069  0.0136  163 HIS A CG  
1265 N ND1 . HIS A 163 ? 0.1761 0.2040 0.1886 0.0090  0.0067  0.0122  163 HIS A ND1 
1266 C CD2 . HIS A 163 ? 0.2074 0.2448 0.2251 0.0111  0.0069  0.0154  163 HIS A CD2 
1267 C CE1 . HIS A 163 ? 0.1564 0.1872 0.1707 0.0059  0.0065  0.0128  163 HIS A CE1 
1268 N NE2 . HIS A 163 ? 0.2090 0.2465 0.2271 0.0069  0.0064  0.0148  163 HIS A NE2 
1269 N N   . HIS A 164 ? 0.2115 0.2408 0.2216 0.0102  0.0038  0.0116  164 HIS A N   
1270 C CA  . HIS A 164 ? 0.2140 0.2479 0.2246 0.0092  0.0021  0.0124  164 HIS A CA  
1271 C C   . HIS A 164 ? 0.2248 0.2644 0.2381 0.0057  0.0009  0.0130  164 HIS A C   
1272 O O   . HIS A 164 ? 0.2683 0.3159 0.2847 0.0062  -0.0001 0.0148  164 HIS A O   
1273 C CB  . HIS A 164 ? 0.1896 0.2189 0.1962 0.0081  0.0012  0.0108  164 HIS A CB  
1274 C CG  . HIS A 164 ? 0.1991 0.2250 0.2036 0.0113  0.0023  0.0107  164 HIS A CG  
1275 N ND1 . HIS A 164 ? 0.2133 0.2399 0.2157 0.0128  0.0018  0.0113  164 HIS A ND1 
1276 C CD2 . HIS A 164 ? 0.1891 0.2108 0.1929 0.0129  0.0041  0.0099  164 HIS A CD2 
1277 C CE1 . HIS A 164 ? 0.2021 0.2239 0.2024 0.0151  0.0037  0.0109  164 HIS A CE1 
1278 N NE2 . HIS A 164 ? 0.2039 0.2230 0.2051 0.0148  0.0050  0.0099  164 HIS A NE2 
1279 N N   . MET A 165 ? 0.2051 0.2408 0.2172 0.0023  0.0012  0.0116  165 MET A N   
1280 C CA  . MET A 165 ? 0.2226 0.2629 0.2365 -0.0023 0.0001  0.0117  165 MET A CA  
1281 C C   . MET A 165 ? 0.2367 0.2718 0.2494 -0.0052 0.0020  0.0108  165 MET A C   
1282 O O   . MET A 165 ? 0.2214 0.2488 0.2308 -0.0036 0.0039  0.0099  165 MET A O   
1283 C CB  . MET A 165 ? 0.3070 0.3476 0.3180 -0.0055 -0.0023 0.0103  165 MET A CB  
1284 C CG  . MET A 165 ? 0.2743 0.3053 0.2794 -0.0052 -0.0018 0.0085  165 MET A CG  
1285 S SD  . MET A 165 ? 0.3359 0.3669 0.3366 -0.0074 -0.0046 0.0072  165 MET A SD  
1286 C CE  . MET A 165 ? 0.3470 0.3646 0.3405 -0.0090 -0.0025 0.0050  165 MET A CE  
1287 N N   . GLU A 166 ? 0.2267 0.2665 0.2418 -0.0096 0.0017  0.0111  166 GLU A N   
1288 C CA  . GLU A 166 ? 0.2472 0.2811 0.2601 -0.0132 0.0040  0.0102  166 GLU A CA  
1289 C C   . GLU A 166 ? 0.3208 0.3509 0.3292 -0.0192 0.0030  0.0080  166 GLU A C   
1290 O O   . GLU A 166 ? 0.3172 0.3547 0.3275 -0.0224 0.0002  0.0078  166 GLU A O   
1291 C CB  . GLU A 166 ? 0.2694 0.3100 0.2879 -0.0144 0.0053  0.0120  166 GLU A CB  
1292 C CG  . GLU A 166 ? 0.2956 0.3294 0.3112 -0.0188 0.0082  0.0111  166 GLU A CG  
1293 C CD  . GLU A 166 ? 0.2952 0.3336 0.3157 -0.0185 0.0105  0.0132  166 GLU A CD  
1294 O OE1 . GLU A 166 ? 0.2787 0.3189 0.3015 -0.0128 0.0114  0.0150  166 GLU A OE1 
1295 O OE2 . GLU A 166 ? 0.3265 0.3672 0.3485 -0.0244 0.0115  0.0130  166 GLU A OE2 
1296 N N   . LEU A 167 ? 0.2739 0.2924 0.2757 -0.0202 0.0055  0.0065  167 LEU A N   
1297 C CA  . LEU A 167 ? 0.3237 0.3356 0.3192 -0.0260 0.0054  0.0043  167 LEU A CA  
1298 C C   . LEU A 167 ? 0.3333 0.3451 0.3291 -0.0324 0.0071  0.0038  167 LEU A C   
1299 O O   . LEU A 167 ? 0.3367 0.3523 0.3373 -0.0317 0.0089  0.0054  167 LEU A O   
1300 C CB  . LEU A 167 ? 0.3011 0.2997 0.2883 -0.0236 0.0079  0.0033  167 LEU A CB  
1301 C CG  . LEU A 167 ? 0.3467 0.3460 0.3345 -0.0175 0.0067  0.0038  167 LEU A CG  
1302 C CD1 . LEU A 167 ? 0.3905 0.3790 0.3719 -0.0141 0.0097  0.0035  167 LEU A CD1 
1303 C CD2 . LEU A 167 ? 0.3876 0.3910 0.3751 -0.0189 0.0033  0.0030  167 LEU A CD2 
1304 N N   . PRO A 168 ? 0.3550 0.3621 0.3453 -0.0392 0.0068  0.0015  168 PRO A N   
1305 C CA  . PRO A 168 ? 0.3254 0.3330 0.3162 -0.0467 0.0083  0.0007  168 PRO A CA  
1306 C C   . PRO A 168 ? 0.3753 0.3731 0.3630 -0.0458 0.0138  0.0014  168 PRO A C   
1307 O O   . PRO A 168 ? 0.4133 0.4147 0.4046 -0.0500 0.0155  0.0019  168 PRO A O   
1308 C CB  . PRO A 168 ? 0.3337 0.3345 0.3163 -0.0538 0.0073  -0.0024 168 PRO A CB  
1309 C CG  . PRO A 168 ? 0.3777 0.3831 0.3605 -0.0504 0.0031  -0.0026 168 PRO A CG  
1310 C CD  . PRO A 168 ? 0.4157 0.4194 0.4003 -0.0410 0.0042  -0.0005 168 PRO A CD  
1311 N N   . THR A 169 ? 0.3773 0.3632 0.3585 -0.0402 0.0167  0.0017  169 THR A N   
1312 C CA  . THR A 169 ? 0.3701 0.3468 0.3477 -0.0379 0.0220  0.0028  169 THR A CA  
1313 C C   . THR A 169 ? 0.3671 0.3521 0.3526 -0.0321 0.0222  0.0055  169 THR A C   
1314 O O   . THR A 169 ? 0.4081 0.3867 0.3911 -0.0292 0.0263  0.0066  169 THR A O   
1315 C CB  . THR A 169 ? 0.4222 0.3846 0.3897 -0.0334 0.0251  0.0024  169 THR A CB  
1316 O OG1 . THR A 169 ? 0.4139 0.3807 0.3838 -0.0270 0.0222  0.0031  169 THR A OG1 
1317 C CG2 . THR A 169 ? 0.4454 0.3959 0.4026 -0.0395 0.0265  -0.0001 169 THR A CG2 
1318 N N   . GLY A 170 ? 0.3230 0.3211 0.3169 -0.0299 0.0182  0.0065  170 GLY A N   
1319 C CA  . GLY A 170 ? 0.3156 0.3205 0.3159 -0.0245 0.0186  0.0089  170 GLY A CA  
1320 C C   . GLY A 170 ? 0.3333 0.3350 0.3319 -0.0167 0.0188  0.0097  170 GLY A C   
1321 O O   . GLY A 170 ? 0.3535 0.3584 0.3554 -0.0121 0.0196  0.0114  170 GLY A O   
1322 N N   . VAL A 171 ? 0.3254 0.3210 0.3187 -0.0151 0.0181  0.0084  171 VAL A N   
1323 C CA  . VAL A 171 ? 0.2692 0.2641 0.2621 -0.0083 0.0177  0.0089  171 VAL A CA  
1324 C C   . VAL A 171 ? 0.2685 0.2712 0.2657 -0.0075 0.0137  0.0087  171 VAL A C   
1325 O O   . VAL A 171 ? 0.2731 0.2811 0.2727 -0.0114 0.0113  0.0082  171 VAL A O   
1326 C CB  . VAL A 171 ? 0.2616 0.2457 0.2463 -0.0062 0.0201  0.0082  171 VAL A CB  
1327 C CG1 . VAL A 171 ? 0.3481 0.3231 0.3271 -0.0070 0.0247  0.0087  171 VAL A CG1 
1328 C CG2 . VAL A 171 ? 0.2878 0.2683 0.2686 -0.0097 0.0187  0.0065  171 VAL A CG2 
1329 N N   . HIS A 172 ? 0.2343 0.2377 0.2319 -0.0025 0.0130  0.0089  172 HIS A N   
1330 C CA  . HIS A 172 ? 0.2090 0.2195 0.2109 -0.0008 0.0102  0.0091  172 HIS A CA  
1331 C C   . HIS A 172 ? 0.2156 0.2231 0.2147 0.0010  0.0093  0.0081  172 HIS A C   
1332 O O   . HIS A 172 ? 0.2033 0.2052 0.1987 0.0031  0.0109  0.0077  172 HIS A O   
1333 C CB  . HIS A 172 ? 0.2086 0.2234 0.2143 0.0031  0.0107  0.0105  172 HIS A CB  
1334 C CG  . HIS A 172 ? 0.2245 0.2426 0.2332 0.0016  0.0119  0.0119  172 HIS A CG  
1335 N ND1 . HIS A 172 ? 0.2371 0.2515 0.2443 0.0028  0.0147  0.0127  172 HIS A ND1 
1336 C CD2 . HIS A 172 ? 0.2172 0.2423 0.2302 -0.0012 0.0108  0.0129  172 HIS A CD2 
1337 C CE1 . HIS A 172 ? 0.2448 0.2635 0.2556 0.0007  0.0155  0.0140  172 HIS A CE1 
1338 N NE2 . HIS A 172 ? 0.2525 0.2784 0.2673 -0.0019 0.0131  0.0141  172 HIS A NE2 
1339 N N   . ALA A 173 ? 0.1966 0.2082 0.1975 0.0004  0.0070  0.0079  173 ALA A N   
1340 C CA  . ALA A 173 ? 0.1872 0.1963 0.1857 0.0019  0.0063  0.0070  173 ALA A CA  
1341 C C   . ALA A 173 ? 0.1632 0.1772 0.1649 0.0044  0.0051  0.0075  173 ALA A C   
1342 O O   . ALA A 173 ? 0.1984 0.2182 0.2034 0.0045  0.0041  0.0086  173 ALA A O   
1343 C CB  . ALA A 173 ? 0.1967 0.2032 0.1916 -0.0016 0.0050  0.0060  173 ALA A CB  
1344 N N   . GLY A 174 ? 0.1756 0.1873 0.1761 0.0067  0.0056  0.0069  174 GLY A N   
1345 C CA  . GLY A 174 ? 0.2013 0.2156 0.2035 0.0087  0.0052  0.0072  174 GLY A CA  
1346 C C   . GLY A 174 ? 0.1900 0.2010 0.1903 0.0098  0.0058  0.0062  174 GLY A C   
1347 O O   . GLY A 174 ? 0.2008 0.2081 0.1985 0.0092  0.0064  0.0055  174 GLY A O   
1348 N N   . THR A 175 ? 0.1817 0.1936 0.1829 0.0113  0.0062  0.0061  175 THR A N   
1349 C CA  . THR A 175 ? 0.1839 0.1932 0.1837 0.0118  0.0072  0.0052  175 THR A CA  
1350 C C   . THR A 175 ? 0.2021 0.2122 0.2033 0.0125  0.0082  0.0043  175 THR A C   
1351 O O   . THR A 175 ? 0.2108 0.2229 0.2133 0.0131  0.0081  0.0045  175 THR A O   
1352 C CB  . THR A 175 ? 0.1773 0.1858 0.1757 0.0124  0.0072  0.0056  175 THR A CB  
1353 O OG1 . THR A 175 ? 0.1986 0.2086 0.1979 0.0138  0.0078  0.0063  175 THR A OG1 
1354 C CG2 . THR A 175 ? 0.2007 0.2101 0.1977 0.0116  0.0056  0.0064  175 THR A CG2 
1355 N N   . ASP A 176 ? 0.1853 0.1942 0.1861 0.0123  0.0092  0.0033  176 ASP A N   
1356 C CA  . ASP A 176 ? 0.2158 0.2260 0.2178 0.0121  0.0100  0.0022  176 ASP A CA  
1357 C C   . ASP A 176 ? 0.2360 0.2437 0.2364 0.0121  0.0110  0.0022  176 ASP A C   
1358 O O   . ASP A 176 ? 0.2224 0.2286 0.2213 0.0130  0.0108  0.0034  176 ASP A O   
1359 C CB  . ASP A 176 ? 0.1987 0.2098 0.2015 0.0114  0.0110  0.0012  176 ASP A CB  
1360 C CG  . ASP A 176 ? 0.2426 0.2502 0.2437 0.0111  0.0122  0.0013  176 ASP A CG  
1361 O OD1 . ASP A 176 ? 0.2168 0.2211 0.2158 0.0112  0.0126  0.0017  176 ASP A OD1 
1362 O OD2 . ASP A 176 ? 0.2711 0.2795 0.2728 0.0111  0.0130  0.0012  176 ASP A OD2 
1363 N N   . LEU A 177 ? 0.2027 0.2097 0.2028 0.0113  0.0121  0.0009  177 LEU A N   
1364 C CA  . LEU A 177 ? 0.1985 0.2013 0.1956 0.0117  0.0138  0.0011  177 LEU A CA  
1365 C C   . LEU A 177 ? 0.2193 0.2179 0.2141 0.0113  0.0157  0.0010  177 LEU A C   
1366 O O   . LEU A 177 ? 0.2520 0.2457 0.2431 0.0121  0.0178  0.0013  177 LEU A O   
1367 C CB  . LEU A 177 ? 0.2268 0.2288 0.2229 0.0104  0.0147  -0.0005 177 LEU A CB  
1368 C CG  . LEU A 177 ? 0.2303 0.2332 0.2260 0.0122  0.0140  0.0004  177 LEU A CG  
1369 C CD1 . LEU A 177 ? 0.2343 0.2342 0.2274 0.0148  0.0151  0.0026  177 LEU A CD1 
1370 C CD2 . LEU A 177 ? 0.2410 0.2493 0.2402 0.0130  0.0116  0.0012  177 LEU A CD2 
1371 N N   . GLU A 178 ? 0.2207 0.2201 0.2168 0.0104  0.0156  0.0006  178 GLU A N   
1372 C CA  . GLU A 178 ? 0.2615 0.2567 0.2551 0.0107  0.0173  0.0009  178 GLU A CA  
1373 C C   . GLU A 178 ? 0.2725 0.2672 0.2643 0.0129  0.0160  0.0028  178 GLU A C   
1374 O O   . GLU A 178 ? 0.2485 0.2395 0.2374 0.0137  0.0171  0.0033  178 GLU A O   
1375 C CB  . GLU A 178 ? 0.2554 0.2519 0.2509 0.0091  0.0180  0.0000  178 GLU A CB  
1376 C CG  . GLU A 178 ? 0.3363 0.3359 0.3346 0.0063  0.0190  -0.0020 178 GLU A CG  
1377 C CD  . GLU A 178 ? 0.3698 0.3653 0.3659 0.0041  0.0214  -0.0034 178 GLU A CD  
1378 O OE1 . GLU A 178 ? 0.4033 0.3921 0.3949 0.0053  0.0235  -0.0026 178 GLU A OE1 
1379 O OE2 . GLU A 178 ? 0.3906 0.3894 0.3887 0.0012  0.0215  -0.0053 178 GLU A OE2 
1380 N N   . GLY A 179 ? 0.2343 0.2326 0.2276 0.0136  0.0136  0.0037  179 GLY A N   
1381 C CA  . GLY A 179 ? 0.2535 0.2527 0.2455 0.0148  0.0119  0.0051  179 GLY A CA  
1382 C C   . GLY A 179 ? 0.2435 0.2428 0.2353 0.0137  0.0105  0.0049  179 GLY A C   
1383 O O   . GLY A 179 ? 0.2354 0.2348 0.2252 0.0140  0.0090  0.0056  179 GLY A O   
1384 N N   . ASN A 180 ? 0.2284 0.2277 0.2217 0.0127  0.0111  0.0039  180 ASN A N   
1385 C CA  . ASN A 180 ? 0.1817 0.1793 0.1734 0.0123  0.0107  0.0038  180 ASN A CA  
1386 C C   . ASN A 180 ? 0.2012 0.2010 0.1941 0.0116  0.0093  0.0040  180 ASN A C   
1387 O O   . ASN A 180 ? 0.2035 0.2061 0.1992 0.0118  0.0095  0.0037  180 ASN A O   
1388 C CB  . ASN A 180 ? 0.2006 0.1972 0.1928 0.0123  0.0128  0.0032  180 ASN A CB  
1389 C CG  . ASN A 180 ? 0.2373 0.2311 0.2283 0.0125  0.0148  0.0030  180 ASN A CG  
1390 O OD1 . ASN A 180 ? 0.2824 0.2776 0.2757 0.0116  0.0163  0.0022  180 ASN A OD1 
1391 N ND2 . ASN A 180 ? 0.2230 0.2128 0.2100 0.0134  0.0150  0.0036  180 ASN A ND2 
1392 N N   . PHE A 181 ? 0.2186 0.2326 0.1982 0.0291  -0.0188 0.0147  181 PHE A N   
1393 C CA  . PHE A 181 ? 0.2175 0.2221 0.1988 0.0287  -0.0238 0.0135  181 PHE A CA  
1394 C C   . PHE A 181 ? 0.2166 0.2227 0.1945 0.0340  -0.0220 0.0105  181 PHE A C   
1395 O O   . PHE A 181 ? 0.2027 0.2120 0.1721 0.0398  -0.0196 0.0080  181 PHE A O   
1396 C CB  . PHE A 181 ? 0.2076 0.1986 0.1810 0.0298  -0.0319 0.0115  181 PHE A CB  
1397 C CG  . PHE A 181 ? 0.2156 0.2010 0.1972 0.0232  -0.0362 0.0147  181 PHE A CG  
1398 C CD1 . PHE A 181 ? 0.2409 0.2202 0.2302 0.0202  -0.0390 0.0155  181 PHE A CD1 
1399 C CD2 . PHE A 181 ? 0.2118 0.1989 0.1947 0.0199  -0.0367 0.0175  181 PHE A CD2 
1400 C CE1 . PHE A 181 ? 0.2231 0.1975 0.2209 0.0142  -0.0426 0.0189  181 PHE A CE1 
1401 C CE2 . PHE A 181 ? 0.2304 0.2130 0.2219 0.0138  -0.0403 0.0209  181 PHE A CE2 
1402 C CZ  . PHE A 181 ? 0.2691 0.2454 0.2684 0.0109  -0.0433 0.0217  181 PHE A CZ  
1403 N N   . TYR A 182 ? 0.1808 0.1848 0.1658 0.0320  -0.0228 0.0111  182 TYR A N   
1404 C CA  . TYR A 182 ? 0.1673 0.1683 0.1479 0.0372  -0.0234 0.0081  182 TYR A CA  
1405 C C   . TYR A 182 ? 0.2106 0.1973 0.1822 0.0402  -0.0303 0.0051  182 TYR A C   
1406 O O   . TYR A 182 ? 0.2448 0.2227 0.2202 0.0362  -0.0353 0.0061  182 TYR A O   
1407 C CB  . TYR A 182 ? 0.1647 0.1677 0.1554 0.0343  -0.0220 0.0098  182 TYR A CB  
1408 C CG  . TYR A 182 ? 0.1863 0.2032 0.1846 0.0320  -0.0152 0.0121  182 TYR A CG  
1409 C CD1 . TYR A 182 ? 0.2159 0.2414 0.2115 0.0368  -0.0110 0.0105  182 TYR A CD1 
1410 C CD2 . TYR A 182 ? 0.1866 0.2081 0.1951 0.0251  -0.0128 0.0159  182 TYR A CD2 
1411 C CE1 . TYR A 182 ? 0.1719 0.2107 0.1748 0.0345  -0.0049 0.0124  182 TYR A CE1 
1412 C CE2 . TYR A 182 ? 0.1547 0.1888 0.1699 0.0228  -0.0064 0.0177  182 TYR A CE2 
1413 C CZ  . TYR A 182 ? 0.1635 0.2061 0.1757 0.0274  -0.0028 0.0158  182 TYR A CZ  
1414 O OH  . TYR A 182 ? 0.1777 0.2327 0.1966 0.0249  0.0031  0.0174  182 TYR A OH  
1415 N N   . GLY A 183 ? 0.2272 0.2113 0.1872 0.0471  -0.0305 0.0015  183 GLY A N   
1416 C CA  . GLY A 183 ? 0.2475 0.2175 0.1976 0.0503  -0.0368 -0.0019 183 GLY A CA  
1417 C C   . GLY A 183 ? 0.2591 0.2226 0.2017 0.0494  -0.0410 -0.0026 183 GLY A C   
1418 O O   . GLY A 183 ? 0.2509 0.2207 0.1961 0.0463  -0.0393 -0.0002 183 GLY A O   
1419 N N   . PRO A 184 ? 0.2833 0.2338 0.2163 0.0522  -0.0469 -0.0060 184 PRO A N   
1420 C CA  . PRO A 184 ? 0.2887 0.2320 0.2118 0.0525  -0.0514 -0.0075 184 PRO A CA  
1421 C C   . PRO A 184 ? 0.3391 0.2764 0.2689 0.0457  -0.0574 -0.0052 184 PRO A C   
1422 O O   . PRO A 184 ? 0.3975 0.3223 0.3217 0.0454  -0.0644 -0.0075 184 PRO A O   
1423 C CB  . PRO A 184 ? 0.3372 0.2687 0.2468 0.0588  -0.0546 -0.0124 184 PRO A CB  
1424 C CG  . PRO A 184 ? 0.3390 0.2668 0.2553 0.0584  -0.0554 -0.0127 184 PRO A CG  
1425 C CD  . PRO A 184 ? 0.3273 0.2687 0.2571 0.0556  -0.0493 -0.0088 184 PRO A CD  
1426 N N   . PHE A 185 ? 0.2966 0.2428 0.2387 0.0400  -0.0546 -0.0007 185 PHE A N   
1427 C CA  . PHE A 185 ? 0.3023 0.2445 0.2532 0.0332  -0.0593 0.0023  185 PHE A CA  
1428 C C   . PHE A 185 ? 0.2885 0.2378 0.2409 0.0303  -0.0577 0.0054  185 PHE A C   
1429 O O   . PHE A 185 ? 0.3023 0.2621 0.2535 0.0322  -0.0513 0.0062  185 PHE A O   
1430 C CB  . PHE A 185 ? 0.2779 0.2230 0.2434 0.0288  -0.0573 0.0054  185 PHE A CB  
1431 C CG  . PHE A 185 ? 0.2779 0.2169 0.2421 0.0321  -0.0582 0.0026  185 PHE A CG  
1432 C CD1 . PHE A 185 ? 0.3169 0.2421 0.2752 0.0334  -0.0651 -0.0004 185 PHE A CD1 
1433 C CD2 . PHE A 185 ? 0.2750 0.2218 0.2430 0.0342  -0.0522 0.0029  185 PHE A CD2 
1434 C CE1 . PHE A 185 ? 0.3201 0.2393 0.2768 0.0368  -0.0655 -0.0030 185 PHE A CE1 
1435 C CE2 . PHE A 185 ? 0.3050 0.2462 0.2713 0.0377  -0.0529 0.0005  185 PHE A CE2 
1436 C CZ  . PHE A 185 ? 0.3062 0.2336 0.2669 0.0391  -0.0593 -0.0024 185 PHE A CZ  
1437 N N   . VAL A 186 ? 0.3104 0.2540 0.2658 0.0257  -0.0634 0.0074  186 VAL A N   
1438 C CA  . VAL A 186 ? 0.2756 0.2249 0.2330 0.0226  -0.0626 0.0107  186 VAL A CA  
1439 C C   . VAL A 186 ? 0.2784 0.2273 0.2502 0.0152  -0.0648 0.0155  186 VAL A C   
1440 O O   . VAL A 186 ? 0.3154 0.2557 0.2917 0.0129  -0.0699 0.0153  186 VAL A O   
1441 C CB  . VAL A 186 ? 0.3223 0.2646 0.2658 0.0254  -0.0681 0.0082  186 VAL A CB  
1442 C CG1 . VAL A 186 ? 0.3490 0.2926 0.2785 0.0329  -0.0646 0.0040  186 VAL A CG1 
1443 C CG2 . VAL A 186 ? 0.3792 0.3074 0.3196 0.0241  -0.0775 0.0059  186 VAL A CG2 
1444 N N   . ASP A 187 ? 0.2628 0.2206 0.2417 0.0115  -0.0606 0.0200  187 ASP A N   
1445 C CA  . ASP A 187 ? 0.2921 0.2510 0.2855 0.0045  -0.0612 0.0253  187 ASP A CA  
1446 C C   . ASP A 187 ? 0.3342 0.2862 0.3262 0.0019  -0.0688 0.0267  187 ASP A C   
1447 O O   . ASP A 187 ? 0.3448 0.3018 0.3401 -0.0009 -0.0678 0.0305  187 ASP A O   
1448 C CB  . ASP A 187 ? 0.2663 0.2379 0.2687 0.0018  -0.0524 0.0295  187 ASP A CB  
1449 C CG  . ASP A 187 ? 0.3151 0.2944 0.3104 0.0042  -0.0485 0.0297  187 ASP A CG  
1450 O OD1 . ASP A 187 ? 0.2998 0.2759 0.2817 0.0092  -0.0512 0.0261  187 ASP A OD1 
1451 O OD2 . ASP A 187 ? 0.2468 0.2359 0.2501 0.0013  -0.0417 0.0335  187 ASP A OD2 
1452 N N   . ARG A 188 ? 0.3423 0.2827 0.3293 0.0029  -0.0766 0.0235  188 ARG A N   
1453 C CA  . ARG A 188 ? 0.4597 0.3917 0.4445 0.0006  -0.0854 0.0238  188 ARG A CA  
1454 C C   . ARG A 188 ? 0.5639 0.4859 0.5553 -0.0020 -0.0911 0.0233  188 ARG A C   
1455 O O   . ARG A 188 ? 0.4837 0.4016 0.4727 0.0009  -0.0904 0.0198  188 ARG A O   
1456 C CB  . ARG A 188 ? 0.4492 0.3755 0.4161 0.0059  -0.0898 0.0189  188 ARG A CB  
1457 C CG  . ARG A 188 ? 0.6238 0.5586 0.5832 0.0086  -0.0851 0.0195  188 ARG A CG  
1458 C CD  . ARG A 188 ? 0.6748 0.6023 0.6168 0.0130  -0.0909 0.0153  188 ARG A CD  
1459 N NE  . ARG A 188 ? 0.7288 0.6489 0.6589 0.0187  -0.0918 0.0092  188 ARG A NE  
1460 N N   . GLN A 189 ? 0.5770 0.4951 0.5769 -0.0074 -0.0967 0.0268  189 GLN A N   
1461 C CA  . GLN A 189 ? 0.6521 0.5601 0.6589 -0.0101 -0.1027 0.0266  189 GLN A CA  
1462 C C   . GLN A 189 ? 0.7135 0.6099 0.7068 -0.0065 -0.1103 0.0204  189 GLN A C   
1463 O O   . GLN A 189 ? 0.6916 0.5805 0.6836 -0.0088 -0.1187 0.0201  189 GLN A O   
1464 C CB  . GLN A 189 ? 0.6912 0.5986 0.7111 -0.0168 -0.1066 0.0324  189 GLN A CB  
1465 C CG  . GLN A 189 ? 0.6698 0.5853 0.7055 -0.0210 -0.0993 0.0385  189 GLN A CG  
1466 C CD  . GLN A 189 ? 0.8479 0.7568 0.8968 -0.0250 -0.1015 0.0408  189 GLN A CD  
1467 O OE1 . GLN A 189 ? 0.8211 0.7223 0.8674 -0.0229 -0.1037 0.0370  189 GLN A OE1 
1468 N NE2 . GLN A 189 ? 0.7562 0.6686 0.8194 -0.0306 -0.1002 0.0471  189 GLN A NE2 
1469 N N   . THR A 190 ? 0.6311 0.5259 0.6144 -0.0008 -0.1075 0.0154  190 THR A N   
1470 C CA  . THR A 190 ? 0.6924 0.5760 0.6618 0.0034  -0.1132 0.0092  190 THR A CA  
1471 C C   . THR A 190 ? 0.7521 0.6307 0.7236 0.0055  -0.1115 0.0066  190 THR A C   
1472 O O   . THR A 190 ? 0.6632 0.5492 0.6422 0.0059  -0.1042 0.0085  190 THR A O   
1473 C CB  . THR A 190 ? 0.6048 0.4909 0.5573 0.0094  -0.1110 0.0054  190 THR A CB  
1474 O OG1 . THR A 190 ? 0.8188 0.7076 0.7680 0.0077  -0.1139 0.0075  190 THR A OG1 
1475 C CG2 . THR A 190 ? 0.7207 0.5949 0.6583 0.0145  -0.1155 -0.0013 190 THR A CG2 
1476 N N   . ALA A 191 ? 0.6727 0.5386 0.6376 0.0069  -0.1182 0.0022  191 ALA A N   
1477 C CA  . ALA A 191 ? 0.8355 0.6950 0.8009 0.0094  -0.1171 -0.0007 191 ALA A CA  
1478 C C   . ALA A 191 ? 0.7763 0.6387 0.7290 0.0167  -0.1115 -0.0048 191 ALA A C   
1479 O O   . ALA A 191 ? 0.8233 0.6791 0.7608 0.0210  -0.1144 -0.0096 191 ALA A O   
1480 C CB  . ALA A 191 ? 0.8470 0.6917 0.8096 0.0083  -0.1259 -0.0040 191 ALA A CB  
1481 N N   . GLN A 192 ? 0.7555 0.6278 0.7142 0.0180  -0.1034 -0.0027 192 GLN A N   
1482 C CA  . GLN A 192 ? 0.5425 0.4193 0.4916 0.0246  -0.0973 -0.0057 192 GLN A CA  
1483 C C   . GLN A 192 ? 0.5564 0.4306 0.5102 0.0265  -0.0947 -0.0066 192 GLN A C   
1484 O O   . GLN A 192 ? 0.6605 0.5362 0.6280 0.0223  -0.0936 -0.0030 192 GLN A O   
1485 C CB  . GLN A 192 ? 0.5240 0.4158 0.4763 0.0246  -0.0898 -0.0024 192 GLN A CB  
1486 C CG  . GLN A 192 ? 0.5444 0.4403 0.4986 0.0207  -0.0916 0.0007  192 GLN A CG  
1487 C CD  . GLN A 192 ? 0.4076 0.3180 0.3668 0.0200  -0.0838 0.0043  192 GLN A CD  
1488 O OE1 . GLN A 192 ? 0.3664 0.2838 0.3211 0.0244  -0.0776 0.0029  192 GLN A OE1 
1489 N NE2 . GLN A 192 ? 0.3997 0.3148 0.3690 0.0142  -0.0840 0.0091  192 GLN A NE2 
1490 N N   . ALA A 193 ? 0.5370 0.4072 0.4796 0.0329  -0.0933 -0.0111 193 ALA A N   
1491 C CA  . ALA A 193 ? 0.4634 0.3303 0.4096 0.0353  -0.0911 -0.0121 193 ALA A CA  
1492 C C   . ALA A 193 ? 0.4311 0.3089 0.3755 0.0401  -0.0828 -0.0120 193 ALA A C   
1493 O O   . ALA A 193 ? 0.4888 0.3713 0.4231 0.0443  -0.0801 -0.0138 193 ALA A O   
1494 C CB  . ALA A 193 ? 0.4951 0.3471 0.4310 0.0387  -0.0963 -0.0173 193 ALA A CB  
1495 N N   . ALA A 194 ? 0.4739 0.3559 0.4287 0.0394  -0.0789 -0.0097 194 ALA A N   
1496 C CA  . ALA A 194 ? 0.5126 0.4039 0.4660 0.0441  -0.0718 -0.0099 194 ALA A CA  
1497 C C   . ALA A 194 ? 0.5658 0.4497 0.5066 0.0514  -0.0721 -0.0147 194 ALA A C   
1498 O O   . ALA A 194 ? 0.5579 0.4290 0.4959 0.0521  -0.0767 -0.0172 194 ALA A O   
1499 C CB  . ALA A 194 ? 0.5400 0.4358 0.5068 0.0415  -0.0684 -0.0064 194 ALA A CB  
1500 N N   . GLY A 195 ? 0.4941 0.3857 0.4273 0.0568  -0.0670 -0.0160 195 GLY A N   
1501 C CA  . GLY A 195 ? 0.4837 0.3696 0.4055 0.0642  -0.0660 -0.0200 195 GLY A CA  
1502 C C   . GLY A 195 ? 0.4812 0.3660 0.4087 0.0664  -0.0637 -0.0196 195 GLY A C   
1503 O O   . GLY A 195 ? 0.4662 0.3542 0.4062 0.0620  -0.0630 -0.0164 195 GLY A O   
1504 N N   . THR A 196 ? 0.4452 0.3249 0.3633 0.0732  -0.0623 -0.0229 196 THR A N   
1505 C CA  . THR A 196 ? 0.4167 0.2951 0.3397 0.0758  -0.0600 -0.0224 196 THR A CA  
1506 C C   . THR A 196 ? 0.4312 0.3253 0.3630 0.0758  -0.0536 -0.0189 196 THR A C   
1507 O O   . THR A 196 ? 0.4530 0.3587 0.3832 0.0770  -0.0497 -0.0180 196 THR A O   
1508 C CB  . THR A 196 ? 0.5031 0.3732 0.4139 0.0835  -0.0592 -0.0264 196 THR A CB  
1509 O OG1 . THR A 196 ? 0.5963 0.4746 0.4987 0.0886  -0.0548 -0.0273 196 THR A OG1 
1510 C CG2 . THR A 196 ? 0.5405 0.3935 0.4423 0.0832  -0.0658 -0.0303 196 THR A CG2 
1511 N N   . ASP A 197 ? 0.4184 0.3127 0.3593 0.0748  -0.0526 -0.0169 197 ASP A N   
1512 C CA  . ASP A 197 ? 0.3459 0.2540 0.2955 0.0745  -0.0471 -0.0135 197 ASP A CA  
1513 C C   . ASP A 197 ? 0.4200 0.3280 0.3674 0.0810  -0.0440 -0.0143 197 ASP A C   
1514 O O   . ASP A 197 ? 0.4440 0.3400 0.3854 0.0848  -0.0462 -0.0170 197 ASP A O   
1515 C CB  . ASP A 197 ? 0.3588 0.2683 0.3217 0.0672  -0.0481 -0.0098 197 ASP A CB  
1516 C CG  . ASP A 197 ? 0.4103 0.3354 0.3817 0.0652  -0.0426 -0.0062 197 ASP A CG  
1517 O OD1 . ASP A 197 ? 0.3807 0.3170 0.3488 0.0682  -0.0385 -0.0064 197 ASP A OD1 
1518 O OD2 . ASP A 197 ? 0.3829 0.3089 0.3646 0.0605  -0.0424 -0.0032 197 ASP A OD2 
1519 N N   . THR A 198 ? 0.3670 0.2887 0.3194 0.0824  -0.0388 -0.0119 198 THR A N   
1520 C CA  . THR A 198 ? 0.3510 0.2749 0.3021 0.0886  -0.0354 -0.0120 198 THR A CA  
1521 C C   . THR A 198 ? 0.3424 0.2762 0.3051 0.0855  -0.0325 -0.0082 198 THR A C   
1522 O O   . THR A 198 ? 0.3543 0.2949 0.3245 0.0793  -0.0322 -0.0058 198 THR A O   
1523 C CB  . THR A 198 ? 0.5053 0.4369 0.4479 0.0952  -0.0315 -0.0135 198 THR A CB  
1524 O OG1 . THR A 198 ? 0.6339 0.5666 0.5749 0.1017  -0.0285 -0.0136 198 THR A OG1 
1525 C CG2 . THR A 198 ? 0.3922 0.3403 0.3399 0.0925  -0.0278 -0.0111 198 THR A CG2 
1526 N N   . THR A 199 ? 0.3627 0.2968 0.3266 0.0899  -0.0304 -0.0077 199 THR A N   
1527 C CA  . THR A 199 ? 0.3260 0.2698 0.2996 0.0877  -0.0275 -0.0042 199 THR A CA  
1528 C C   . THR A 199 ? 0.3424 0.3031 0.3163 0.0900  -0.0227 -0.0030 199 THR A C   
1529 O O   . THR A 199 ? 0.3688 0.3326 0.3355 0.0964  -0.0208 -0.0047 199 THR A O   
1530 C CB  . THR A 199 ? 0.3970 0.3336 0.3721 0.0911  -0.0274 -0.0037 199 THR A CB  
1531 O OG1 . THR A 199 ? 0.3793 0.3007 0.3558 0.0881  -0.0318 -0.0045 199 THR A OG1 
1532 C CG2 . THR A 199 ? 0.3412 0.2880 0.3253 0.0892  -0.0244 -0.0001 199 THR A CG2 
1533 N N   . ILE A 200 ? 0.2963 0.2679 0.2786 0.0848  -0.0208 -0.0002 200 ILE A N   
1534 C CA  . ILE A 200 ? 0.2907 0.2789 0.2744 0.0857  -0.0165 0.0009  200 ILE A CA  
1535 C C   . ILE A 200 ? 0.3507 0.3456 0.3365 0.0902  -0.0138 0.0023  200 ILE A C   
1536 O O   . ILE A 200 ? 0.3052 0.3041 0.2984 0.0869  -0.0129 0.0048  200 ILE A O   
1537 C CB  . ILE A 200 ? 0.2892 0.2858 0.2806 0.0779  -0.0155 0.0032  200 ILE A CB  
1538 C CG1 . ILE A 200 ? 0.3085 0.2965 0.2984 0.0733  -0.0188 0.0023  200 ILE A CG1 
1539 C CG2 . ILE A 200 ? 0.2946 0.3080 0.2869 0.0788  -0.0112 0.0039  200 ILE A CG2 
1540 C CD1 . ILE A 200 ? 0.3595 0.3492 0.3585 0.0649  -0.0190 0.0050  200 ILE A CD1 
1541 N N   . THR A 201 ? 0.3009 0.2976 0.2801 0.0978  -0.0121 0.0009  201 THR A N   
1542 C CA  . THR A 201 ? 0.3264 0.3269 0.3064 0.1033  -0.0101 0.0021  201 THR A CA  
1543 C C   . THR A 201 ? 0.3113 0.3284 0.2989 0.1012  -0.0070 0.0050  201 THR A C   
1544 O O   . THR A 201 ? 0.3000 0.3186 0.2920 0.1015  -0.0065 0.0069  201 THR A O   
1545 C CB  . THR A 201 ? 0.3744 0.3744 0.3457 0.1118  -0.0085 0.0002  201 THR A CB  
1546 O OG1 . THR A 201 ? 0.4107 0.3951 0.3743 0.1131  -0.0115 -0.0028 201 THR A OG1 
1547 C CG2 . THR A 201 ? 0.3606 0.3621 0.3321 0.1183  -0.0066 0.0014  201 THR A CG2 
1548 N N   . VAL A 202 ? 0.2863 0.3160 0.2751 0.0995  -0.0047 0.0052  202 VAL A N   
1549 C CA  . VAL A 202 ? 0.3262 0.3719 0.3219 0.0973  -0.0019 0.0076  202 VAL A CA  
1550 C C   . VAL A 202 ? 0.2547 0.2991 0.2578 0.0900  -0.0029 0.0096  202 VAL A C   
1551 O O   . VAL A 202 ? 0.2804 0.3328 0.2884 0.0893  -0.0015 0.0117  202 VAL A O   
1552 C CB  . VAL A 202 ? 0.3161 0.3745 0.3122 0.0960  0.0007  0.0074  202 VAL A CB  
1553 C CG1 . VAL A 202 ? 0.3174 0.3725 0.3154 0.0885  -0.0004 0.0071  202 VAL A CG1 
1554 C CG2 . VAL A 202 ? 0.3268 0.4024 0.3295 0.0950  0.0037  0.0097  202 VAL A CG2 
1555 N N   . ASN A 203 ? 0.2481 0.2821 0.2521 0.0846  -0.0054 0.0092  203 ASN A N   
1556 C CA  . ASN A 203 ? 0.2498 0.2814 0.2609 0.0776  -0.0060 0.0113  203 ASN A CA  
1557 C C   . ASN A 203 ? 0.2600 0.2829 0.2720 0.0800  -0.0073 0.0123  203 ASN A C   
1558 O O   . ASN A 203 ? 0.2451 0.2716 0.2625 0.0772  -0.0062 0.0146  203 ASN A O   
1559 C CB  . ASN A 203 ? 0.2461 0.2686 0.2581 0.0717  -0.0083 0.0109  203 ASN A CB  
1560 C CG  . ASN A 203 ? 0.2422 0.2746 0.2558 0.0674  -0.0064 0.0109  203 ASN A CG  
1561 O OD1 . ASN A 203 ? 0.2728 0.3185 0.2863 0.0693  -0.0034 0.0110  203 ASN A OD1 
1562 N ND2 . ASN A 203 ? 0.2087 0.2348 0.2239 0.0619  -0.0081 0.0111  203 ASN A ND2 
1563 N N   . VAL A 204 ? 0.2507 0.2615 0.2570 0.0852  -0.0094 0.0105  204 VAL A N   
1564 C CA  . VAL A 204 ? 0.2861 0.2887 0.2930 0.0883  -0.0101 0.0114  204 VAL A CA  
1565 C C   . VAL A 204 ? 0.2998 0.3143 0.3081 0.0924  -0.0073 0.0131  204 VAL A C   
1566 O O   . VAL A 204 ? 0.2631 0.2767 0.2752 0.0916  -0.0069 0.0152  204 VAL A O   
1567 C CB  . VAL A 204 ? 0.2689 0.2575 0.2690 0.0937  -0.0124 0.0089  204 VAL A CB  
1568 C CG1 . VAL A 204 ? 0.3330 0.3137 0.3337 0.0976  -0.0125 0.0099  204 VAL A CG1 
1569 C CG2 . VAL A 204 ? 0.3070 0.2833 0.3065 0.0889  -0.0158 0.0074  204 VAL A CG2 
1570 N N   . LEU A 205 ? 0.2626 0.2881 0.2676 0.0970  -0.0053 0.0124  205 LEU A N   
1571 C CA  . LEU A 205 ? 0.2707 0.3082 0.2774 0.1010  -0.0030 0.0142  205 LEU A CA  
1572 C C   . LEU A 205 ? 0.2577 0.3066 0.2714 0.0945  -0.0017 0.0165  205 LEU A C   
1573 O O   . LEU A 205 ? 0.2725 0.3257 0.2890 0.0953  -0.0010 0.0186  205 LEU A O   
1574 C CB  . LEU A 205 ? 0.2865 0.3337 0.2889 0.1073  -0.0010 0.0133  205 LEU A CB  
1575 C CG  . LEU A 205 ? 0.3065 0.3430 0.3010 0.1147  -0.0015 0.0111  205 LEU A CG  
1576 C CD1 . LEU A 205 ? 0.3852 0.4304 0.3755 0.1192  0.0007  0.0100  205 LEU A CD1 
1577 C CD2 . LEU A 205 ? 0.3149 0.3465 0.3083 0.1185  -0.0011 0.0122  205 LEU A CD2 
1578 N N   . ALA A 206 ? 0.2537 0.3068 0.2700 0.0881  -0.0014 0.0161  206 ALA A N   
1579 C CA  . ALA A 206 ? 0.2228 0.2855 0.2455 0.0815  0.0000  0.0181  206 ALA A CA  
1580 C C   . ALA A 206 ? 0.2382 0.2916 0.2642 0.0779  -0.0010 0.0199  206 ALA A C   
1581 O O   . ALA A 206 ? 0.2221 0.2822 0.2516 0.0760  0.0002  0.0218  206 ALA A O   
1582 C CB  . ALA A 206 ? 0.2426 0.3093 0.2673 0.0752  0.0007  0.0174  206 ALA A CB  
1583 N N   . TRP A 207 ? 0.2094 0.2473 0.2342 0.0772  -0.0033 0.0192  207 TRP A N   
1584 C CA  . TRP A 207 ? 0.2533 0.2808 0.2815 0.0739  -0.0041 0.0210  207 TRP A CA  
1585 C C   . TRP A 207 ? 0.2421 0.2676 0.2691 0.0797  -0.0039 0.0222  207 TRP A C   
1586 O O   . TRP A 207 ? 0.2625 0.2865 0.2929 0.0773  -0.0032 0.0244  207 TRP A O   
1587 C CB  . TRP A 207 ? 0.2654 0.2774 0.2929 0.0721  -0.0067 0.0199  207 TRP A CB  
1588 C CG  . TRP A 207 ? 0.2310 0.2301 0.2622 0.0693  -0.0078 0.0216  207 TRP A CG  
1589 C CD1 . TRP A 207 ? 0.2459 0.2433 0.2829 0.0623  -0.0070 0.0240  207 TRP A CD1 
1590 C CD2 . TRP A 207 ? 0.2376 0.2231 0.2667 0.0737  -0.0096 0.0213  207 TRP A CD2 
1591 N NE1 . TRP A 207 ? 0.2721 0.2554 0.3112 0.0621  -0.0083 0.0252  207 TRP A NE1 
1592 C CE2 . TRP A 207 ? 0.2668 0.2429 0.3013 0.0690  -0.0099 0.0235  207 TRP A CE2 
1593 C CE3 . TRP A 207 ? 0.3073 0.2874 0.3307 0.0811  -0.0107 0.0193  207 TRP A CE3 
1594 C CZ2 . TRP A 207 ? 0.3288 0.2906 0.3635 0.0716  -0.0113 0.0238  207 TRP A CZ2 
1595 C CZ3 . TRP A 207 ? 0.3283 0.2941 0.3517 0.0834  -0.0121 0.0195  207 TRP A CZ3 
1596 C CH2 . TRP A 207 ? 0.2996 0.2572 0.3291 0.0773  -0.0124 0.0214  207 TRP A CH2 
1597 N N   . LEU A 208 ? 0.2340 0.2588 0.2559 0.0875  -0.0042 0.0208  208 LEU A N   
1598 C CA  . LEU A 208 ? 0.2528 0.2775 0.2734 0.0936  -0.0035 0.0222  208 LEU A CA  
1599 C C   . LEU A 208 ? 0.2565 0.2971 0.2799 0.0930  -0.0015 0.0242  208 LEU A C   
1600 O O   . LEU A 208 ? 0.2594 0.2995 0.2841 0.0940  -0.0010 0.0264  208 LEU A O   
1601 C CB  . LEU A 208 ? 0.2500 0.2717 0.2644 0.1009  -0.0036 0.0202  208 LEU A CB  
1602 C CG  . LEU A 208 ? 0.2777 0.2817 0.2889 0.1013  -0.0057 0.0181  208 LEU A CG  
1603 C CD1 . LEU A 208 ? 0.3054 0.3073 0.3097 0.1072  -0.0054 0.0158  208 LEU A CD1 
1604 C CD2 . LEU A 208 ? 0.3077 0.2989 0.3216 0.0981  -0.0066 0.0191  208 LEU A CD2 
1605 N N   . TYR A 209 ? 0.2711 0.3257 0.2953 0.0914  -0.0004 0.0236  209 TYR A N   
1606 C CA  . TYR A 209 ? 0.2769 0.3468 0.3042 0.0897  0.0012  0.0254  209 TYR A CA  
1607 C C   . TYR A 209 ? 0.2731 0.3411 0.3048 0.0819  0.0014  0.0271  209 TYR A C   
1608 O O   . TYR A 209 ? 0.2488 0.3223 0.2820 0.0817  0.0021  0.0290  209 TYR A O   
1609 C CB  . TYR A 209 ? 0.2683 0.3531 0.2964 0.0887  0.0025  0.0244  209 TYR A CB  
1610 C CG  . TYR A 209 ? 0.2674 0.3594 0.2921 0.0971  0.0031  0.0239  209 TYR A CG  
1611 C CD1 . TYR A 209 ? 0.3437 0.4426 0.3677 0.0998  0.0038  0.0253  209 TYR A CD1 
1612 C CD2 . TYR A 209 ? 0.2772 0.3667 0.2981 0.1003  0.0033  0.0217  209 TYR A CD2 
1613 C CE1 . TYR A 209 ? 0.3649 0.4678 0.3849 0.1050  0.0047  0.0247  209 TYR A CE1 
1614 C CE2 . TYR A 209 ? 0.3327 0.4262 0.3493 0.1060  0.0044  0.0211  209 TYR A CE2 
1615 C CZ  . TYR A 209 ? 0.4107 0.5107 0.4271 0.1081  0.0052  0.0227  209 TYR A CZ  
1616 O OH  . TYR A 209 ? 0.3623 0.4659 0.3747 0.1133  0.0065  0.0224  209 TYR A OH  
1617 N N   . ALA A 210 ? 0.2342 0.2950 0.2680 0.0755  0.0011  0.0265  210 ALA A N   
1618 C CA  . ALA A 210 ? 0.2222 0.2784 0.2599 0.0684  0.0016  0.0282  210 ALA A CA  
1619 C C   . ALA A 210 ? 0.2662 0.3118 0.3034 0.0710  0.0011  0.0300  210 ALA A C   
1620 O O   . ALA A 210 ? 0.2651 0.3122 0.3043 0.0680  0.0022  0.0321  210 ALA A O   
1621 C CB  . ALA A 210 ? 0.2674 0.3148 0.3072 0.0623  0.0011  0.0276  210 ALA A CB  
1622 N N   . ALA A 211 ? 0.2328 0.2671 0.2672 0.0766  -0.0004 0.0293  211 ALA A N   
1623 C CA  . ALA A 211 ? 0.2643 0.2877 0.2984 0.0794  -0.0006 0.0310  211 ALA A CA  
1624 C C   . ALA A 211 ? 0.3030 0.3360 0.3358 0.0838  0.0005  0.0327  211 ALA A C   
1625 O O   . ALA A 211 ? 0.2787 0.3088 0.3127 0.0825  0.0013  0.0350  211 ALA A O   
1626 C CB  . ALA A 211 ? 0.2574 0.2677 0.2884 0.0848  -0.0022 0.0295  211 ALA A CB  
1627 N N   . VAL A 212 ? 0.2481 0.2927 0.2783 0.0892  0.0007  0.0318  212 VAL A N   
1628 C CA  . VAL A 212 ? 0.2905 0.3449 0.3192 0.0921  0.0014  0.0330  212 VAL A CA  
1629 C C   . VAL A 212 ? 0.3212 0.3866 0.3534 0.0872  0.0023  0.0350  212 VAL A C   
1630 O O   . VAL A 212 ? 0.3010 0.3677 0.3330 0.0880  0.0027  0.0371  212 VAL A O   
1631 C CB  . VAL A 212 ? 0.2918 0.3565 0.3174 0.0967  0.0017  0.0314  212 VAL A CB  
1632 C CG1 . VAL A 212 ? 0.3321 0.4055 0.3561 0.0994  0.0023  0.0330  212 VAL A CG1 
1633 C CG2 . VAL A 212 ? 0.2972 0.3499 0.3186 0.1005  0.0011  0.0293  212 VAL A CG2 
1634 N N   . ILE A 213 ? 0.3061 0.3788 0.3409 0.0808  0.0028  0.0338  213 ILE A N   
1635 C CA  . ILE A 213 ? 0.3021 0.3840 0.3395 0.0742  0.0039  0.0349  213 ILE A CA  
1636 C C   . ILE A 213 ? 0.3550 0.4254 0.3933 0.0701  0.0044  0.0368  213 ILE A C   
1637 O O   . ILE A 213 ? 0.3136 0.3891 0.3520 0.0678  0.0051  0.0384  213 ILE A O   
1638 C CB  . ILE A 213 ? 0.3427 0.4320 0.3829 0.0677  0.0047  0.0333  213 ILE A CB  
1639 C CG1 . ILE A 213 ? 0.2913 0.3943 0.3308 0.0719  0.0047  0.0318  213 ILE A CG1 
1640 C CG2 . ILE A 213 ? 0.3633 0.4585 0.4063 0.0598  0.0061  0.0343  213 ILE A CG2 
1641 C CD1 . ILE A 213 ? 0.3202 0.4269 0.3616 0.0674  0.0055  0.0299  213 ILE A CD1 
1642 N N   . ASN A 214 ? 0.2767 0.3525 0.3539 0.0039  -0.0361 0.0751  214 ASN A N   
1643 C CA  . ASN A 214 ? 0.2916 0.3492 0.3624 -0.0074 -0.0384 0.0716  214 ASN A CA  
1644 C C   . ASN A 214 ? 0.3585 0.3980 0.4149 -0.0031 -0.0432 0.0709  214 ASN A C   
1645 O O   . ASN A 214 ? 0.3800 0.4018 0.4292 -0.0107 -0.0447 0.0685  214 ASN A O   
1646 C CB  . ASN A 214 ? 0.3127 0.3565 0.3805 -0.0124 -0.0352 0.0680  214 ASN A CB  
1647 C CG  . ASN A 214 ? 0.3651 0.4233 0.4475 -0.0224 -0.0312 0.0683  214 ASN A CG  
1648 O OD1 . ASN A 214 ? 0.3694 0.4264 0.4563 -0.0347 -0.0316 0.0672  214 ASN A OD1 
1649 N ND2 . ASN A 214 ? 0.3654 0.4375 0.4554 -0.0170 -0.0272 0.0702  214 ASN A ND2 
1650 N N   . GLY A 215 ? 0.3671 0.4107 0.4197 0.0091  -0.0454 0.0734  215 GLY A N   
1651 C CA  . GLY A 215 ? 0.3735 0.4028 0.4144 0.0131  -0.0503 0.0738  215 GLY A CA  
1652 C C   . GLY A 215 ? 0.4324 0.4379 0.4584 0.0215  -0.0519 0.0713  215 GLY A C   
1653 O O   . GLY A 215 ? 0.4073 0.3998 0.4240 0.0243  -0.0561 0.0719  215 GLY A O   
1654 N N   . ASP A 216 ? 0.3487 0.3471 0.3716 0.0256  -0.0491 0.0685  216 ASP A N   
1655 C CA  . ASP A 216 ? 0.3932 0.3701 0.4018 0.0359  -0.0516 0.0662  216 ASP A CA  
1656 C C   . ASP A 216 ? 0.5012 0.4880 0.5081 0.0519  -0.0513 0.0682  216 ASP A C   
1657 O O   . ASP A 216 ? 0.3911 0.3935 0.4043 0.0573  -0.0469 0.0690  216 ASP A O   
1658 C CB  . ASP A 216 ? 0.4394 0.4011 0.4430 0.0343  -0.0500 0.0619  216 ASP A CB  
1659 C CG  . ASP A 216 ? 0.5704 0.5232 0.5770 0.0190  -0.0496 0.0603  216 ASP A CG  
1660 O OD1 . ASP A 216 ? 0.5755 0.5160 0.5779 0.0135  -0.0529 0.0608  216 ASP A OD1 
1661 O OD2 . ASP A 216 ? 0.5222 0.4776 0.5340 0.0135  -0.0461 0.0585  216 ASP A OD2 
1662 N N   . ARG A 217 ? 0.3814 0.3584 0.3795 0.0598  -0.0556 0.0693  217 ARG A N   
1663 C CA  . ARG A 217 ? 0.3866 0.3731 0.3834 0.0752  -0.0556 0.0718  217 ARG A CA  
1664 C C   . ARG A 217 ? 0.3650 0.3285 0.3460 0.0875  -0.0591 0.0694  217 ARG A C   
1665 O O   . ARG A 217 ? 0.3573 0.3266 0.3357 0.1017  -0.0589 0.0711  217 ARG A O   
1666 C CB  . ARG A 217 ? 0.3994 0.4020 0.4037 0.0742  -0.0578 0.0769  217 ARG A CB  
1667 C CG  . ARG A 217 ? 0.4094 0.4394 0.4306 0.0670  -0.0546 0.0801  217 ARG A CG  
1668 C CD  . ARG A 217 ? 0.3535 0.3976 0.3812 0.0658  -0.0581 0.0849  217 ARG A CD  
1669 N NE  . ARG A 217 ? 0.3027 0.3594 0.3326 0.0810  -0.0576 0.0887  217 ARG A NE  
1670 C CZ  . ARG A 217 ? 0.3571 0.4395 0.4010 0.0847  -0.0540 0.0927  217 ARG A CZ  
1671 N NH1 . ARG A 217 ? 0.3828 0.4809 0.4399 0.0745  -0.0509 0.0932  217 ARG A NH1 
1672 N NH2 . ARG A 217 ? 0.3214 0.4136 0.3665 0.0995  -0.0533 0.0964  217 ARG A NH2 
1673 N N   . TRP A 218 ? 0.3422 0.2799 0.3132 0.0827  -0.0624 0.0656  218 TRP A N   
1674 C CA  . TRP A 218 ? 0.3695 0.2833 0.3262 0.0924  -0.0675 0.0637  218 TRP A CA  
1675 C C   . TRP A 218 ? 0.4219 0.3315 0.3701 0.1084  -0.0663 0.0609  218 TRP A C   
1676 O O   . TRP A 218 ? 0.4291 0.3262 0.3673 0.1205  -0.0698 0.0605  218 TRP A O   
1677 C CB  . TRP A 218 ? 0.4429 0.3308 0.3928 0.0826  -0.0713 0.0607  218 TRP A CB  
1678 C CG  . TRP A 218 ? 0.4403 0.3206 0.3896 0.0770  -0.0692 0.0564  218 TRP A CG  
1679 C CD1 . TRP A 218 ? 0.3849 0.2713 0.3432 0.0627  -0.0662 0.0561  218 TRP A CD1 
1680 C CD2 . TRP A 218 ? 0.4367 0.3016 0.3757 0.0859  -0.0704 0.0517  218 TRP A CD2 
1681 N NE1 . TRP A 218 ? 0.4225 0.2985 0.3772 0.0620  -0.0655 0.0519  218 TRP A NE1 
1682 C CE2 . TRP A 218 ? 0.4242 0.2868 0.3666 0.0761  -0.0682 0.0491  218 TRP A CE2 
1683 C CE3 . TRP A 218 ? 0.4799 0.3321 0.4065 0.1016  -0.0732 0.0493  218 TRP A CE3 
1684 C CZ2 . TRP A 218 ? 0.5003 0.3487 0.4339 0.0813  -0.0692 0.0442  218 TRP A CZ2 
1685 C CZ3 . TRP A 218 ? 0.5332 0.3704 0.4501 0.1070  -0.0742 0.0440  218 TRP A CZ3 
1686 C CH2 . TRP A 218 ? 0.5191 0.3547 0.4395 0.0967  -0.0724 0.0416  218 TRP A CH2 
1687 N N   . PHE A 219 ? 0.4208 0.3398 0.3722 0.1089  -0.0613 0.0590  219 PHE A N   
1688 C CA  . PHE A 219 ? 0.4467 0.3619 0.3889 0.1238  -0.0594 0.0561  219 PHE A CA  
1689 C C   . PHE A 219 ? 0.3998 0.3380 0.3470 0.1372  -0.0552 0.0602  219 PHE A C   
1690 O O   . PHE A 219 ? 0.4421 0.3784 0.3810 0.1516  -0.0530 0.0583  219 PHE A O   
1691 C CB  . PHE A 219 ? 0.4003 0.3170 0.3439 0.1186  -0.0556 0.0529  219 PHE A CB  
1692 C CG  . PHE A 219 ? 0.3821 0.3247 0.3431 0.1071  -0.0502 0.0566  219 PHE A CG  
1693 C CD1 . PHE A 219 ? 0.3430 0.3122 0.3134 0.1138  -0.0441 0.0604  219 PHE A CD1 
1694 C CD2 . PHE A 219 ? 0.3461 0.2864 0.3144 0.0898  -0.0511 0.0566  219 PHE A CD2 
1695 C CE1 . PHE A 219 ? 0.3259 0.3187 0.3134 0.1030  -0.0397 0.0641  219 PHE A CE1 
1696 C CE2 . PHE A 219 ? 0.3602 0.3234 0.3443 0.0793  -0.0466 0.0596  219 PHE A CE2 
1697 C CZ  . PHE A 219 ? 0.3408 0.3302 0.3349 0.0857  -0.0412 0.0633  219 PHE A CZ  
1698 N N   . LEU A 220 ? 0.3825 0.3425 0.3432 0.1329  -0.0541 0.0660  220 LEU A N   
1699 C CA  . LEU A 220 ? 0.3921 0.3754 0.3598 0.1451  -0.0503 0.0709  220 LEU A CA  
1700 C C   . LEU A 220 ? 0.4803 0.4509 0.4366 0.1601  -0.0540 0.0710  220 LEU A C   
1701 O O   . LEU A 220 ? 0.4655 0.4139 0.4126 0.1581  -0.0602 0.0689  220 LEU A O   
1702 C CB  . LEU A 220 ? 0.3984 0.4075 0.3842 0.1353  -0.0493 0.0770  220 LEU A CB  
1703 C CG  . LEU A 220 ? 0.3043 0.3307 0.3042 0.1216  -0.0452 0.0780  220 LEU A CG  
1704 C CD1 . LEU A 220 ? 0.3071 0.3578 0.3236 0.1142  -0.0456 0.0840  220 LEU A CD1 
1705 C CD2 . LEU A 220 ? 0.3119 0.3508 0.3146 0.1295  -0.0383 0.0782  220 LEU A CD2 
1706 N N   . ASN A 221 ? 0.4827 0.4683 0.4407 0.1754  -0.0500 0.0739  221 ASN A N   
1707 C CA  . ASN A 221 ? 0.5078 0.4835 0.4559 0.1912  -0.0528 0.0743  221 ASN A CA  
1708 C C   . ASN A 221 ? 0.6421 0.6462 0.6017 0.2016  -0.0472 0.0804  221 ASN A C   
1709 O O   . ASN A 221 ? 0.4885 0.5172 0.4607 0.2011  -0.0413 0.0843  221 ASN A O   
1710 C CB  . ASN A 221 ? 0.5621 0.5109 0.4913 0.1998  -0.0536 0.0663  221 ASN A CB  
1711 C CG  . ASN A 221 ? 0.6799 0.6378 0.6069 0.2075  -0.0464 0.0642  221 ASN A CG  
1712 O OD1 . ASN A 221 ? 0.7105 0.6949 0.6484 0.2131  -0.0397 0.0691  221 ASN A OD1 
1713 N ND2 . ASN A 221 ? 0.6528 0.5891 0.5663 0.2068  -0.0477 0.0571  221 ASN A ND2 
1714 N N   . ARG A 222 ? 0.5574 0.5583 0.5142 0.2089  -0.0490 0.0811  222 ARG A N   
1715 C CA  . ARG A 222 ? 0.6465 0.6714 0.6133 0.2182  -0.0436 0.0859  222 ARG A CA  
1716 C C   . ARG A 222 ? 0.7417 0.7663 0.7002 0.2309  -0.0365 0.0824  222 ARG A C   
1717 O O   . ARG A 222 ? 0.8027 0.8493 0.7702 0.2384  -0.0304 0.0868  222 ARG A O   
1718 C CB  . ARG A 222 ? 0.6553 0.6764 0.6216 0.2222  -0.0478 0.0881  222 ARG A CB  
1719 C CG  . ARG A 222 ? 0.8931 0.9389 0.8705 0.2315  -0.0425 0.0935  222 ARG A CG  
1720 C CD  . ARG A 222 ? 0.9812 1.0257 0.9599 0.2355  -0.0466 0.0965  222 ARG A CD  
1721 N NE  . ARG A 222 ? 1.0815 1.1508 1.0719 0.2440  -0.0409 0.1020  222 ARG A NE  
1722 C CZ  . ARG A 222 ? 1.0222 1.0995 1.0191 0.2477  -0.0430 0.1066  222 ARG A CZ  
1723 N NH1 . ARG A 222 ? 1.0526 1.1149 1.0448 0.2445  -0.0506 0.1064  222 ARG A NH1 
1724 N NH2 . ARG A 222 ? 1.0712 1.1720 1.0799 0.2547  -0.0372 0.1119  222 ARG A NH2 
1725 N N   . PHE A 223 ? 0.7509 0.7512 0.6923 0.2332  -0.0372 0.0746  223 PHE A N   
1726 C CA  . PHE A 223 ? 0.7124 0.7114 0.6436 0.2452  -0.0308 0.0709  223 PHE A CA  
1727 C C   . PHE A 223 ? 0.7508 0.7778 0.6949 0.2452  -0.0225 0.0758  223 PHE A C   
1728 O O   . PHE A 223 ? 0.6796 0.7216 0.6381 0.2342  -0.0225 0.0800  223 PHE A O   
1729 C CB  . PHE A 223 ? 0.8499 0.8187 0.7615 0.2451  -0.0341 0.0616  223 PHE A CB  
1730 C CG  . PHE A 223 ? 1.0146 0.9551 0.9109 0.2487  -0.0405 0.0558  223 PHE A CG  
1731 C CD1 . PHE A 223 ? 1.0380 0.9804 0.9376 0.2528  -0.0426 0.0589  223 PHE A CD1 
1732 C CD2 . PHE A 223 ? 1.0767 0.9888 0.9559 0.2477  -0.0446 0.0473  223 PHE A CD2 
1733 C CE1 . PHE A 223 ? 1.1364 1.0532 1.0229 0.2558  -0.0483 0.0538  223 PHE A CE1 
1734 C CE2 . PHE A 223 ? 1.1905 1.0773 1.0569 0.2502  -0.0506 0.0420  223 PHE A CE2 
1735 C CZ  . PHE A 223 ? 1.1924 1.0815 1.0625 0.2543  -0.0523 0.0454  223 PHE A CZ  
1736 N N   . THR A 224 ? 0.6154 0.6493 0.5539 0.2576  -0.0152 0.0753  224 THR A N   
1737 C CA  . THR A 224 ? 0.7195 0.7739 0.6650 0.2589  -0.0068 0.0784  224 THR A CA  
1738 C C   . THR A 224 ? 0.7067 0.7463 0.6314 0.2711  -0.0028 0.0719  224 THR A C   
1739 O O   . THR A 224 ? 0.7238 0.7391 0.6302 0.2784  -0.0065 0.0653  224 THR A O   
1740 C CB  . THR A 224 ? 0.7407 0.8288 0.7061 0.2610  -0.0001 0.0878  224 THR A CB  
1741 O OG1 . THR A 224 ? 0.5843 0.6936 0.5623 0.2556  0.0061  0.0921  224 THR A OG1 
1742 C CG2 . THR A 224 ? 0.6770 0.7667 0.6332 0.2771  0.0056  0.0878  224 THR A CG2 
1743 N N   . THR A 225 ? 0.7256 0.7801 0.6531 0.2729  0.0048  0.0741  225 THR A N   
1744 C CA  . THR A 225 ? 0.7223 0.7650 0.6297 0.2843  0.0091  0.0686  225 THR A CA  
1745 C C   . THR A 225 ? 0.7723 0.8435 0.6895 0.2889  0.0199  0.0756  225 THR A C   
1746 O O   . THR A 225 ? 0.6835 0.7817 0.6237 0.2812  0.0233  0.0840  225 THR A O   
1747 C CB  . THR A 225 ? 0.7576 0.7756 0.6506 0.2790  0.0039  0.0606  225 THR A CB  
1748 O OG1 . THR A 225 ? 0.7673 0.7741 0.6395 0.2907  0.0077  0.0553  225 THR A OG1 
1749 C CG2 . THR A 225 ? 0.6217 0.6552 0.5310 0.2664  0.0054  0.0649  225 THR A CG2 
1750 N N   . THR A 226 ? 0.7655 0.8303 0.6648 0.3011  0.0251  0.0724  226 THR A N   
1751 C CA  . THR A 226 ? 0.7815 0.8697 0.6864 0.3053  0.0355  0.0785  226 THR A CA  
1752 C C   . THR A 226 ? 0.7171 0.7986 0.6161 0.3000  0.0357  0.0751  226 THR A C   
1753 O O   . THR A 226 ? 0.6922 0.7467 0.5761 0.2973  0.0283  0.0665  226 THR A O   
1754 C CB  . THR A 226 ? 0.8283 0.9150 0.7163 0.3227  0.0418  0.0781  226 THR A CB  
1755 O OG1 . THR A 226 ? 0.9063 1.0144 0.7985 0.3261  0.0518  0.0845  226 THR A OG1 
1756 C CG2 . THR A 226 ? 0.8196 0.8724 0.6779 0.3305  0.0366  0.0667  226 THR A CG2 
1757 N N   . LEU A 227 ? 0.7090 0.8152 0.6203 0.2983  0.0440  0.0824  227 LEU A N   
1758 C CA  . LEU A 227 ? 0.7165 0.8193 0.6235 0.2937  0.0452  0.0804  227 LEU A CA  
1759 C C   . LEU A 227 ? 0.7672 0.8427 0.6434 0.3050  0.0437  0.0710  227 LEU A C   
1760 O O   . LEU A 227 ? 0.6729 0.7297 0.5394 0.2999  0.0384  0.0645  227 LEU A O   
1761 C CB  . LEU A 227 ? 0.7036 0.8381 0.6277 0.2917  0.0553  0.0905  227 LEU A CB  
1762 C CG  . LEU A 227 ? 0.7595 0.8975 0.6868 0.2839  0.0572  0.0910  227 LEU A CG  
1763 C CD1 . LEU A 227 ? 0.6679 0.8399 0.6205 0.2768  0.0653  0.1027  227 LEU A CD1 
1764 C CD2 . LEU A 227 ? 0.7828 0.9035 0.6828 0.2959  0.0595  0.0850  227 LEU A CD2 
1765 N N   . ASN A 228 ? 0.8031 0.8752 0.6631 0.3202  0.0476  0.0701  228 ASN A N   
1766 C CA  . ASN A 228 ? 0.8243 0.8720 0.6541 0.3314  0.0463  0.0615  228 ASN A CA  
1767 C C   . ASN A 228 ? 0.7874 0.7999 0.5997 0.3304  0.0346  0.0502  228 ASN A C   
1768 O O   . ASN A 228 ? 0.7809 0.7702 0.5741 0.3311  0.0297  0.0420  228 ASN A O   
1769 C CB  . ASN A 228 ? 1.0518 1.1074 0.8692 0.3481  0.0544  0.0647  228 ASN A CB  
1770 C CG  . ASN A 228 ? 1.0763 1.1649 0.9095 0.3488  0.0658  0.0764  228 ASN A CG  
1771 O OD1 . ASN A 228 ? 1.1374 1.2476 0.9842 0.3520  0.0718  0.0849  228 ASN A OD1 
1772 N ND2 . ASN A 228 ? 1.0354 1.1279 0.8673 0.3452  0.0686  0.0774  228 ASN A ND2 
1773 N N   . ASP A 229 ? 0.8436 0.8512 0.6625 0.3281  0.0296  0.0496  229 ASP A N   
1774 C CA  . ASP A 229 ? 0.8586 0.8330 0.6631 0.3249  0.0181  0.0397  229 ASP A CA  
1775 C C   . ASP A 229 ? 0.7179 0.6829 0.5304 0.3089  0.0111  0.0372  229 ASP A C   
1776 O O   . ASP A 229 ? 0.7813 0.7180 0.5773 0.3062  0.0031  0.0285  229 ASP A O   
1777 C CB  . ASP A 229 ? 0.8160 0.7882 0.6259 0.3264  0.0146  0.0406  229 ASP A CB  
1778 C CG  . ASP A 229 ? 1.0834 1.0545 0.8785 0.3433  0.0191  0.0401  229 ASP A CG  
1779 O OD1 . ASP A 229 ? 1.1265 1.0712 0.8968 0.3511  0.0144  0.0314  229 ASP A OD1 
1780 O OD2 . ASP A 229 ? 1.1073 1.1036 0.9153 0.3486  0.0269  0.0485  229 ASP A OD2 
1781 N N   . PHE A 230 ? 0.7118 0.7004 0.5496 0.2980  0.0139  0.0452  230 PHE A N   
1782 C CA  . PHE A 230 ? 0.7176 0.6998 0.5630 0.2836  0.0087  0.0438  230 PHE A CA  
1783 C C   . PHE A 230 ? 0.6781 0.6496 0.5084 0.2857  0.0095  0.0391  230 PHE A C   
1784 O O   . PHE A 230 ? 0.6725 0.6188 0.4923 0.2793  0.0013  0.0319  230 PHE A O   
1785 C CB  . PHE A 230 ? 0.6947 0.7071 0.5690 0.2727  0.0129  0.0537  230 PHE A CB  
1786 C CG  . PHE A 230 ? 0.6140 0.6202 0.4955 0.2584  0.0080  0.0527  230 PHE A CG  
1787 C CD1 . PHE A 230 ? 0.5465 0.5332 0.4283 0.2482  -0.0018 0.0491  230 PHE A CD1 
1788 C CD2 . PHE A 230 ? 0.5789 0.5967 0.4650 0.2556  0.0131  0.0552  230 PHE A CD2 
1789 C CE1 . PHE A 230 ? 0.5235 0.5032 0.4108 0.2352  -0.0063 0.0484  230 PHE A CE1 
1790 C CE2 . PHE A 230 ? 0.5958 0.6070 0.4881 0.2427  0.0084  0.0544  230 PHE A CE2 
1791 C CZ  . PHE A 230 ? 0.5435 0.5354 0.4363 0.2312  -0.0011 0.0507  230 PHE A CZ  
1792 N N   . ASN A 231 ? 0.7124 0.7030 0.5419 0.2941  0.0193  0.0436  231 ASN A N   
1793 C CA  . ASN A 231 ? 0.7580 0.7406 0.5735 0.2966  0.0206  0.0400  231 ASN A CA  
1794 C C   . ASN A 231 ? 0.7637 0.7122 0.5486 0.3047  0.0134  0.0288  231 ASN A C   
1795 O O   . ASN A 231 ? 0.7668 0.6973 0.5396 0.3015  0.0086  0.0229  231 ASN A O   
1796 C CB  . ASN A 231 ? 0.7000 0.7106 0.5199 0.3049  0.0329  0.0479  231 ASN A CB  
1797 C CG  . ASN A 231 ? 0.6763 0.7164 0.5245 0.2932  0.0386  0.0576  231 ASN A CG  
1798 O OD1 . ASN A 231 ? 0.7366 0.7744 0.5986 0.2795  0.0332  0.0575  231 ASN A OD1 
1799 N ND2 . ASN A 231 ? 0.7718 0.8395 0.6292 0.2981  0.0493  0.0664  231 ASN A ND2 
1800 N N   . LEU A 232 ? 0.7581 0.6972 0.5307 0.3149  0.0121  0.0258  232 LEU A N   
1801 C CA  . LEU A 232 ? 0.8338 0.7395 0.5786 0.3211  0.0038  0.0149  232 LEU A CA  
1802 C C   . LEU A 232 ? 0.8400 0.7200 0.5847 0.3072  -0.0084 0.0083  232 LEU A C   
1803 O O   . LEU A 232 ? 0.8667 0.7208 0.5923 0.3069  -0.0159 -0.0001 232 LEU A O   
1804 C CB  . LEU A 232 ? 0.8907 0.7921 0.6256 0.3331  0.0042  0.0138  232 LEU A CB  
1805 C CG  . LEU A 232 ? 1.0157 0.9178 0.7290 0.3510  0.0103  0.0129  232 LEU A CG  
1806 C CD1 . LEU A 232 ? 0.8896 0.7620 0.5744 0.3551  0.0028  0.0027  232 LEU A CD1 
1807 C CD2 . LEU A 232 ? 1.0374 0.9722 0.7620 0.3555  0.0232  0.0229  232 LEU A CD2 
1808 N N   . VAL A 233 ? 0.7733 0.6602 0.5393 0.2952  -0.0109 0.0123  233 VAL A N   
1809 C CA  . VAL A 233 ? 0.8158 0.6794 0.5829 0.2810  -0.0219 0.0072  233 VAL A CA  
1810 C C   . VAL A 233 ? 0.8209 0.6864 0.5949 0.2703  -0.0224 0.0080  233 VAL A C   
1811 O O   . VAL A 233 ? 0.8860 0.7271 0.6502 0.2629  -0.0310 0.0013  233 VAL A O   
1812 C CB  . VAL A 233 ? 0.8757 0.7442 0.6607 0.2726  -0.0248 0.0113  233 VAL A CB  
1813 C CG1 . VAL A 233 ? 0.8162 0.6655 0.6060 0.2562  -0.0346 0.0082  233 VAL A CG1 
1814 C CG2 . VAL A 233 ? 0.8632 0.7219 0.6376 0.2824  -0.0268 0.0084  233 VAL A CG2 
1815 N N   . ALA A 234 ? 0.8150 0.7098 0.6069 0.2688  -0.0135 0.0166  234 ALA A N   
1816 C CA  . ALA A 234 ? 0.7753 0.6747 0.5750 0.2595  -0.0130 0.0185  234 ALA A CA  
1817 C C   . ALA A 234 ? 0.8032 0.6832 0.5802 0.2648  -0.0156 0.0111  234 ALA A C   
1818 O O   . ALA A 234 ? 0.8246 0.6853 0.5977 0.2549  -0.0232 0.0065  234 ALA A O   
1819 C CB  . ALA A 234 ? 0.7407 0.6772 0.5615 0.2599  -0.0016 0.0292  234 ALA A CB  
1820 N N   . MET A 235 ? 0.8373 0.7222 0.5987 0.2804  -0.0095 0.0103  235 MET A N   
1821 C CA  . MET A 235 ? 0.8562 0.7222 0.5930 0.2872  -0.0123 0.0031  235 MET A CA  
1822 C C   . MET A 235 ? 0.8308 0.6609 0.5527 0.2805  -0.0261 -0.0071 235 MET A C   
1823 O O   . MET A 235 ? 0.8170 0.6312 0.5306 0.2748  -0.0319 -0.0117 235 MET A O   
1824 C CB  . MET A 235 ? 0.9826 0.8543 0.7013 0.3058  -0.0055 0.0029  235 MET A CB  
1825 C CG  . MET A 235 ? 1.0861 0.9924 0.8166 0.3124  0.0083  0.0130  235 MET A CG  
1826 S SD  . MET A 235 ? 1.4436 1.3501 1.1567 0.3199  0.0126  0.0123  235 MET A SD  
1827 C CE  . MET A 235 ? 1.1208 1.0018 0.7968 0.3374  0.0083  0.0034  235 MET A CE  
1828 N N   . LYS A 236 ? 0.8377 0.6556 0.5574 0.2803  -0.0316 -0.0101 236 LYS A N   
1829 C CA  . LYS A 236 ? 0.8081 0.5935 0.5151 0.2735  -0.0446 -0.0190 236 LYS A CA  
1830 C C   . LYS A 236 ? 0.8314 0.6092 0.5532 0.2545  -0.0511 -0.0187 236 LYS A C   
1831 O O   . LYS A 236 ? 0.8747 0.6281 0.5866 0.2472  -0.0611 -0.0254 236 LYS A O   
1832 C CB  . LYS A 236 ? 0.8546 0.6310 0.5591 0.2765  -0.0484 -0.0209 236 LYS A CB  
1833 C CG  . LYS A 236 ? 0.8850 0.6336 0.5864 0.2644  -0.0614 -0.0272 236 LYS A CG  
1834 C CD  . LYS A 236 ? 0.9572 0.6938 0.6500 0.2709  -0.0655 -0.0304 236 LYS A CD  
1835 C CE  . LYS A 236 ? 0.9322 0.6539 0.6354 0.2559  -0.0748 -0.0316 236 LYS A CE  
1836 N NZ  . LYS A 236 ? 1.0015 0.7126 0.6979 0.2620  -0.0785 -0.0339 236 LYS A NZ  
1837 N N   . TYR A 237 ? 0.7904 0.5890 0.5361 0.2459  -0.0459 -0.0107 237 TYR A N   
1838 C CA  . TYR A 237 ? 0.6765 0.4682 0.4359 0.2279  -0.0516 -0.0099 237 TYR A CA  
1839 C C   . TYR A 237 ? 0.7413 0.5447 0.5076 0.2239  -0.0473 -0.0062 237 TYR A C   
1840 O O   . TYR A 237 ? 0.6181 0.4213 0.3993 0.2091  -0.0501 -0.0034 237 TYR A O   
1841 C CB  . TYR A 237 ? 0.6333 0.4353 0.4137 0.2186  -0.0513 -0.0039 237 TYR A CB  
1842 C CG  . TYR A 237 ? 0.7332 0.5166 0.5076 0.2173  -0.0587 -0.0084 237 TYR A CG  
1843 C CD1 . TYR A 237 ? 0.6799 0.4672 0.4469 0.2305  -0.0559 -0.0087 237 TYR A CD1 
1844 C CD2 . TYR A 237 ? 0.6666 0.4294 0.4433 0.2028  -0.0683 -0.0118 237 TYR A CD2 
1845 C CE1 . TYR A 237 ? 0.7805 0.5509 0.5423 0.2296  -0.0627 -0.0124 237 TYR A CE1 
1846 C CE2 . TYR A 237 ? 0.7408 0.4882 0.5131 0.2015  -0.0746 -0.0151 237 TYR A CE2 
1847 C CZ  . TYR A 237 ? 0.7718 0.5226 0.5365 0.2150  -0.0720 -0.0154 237 TYR A CZ  
1848 O OH  . TYR A 237 ? 0.8383 0.5739 0.5991 0.2139  -0.0784 -0.0183 237 TYR A OH  
1849 N N   . ASN A 238 ? 0.6569 0.4696 0.4121 0.2364  -0.0408 -0.0060 238 ASN A N   
1850 C CA  . ASN A 238 ? 0.6015 0.4253 0.3623 0.2335  -0.0366 -0.0023 238 ASN A CA  
1851 C C   . ASN A 238 ? 0.6107 0.4663 0.4003 0.2226  -0.0283 0.0079  238 ASN A C   
1852 O O   . ASN A 238 ? 0.5906 0.4529 0.3944 0.2061  -0.0281 0.0102  238 ASN A O   
1853 C CB  . ASN A 238 ? 0.6298 0.4285 0.3847 0.2212  -0.0469 -0.0082 238 ASN A CB  
1854 C CG  . ASN A 238 ? 0.7006 0.5090 0.4562 0.2194  -0.0427 -0.0058 238 ASN A CG  
1855 O OD1 . ASN A 238 ? 0.6925 0.5191 0.4436 0.2315  -0.0334 -0.0025 238 ASN A OD1 
1856 N ND2 . ASN A 238 ? 0.7153 0.5140 0.4783 0.2023  -0.0486 -0.0071 238 ASN A ND2 
1857 N N   . TYR A 239 ? 0.6016 0.4786 0.4008 0.2299  -0.0212 0.0137  239 TYR A N   
1858 C CA  . TYR A 239 ? 0.5646 0.4747 0.3914 0.2193  -0.0129 0.0231  239 TYR A CA  
1859 C C   . TYR A 239 ? 0.5831 0.5201 0.4118 0.2319  -0.0011 0.0294  239 TYR A C   
1860 O O   . TYR A 239 ? 0.5970 0.5302 0.4076 0.2517  0.0016  0.0275  239 TYR A O   
1861 C CB  . TYR A 239 ? 0.5051 0.4212 0.3433 0.2179  -0.0139 0.0260  239 TYR A CB  
1862 C CG  . TYR A 239 ? 0.5250 0.4321 0.3762 0.1983  -0.0210 0.0254  239 TYR A CG  
1863 C CD1 . TYR A 239 ? 0.5530 0.4283 0.3924 0.1920  -0.0315 0.0180  239 TYR A CD1 
1864 C CD2 . TYR A 239 ? 0.5065 0.4365 0.3815 0.1867  -0.0173 0.0323  239 TYR A CD2 
1865 C CE1 . TYR A 239 ? 0.5484 0.4158 0.3995 0.1748  -0.0373 0.0180  239 TYR A CE1 
1866 C CE2 . TYR A 239 ? 0.4884 0.4097 0.3737 0.1697  -0.0235 0.0317  239 TYR A CE2 
1867 C CZ  . TYR A 239 ? 0.5222 0.4127 0.3955 0.1641  -0.0329 0.0248  239 TYR A CZ  
1868 O OH  . TYR A 239 ? 0.5068 0.3891 0.3903 0.1479  -0.0382 0.0248  239 TYR A OH  
1869 N N   . GLU A 240 ? 0.5499 0.5137 0.4001 0.2209  0.0060  0.0369  240 GLU A N   
1870 C CA  . GLU A 240 ? 0.5301 0.5226 0.3861 0.2317  0.0179  0.0446  240 GLU A CA  
1871 C C   . GLU A 240 ? 0.5694 0.5771 0.4290 0.2456  0.0230  0.0492  240 GLU A C   
1872 O O   . GLU A 240 ? 0.4951 0.5052 0.3668 0.2389  0.0198  0.0506  240 GLU A O   
1873 C CB  . GLU A 240 ? 0.5535 0.5730 0.4365 0.2154  0.0238  0.0528  240 GLU A CB  
1874 C CG  . GLU A 240 ? 0.7301 0.7684 0.6139 0.2217  0.0332  0.0582  240 GLU A CG  
1875 C CD  . GLU A 240 ? 0.7997 0.8207 0.6720 0.2155  0.0291  0.0531  240 GLU A CD  
1876 O OE1 . GLU A 240 ? 0.7650 0.7638 0.6105 0.2282  0.0256  0.0462  240 GLU A OE1 
1877 O OE2 . GLU A 240 ? 0.9117 0.9408 0.8014 0.1979  0.0292  0.0561  240 GLU A OE2 
1878 N N   . PRO A 241 ? 0.5614 0.5798 0.4107 0.2640  0.0310  0.0518  241 PRO A N   
1879 C CA  . PRO A 241 ? 0.5839 0.6189 0.4384 0.2716  0.0367  0.0562  241 PRO A CA  
1880 C C   . PRO A 241 ? 0.6195 0.6876 0.5066 0.2612  0.0423  0.0671  241 PRO A C   
1881 O O   . PRO A 241 ? 0.5791 0.6674 0.4820 0.2544  0.0479  0.0736  241 PRO A O   
1882 C CB  . PRO A 241 ? 0.6663 0.7085 0.5047 0.2866  0.0453  0.0577  241 PRO A CB  
1883 C CG  . PRO A 241 ? 0.6090 0.6245 0.4229 0.2903  0.0400  0.0489  241 PRO A CG  
1884 C CD  . PRO A 241 ? 0.6348 0.6453 0.4627 0.2744  0.0340  0.0485  241 PRO A CD  
1885 N N   . LEU A 242 ? 0.6148 0.6889 0.5123 0.2595  0.0407  0.0692  242 LEU A N   
1886 C CA  . LEU A 242 ? 0.6210 0.7263 0.5488 0.2495  0.0452  0.0793  242 LEU A CA  
1887 C C   . LEU A 242 ? 0.5577 0.6896 0.4919 0.2572  0.0561  0.0876  242 LEU A C   
1888 O O   . LEU A 242 ? 0.5912 0.7179 0.5098 0.2707  0.0584  0.0860  242 LEU A O   
1889 C CB  . LEU A 242 ? 0.5072 0.6085 0.4434 0.2444  0.0385  0.0787  242 LEU A CB  
1890 C CG  . LEU A 242 ? 0.5091 0.6368 0.4761 0.2305  0.0395  0.0873  242 LEU A CG  
1891 C CD1 . LEU A 242 ? 0.4737 0.6031 0.4530 0.2125  0.0375  0.0875  242 LEU A CD1 
1892 C CD2 . LEU A 242 ? 0.5985 0.7206 0.5699 0.2277  0.0327  0.0864  242 LEU A CD2 
1893 N N   . THR A 243 ? 0.5426 0.7021 0.5000 0.2480  0.0624  0.0967  243 THR A N   
1894 C CA  . THR A 243 ? 0.6315 0.8159 0.5966 0.2529  0.0722  0.1060  243 THR A CA  
1895 C C   . THR A 243 ? 0.6100 0.8176 0.6019 0.2435  0.0729  0.1140  243 THR A C   
1896 O O   . THR A 243 ? 0.5408 0.7483 0.5471 0.2316  0.0665  0.1131  243 THR A O   
1897 C CB  . THR A 243 ? 0.5992 0.7964 0.5690 0.2494  0.0787  0.1112  243 THR A CB  
1898 O OG1 . THR A 243 ? 0.5675 0.7800 0.5639 0.2312  0.0776  0.1159  243 THR A OG1 
1899 C CG2 . THR A 243 ? 0.5378 0.7113 0.4831 0.2561  0.0763  0.1027  243 THR A CG2 
1900 N N   . GLN A 244 ? 0.5319 0.7589 0.5297 0.2490  0.0802  0.1224  244 GLN A N   
1901 C CA  . GLN A 244 ? 0.5797 0.8291 0.6031 0.2399  0.0808  0.1306  244 GLN A CA  
1902 C C   . GLN A 244 ? 0.5433 0.8076 0.5911 0.2211  0.0799  0.1354  244 GLN A C   
1903 O O   . GLN A 244 ? 0.5070 0.7819 0.5748 0.2096  0.0761  0.1384  244 GLN A O   
1904 C CB  . GLN A 244 ? 0.5607 0.8271 0.5854 0.2496  0.0888  0.1393  244 GLN A CB  
1905 C CG  . GLN A 244 ? 0.5546 0.8419 0.6042 0.2414  0.0885  0.1474  244 GLN A CG  
1906 C CD  . GLN A 244 ? 0.5822 0.8610 0.6326 0.2415  0.0814  0.1426  244 GLN A CD  
1907 O OE1 . GLN A 244 ? 0.6149 0.8759 0.6452 0.2541  0.0796  0.1361  244 GLN A OE1 
1908 N NE2 . GLN A 244 ? 0.5715 0.8619 0.6446 0.2273  0.0767  0.1459  244 GLN A NE2 
1909 N N   . ASP A 245 ? 0.5275 0.7922 0.5737 0.2173  0.0830  0.1361  245 ASP A N   
1910 C CA  . ASP A 245 ? 0.5247 0.8006 0.5931 0.1986  0.0814  0.1397  245 ASP A CA  
1911 C C   . ASP A 245 ? 0.5073 0.7713 0.5804 0.1882  0.0729  0.1327  245 ASP A C   
1912 O O   . ASP A 245 ? 0.4570 0.7309 0.5509 0.1728  0.0694  0.1353  245 ASP A O   
1913 C CB  . ASP A 245 ? 0.5945 0.8721 0.6594 0.1971  0.0861  0.1418  245 ASP A CB  
1914 C CG  . ASP A 245 ? 0.6840 0.9719 0.7715 0.1773  0.0844  0.1455  245 ASP A CG  
1915 O OD1 . ASP A 245 ? 0.5415 0.8439 0.6486 0.1675  0.0834  0.1514  245 ASP A OD1 
1916 O OD2 . ASP A 245 ? 0.8331 1.1132 0.9182 0.1713  0.0834  0.1420  245 ASP A OD2 
1917 N N   . HIS A 246 ? 0.4800 0.7209 0.5328 0.1966  0.0689  0.1238  246 HIS A N   
1918 C CA  . HIS A 246 ? 0.4638 0.6908 0.5190 0.1884  0.0600  0.1177  246 HIS A CA  
1919 C C   . HIS A 246 ? 0.4828 0.7151 0.5489 0.1850  0.0553  0.1192  246 HIS A C   
1920 O O   . HIS A 246 ? 0.4406 0.6785 0.5238 0.1706  0.0504  0.1203  246 HIS A O   
1921 C CB  . HIS A 246 ? 0.4546 0.6518 0.4827 0.1997  0.0555  0.1081  246 HIS A CB  
1922 C CG  . HIS A 246 ? 0.4928 0.6830 0.5113 0.2010  0.0582  0.1059  246 HIS A CG  
1923 N ND1 . HIS A 246 ? 0.4926 0.6582 0.4827 0.2136  0.0567  0.0983  246 HIS A ND1 
1924 C CD2 . HIS A 246 ? 0.4488 0.6507 0.4811 0.1888  0.0613  0.1096  246 HIS A CD2 
1925 C CE1 . HIS A 246 ? 0.4636 0.6266 0.4502 0.2089  0.0588  0.0974  246 HIS A CE1 
1926 N NE2 . HIS A 246 ? 0.5205 0.7052 0.5326 0.1939  0.0618  0.1043  246 HIS A NE2 
1927 N N   . VAL A 247 ? 0.4876 0.7182 0.5435 0.1980  0.0566  0.1193  247 VAL A N   
1928 C CA  . VAL A 247 ? 0.4155 0.6532 0.4824 0.1954  0.0527  0.1217  247 VAL A CA  
1929 C C   . VAL A 247 ? 0.3992 0.6620 0.4934 0.1804  0.0541  0.1299  247 VAL A C   
1930 O O   . VAL A 247 ? 0.3879 0.6545 0.4958 0.1694  0.0481  0.1304  247 VAL A O   
1931 C CB  . VAL A 247 ? 0.4940 0.7302 0.5479 0.2118  0.0561  0.1223  247 VAL A CB  
1932 C CG1 . VAL A 247 ? 0.4891 0.7383 0.5581 0.2085  0.0536  0.1270  247 VAL A CG1 
1933 C CG2 . VAL A 247 ? 0.4939 0.7005 0.5200 0.2244  0.0521  0.1126  247 VAL A CG2 
1934 N N   . ASP A 248 ? 0.4657 0.7442 0.5671 0.1792  0.0615  0.1362  248 ASP A N   
1935 C CA  . ASP A 248 ? 0.4572 0.7560 0.5826 0.1648  0.0621  0.1437  248 ASP A CA  
1936 C C   . ASP A 248 ? 0.3563 0.6529 0.4941 0.1468  0.0566  0.1411  248 ASP A C   
1937 O O   . ASP A 248 ? 0.4710 0.7752 0.6249 0.1346  0.0518  0.1429  248 ASP A O   
1938 C CB  . ASP A 248 ? 0.5155 0.8267 0.6431 0.1673  0.0703  0.1507  248 ASP A CB  
1939 C CG  . ASP A 248 ? 0.5728 0.8921 0.6948 0.1821  0.0758  0.1559  248 ASP A CG  
1940 O OD1 . ASP A 248 ? 0.5954 0.9162 0.7193 0.1862  0.0730  0.1560  248 ASP A OD1 
1941 O OD2 . ASP A 248 ? 0.5546 0.8787 0.6700 0.1897  0.0829  0.1602  248 ASP A OD2 
1942 N N   . ILE A 249 ? 0.4378 0.7235 0.5678 0.1449  0.0571  0.1368  249 ILE A N   
1943 C CA  . ILE A 249 ? 0.3369 0.6202 0.4782 0.1276  0.0528  0.1345  249 ILE A CA  
1944 C C   . ILE A 249 ? 0.3875 0.6628 0.5315 0.1221  0.0444  0.1302  249 ILE A C   
1945 O O   . ILE A 249 ? 0.3884 0.6659 0.5459 0.1057  0.0400  0.1297  249 ILE A O   
1946 C CB  . ILE A 249 ? 0.3451 0.6172 0.4755 0.1291  0.0552  0.1307  249 ILE A CB  
1947 C CG1 . ILE A 249 ? 0.4652 0.7472 0.5974 0.1290  0.0625  0.1361  249 ILE A CG1 
1948 C CG2 . ILE A 249 ? 0.3498 0.6150 0.4885 0.1135  0.0498  0.1268  249 ILE A CG2 
1949 C CD1 . ILE A 249 ? 0.4575 0.7292 0.5706 0.1412  0.0669  0.1333  249 ILE A CD1 
1950 N N   . LEU A 250 ? 0.3488 0.6123 0.4781 0.1354  0.0415  0.1267  250 LEU A N   
1951 C CA  . LEU A 250 ? 0.3861 0.6384 0.5143 0.1309  0.0328  0.1228  250 LEU A CA  
1952 C C   . LEU A 250 ? 0.4267 0.6945 0.5694 0.1275  0.0302  0.1277  250 LEU A C   
1953 O O   . LEU A 250 ? 0.3623 0.6227 0.5050 0.1230  0.0228  0.1253  250 LEU A O   
1954 C CB  . LEU A 250 ? 0.3682 0.5915 0.4683 0.1429  0.0295  0.1147  250 LEU A CB  
1955 C CG  . LEU A 250 ? 0.3238 0.5228 0.4050 0.1417  0.0291  0.1069  250 LEU A CG  
1956 C CD1 . LEU A 250 ? 0.2978 0.4707 0.3520 0.1564  0.0265  0.0999  250 LEU A CD1 
1957 C CD2 . LEU A 250 ? 0.3467 0.5318 0.4309 0.1214  0.0230  0.1018  250 LEU A CD2 
1958 N N   . GLY A 251 ? 0.4093 0.6945 0.5616 0.1280  0.0357  0.1338  251 GLY A N   
1959 C CA  . GLY A 251 ? 0.3653 0.6638 0.5303 0.1247  0.0332  0.1383  251 GLY A CA  
1960 C C   . GLY A 251 ? 0.3349 0.6349 0.5132 0.1081  0.0254  0.1373  251 GLY A C   
1961 O O   . GLY A 251 ? 0.3893 0.6871 0.5677 0.1086  0.0193  0.1365  251 GLY A O   
1962 N N   . PRO A 252 ? 0.4080 0.7104 0.5962 0.0929  0.0254  0.1369  252 PRO A N   
1963 C CA  . PRO A 252 ? 0.3911 0.6932 0.5901 0.0763  0.0181  0.1351  252 PRO A CA  
1964 C C   . PRO A 252 ? 0.3739 0.6633 0.5658 0.0759  0.0108  0.1305  252 PRO A C   
1965 O O   . PRO A 252 ? 0.4097 0.7010 0.6066 0.0706  0.0043  0.1308  252 PRO A O   
1966 C CB  . PRO A 252 ? 0.3685 0.6681 0.5726 0.0630  0.0203  0.1335  252 PRO A CB  
1967 C CG  . PRO A 252 ? 0.4082 0.7156 0.6117 0.0706  0.0282  0.1380  252 PRO A CG  
1968 C CD  . PRO A 252 ? 0.4260 0.7321 0.6163 0.0900  0.0320  0.1388  252 PRO A CD  
1969 N N   . LEU A 253 ? 0.3293 0.6013 0.5066 0.0799  0.0112  0.1255  253 LEU A N   
1970 C CA  . LEU A 253 ? 0.3098 0.5540 0.4684 0.0763  0.0043  0.1172  253 LEU A CA  
1971 C C   . LEU A 253 ? 0.2889 0.5300 0.4390 0.0887  0.0010  0.1180  253 LEU A C   
1972 O O   . LEU A 253 ? 0.3055 0.5361 0.4512 0.0832  -0.0059 0.1152  253 LEU A O   
1973 C CB  . LEU A 253 ? 0.2705 0.4894 0.4094 0.0777  0.0058  0.1098  253 LEU A CB  
1974 C CG  . LEU A 253 ? 0.2952 0.5130 0.4411 0.0633  0.0075  0.1080  253 LEU A CG  
1975 C CD1 . LEU A 253 ? 0.2531 0.4467 0.3798 0.0657  0.0087  0.1012  253 LEU A CD1 
1976 C CD2 . LEU A 253 ? 0.2464 0.4594 0.3988 0.0463  0.0014  0.1053  253 LEU A CD2 
1977 N N   . SER A 254 ? 0.3165 0.5661 0.4637 0.1060  0.0061  0.1219  254 SER A N   
1978 C CA  . SER A 254 ? 0.3184 0.5679 0.4598 0.1189  0.0037  0.1238  254 SER A CA  
1979 C C   . SER A 254 ? 0.4113 0.6809 0.5718 0.1126  -0.0007 0.1298  254 SER A C   
1980 O O   . SER A 254 ? 0.4190 0.6802 0.5733 0.1138  -0.0069 0.1284  254 SER A O   
1981 C CB  . SER A 254 ? 0.3126 0.5713 0.4503 0.1375  0.0114  0.1276  254 SER A CB  
1982 O OG  . SER A 254 ? 0.4229 0.6740 0.5494 0.1501  0.0094  0.1269  254 SER A OG  
1983 N N   . ALA A 255 ? 0.3887 0.6779 0.5676 0.1031  0.0024  0.1342  255 ALA A N   
1984 C CA  . ALA A 255 ? 0.3957 0.6982 0.5889 0.0946  -0.0019 0.1378  255 ALA A CA  
1985 C C   . ALA A 255 ? 0.3955 0.6913 0.5909 0.0815  -0.0109 0.1348  255 ALA A C   
1986 O O   . ALA A 255 ? 0.4359 0.7316 0.6313 0.0814  -0.0174 0.1356  255 ALA A O   
1987 C CB  . ALA A 255 ? 0.3722 0.6909 0.5809 0.0863  0.0030  0.1419  255 ALA A CB  
1988 N N   . GLN A 256 ? 0.3331 0.6221 0.5292 0.0704  -0.0114 0.1313  256 GLN A N   
1989 C CA  . GLN A 256 ? 0.3949 0.6719 0.5889 0.0549  -0.0187 0.1263  256 GLN A CA  
1990 C C   . GLN A 256 ? 0.4117 0.6623 0.5833 0.0582  -0.0236 0.1200  256 GLN A C   
1991 O O   . GLN A 256 ? 0.5111 0.7556 0.6811 0.0493  -0.0304 0.1180  256 GLN A O   
1992 C CB  . GLN A 256 ? 0.3994 0.6700 0.5959 0.0411  -0.0167 0.1222  256 GLN A CB  
1993 C CG  . GLN A 256 ? 0.3804 0.6259 0.5630 0.0292  -0.0218 0.1140  256 GLN A CG  
1994 C CD  . GLN A 256 ? 0.4913 0.7291 0.6749 0.0179  -0.0187 0.1100  256 GLN A CD  
1995 O OE1 . GLN A 256 ? 0.4968 0.7402 0.6840 0.0217  -0.0123 0.1116  256 GLN A OE1 
1996 N NE2 . GLN A 256 ? 0.4780 0.7027 0.6581 0.0042  -0.0230 0.1049  256 GLN A NE2 
1997 N N   . THR A 257 ? 0.4122 0.6470 0.5664 0.0711  -0.0207 0.1171  257 THR A N   
1998 C CA  . THR A 257 ? 0.3289 0.5391 0.4630 0.0752  -0.0257 0.1121  257 THR A CA  
1999 C C   . THR A 257 ? 0.3700 0.5861 0.5020 0.0899  -0.0273 0.1163  257 THR A C   
2000 O O   . THR A 257 ? 0.3818 0.5812 0.5009 0.0918  -0.0327 0.1135  257 THR A O   
2001 C CB  . THR A 257 ? 0.3759 0.5603 0.4904 0.0793  -0.0232 0.1052  257 THR A CB  
2002 O OG1 . THR A 257 ? 0.3430 0.5335 0.4548 0.0949  -0.0170 0.1075  257 THR A OG1 
2003 C CG2 . THR A 257 ? 0.2987 0.4758 0.4149 0.0647  -0.0219 0.1011  257 THR A CG2 
2004 N N   . GLY A 258 ? 0.3548 0.5939 0.4991 0.1007  -0.0225 0.1232  258 GLY A N   
2005 C CA  . GLY A 258 ? 0.4168 0.6617 0.5592 0.1161  -0.0231 0.1275  258 GLY A CA  
2006 C C   . GLY A 258 ? 0.4511 0.6738 0.5714 0.1310  -0.0213 0.1229  258 GLY A C   
2007 O O   . GLY A 258 ? 0.4385 0.6580 0.5526 0.1424  -0.0237 0.1245  258 GLY A O   
2008 N N   . ILE A 259 ? 0.3609 0.5671 0.4688 0.1311  -0.0177 0.1171  259 ILE A N   
2009 C CA  . ILE A 259 ? 0.3953 0.5798 0.4819 0.1455  -0.0161 0.1123  259 ILE A CA  
2010 C C   . ILE A 259 ? 0.3656 0.5636 0.4551 0.1569  -0.0073 0.1152  259 ILE A C   
2011 O O   . ILE A 259 ? 0.3544 0.5570 0.4490 0.1496  -0.0033 0.1146  259 ILE A O   
2012 C CB  . ILE A 259 ? 0.4135 0.5666 0.4822 0.1374  -0.0197 0.1032  259 ILE A CB  
2013 C CG1 . ILE A 259 ? 0.4573 0.5950 0.5202 0.1292  -0.0279 0.1007  259 ILE A CG1 
2014 C CG2 . ILE A 259 ? 0.3482 0.4804 0.3962 0.1519  -0.0177 0.0981  259 ILE A CG2 
2015 C CD1 . ILE A 259 ? 0.4612 0.5894 0.5254 0.1105  -0.0307 0.0968  259 ILE A CD1 
2016 N N   . ALA A 260 ? 0.3683 0.5722 0.4544 0.1741  -0.0038 0.1183  260 ALA A N   
2017 C CA  . ALA A 260 ? 0.3662 0.5792 0.4514 0.1827  0.0056  0.1194  260 ALA A CA  
2018 C C   . ALA A 260 ? 0.3735 0.5662 0.4409 0.1872  0.0074  0.1130  260 ALA A C   
2019 O O   . ALA A 260 ? 0.3678 0.5336 0.4177 0.1880  0.0016  0.1063  260 ALA A O   
2020 C CB  . ALA A 260 ? 0.3829 0.5977 0.4618 0.1972  0.0090  0.1207  260 ALA A CB  
2021 N N   . VAL A 261 ? 0.3976 0.4665 0.3526 0.1075  0.0215  0.0785  261 VAL A N   
2022 C CA  . VAL A 261 ? 0.4270 0.4821 0.3803 0.1085  0.0187  0.0730  261 VAL A CA  
2023 C C   . VAL A 261 ? 0.4398 0.4826 0.3893 0.1164  0.0166  0.0709  261 VAL A C   
2024 O O   . VAL A 261 ? 0.3924 0.4219 0.3431 0.1153  0.0137  0.0672  261 VAL A O   
2025 C CB  . VAL A 261 ? 0.4452 0.5043 0.3950 0.1092  0.0187  0.0722  261 VAL A CB  
2026 C CG1 . VAL A 261 ? 0.4155 0.4602 0.3622 0.1123  0.0156  0.0669  261 VAL A CG1 
2027 C CG2 . VAL A 261 ? 0.4504 0.5170 0.4040 0.1002  0.0192  0.0731  261 VAL A CG2 
2028 N N   . LEU A 262 ? 0.4758 0.5229 0.4206 0.1246  0.0178  0.0735  262 LEU A N   
2029 C CA  . LEU A 262 ? 0.4777 0.5117 0.4178 0.1328  0.0152  0.0712  262 LEU A CA  
2030 C C   . LEU A 262 ? 0.4352 0.4616 0.3789 0.1308  0.0136  0.0719  262 LEU A C   
2031 O O   . LEU A 262 ? 0.5200 0.5312 0.4612 0.1342  0.0100  0.0689  262 LEU A O   
2032 C CB  . LEU A 262 ? 0.5396 0.5808 0.4734 0.1428  0.0170  0.0737  262 LEU A CB  
2033 C CG  . LEU A 262 ? 0.6017 0.6482 0.5306 0.1459  0.0179  0.0727  262 LEU A CG  
2034 C CD1 . LEU A 262 ? 0.6610 0.7197 0.5849 0.1551  0.0206  0.0764  262 LEU A CD1 
2035 C CD2 . LEU A 262 ? 0.6780 0.7083 0.6023 0.1489  0.0143  0.0667  262 LEU A CD2 
2036 N N   . ASP A 263 ? 0.4382 0.4745 0.3876 0.1249  0.0157  0.0757  263 ASP A N   
2037 C CA  . ASP A 263 ? 0.4944 0.5243 0.4483 0.1210  0.0141  0.0763  263 ASP A CA  
2038 C C   . ASP A 263 ? 0.4646 0.4836 0.4220 0.1149  0.0113  0.0721  263 ASP A C   
2039 O O   . ASP A 263 ? 0.4465 0.4530 0.4043 0.1152  0.0079  0.0707  263 ASP A O   
2040 C CB  . ASP A 263 ? 0.4855 0.5294 0.4448 0.1151  0.0172  0.0811  263 ASP A CB  
2041 C CG  . ASP A 263 ? 0.6852 0.7378 0.6422 0.1211  0.0191  0.0860  263 ASP A CG  
2042 O OD1 . ASP A 263 ? 0.6803 0.7365 0.6321 0.1286  0.0200  0.0864  263 ASP A OD1 
2043 O OD2 . ASP A 263 ? 0.6591 0.7153 0.6197 0.1185  0.0196  0.0895  263 ASP A OD2 
2044 N N   . MET A 264 ? 0.3950 0.4187 0.3550 0.1091  0.0125  0.0703  264 MET A N   
2045 C CA  . MET A 264 ? 0.3595 0.3740 0.3231 0.1037  0.0100  0.0665  264 MET A CA  
2046 C C   . MET A 264 ? 0.4130 0.4125 0.3717 0.1090  0.0062  0.0625  264 MET A C   
2047 O O   . MET A 264 ? 0.4448 0.4333 0.4058 0.1066  0.0029  0.0602  264 MET A O   
2048 C CB  . MET A 264 ? 0.3326 0.3546 0.2995 0.0973  0.0117  0.0651  264 MET A CB  
2049 C CG  . MET A 264 ? 0.3174 0.3311 0.2886 0.0919  0.0093  0.0613  264 MET A CG  
2050 S SD  . MET A 264 ? 0.3408 0.3580 0.3191 0.0859  0.0099  0.0639  264 MET A SD  
2051 C CE  . MET A 264 ? 0.3184 0.3515 0.2993 0.0801  0.0140  0.0658  264 MET A CE  
2052 N N   . CYS A 265 ? 0.4462 0.4455 0.3982 0.1162  0.0064  0.0617  265 CYS A N   
2053 C CA  . CYS A 265 ? 0.4015 0.3861 0.3475 0.1221  0.0026  0.0580  265 CYS A CA  
2054 C C   . CYS A 265 ? 0.4817 0.4544 0.4258 0.1259  -0.0007 0.0584  265 CYS A C   
2055 O O   . CYS A 265 ? 0.4256 0.3834 0.3679 0.1265  -0.0051 0.0552  265 CYS A O   
2056 C CB  . CYS A 265 ? 0.4695 0.4576 0.4080 0.1299  0.0039  0.0574  265 CYS A CB  
2057 S SG  . CYS A 265 ? 0.4584 0.4577 0.3977 0.1257  0.0064  0.0569  265 CYS A SG  
2058 N N   . ALA A 266 ? 0.4762 0.4548 0.4204 0.1284  0.0009  0.0624  266 ALA A N   
2059 C CA  . ALA A 266 ? 0.4936 0.4607 0.4366 0.1310  -0.0027 0.0633  266 ALA A CA  
2060 C C   . ALA A 266 ? 0.5193 0.4802 0.4691 0.1223  -0.0054 0.0631  266 ALA A C   
2061 O O   . ALA A 266 ? 0.5105 0.4564 0.4586 0.1231  -0.0104 0.0617  266 ALA A O   
2062 C CB  . ALA A 266 ? 0.4972 0.4736 0.4402 0.1342  -0.0002 0.0682  266 ALA A CB  
2063 N N   . SER A 267 ? 0.4147 0.3873 0.3720 0.1141  -0.0023 0.0646  267 SER A N   
2064 C CA  . SER A 267 ? 0.4266 0.3956 0.3908 0.1059  -0.0043 0.0643  267 SER A CA  
2065 C C   . SER A 267 ? 0.4213 0.3780 0.3845 0.1052  -0.0081 0.0598  267 SER A C   
2066 O O   . SER A 267 ? 0.4501 0.3963 0.4152 0.1025  -0.0123 0.0595  267 SER A O   
2067 C CB  . SER A 267 ? 0.4857 0.4696 0.4570 0.0983  0.0000  0.0656  267 SER A CB  
2068 O OG  . SER A 267 ? 0.4608 0.4545 0.4344 0.0971  0.0025  0.0702  267 SER A OG  
2069 N N   . LEU A 268 ? 0.4098 0.3681 0.3703 0.1069  -0.0068 0.0566  268 LEU A N   
2070 C CA  . LEU A 268 ? 0.4217 0.3692 0.3813 0.1059  -0.0103 0.0524  268 LEU A CA  
2071 C C   . LEU A 268 ? 0.4764 0.4070 0.4292 0.1119  -0.0156 0.0507  268 LEU A C   
2072 O O   . LEU A 268 ? 0.4425 0.3616 0.3963 0.1092  -0.0201 0.0489  268 LEU A O   
2073 C CB  . LEU A 268 ? 0.3679 0.3211 0.3254 0.1070  -0.0079 0.0498  268 LEU A CB  
2074 C CG  . LEU A 268 ? 0.4108 0.3539 0.3671 0.1062  -0.0113 0.0454  268 LEU A CG  
2075 C CD1 . LEU A 268 ? 0.3697 0.3091 0.3336 0.0988  -0.0136 0.0448  268 LEU A CD1 
2076 C CD2 . LEU A 268 ? 0.4071 0.3579 0.3624 0.1059  -0.0087 0.0437  268 LEU A CD2 
2077 N N   . LYS A 269 ? 0.4828 0.4114 0.4281 0.1203  -0.0153 0.0514  269 LYS A N   
2078 C CA  . LYS A 269 ? 0.5164 0.4278 0.4540 0.1267  -0.0207 0.0497  269 LYS A CA  
2079 C C   . LYS A 269 ? 0.4975 0.3995 0.4387 0.1224  -0.0251 0.0518  269 LYS A C   
2080 O O   . LYS A 269 ? 0.5140 0.4009 0.4531 0.1217  -0.0308 0.0498  269 LYS A O   
2081 C CB  . LYS A 269 ? 0.6390 0.5518 0.5685 0.1368  -0.0192 0.0504  269 LYS A CB  
2082 C CG  . LYS A 269 ? 0.7271 0.6211 0.6476 0.1445  -0.0250 0.0485  269 LYS A CG  
2083 C CD  . LYS A 269 ? 0.8030 0.6997 0.7163 0.1548  -0.0233 0.0498  269 LYS A CD  
2084 C CE  . LYS A 269 ? 0.9231 0.8097 0.8249 0.1650  -0.0255 0.0454  269 LYS A CE  
2085 N NZ  . LYS A 269 ? 0.9524 0.8319 0.8461 0.1742  -0.0273 0.0451  269 LYS A NZ  
2086 N N   . GLU A 270 ? 0.5067 0.4179 0.4532 0.1192  -0.0228 0.0563  270 GLU A N   
2087 C CA  . GLU A 270 ? 0.5725 0.4766 0.5232 0.1140  -0.0270 0.0591  270 GLU A CA  
2088 C C   . GLU A 270 ? 0.5710 0.4730 0.5285 0.1055  -0.0292 0.0580  270 GLU A C   
2089 O O   . GLU A 270 ? 0.5380 0.4277 0.4959 0.1028  -0.0349 0.0587  270 GLU A O   
2090 C CB  . GLU A 270 ? 0.5726 0.4893 0.5287 0.1111  -0.0236 0.0643  270 GLU A CB  
2091 C CG  . GLU A 270 ? 0.7948 0.7115 0.7444 0.1196  -0.0227 0.0660  270 GLU A CG  
2092 C CD  . GLU A 270 ? 0.9755 0.8723 0.9165 0.1266  -0.0293 0.0645  270 GLU A CD  
2093 O OE1 . GLU A 270 ? 0.9327 0.8258 0.8652 0.1363  -0.0290 0.0622  270 GLU A OE1 
2094 O OE2 . GLU A 270 ? 0.9675 0.8527 0.9102 0.1223  -0.0349 0.0656  270 GLU A OE2 
2095 N N   . LEU A 271 ? 0.4777 0.3917 0.4406 0.1010  -0.0249 0.0567  271 LEU A N   
2096 C CA  . LEU A 271 ? 0.4724 0.3859 0.4423 0.0933  -0.0266 0.0557  271 LEU A CA  
2097 C C   . LEU A 271 ? 0.5356 0.4336 0.5009 0.0952  -0.0319 0.0519  271 LEU A C   
2098 O O   . LEU A 271 ? 0.5163 0.4075 0.4854 0.0901  -0.0362 0.0523  271 LEU A O   
2099 C CB  . LEU A 271 ? 0.4616 0.3905 0.4373 0.0891  -0.0210 0.0547  271 LEU A CB  
2100 C CG  . LEU A 271 ? 0.4619 0.4061 0.4442 0.0842  -0.0164 0.0584  271 LEU A CG  
2101 C CD1 . LEU A 271 ? 0.4293 0.3859 0.4157 0.0807  -0.0118 0.0564  271 LEU A CD1 
2102 C CD2 . LEU A 271 ? 0.4725 0.4163 0.4614 0.0778  -0.0189 0.0617  271 LEU A CD2 
2103 N N   . LEU A 272 ? 0.4997 0.3925 0.4565 0.1026  -0.0318 0.0486  272 LEU A N   
2104 C CA  . LEU A 272 ? 0.5482 0.4262 0.4996 0.1050  -0.0368 0.0448  272 LEU A CA  
2105 C C   . LEU A 272 ? 0.6222 0.4827 0.5681 0.1076  -0.0437 0.0455  272 LEU A C   
2106 O O   . LEU A 272 ? 0.6460 0.4935 0.5905 0.1057  -0.0494 0.0438  272 LEU A O   
2107 C CB  . LEU A 272 ? 0.5382 0.4170 0.4819 0.1123  -0.0345 0.0412  272 LEU A CB  
2108 C CG  . LEU A 272 ? 0.5421 0.4346 0.4907 0.1088  -0.0295 0.0399  272 LEU A CG  
2109 C CD1 . LEU A 272 ? 0.5497 0.4469 0.4911 0.1158  -0.0263 0.0382  272 LEU A CD1 
2110 C CD2 . LEU A 272 ? 0.5140 0.4014 0.4666 0.1035  -0.0325 0.0374  272 LEU A CD2 
2111 N N   . GLN A 273 ? 0.6756 0.5350 0.6180 0.1118  -0.0436 0.0481  273 GLN A N   
2112 C CA  . GLN A 273 ? 0.7139 0.5554 0.6497 0.1152  -0.0506 0.0487  273 GLN A CA  
2113 C C   . GLN A 273 ? 0.7608 0.5992 0.7037 0.1069  -0.0547 0.0532  273 GLN A C   
2114 O O   . GLN A 273 ? 0.7469 0.5684 0.6860 0.1065  -0.0622 0.0533  273 GLN A O   
2115 C CB  . GLN A 273 ? 0.6466 0.4880 0.5751 0.1243  -0.0489 0.0496  273 GLN A CB  
2116 C CG  . GLN A 273 ? 0.6975 0.5341 0.6154 0.1343  -0.0482 0.0449  273 GLN A CG  
2117 C CD  . GLN A 273 ? 0.7798 0.6211 0.6918 0.1436  -0.0451 0.0460  273 GLN A CD  
2118 O OE1 . GLN A 273 ? 0.8116 0.6505 0.7147 0.1527  -0.0442 0.0427  273 GLN A OE1 
2119 N NE2 . GLN A 273 ? 0.7986 0.6474 0.7155 0.1414  -0.0433 0.0507  273 GLN A NE2 
2120 N N   . ASN A 274 ? 0.6936 0.5482 0.6466 0.1001  -0.0502 0.0569  274 ASN A N   
2121 C CA  . ASN A 274 ? 0.7201 0.5745 0.6802 0.0922  -0.0535 0.0618  274 ASN A CA  
2122 C C   . ASN A 274 ? 0.7136 0.5785 0.6844 0.0827  -0.0519 0.0627  274 ASN A C   
2123 O O   . ASN A 274 ? 0.6871 0.5527 0.6640 0.0756  -0.0549 0.0670  274 ASN A O   
2124 C CB  . ASN A 274 ? 0.7647 0.6289 0.7271 0.0923  -0.0502 0.0664  274 ASN A CB  
2125 C CG  . ASN A 274 ? 0.8943 0.7494 0.8468 0.1021  -0.0516 0.0660  274 ASN A CG  
2126 O OD1 . ASN A 274 ? 0.9162 0.7823 0.8682 0.1059  -0.0463 0.0672  274 ASN A OD1 
2127 N ND2 . ASN A 274 ? 0.9461 0.7809 0.8901 0.1064  -0.0589 0.0643  274 ASN A ND2 
2128 N N   . GLY A 275 ? 0.6295 0.5028 0.6025 0.0824  -0.0476 0.0591  275 GLY A N   
2129 C CA  . GLY A 275 ? 0.6391 0.5234 0.6222 0.0742  -0.0457 0.0598  275 GLY A CA  
2130 C C   . GLY A 275 ? 0.5868 0.4888 0.5775 0.0699  -0.0401 0.0634  275 GLY A C   
2131 O O   . GLY A 275 ? 0.6414 0.5487 0.6297 0.0732  -0.0368 0.0650  275 GLY A O   
2132 N N   . MET A 276 ? 0.6462 0.5577 0.6461 0.0624  -0.0392 0.0648  276 MET A N   
2133 C CA  . MET A 276 ? 0.6955 0.6246 0.7027 0.0580  -0.0337 0.0677  276 MET A CA  
2134 C C   . MET A 276 ? 0.8170 0.7483 0.8294 0.0521  -0.0364 0.0736  276 MET A C   
2135 O O   . MET A 276 ? 0.7105 0.6552 0.7274 0.0492  -0.0323 0.0767  276 MET A O   
2136 C CB  . MET A 276 ? 0.6632 0.6038 0.6769 0.0542  -0.0299 0.0650  276 MET A CB  
2137 C CG  . MET A 276 ? 0.6062 0.5485 0.6158 0.0590  -0.0261 0.0599  276 MET A CG  
2138 S SD  . MET A 276 ? 0.6465 0.6059 0.6635 0.0549  -0.0202 0.0578  276 MET A SD  
2139 C CE  . MET A 276 ? 0.4996 0.4541 0.5099 0.0606  -0.0189 0.0522  276 MET A CE  
2140 N N   . ASN A 277 ? 0.8828 0.8014 0.8948 0.0498  -0.0435 0.0755  277 ASN A N   
2141 C CA  . ASN A 277 ? 0.9207 0.8404 0.9378 0.0434  -0.0472 0.0818  277 ASN A CA  
2142 C C   . ASN A 277 ? 0.8247 0.7640 0.8523 0.0363  -0.0426 0.0842  277 ASN A C   
2143 O O   . ASN A 277 ? 0.8708 0.8212 0.9018 0.0338  -0.0396 0.0881  277 ASN A O   
2144 C CB  . ASN A 277 ? 0.9550 0.8699 0.9673 0.0461  -0.0486 0.0855  277 ASN A CB  
2145 C CG  . ASN A 277 ? 1.1324 1.0309 1.1419 0.0443  -0.0575 0.0892  277 ASN A CG  
2146 O OD1 . ASN A 277 ? 1.1475 1.0302 1.1520 0.0463  -0.0632 0.0867  277 ASN A OD1 
2147 N ND2 . ASN A 277 ? 1.1346 1.0362 1.1470 0.0402  -0.0593 0.0955  277 ASN A ND2 
2148 N N   . GLY A 278 ? 0.7752 0.7188 0.8078 0.0336  -0.0422 0.0817  278 GLY A N   
2149 C CA  . GLY A 278 ? 0.7712 0.7324 0.8136 0.0273  -0.0387 0.0838  278 GLY A CA  
2150 C C   . GLY A 278 ? 0.7075 0.6852 0.7521 0.0282  -0.0306 0.0821  278 GLY A C   
2151 O O   . GLY A 278 ? 0.6972 0.6900 0.7492 0.0234  -0.0275 0.0840  278 GLY A O   
2152 N N   . ARG A 279 ? 0.6841 0.6594 0.7221 0.0341  -0.0273 0.0789  279 ARG A N   
2153 C CA  . ARG A 279 ? 0.5981 0.5875 0.6369 0.0350  -0.0202 0.0771  279 ARG A CA  
2154 C C   . ARG A 279 ? 0.5138 0.5037 0.5514 0.0380  -0.0175 0.0708  279 ARG A C   
2155 O O   . ARG A 279 ? 0.4891 0.4674 0.5235 0.0407  -0.0209 0.0678  279 ARG A O   
2156 C CB  . ARG A 279 ? 0.5596 0.5471 0.5922 0.0392  -0.0186 0.0785  279 ARG A CB  
2157 C CG  . ARG A 279 ? 0.5977 0.5907 0.6329 0.0356  -0.0190 0.0849  279 ARG A CG  
2158 C CD  . ARG A 279 ? 0.5630 0.5554 0.5922 0.0403  -0.0169 0.0858  279 ARG A CD  
2159 N NE  . ARG A 279 ? 0.6532 0.6282 0.6750 0.0461  -0.0217 0.0849  279 ARG A NE  
2160 C CZ  . ARG A 279 ? 0.6553 0.6249 0.6713 0.0507  -0.0224 0.0868  279 ARG A CZ  
2161 N NH1 . ARG A 279 ? 0.6141 0.5943 0.6313 0.0498  -0.0189 0.0903  279 ARG A NH1 
2162 N NH2 . ARG A 279 ? 0.6114 0.5648 0.6201 0.0567  -0.0268 0.0850  279 ARG A NH2 
2163 N N   . THR A 280 ? 0.4253 0.4285 0.4652 0.0374  -0.0118 0.0689  280 THR A N   
2164 C CA  . THR A 280 ? 0.3984 0.4024 0.4372 0.0397  -0.0095 0.0633  280 THR A CA  
2165 C C   . THR A 280 ? 0.3260 0.3347 0.3599 0.0429  -0.0050 0.0615  280 THR A C   
2166 O O   . THR A 280 ? 0.3198 0.3350 0.3529 0.0425  -0.0026 0.0645  280 THR A O   
2167 C CB  . THR A 280 ? 0.4098 0.4247 0.4561 0.0358  -0.0076 0.0619  280 THR A CB  
2168 O OG1 . THR A 280 ? 0.3743 0.4036 0.4241 0.0327  -0.0035 0.0643  280 THR A OG1 
2169 C CG2 . THR A 280 ? 0.4044 0.4152 0.4560 0.0324  -0.0124 0.0639  280 THR A CG2 
2170 N N   . ILE A 281 ? 0.2976 0.3030 0.3282 0.0460  -0.0042 0.0568  281 ILE A N   
2171 C CA  . ILE A 281 ? 0.3092 0.3195 0.3355 0.0484  -0.0003 0.0549  281 ILE A CA  
2172 C C   . ILE A 281 ? 0.3226 0.3380 0.3514 0.0471  0.0016  0.0506  281 ILE A C   
2173 O O   . ILE A 281 ? 0.2946 0.3033 0.3238 0.0481  -0.0008 0.0474  281 ILE A O   
2174 C CB  . ILE A 281 ? 0.3096 0.3102 0.3282 0.0540  -0.0017 0.0539  281 ILE A CB  
2175 C CG1 . ILE A 281 ? 0.3119 0.3050 0.3275 0.0562  -0.0045 0.0576  281 ILE A CG1 
2176 C CG2 . ILE A 281 ? 0.2894 0.2966 0.3041 0.0558  0.0021  0.0527  281 ILE A CG2 
2177 C CD1 . ILE A 281 ? 0.3388 0.3231 0.3462 0.0627  -0.0056 0.0566  281 ILE A CD1 
2178 N N   . LEU A 282 ? 0.2965 0.3231 0.3265 0.0451  0.0055  0.0504  282 LEU A N   
2179 C CA  . LEU A 282 ? 0.3072 0.3386 0.3391 0.0441  0.0072  0.0462  282 LEU A CA  
2180 C C   . LEU A 282 ? 0.3506 0.3799 0.3882 0.0428  0.0049  0.0443  282 LEU A C   
2181 O O   . LEU A 282 ? 0.3197 0.3451 0.3573 0.0440  0.0037  0.0403  282 LEU A O   
2182 C CB  . LEU A 282 ? 0.2730 0.2996 0.2990 0.0471  0.0072  0.0430  282 LEU A CB  
2183 C CG  . LEU A 282 ? 0.3019 0.3343 0.3232 0.0475  0.0101  0.0448  282 LEU A CG  
2184 C CD1 . LEU A 282 ? 0.2918 0.3191 0.3069 0.0505  0.0095  0.0432  282 LEU A CD1 
2185 C CD2 . LEU A 282 ? 0.3001 0.3435 0.3234 0.0442  0.0133  0.0442  282 LEU A CD2 
2186 N N   . GLY A 283 ? 0.3438 0.3762 0.3865 0.0400  0.0039  0.0477  283 GLY A N   
2187 C CA  . GLY A 283 ? 0.3795 0.4126 0.4286 0.0381  0.0019  0.0469  283 GLY A CA  
2188 C C   . GLY A 283 ? 0.4444 0.4648 0.4928 0.0397  -0.0029 0.0460  283 GLY A C   
2189 O O   . GLY A 283 ? 0.4953 0.5160 0.5488 0.0384  -0.0047 0.0448  283 GLY A O   
2190 N N   . SER A 284 ? 0.3395 0.3491 0.3816 0.0426  -0.0050 0.0465  284 SER A N   
2191 C CA  . SER A 284 ? 0.3079 0.3044 0.3481 0.0444  -0.0097 0.0453  284 SER A CA  
2192 C C   . SER A 284 ? 0.3519 0.3399 0.3893 0.0448  -0.0131 0.0493  284 SER A C   
2193 O O   . SER A 284 ? 0.3527 0.3424 0.3869 0.0457  -0.0116 0.0519  284 SER A O   
2194 C CB  . SER A 284 ? 0.3458 0.3355 0.3797 0.0485  -0.0097 0.0412  284 SER A CB  
2195 O OG  . SER A 284 ? 0.4391 0.4155 0.4698 0.0506  -0.0143 0.0404  284 SER A OG  
2196 N N   . ALA A 285 ? 0.3536 0.3321 0.3920 0.0440  -0.0182 0.0498  285 ALA A N   
2197 C CA  . ALA A 285 ? 0.3555 0.3234 0.3905 0.0445  -0.0227 0.0532  285 ALA A CA  
2198 C C   . ALA A 285 ? 0.3934 0.3462 0.4199 0.0497  -0.0258 0.0505  285 ALA A C   
2199 O O   . ALA A 285 ? 0.4209 0.3622 0.4433 0.0509  -0.0303 0.0524  285 ALA A O   
2200 C CB  . ALA A 285 ? 0.3710 0.3381 0.4125 0.0394  -0.0270 0.0566  285 ALA A CB  
2201 N N   . LEU A 286 ? 0.3769 0.3294 0.4003 0.0529  -0.0238 0.0461  286 LEU A N   
2202 C CA  . LEU A 286 ? 0.3914 0.3320 0.4060 0.0583  -0.0259 0.0436  286 LEU A CA  
2203 C C   . LEU A 286 ? 0.4004 0.3473 0.4108 0.0617  -0.0210 0.0417  286 LEU A C   
2204 O O   . LEU A 286 ? 0.4133 0.3724 0.4276 0.0595  -0.0166 0.0418  286 LEU A O   
2205 C CB  . LEU A 286 ? 0.4429 0.3745 0.4572 0.0585  -0.0298 0.0404  286 LEU A CB  
2206 C CG  . LEU A 286 ? 0.4661 0.4055 0.4872 0.0556  -0.0282 0.0380  286 LEU A CG  
2207 C CD1 . LEU A 286 ? 0.4711 0.4165 0.4894 0.0581  -0.0238 0.0349  286 LEU A CD1 
2208 C CD2 . LEU A 286 ? 0.4391 0.3686 0.4607 0.0550  -0.0334 0.0362  286 LEU A CD2 
2209 N N   . LEU A 287 ? 0.3649 0.3038 0.3672 0.0671  -0.0220 0.0401  287 LEU A N   
2210 C CA  . LEU A 287 ? 0.3416 0.2867 0.3394 0.0704  -0.0178 0.0392  287 LEU A CA  
2211 C C   . LEU A 287 ? 0.3776 0.3247 0.3759 0.0699  -0.0170 0.0355  287 LEU A C   
2212 O O   . LEU A 287 ? 0.3897 0.3276 0.3854 0.0716  -0.0202 0.0330  287 LEU A O   
2213 C CB  . LEU A 287 ? 0.3742 0.3113 0.3629 0.0768  -0.0190 0.0396  287 LEU A CB  
2214 C CG  . LEU A 287 ? 0.3556 0.2901 0.3434 0.0776  -0.0202 0.0433  287 LEU A CG  
2215 C CD1 . LEU A 287 ? 0.4368 0.3593 0.4154 0.0846  -0.0232 0.0429  287 LEU A CD1 
2216 C CD2 . LEU A 287 ? 0.3690 0.3168 0.3595 0.0762  -0.0153 0.0464  287 LEU A CD2 
2217 N N   . GLU A 288 ? 0.3258 0.2841 0.3273 0.0675  -0.0130 0.0352  288 GLU A N   
2218 C CA  . GLU A 288 ? 0.2991 0.2595 0.3024 0.0661  -0.0126 0.0319  288 GLU A CA  
2219 C C   . GLU A 288 ? 0.2723 0.2322 0.2686 0.0697  -0.0116 0.0309  288 GLU A C   
2220 O O   . GLU A 288 ? 0.2992 0.2652 0.2922 0.0712  -0.0087 0.0330  288 GLU A O   
2221 C CB  . GLU A 288 ? 0.3044 0.2764 0.3136 0.0620  -0.0092 0.0320  288 GLU A CB  
2222 C CG  . GLU A 288 ? 0.3541 0.3293 0.3711 0.0582  -0.0098 0.0329  288 GLU A CG  
2223 C CD  . GLU A 288 ? 0.4950 0.4656 0.5164 0.0568  -0.0129 0.0305  288 GLU A CD  
2224 O OE1 . GLU A 288 ? 0.4310 0.3990 0.4511 0.0578  -0.0136 0.0272  288 GLU A OE1 
2225 O OE2 . GLU A 288 ? 0.4597 0.4301 0.4861 0.0544  -0.0146 0.0322  288 GLU A OE2 
2226 N N   . ASP A 289 ? 0.2967 0.2506 0.2909 0.0708  -0.0140 0.0280  289 ASP A N   
2227 C CA  . ASP A 289 ? 0.2804 0.2341 0.2677 0.0741  -0.0134 0.0275  289 ASP A CA  
2228 C C   . ASP A 289 ? 0.2968 0.2533 0.2851 0.0720  -0.0133 0.0252  289 ASP A C   
2229 O O   . ASP A 289 ? 0.3001 0.2553 0.2830 0.0742  -0.0138 0.0247  289 ASP A O   
2230 C CB  . ASP A 289 ? 0.3211 0.2638 0.3019 0.0790  -0.0166 0.0267  289 ASP A CB  
2231 C CG  . ASP A 289 ? 0.3352 0.2690 0.3165 0.0783  -0.0206 0.0235  289 ASP A CG  
2232 O OD1 . ASP A 289 ? 0.3222 0.2571 0.3103 0.0742  -0.0213 0.0222  289 ASP A OD1 
2233 O OD2 . ASP A 289 ? 0.3540 0.2797 0.3288 0.0824  -0.0230 0.0224  289 ASP A OD2 
2234 N N   . GLU A 290 ? 0.2725 0.2333 0.2673 0.0678  -0.0127 0.0240  290 GLU A N   
2235 C CA  . GLU A 290 ? 0.3271 0.2891 0.3226 0.0660  -0.0132 0.0216  290 GLU A CA  
2236 C C   . GLU A 290 ? 0.2844 0.2562 0.2809 0.0633  -0.0101 0.0224  290 GLU A C   
2237 O O   . GLU A 290 ? 0.2936 0.2668 0.2926 0.0609  -0.0105 0.0202  290 GLU A O   
2238 C CB  . GLU A 290 ? 0.3163 0.2735 0.3176 0.0642  -0.0159 0.0187  290 GLU A CB  
2239 C CG  . GLU A 290 ? 0.3121 0.2586 0.3106 0.0667  -0.0198 0.0177  290 GLU A CG  
2240 C CD  . GLU A 290 ? 0.3602 0.3017 0.3630 0.0651  -0.0231 0.0148  290 GLU A CD  
2241 O OE1 . GLU A 290 ? 0.3448 0.2911 0.3527 0.0627  -0.0223 0.0133  290 GLU A OE1 
2242 O OE2 . GLU A 290 ? 0.3570 0.2896 0.3575 0.0667  -0.0266 0.0139  290 GLU A OE2 
2243 N N   . PHE A 291 ? 0.2586 0.2366 0.2526 0.0639  -0.0073 0.0255  291 PHE A N   
2244 C CA  . PHE A 291 ? 0.2315 0.2183 0.2247 0.0615  -0.0047 0.0269  291 PHE A CA  
2245 C C   . PHE A 291 ? 0.2294 0.2191 0.2159 0.0637  -0.0039 0.0297  291 PHE A C   
2246 O O   . PHE A 291 ? 0.2604 0.2506 0.2442 0.0669  -0.0028 0.0322  291 PHE A O   
2247 C CB  . PHE A 291 ? 0.2418 0.2356 0.2385 0.0598  -0.0018 0.0288  291 PHE A CB  
2248 C CG  . PHE A 291 ? 0.3157 0.3100 0.3191 0.0573  -0.0020 0.0265  291 PHE A CG  
2249 C CD1 . PHE A 291 ? 0.3786 0.3760 0.3842 0.0547  -0.0017 0.0239  291 PHE A CD1 
2250 C CD2 . PHE A 291 ? 0.3275 0.3188 0.3347 0.0579  -0.0027 0.0270  291 PHE A CD2 
2251 C CE1 . PHE A 291 ? 0.4007 0.3996 0.4125 0.0532  -0.0016 0.0218  291 PHE A CE1 
2252 C CE2 . PHE A 291 ? 0.4165 0.4099 0.4304 0.0556  -0.0028 0.0255  291 PHE A CE2 
2253 C CZ  . PHE A 291 ? 0.3904 0.3882 0.4067 0.0535  -0.0020 0.0228  291 PHE A CZ  
2254 N N   . THR A 292 ? 0.2520 0.2440 0.2358 0.0621  -0.0045 0.0297  292 THR A N   
2255 C CA  . THR A 292 ? 0.2923 0.2893 0.2702 0.0636  -0.0036 0.0332  292 THR A CA  
2256 C C   . THR A 292 ? 0.2918 0.2990 0.2695 0.0618  -0.0004 0.0367  292 THR A C   
2257 O O   . THR A 292 ? 0.2677 0.2778 0.2492 0.0586  0.0007  0.0360  292 THR A O   
2258 C CB  . THR A 292 ? 0.3084 0.3047 0.2834 0.0618  -0.0058 0.0327  292 THR A CB  
2259 O OG1 . THR A 292 ? 0.3065 0.3064 0.2833 0.0570  -0.0059 0.0322  292 THR A OG1 
2260 C CG2 . THR A 292 ? 0.2699 0.2562 0.2453 0.0631  -0.0092 0.0291  292 THR A CG2 
2261 N N   . PRO A 293 ? 0.2821 0.2954 0.2554 0.0640  0.0010  0.0407  293 PRO A N   
2262 C CA  . PRO A 293 ? 0.2980 0.3218 0.2709 0.0617  0.0036  0.0445  293 PRO A CA  
2263 C C   . PRO A 293 ? 0.3011 0.3277 0.2749 0.0558  0.0028  0.0438  293 PRO A C   
2264 O O   . PRO A 293 ? 0.3191 0.3510 0.2948 0.0529  0.0045  0.0448  293 PRO A O   
2265 C CB  . PRO A 293 ? 0.2962 0.3261 0.2637 0.0651  0.0045  0.0487  293 PRO A CB  
2266 C CG  . PRO A 293 ? 0.3118 0.3337 0.2772 0.0709  0.0034  0.0469  293 PRO A CG  
2267 C CD  . PRO A 293 ? 0.3025 0.3140 0.2707 0.0691  0.0005  0.0419  293 PRO A CD  
2268 N N   . PHE A 294 ? 0.3158 0.3383 0.2880 0.0542  -0.0001 0.0421  294 PHE A N   
2269 C CA  . PHE A 294 ? 0.3310 0.3541 0.3033 0.0489  -0.0017 0.0410  294 PHE A CA  
2270 C C   . PHE A 294 ? 0.3199 0.3389 0.2971 0.0474  -0.0016 0.0366  294 PHE A C   
2271 O O   . PHE A 294 ? 0.3409 0.3635 0.3185 0.0438  -0.0011 0.0364  294 PHE A O   
2272 C CB  . PHE A 294 ? 0.3278 0.3459 0.2976 0.0477  -0.0055 0.0400  294 PHE A CB  
2273 C CG  . PHE A 294 ? 0.5100 0.5257 0.4796 0.0427  -0.0082 0.0380  294 PHE A CG  
2274 C CD1 . PHE A 294 ? 0.5743 0.5961 0.5404 0.0385  -0.0090 0.0417  294 PHE A CD1 
2275 C CD2 . PHE A 294 ? 0.4791 0.4865 0.4520 0.0424  -0.0101 0.0326  294 PHE A CD2 
2276 C CE1 . PHE A 294 ? 0.6154 0.6334 0.5804 0.0339  -0.0122 0.0396  294 PHE A CE1 
2277 C CE2 . PHE A 294 ? 0.5885 0.5928 0.5607 0.0385  -0.0128 0.0304  294 PHE A CE2 
2278 C CZ  . PHE A 294 ? 0.5512 0.5601 0.5191 0.0342  -0.0141 0.0338  294 PHE A CZ  
2279 N N   . ASP A 295 ? 0.2683 0.2803 0.2490 0.0500  -0.0022 0.0332  295 ASP A N   
2280 C CA  . ASP A 295 ? 0.3006 0.3103 0.2865 0.0490  -0.0019 0.0294  295 ASP A CA  
2281 C C   . ASP A 295 ? 0.3068 0.3239 0.2946 0.0481  0.0015  0.0314  295 ASP A C   
2282 O O   . ASP A 295 ? 0.3094 0.3291 0.2993 0.0455  0.0022  0.0296  295 ASP A O   
2283 C CB  . ASP A 295 ? 0.3088 0.3112 0.2982 0.0520  -0.0030 0.0268  295 ASP A CB  
2284 C CG  . ASP A 295 ? 0.3165 0.3112 0.3047 0.0526  -0.0066 0.0244  295 ASP A CG  
2285 O OD1 . ASP A 295 ? 0.3158 0.3103 0.3015 0.0502  -0.0084 0.0239  295 ASP A OD1 
2286 O OD2 . ASP A 295 ? 0.3099 0.2985 0.2994 0.0553  -0.0079 0.0231  295 ASP A OD2 
2287 N N   . VAL A 296 ? 0.2574 0.2780 0.2444 0.0505  0.0035  0.0350  296 VAL A N   
2288 C CA  . VAL A 296 ? 0.2274 0.2550 0.2161 0.0497  0.0066  0.0375  296 VAL A CA  
2289 C C   . VAL A 296 ? 0.3091 0.3442 0.2953 0.0459  0.0075  0.0394  296 VAL A C   
2290 O O   . VAL A 296 ? 0.3204 0.3595 0.3086 0.0433  0.0090  0.0387  296 VAL A O   
2291 C CB  . VAL A 296 ? 0.2693 0.2983 0.2568 0.0534  0.0080  0.0412  296 VAL A CB  
2292 C CG1 . VAL A 296 ? 0.2930 0.3301 0.2819 0.0522  0.0109  0.0444  296 VAL A CG1 
2293 C CG2 . VAL A 296 ? 0.2528 0.2733 0.2426 0.0567  0.0065  0.0391  296 VAL A CG2 
2294 N N   . VAL A 297 ? 0.2991 0.3365 0.2806 0.0453  0.0066  0.0420  297 VAL A N   
2295 C CA  . VAL A 297 ? 0.3615 0.4060 0.3402 0.0411  0.0070  0.0446  297 VAL A CA  
2296 C C   . VAL A 297 ? 0.3986 0.4397 0.3778 0.0375  0.0052  0.0403  297 VAL A C   
2297 O O   . VAL A 297 ? 0.4240 0.4698 0.4026 0.0344  0.0062  0.0407  297 VAL A O   
2298 C CB  . VAL A 297 ? 0.3567 0.4044 0.3304 0.0408  0.0057  0.0486  297 VAL A CB  
2299 C CG1 . VAL A 297 ? 0.5020 0.5544 0.4726 0.0353  0.0044  0.0504  297 VAL A CG1 
2300 C CG2 . VAL A 297 ? 0.3700 0.4242 0.3428 0.0445  0.0082  0.0533  297 VAL A CG2 
2301 N N   . ARG A 298 ? 0.3908 0.4234 0.3707 0.0382  0.0024  0.0361  298 ARG A N   
2302 C CA  . ARG A 298 ? 0.4057 0.4343 0.3857 0.0356  0.0004  0.0316  298 ARG A CA  
2303 C C   . ARG A 298 ? 0.4310 0.4620 0.4151 0.0358  0.0029  0.0290  298 ARG A C   
2304 O O   . ARG A 298 ? 0.4558 0.4886 0.4384 0.0332  0.0028  0.0273  298 ARG A O   
2305 C CB  . ARG A 298 ? 0.4446 0.4636 0.4253 0.0370  -0.0030 0.0277  298 ARG A CB  
2306 C CG  . ARG A 298 ? 0.5591 0.5731 0.5384 0.0346  -0.0061 0.0234  298 ARG A CG  
2307 C CD  . ARG A 298 ? 0.5537 0.5579 0.5344 0.0362  -0.0096 0.0191  298 ARG A CD  
2308 N NE  . ARG A 298 ? 0.6557 0.6578 0.6417 0.0399  -0.0083 0.0177  298 ARG A NE  
2309 C CZ  . ARG A 298 ? 0.6085 0.6050 0.5985 0.0418  -0.0097 0.0131  298 ARG A CZ  
2310 N NH1 . ARG A 298 ? 0.5268 0.5189 0.5162 0.0410  -0.0122 0.0091  298 ARG A NH1 
2311 N NH2 . ARG A 298 ? 0.5429 0.5382 0.5374 0.0446  -0.0086 0.0127  298 ARG A NH2 
2312 N N   . GLN A 299 ? 0.3859 0.4172 0.3749 0.0387  0.0049  0.0288  299 GLN A N   
2313 C CA  . GLN A 299 ? 0.3770 0.4118 0.3702 0.0385  0.0071  0.0267  299 GLN A CA  
2314 C C   . GLN A 299 ? 0.4523 0.4962 0.4455 0.0371  0.0104  0.0306  299 GLN A C   
2315 O O   . GLN A 299 ? 0.4526 0.5008 0.4482 0.0360  0.0122  0.0291  299 GLN A O   
2316 C CB  . GLN A 299 ? 0.4249 0.4568 0.4240 0.0414  0.0075  0.0253  299 GLN A CB  
2317 C CG  . GLN A 299 ? 0.5162 0.5414 0.5178 0.0426  0.0051  0.0205  299 GLN A CG  
2318 C CD  . GLN A 299 ? 0.3655 0.3901 0.3734 0.0445  0.0058  0.0198  299 GLN A CD  
2319 O OE1 . GLN A 299 ? 0.2982 0.3289 0.3101 0.0439  0.0080  0.0200  299 GLN A OE1 
2320 N NE2 . GLN A 299 ? 0.3277 0.3455 0.3364 0.0465  0.0037  0.0197  299 GLN A NE2 
2321 N N   . CYS A 300 ? 0.3429 0.3903 0.3337 0.0373  0.0113  0.0355  300 CYS A N   
2322 C CA  . CYS A 300 ? 0.3584 0.4141 0.3498 0.0365  0.0143  0.0396  300 CYS A CA  
2323 C C   . CYS A 300 ? 0.5500 0.6120 0.5366 0.0332  0.0147  0.0428  300 CYS A C   
2324 O O   . CYS A 300 ? 0.6110 0.6806 0.5978 0.0321  0.0170  0.0462  300 CYS A O   
2325 C CB  . CYS A 300 ? 0.3423 0.3979 0.3351 0.0399  0.0153  0.0432  300 CYS A CB  
2326 S SG  . CYS A 300 ? 0.4175 0.4662 0.4159 0.0430  0.0147  0.0407  300 CYS A SG  
2327 N N   . SER A 301 ? 0.4424 0.5015 0.4247 0.0314  0.0120  0.0420  301 SER A N   
2328 C CA  . SER A 301 ? 0.5950 0.6596 0.5725 0.0275  0.0115  0.0452  301 SER A CA  
2329 C C   . SER A 301 ? 0.5627 0.6223 0.5366 0.0243  0.0082  0.0414  301 SER A C   
2330 O O   . SER A 301 ? 0.6292 0.6805 0.6034 0.0255  0.0057  0.0373  301 SER A O   
# 
