data_9KSI
# 
_entry.id   9KSI 
# 
_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   9KSI         pdb_00009ksi 10.2210/pdb9ksi/pdb 
WWPDB D_1300054129 ?            ?                   
# 
_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                        9KSI 
_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' 33697.418 1  3.4.22.69 ? ? ? 
2 non-polymer syn 
;(6E)-1-[[5-chloranyl-4-fluoranyl-2-(4-fluoranylphenoxy)phenyl]methyl]-6-(6-chloranyl-2-methyl-indazol-5-yl)imino-3-(5-methoxypyridin-3-yl)-1,3,5-triazinane-2,4-dione
;
652.435   1  ?         ? ? ? 
3 water       nat water 18.015    28 ?         ? ? ? 
# 
_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
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTF
;
_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 
;(6E)-1-[[5-chloranyl-4-fluoranyl-2-(4-fluoranylphenoxy)phenyl]methyl]-6-(6-chloranyl-2-methyl-indazol-5-yl)imino-3-(5-methoxypyridin-3-yl)-1,3,5-triazinane-2,4-dione
;
A1EGP 
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 PRO 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 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE 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                   305 
_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 
A1EGP non-polymer         . 
;(6E)-1-[[5-chloranyl-4-fluoranyl-2-(4-fluoranylphenoxy)phenyl]methyl]-6-(6-chloranyl-2-methyl-indazol-5-yl)imino-3-(5-methoxypyridin-3-yl)-1,3,5-triazinane-2,4-dione
;
? 'C30 H21 Cl2 F2 N7 O4' 652.435 
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 PRO 132 132 132 PRO PRO 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 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EGP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EGP 
_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 A1EGP 1  401 401 A1EGP 234 A . 
C 3 HOH   1  501 25  HOH   HOH A . 
C 3 HOH   2  502 20  HOH   HOH A . 
C 3 HOH   3  503 22  HOH   HOH A . 
C 3 HOH   4  504 7   HOH   HOH A . 
C 3 HOH   5  505 4   HOH   HOH A . 
C 3 HOH   6  506 3   HOH   HOH A . 
C 3 HOH   7  507 30  HOH   HOH A . 
C 3 HOH   8  508 2   HOH   HOH A . 
C 3 HOH   9  509 28  HOH   HOH A . 
C 3 HOH   10 510 16  HOH   HOH A . 
C 3 HOH   11 511 1   HOH   HOH A . 
C 3 HOH   12 512 10  HOH   HOH A . 
C 3 HOH   13 513 21  HOH   HOH A . 
C 3 HOH   14 514 24  HOH   HOH A . 
C 3 HOH   15 515 15  HOH   HOH A . 
C 3 HOH   16 516 6   HOH   HOH A . 
C 3 HOH   17 517 14  HOH   HOH A . 
C 3 HOH   18 518 5   HOH   HOH A . 
C 3 HOH   19 519 13  HOH   HOH A . 
C 3 HOH   20 520 23  HOH   HOH A . 
C 3 HOH   21 521 18  HOH   HOH A . 
C 3 HOH   22 522 29  HOH   HOH A . 
C 3 HOH   23 523 19  HOH   HOH A . 
C 3 HOH   24 524 12  HOH   HOH A . 
C 3 HOH   25 525 9   HOH   HOH A . 
C 3 HOH   26 526 17  HOH   HOH A . 
C 3 HOH   27 527 11  HOH   HOH A . 
C 3 HOH   28 528 27  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? '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                   115.80 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KSI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     98.125 
_cell.length_a_esd                 ? 
_cell.length_b                     83.678 
_cell.length_b_esd                 ? 
_cell.length_c                     51.794 
_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                         9KSI 
_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                   9KSI 
_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             2.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.70 
_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 EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-24 
_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   0.979145 
_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 BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979145 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KSI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.3 
_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                                     16884 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.476 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.07 
_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                                    2.30 
_reflns_shell.d_res_low                                     2.36 
_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                             2270 
_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                                  0.34 
_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                                 9KSI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.30 
_refine.ls_d_res_low                             31.14 
_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                     16793 
_refine.ls_number_reflns_R_free                  808 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.50 
_refine.ls_percent_reflns_R_free                 4.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1852 
_refine.ls_R_factor_R_free                       0.2428 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1824 
_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                 26.57 
_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                            0.34 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.30 
_refine_hist.d_res_low                        31.14 
_refine_hist.number_atoms_solvent             28 
_refine_hist.number_atoms_total               2431 
_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        2358 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_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' ? 0.003 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.537 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.103 ? 332 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041 ? 371 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003 ? 431 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.30 2.44  . . 153 2581 97.00  . . . . 0.2912 . . . . . . . . . . . 0.3290 
'X-RAY DIFFRACTION' 2.44 2.63  . . 136 2656 100.00 . . . . 0.2426 . . . . . . . . . . . 0.2717 
'X-RAY DIFFRACTION' 2.63 2.89  . . 141 2659 100.00 . . . . 0.2161 . . . . . . . . . . . 0.2845 
'X-RAY DIFFRACTION' 2.89 3.31  . . 127 2661 100.00 . . . . 0.1929 . . . . . . . . . . . 0.2793 
'X-RAY DIFFRACTION' 3.31 4.17  . . 114 2702 100.00 . . . . 0.1733 . . . . . . . . . . . 0.2127 
'X-RAY DIFFRACTION' 4.17 31.14 . . 137 2726 100.00 . . . . 0.1509 . . . . . . . . . . . 0.2148 
# 
_struct.entry_id                     9KSI 
_struct.title                        'Crystal Structure of SARS-CoV-2 main protease in complex with compound 5' 
_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        9KSI 
_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
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTF
;
_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              9KSI 
_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                 305 
_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                  3568 
_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       305 
# 
_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)' 2730  ? 
1 MORE         -15   ? 
1 'SSA (A^2)'  25760 ? 
# 
_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 -22.5423595609 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 46.6311104460 
# 
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  ? ILE A 59  ? ASN A 53  ILE A 59  1 ? 7  
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 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
# 
_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 TYR A 101 ? PHE A 103 ? TYR A 101 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 TYR A 101 ? PHE A 103 ? TYR A 101 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 LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA1 2 3 O GLN A 69  ? O GLN A 69  N GLN A 19  ? N GLN A 19  
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 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
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 PHE A 112 ? N PHE A 112 O CYS A 128 ? O CYS A 128 
AA3 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA3 2 3 N MET A 162 ? N MET A 162 O THR A 175 ? O THR A 175 
# 
_pdbx_entry_details.entry_id                   9KSI 
_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  ? ? 58.09   -129.12 
2 1 ASN A 51  ? ? -163.91 71.78   
3 1 ASN A 84  ? ? 56.09   -126.93 
4 1 ASP A 155 ? ? 78.45   -18.51  
5 1 HIS A 164 ? ? -121.10 -50.92  
6 1 PRO A 184 ? ? -88.06  48.76   
7 1 GLN A 189 ? ? -73.94  44.67   
8 1 ARG A 217 ? ? -150.35 2.18    
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -13.2460 42.2394 10.7112 0.3532 ? 0.0359 ? 0.0486  ? 0.3100 ? 0.0280 ? 0.4132 ? 1.9032 ? -0.5305 ? 
1.1514  ? 2.9509 ? -1.0613 ? 4.9236 ? -0.0092 ? -0.0587 ? 0.0523  ? 0.2845  ? 0.1883  ? 0.5175  ? -0.5033 ? -0.2640 ? -0.1474 ? 
2 'X-RAY DIFFRACTION' ? refined -16.4773 48.4453 -1.3367 0.6196 ? 0.1060 ? -0.0613 ? 0.4642 ? 0.1260 ? 0.5493 ? 2.4244 ? -0.2646 ? 
0.5349  ? 3.3763 ? -0.0656 ? 5.4602 ? 0.0435  ? 0.2801  ? 0.3307  ? -0.3521 ? -0.0758 ? 0.5356  ? -0.8800 ? -0.7590 ? 0.0387  ? 
3 'X-RAY DIFFRACTION' ? refined -9.2433  33.9244 10.0199 0.3207 ? 0.0154 ? -0.0379 ? 0.3286 ? 0.0241 ? 0.3195 ? 2.1321 ? -0.7685 ? 
-1.1173 ? 4.6799 ? -0.1386 ? 3.3788 ? 0.1066  ? 0.0097  ? -0.0741 ? -0.1146 ? -0.0066 ? -0.0306 ? 0.0661  ? -0.0308 ? -0.0818 ? 
4 'X-RAY DIFFRACTION' ? refined 0.2856   15.5760 13.6855 0.3431 ? 0.0587 ? 0.0430  ? 0.3722 ? 0.0123 ? 0.3885 ? 1.3406 ? -0.8495 ? 
0.3848  ? 3.3108 ? -1.1096 ? 3.6268 ? 0.1242  ? -0.0035 ? -0.3206 ? -0.3177 ? 0.0444  ? 0.0910  ? 0.7394  ? 0.3640  ? -0.1341 ? 
5 'X-RAY DIFFRACTION' ? refined 8.3308   14.1431 18.3132 0.3969 ? 0.0486 ? 0.0138  ? 0.7096 ? 0.1227 ? 0.5459 ? 4.9254 ? 1.6659  ? 
2.3588  ? 4.0909 ? 2.4414  ? 6.1472 ? -0.1583 ? 0.5180  ? -0.1654 ? -0.2725 ? 0.1970  ? -0.2777 ? 0.3239  ? 1.3351  ? -0.0233 ? 
6 'X-RAY DIFFRACTION' ? refined -1.0351  19.5257 25.4843 0.4355 ? 0.0969 ? 0.0519  ? 0.5067 ? 0.0218 ? 0.4249 ? 5.6700 ? 0.9737  ? 
0.4821  ? 4.3144 ? -1.4177 ? 6.3984 ? -0.2153 ? -0.3453 ? 0.1876  ? 0.2759  ? -0.0861 ? 0.6311  ? -0.4865 ? -0.3770 ? 0.2875  ? 
# 
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 100 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 101 through 180 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 181 through 237 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 238 through 274 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 275 through 305 )
;
# 
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 
A1EGP C14  C  N N 1   
A1EGP C15  C  N N 2   
A1EGP C16  C  Y N 3   
A1EGP C35  C  Y N 4   
A1EGP C36  C  Y N 5   
A1EGP C37  C  Y N 6   
A1EGP C38  C  Y N 7   
A1EGP C39  C  Y N 8   
A1EGP C40  C  Y N 9   
A1EGP C41  C  Y N 10  
A1EGP C01  C  N N 11  
A1EGP C03  C  N N 12  
A1EGP C05  C  N N 13  
A1EGP C07  C  Y N 14  
A1EGP C08  C  Y N 15  
A1EGP C10  C  Y N 16  
A1EGP C11  C  Y N 17  
A1EGP C12  C  Y N 18  
A1EGP C17  C  Y N 19  
A1EGP C18  C  Y N 20  
A1EGP C19  C  Y N 21  
A1EGP C20  C  Y N 22  
A1EGP C21  C  Y N 23  
A1EGP C25  C  Y N 24  
A1EGP C26  C  Y N 25  
A1EGP C27  C  Y N 26  
A1EGP C28  C  Y N 27  
A1EGP C29  C  Y N 28  
A1EGP C30  C  Y N 29  
A1EGP C45  C  N N 30  
A1EGP F23  F  N N 31  
A1EGP F31  F  N N 32  
A1EGP N02  N  N N 33  
A1EGP N04  N  N N 34  
A1EGP N06  N  N N 35  
A1EGP N09  N  Y N 36  
A1EGP N32  N  N N 37  
A1EGP N42  N  Y N 38  
A1EGP N43  N  Y N 39  
A1EGP O13  O  N N 40  
A1EGP O24  O  N N 41  
A1EGP O33  O  N N 42  
A1EGP O34  O  N N 43  
A1EGP CL22 CL N N 44  
A1EGP CL44 CL N N 45  
A1EGP H141 H  N N 46  
A1EGP H142 H  N N 47  
A1EGP H143 H  N N 48  
A1EGP H152 H  N N 49  
A1EGP H151 H  N N 50  
A1EGP H361 H  N N 51  
A1EGP H391 H  N N 52  
A1EGP H411 H  N N 53  
A1EGP H081 H  N N 54  
A1EGP H101 H  N N 55  
A1EGP H121 H  N N 56  
A1EGP H181 H  N N 57  
A1EGP H211 H  N N 58  
A1EGP H261 H  N N 59  
A1EGP H271 H  N N 60  
A1EGP H291 H  N N 61  
A1EGP H301 H  N N 62  
A1EGP H452 H  N N 63  
A1EGP H453 H  N N 64  
A1EGP H451 H  N N 65  
A1EGP H2   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 
A1EGP F23 C19  sing N N 1   
A1EGP C18 C19  doub Y N 2   
A1EGP C18 C17  sing Y N 3   
A1EGP O24 C25  sing N N 4   
A1EGP O24 C17  sing N N 5   
A1EGP C30 C25  doub Y N 6   
A1EGP C30 C29  sing Y N 7   
A1EGP C25 C26  sing Y N 8   
A1EGP C29 C28  doub Y N 9   
A1EGP C19 C20  sing Y N 10  
A1EGP C17 C16  doub Y N 11  
A1EGP C26 C27  doub Y N 12  
A1EGP C28 C27  sing Y N 13  
A1EGP C28 F31  sing N N 14  
A1EGP C20 CL22 sing N N 15  
A1EGP C20 C21  doub Y N 16  
A1EGP C16 C21  sing Y N 17  
A1EGP C16 C15  sing N N 18  
A1EGP C15 N04  sing N N 19  
A1EGP N32 C35  sing N N 20  
A1EGP N32 C03  doub N N 21  
A1EGP C36 C35  doub Y N 22  
A1EGP C36 C37  sing Y N 23  
A1EGP C35 C40  sing Y N 24  
A1EGP C41 C37  doub Y N 25  
A1EGP C41 N42  sing Y N 26  
A1EGP C37 C38  sing Y N 27  
A1EGP C40 CL44 sing N N 28  
A1EGP C40 C39  doub Y N 29  
A1EGP N42 C45  sing N N 30  
A1EGP N42 N43  sing Y N 31  
A1EGP C38 C39  sing Y N 32  
A1EGP C38 N43  doub Y N 33  
A1EGP N04 C03  sing N N 34  
A1EGP N04 C05  sing N N 35  
A1EGP C03 N02  sing N N 36  
A1EGP O34 C05  doub N N 37  
A1EGP C05 N06  sing N N 38  
A1EGP N02 C01  sing N N 39  
A1EGP N06 C01  sing N N 40  
A1EGP N06 C07  sing N N 41  
A1EGP C01 O33  doub N N 42  
A1EGP C07 C12  doub Y N 43  
A1EGP C07 C08  sing Y N 44  
A1EGP C12 C11  sing Y N 45  
A1EGP C08 N09  doub Y N 46  
A1EGP C11 O13  sing N N 47  
A1EGP C11 C10  doub Y N 48  
A1EGP N09 C10  sing Y N 49  
A1EGP O13 C14  sing N N 50  
A1EGP C14 H141 sing N N 51  
A1EGP C14 H142 sing N N 52  
A1EGP C14 H143 sing N N 53  
A1EGP C15 H152 sing N N 54  
A1EGP C15 H151 sing N N 55  
A1EGP C36 H361 sing N N 56  
A1EGP C39 H391 sing N N 57  
A1EGP C41 H411 sing N N 58  
A1EGP C08 H081 sing N N 59  
A1EGP C10 H101 sing N N 60  
A1EGP C12 H121 sing N N 61  
A1EGP C18 H181 sing N N 62  
A1EGP C21 H211 sing N N 63  
A1EGP C26 H261 sing N N 64  
A1EGP C27 H271 sing N N 65  
A1EGP C29 H291 sing N N 66  
A1EGP C30 H301 sing N N 67  
A1EGP C45 H452 sing N N 68  
A1EGP C45 H453 sing N N 69  
A1EGP C45 H451 sing N N 70  
A1EGP N02 H2   sing N N 71  
ALA   N   CA   sing N N 72  
ALA   N   H    sing N N 73  
ALA   N   H2   sing N N 74  
ALA   CA  C    sing N N 75  
ALA   CA  CB   sing N N 76  
ALA   CA  HA   sing N N 77  
ALA   C   O    doub N N 78  
ALA   C   OXT  sing N N 79  
ALA   CB  HB1  sing N N 80  
ALA   CB  HB2  sing N N 81  
ALA   CB  HB3  sing N N 82  
ALA   OXT HXT  sing N N 83  
ARG   N   CA   sing N N 84  
ARG   N   H    sing N N 85  
ARG   N   H2   sing N N 86  
ARG   CA  C    sing N N 87  
ARG   CA  CB   sing N N 88  
ARG   CA  HA   sing N N 89  
ARG   C   O    doub N N 90  
ARG   C   OXT  sing N N 91  
ARG   CB  CG   sing N N 92  
ARG   CB  HB2  sing N N 93  
ARG   CB  HB3  sing N N 94  
ARG   CG  CD   sing N N 95  
ARG   CG  HG2  sing N N 96  
ARG   CG  HG3  sing N N 97  
ARG   CD  NE   sing N N 98  
ARG   CD  HD2  sing N N 99  
ARG   CD  HD3  sing N N 100 
ARG   NE  CZ   sing N N 101 
ARG   NE  HE   sing N N 102 
ARG   CZ  NH1  sing N N 103 
ARG   CZ  NH2  doub N N 104 
ARG   NH1 HH11 sing N N 105 
ARG   NH1 HH12 sing N N 106 
ARG   NH2 HH21 sing N N 107 
ARG   NH2 HH22 sing N N 108 
ARG   OXT HXT  sing N N 109 
ASN   N   CA   sing N N 110 
ASN   N   H    sing N N 111 
ASN   N   H2   sing N N 112 
ASN   CA  C    sing N N 113 
ASN   CA  CB   sing N N 114 
ASN   CA  HA   sing N N 115 
ASN   C   O    doub N N 116 
ASN   C   OXT  sing N N 117 
ASN   CB  CG   sing N N 118 
ASN   CB  HB2  sing N N 119 
ASN   CB  HB3  sing N N 120 
ASN   CG  OD1  doub N N 121 
ASN   CG  ND2  sing N N 122 
ASN   ND2 HD21 sing N N 123 
ASN   ND2 HD22 sing N N 124 
ASN   OXT HXT  sing N N 125 
ASP   N   CA   sing N N 126 
ASP   N   H    sing N N 127 
ASP   N   H2   sing N N 128 
ASP   CA  C    sing N N 129 
ASP   CA  CB   sing N N 130 
ASP   CA  HA   sing N N 131 
ASP   C   O    doub N N 132 
ASP   C   OXT  sing N N 133 
ASP   CB  CG   sing N N 134 
ASP   CB  HB2  sing N N 135 
ASP   CB  HB3  sing N N 136 
ASP   CG  OD1  doub N N 137 
ASP   CG  OD2  sing N N 138 
ASP   OD2 HD2  sing N N 139 
ASP   OXT HXT  sing N N 140 
CYS   N   CA   sing N N 141 
CYS   N   H    sing N N 142 
CYS   N   H2   sing N N 143 
CYS   CA  C    sing N N 144 
CYS   CA  CB   sing N N 145 
CYS   CA  HA   sing N N 146 
CYS   C   O    doub N N 147 
CYS   C   OXT  sing N N 148 
CYS   CB  SG   sing N N 149 
CYS   CB  HB2  sing N N 150 
CYS   CB  HB3  sing N N 151 
CYS   SG  HG   sing N N 152 
CYS   OXT HXT  sing N N 153 
GLN   N   CA   sing N N 154 
GLN   N   H    sing N N 155 
GLN   N   H2   sing N N 156 
GLN   CA  C    sing N N 157 
GLN   CA  CB   sing N N 158 
GLN   CA  HA   sing N N 159 
GLN   C   O    doub N N 160 
GLN   C   OXT  sing N N 161 
GLN   CB  CG   sing N N 162 
GLN   CB  HB2  sing N N 163 
GLN   CB  HB3  sing N N 164 
GLN   CG  CD   sing N N 165 
GLN   CG  HG2  sing N N 166 
GLN   CG  HG3  sing N N 167 
GLN   CD  OE1  doub N N 168 
GLN   CD  NE2  sing N N 169 
GLN   NE2 HE21 sing N N 170 
GLN   NE2 HE22 sing N N 171 
GLN   OXT HXT  sing N N 172 
GLU   N   CA   sing N N 173 
GLU   N   H    sing N N 174 
GLU   N   H2   sing N N 175 
GLU   CA  C    sing N N 176 
GLU   CA  CB   sing N N 177 
GLU   CA  HA   sing N N 178 
GLU   C   O    doub N N 179 
GLU   C   OXT  sing N N 180 
GLU   CB  CG   sing N N 181 
GLU   CB  HB2  sing N N 182 
GLU   CB  HB3  sing N N 183 
GLU   CG  CD   sing N N 184 
GLU   CG  HG2  sing N N 185 
GLU   CG  HG3  sing N N 186 
GLU   CD  OE1  doub N N 187 
GLU   CD  OE2  sing N N 188 
GLU   OE2 HE2  sing N N 189 
GLU   OXT HXT  sing N N 190 
GLY   N   CA   sing N N 191 
GLY   N   H    sing N N 192 
GLY   N   H2   sing N N 193 
GLY   CA  C    sing N N 194 
GLY   CA  HA2  sing N N 195 
GLY   CA  HA3  sing N N 196 
GLY   C   O    doub N N 197 
GLY   C   OXT  sing N N 198 
GLY   OXT HXT  sing N N 199 
HIS   N   CA   sing N N 200 
HIS   N   H    sing N N 201 
HIS   N   H2   sing N N 202 
HIS   CA  C    sing N N 203 
HIS   CA  CB   sing N N 204 
HIS   CA  HA   sing N N 205 
HIS   C   O    doub N N 206 
HIS   C   OXT  sing N N 207 
HIS   CB  CG   sing N N 208 
HIS   CB  HB2  sing N N 209 
HIS   CB  HB3  sing N N 210 
HIS   CG  ND1  sing Y N 211 
HIS   CG  CD2  doub Y N 212 
HIS   ND1 CE1  doub Y N 213 
HIS   ND1 HD1  sing N N 214 
HIS   CD2 NE2  sing Y N 215 
HIS   CD2 HD2  sing N N 216 
HIS   CE1 NE2  sing Y N 217 
HIS   CE1 HE1  sing N N 218 
HIS   NE2 HE2  sing N N 219 
HIS   OXT HXT  sing N N 220 
HOH   O   H1   sing N N 221 
HOH   O   H2   sing N N 222 
ILE   N   CA   sing N N 223 
ILE   N   H    sing N N 224 
ILE   N   H2   sing N N 225 
ILE   CA  C    sing N N 226 
ILE   CA  CB   sing N N 227 
ILE   CA  HA   sing N N 228 
ILE   C   O    doub N N 229 
ILE   C   OXT  sing N N 230 
ILE   CB  CG1  sing N N 231 
ILE   CB  CG2  sing N N 232 
ILE   CB  HB   sing N N 233 
ILE   CG1 CD1  sing N N 234 
ILE   CG1 HG12 sing N N 235 
ILE   CG1 HG13 sing N N 236 
ILE   CG2 HG21 sing N N 237 
ILE   CG2 HG22 sing N N 238 
ILE   CG2 HG23 sing N N 239 
ILE   CD1 HD11 sing N N 240 
ILE   CD1 HD12 sing N N 241 
ILE   CD1 HD13 sing N N 242 
ILE   OXT HXT  sing N N 243 
LEU   N   CA   sing N N 244 
LEU   N   H    sing N N 245 
LEU   N   H2   sing N N 246 
LEU   CA  C    sing N N 247 
LEU   CA  CB   sing N N 248 
LEU   CA  HA   sing N N 249 
LEU   C   O    doub N N 250 
LEU   C   OXT  sing N N 251 
LEU   CB  CG   sing N N 252 
LEU   CB  HB2  sing N N 253 
LEU   CB  HB3  sing N N 254 
LEU   CG  CD1  sing N N 255 
LEU   CG  CD2  sing N N 256 
LEU   CG  HG   sing N N 257 
LEU   CD1 HD11 sing N N 258 
LEU   CD1 HD12 sing N N 259 
LEU   CD1 HD13 sing N N 260 
LEU   CD2 HD21 sing N N 261 
LEU   CD2 HD22 sing N N 262 
LEU   CD2 HD23 sing N N 263 
LEU   OXT HXT  sing N N 264 
LYS   N   CA   sing N N 265 
LYS   N   H    sing N N 266 
LYS   N   H2   sing N N 267 
LYS   CA  C    sing N N 268 
LYS   CA  CB   sing N N 269 
LYS   CA  HA   sing N N 270 
LYS   C   O    doub N N 271 
LYS   C   OXT  sing N N 272 
LYS   CB  CG   sing N N 273 
LYS   CB  HB2  sing N N 274 
LYS   CB  HB3  sing N N 275 
LYS   CG  CD   sing N N 276 
LYS   CG  HG2  sing N N 277 
LYS   CG  HG3  sing N N 278 
LYS   CD  CE   sing N N 279 
LYS   CD  HD2  sing N N 280 
LYS   CD  HD3  sing N N 281 
LYS   CE  NZ   sing N N 282 
LYS   CE  HE2  sing N N 283 
LYS   CE  HE3  sing N N 284 
LYS   NZ  HZ1  sing N N 285 
LYS   NZ  HZ2  sing N N 286 
LYS   NZ  HZ3  sing N N 287 
LYS   OXT HXT  sing N N 288 
MET   N   CA   sing N N 289 
MET   N   H    sing N N 290 
MET   N   H2   sing N N 291 
MET   CA  C    sing N N 292 
MET   CA  CB   sing N N 293 
MET   CA  HA   sing N N 294 
MET   C   O    doub N N 295 
MET   C   OXT  sing N N 296 
MET   CB  CG   sing N N 297 
MET   CB  HB2  sing N N 298 
MET   CB  HB3  sing N N 299 
MET   CG  SD   sing N N 300 
MET   CG  HG2  sing N N 301 
MET   CG  HG3  sing N N 302 
MET   SD  CE   sing N N 303 
MET   CE  HE1  sing N N 304 
MET   CE  HE2  sing N N 305 
MET   CE  HE3  sing N N 306 
MET   OXT HXT  sing N N 307 
PHE   N   CA   sing N N 308 
PHE   N   H    sing N N 309 
PHE   N   H2   sing N N 310 
PHE   CA  C    sing N N 311 
PHE   CA  CB   sing N N 312 
PHE   CA  HA   sing N N 313 
PHE   C   O    doub N N 314 
PHE   C   OXT  sing N N 315 
PHE   CB  CG   sing N N 316 
PHE   CB  HB2  sing N N 317 
PHE   CB  HB3  sing N N 318 
PHE   CG  CD1  doub Y N 319 
PHE   CG  CD2  sing Y N 320 
PHE   CD1 CE1  sing Y N 321 
PHE   CD1 HD1  sing N N 322 
PHE   CD2 CE2  doub Y N 323 
PHE   CD2 HD2  sing N N 324 
PHE   CE1 CZ   doub Y N 325 
PHE   CE1 HE1  sing N N 326 
PHE   CE2 CZ   sing Y N 327 
PHE   CE2 HE2  sing N N 328 
PHE   CZ  HZ   sing N N 329 
PHE   OXT HXT  sing N N 330 
PRO   N   CA   sing N N 331 
PRO   N   CD   sing N N 332 
PRO   N   H    sing N N 333 
PRO   CA  C    sing N N 334 
PRO   CA  CB   sing N N 335 
PRO   CA  HA   sing N N 336 
PRO   C   O    doub N N 337 
PRO   C   OXT  sing N N 338 
PRO   CB  CG   sing N N 339 
PRO   CB  HB2  sing N N 340 
PRO   CB  HB3  sing N N 341 
PRO   CG  CD   sing N N 342 
PRO   CG  HG2  sing N N 343 
PRO   CG  HG3  sing N N 344 
PRO   CD  HD2  sing N N 345 
PRO   CD  HD3  sing N N 346 
PRO   OXT HXT  sing N N 347 
SER   N   CA   sing N N 348 
SER   N   H    sing N N 349 
SER   N   H2   sing N N 350 
SER   CA  C    sing N N 351 
SER   CA  CB   sing N N 352 
SER   CA  HA   sing N N 353 
SER   C   O    doub N N 354 
SER   C   OXT  sing N N 355 
SER   CB  OG   sing N N 356 
SER   CB  HB2  sing N N 357 
SER   CB  HB3  sing N N 358 
SER   OG  HG   sing N N 359 
SER   OXT HXT  sing N N 360 
THR   N   CA   sing N N 361 
THR   N   H    sing N N 362 
THR   N   H2   sing N N 363 
THR   CA  C    sing N N 364 
THR   CA  CB   sing N N 365 
THR   CA  HA   sing N N 366 
THR   C   O    doub N N 367 
THR   C   OXT  sing N N 368 
THR   CB  OG1  sing N N 369 
THR   CB  CG2  sing N N 370 
THR   CB  HB   sing N N 371 
THR   OG1 HG1  sing N N 372 
THR   CG2 HG21 sing N N 373 
THR   CG2 HG22 sing N N 374 
THR   CG2 HG23 sing N N 375 
THR   OXT HXT  sing N N 376 
TRP   N   CA   sing N N 377 
TRP   N   H    sing N N 378 
TRP   N   H2   sing N N 379 
TRP   CA  C    sing N N 380 
TRP   CA  CB   sing N N 381 
TRP   CA  HA   sing N N 382 
TRP   C   O    doub N N 383 
TRP   C   OXT  sing N N 384 
TRP   CB  CG   sing N N 385 
TRP   CB  HB2  sing N N 386 
TRP   CB  HB3  sing N N 387 
TRP   CG  CD1  doub Y N 388 
TRP   CG  CD2  sing Y N 389 
TRP   CD1 NE1  sing Y N 390 
TRP   CD1 HD1  sing N N 391 
TRP   CD2 CE2  doub Y N 392 
TRP   CD2 CE3  sing Y N 393 
TRP   NE1 CE2  sing Y N 394 
TRP   NE1 HE1  sing N N 395 
TRP   CE2 CZ2  sing Y N 396 
TRP   CE3 CZ3  doub Y N 397 
TRP   CE3 HE3  sing N N 398 
TRP   CZ2 CH2  doub Y N 399 
TRP   CZ2 HZ2  sing N N 400 
TRP   CZ3 CH2  sing Y N 401 
TRP   CZ3 HZ3  sing N N 402 
TRP   CH2 HH2  sing N N 403 
TRP   OXT HXT  sing N N 404 
TYR   N   CA   sing N N 405 
TYR   N   H    sing N N 406 
TYR   N   H2   sing N N 407 
TYR   CA  C    sing N N 408 
TYR   CA  CB   sing N N 409 
TYR   CA  HA   sing N N 410 
TYR   C   O    doub N N 411 
TYR   C   OXT  sing N N 412 
TYR   CB  CG   sing N N 413 
TYR   CB  HB2  sing N N 414 
TYR   CB  HB3  sing N N 415 
TYR   CG  CD1  doub Y N 416 
TYR   CG  CD2  sing Y N 417 
TYR   CD1 CE1  sing Y N 418 
TYR   CD1 HD1  sing N N 419 
TYR   CD2 CE2  doub Y N 420 
TYR   CD2 HD2  sing N N 421 
TYR   CE1 CZ   doub Y N 422 
TYR   CE1 HE1  sing N N 423 
TYR   CE2 CZ   sing Y N 424 
TYR   CE2 HE2  sing N N 425 
TYR   CZ  OH   sing N N 426 
TYR   OH  HH   sing N N 427 
TYR   OXT HXT  sing N N 428 
VAL   N   CA   sing N N 429 
VAL   N   H    sing N N 430 
VAL   N   H2   sing N N 431 
VAL   CA  C    sing N N 432 
VAL   CA  CB   sing N N 433 
VAL   CA  HA   sing N N 434 
VAL   C   O    doub N N 435 
VAL   C   OXT  sing N N 436 
VAL   CB  CG1  sing N N 437 
VAL   CB  CG2  sing N N 438 
VAL   CB  HB   sing N N 439 
VAL   CG1 HG11 sing N N 440 
VAL   CG1 HG12 sing N N 441 
VAL   CG1 HG13 sing N N 442 
VAL   CG2 HG21 sing N N 443 
VAL   CG2 HG22 sing N N 444 
VAL   CG2 HG23 sing N N 445 
VAL   OXT HXT  sing N N 446 
# 
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                    9KSI 
_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]   0.010191 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004927 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011951 
_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]   0.021445 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
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   ? -0.517  26.743 36.095  1.00 63.70  ? 1   SER   A N    1 
ATOM   2    C  CA   . SER   A 1 1   ? -0.852  25.398 35.641  1.00 62.21  ? 1   SER   A CA   1 
ATOM   3    C  C    . SER   A 1 1   ? -2.137  25.401 34.811  1.00 63.49  ? 1   SER   A C    1 
ATOM   4    O  O    . SER   A 1 1   ? -2.874  26.392 34.788  1.00 52.29  ? 1   SER   A O    1 
ATOM   5    C  CB   . SER   A 1 1   ? -0.981  24.451 36.838  1.00 66.83  ? 1   SER   A CB   1 
ATOM   6    O  OG   . SER   A 1 1   ? -1.939  23.437 36.599  1.00 70.20  ? 1   SER   A OG   1 
ATOM   7    N  N    . GLY   A 1 2   ? -2.394  24.294 34.123  1.00 61.81  ? 2   GLY   A N    1 
ATOM   8    C  CA   . GLY   A 1 2   ? -3.538  24.176 33.246  1.00 50.36  ? 2   GLY   A CA   1 
ATOM   9    C  C    . GLY   A 1 2   ? -3.174  24.421 31.791  1.00 53.89  ? 2   GLY   A C    1 
ATOM   10   O  O    . GLY   A 1 2   ? -2.160  25.038 31.463  1.00 61.42  ? 2   GLY   A O    1 
ATOM   11   N  N    . PHE   A 1 3   ? -4.026  23.918 30.900  1.00 49.39  ? 3   PHE   A N    1 
ATOM   12   C  CA   . PHE   A 1 3   ? -3.809  24.067 29.467  1.00 46.53  ? 3   PHE   A CA   1 
ATOM   13   C  C    . PHE   A 1 3   ? -5.157  24.149 28.769  1.00 55.59  ? 3   PHE   A C    1 
ATOM   14   O  O    . PHE   A 1 3   ? -6.020  23.292 28.979  1.00 48.92  ? 3   PHE   A O    1 
ATOM   15   C  CB   . PHE   A 1 3   ? -2.983  22.903 28.908  1.00 45.71  ? 3   PHE   A CB   1 
ATOM   16   C  CG   . PHE   A 1 3   ? -2.290  23.218 27.613  1.00 55.21  ? 3   PHE   A CG   1 
ATOM   17   C  CD1  . PHE   A 1 3   ? -1.174  24.040 27.587  1.00 59.59  ? 3   PHE   A CD1  1 
ATOM   18   C  CD2  . PHE   A 1 3   ? -2.758  22.696 26.418  1.00 53.38  ? 3   PHE   A CD2  1 
ATOM   19   C  CE1  . PHE   A 1 3   ? -0.536  24.333 26.390  1.00 54.35  ? 3   PHE   A CE1  1 
ATOM   20   C  CE2  . PHE   A 1 3   ? -2.125  22.985 25.218  1.00 56.02  ? 3   PHE   A CE2  1 
ATOM   21   C  CZ   . PHE   A 1 3   ? -1.014  23.804 25.205  1.00 55.83  ? 3   PHE   A CZ   1 
ATOM   22   N  N    . ARG   A 1 4   ? -5.327  25.171 27.935  1.00 48.85  ? 4   ARG   A N    1 
ATOM   23   C  CA   . ARG   A 1 4   ? -6.617  25.462 27.336  1.00 51.49  ? 4   ARG   A CA   1 
ATOM   24   C  C    . ARG   A 1 4   ? -6.400  26.171 26.008  1.00 51.63  ? 4   ARG   A C    1 
ATOM   25   O  O    . ARG   A 1 4   ? -5.399  26.866 25.815  1.00 53.31  ? 4   ARG   A O    1 
ATOM   26   C  CB   . ARG   A 1 4   ? -7.471  26.322 28.277  1.00 50.53  ? 4   ARG   A CB   1 
ATOM   27   C  CG   . ARG   A 1 4   ? -8.463  25.534 29.117  1.00 55.83  ? 4   ARG   A CG   1 
ATOM   28   C  CD   . ARG   A 1 4   ? -9.815  26.219 29.121  1.00 54.35  ? 4   ARG   A CD   1 
ATOM   29   N  NE   . ARG   A 1 4   ? -10.566 25.948 30.340  1.00 50.76  ? 4   ARG   A NE   1 
ATOM   30   C  CZ   . ARG   A 1 4   ? -11.392 24.922 30.495  1.00 64.92  ? 4   ARG   A CZ   1 
ATOM   31   N  NH1  . ARG   A 1 4   ? -11.623 24.066 29.512  1.00 67.95  ? 4   ARG   A NH1  1 
ATOM   32   N  NH2  . ARG   A 1 4   ? -12.005 24.751 31.664  1.00 56.87  ? 4   ARG   A NH2  1 
ATOM   33   N  N    . LYS   A 1 5   ? -7.341  25.985 25.085  1.00 48.96  ? 5   LYS   A N    1 
ATOM   34   C  CA   . LYS   A 1 5   ? -7.304  26.736 23.835  1.00 52.56  ? 5   LYS   A CA   1 
ATOM   35   C  C    . LYS   A 1 5   ? -7.498  28.212 24.152  1.00 49.92  ? 5   LYS   A C    1 
ATOM   36   O  O    . LYS   A 1 5   ? -8.583  28.626 24.572  1.00 50.55  ? 5   LYS   A O    1 
ATOM   37   C  CB   . LYS   A 1 5   ? -8.371  26.233 22.868  1.00 47.44  ? 5   LYS   A CB   1 
ATOM   38   C  CG   . LYS   A 1 5   ? -7.856  25.217 21.863  1.00 56.06  ? 5   LYS   A CG   1 
ATOM   39   C  CD   . LYS   A 1 5   ? -8.980  24.334 21.347  1.00 62.03  ? 5   LYS   A CD   1 
ATOM   40   C  CE   . LYS   A 1 5   ? -8.449  23.260 20.410  1.00 65.32  ? 5   LYS   A CE   1 
ATOM   41   N  NZ   . LYS   A 1 5   ? -8.973  21.911 20.777  1.00 71.34  ? 5   LYS   A NZ   1 
ATOM   42   N  N    . MET   A 1 6   ? -6.447  29.005 23.960  1.00 43.53  ? 6   MET   A N    1 
ATOM   43   C  CA   . MET   A 1 6   ? -6.426  30.402 24.370  1.00 46.21  ? 6   MET   A CA   1 
ATOM   44   C  C    . MET   A 1 6   ? -6.349  31.307 23.152  1.00 46.05  ? 6   MET   A C    1 
ATOM   45   O  O    . MET   A 1 6   ? -5.495  31.114 22.279  1.00 47.94  ? 6   MET   A O    1 
ATOM   46   C  CB   . MET   A 1 6   ? -5.247  30.682 25.305  1.00 44.54  ? 6   MET   A CB   1 
ATOM   47   C  CG   . MET   A 1 6   ? -5.583  31.653 26.425  1.00 59.81  ? 6   MET   A CG   1 
ATOM   48   S  SD   . MET   A 1 6   ? -4.293  31.794 27.676  1.00 73.14  ? 6   MET   A SD   1 
ATOM   49   C  CE   . MET   A 1 6   ? -4.641  30.350 28.676  1.00 50.44  ? 6   MET   A CE   1 
ATOM   50   N  N    . ALA   A 1 7   ? -7.232  32.294 23.104  1.00 36.03  ? 7   ALA   A N    1 
ATOM   51   C  CA   . ALA   A 1 7   ? -7.215  33.298 22.055  1.00 41.51  ? 7   ALA   A CA   1 
ATOM   52   C  C    . ALA   A 1 7   ? -6.582  34.578 22.579  1.00 48.54  ? 7   ALA   A C    1 
ATOM   53   O  O    . ALA   A 1 7   ? -6.551  34.838 23.784  1.00 37.67  ? 7   ALA   A O    1 
ATOM   54   C  CB   . ALA   A 1 7   ? -8.628  33.584 21.542  1.00 40.46  ? 7   ALA   A CB   1 
ATOM   55   N  N    . PHE   A 1 8   ? -6.063  35.374 21.655  1.00 41.01  ? 8   PHE   A N    1 
ATOM   56   C  CA   . PHE   A 1 8   ? -5.550  36.674 22.031  1.00 47.20  ? 8   PHE   A CA   1 
ATOM   57   C  C    . PHE   A 1 8   ? -6.709  37.602 22.391  1.00 45.29  ? 8   PHE   A C    1 
ATOM   58   O  O    . PHE   A 1 8   ? -7.805  37.480 21.839  1.00 45.18  ? 8   PHE   A O    1 
ATOM   59   C  CB   . PHE   A 1 8   ? -4.734  37.273 20.893  1.00 37.47  ? 8   PHE   A CB   1 
ATOM   60   C  CG   . PHE   A 1 8   ? -3.399  36.621 20.703  1.00 47.21  ? 8   PHE   A CG   1 
ATOM   61   C  CD1  . PHE   A 1 8   ? -2.333  36.942 21.526  1.00 52.27  ? 8   PHE   A CD1  1 
ATOM   62   C  CD2  . PHE   A 1 8   ? -3.207  35.685 19.701  1.00 42.45  ? 8   PHE   A CD2  1 
ATOM   63   C  CE1  . PHE   A 1 8   ? -1.098  36.342 21.352  1.00 45.73  ? 8   PHE   A CE1  1 
ATOM   64   C  CE2  . PHE   A 1 8   ? -1.973  35.082 19.524  1.00 49.67  ? 8   PHE   A CE2  1 
ATOM   65   C  CZ   . PHE   A 1 8   ? -0.918  35.414 20.353  1.00 38.25  ? 8   PHE   A CZ   1 
ATOM   66   N  N    . PRO   A 1 9   ? -6.503  38.521 23.330  1.00 48.86  ? 9   PRO   A N    1 
ATOM   67   C  CA   . PRO   A 1 9   ? -7.539  39.521 23.611  1.00 41.18  ? 9   PRO   A CA   1 
ATOM   68   C  C    . PRO   A 1 9   ? -7.921  40.252 22.333  1.00 49.66  ? 9   PRO   A C    1 
ATOM   69   O  O    . PRO   A 1 9   ? -7.061  40.702 21.576  1.00 44.24  ? 9   PRO   A O    1 
ATOM   70   C  CB   . PRO   A 1 9   ? -6.867  40.451 24.624  1.00 39.01  ? 9   PRO   A CB   1 
ATOM   71   C  CG   . PRO   A 1 9   ? -5.801  39.603 25.260  1.00 54.06  ? 9   PRO   A CG   1 
ATOM   72   C  CD   . PRO   A 1 9   ? -5.309  38.702 24.172  1.00 38.56  ? 9   PRO   A CD   1 
ATOM   73   N  N    . SER   A 1 10  ? -9.223  40.361 22.087  1.00 42.46  ? 10  SER   A N    1 
ATOM   74   C  CA   . SER   A 1 10  ? -9.734  40.886 20.827  1.00 48.66  ? 10  SER   A CA   1 
ATOM   75   C  C    . SER   A 1 10  ? -10.001 42.385 20.857  1.00 41.97  ? 10  SER   A C    1 
ATOM   76   O  O    . SER   A 1 10  ? -10.506 42.925 19.867  1.00 50.38  ? 10  SER   A O    1 
ATOM   77   C  CB   . SER   A 1 10  ? -11.023 40.155 20.445  1.00 43.17  ? 10  SER   A CB   1 
ATOM   78   O  OG   . SER   A 1 10  ? -12.023 40.378 21.426  1.00 46.59  ? 10  SER   A OG   1 
ATOM   79   N  N    . GLY   A 1 11  ? -9.683  43.066 21.959  1.00 46.59  ? 11  GLY   A N    1 
ATOM   80   C  CA   . GLY   A 1 11  ? -10.019 44.478 22.070  1.00 44.07  ? 11  GLY   A CA   1 
ATOM   81   C  C    . GLY   A 1 11  ? -9.491  45.306 20.917  1.00 44.23  ? 11  GLY   A C    1 
ATOM   82   O  O    . GLY   A 1 11  ? -10.227 46.080 20.301  1.00 54.27  ? 11  GLY   A O    1 
ATOM   83   N  N    . LYS   A 1 12  ? -8.202  45.154 20.602  1.00 50.75  ? 12  LYS   A N    1 
ATOM   84   C  CA   . LYS   A 1 12  ? -7.604  45.983 19.559  1.00 48.35  ? 12  LYS   A CA   1 
ATOM   85   C  C    . LYS   A 1 12  ? -8.264  45.757 18.206  1.00 47.40  ? 12  LYS   A C    1 
ATOM   86   O  O    . LYS   A 1 12  ? -8.234  46.646 17.346  1.00 44.28  ? 12  LYS   A O    1 
ATOM   87   C  CB   . LYS   A 1 12  ? -6.104  45.712 19.464  1.00 44.31  ? 12  LYS   A CB   1 
ATOM   88   C  CG   . LYS   A 1 12  ? -5.299  46.306 20.603  1.00 50.61  ? 12  LYS   A CG   1 
ATOM   89   C  CD   . LYS   A 1 12  ? -3.818  46.294 20.278  1.00 46.90  ? 12  LYS   A CD   1 
ATOM   90   C  CE   . LYS   A 1 12  ? -2.968  46.320 21.538  1.00 70.62  ? 12  LYS   A CE   1 
ATOM   91   N  NZ   . LYS   A 1 12  ? -3.701  46.873 22.714  1.00 70.49  ? 12  LYS   A NZ   1 
ATOM   92   N  N    . VAL   A 1 13  ? -8.855  44.586 17.992  1.00 46.29  ? 13  VAL   A N    1 
ATOM   93   C  CA   . VAL   A 1 13  ? -9.484  44.311 16.706  1.00 49.17  ? 13  VAL   A CA   1 
ATOM   94   C  C    . VAL   A 1 13  ? -10.958 44.709 16.701  1.00 55.44  ? 13  VAL   A C    1 
ATOM   95   O  O    . VAL   A 1 13  ? -11.504 45.036 15.639  1.00 44.43  ? 13  VAL   A O    1 
ATOM   96   C  CB   . VAL   A 1 13  ? -9.311  42.830 16.332  1.00 39.85  ? 13  VAL   A CB   1 
ATOM   97   C  CG1  . VAL   A 1 13  ? -10.198 42.474 15.136  1.00 41.90  ? 13  VAL   A CG1  1 
ATOM   98   C  CG2  . VAL   A 1 13  ? -7.848  42.532 16.036  1.00 40.41  ? 13  VAL   A CG2  1 
ATOM   99   N  N    . GLU   A 1 14  ? -11.610 44.700 17.868  1.00 45.52  ? 14  GLU   A N    1 
ATOM   100  C  CA   . GLU   A 1 14  ? -13.027 45.045 17.935  1.00 46.01  ? 14  GLU   A CA   1 
ATOM   101  C  C    . GLU   A 1 14  ? -13.276 46.446 17.385  1.00 53.32  ? 14  GLU   A C    1 
ATOM   102  O  O    . GLU   A 1 14  ? -14.231 46.667 16.628  1.00 47.06  ? 14  GLU   A O    1 
ATOM   103  C  CB   . GLU   A 1 14  ? -13.522 44.924 19.383  1.00 45.87  ? 14  GLU   A CB   1 
ATOM   104  C  CG   . GLU   A 1 14  ? -13.917 43.501 19.813  1.00 44.73  ? 14  GLU   A CG   1 
ATOM   105  C  CD   . GLU   A 1 14  ? -14.073 43.353 21.328  1.00 54.58  ? 14  GLU   A CD   1 
ATOM   106  O  OE1  . GLU   A 1 14  ? -13.349 42.526 21.926  1.00 50.23  ? 14  GLU   A OE1  1 
ATOM   107  O  OE2  . GLU   A 1 14  ? -14.913 44.064 21.924  1.00 50.44  ? 14  GLU   A OE2  1 
ATOM   108  N  N    . GLY   A 1 15  ? -12.402 47.385 17.711  1.00 52.45  ? 15  GLY   A N    1 
ATOM   109  C  CA   . GLY   A 1 15  ? -12.555 48.749 17.235  1.00 55.63  ? 15  GLY   A CA   1 
ATOM   110  C  C    . GLY   A 1 15  ? -12.358 48.990 15.760  1.00 47.88  ? 15  GLY   A C    1 
ATOM   111  O  O    . GLY   A 1 15  ? -12.255 50.124 15.338  1.00 55.21  ? 15  GLY   A O    1 
ATOM   112  N  N    . CYS   A 1 16  ? -12.309 47.932 14.983  1.00 42.40  ? 16  CYS   A N    1 
ATOM   113  C  CA   . CYS   A 1 16  ? -12.125 48.054 13.566  1.00 47.65  ? 16  CYS   A CA   1 
ATOM   114  C  C    . CYS   A 1 16  ? -13.224 47.369 12.740  1.00 43.40  ? 16  CYS   A C    1 
ATOM   115  O  O    . CYS   A 1 16  ? -13.276 47.554 11.548  1.00 51.64  ? 16  CYS   A O    1 
ATOM   116  C  CB   . CYS   A 1 16  ? -10.755 47.519 13.191  1.00 36.17  ? 16  CYS   A CB   1 
ATOM   117  S  SG   . CYS   A 1 16  ? -9.364  48.139 14.145  1.00 54.02  ? 16  CYS   A SG   1 
ATOM   118  N  N    . MET   A 1 17  ? -14.104 46.601 13.368  1.00 38.72  ? 17  MET   A N    1 
ATOM   119  C  CA   . MET   A 1 17  ? -15.168 45.934 12.630  1.00 40.45  ? 17  MET   A CA   1 
ATOM   120  C  C    . MET   A 1 17  ? -16.229 46.947 12.199  1.00 50.54  ? 17  MET   A C    1 
ATOM   121  O  O    . MET   A 1 17  ? -16.707 47.746 13.008  1.00 46.04  ? 17  MET   A O    1 
ATOM   122  C  CB   . MET   A 1 17  ? -15.793 44.841 13.492  1.00 43.10  ? 17  MET   A CB   1 
ATOM   123  C  CG   . MET   A 1 17  ? -14.897 43.611 13.708  1.00 36.83  ? 17  MET   A CG   1 
ATOM   124  S  SD   . MET   A 1 17  ? -13.609 43.348 12.467  1.00 51.75  ? 17  MET   A SD   1 
ATOM   125  C  CE   . MET   A 1 17  ? -14.603 42.839 11.062  1.00 43.34  ? 17  MET   A CE   1 
ATOM   126  N  N    . VAL   A 1 18  ? -16.595 46.918 10.917  1.00 43.53  ? 18  VAL   A N    1 
ATOM   127  C  CA   . VAL   A 1 18  ? -17.660 47.753 10.377  1.00 44.39  ? 18  VAL   A CA   1 
ATOM   128  C  C    . VAL   A 1 18  ? -18.559 46.882 9.509   1.00 46.34  ? 18  VAL   A C    1 
ATOM   129  O  O    . VAL   A 1 18  ? -18.208 45.760 9.139   1.00 45.52  ? 18  VAL   A O    1 
ATOM   130  C  CB   . VAL   A 1 18  ? -17.117 48.941 9.558   1.00 43.42  ? 18  VAL   A CB   1 
ATOM   131  C  CG1  . VAL   A 1 18  ? -16.214 49.808 10.417  1.00 49.29  ? 18  VAL   A CG1  1 
ATOM   132  C  CG2  . VAL   A 1 18  ? -16.373 48.433 8.333   1.00 40.40  ? 18  VAL   A CG2  1 
ATOM   133  N  N    . GLN   A 1 19  ? -19.735 47.415 9.188   1.00 48.03  ? 19  GLN   A N    1 
ATOM   134  C  CA   . GLN   A 1 19  ? -20.665 46.775 8.268   1.00 49.31  ? 19  GLN   A CA   1 
ATOM   135  C  C    . GLN   A 1 19  ? -20.547 47.427 6.897   1.00 43.74  ? 19  GLN   A C    1 
ATOM   136  O  O    . GLN   A 1 19  ? -20.540 48.657 6.788   1.00 50.76  ? 19  GLN   A O    1 
ATOM   137  C  CB   . GLN   A 1 19  ? -22.102 46.879 8.778   1.00 44.87  ? 19  GLN   A CB   1 
ATOM   138  C  CG   . GLN   A 1 19  ? -23.095 46.042 7.994   1.00 52.34  ? 19  GLN   A CG   1 
ATOM   139  C  CD   . GLN   A 1 19  ? -24.465 45.998 8.642   1.00 68.82  ? 19  GLN   A CD   1 
ATOM   140  O  OE1  . GLN   A 1 19  ? -24.715 46.670 9.645   1.00 73.17  ? 19  GLN   A OE1  1 
ATOM   141  N  NE2  . GLN   A 1 19  ? -25.360 45.199 8.074   1.00 66.63  ? 19  GLN   A NE2  1 
ATOM   142  N  N    . VAL   A 1 20  ? -20.453 46.604 5.857   1.00 47.12  ? 20  VAL   A N    1 
ATOM   143  C  CA   . VAL   A 1 20  ? -20.338 47.068 4.478   1.00 47.91  ? 20  VAL   A CA   1 
ATOM   144  C  C    . VAL   A 1 20  ? -21.529 46.538 3.693   1.00 52.14  ? 20  VAL   A C    1 
ATOM   145  O  O    . VAL   A 1 20  ? -21.830 45.339 3.750   1.00 47.99  ? 20  VAL   A O    1 
ATOM   146  C  CB   . VAL   A 1 20  ? -19.019 46.608 3.832   1.00 45.89  ? 20  VAL   A CB   1 
ATOM   147  C  CG1  . VAL   A 1 20  ? -18.993 46.985 2.354   1.00 46.83  ? 20  VAL   A CG1  1 
ATOM   148  C  CG2  . VAL   A 1 20  ? -17.821 47.188 4.577   1.00 38.81  ? 20  VAL   A CG2  1 
ATOM   149  N  N    . THR   A 1 21  ? -22.199 47.424 2.959   1.00 50.44  ? 21  THR   A N    1 
ATOM   150  C  CA   . THR   A 1 21  ? -23.372 47.058 2.178   1.00 53.74  ? 21  THR   A CA   1 
ATOM   151  C  C    . THR   A 1 21  ? -23.255 47.588 0.756   1.00 54.82  ? 21  THR   A C    1 
ATOM   152  O  O    . THR   A 1 21  ? -22.855 48.734 0.537   1.00 52.23  ? 21  THR   A O    1 
ATOM   153  C  CB   . THR   A 1 21  ? -24.663 47.594 2.811   1.00 62.13  ? 21  THR   A CB   1 
ATOM   154  O  OG1  . THR   A 1 21  ? -24.814 47.053 4.129   1.00 51.88  ? 21  THR   A OG1  1 
ATOM   155  C  CG2  . THR   A 1 21  ? -25.874 47.213 1.959   1.00 56.26  ? 21  THR   A CG2  1 
ATOM   156  N  N    . CYS   A 1 22  ? -23.613 46.739 -0.204  1.00 56.52  ? 22  CYS   A N    1 
ATOM   157  C  CA   . CYS   A 1 22  ? -23.692 47.095 -1.616  1.00 50.59  ? 22  CYS   A CA   1 
ATOM   158  C  C    . CYS   A 1 22  ? -24.996 46.517 -2.147  1.00 52.95  ? 22  CYS   A C    1 
ATOM   159  O  O    . CYS   A 1 22  ? -25.130 45.295 -2.274  1.00 65.55  ? 22  CYS   A O    1 
ATOM   160  C  CB   . CYS   A 1 22  ? -22.491 46.556 -2.397  1.00 51.25  ? 22  CYS   A CB   1 
ATOM   161  S  SG   . CYS   A 1 22  ? -22.204 47.366 -4.000  1.00 73.43  ? 22  CYS   A SG   1 
ATOM   162  N  N    . GLY   A 1 23  ? -25.959 47.384 -2.440  1.00 55.56  ? 23  GLY   A N    1 
ATOM   163  C  CA   . GLY   A 1 23  ? -27.279 46.928 -2.831  1.00 64.33  ? 23  GLY   A CA   1 
ATOM   164  C  C    . GLY   A 1 23  ? -27.992 46.253 -1.678  1.00 64.98  ? 23  GLY   A C    1 
ATOM   165  O  O    . GLY   A 1 23  ? -28.313 46.902 -0.677  1.00 65.02  ? 23  GLY   A O    1 
ATOM   166  N  N    . THR   A 1 24  ? -28.241 44.950 -1.801  1.00 68.49  ? 24  THR   A N    1 
ATOM   167  C  CA   . THR   A 1 24  ? -28.812 44.159 -0.718  1.00 60.02  ? 24  THR   A CA   1 
ATOM   168  C  C    . THR   A 1 24  ? -27.820 43.168 -0.129  1.00 65.97  ? 24  THR   A C    1 
ATOM   169  O  O    . THR   A 1 24  ? -28.174 42.437 0.801   1.00 60.97  ? 24  THR   A O    1 
ATOM   170  C  CB   . THR   A 1 24  ? -30.058 43.404 -1.198  1.00 66.15  ? 24  THR   A CB   1 
ATOM   171  O  OG1  . THR   A 1 24  ? -29.813 42.849 -2.496  1.00 74.35  ? 24  THR   A OG1  1 
ATOM   172  C  CG2  . THR   A 1 24  ? -31.255 44.346 -1.270  1.00 63.97  ? 24  THR   A CG2  1 
ATOM   173  N  N    . THR   A 1 25  ? -26.596 43.116 -0.648  1.00 59.96  ? 25  THR   A N    1 
ATOM   174  C  CA   . THR   A 1 25  ? -25.563 42.242 -0.114  1.00 59.64  ? 25  THR   A CA   1 
ATOM   175  C  C    . THR   A 1 25  ? -24.825 42.970 1.002   1.00 61.45  ? 25  THR   A C    1 
ATOM   176  O  O    . THR   A 1 25  ? -24.410 44.121 0.831   1.00 52.33  ? 25  THR   A O    1 
ATOM   177  C  CB   . THR   A 1 25  ? -24.588 41.817 -1.213  1.00 60.92  ? 25  THR   A CB   1 
ATOM   178  O  OG1  . THR   A 1 25  ? -25.318 41.281 -2.324  1.00 58.55  ? 25  THR   A OG1  1 
ATOM   179  C  CG2  . THR   A 1 25  ? -23.628 40.754 -0.692  1.00 56.96  ? 25  THR   A CG2  1 
ATOM   180  N  N    . THR   A 1 26  ? -24.661 42.299 2.140   1.00 59.67  ? 26  THR   A N    1 
ATOM   181  C  CA   . THR   A 1 26  ? -24.100 42.933 3.322   1.00 54.42  ? 26  THR   A CA   1 
ATOM   182  C  C    . THR   A 1 26  ? -23.159 41.967 4.028   1.00 48.02  ? 26  THR   A C    1 
ATOM   183  O  O    . THR   A 1 26  ? -23.402 40.758 4.057   1.00 51.41  ? 26  THR   A O    1 
ATOM   184  C  CB   . THR   A 1 26  ? -25.215 43.396 4.273   1.00 53.49  ? 26  THR   A CB   1 
ATOM   185  O  OG1  . THR   A 1 26  ? -24.699 44.369 5.189   1.00 62.66  ? 26  THR   A OG1  1 
ATOM   186  C  CG2  . THR   A 1 26  ? -25.793 42.218 5.042   1.00 55.39  ? 26  THR   A CG2  1 
ATOM   187  N  N    . LEU   A 1 27  ? -22.082 42.505 4.591   1.00 44.91  ? 27  LEU   A N    1 
ATOM   188  C  CA   . LEU   A 1 27  ? -21.088 41.680 5.264   1.00 45.99  ? 27  LEU   A CA   1 
ATOM   189  C  C    . LEU   A 1 27  ? -20.188 42.582 6.098   1.00 48.32  ? 27  LEU   A C    1 
ATOM   190  O  O    . LEU   A 1 27  ? -20.332 43.809 6.101   1.00 42.95  ? 27  LEU   A O    1 
ATOM   191  C  CB   . LEU   A 1 27  ? -20.284 40.850 4.259   1.00 43.58  ? 27  LEU   A CB   1 
ATOM   192  C  CG   . LEU   A 1 27  ? -19.795 41.541 2.985   1.00 42.95  ? 27  LEU   A CG   1 
ATOM   193  C  CD1  . LEU   A 1 27  ? -18.849 42.697 3.306   1.00 40.42  ? 27  LEU   A CD1  1 
ATOM   194  C  CD2  . LEU   A 1 27  ? -19.126 40.527 2.064   1.00 40.40  ? 27  LEU   A CD2  1 
ATOM   195  N  N    . ASN   A 1 28  ? -19.247 41.957 6.799   1.00 33.74  ? 28  ASN   A N    1 
ATOM   196  C  CA   . ASN   A 1 28  ? -18.370 42.643 7.734   1.00 37.84  ? 28  ASN   A CA   1 
ATOM   197  C  C    . ASN   A 1 28  ? -17.146 43.196 7.023   1.00 41.41  ? 28  ASN   A C    1 
ATOM   198  O  O    . ASN   A 1 28  ? -16.678 42.639 6.027   1.00 43.87  ? 28  ASN   A O    1 
ATOM   199  C  CB   . ASN   A 1 28  ? -17.919 41.695 8.848   1.00 38.98  ? 28  ASN   A CB   1 
ATOM   200  C  CG   . ASN   A 1 28  ? -19.080 41.077 9.591   1.00 41.69  ? 28  ASN   A CG   1 
ATOM   201  O  OD1  . ASN   A 1 28  ? -19.817 41.764 10.297  1.00 49.54  ? 28  ASN   A OD1  1 
ATOM   202  N  ND2  . ASN   A 1 28  ? -19.249 39.771 9.438   1.00 46.97  ? 28  ASN   A ND2  1 
ATOM   203  N  N    . GLY   A 1 29  ? -16.616 44.293 7.567   1.00 34.60  ? 29  GLY   A N    1 
ATOM   204  C  CA   . GLY   A 1 29  ? -15.430 44.912 7.021   1.00 37.55  ? 29  GLY   A CA   1 
ATOM   205  C  C    . GLY   A 1 29  ? -14.460 45.297 8.120   1.00 45.27  ? 29  GLY   A C    1 
ATOM   206  O  O    . GLY   A 1 29  ? -14.811 45.364 9.300   1.00 39.67  ? 29  GLY   A O    1 
ATOM   207  N  N    . LEU   A 1 30  ? -13.219 45.555 7.708   1.00 35.87  ? 30  LEU   A N    1 
ATOM   208  C  CA   . LEU   A 1 30  ? -12.129 45.896 8.615   1.00 38.04  ? 30  LEU   A CA   1 
ATOM   209  C  C    . LEU   A 1 30  ? -11.629 47.294 8.276   1.00 39.99  ? 30  LEU   A C    1 
ATOM   210  O  O    . LEU   A 1 30  ? -11.100 47.523 7.182   1.00 40.52  ? 30  LEU   A O    1 
ATOM   211  C  CB   . LEU   A 1 30  ? -10.996 44.866 8.530   1.00 30.22  ? 30  LEU   A CB   1 
ATOM   212  C  CG   . LEU   A 1 30  ? -9.872  44.967 9.569   1.00 47.37  ? 30  LEU   A CG   1 
ATOM   213  C  CD1  . LEU   A 1 30  ? -10.362 44.577 10.963  1.00 34.36  ? 30  LEU   A CD1  1 
ATOM   214  C  CD2  . LEU   A 1 30  ? -8.674  44.110 9.165   1.00 33.02  ? 30  LEU   A CD2  1 
ATOM   215  N  N    . TRP   A 1 31  ? -11.787 48.219 9.223   1.00 44.34  ? 31  TRP   A N    1 
ATOM   216  C  CA   . TRP   A 1 31  ? -11.481 49.632 9.025   1.00 41.11  ? 31  TRP   A CA   1 
ATOM   217  C  C    . TRP   A 1 31  ? -10.143 49.942 9.688   1.00 46.59  ? 31  TRP   A C    1 
ATOM   218  O  O    . TRP   A 1 31  ? -10.048 49.990 10.918  1.00 42.84  ? 31  TRP   A O    1 
ATOM   219  C  CB   . TRP   A 1 31  ? -12.603 50.493 9.603   1.00 38.02  ? 31  TRP   A CB   1 
ATOM   220  C  CG   . TRP   A 1 31  ? -12.424 51.977 9.462   1.00 45.35  ? 31  TRP   A CG   1 
ATOM   221  C  CD1  . TRP   A 1 31  ? -11.674 52.636 8.530   1.00 49.03  ? 31  TRP   A CD1  1 
ATOM   222  C  CD2  . TRP   A 1 31  ? -13.028 52.988 10.279  1.00 52.10  ? 31  TRP   A CD2  1 
ATOM   223  N  NE1  . TRP   A 1 31  ? -11.770 53.998 8.721   1.00 47.51  ? 31  TRP   A NE1  1 
ATOM   224  C  CE2  . TRP   A 1 31  ? -12.596 54.238 9.788   1.00 50.72  ? 31  TRP   A CE2  1 
ATOM   225  C  CE3  . TRP   A 1 31  ? -13.890 52.956 11.381  1.00 48.88  ? 31  TRP   A CE3  1 
ATOM   226  C  CZ2  . TRP   A 1 31  ? -12.996 55.443 10.362  1.00 53.38  ? 31  TRP   A CZ2  1 
ATOM   227  C  CZ3  . TRP   A 1 31  ? -14.287 54.153 11.948  1.00 56.32  ? 31  TRP   A CZ3  1 
ATOM   228  C  CH2  . TRP   A 1 31  ? -13.840 55.381 11.437  1.00 52.69  ? 31  TRP   A CH2  1 
ATOM   229  N  N    . LEU   A 1 32  ? -9.109  50.144 8.875   1.00 42.85  ? 32  LEU   A N    1 
ATOM   230  C  CA   . LEU   A 1 32  ? -7.789  50.527 9.362   1.00 45.28  ? 32  LEU   A CA   1 
ATOM   231  C  C    . LEU   A 1 32  ? -7.367  51.799 8.645   1.00 52.28  ? 32  LEU   A C    1 
ATOM   232  O  O    . LEU   A 1 32  ? -7.353  51.842 7.411   1.00 46.72  ? 32  LEU   A O    1 
ATOM   233  C  CB   . LEU   A 1 32  ? -6.768  49.411 9.132   1.00 44.40  ? 32  LEU   A CB   1 
ATOM   234  C  CG   . LEU   A 1 32  ? -7.145  48.049 9.718   1.00 45.73  ? 32  LEU   A CG   1 
ATOM   235  C  CD1  . LEU   A 1 32  ? -6.447  46.926 8.969   1.00 35.13  ? 32  LEU   A CD1  1 
ATOM   236  C  CD2  . LEU   A 1 32  ? -6.818  47.996 11.207  1.00 39.78  ? 32  LEU   A CD2  1 
ATOM   237  N  N    . ASP   A 1 33  ? -7.022  52.826 9.416   1.00 54.27  ? 33  ASP   A N    1 
ATOM   238  C  CA   . ASP   A 1 33  ? -6.698  54.152 8.877   1.00 56.89  ? 33  ASP   A CA   1 
ATOM   239  C  C    . ASP   A 1 33  ? -7.925  54.616 8.094   1.00 58.24  ? 33  ASP   A C    1 
ATOM   240  O  O    . ASP   A 1 33  ? -9.041  54.566 8.634   1.00 56.28  ? 33  ASP   A O    1 
ATOM   241  C  CB   . ASP   A 1 33  ? -5.396  54.083 8.089   1.00 63.43  ? 33  ASP   A CB   1 
ATOM   242  C  CG   . ASP   A 1 33  ? -4.208  53.699 8.954   1.00 75.58  ? 33  ASP   A CG   1 
ATOM   243  O  OD1  . ASP   A 1 33  ? -4.165  54.106 10.136  1.00 77.21  ? 33  ASP   A OD1  1 
ATOM   244  O  OD2  . ASP   A 1 33  ? -3.314  52.987 8.446   1.00 77.22  ? 33  ASP   A OD2  1 
ATOM   245  N  N    . ASP   A 1 34  ? -7.781  55.056 6.845   1.00 55.31  ? 34  ASP   A N    1 
ATOM   246  C  CA   . ASP   A 1 34  ? -8.903  55.531 6.046   1.00 56.06  ? 34  ASP   A CA   1 
ATOM   247  C  C    . ASP   A 1 34  ? -9.264  54.555 4.930   1.00 53.62  ? 34  ASP   A C    1 
ATOM   248  O  O    . ASP   A 1 34  ? -9.770  54.963 3.881   1.00 55.73  ? 34  ASP   A O    1 
ATOM   249  C  CB   . ASP   A 1 34  ? -8.601  56.912 5.469   1.00 50.27  ? 34  ASP   A CB   1 
ATOM   250  C  CG   . ASP   A 1 34  ? -7.498  56.880 4.427   1.00 68.46  ? 34  ASP   A CG   1 
ATOM   251  O  OD1  . ASP   A 1 34  ? -6.635  55.980 4.503   1.00 68.25  ? 34  ASP   A OD1  1 
ATOM   252  O  OD2  . ASP   A 1 34  ? -7.490  57.756 3.534   1.00 81.43  ? 34  ASP   A OD2  1 
ATOM   253  N  N    . VAL   A 1 35  ? -9.007  53.266 5.139   1.00 49.37  ? 35  VAL   A N    1 
ATOM   254  C  CA   . VAL   A 1 35  ? -9.330  52.229 4.167   1.00 45.91  ? 35  VAL   A CA   1 
ATOM   255  C  C    . VAL   A 1 35  ? -10.169 51.167 4.856   1.00 46.24  ? 35  VAL   A C    1 
ATOM   256  O  O    . VAL   A 1 35  ? -9.937  50.840 6.025   1.00 46.58  ? 35  VAL   A O    1 
ATOM   257  C  CB   . VAL   A 1 35  ? -8.067  51.594 3.549   1.00 46.04  ? 35  VAL   A CB   1 
ATOM   258  C  CG1  . VAL   A 1 35  ? -8.442  50.369 2.723   1.00 42.98  ? 35  VAL   A CG1  1 
ATOM   259  C  CG2  . VAL   A 1 35  ? -7.329  52.606 2.698   1.00 43.18  ? 35  VAL   A CG2  1 
ATOM   260  N  N    . VAL   A 1 36  ? -11.139 50.623 4.130   1.00 44.14  ? 36  VAL   A N    1 
ATOM   261  C  CA   . VAL   A 1 36  ? -11.992 49.556 4.636   1.00 46.13  ? 36  VAL   A CA   1 
ATOM   262  C  C    . VAL   A 1 36  ? -11.787 48.339 3.746   1.00 47.36  ? 36  VAL   A C    1 
ATOM   263  O  O    . VAL   A 1 36  ? -11.967 48.418 2.524   1.00 46.34  ? 36  VAL   A O    1 
ATOM   264  C  CB   . VAL   A 1 36  ? -13.468 49.977 4.681   1.00 49.49  ? 36  VAL   A CB   1 
ATOM   265  C  CG1  . VAL   A 1 36  ? -14.355 48.785 5.007   1.00 40.48  ? 36  VAL   A CG1  1 
ATOM   266  C  CG2  . VAL   A 1 36  ? -13.661 51.091 5.698   1.00 42.81  ? 36  VAL   A CG2  1 
ATOM   267  N  N    . TYR   A 1 37  ? -11.398 47.226 4.355   1.00 38.80  ? 37  TYR   A N    1 
ATOM   268  C  CA   . TYR   A 1 37  ? -11.171 45.973 3.653   1.00 34.64  ? 37  TYR   A CA   1 
ATOM   269  C  C    . TYR   A 1 37  ? -12.349 45.042 3.889   1.00 42.80  ? 37  TYR   A C    1 
ATOM   270  O  O    . TYR   A 1 37  ? -12.849 44.928 5.012   1.00 48.42  ? 37  TYR   A O    1 
ATOM   271  C  CB   . TYR   A 1 37  ? -9.879  45.296 4.127   1.00 38.53  ? 37  TYR   A CB   1 
ATOM   272  C  CG   . TYR   A 1 37  ? -8.664  46.193 4.101   1.00 39.84  ? 37  TYR   A CG   1 
ATOM   273  C  CD1  . TYR   A 1 37  ? -8.464  47.158 5.083   1.00 36.29  ? 37  TYR   A CD1  1 
ATOM   274  C  CD2  . TYR   A 1 37  ? -7.728  46.092 3.079   1.00 43.94  ? 37  TYR   A CD2  1 
ATOM   275  C  CE1  . TYR   A 1 37  ? -7.358  47.988 5.051   1.00 45.04  ? 37  TYR   A CE1  1 
ATOM   276  C  CE2  . TYR   A 1 37  ? -6.620  46.918 3.038   1.00 34.05  ? 37  TYR   A CE2  1 
ATOM   277  C  CZ   . TYR   A 1 37  ? -6.440  47.863 4.025   1.00 40.43  ? 37  TYR   A CZ   1 
ATOM   278  O  OH   . TYR   A 1 37  ? -5.338  48.684 3.988   1.00 46.50  ? 37  TYR   A OH   1 
ATOM   279  N  N    . CYS   A 1 38  ? -12.787 44.374 2.827   1.00 41.41  ? 38  CYS   A N    1 
ATOM   280  C  CA   . CYS   A 1 38  ? -13.870 43.409 2.916   1.00 32.44  ? 38  CYS   A CA   1 
ATOM   281  C  C    . CYS   A 1 38  ? -13.818 42.518 1.687   1.00 38.51  ? 38  CYS   A C    1 
ATOM   282  O  O    . CYS   A 1 38  ? -13.143 42.849 0.705   1.00 42.92  ? 38  CYS   A O    1 
ATOM   283  C  CB   . CYS   A 1 38  ? -15.235 44.106 3.025   1.00 44.10  ? 38  CYS   A CB   1 
ATOM   284  S  SG   . CYS   A 1 38  ? -15.798 44.884 1.492   1.00 48.94  ? 38  CYS   A SG   1 
ATOM   285  N  N    . PRO   A 1 39  ? -14.493 41.372 1.716   1.00 41.65  ? 39  PRO   A N    1 
ATOM   286  C  CA   . PRO   A 1 39  ? -14.526 40.512 0.528   1.00 40.77  ? 39  PRO   A CA   1 
ATOM   287  C  C    . PRO   A 1 39  ? -15.200 41.218 -0.639  1.00 46.23  ? 39  PRO   A C    1 
ATOM   288  O  O    . PRO   A 1 39  ? -16.226 41.883 -0.480  1.00 40.70  ? 39  PRO   A O    1 
ATOM   289  C  CB   . PRO   A 1 39  ? -15.333 39.294 0.991   1.00 39.15  ? 39  PRO   A CB   1 
ATOM   290  C  CG   . PRO   A 1 39  ? -15.208 39.295 2.486   1.00 41.82  ? 39  PRO   A CG   1 
ATOM   291  C  CD   . PRO   A 1 39  ? -15.137 40.742 2.881   1.00 41.07  ? 39  PRO   A CD   1 
ATOM   292  N  N    . ARG   A 1 40  ? -14.605 41.070 -1.824  1.00 38.75  ? 40  ARG   A N    1 
ATOM   293  C  CA   . ARG   A 1 40  ? -15.199 41.644 -3.025  1.00 49.72  ? 40  ARG   A CA   1 
ATOM   294  C  C    . ARG   A 1 40  ? -16.547 41.015 -3.355  1.00 43.89  ? 40  ARG   A C    1 
ATOM   295  O  O    . ARG   A 1 40  ? -17.326 41.605 -4.110  1.00 47.23  ? 40  ARG   A O    1 
ATOM   296  C  CB   . ARG   A 1 40  ? -14.238 41.497 -4.206  1.00 44.04  ? 40  ARG   A CB   1 
ATOM   297  C  CG   . ARG   A 1 40  ? -14.101 40.081 -4.724  1.00 36.05  ? 40  ARG   A CG   1 
ATOM   298  C  CD   . ARG   A 1 40  ? -13.215 40.040 -5.956  1.00 46.20  ? 40  ARG   A CD   1 
ATOM   299  N  NE   . ARG   A 1 40  ? -12.917 38.675 -6.369  1.00 47.81  ? 40  ARG   A NE   1 
ATOM   300  C  CZ   . ARG   A 1 40  ? -12.198 38.360 -7.437  1.00 55.88  ? 40  ARG   A CZ   1 
ATOM   301  N  NH1  . ARG   A 1 40  ? -11.692 39.291 -8.230  1.00 39.70  ? 40  ARG   A NH1  1 
ATOM   302  N  NH2  . ARG   A 1 40  ? -11.985 37.077 -7.719  1.00 45.57  ? 40  ARG   A NH2  1 
ATOM   303  N  N    . HIS   A 1 41  ? -16.845 39.842 -2.792  1.00 44.39  ? 41  HIS   A N    1 
ATOM   304  C  CA   . HIS   A 1 41  ? -18.133 39.197 -3.028  1.00 49.38  ? 41  HIS   A CA   1 
ATOM   305  C  C    . HIS   A 1 41  ? -19.308 40.108 -2.691  1.00 44.88  ? 41  HIS   A C    1 
ATOM   306  O  O    . HIS   A 1 41  ? -20.417 39.879 -3.186  1.00 48.59  ? 41  HIS   A O    1 
ATOM   307  C  CB   . HIS   A 1 41  ? -18.214 37.902 -2.211  1.00 51.72  ? 41  HIS   A CB   1 
ATOM   308  C  CG   . HIS   A 1 41  ? -19.324 36.987 -2.627  1.00 58.51  ? 41  HIS   A CG   1 
ATOM   309  N  ND1  . HIS   A 1 41  ? -19.364 36.381 -3.864  1.00 60.11  ? 41  HIS   A ND1  1 
ATOM   310  C  CD2  . HIS   A 1 41  ? -20.429 36.567 -1.966  1.00 61.10  ? 41  HIS   A CD2  1 
ATOM   311  C  CE1  . HIS   A 1 41  ? -20.450 35.634 -3.951  1.00 66.35  ? 41  HIS   A CE1  1 
ATOM   312  N  NE2  . HIS   A 1 41  ? -21.113 35.729 -2.812  1.00 72.01  ? 41  HIS   A NE2  1 
ATOM   313  N  N    . VAL   A 1 42  ? -19.088 41.141 -1.872  1.00 36.83  ? 42  VAL   A N    1 
ATOM   314  C  CA   . VAL   A 1 42  ? -20.168 42.037 -1.473  1.00 48.74  ? 42  VAL   A CA   1 
ATOM   315  C  C    . VAL   A 1 42  ? -20.795 42.762 -2.657  1.00 54.02  ? 42  VAL   A C    1 
ATOM   316  O  O    . VAL   A 1 42  ? -21.947 43.199 -2.569  1.00 50.02  ? 42  VAL   A O    1 
ATOM   317  C  CB   . VAL   A 1 42  ? -19.663 43.055 -0.430  1.00 40.63  ? 42  VAL   A CB   1 
ATOM   318  C  CG1  . VAL   A 1 42  ? -18.680 44.022 -1.067  1.00 41.21  ? 42  VAL   A CG1  1 
ATOM   319  C  CG2  . VAL   A 1 42  ? -20.836 43.811 0.178   1.00 43.53  ? 42  VAL   A CG2  1 
ATOM   320  N  N    . ILE   A 1 43  ? -20.062 42.917 -3.766  1.00 48.09  ? 43  ILE   A N    1 
ATOM   321  C  CA   . ILE   A 1 43  ? -20.598 43.636 -4.922  1.00 57.35  ? 43  ILE   A CA   1 
ATOM   322  C  C    . ILE   A 1 43  ? -21.449 42.757 -5.822  1.00 55.47  ? 43  ILE   A C    1 
ATOM   323  O  O    . ILE   A 1 43  ? -21.949 43.240 -6.846  1.00 61.99  ? 43  ILE   A O    1 
ATOM   324  C  CB   . ILE   A 1 43  ? -19.469 44.268 -5.760  1.00 57.54  ? 43  ILE   A CB   1 
ATOM   325  C  CG1  . ILE   A 1 43  ? -18.801 43.210 -6.637  1.00 54.67  ? 43  ILE   A CG1  1 
ATOM   326  C  CG2  . ILE   A 1 43  ? -18.449 44.948 -4.855  1.00 46.48  ? 43  ILE   A CG2  1 
ATOM   327  C  CD1  . ILE   A 1 43  ? -17.647 43.740 -7.461  1.00 57.58  ? 43  ILE   A CD1  1 
ATOM   328  N  N    . CYS   A 1 44  ? -21.628 41.484 -5.476  1.00 55.84  ? 44  CYS   A N    1 
ATOM   329  C  CA   . CYS   A 1 44  ? -22.460 40.575 -6.251  1.00 59.41  ? 44  CYS   A CA   1 
ATOM   330  C  C    . CYS   A 1 44  ? -23.905 40.653 -5.781  1.00 68.59  ? 44  CYS   A C    1 
ATOM   331  O  O    . CYS   A 1 44  ? -24.175 40.622 -4.576  1.00 66.44  ? 44  CYS   A O    1 
ATOM   332  C  CB   . CYS   A 1 44  ? -21.970 39.131 -6.120  1.00 60.15  ? 44  CYS   A CB   1 
ATOM   333  S  SG   . CYS   A 1 44  ? -20.350 38.783 -6.818  1.00 62.29  ? 44  CYS   A SG   1 
ATOM   334  N  N    . THR   A 1 45  ? -24.827 40.749 -6.731  1.00 70.03  ? 45  THR   A N    1 
ATOM   335  C  CA   . THR   A 1 45  ? -26.218 40.470 -6.429  1.00 74.29  ? 45  THR   A CA   1 
ATOM   336  C  C    . THR   A 1 45  ? -26.433 38.958 -6.391  1.00 79.29  ? 45  THR   A C    1 
ATOM   337  O  O    . THR   A 1 45  ? -25.559 38.170 -6.762  1.00 78.67  ? 45  THR   A O    1 
ATOM   338  C  CB   . THR   A 1 45  ? -27.133 41.131 -7.458  1.00 85.58  ? 45  THR   A CB   1 
ATOM   339  O  OG1  . THR   A 1 45  ? -26.993 40.469 -8.722  1.00 80.43  ? 45  THR   A OG1  1 
ATOM   340  C  CG2  . THR   A 1 45  ? -26.764 42.597 -7.619  1.00 78.79  ? 45  THR   A CG2  1 
ATOM   341  N  N    . SER   A 1 46  ? -27.613 38.549 -5.924  1.00 79.75  ? 46  SER   A N    1 
ATOM   342  C  CA   . SER   A 1 46  ? -27.887 37.123 -5.774  1.00 86.13  ? 46  SER   A CA   1 
ATOM   343  C  C    . SER   A 1 46  ? -27.600 36.355 -7.062  1.00 95.97  ? 46  SER   A C    1 
ATOM   344  O  O    . SER   A 1 46  ? -26.994 35.276 -7.029  1.00 91.36  ? 46  SER   A O    1 
ATOM   345  C  CB   . SER   A 1 46  ? -29.334 36.915 -5.324  1.00 83.63  ? 46  SER   A CB   1 
ATOM   346  O  OG   . SER   A 1 46  ? -30.166 36.561 -6.415  1.00 99.06  ? 46  SER   A OG   1 
ATOM   347  N  N    . GLU   A 1 47  ? -28.009 36.903 -8.210  1.00 89.58  ? 47  GLU   A N    1 
ATOM   348  C  CA   . GLU   A 1 47  ? -27.826 36.232 -9.493  1.00 89.90  ? 47  GLU   A CA   1 
ATOM   349  C  C    . GLU   A 1 47  ? -26.394 36.298 -10.014 1.00 95.08  ? 47  GLU   A C    1 
ATOM   350  O  O    . GLU   A 1 47  ? -26.053 35.539 -10.926 1.00 96.45  ? 47  GLU   A O    1 
ATOM   351  C  CB   . GLU   A 1 47  ? -28.774 36.826 -10.539 1.00 102.32 ? 47  GLU   A CB   1 
ATOM   352  C  CG   . GLU   A 1 47  ? -30.250 36.698 -10.194 1.00 99.48  ? 47  GLU   A CG   1 
ATOM   353  C  CD   . GLU   A 1 47  ? -30.705 37.729 -9.181  1.00 107.17 ? 47  GLU   A CD   1 
ATOM   354  O  OE1  . GLU   A 1 47  ? -29.955 38.699 -8.940  1.00 102.43 ? 47  GLU   A OE1  1 
ATOM   355  O  OE2  . GLU   A 1 47  ? -31.811 37.566 -8.624  1.00 112.19 ? 47  GLU   A OE2  1 
ATOM   356  N  N    . ASP   A 1 48  ? -25.555 37.179 -9.468  1.00 90.35  ? 48  ASP   A N    1 
ATOM   357  C  CA   . ASP   A 1 48  ? -24.156 37.264 -9.868  1.00 91.54  ? 48  ASP   A CA   1 
ATOM   358  C  C    . ASP   A 1 48  ? -23.260 36.292 -9.117  1.00 86.80  ? 48  ASP   A C    1 
ATOM   359  O  O    . ASP   A 1 48  ? -22.123 36.059 -9.545  1.00 81.40  ? 48  ASP   A O    1 
ATOM   360  C  CB   . ASP   A 1 48  ? -23.621 38.685 -9.649  1.00 83.59  ? 48  ASP   A CB   1 
ATOM   361  C  CG   . ASP   A 1 48  ? -24.395 39.729 -10.425 1.00 88.96  ? 48  ASP   A CG   1 
ATOM   362  O  OD1  . ASP   A 1 48  ? -24.912 39.400 -11.515 1.00 85.35  ? 48  ASP   A OD1  1 
ATOM   363  O  OD2  . ASP   A 1 48  ? -24.484 40.877 -9.941  1.00 81.91  ? 48  ASP   A OD2  1 
ATOM   364  N  N    . MET   A 1 49  ? -23.746 35.721 -8.012  1.00 87.71  ? 49  MET   A N    1 
ATOM   365  C  CA   . MET   A 1 49  ? -22.890 34.928 -7.136  1.00 87.79  ? 49  MET   A CA   1 
ATOM   366  C  C    . MET   A 1 49  ? -22.496 33.599 -7.768  1.00 84.48  ? 49  MET   A C    1 
ATOM   367  O  O    . MET   A 1 49  ? -21.431 33.057 -7.451  1.00 71.03  ? 49  MET   A O    1 
ATOM   368  C  CB   . MET   A 1 49  ? -23.597 34.692 -5.799  1.00 86.62  ? 49  MET   A CB   1 
ATOM   369  C  CG   . MET   A 1 49  ? -24.071 35.971 -5.106  1.00 82.93  ? 49  MET   A CG   1 
ATOM   370  S  SD   . MET   A 1 49  ? -24.599 35.741 -3.392  1.00 86.09  ? 49  MET   A SD   1 
ATOM   371  C  CE   . MET   A 1 49  ? -24.886 37.434 -2.870  1.00 66.29  ? 49  MET   A CE   1 
ATOM   372  N  N    . LEU   A 1 50  ? -23.330 33.063 -8.663  1.00 88.68  ? 50  LEU   A N    1 
ATOM   373  C  CA   . LEU   A 1 50  ? -23.076 31.726 -9.193  1.00 89.77  ? 50  LEU   A CA   1 
ATOM   374  C  C    . LEU   A 1 50  ? -21.907 31.711 -10.171 1.00 91.47  ? 50  LEU   A C    1 
ATOM   375  O  O    . LEU   A 1 50  ? -21.242 30.678 -10.323 1.00 90.44  ? 50  LEU   A O    1 
ATOM   376  C  CB   . LEU   A 1 50  ? -24.337 31.180 -9.858  1.00 89.37  ? 50  LEU   A CB   1 
ATOM   377  C  CG   . LEU   A 1 50  ? -25.595 31.171 -8.992  1.00 98.51  ? 50  LEU   A CG   1 
ATOM   378  C  CD1  . LEU   A 1 50  ? -26.772 31.801 -9.729  1.00 90.58  ? 50  LEU   A CD1  1 
ATOM   379  C  CD2  . LEU   A 1 50  ? -25.937 29.758 -8.533  1.00 92.89  ? 50  LEU   A CD2  1 
ATOM   380  N  N    . ASN   A 1 51  ? -21.636 32.834 -10.836 1.00 87.54  ? 51  ASN   A N    1 
ATOM   381  C  CA   . ASN   A 1 51  ? -20.564 32.886 -11.820 1.00 81.89  ? 51  ASN   A CA   1 
ATOM   382  C  C    . ASN   A 1 51  ? -20.212 34.338 -12.126 1.00 72.64  ? 51  ASN   A C    1 
ATOM   383  O  O    . ASN   A 1 51  ? -20.517 34.843 -13.213 1.00 77.91  ? 51  ASN   A O    1 
ATOM   384  C  CB   . ASN   A 1 51  ? -20.977 32.147 -13.092 1.00 75.98  ? 51  ASN   A CB   1 
ATOM   385  C  CG   . ASN   A 1 51  ? -19.959 32.277 -14.195 1.00 90.56  ? 51  ASN   A CG   1 
ATOM   386  O  OD1  . ASN   A 1 51  ? -20.307 32.334 -15.374 1.00 93.70  ? 51  ASN   A OD1  1 
ATOM   387  N  ND2  . ASN   A 1 51  ? -18.686 32.320 -13.819 1.00 88.32  ? 51  ASN   A ND2  1 
ATOM   388  N  N    . PRO   A 1 52  ? -19.571 35.037 -11.196 1.00 76.02  ? 52  PRO   A N    1 
ATOM   389  C  CA   . PRO   A 1 52  ? -19.292 36.462 -11.385 1.00 67.44  ? 52  PRO   A CA   1 
ATOM   390  C  C    . PRO   A 1 52  ? -18.025 36.740 -12.176 1.00 63.35  ? 52  PRO   A C    1 
ATOM   391  O  O    . PRO   A 1 52  ? -17.067 35.967 -12.180 1.00 64.71  ? 52  PRO   A O    1 
ATOM   392  C  CB   . PRO   A 1 52  ? -19.135 36.964 -9.944  1.00 57.03  ? 52  PRO   A CB   1 
ATOM   393  C  CG   . PRO   A 1 52  ? -18.552 35.793 -9.226  1.00 66.46  ? 52  PRO   A CG   1 
ATOM   394  C  CD   . PRO   A 1 52  ? -19.159 34.564 -9.863  1.00 71.51  ? 52  PRO   A CD   1 
ATOM   395  N  N    . ASN   A 1 53  ? -18.040 37.881 -12.854 1.00 62.51  ? 53  ASN   A N    1 
ATOM   396  C  CA   . ASN   A 1 53  ? -16.839 38.495 -13.411 1.00 55.62  ? 53  ASN   A CA   1 
ATOM   397  C  C    . ASN   A 1 53  ? -16.634 39.790 -12.630 1.00 56.65  ? 53  ASN   A C    1 
ATOM   398  O  O    . ASN   A 1 53  ? -17.196 40.832 -12.969 1.00 60.27  ? 53  ASN   A O    1 
ATOM   399  C  CB   . ASN   A 1 53  ? -16.973 38.751 -14.905 1.00 64.44  ? 53  ASN   A CB   1 
ATOM   400  C  CG   . ASN   A 1 53  ? -15.633 38.932 -15.579 1.00 68.57  ? 53  ASN   A CG   1 
ATOM   401  O  OD1  . ASN   A 1 53  ? -14.782 39.680 -15.097 1.00 67.71  ? 53  ASN   A OD1  1 
ATOM   402  N  ND2  . ASN   A 1 53  ? -15.436 38.252 -16.700 1.00 71.01  ? 53  ASN   A ND2  1 
ATOM   403  N  N    . TYR   A 1 54  ? -15.818 39.714 -11.576 1.00 58.81  ? 54  TYR   A N    1 
ATOM   404  C  CA   . TYR   A 1 54  ? -15.782 40.788 -10.587 1.00 55.66  ? 54  TYR   A CA   1 
ATOM   405  C  C    . TYR   A 1 54  ? -15.318 42.111 -11.188 1.00 58.27  ? 54  TYR   A C    1 
ATOM   406  O  O    . TYR   A 1 54  ? -15.884 43.166 -10.880 1.00 55.05  ? 54  TYR   A O    1 
ATOM   407  C  CB   . TYR   A 1 54  ? -14.895 40.391 -9.406  1.00 49.78  ? 54  TYR   A CB   1 
ATOM   408  C  CG   . TYR   A 1 54  ? -15.524 39.360 -8.495  1.00 50.41  ? 54  TYR   A CG   1 
ATOM   409  C  CD1  . TYR   A 1 54  ? -16.468 39.727 -7.541  1.00 43.53  ? 54  TYR   A CD1  1 
ATOM   410  C  CD2  . TYR   A 1 54  ? -15.176 38.019 -8.589  1.00 45.29  ? 54  TYR   A CD2  1 
ATOM   411  C  CE1  . TYR   A 1 54  ? -17.044 38.786 -6.708  1.00 49.41  ? 54  TYR   A CE1  1 
ATOM   412  C  CE2  . TYR   A 1 54  ? -15.746 37.072 -7.761  1.00 43.41  ? 54  TYR   A CE2  1 
ATOM   413  C  CZ   . TYR   A 1 54  ? -16.679 37.460 -6.824  1.00 48.04  ? 54  TYR   A CZ   1 
ATOM   414  O  OH   . TYR   A 1 54  ? -17.247 36.518 -6.000  1.00 52.23  ? 54  TYR   A OH   1 
ATOM   415  N  N    . GLU   A 1 55  ? -14.281 42.092 -12.030 1.00 50.45  ? 55  GLU   A N    1 
ATOM   416  C  CA   . GLU   A 1 55  ? -13.824 43.363 -12.577 1.00 53.11  ? 55  GLU   A CA   1 
ATOM   417  C  C    . GLU   A 1 55  ? -14.796 43.902 -13.618 1.00 62.97  ? 55  GLU   A C    1 
ATOM   418  O  O    . GLU   A 1 55  ? -14.688 45.069 -14.005 1.00 62.00  ? 55  GLU   A O    1 
ATOM   419  C  CB   . GLU   A 1 55  ? -12.406 43.223 -13.137 1.00 55.56  ? 55  GLU   A CB   1 
ATOM   420  C  CG   . GLU   A 1 55  ? -12.265 42.285 -14.316 1.00 75.73  ? 55  GLU   A CG   1 
ATOM   421  C  CD   . GLU   A 1 55  ? -11.833 42.989 -15.597 1.00 93.64  ? 55  GLU   A CD   1 
ATOM   422  O  OE1  . GLU   A 1 55  ? -11.661 44.228 -15.583 1.00 100.36 ? 55  GLU   A OE1  1 
ATOM   423  O  OE2  . GLU   A 1 55  ? -11.638 42.285 -16.608 1.00 100.64 ? 55  GLU   A OE2  1 
ATOM   424  N  N    . ASP   A 1 56  ? -15.751 43.081 -14.065 1.00 62.84  ? 56  ASP   A N    1 
ATOM   425  C  CA   . ASP   A 1 56  ? -16.858 43.577 -14.876 1.00 71.37  ? 56  ASP   A CA   1 
ATOM   426  C  C    . ASP   A 1 56  ? -17.968 44.171 -14.018 1.00 67.90  ? 56  ASP   A C    1 
ATOM   427  O  O    . ASP   A 1 56  ? -18.659 45.094 -14.462 1.00 59.03  ? 56  ASP   A O    1 
ATOM   428  C  CB   . ASP   A 1 56  ? -17.425 42.458 -15.756 1.00 63.70  ? 56  ASP   A CB   1 
ATOM   429  C  CG   . ASP   A 1 56  ? -18.218 42.990 -16.937 1.00 77.73  ? 56  ASP   A CG   1 
ATOM   430  O  OD1  . ASP   A 1 56  ? -17.642 43.722 -17.769 1.00 86.92  ? 56  ASP   A OD1  1 
ATOM   431  O  OD2  . ASP   A 1 56  ? -19.426 42.683 -17.032 1.00 83.33  ? 56  ASP   A OD2  1 
ATOM   432  N  N    . LEU   A 1 57  ? -18.161 43.653 -12.803 1.00 54.69  ? 57  LEU   A N    1 
ATOM   433  C  CA   . LEU   A 1 57  ? -19.155 44.202 -11.889 1.00 59.69  ? 57  LEU   A CA   1 
ATOM   434  C  C    . LEU   A 1 57  ? -18.654 45.432 -11.148 1.00 60.43  ? 57  LEU   A C    1 
ATOM   435  O  O    . LEU   A 1 57  ? -19.471 46.256 -10.721 1.00 59.71  ? 57  LEU   A O    1 
ATOM   436  C  CB   . LEU   A 1 57  ? -19.586 43.141 -10.870 1.00 56.65  ? 57  LEU   A CB   1 
ATOM   437  C  CG   . LEU   A 1 57  ? -19.767 41.696 -11.334 1.00 63.46  ? 57  LEU   A CG   1 
ATOM   438  C  CD1  . LEU   A 1 57  ? -20.095 40.820 -10.138 1.00 59.21  ? 57  LEU   A CD1  1 
ATOM   439  C  CD2  . LEU   A 1 57  ? -20.897 41.632 -12.342 1.00 56.79  ? 57  LEU   A CD2  1 
ATOM   440  N  N    . LEU   A 1 58  ? -17.337 45.573 -10.986 1.00 51.29  ? 58  LEU   A N    1 
ATOM   441  C  CA   . LEU   A 1 58  ? -16.796 46.693 -10.225 1.00 55.28  ? 58  LEU   A CA   1 
ATOM   442  C  C    . LEU   A 1 58  ? -16.776 47.972 -11.048 1.00 55.86  ? 58  LEU   A C    1 
ATOM   443  O  O    . LEU   A 1 58  ? -17.037 49.061 -10.521 1.00 61.44  ? 58  LEU   A O    1 
ATOM   444  C  CB   . LEU   A 1 58  ? -15.388 46.365 -9.727  1.00 47.97  ? 58  LEU   A CB   1 
ATOM   445  C  CG   . LEU   A 1 58  ? -14.765 47.414 -8.807  1.00 51.94  ? 58  LEU   A CG   1 
ATOM   446  C  CD1  . LEU   A 1 58  ? -15.653 47.647 -7.596  1.00 55.59  ? 58  LEU   A CD1  1 
ATOM   447  C  CD2  . LEU   A 1 58  ? -13.365 46.996 -8.378  1.00 61.06  ? 58  LEU   A CD2  1 
ATOM   448  N  N    . ILE   A 1 59  ? -16.461 47.863 -12.340 1.00 56.67  ? 59  ILE   A N    1 
ATOM   449  C  CA   . ILE   A 1 59  ? -16.519 49.035 -13.204 1.00 57.14  ? 59  ILE   A CA   1 
ATOM   450  C  C    . ILE   A 1 59  ? -17.935 49.590 -13.248 1.00 59.57  ? 59  ILE   A C    1 
ATOM   451  O  O    . ILE   A 1 59  ? -18.131 50.797 -13.437 1.00 61.73  ? 59  ILE   A O    1 
ATOM   452  C  CB   . ILE   A 1 59  ? -15.991 48.691 -14.611 1.00 60.37  ? 59  ILE   A CB   1 
ATOM   453  C  CG1  . ILE   A 1 59  ? -15.433 49.938 -15.306 1.00 68.52  ? 59  ILE   A CG1  1 
ATOM   454  C  CG2  . ILE   A 1 59  ? -17.082 48.047 -15.462 1.00 67.79  ? 59  ILE   A CG2  1 
ATOM   455  C  CD1  . ILE   A 1 59  ? -13.966 50.197 -15.022 1.00 67.65  ? 59  ILE   A CD1  1 
ATOM   456  N  N    . ARG   A 1 60  ? -18.940 48.735 -13.045 1.00 59.59  ? 60  ARG   A N    1 
ATOM   457  C  CA   . ARG   A 1 60  ? -20.331 49.171 -13.091 1.00 70.07  ? 60  ARG   A CA   1 
ATOM   458  C  C    . ARG   A 1 60  ? -20.799 49.820 -11.795 1.00 61.83  ? 60  ARG   A C    1 
ATOM   459  O  O    . ARG   A 1 60  ? -21.965 50.218 -11.712 1.00 66.55  ? 60  ARG   A O    1 
ATOM   460  C  CB   . ARG   A 1 60  ? -21.256 47.994 -13.431 1.00 65.74  ? 60  ARG   A CB   1 
ATOM   461  C  CG   . ARG   A 1 60  ? -21.004 47.357 -14.792 1.00 64.43  ? 60  ARG   A CG   1 
ATOM   462  C  CD   . ARG   A 1 60  ? -21.789 46.058 -14.936 1.00 64.97  ? 60  ARG   A CD   1 
ATOM   463  N  NE   . ARG   A 1 60  ? -21.382 45.285 -16.104 1.00 65.85  ? 60  ARG   A NE   1 
ATOM   464  C  CZ   . ARG   A 1 60  ? -21.911 45.410 -17.314 1.00 76.55  ? 60  ARG   A CZ   1 
ATOM   465  N  NH1  . ARG   A 1 60  ? -22.856 46.303 -17.568 1.00 72.25  ? 60  ARG   A NH1  1 
ATOM   466  N  NH2  . ARG   A 1 60  ? -21.479 44.623 -18.296 1.00 71.93  ? 60  ARG   A NH2  1 
ATOM   467  N  N    . LYS   A 1 61  ? -19.932 49.940 -10.794 1.00 59.07  ? 61  LYS   A N    1 
ATOM   468  C  CA   . LYS   A 1 61  ? -20.288 50.495 -9.497  1.00 58.61  ? 61  LYS   A CA   1 
ATOM   469  C  C    . LYS   A 1 61  ? -19.595 51.836 -9.282  1.00 63.49  ? 61  LYS   A C    1 
ATOM   470  O  O    . LYS   A 1 61  ? -18.512 52.088 -9.818  1.00 59.78  ? 61  LYS   A O    1 
ATOM   471  C  CB   . LYS   A 1 61  ? -19.908 49.532 -8.363  1.00 61.49  ? 61  LYS   A CB   1 
ATOM   472  C  CG   . LYS   A 1 61  ? -20.727 48.251 -8.332  1.00 61.06  ? 61  LYS   A CG   1 
ATOM   473  C  CD   . LYS   A 1 61  ? -22.089 48.481 -7.696  1.00 69.74  ? 61  LYS   A CD   1 
ATOM   474  C  CE   . LYS   A 1 61  ? -22.854 47.175 -7.531  1.00 65.19  ? 61  LYS   A CE   1 
ATOM   475  N  NZ   . LYS   A 1 61  ? -22.306 46.081 -8.385  1.00 69.48  ? 61  LYS   A NZ   1 
ATOM   476  N  N    . SER   A 1 62  ? -20.223 52.692 -8.480  1.00 60.49  ? 62  SER   A N    1 
ATOM   477  C  CA   . SER   A 1 62  ? -19.638 53.964 -8.077  1.00 61.65  ? 62  SER   A CA   1 
ATOM   478  C  C    . SER   A 1 62  ? -19.484 54.012 -6.559  1.00 64.89  ? 62  SER   A C    1 
ATOM   479  O  O    . SER   A 1 62  ? -20.020 53.172 -5.828  1.00 61.91  ? 62  SER   A O    1 
ATOM   480  C  CB   . SER   A 1 62  ? -20.485 55.148 -8.565  1.00 75.20  ? 62  SER   A CB   1 
ATOM   481  O  OG   . SER   A 1 62  ? -21.850 54.970 -8.233  1.00 80.73  ? 62  SER   A OG   1 
ATOM   482  N  N    . ASN   A 1 63  ? -18.736 55.015 -6.085  1.00 64.35  ? 63  ASN   A N    1 
ATOM   483  C  CA   . ASN   A 1 63  ? -18.481 55.149 -4.652  1.00 64.28  ? 63  ASN   A CA   1 
ATOM   484  C  C    . ASN   A 1 63  ? -19.778 55.146 -3.852  1.00 67.57  ? 63  ASN   A C    1 
ATOM   485  O  O    . ASN   A 1 63  ? -19.907 54.423 -2.858  1.00 67.75  ? 63  ASN   A O    1 
ATOM   486  C  CB   . ASN   A 1 63  ? -17.678 56.422 -4.371  1.00 59.50  ? 63  ASN   A CB   1 
ATOM   487  C  CG   . ASN   A 1 63  ? -16.212 56.281 -4.739  1.00 67.16  ? 63  ASN   A CG   1 
ATOM   488  O  OD1  . ASN   A 1 63  ? -15.695 55.168 -4.851  1.00 64.07  ? 63  ASN   A OD1  1 
ATOM   489  N  ND2  . ASN   A 1 63  ? -15.530 57.410 -4.911  1.00 59.67  ? 63  ASN   A ND2  1 
ATOM   490  N  N    . HIS   A 1 64  ? -20.759 55.942 -4.280  1.00 63.11  ? 64  HIS   A N    1 
ATOM   491  C  CA   . HIS   A 1 64  ? -22.002 56.075 -3.529  1.00 65.08  ? 64  HIS   A CA   1 
ATOM   492  C  C    . HIS   A 1 64  ? -22.856 54.810 -3.541  1.00 64.29  ? 64  HIS   A C    1 
ATOM   493  O  O    . HIS   A 1 64  ? -23.926 54.812 -2.924  1.00 68.30  ? 64  HIS   A O    1 
ATOM   494  C  CB   . HIS   A 1 64  ? -22.804 57.270 -4.056  1.00 69.60  ? 64  HIS   A CB   1 
ATOM   495  C  CG   . HIS   A 1 64  ? -23.416 57.053 -5.406  1.00 81.83  ? 64  HIS   A CG   1 
ATOM   496  N  ND1  . HIS   A 1 64  ? -24.510 56.239 -5.609  1.00 81.13  ? 64  HIS   A ND1  1 
ATOM   497  C  CD2  . HIS   A 1 64  ? -23.099 57.565 -6.620  1.00 79.17  ? 64  HIS   A CD2  1 
ATOM   498  C  CE1  . HIS   A 1 64  ? -24.833 56.249 -6.890  1.00 87.80  ? 64  HIS   A CE1  1 
ATOM   499  N  NE2  . HIS   A 1 64  ? -23.992 57.046 -7.526  1.00 83.26  ? 64  HIS   A NE2  1 
ATOM   500  N  N    . ASN   A 1 65  ? -22.424 53.736 -4.204  1.00 62.08  ? 65  ASN   A N    1 
ATOM   501  C  CA   . ASN   A 1 65  ? -23.119 52.459 -4.094  1.00 61.16  ? 65  ASN   A CA   1 
ATOM   502  C  C    . ASN   A 1 65  ? -22.713 51.669 -2.855  1.00 64.26  ? 65  ASN   A C    1 
ATOM   503  O  O    . ASN   A 1 65  ? -23.332 50.638 -2.569  1.00 61.92  ? 65  ASN   A O    1 
ATOM   504  C  CB   . ASN   A 1 65  ? -22.869 51.602 -5.339  1.00 60.37  ? 65  ASN   A CB   1 
ATOM   505  C  CG   . ASN   A 1 65  ? -23.461 52.206 -6.592  1.00 68.80  ? 65  ASN   A CG   1 
ATOM   506  O  OD1  . ASN   A 1 65  ? -22.830 52.213 -7.648  1.00 69.68  ? 65  ASN   A OD1  1 
ATOM   507  N  ND2  . ASN   A 1 65  ? -24.683 52.714 -6.485  1.00 73.00  ? 65  ASN   A ND2  1 
ATOM   508  N  N    . PHE   A 1 66  ? -21.703 52.122 -2.120  1.00 58.01  ? 66  PHE   A N    1 
ATOM   509  C  CA   . PHE   A 1 66  ? -21.164 51.400 -0.972  1.00 66.67  ? 66  PHE   A CA   1 
ATOM   510  C  C    . PHE   A 1 66  ? -21.536 52.132 0.311   1.00 62.81  ? 66  PHE   A C    1 
ATOM   511  O  O    . PHE   A 1 66  ? -21.101 53.268 0.532   1.00 67.45  ? 66  PHE   A O    1 
ATOM   512  C  CB   . PHE   A 1 66  ? -19.645 51.259 -1.078  1.00 51.46  ? 66  PHE   A CB   1 
ATOM   513  C  CG   . PHE   A 1 66  ? -19.182 50.448 -2.256  1.00 57.84  ? 66  PHE   A CG   1 
ATOM   514  C  CD1  . PHE   A 1 66  ? -19.140 49.064 -2.188  1.00 52.35  ? 66  PHE   A CD1  1 
ATOM   515  C  CD2  . PHE   A 1 66  ? -18.773 51.069 -3.424  1.00 52.87  ? 66  PHE   A CD2  1 
ATOM   516  C  CE1  . PHE   A 1 66  ? -18.705 48.315 -3.267  1.00 53.18  ? 66  PHE   A CE1  1 
ATOM   517  C  CE2  . PHE   A 1 66  ? -18.338 50.327 -4.506  1.00 57.28  ? 66  PHE   A CE2  1 
ATOM   518  C  CZ   . PHE   A 1 66  ? -18.304 48.947 -4.428  1.00 59.49  ? 66  PHE   A CZ   1 
ATOM   519  N  N    . LEU   A 1 67  ? -22.327 51.480 1.155   1.00 57.45  ? 67  LEU   A N    1 
ATOM   520  C  CA   . LEU   A 1 67  ? -22.691 52.013 2.459   1.00 56.47  ? 67  LEU   A CA   1 
ATOM   521  C  C    . LEU   A 1 67  ? -21.807 51.357 3.513   1.00 59.42  ? 67  LEU   A C    1 
ATOM   522  O  O    . LEU   A 1 67  ? -21.808 50.128 3.654   1.00 52.69  ? 67  LEU   A O    1 
ATOM   523  C  CB   . LEU   A 1 67  ? -24.169 51.764 2.750   1.00 63.49  ? 67  LEU   A CB   1 
ATOM   524  C  CG   . LEU   A 1 67  ? -24.633 51.924 4.196   1.00 75.48  ? 67  LEU   A CG   1 
ATOM   525  C  CD1  . LEU   A 1 67  ? -24.615 53.390 4.583   1.00 68.90  ? 67  LEU   A CD1  1 
ATOM   526  C  CD2  . LEU   A 1 67  ? -26.025 51.340 4.374   1.00 73.25  ? 67  LEU   A CD2  1 
ATOM   527  N  N    . VAL   A 1 68  ? -21.036 52.169 4.229   1.00 55.00  ? 68  VAL   A N    1 
ATOM   528  C  CA   . VAL   A 1 68  ? -20.160 51.692 5.292   1.00 52.12  ? 68  VAL   A CA   1 
ATOM   529  C  C    . VAL   A 1 68  ? -20.674 52.266 6.601   1.00 57.52  ? 68  VAL   A C    1 
ATOM   530  O  O    . VAL   A 1 68  ? -20.787 53.490 6.749   1.00 55.30  ? 68  VAL   A O    1 
ATOM   531  C  CB   . VAL   A 1 68  ? -18.697 52.092 5.050   1.00 49.63  ? 68  VAL   A CB   1 
ATOM   532  C  CG1  . VAL   A 1 68  ? -17.819 51.629 6.212   1.00 49.60  ? 68  VAL   A CG1  1 
ATOM   533  C  CG2  . VAL   A 1 68  ? -18.205 51.516 3.737   1.00 47.58  ? 68  VAL   A CG2  1 
ATOM   534  N  N    . GLN   A 1 69  ? -20.998 51.386 7.543   1.00 52.45  ? 69  GLN   A N    1 
ATOM   535  C  CA   . GLN   A 1 69  ? -21.530 51.786 8.839   1.00 54.53  ? 69  GLN   A CA   1 
ATOM   536  C  C    . GLN   A 1 69  ? -20.604 51.291 9.937   1.00 58.72  ? 69  GLN   A C    1 
ATOM   537  O  O    . GLN   A 1 69  ? -20.404 50.080 10.090  1.00 56.02  ? 69  GLN   A O    1 
ATOM   538  C  CB   . GLN   A 1 69  ? -22.947 51.250 9.047   1.00 60.30  ? 69  GLN   A CB   1 
ATOM   539  C  CG   . GLN   A 1 69  ? -23.809 51.308 7.800   1.00 68.52  ? 69  GLN   A CG   1 
ATOM   540  C  CD   . GLN   A 1 69  ? -25.269 51.048 8.099   1.00 79.99  ? 69  GLN   A CD   1 
ATOM   541  O  OE1  . GLN   A 1 69  ? -25.910 50.218 7.455   1.00 84.10  ? 69  GLN   A OE1  1 
ATOM   542  N  NE2  . GLN   A 1 69  ? -25.803 51.756 9.087   1.00 79.95  ? 69  GLN   A NE2  1 
ATOM   543  N  N    . ALA   A 1 70  ? -20.036 52.227 10.688  1.00 63.94  ? 70  ALA   A N    1 
ATOM   544  C  CA   . ALA   A 1 70  ? -19.279 51.928 11.899  1.00 66.71  ? 70  ALA   A CA   1 
ATOM   545  C  C    . ALA   A 1 70  ? -20.210 52.216 13.069  1.00 66.63  ? 70  ALA   A C    1 
ATOM   546  O  O    . ALA   A 1 70  ? -20.398 53.372 13.456  1.00 72.55  ? 70  ALA   A O    1 
ATOM   547  C  CB   . ALA   A 1 70  ? -18.002 52.758 11.967  1.00 59.11  ? 70  ALA   A CB   1 
ATOM   548  N  N    . GLY   A 1 71  ? -20.804 51.165 13.620  1.00 68.59  ? 71  GLY   A N    1 
ATOM   549  C  CA   . GLY   A 1 71  ? -21.844 51.360 14.616  1.00 76.92  ? 71  GLY   A CA   1 
ATOM   550  C  C    . GLY   A 1 71  ? -23.038 52.033 13.968  1.00 83.70  ? 71  GLY   A C    1 
ATOM   551  O  O    . GLY   A 1 71  ? -23.626 51.518 13.010  1.00 84.96  ? 71  GLY   A O    1 
ATOM   552  N  N    . ASN   A 1 72  ? -23.409 53.204 14.482  1.00 85.81  ? 72  ASN   A N    1 
ATOM   553  C  CA   . ASN   A 1 72  ? -24.445 54.017 13.863  1.00 93.41  ? 72  ASN   A CA   1 
ATOM   554  C  C    . ASN   A 1 72  ? -23.878 55.135 13.002  1.00 91.37  ? 72  ASN   A C    1 
ATOM   555  O  O    . ASN   A 1 72  ? -24.643 55.805 12.300  1.00 94.48  ? 72  ASN   A O    1 
ATOM   556  C  CB   . ASN   A 1 72  ? -25.364 54.616 14.935  1.00 100.21 ? 72  ASN   A CB   1 
ATOM   557  C  CG   . ASN   A 1 72  ? -24.635 54.897 16.231  1.00 110.91 ? 72  ASN   A CG   1 
ATOM   558  O  OD1  . ASN   A 1 72  ? -23.787 55.787 16.301  1.00 113.85 ? 72  ASN   A OD1  1 
ATOM   559  N  ND2  . ASN   A 1 72  ? -24.959 54.134 17.268  1.00 115.04 ? 72  ASN   A ND2  1 
ATOM   560  N  N    . VAL   A 1 73  ? -22.567 55.345 13.034  1.00 85.52  ? 73  VAL   A N    1 
ATOM   561  C  CA   . VAL   A 1 73  ? -21.937 56.406 12.258  1.00 78.09  ? 73  VAL   A CA   1 
ATOM   562  C  C    . VAL   A 1 73  ? -21.706 55.908 10.838  1.00 76.57  ? 73  VAL   A C    1 
ATOM   563  O  O    . VAL   A 1 73  ? -20.995 54.921 10.620  1.00 71.70  ? 73  VAL   A O    1 
ATOM   564  C  CB   . VAL   A 1 73  ? -20.621 56.857 12.907  1.00 77.61  ? 73  VAL   A CB   1 
ATOM   565  C  CG1  . VAL   A 1 73  ? -19.725 57.527 11.879  1.00 78.63  ? 73  VAL   A CG1  1 
ATOM   566  C  CG2  . VAL   A 1 73  ? -20.905 57.792 14.074  1.00 85.13  ? 73  VAL   A CG2  1 
ATOM   567  N  N    . GLN   A 1 74  ? -22.315 56.586 9.870   1.00 72.48  ? 74  GLN   A N    1 
ATOM   568  C  CA   . GLN   A 1 74  ? -22.120 56.265 8.465   1.00 66.43  ? 74  GLN   A CA   1 
ATOM   569  C  C    . GLN   A 1 74  ? -20.813 56.874 7.974   1.00 64.71  ? 74  GLN   A C    1 
ATOM   570  O  O    . GLN   A 1 74  ? -20.523 58.043 8.246   1.00 79.92  ? 74  GLN   A O    1 
ATOM   571  C  CB   . GLN   A 1 74  ? -23.293 56.792 7.639   1.00 68.21  ? 74  GLN   A CB   1 
ATOM   572  C  CG   . GLN   A 1 74  ? -23.232 56.451 6.162   1.00 80.53  ? 74  GLN   A CG   1 
ATOM   573  C  CD   . GLN   A 1 74  ? -24.607 56.395 5.527   1.00 95.30  ? 74  GLN   A CD   1 
ATOM   574  O  OE1  . GLN   A 1 74  ? -24.813 56.885 4.415   1.00 89.94  ? 74  GLN   A OE1  1 
ATOM   575  N  NE2  . GLN   A 1 74  ? -25.561 55.799 6.235   1.00 94.95  ? 74  GLN   A NE2  1 
ATOM   576  N  N    . LEU   A 1 75  ? -20.022 56.085 7.255   1.00 62.62  ? 75  LEU   A N    1 
ATOM   577  C  CA   . LEU   A 1 75  ? -18.794 56.570 6.642   1.00 61.27  ? 75  LEU   A CA   1 
ATOM   578  C  C    . LEU   A 1 75  ? -19.005 56.775 5.146   1.00 73.31  ? 75  LEU   A C    1 
ATOM   579  O  O    . LEU   A 1 75  ? -19.674 55.975 4.485   1.00 67.54  ? 75  LEU   A O    1 
ATOM   580  C  CB   . LEU   A 1 75  ? -17.635 55.600 6.884   1.00 57.93  ? 75  LEU   A CB   1 
ATOM   581  C  CG   . LEU   A 1 75  ? -17.363 55.208 8.337   1.00 58.44  ? 75  LEU   A CG   1 
ATOM   582  C  CD1  . LEU   A 1 75  ? -16.590 53.900 8.414   1.00 56.21  ? 75  LEU   A CD1  1 
ATOM   583  C  CD2  . LEU   A 1 75  ? -16.613 56.316 9.054   1.00 58.72  ? 75  LEU   A CD2  1 
ATOM   584  N  N    . ARG   A 1 76  ? -18.432 57.855 4.620   1.00 69.93  ? 76  ARG   A N    1 
ATOM   585  C  CA   . ARG   A 1 76  ? -18.568 58.216 3.215   1.00 67.07  ? 76  ARG   A CA   1 
ATOM   586  C  C    . ARG   A 1 76  ? -17.386 57.668 2.424   1.00 66.35  ? 76  ARG   A C    1 
ATOM   587  O  O    . ARG   A 1 76  ? -16.229 57.904 2.785   1.00 58.46  ? 76  ARG   A O    1 
ATOM   588  C  CB   . ARG   A 1 76  ? -18.658 59.735 3.053   1.00 70.84  ? 76  ARG   A CB   1 
ATOM   589  C  CG   . ARG   A 1 76  ? -19.102 60.188 1.669   1.00 83.06  ? 76  ARG   A CG   1 
ATOM   590  C  CD   . ARG   A 1 76  ? -19.246 61.702 1.605   1.00 86.87  ? 76  ARG   A CD   1 
ATOM   591  N  NE   . ARG   A 1 76  ? -18.005 62.350 1.196   1.00 91.56  ? 76  ARG   A NE   1 
ATOM   592  C  CZ   . ARG   A 1 76  ? -17.225 63.048 2.010   1.00 101.69 ? 76  ARG   A CZ   1 
ATOM   593  N  NH1  . ARG   A 1 76  ? -17.521 63.198 3.293   1.00 85.17  ? 76  ARG   A NH1  1 
ATOM   594  N  NH2  . ARG   A 1 76  ? -16.118 63.607 1.528   1.00 95.77  ? 76  ARG   A NH2  1 
ATOM   595  N  N    . VAL   A 1 77  ? -17.681 56.947 1.346   1.00 63.28  ? 77  VAL   A N    1 
ATOM   596  C  CA   . VAL   A 1 77  ? -16.655 56.336 0.507   1.00 58.34  ? 77  VAL   A CA   1 
ATOM   597  C  C    . VAL   A 1 77  ? -16.188 57.348 -0.531  1.00 59.52  ? 77  VAL   A C    1 
ATOM   598  O  O    . VAL   A 1 77  ? -16.999 57.904 -1.282  1.00 66.50  ? 77  VAL   A O    1 
ATOM   599  C  CB   . VAL   A 1 77  ? -17.187 55.063 -0.169  1.00 58.11  ? 77  VAL   A CB   1 
ATOM   600  C  CG1  . VAL   A 1 77  ? -16.145 54.500 -1.124  1.00 59.68  ? 77  VAL   A CG1  1 
ATOM   601  C  CG2  . VAL   A 1 77  ? -17.574 54.028 0.881   1.00 54.61  ? 77  VAL   A CG2  1 
ATOM   602  N  N    . ILE   A 1 78  ? -14.877 57.584 -0.576  1.00 56.94  ? 78  ILE   A N    1 
ATOM   603  C  CA   . ILE   A 1 78  ? -14.275 58.536 -1.504  1.00 61.61  ? 78  ILE   A CA   1 
ATOM   604  C  C    . ILE   A 1 78  ? -13.430 57.858 -2.567  1.00 61.77  ? 78  ILE   A C    1 
ATOM   605  O  O    . ILE   A 1 78  ? -12.820 58.553 -3.398  1.00 58.87  ? 78  ILE   A O    1 
ATOM   606  C  CB   . ILE   A 1 78  ? -13.442 59.596 -0.758  1.00 66.10  ? 78  ILE   A CB   1 
ATOM   607  C  CG1  . ILE   A 1 78  ? -12.282 58.936 -0.004  1.00 69.47  ? 78  ILE   A CG1  1 
ATOM   608  C  CG2  . ILE   A 1 78  ? -14.323 60.427 0.170   1.00 65.40  ? 78  ILE   A CG2  1 
ATOM   609  C  CD1  . ILE   A 1 78  ? -11.319 59.924 0.619   1.00 68.32  ? 78  ILE   A CD1  1 
ATOM   610  N  N    . GLY   A 1 79  ? -13.373 56.531 -2.575  1.00 61.35  ? 79  GLY   A N    1 
ATOM   611  C  CA   . GLY   A 1 79  ? -12.617 55.823 -3.584  1.00 54.21  ? 79  GLY   A CA   1 
ATOM   612  C  C    . GLY   A 1 79  ? -12.702 54.328 -3.383  1.00 52.43  ? 79  GLY   A C    1 
ATOM   613  O  O    . GLY   A 1 79  ? -12.876 53.859 -2.256  1.00 54.40  ? 79  GLY   A O    1 
ATOM   614  N  N    . HIS   A 1 80  ? -12.591 53.564 -4.463  1.00 52.59  ? 80  HIS   A N    1 
ATOM   615  C  CA   . HIS   A 1 80  ? -12.641 52.114 -4.371  1.00 54.70  ? 80  HIS   A CA   1 
ATOM   616  C  C    . HIS   A 1 80  ? -11.584 51.519 -5.286  1.00 54.23  ? 80  HIS   A C    1 
ATOM   617  O  O    . HIS   A 1 80  ? -11.087 52.169 -6.208  1.00 55.59  ? 80  HIS   A O    1 
ATOM   618  C  CB   . HIS   A 1 80  ? -14.032 51.566 -4.722  1.00 57.78  ? 80  HIS   A CB   1 
ATOM   619  C  CG   . HIS   A 1 80  ? -14.448 51.824 -6.137  1.00 60.25  ? 80  HIS   A CG   1 
ATOM   620  N  ND1  . HIS   A 1 80  ? -13.915 51.139 -7.208  1.00 66.82  ? 80  HIS   A ND1  1 
ATOM   621  C  CD2  . HIS   A 1 80  ? -15.351 52.690 -6.656  1.00 59.26  ? 80  HIS   A CD2  1 
ATOM   622  C  CE1  . HIS   A 1 80  ? -14.469 51.573 -8.326  1.00 72.60  ? 80  HIS   A CE1  1 
ATOM   623  N  NE2  . HIS   A 1 80  ? -15.343 52.515 -8.019  1.00 69.88  ? 80  HIS   A NE2  1 
ATOM   624  N  N    . SER   A 1 81  ? -11.244 50.265 -5.015  1.00 50.96  ? 81  SER   A N    1 
ATOM   625  C  CA   . SER   A 1 81  ? -10.213 49.567 -5.766  1.00 55.43  ? 81  SER   A CA   1 
ATOM   626  C  C    . SER   A 1 81  ? -10.239 48.107 -5.354  1.00 58.26  ? 81  SER   A C    1 
ATOM   627  O  O    . SER   A 1 81  ? -10.652 47.772 -4.241  1.00 52.00  ? 81  SER   A O    1 
ATOM   628  C  CB   . SER   A 1 81  ? -8.826  50.173 -5.517  1.00 58.83  ? 81  SER   A CB   1 
ATOM   629  O  OG   . SER   A 1 81  ? -8.253  49.657 -4.329  1.00 63.44  ? 81  SER   A OG   1 
ATOM   630  N  N    . MET   A 1 82  ? -9.797  47.246 -6.261  1.00 56.25  ? 82  MET   A N    1 
ATOM   631  C  CA   . MET   A 1 82  ? -9.850  45.807 -6.063  1.00 52.97  ? 82  MET   A CA   1 
ATOM   632  C  C    . MET   A 1 82  ? -8.426  45.280 -5.972  1.00 54.31  ? 82  MET   A C    1 
ATOM   633  O  O    . MET   A 1 82  ? -7.575  45.643 -6.791  1.00 59.05  ? 82  MET   A O    1 
ATOM   634  C  CB   . MET   A 1 82  ? -10.599 45.135 -7.212  1.00 58.64  ? 82  MET   A CB   1 
ATOM   635  C  CG   . MET   A 1 82  ? -10.618 43.624 -7.156  1.00 62.94  ? 82  MET   A CG   1 
ATOM   636  S  SD   . MET   A 1 82  ? -12.307 43.031 -7.377  1.00 68.57  ? 82  MET   A SD   1 
ATOM   637  C  CE   . MET   A 1 82  ? -12.595 43.535 -9.068  1.00 60.15  ? 82  MET   A CE   1 
ATOM   638  N  N    . GLN   A 1 83  ? -8.164  44.444 -4.970  1.00 51.80  ? 83  GLN   A N    1 
ATOM   639  C  CA   . GLN   A 1 83  ? -6.867  43.786 -4.804  1.00 53.90  ? 83  GLN   A CA   1 
ATOM   640  C  C    . GLN   A 1 83  ? -7.130  42.290 -4.666  1.00 48.24  ? 83  GLN   A C    1 
ATOM   641  O  O    . GLN   A 1 83  ? -7.415  41.804 -3.569  1.00 39.33  ? 83  GLN   A O    1 
ATOM   642  C  CB   . GLN   A 1 83  ? -6.109  44.324 -3.593  1.00 45.28  ? 83  GLN   A CB   1 
ATOM   643  C  CG   . GLN   A 1 83  ? -5.036  43.369 -3.074  1.00 64.92  ? 83  GLN   A CG   1 
ATOM   644  C  CD   . GLN   A 1 83  ? -3.797  44.085 -2.572  1.00 68.01  ? 83  GLN   A CD   1 
ATOM   645  O  OE1  . GLN   A 1 83  ? -3.889  45.062 -1.829  1.00 64.70  ? 83  GLN   A OE1  1 
ATOM   646  N  NE2  . GLN   A 1 83  ? -2.627  43.604 -2.984  1.00 67.22  ? 83  GLN   A NE2  1 
ATOM   647  N  N    . ASN   A 1 84  ? -7.033  41.562 -5.772  1.00 40.77  ? 84  ASN   A N    1 
ATOM   648  C  CA   . ASN   A 1 84  ? -7.342  40.132 -5.780  1.00 38.37  ? 84  ASN   A CA   1 
ATOM   649  C  C    . ASN   A 1 84  ? -8.772  39.987 -5.252  1.00 47.43  ? 84  ASN   A C    1 
ATOM   650  O  O    . ASN   A 1 84  ? -9.673  40.667 -5.764  1.00 50.87  ? 84  ASN   A O    1 
ATOM   651  C  CB   . ASN   A 1 84  ? -6.262  39.384 -5.014  1.00 36.07  ? 84  ASN   A CB   1 
ATOM   652  C  CG   . ASN   A 1 84  ? -4.866  39.702 -5.524  1.00 40.63  ? 84  ASN   A CG   1 
ATOM   653  O  OD1  . ASN   A 1 84  ? -4.546  39.436 -6.679  1.00 51.88  ? 84  ASN   A OD1  1 
ATOM   654  N  ND2  . ASN   A 1 84  ? -4.028  40.270 -4.661  1.00 39.48  ? 84  ASN   A ND2  1 
ATOM   655  N  N    . CYS   A 1 85  ? -9.024  39.161 -4.239  1.00 37.90  ? 85  CYS   A N    1 
ATOM   656  C  CA   . CYS   A 1 85  ? -10.384 38.905 -3.783  1.00 41.48  ? 85  CYS   A CA   1 
ATOM   657  C  C    . CYS   A 1 85  ? -10.843 39.870 -2.699  1.00 40.69  ? 85  CYS   A C    1 
ATOM   658  O  O    . CYS   A 1 85  ? -11.917 39.674 -2.121  1.00 43.73  ? 85  CYS   A O    1 
ATOM   659  C  CB   . CYS   A 1 85  ? -10.499 37.465 -3.287  1.00 34.97  ? 85  CYS   A CB   1 
ATOM   660  S  SG   . CYS   A 1 85  ? -10.074 36.264 -4.559  1.00 43.76  ? 85  CYS   A SG   1 
ATOM   661  N  N    . VAL   A 1 86  ? -10.068 40.906 -2.415  1.00 36.90  ? 86  VAL   A N    1 
ATOM   662  C  CA   . VAL   A 1 86  ? -10.389 41.860 -1.366  1.00 39.28  ? 86  VAL   A CA   1 
ATOM   663  C  C    . VAL   A 1 86  ? -10.720 43.194 -2.012  1.00 45.95  ? 86  VAL   A C    1 
ATOM   664  O  O    . VAL   A 1 86  ? -10.021 43.653 -2.924  1.00 44.60  ? 86  VAL   A O    1 
ATOM   665  C  CB   . VAL   A 1 86  ? -9.233  41.998 -0.357  1.00 40.98  ? 86  VAL   A CB   1 
ATOM   666  C  CG1  . VAL   A 1 86  ? -9.443  43.210 0.535   1.00 43.50  ? 86  VAL   A CG1  1 
ATOM   667  C  CG2  . VAL   A 1 86  ? -9.126  40.738 0.478   1.00 42.54  ? 86  VAL   A CG2  1 
ATOM   668  N  N    . LEU   A 1 87  ? -11.803 43.803 -1.550  1.00 40.17  ? 87  LEU   A N    1 
ATOM   669  C  CA   . LEU   A 1 87  ? -12.197 45.133 -1.981  1.00 42.14  ? 87  LEU   A CA   1 
ATOM   670  C  C    . LEU   A 1 87  ? -11.674 46.142 -0.971  1.00 46.07  ? 87  LEU   A C    1 
ATOM   671  O  O    . LEU   A 1 87  ? -11.803 45.935 0.242   1.00 45.89  ? 87  LEU   A O    1 
ATOM   672  C  CB   . LEU   A 1 87  ? -13.716 45.233 -2.101  1.00 44.37  ? 87  LEU   A CB   1 
ATOM   673  C  CG   . LEU   A 1 87  ? -14.294 46.636 -2.242  1.00 55.49  ? 87  LEU   A CG   1 
ATOM   674  C  CD1  . LEU   A 1 87  ? -13.958 47.225 -3.610  1.00 55.44  ? 87  LEU   A CD1  1 
ATOM   675  C  CD2  . LEU   A 1 87  ? -15.795 46.593 -2.009  1.00 56.28  ? 87  LEU   A CD2  1 
ATOM   676  N  N    . LYS   A 1 88  ? -11.078 47.219 -1.471  1.00 42.54  ? 88  LYS   A N    1 
ATOM   677  C  CA   . LYS   A 1 88  ? -10.523 48.282 -0.644  1.00 48.64  ? 88  LYS   A CA   1 
ATOM   678  C  C    . LYS   A 1 88  ? -11.352 49.542 -0.852  1.00 50.41  ? 88  LYS   A C    1 
ATOM   679  O  O    . LYS   A 1 88  ? -11.376 50.097 -1.955  1.00 52.94  ? 88  LYS   A O    1 
ATOM   680  C  CB   . LYS   A 1 88  ? -9.058  48.538 -0.996  1.00 50.16  ? 88  LYS   A CB   1 
ATOM   681  C  CG   . LYS   A 1 88  ? -8.120  47.435 -0.550  1.00 52.32  ? 88  LYS   A CG   1 
ATOM   682  C  CD   . LYS   A 1 88  ? -6.682  47.918 -0.517  1.00 55.77  ? 88  LYS   A CD   1 
ATOM   683  C  CE   . LYS   A 1 88  ? -6.075  47.914 -1.904  1.00 63.78  ? 88  LYS   A CE   1 
ATOM   684  N  NZ   . LYS   A 1 88  ? -4.729  48.543 -1.904  1.00 78.53  ? 88  LYS   A NZ   1 
ATOM   685  N  N    . LEU   A 1 89  ? -12.024 49.989 0.202   1.00 48.37  ? 89  LEU   A N    1 
ATOM   686  C  CA   . LEU   A 1 89  ? -12.893 51.159 0.151   1.00 49.79  ? 89  LEU   A CA   1 
ATOM   687  C  C    . LEU   A 1 89  ? -12.219 52.294 0.912   1.00 54.23  ? 89  LEU   A C    1 
ATOM   688  O  O    . LEU   A 1 89  ? -12.051 52.214 2.132   1.00 57.08  ? 89  LEU   A O    1 
ATOM   689  C  CB   . LEU   A 1 89  ? -14.261 50.842 0.747   1.00 45.06  ? 89  LEU   A CB   1 
ATOM   690  C  CG   . LEU   A 1 89  ? -15.044 49.732 0.054   1.00 49.73  ? 89  LEU   A CG   1 
ATOM   691  C  CD1  . LEU   A 1 89  ? -16.301 49.419 0.840   1.00 52.33  ? 89  LEU   A CD1  1 
ATOM   692  C  CD2  . LEU   A 1 89  ? -15.387 50.141 -1.362  1.00 47.08  ? 89  LEU   A CD2  1 
ATOM   693  N  N    . LYS   A 1 90  ? -11.841 53.348 0.194   1.00 49.32  ? 90  LYS   A N    1 
ATOM   694  C  CA   . LYS   A 1 90  ? -11.225 54.513 0.816   1.00 52.73  ? 90  LYS   A CA   1 
ATOM   695  C  C    . LYS   A 1 90  ? -12.313 55.409 1.397   1.00 55.13  ? 90  LYS   A C    1 
ATOM   696  O  O    . LYS   A 1 90  ? -13.206 55.856 0.671   1.00 57.25  ? 90  LYS   A O    1 
ATOM   697  C  CB   . LYS   A 1 90  ? -10.382 55.274 -0.202  1.00 59.12  ? 90  LYS   A CB   1 
ATOM   698  C  CG   . LYS   A 1 90  ? -9.637  56.467 0.374   1.00 70.79  ? 90  LYS   A CG   1 
ATOM   699  C  CD   . LYS   A 1 90  ? -8.197  56.496 -0.112  1.00 77.96  ? 90  LYS   A CD   1 
ATOM   700  C  CE   . LYS   A 1 90  ? -7.645  57.912 -0.102  1.00 78.12  ? 90  LYS   A CE   1 
ATOM   701  N  NZ   . LYS   A 1 90  ? -6.500  58.069 -1.041  1.00 83.68  ? 90  LYS   A NZ   1 
ATOM   702  N  N    . VAL   A 1 91  ? -12.242 55.670 2.699   1.00 55.37  ? 91  VAL   A N    1 
ATOM   703  C  CA   . VAL   A 1 91  ? -13.224 56.498 3.384   1.00 59.49  ? 91  VAL   A CA   1 
ATOM   704  C  C    . VAL   A 1 91  ? -12.580 57.830 3.763   1.00 64.82  ? 91  VAL   A C    1 
ATOM   705  O  O    . VAL   A 1 91  ? -11.369 58.017 3.655   1.00 70.41  ? 91  VAL   A O    1 
ATOM   706  C  CB   . VAL   A 1 91  ? -13.817 55.793 4.620   1.00 60.84  ? 91  VAL   A CB   1 
ATOM   707  C  CG1  . VAL   A 1 91  ? -14.798 54.712 4.188   1.00 56.64  ? 91  VAL   A CG1  1 
ATOM   708  C  CG2  . VAL   A 1 91  ? -12.710 55.215 5.496   1.00 55.64  ? 91  VAL   A CG2  1 
ATOM   709  N  N    . ASP   A 1 92  ? -13.416 58.764 4.217   1.00 72.43  ? 92  ASP   A N    1 
ATOM   710  C  CA   . ASP   A 1 92  ? -12.969 60.113 4.542   1.00 79.00  ? 92  ASP   A CA   1 
ATOM   711  C  C    . ASP   A 1 92  ? -12.396 60.245 5.947   1.00 80.66  ? 92  ASP   A C    1 
ATOM   712  O  O    . ASP   A 1 92  ? -11.640 61.189 6.205   1.00 80.74  ? 92  ASP   A O    1 
ATOM   713  C  CB   . ASP   A 1 92  ? -14.127 61.107 4.364   1.00 85.85  ? 92  ASP   A CB   1 
ATOM   714  C  CG   . ASP   A 1 92  ? -15.270 60.869 5.343   1.00 97.61  ? 92  ASP   A CG   1 
ATOM   715  O  OD1  . ASP   A 1 92  ? -15.013 60.713 6.557   1.00 99.88  ? 92  ASP   A OD1  1 
ATOM   716  O  OD2  . ASP   A 1 92  ? -16.436 60.838 4.894   1.00 97.70  ? 92  ASP   A OD2  1 
ATOM   717  N  N    . THR   A 1 93  ? -12.733 59.334 6.854   1.00 75.10  ? 93  THR   A N    1 
ATOM   718  C  CA   . THR   A 1 93  ? -12.290 59.396 8.240   1.00 71.24  ? 93  THR   A CA   1 
ATOM   719  C  C    . THR   A 1 93  ? -11.282 58.291 8.509   1.00 66.45  ? 93  THR   A C    1 
ATOM   720  O  O    . THR   A 1 93  ? -11.526 57.128 8.172   1.00 59.02  ? 93  THR   A O    1 
ATOM   721  C  CB   . THR   A 1 93  ? -13.472 59.261 9.206   1.00 71.25  ? 93  THR   A CB   1 
ATOM   722  O  OG1  . THR   A 1 93  ? -14.594 59.999 8.705   1.00 78.96  ? 93  THR   A OG1  1 
ATOM   723  C  CG2  . THR   A 1 93  ? -13.096 59.767 10.595  1.00 76.58  ? 93  THR   A CG2  1 
ATOM   724  N  N    . ALA   A 1 94  ? -10.154 58.654 9.113   1.00 68.10  ? 94  ALA   A N    1 
ATOM   725  C  CA   . ALA   A 1 94  ? -9.212  57.661 9.606   1.00 55.03  ? 94  ALA   A CA   1 
ATOM   726  C  C    . ALA   A 1 94  ? -9.705  57.132 10.944  1.00 59.84  ? 94  ALA   A C    1 
ATOM   727  O  O    . ALA   A 1 94  ? -10.042 57.909 11.842  1.00 59.77  ? 94  ALA   A O    1 
ATOM   728  C  CB   . ALA   A 1 94  ? -7.814  58.258 9.752   1.00 58.44  ? 94  ALA   A CB   1 
ATOM   729  N  N    . ASN   A 1 95  ? -9.758  55.814 11.070  1.00 56.82  ? 95  ASN   A N    1 
ATOM   730  C  CA   . ASN   A 1 95  ? -10.225 55.189 12.295  1.00 51.43  ? 95  ASN   A CA   1 
ATOM   731  C  C    . ASN   A 1 95  ? -9.370  55.643 13.476  1.00 61.10  ? 95  ASN   A C    1 
ATOM   732  O  O    . ASN   A 1 95  ? -8.157  55.384 13.489  1.00 59.22  ? 95  ASN   A O    1 
ATOM   733  C  CB   . ASN   A 1 95  ? -10.184 53.670 12.149  1.00 52.11  ? 95  ASN   A CB   1 
ATOM   734  C  CG   . ASN   A 1 95  ? -10.719 52.944 13.372  1.00 53.48  ? 95  ASN   A CG   1 
ATOM   735  O  OD1  . ASN   A 1 95  ? -11.129 53.561 14.355  1.00 51.03  ? 95  ASN   A OD1  1 
ATOM   736  N  ND2  . ASN   A 1 95  ? -10.715 51.618 13.311  1.00 51.55  ? 95  ASN   A ND2  1 
ATOM   737  N  N    . PRO   A 1 96  ? -9.952  56.315 14.475  1.00 59.38  ? 96  PRO   A N    1 
ATOM   738  C  CA   . PRO   A 1 96  ? -9.154  56.753 15.634  1.00 61.10  ? 96  PRO   A CA   1 
ATOM   739  C  C    . PRO   A 1 96  ? -8.633  55.609 16.489  1.00 57.15  ? 96  PRO   A C    1 
ATOM   740  O  O    . PRO   A 1 96  ? -7.627  55.788 17.186  1.00 57.95  ? 96  PRO   A O    1 
ATOM   741  C  CB   . PRO   A 1 96  ? -10.132 57.636 16.430  1.00 57.95  ? 96  PRO   A CB   1 
ATOM   742  C  CG   . PRO   A 1 96  ? -11.332 57.834 15.536  1.00 60.97  ? 96  PRO   A CG   1 
ATOM   743  C  CD   . PRO   A 1 96  ? -11.372 56.671 14.605  1.00 54.36  ? 96  PRO   A CD   1 
ATOM   744  N  N    . LYS   A 1 97  ? -9.286  54.448 16.471  1.00 58.64  ? 97  LYS   A N    1 
ATOM   745  C  CA   . LYS   A 1 97  ? -8.850  53.294 17.245  1.00 63.16  ? 97  LYS   A CA   1 
ATOM   746  C  C    . LYS   A 1 97  ? -7.971  52.345 16.440  1.00 55.52  ? 97  LYS   A C    1 
ATOM   747  O  O    . LYS   A 1 97  ? -7.851  51.168 16.799  1.00 57.34  ? 97  LYS   A O    1 
ATOM   748  C  CB   . LYS   A 1 97  ? -10.064 52.549 17.802  1.00 57.14  ? 97  LYS   A CB   1 
ATOM   749  C  CG   . LYS   A 1 97  ? -11.120 53.468 18.386  1.00 59.02  ? 97  LYS   A CG   1 
ATOM   750  C  CD   . LYS   A 1 97  ? -12.178 52.691 19.147  1.00 66.68  ? 97  LYS   A CD   1 
ATOM   751  C  CE   . LYS   A 1 97  ? -13.412 52.460 18.292  1.00 79.97  ? 97  LYS   A CE   1 
ATOM   752  N  NZ   . LYS   A 1 97  ? -14.646 52.458 19.124  1.00 91.32  ? 97  LYS   A NZ   1 
ATOM   753  N  N    . THR   A 1 98  ? -7.358  52.831 15.370  1.00 56.07  ? 98  THR   A N    1 
ATOM   754  C  CA   . THR   A 1 98  ? -6.491  51.999 14.545  1.00 54.14  ? 98  THR   A CA   1 
ATOM   755  C  C    . THR   A 1 98  ? -5.249  51.592 15.325  1.00 53.73  ? 98  THR   A C    1 
ATOM   756  O  O    . THR   A 1 98  ? -4.460  52.464 15.715  1.00 55.79  ? 98  THR   A O    1 
ATOM   757  C  CB   . THR   A 1 98  ? -6.080  52.742 13.279  1.00 58.79  ? 98  THR   A CB   1 
ATOM   758  O  OG1  . THR   A 1 98  ? -7.241  53.043 12.498  1.00 60.99  ? 98  THR   A OG1  1 
ATOM   759  C  CG2  . THR   A 1 98  ? -5.122  51.890 12.459  1.00 50.24  ? 98  THR   A CG2  1 
ATOM   760  N  N    . PRO   A 1 99  ? -5.023  50.308 15.563  1.00 52.66  ? 99  PRO   A N    1 
ATOM   761  C  CA   . PRO   A 1 99  ? -3.806  49.874 16.246  1.00 45.23  ? 99  PRO   A CA   1 
ATOM   762  C  C    . PRO   A 1 99  ? -2.660  49.712 15.254  1.00 49.99  ? 99  PRO   A C    1 
ATOM   763  O  O    . PRO   A 1 99  ? -2.847  49.726 14.036  1.00 50.28  ? 99  PRO   A O    1 
ATOM   764  C  CB   . PRO   A 1 99  ? -4.219  48.520 16.828  1.00 46.31  ? 99  PRO   A CB   1 
ATOM   765  C  CG   . PRO   A 1 99  ? -5.148  47.970 15.781  1.00 52.93  ? 99  PRO   A CG   1 
ATOM   766  C  CD   . PRO   A 1 99  ? -5.873  49.164 15.181  1.00 52.43  ? 99  PRO   A CD   1 
ATOM   767  N  N    . LYS   A 1 100 ? -1.458  49.559 15.803  1.00 46.02  ? 100 LYS   A N    1 
ATOM   768  C  CA   . LYS   A 1 100 ? -0.348  49.094 14.985  1.00 52.04  ? 100 LYS   A CA   1 
ATOM   769  C  C    . LYS   A 1 100 ? -0.711  47.739 14.393  1.00 49.65  ? 100 LYS   A C    1 
ATOM   770  O  O    . LYS   A 1 100 ? -1.231  46.865 15.093  1.00 49.59  ? 100 LYS   A O    1 
ATOM   771  C  CB   . LYS   A 1 100 ? 0.932   48.993 15.817  1.00 58.04  ? 100 LYS   A CB   1 
ATOM   772  C  CG   . LYS   A 1 100 ? 1.668   50.317 16.011  1.00 64.83  ? 100 LYS   A CG   1 
ATOM   773  C  CD   . LYS   A 1 100 ? 0.741   51.418 16.513  1.00 70.01  ? 100 LYS   A CD   1 
ATOM   774  C  CE   . LYS   A 1 100 ? 1.362   52.800 16.331  1.00 74.37  ? 100 LYS   A CE   1 
ATOM   775  N  NZ   . LYS   A 1 100 ? 0.355   53.888 16.491  1.00 79.54  ? 100 LYS   A NZ   1 
ATOM   776  N  N    . TYR   A 1 101 ? -0.464  47.566 13.097  1.00 39.16  ? 101 TYR   A N    1 
ATOM   777  C  CA   . TYR   A 1 101 ? -0.865  46.331 12.445  1.00 43.34  ? 101 TYR   A CA   1 
ATOM   778  C  C    . TYR   A 1 101 ? 0.100   45.992 11.320  1.00 44.72  ? 101 TYR   A C    1 
ATOM   779  O  O    . TYR   A 1 101 ? 0.814   46.852 10.799  1.00 39.46  ? 101 TYR   A O    1 
ATOM   780  C  CB   . TYR   A 1 101 ? -2.295  46.425 11.897  1.00 43.58  ? 101 TYR   A CB   1 
ATOM   781  C  CG   . TYR   A 1 101 ? -2.438  47.407 10.756  1.00 43.99  ? 101 TYR   A CG   1 
ATOM   782  C  CD1  . TYR   A 1 101 ? -2.603  48.764 11.000  1.00 47.38  ? 101 TYR   A CD1  1 
ATOM   783  C  CD2  . TYR   A 1 101 ? -2.394  46.980 9.434   1.00 47.86  ? 101 TYR   A CD2  1 
ATOM   784  C  CE1  . TYR   A 1 101 ? -2.729  49.669 9.962   1.00 52.62  ? 101 TYR   A CE1  1 
ATOM   785  C  CE2  . TYR   A 1 101 ? -2.519  47.880 8.385   1.00 45.63  ? 101 TYR   A CE2  1 
ATOM   786  C  CZ   . TYR   A 1 101 ? -2.687  49.221 8.658   1.00 51.55  ? 101 TYR   A CZ   1 
ATOM   787  O  OH   . TYR   A 1 101 ? -2.810  50.120 7.626   1.00 69.81  ? 101 TYR   A OH   1 
ATOM   788  N  N    . LYS   A 1 102 ? 0.117   44.708 10.970  1.00 38.38  ? 102 LYS   A N    1 
ATOM   789  C  CA   . LYS   A 1 102 ? 0.739   44.213 9.755   1.00 39.95  ? 102 LYS   A CA   1 
ATOM   790  C  C    . LYS   A 1 102 ? -0.238  43.267 9.077   1.00 38.44  ? 102 LYS   A C    1 
ATOM   791  O  O    . LYS   A 1 102 ? -1.187  42.777 9.696   1.00 35.37  ? 102 LYS   A O    1 
ATOM   792  C  CB   . LYS   A 1 102 ? 2.055   43.470 10.018  1.00 42.03  ? 102 LYS   A CB   1 
ATOM   793  C  CG   . LYS   A 1 102 ? 2.892   44.029 11.136  1.00 47.86  ? 102 LYS   A CG   1 
ATOM   794  C  CD   . LYS   A 1 102 ? 3.852   42.977 11.662  1.00 52.53  ? 102 LYS   A CD   1 
ATOM   795  C  CE   . LYS   A 1 102 ? 5.247   43.178 11.098  1.00 69.59  ? 102 LYS   A CE   1 
ATOM   796  N  NZ   . LYS   A 1 102 ? 6.292   42.873 12.116  1.00 68.98  ? 102 LYS   A NZ   1 
ATOM   797  N  N    . PHE   A 1 103 ? 0.010   43.019 7.795   1.00 35.89  ? 103 PHE   A N    1 
ATOM   798  C  CA   . PHE   A 1 103 ? -0.687  41.999 7.025   1.00 33.24  ? 103 PHE   A CA   1 
ATOM   799  C  C    . PHE   A 1 103 ? 0.282   40.852 6.790   1.00 36.42  ? 103 PHE   A C    1 
ATOM   800  O  O    . PHE   A 1 103 ? 1.303   41.028 6.116   1.00 35.40  ? 103 PHE   A O    1 
ATOM   801  C  CB   . PHE   A 1 103 ? -1.185  42.558 5.695   1.00 43.23  ? 103 PHE   A CB   1 
ATOM   802  C  CG   . PHE   A 1 103 ? -2.394  43.436 5.817   1.00 46.02  ? 103 PHE   A CG   1 
ATOM   803  C  CD1  . PHE   A 1 103 ? -3.071  43.551 7.019   1.00 43.50  ? 103 PHE   A CD1  1 
ATOM   804  C  CD2  . PHE   A 1 103 ? -2.843  44.162 4.726   1.00 51.49  ? 103 PHE   A CD2  1 
ATOM   805  C  CE1  . PHE   A 1 103 ? -4.185  44.365 7.127   1.00 45.78  ? 103 PHE   A CE1  1 
ATOM   806  C  CE2  . PHE   A 1 103 ? -3.952  44.979 4.827   1.00 49.57  ? 103 PHE   A CE2  1 
ATOM   807  C  CZ   . PHE   A 1 103 ? -4.625  45.082 6.027   1.00 47.13  ? 103 PHE   A CZ   1 
ATOM   808  N  N    . VAL   A 1 104 ? -0.030  39.689 7.349   1.00 32.58  ? 104 VAL   A N    1 
ATOM   809  C  CA   . VAL   A 1 104 ? 0.847   38.531 7.269   1.00 34.70  ? 104 VAL   A CA   1 
ATOM   810  C  C    . VAL   A 1 104 ? 0.050   37.337 6.769   1.00 37.94  ? 104 VAL   A C    1 
ATOM   811  O  O    . VAL   A 1 104 ? -1.151  37.215 7.025   1.00 45.05  ? 104 VAL   A O    1 
ATOM   812  C  CB   . VAL   A 1 104 ? 1.491   38.217 8.638   1.00 42.52  ? 104 VAL   A CB   1 
ATOM   813  C  CG1  . VAL   A 1 104 ? 2.452   37.044 8.522   1.00 43.39  ? 104 VAL   A CG1  1 
ATOM   814  C  CG2  . VAL   A 1 104 ? 2.199   39.451 9.184   1.00 42.39  ? 104 VAL   A CG2  1 
ATOM   815  N  N    . ARG   A 1 105 ? 0.729   36.452 6.050   1.00 32.77  ? 105 ARG   A N    1 
ATOM   816  C  CA   . ARG   A 1 105 ? 0.155   35.188 5.615   1.00 32.07  ? 105 ARG   A CA   1 
ATOM   817  C  C    . ARG   A 1 105 ? 0.748   34.061 6.451   1.00 36.95  ? 105 ARG   A C    1 
ATOM   818  O  O    . ARG   A 1 105 ? 1.971   33.965 6.589   1.00 34.98  ? 105 ARG   A O    1 
ATOM   819  C  CB   . ARG   A 1 105 ? 0.423   34.952 4.130   1.00 39.19  ? 105 ARG   A CB   1 
ATOM   820  C  CG   . ARG   A 1 105 ? -0.355  33.799 3.542   1.00 32.61  ? 105 ARG   A CG   1 
ATOM   821  C  CD   . ARG   A 1 105 ? -0.040  33.643 2.068   1.00 35.38  ? 105 ARG   A CD   1 
ATOM   822  N  NE   . ARG   A 1 105 ? -0.625  32.421 1.531   1.00 34.05  ? 105 ARG   A NE   1 
ATOM   823  C  CZ   . ARG   A 1 105 ? -1.824  32.355 0.969   1.00 38.28  ? 105 ARG   A CZ   1 
ATOM   824  N  NH1  . ARG   A 1 105 ? -2.593  33.426 0.847   1.00 32.95  ? 105 ARG   A NH1  1 
ATOM   825  N  NH2  . ARG   A 1 105 ? -2.264  31.185 0.519   1.00 33.98  ? 105 ARG   A NH2  1 
ATOM   826  N  N    . ILE   A 1 106 ? -0.116  33.218 7.012   1.00 31.26  ? 106 ILE   A N    1 
ATOM   827  C  CA   . ILE   A 1 106 ? 0.330   32.137 7.878   1.00 34.85  ? 106 ILE   A CA   1 
ATOM   828  C  C    . ILE   A 1 106 ? 0.478   30.861 7.062   1.00 44.64  ? 106 ILE   A C    1 
ATOM   829  O  O    . ILE   A 1 106 ? -0.108  30.699 5.988   1.00 39.97  ? 106 ILE   A O    1 
ATOM   830  C  CB   . ILE   A 1 106 ? -0.620  31.912 9.075   1.00 38.58  ? 106 ILE   A CB   1 
ATOM   831  C  CG1  . ILE   A 1 106 ? -2.070  31.831 8.603   1.00 36.65  ? 106 ILE   A CG1  1 
ATOM   832  C  CG2  . ILE   A 1 106 ? -0.433  33.004 10.130  1.00 40.23  ? 106 ILE   A CG2  1 
ATOM   833  C  CD1  . ILE   A 1 106 ? -2.873  30.760 9.303   1.00 46.42  ? 106 ILE   A CD1  1 
ATOM   834  N  N    . GLN   A 1 107 ? 1.271   29.945 7.587   1.00 34.22  ? 107 GLN   A N    1 
ATOM   835  C  CA   . GLN   A 1 107 ? 1.563   28.658 6.987   1.00 38.53  ? 107 GLN   A CA   1 
ATOM   836  C  C    . GLN   A 1 107 ? 0.618   27.591 7.520   1.00 41.69  ? 107 GLN   A C    1 
ATOM   837  O  O    . GLN   A 1 107 ? -0.008  27.765 8.569   1.00 36.51  ? 107 GLN   A O    1 
ATOM   838  C  CB   . GLN   A 1 107 ? 3.012   28.267 7.275   1.00 47.38  ? 107 GLN   A CB   1 
ATOM   839  C  CG   . GLN   A 1 107 ? 4.032   29.148 6.576   1.00 47.50  ? 107 GLN   A CG   1 
ATOM   840  C  CD   . GLN   A 1 107 ? 4.489   28.568 5.256   1.00 52.16  ? 107 GLN   A CD   1 
ATOM   841  O  OE1  . GLN   A 1 107 ? 4.393   27.362 5.032   1.00 56.72  ? 107 GLN   A OE1  1 
ATOM   842  N  NE2  . GLN   A 1 107 ? 4.963   29.428 4.362   1.00 50.00  ? 107 GLN   A NE2  1 
ATOM   843  N  N    . PRO   A 1 108 ? 0.481   26.473 6.809   1.00 41.91  ? 108 PRO   A N    1 
ATOM   844  C  CA   . PRO   A 1 108 ? -0.271  25.346 7.367   1.00 50.44  ? 108 PRO   A CA   1 
ATOM   845  C  C    . PRO   A 1 108 ? 0.336   24.913 8.692   1.00 46.51  ? 108 PRO   A C    1 
ATOM   846  O  O    . PRO   A 1 108 ? 1.558   24.846 8.843   1.00 44.82  ? 108 PRO   A O    1 
ATOM   847  C  CB   . PRO   A 1 108 ? -0.135  24.255 6.298   1.00 40.40  ? 108 PRO   A CB   1 
ATOM   848  C  CG   . PRO   A 1 108 ? 0.236   24.964 5.057   1.00 47.41  ? 108 PRO   A CG   1 
ATOM   849  C  CD   . PRO   A 1 108 ? 1.011   26.182 5.468   1.00 41.90  ? 108 PRO   A CD   1 
ATOM   850  N  N    . GLY   A 1 109 ? -0.531  24.631 9.662   1.00 45.52  ? 109 GLY   A N    1 
ATOM   851  C  CA   . GLY   A 1 109 ? -0.103  24.248 10.987  1.00 37.76  ? 109 GLY   A CA   1 
ATOM   852  C  C    . GLY   A 1 109 ? -0.039  25.380 11.990  1.00 45.45  ? 109 GLY   A C    1 
ATOM   853  O  O    . GLY   A 1 109 ? -0.082  25.119 13.198  1.00 41.79  ? 109 GLY   A O    1 
ATOM   854  N  N    . GLN   A 1 110 ? 0.072   26.627 11.534  1.00 42.13  ? 110 GLN   A N    1 
ATOM   855  C  CA   . GLN   A 1 110 ? 0.072   27.749 12.458  1.00 33.55  ? 110 GLN   A CA   1 
ATOM   856  C  C    . GLN   A 1 110 ? -1.340  28.027 12.965  1.00 43.35  ? 110 GLN   A C    1 
ATOM   857  O  O    . GLN   A 1 110 ? -2.341  27.614 12.369  1.00 38.74  ? 110 GLN   A O    1 
ATOM   858  C  CB   . GLN   A 1 110 ? 0.645   29.008 11.805  1.00 33.18  ? 110 GLN   A CB   1 
ATOM   859  C  CG   . GLN   A 1 110 ? 2.157   29.006 11.664  1.00 49.49  ? 110 GLN   A CG   1 
ATOM   860  C  CD   . GLN   A 1 110 ? 2.682   30.220 10.908  1.00 59.10  ? 110 GLN   A CD   1 
ATOM   861  O  OE1  . GLN   A 1 110 ? 2.985   30.150 9.719   1.00 56.04  ? 110 GLN   A OE1  1 
ATOM   862  N  NE2  . GLN   A 1 110 ? 2.786   31.348 11.608  1.00 63.11  ? 110 GLN   A NE2  1 
ATOM   863  N  N    . THR   A 1 111 ? -1.411  28.738 14.086  1.00 37.80  ? 111 THR   A N    1 
ATOM   864  C  CA   . THR   A 1 111 ? -2.674  29.078 14.718  1.00 37.46  ? 111 THR   A CA   1 
ATOM   865  C  C    . THR   A 1 111 ? -2.898  30.580 14.682  1.00 34.64  ? 111 THR   A C    1 
ATOM   866  O  O    . THR   A 1 111 ? -1.975  31.370 14.473  1.00 40.85  ? 111 THR   A O    1 
ATOM   867  C  CB   . THR   A 1 111 ? -2.723  28.603 16.174  1.00 40.96  ? 111 THR   A CB   1 
ATOM   868  O  OG1  . THR   A 1 111 ? -1.584  29.113 16.880  1.00 37.81  ? 111 THR   A OG1  1 
ATOM   869  C  CG2  . THR   A 1 111 ? -2.742  27.084 16.250  1.00 38.79  ? 111 THR   A CG2  1 
ATOM   870  N  N    . PHE   A 1 112 ? -4.146  30.962 14.910  1.00 35.27  ? 112 PHE   A N    1 
ATOM   871  C  CA   . PHE   A 1 112 ? -4.513  32.364 15.004  1.00 32.08  ? 112 PHE   A CA   1 
ATOM   872  C  C    . PHE   A 1 112 ? -5.827  32.458 15.763  1.00 38.43  ? 112 PHE   A C    1 
ATOM   873  O  O    . PHE   A 1 112 ? -6.525  31.462 15.974  1.00 43.88  ? 112 PHE   A O    1 
ATOM   874  C  CB   . PHE   A 1 112 ? -4.617  33.013 13.620  1.00 38.58  ? 112 PHE   A CB   1 
ATOM   875  C  CG   . PHE   A 1 112 ? -5.521  32.283 12.663  1.00 36.58  ? 112 PHE   A CG   1 
ATOM   876  C  CD1  . PHE   A 1 112 ? -5.111  31.104 12.065  1.00 37.28  ? 112 PHE   A CD1  1 
ATOM   877  C  CD2  . PHE   A 1 112 ? -6.766  32.793 12.340  1.00 40.34  ? 112 PHE   A CD2  1 
ATOM   878  C  CE1  . PHE   A 1 112 ? -5.936  30.437 11.173  1.00 49.53  ? 112 PHE   A CE1  1 
ATOM   879  C  CE2  . PHE   A 1 112 ? -7.597  32.131 11.444  1.00 38.29  ? 112 PHE   A CE2  1 
ATOM   880  C  CZ   . PHE   A 1 112 ? -7.181  30.953 10.860  1.00 32.93  ? 112 PHE   A CZ   1 
ATOM   881  N  N    . SER   A 1 113 ? -6.145  33.671 16.186  1.00 34.66  ? 113 SER   A N    1 
ATOM   882  C  CA   . SER   A 1 113 ? -7.389  33.958 16.880  1.00 40.86  ? 113 SER   A CA   1 
ATOM   883  C  C    . SER   A 1 113 ? -8.398  34.494 15.876  1.00 38.79  ? 113 SER   A C    1 
ATOM   884  O  O    . SER   A 1 113 ? -8.035  35.226 14.951  1.00 35.04  ? 113 SER   A O    1 
ATOM   885  C  CB   . SER   A 1 113 ? -7.164  34.971 18.004  1.00 30.03  ? 113 SER   A CB   1 
ATOM   886  O  OG   . SER   A 1 113 ? -6.347  34.421 19.022  1.00 40.48  ? 113 SER   A OG   1 
ATOM   887  N  N    . VAL   A 1 114 ? -9.662  34.117 16.052  1.00 30.64  ? 114 VAL   A N    1 
ATOM   888  C  CA   . VAL   A 1 114 ? -10.731 34.482 15.131  1.00 34.68  ? 114 VAL   A CA   1 
ATOM   889  C  C    . VAL   A 1 114 ? -11.781 35.270 15.895  1.00 36.39  ? 114 VAL   A C    1 
ATOM   890  O  O    . VAL   A 1 114 ? -12.239 34.839 16.961  1.00 37.57  ? 114 VAL   A O    1 
ATOM   891  C  CB   . VAL   A 1 114 ? -11.372 33.248 14.470  1.00 37.86  ? 114 VAL   A CB   1 
ATOM   892  C  CG1  . VAL   A 1 114 ? -12.625 33.665 13.708  1.00 37.27  ? 114 VAL   A CG1  1 
ATOM   893  C  CG2  . VAL   A 1 114 ? -10.380 32.549 13.550  1.00 36.17  ? 114 VAL   A CG2  1 
ATOM   894  N  N    . LEU   A 1 115 ? -12.170 36.408 15.346  1.00 34.16  ? 115 LEU   A N    1 
ATOM   895  C  CA   . LEU   A 1 115 ? -13.227 37.233 15.916  1.00 41.11  ? 115 LEU   A CA   1 
ATOM   896  C  C    . LEU   A 1 115 ? -14.460 37.067 15.033  1.00 38.47  ? 115 LEU   A C    1 
ATOM   897  O  O    . LEU   A 1 115 ? -14.575 37.713 13.989  1.00 45.51  ? 115 LEU   A O    1 
ATOM   898  C  CB   . LEU   A 1 115 ? -12.784 38.688 16.009  1.00 39.40  ? 115 LEU   A CB   1 
ATOM   899  C  CG   . LEU   A 1 115 ? -13.784 39.660 16.632  1.00 45.06  ? 115 LEU   A CG   1 
ATOM   900  C  CD1  . LEU   A 1 115 ? -13.943 39.409 18.130  1.00 40.59  ? 115 LEU   A CD1  1 
ATOM   901  C  CD2  . LEU   A 1 115 ? -13.360 41.088 16.350  1.00 40.69  ? 115 LEU   A CD2  1 
ATOM   902  N  N    . ALA   A 1 116 ? -15.367 36.182 15.442  1.00 39.47  ? 116 ALA   A N    1 
ATOM   903  C  CA   . ALA   A 1 116 ? -16.615 35.998 14.712  1.00 41.32  ? 116 ALA   A CA   1 
ATOM   904  C  C    . ALA   A 1 116 ? -17.449 37.268 14.797  1.00 43.77  ? 116 ALA   A C    1 
ATOM   905  O  O    . ALA   A 1 116 ? -17.663 37.808 15.888  1.00 47.90  ? 116 ALA   A O    1 
ATOM   906  C  CB   . ALA   A 1 116 ? -17.391 34.808 15.274  1.00 47.98  ? 116 ALA   A CB   1 
ATOM   907  N  N    . CYS   A 1 117 ? -17.927 37.743 13.646  1.00 36.84  ? 117 CYS   A N    1 
ATOM   908  C  CA   A CYS   A 1 117 ? -18.634 39.011 13.579  0.65 47.47  ? 117 CYS   A CA   1 
ATOM   909  C  CA   B CYS   A 1 117 ? -18.627 39.017 13.568  0.35 46.54  ? 117 CYS   A CA   1 
ATOM   910  C  C    . CYS   A 1 117 ? -19.856 38.883 12.682  1.00 53.25  ? 117 CYS   A C    1 
ATOM   911  O  O    . CYS   A 1 117 ? -19.828 38.178 11.669  1.00 41.41  ? 117 CYS   A O    1 
ATOM   912  C  CB   A CYS   A 1 117 ? -17.716 40.128 13.069  0.65 43.48  ? 117 CYS   A CB   1 
ATOM   913  C  CB   B CYS   A 1 117 ? -17.716 40.124 13.023  0.35 43.20  ? 117 CYS   A CB   1 
ATOM   914  S  SG   A CYS   A 1 117 ? -16.524 40.708 14.304  0.65 53.07  ? 117 CYS   A SG   1 
ATOM   915  S  SG   B CYS   A 1 117 ? -18.105 41.783 13.633  0.35 58.35  ? 117 CYS   A SG   1 
ATOM   916  N  N    . TYR   A 1 118 ? -20.928 39.571 13.071  1.00 48.78  ? 118 TYR   A N    1 
ATOM   917  C  CA   . TYR   A 1 118 ? -22.178 39.586 12.326  1.00 51.52  ? 118 TYR   A CA   1 
ATOM   918  C  C    . TYR   A 1 118 ? -22.683 41.017 12.272  1.00 52.31  ? 118 TYR   A C    1 
ATOM   919  O  O    . TYR   A 1 118 ? -22.783 41.684 13.307  1.00 48.91  ? 118 TYR   A O    1 
ATOM   920  C  CB   . TYR   A 1 118 ? -23.213 38.662 12.975  1.00 37.11  ? 118 TYR   A CB   1 
ATOM   921  C  CG   . TYR   A 1 118 ? -22.729 37.234 13.062  1.00 55.72  ? 118 TYR   A CG   1 
ATOM   922  C  CD1  . TYR   A 1 118 ? -21.963 36.806 14.138  1.00 53.61  ? 118 TYR   A CD1  1 
ATOM   923  C  CD2  . TYR   A 1 118 ? -23.014 36.320 12.054  1.00 49.37  ? 118 TYR   A CD2  1 
ATOM   924  C  CE1  . TYR   A 1 118 ? -21.504 35.508 14.217  1.00 49.19  ? 118 TYR   A CE1  1 
ATOM   925  C  CE2  . TYR   A 1 118 ? -22.560 35.018 12.126  1.00 49.96  ? 118 TYR   A CE2  1 
ATOM   926  C  CZ   . TYR   A 1 118 ? -21.805 34.617 13.210  1.00 49.37  ? 118 TYR   A CZ   1 
ATOM   927  O  OH   . TYR   A 1 118 ? -21.348 33.320 13.289  1.00 52.10  ? 118 TYR   A OH   1 
ATOM   928  N  N    . ASN   A 1 119 ? -22.970 41.493 11.062  1.00 50.99  ? 119 ASN   A N    1 
ATOM   929  C  CA   . ASN   A 1 119 ? -23.462 42.854 10.849  1.00 57.71  ? 119 ASN   A CA   1 
ATOM   930  C  C    . ASN   A 1 119 ? -22.530 43.898 11.455  1.00 54.88  ? 119 ASN   A C    1 
ATOM   931  O  O    . ASN   A 1 119 ? -22.974 44.965 11.885  1.00 59.45  ? 119 ASN   A O    1 
ATOM   932  C  CB   . ASN   A 1 119 ? -24.879 43.020 11.402  1.00 52.82  ? 119 ASN   A CB   1 
ATOM   933  C  CG   . ASN   A 1 119 ? -25.923 42.397 10.507  1.00 68.18  ? 119 ASN   A CG   1 
ATOM   934  O  OD1  . ASN   A 1 119 ? -25.789 42.404 9.284   1.00 74.84  ? 119 ASN   A OD1  1 
ATOM   935  N  ND2  . ASN   A 1 119 ? -26.967 41.841 11.112  1.00 77.32  ? 119 ASN   A ND2  1 
ATOM   936  N  N    . GLY   A 1 120 ? -21.235 43.596 11.505  1.00 52.24  ? 120 GLY   A N    1 
ATOM   937  C  CA   . GLY   A 1 120 ? -20.251 44.539 11.990  1.00 51.86  ? 120 GLY   A CA   1 
ATOM   938  C  C    . GLY   A 1 120 ? -20.041 44.563 13.488  1.00 54.70  ? 120 GLY   A C    1 
ATOM   939  O  O    . GLY   A 1 120 ? -19.213 45.348 13.964  1.00 56.35  ? 120 GLY   A O    1 
ATOM   940  N  N    . SER   A 1 121 ? -20.753 43.737 14.251  1.00 54.75  ? 121 SER   A N    1 
ATOM   941  C  CA   . SER   A 1 121 ? -20.605 43.698 15.703  1.00 52.20  ? 121 SER   A CA   1 
ATOM   942  C  C    . SER   A 1 121 ? -20.056 42.339 16.126  1.00 60.19  ? 121 SER   A C    1 
ATOM   943  O  O    . SER   A 1 121 ? -20.667 41.303 15.809  1.00 49.62  ? 121 SER   A O    1 
ATOM   944  C  CB   . SER   A 1 121 ? -21.940 43.980 16.394  1.00 43.97  ? 121 SER   A CB   1 
ATOM   945  O  OG   . SER   A 1 121 ? -23.013 43.404 15.680  1.00 64.53  ? 121 SER   A OG   1 
ATOM   946  N  N    . PRO   A 1 122 ? -18.922 42.288 16.821  1.00 58.77  ? 122 PRO   A N    1 
ATOM   947  C  CA   . PRO   A 1 122 ? -18.349 40.990 17.191  1.00 50.12  ? 122 PRO   A CA   1 
ATOM   948  C  C    . PRO   A 1 122 ? -19.241 40.234 18.157  1.00 46.55  ? 122 PRO   A C    1 
ATOM   949  O  O    . PRO   A 1 122 ? -19.924 40.818 19.002  1.00 55.95  ? 122 PRO   A O    1 
ATOM   950  C  CB   . PRO   A 1 122 ? -17.015 41.367 17.846  1.00 51.43  ? 122 PRO   A CB   1 
ATOM   951  C  CG   . PRO   A 1 122 ? -16.701 42.723 17.303  1.00 57.32  ? 122 PRO   A CG   1 
ATOM   952  C  CD   . PRO   A 1 122 ? -18.028 43.403 17.167  1.00 47.82  ? 122 PRO   A CD   1 
ATOM   953  N  N    . SER   A 1 123 ? -19.222 38.907 18.026  1.00 50.07  ? 123 SER   A N    1 
ATOM   954  C  CA   . SER   A 1 123 ? -20.004 38.036 18.889  1.00 48.04  ? 123 SER   A CA   1 
ATOM   955  C  C    . SER   A 1 123 ? -19.180 37.012 19.658  1.00 39.17  ? 123 SER   A C    1 
ATOM   956  O  O    . SER   A 1 123 ? -19.675 36.487 20.660  1.00 46.98  ? 123 SER   A O    1 
ATOM   957  C  CB   . SER   A 1 123 ? -21.074 37.291 18.071  1.00 50.81  ? 123 SER   A CB   1 
ATOM   958  O  OG   . SER   A 1 123 ? -20.565 36.075 17.549  1.00 56.78  ? 123 SER   A OG   1 
ATOM   959  N  N    . GLY   A 1 124 ? -17.958 36.707 19.228  1.00 40.51  ? 124 GLY   A N    1 
ATOM   960  C  CA   . GLY   A 1 124 ? -17.154 35.726 19.932  1.00 33.62  ? 124 GLY   A CA   1 
ATOM   961  C  C    . GLY   A 1 124 ? -15.739 35.678 19.404  1.00 42.22  ? 124 GLY   A C    1 
ATOM   962  O  O    . GLY   A 1 124 ? -15.449 36.140 18.294  1.00 35.26  ? 124 GLY   A O    1 
ATOM   963  N  N    . VAL   A 1 125 ? -14.856 35.106 20.226  1.00 38.14  ? 125 VAL   A N    1 
ATOM   964  C  CA   . VAL   A 1 125 ? -13.450 34.921 19.887  1.00 39.68  ? 125 VAL   A CA   1 
ATOM   965  C  C    . VAL   A 1 125 ? -13.038 33.503 20.262  1.00 38.08  ? 125 VAL   A C    1 
ATOM   966  O  O    . VAL   A 1 125 ? -13.479 32.967 21.284  1.00 35.27  ? 125 VAL   A O    1 
ATOM   967  C  CB   . VAL   A 1 125 ? -12.553 35.954 20.600  1.00 40.35  ? 125 VAL   A CB   1 
ATOM   968  C  CG1  . VAL   A 1 125 ? -12.777 35.901 22.101  1.00 38.80  ? 125 VAL   A CG1  1 
ATOM   969  C  CG2  . VAL   A 1 125 ? -11.092 35.709 20.271  1.00 37.11  ? 125 VAL   A CG2  1 
ATOM   970  N  N    . TYR   A 1 126 ? -12.191 32.898 19.434  1.00 30.74  ? 126 TYR   A N    1 
ATOM   971  C  CA   . TYR   A 1 126 ? -11.724 31.543 19.683  1.00 38.27  ? 126 TYR   A CA   1 
ATOM   972  C  C    . TYR   A 1 126 ? -10.460 31.303 18.871  1.00 41.76  ? 126 TYR   A C    1 
ATOM   973  O  O    . TYR   A 1 126 ? -10.141 32.057 17.950  1.00 38.89  ? 126 TYR   A O    1 
ATOM   974  C  CB   . TYR   A 1 126 ? -12.799 30.506 19.342  1.00 45.83  ? 126 TYR   A CB   1 
ATOM   975  C  CG   . TYR   A 1 126 ? -13.298 30.553 17.910  1.00 38.39  ? 126 TYR   A CG   1 
ATOM   976  C  CD1  . TYR   A 1 126 ? -12.596 29.928 16.888  1.00 38.93  ? 126 TYR   A CD1  1 
ATOM   977  C  CD2  . TYR   A 1 126 ? -14.475 31.215 17.586  1.00 42.65  ? 126 TYR   A CD2  1 
ATOM   978  C  CE1  . TYR   A 1 126 ? -13.050 29.963 15.580  1.00 46.65  ? 126 TYR   A CE1  1 
ATOM   979  C  CE2  . TYR   A 1 126 ? -14.938 31.256 16.285  1.00 47.44  ? 126 TYR   A CE2  1 
ATOM   980  C  CZ   . TYR   A 1 126 ? -14.223 30.629 15.286  1.00 50.15  ? 126 TYR   A CZ   1 
ATOM   981  O  OH   . TYR   A 1 126 ? -14.680 30.665 13.990  1.00 47.40  ? 126 TYR   A OH   1 
ATOM   982  N  N    . GLN   A 1 127 ? -9.749  30.236 19.224  1.00 37.43  ? 127 GLN   A N    1 
ATOM   983  C  CA   . GLN   A 1 127 ? -8.478  29.898 18.600  1.00 44.82  ? 127 GLN   A CA   1 
ATOM   984  C  C    . GLN   A 1 127 ? -8.688  28.888 17.478  1.00 43.82  ? 127 GLN   A C    1 
ATOM   985  O  O    . GLN   A 1 127 ? -9.504  27.970 17.597  1.00 50.89  ? 127 GLN   A O    1 
ATOM   986  C  CB   . GLN   A 1 127 ? -7.496  29.346 19.641  1.00 46.25  ? 127 GLN   A CB   1 
ATOM   987  C  CG   . GLN   A 1 127 ? -6.025  29.497 19.257  1.00 45.05  ? 127 GLN   A CG   1 
ATOM   988  C  CD   . GLN   A 1 127 ? -5.555  30.949 19.192  1.00 50.51  ? 127 GLN   A CD   1 
ATOM   989  O  OE1  . GLN   A 1 127 ? -4.380  31.215 18.933  1.00 52.90  ? 127 GLN   A OE1  1 
ATOM   990  N  NE2  . GLN   A 1 127 ? -6.463  31.890 19.447  1.00 49.37  ? 127 GLN   A NE2  1 
ATOM   991  N  N    . CYS   A 1 128 ? -7.947  29.069 16.386  1.00 42.84  ? 128 CYS   A N    1 
ATOM   992  C  CA   . CYS   A 1 128 ? -8.062  28.242 15.193  1.00 46.20  ? 128 CYS   A CA   1 
ATOM   993  C  C    . CYS   A 1 128 ? -6.680  27.862 14.689  1.00 37.42  ? 128 CYS   A C    1 
ATOM   994  O  O    . CYS   A 1 128 ? -5.674  28.482 15.041  1.00 43.89  ? 128 CYS   A O    1 
ATOM   995  C  CB   . CYS   A 1 128 ? -8.820  28.962 14.061  1.00 39.42  ? 128 CYS   A CB   1 
ATOM   996  S  SG   . CYS   A 1 128 ? -10.546 28.493 13.875  1.00 75.75  ? 128 CYS   A SG   1 
ATOM   997  N  N    . ALA   A 1 129 ? -6.651  26.848 13.826  1.00 47.03  ? 129 ALA   A N    1 
ATOM   998  C  CA   . ALA   A 1 129 ? -5.436  26.416 13.154  1.00 44.61  ? 129 ALA   A CA   1 
ATOM   999  C  C    . ALA   A 1 129 ? -5.694  26.304 11.657  1.00 45.32  ? 129 ALA   A C    1 
ATOM   1000 O  O    . ALA   A 1 129 ? -6.791  25.927 11.232  1.00 39.96  ? 129 ALA   A O    1 
ATOM   1001 C  CB   . ALA   A 1 129 ? -4.941  25.071 13.704  1.00 44.44  ? 129 ALA   A CB   1 
ATOM   1002 N  N    . MET   A 1 130 ? -4.680  26.639 10.864  1.00 40.33  ? 130 MET   A N    1 
ATOM   1003 C  CA   . MET   A 1 130 ? -4.730  26.449 9.419   1.00 35.53  ? 130 MET   A CA   1 
ATOM   1004 C  C    . MET   A 1 130 ? -4.381  24.996 9.113   1.00 37.73  ? 130 MET   A C    1 
ATOM   1005 O  O    . MET   A 1 130 ? -3.245  24.564 9.335   1.00 40.25  ? 130 MET   A O    1 
ATOM   1006 C  CB   . MET   A 1 130 ? -3.775  27.416 8.721   1.00 43.20  ? 130 MET   A CB   1 
ATOM   1007 C  CG   . MET   A 1 130 ? -3.696  27.277 7.197   1.00 41.60  ? 130 MET   A CG   1 
ATOM   1008 S  SD   . MET   A 1 130 ? -5.142  27.884 6.300   1.00 52.72  ? 130 MET   A SD   1 
ATOM   1009 C  CE   . MET   A 1 130 ? -5.130  29.626 6.705   1.00 42.53  ? 130 MET   A CE   1 
ATOM   1010 N  N    . ARG   A 1 131 ? -5.355  24.235 8.615   1.00 32.74  ? 131 ARG   A N    1 
ATOM   1011 C  CA   . ARG   A 1 131 ? -5.124  22.832 8.317   1.00 34.25  ? 131 ARG   A CA   1 
ATOM   1012 C  C    . ARG   A 1 131 ? -4.118  22.682 7.175   1.00 34.09  ? 131 ARG   A C    1 
ATOM   1013 O  O    . ARG   A 1 131 ? -3.881  23.622 6.415   1.00 34.90  ? 131 ARG   A O    1 
ATOM   1014 C  CB   . ARG   A 1 131 ? -6.435  22.137 7.953   1.00 37.88  ? 131 ARG   A CB   1 
ATOM   1015 C  CG   . ARG   A 1 131 ? -7.532  22.234 9.008   1.00 41.93  ? 131 ARG   A CG   1 
ATOM   1016 C  CD   . ARG   A 1 131 ? -7.058  21.745 10.367  1.00 41.49  ? 131 ARG   A CD   1 
ATOM   1017 N  NE   . ARG   A 1 131 ? -6.515  20.394 10.309  1.00 41.91  ? 131 ARG   A NE   1 
ATOM   1018 C  CZ   . ARG   A 1 131 ? -5.893  19.795 11.316  1.00 51.41  ? 131 ARG   A CZ   1 
ATOM   1019 N  NH1  . ARG   A 1 131 ? -5.718  20.404 12.479  1.00 48.87  ? 131 ARG   A NH1  1 
ATOM   1020 N  NH2  . ARG   A 1 131 ? -5.434  18.554 11.153  1.00 38.11  ? 131 ARG   A NH2  1 
ATOM   1021 N  N    . PRO   A 1 132 ? -3.493  21.509 7.053   1.00 40.23  ? 132 PRO   A N    1 
ATOM   1022 C  CA   . PRO   A 1 132 ? -2.577  21.280 5.922   1.00 42.07  ? 132 PRO   A CA   1 
ATOM   1023 C  C    . PRO   A 1 132 ? -3.247  21.384 4.564   1.00 46.84  ? 132 PRO   A C    1 
ATOM   1024 O  O    . PRO   A 1 132 ? -2.555  21.628 3.567   1.00 43.71  ? 132 PRO   A O    1 
ATOM   1025 C  CB   . PRO   A 1 132 ? -2.050  19.861 6.181   1.00 39.01  ? 132 PRO   A CB   1 
ATOM   1026 C  CG   . PRO   A 1 132 ? -2.172  19.692 7.663   1.00 44.56  ? 132 PRO   A CG   1 
ATOM   1027 C  CD   . PRO   A 1 132 ? -3.431  20.421 8.045   1.00 36.80  ? 132 PRO   A CD   1 
ATOM   1028 N  N    . ASN   A 1 133 ? -4.564  21.200 4.483   1.00 40.96  ? 133 ASN   A N    1 
ATOM   1029 C  CA   . ASN   A 1 133 ? -5.288  21.362 3.230   1.00 42.92  ? 133 ASN   A CA   1 
ATOM   1030 C  C    . ASN   A 1 133 ? -5.810  22.782 3.034   1.00 43.24  ? 133 ASN   A C    1 
ATOM   1031 O  O    . ASN   A 1 133 ? -6.571  23.027 2.092   1.00 41.03  ? 133 ASN   A O    1 
ATOM   1032 C  CB   . ASN   A 1 133 ? -6.439  20.353 3.146   1.00 45.15  ? 133 ASN   A CB   1 
ATOM   1033 C  CG   . ASN   A 1 133 ? -7.556  20.646 4.137   1.00 42.16  ? 133 ASN   A CG   1 
ATOM   1034 O  OD1  . ASN   A 1 133 ? -7.479  21.591 4.922   1.00 47.86  ? 133 ASN   A OD1  1 
ATOM   1035 N  ND2  . ASN   A 1 133 ? -8.602  19.829 4.103   1.00 42.30  ? 133 ASN   A ND2  1 
ATOM   1036 N  N    . PHE   A 1 134 ? -5.431  23.714 3.908   1.00 39.43  ? 134 PHE   A N    1 
ATOM   1037 C  CA   . PHE   A 1 134 ? -5.690  25.144 3.757   1.00 39.77  ? 134 PHE   A CA   1 
ATOM   1038 C  C    . PHE   A 1 134 ? -7.119  25.540 4.092   1.00 39.42  ? 134 PHE   A C    1 
ATOM   1039 O  O    . PHE   A 1 134 ? -7.556  26.637 3.735   1.00 53.44  ? 134 PHE   A O    1 
ATOM   1040 C  CB   . PHE   A 1 134 ? -5.333  25.624 2.348   1.00 33.89  ? 134 PHE   A CB   1 
ATOM   1041 C  CG   . PHE   A 1 134 ? -3.859  25.713 2.113   1.00 45.42  ? 134 PHE   A CG   1 
ATOM   1042 C  CD1  . PHE   A 1 134 ? -3.106  26.675 2.765   1.00 39.77  ? 134 PHE   A CD1  1 
ATOM   1043 C  CD2  . PHE   A 1 134 ? -3.219  24.820 1.271   1.00 43.21  ? 134 PHE   A CD2  1 
ATOM   1044 C  CE1  . PHE   A 1 134 ? -1.743  26.757 2.569   1.00 50.07  ? 134 PHE   A CE1  1 
ATOM   1045 C  CE2  . PHE   A 1 134 ? -1.856  24.898 1.069   1.00 47.96  ? 134 PHE   A CE2  1 
ATOM   1046 C  CZ   . PHE   A 1 134 ? -1.116  25.869 1.719   1.00 52.13  ? 134 PHE   A CZ   1 
ATOM   1047 N  N    . THR   A 1 135 ? -7.863  24.673 4.761   1.00 36.54  ? 135 THR   A N    1 
ATOM   1048 C  CA   . THR   A 1 135 ? -9.128  25.031 5.378   1.00 35.75  ? 135 THR   A CA   1 
ATOM   1049 C  C    . THR   A 1 135 ? -8.921  25.223 6.876   1.00 37.81  ? 135 THR   A C    1 
ATOM   1050 O  O    . THR   A 1 135 ? -7.864  24.912 7.432   1.00 36.93  ? 135 THR   A O    1 
ATOM   1051 C  CB   . THR   A 1 135 ? -10.184 23.949 5.124   1.00 46.95  ? 135 THR   A CB   1 
ATOM   1052 O  OG1  . THR   A 1 135 ? -9.872  22.783 5.901   1.00 36.99  ? 135 THR   A OG1  1 
ATOM   1053 C  CG2  . THR   A 1 135 ? -10.223 23.571 3.647   1.00 38.66  ? 135 THR   A CG2  1 
ATOM   1054 N  N    . ILE   A 1 136 ? -9.952  25.731 7.537   1.00 34.94  ? 136 ILE   A N    1 
ATOM   1055 C  CA   . ILE   A 1 136 ? -9.961  25.848 8.989   1.00 39.55  ? 136 ILE   A CA   1 
ATOM   1056 C  C    . ILE   A 1 136 ? -11.265 25.268 9.516   1.00 46.34  ? 136 ILE   A C    1 
ATOM   1057 O  O    . ILE   A 1 136 ? -12.312 25.371 8.866   1.00 40.47  ? 136 ILE   A O    1 
ATOM   1058 C  CB   . ILE   A 1 136 ? -9.772  27.308 9.452   1.00 43.96  ? 136 ILE   A CB   1 
ATOM   1059 C  CG1  . ILE   A 1 136 ? -11.018 28.140 9.149   1.00 49.30  ? 136 ILE   A CG1  1 
ATOM   1060 C  CG2  . ILE   A 1 136 ? -8.542  27.922 8.802   1.00 45.85  ? 136 ILE   A CG2  1 
ATOM   1061 C  CD1  . ILE   A 1 136 ? -10.900 29.580 9.610   1.00 43.37  ? 136 ILE   A CD1  1 
ATOM   1062 N  N    . LYS   A 1 137 ? -11.195 24.630 10.681  1.00 46.52  ? 137 LYS   A N    1 
ATOM   1063 C  CA   . LYS   A 1 137 ? -12.380 24.071 11.327  1.00 49.53  ? 137 LYS   A CA   1 
ATOM   1064 C  C    . LYS   A 1 137 ? -12.907 25.068 12.357  1.00 47.66  ? 137 LYS   A C    1 
ATOM   1065 O  O    . LYS   A 1 137 ? -12.801 24.884 13.568  1.00 53.04  ? 137 LYS   A O    1 
ATOM   1066 C  CB   . LYS   A 1 137 ? -12.053 22.720 11.957  1.00 48.24  ? 137 LYS   A CB   1 
ATOM   1067 C  CG   . LYS   A 1 137 ? -11.320 21.772 11.020  1.00 52.14  ? 137 LYS   A CG   1 
ATOM   1068 C  CD   . LYS   A 1 137 ? -11.529 20.316 11.409  1.00 65.33  ? 137 LYS   A CD   1 
ATOM   1069 C  CE   . LYS   A 1 137 ? -10.511 19.416 10.720  1.00 67.36  ? 137 LYS   A CE   1 
ATOM   1070 N  NZ   . LYS   A 1 137 ? -9.993  18.341 11.617  1.00 78.80  ? 137 LYS   A NZ   1 
ATOM   1071 N  N    . GLY   A 1 138 ? -13.480 26.153 11.840  1.00 42.43  ? 138 GLY   A N    1 
ATOM   1072 C  CA   . GLY   A 1 138 ? -13.978 27.228 12.669  1.00 42.55  ? 138 GLY   A CA   1 
ATOM   1073 C  C    . GLY   A 1 138 ? -15.416 27.013 13.091  1.00 44.59  ? 138 GLY   A C    1 
ATOM   1074 O  O    . GLY   A 1 138 ? -16.003 25.944 12.913  1.00 43.99  ? 138 GLY   A O    1 
ATOM   1075 N  N    . SER   A 1 139 ? -15.988 28.059 13.679  1.00 42.90  ? 139 SER   A N    1 
ATOM   1076 C  CA   . SER   A 1 139 ? -17.405 28.082 14.037  1.00 49.46  ? 139 SER   A CA   1 
ATOM   1077 C  C    . SER   A 1 139 ? -17.980 29.381 13.481  1.00 52.12  ? 139 SER   A C    1 
ATOM   1078 O  O    . SER   A 1 139 ? -17.747 30.461 14.034  1.00 42.76  ? 139 SER   A O    1 
ATOM   1079 C  CB   . SER   A 1 139 ? -17.603 27.969 15.543  1.00 42.04  ? 139 SER   A CB   1 
ATOM   1080 O  OG   . SER   A 1 139 ? -18.930 28.308 15.910  1.00 53.94  ? 139 SER   A OG   1 
ATOM   1081 N  N    . PHE   A 1 140 ? -18.717 29.265 12.379  1.00 38.21  ? 140 PHE   A N    1 
ATOM   1082 C  CA   . PHE   A 1 140 ? -19.211 30.406 11.624  1.00 48.97  ? 140 PHE   A CA   1 
ATOM   1083 C  C    . PHE   A 1 140 ? -20.648 30.152 11.203  1.00 46.38  ? 140 PHE   A C    1 
ATOM   1084 O  O    . PHE   A 1 140 ? -20.999 29.037 10.810  1.00 50.06  ? 140 PHE   A O    1 
ATOM   1085 C  CB   . PHE   A 1 140 ? -18.364 30.662 10.370  1.00 44.83  ? 140 PHE   A CB   1 
ATOM   1086 C  CG   . PHE   A 1 140 ? -17.036 31.297 10.647  1.00 47.85  ? 140 PHE   A CG   1 
ATOM   1087 C  CD1  . PHE   A 1 140 ? -16.957 32.517 11.300  1.00 40.33  ? 140 PHE   A CD1  1 
ATOM   1088 C  CD2  . PHE   A 1 140 ? -15.862 30.681 10.239  1.00 47.93  ? 140 PHE   A CD2  1 
ATOM   1089 C  CE1  . PHE   A 1 140 ? -15.730 33.109 11.549  1.00 42.38  ? 140 PHE   A CE1  1 
ATOM   1090 C  CE2  . PHE   A 1 140 ? -14.632 31.267 10.485  1.00 42.55  ? 140 PHE   A CE2  1 
ATOM   1091 C  CZ   . PHE   A 1 140 ? -14.566 32.484 11.139  1.00 41.52  ? 140 PHE   A CZ   1 
ATOM   1092 N  N    . LEU   A 1 141 ? -21.470 31.188 11.274  1.00 46.31  ? 141 LEU   A N    1 
ATOM   1093 C  CA   . LEU   A 1 141 ? -22.834 31.127 10.777  1.00 54.80  ? 141 LEU   A CA   1 
ATOM   1094 C  C    . LEU   A 1 141 ? -23.009 32.089 9.611   1.00 54.66  ? 141 LEU   A C    1 
ATOM   1095 O  O    . LEU   A 1 141 ? -22.102 32.843 9.248   1.00 46.03  ? 141 LEU   A O    1 
ATOM   1096 C  CB   . LEU   A 1 141 ? -23.835 31.446 11.888  1.00 51.67  ? 141 LEU   A CB   1 
ATOM   1097 C  CG   . LEU   A 1 141 ? -23.771 30.489 13.073  1.00 55.84  ? 141 LEU   A CG   1 
ATOM   1098 C  CD1  . LEU   A 1 141 ? -24.612 31.024 14.216  1.00 56.04  ? 141 LEU   A CD1  1 
ATOM   1099 C  CD2  . LEU   A 1 141 ? -24.222 29.098 12.659  1.00 51.18  ? 141 LEU   A CD2  1 
ATOM   1100 N  N    . ASN   A 1 142 ? -24.201 32.059 9.023   1.00 53.93  ? 142 ASN   A N    1 
ATOM   1101 C  CA   . ASN   A 1 142 ? -24.489 32.966 7.924   1.00 53.20  ? 142 ASN   A CA   1 
ATOM   1102 C  C    . ASN   A 1 142 ? -24.317 34.408 8.382   1.00 55.18  ? 142 ASN   A C    1 
ATOM   1103 O  O    . ASN   A 1 142 ? -24.749 34.787 9.474   1.00 55.76  ? 142 ASN   A O    1 
ATOM   1104 C  CB   . ASN   A 1 142 ? -25.902 32.742 7.400   1.00 57.84  ? 142 ASN   A CB   1 
ATOM   1105 C  CG   . ASN   A 1 142 ? -25.955 32.732 5.892   1.00 73.42  ? 142 ASN   A CG   1 
ATOM   1106 O  OD1  . ASN   A 1 142 ? -25.891 33.781 5.252   1.00 85.67  ? 142 ASN   A OD1  1 
ATOM   1107 N  ND2  . ASN   A 1 142 ? -26.069 31.541 5.310   1.00 67.15  ? 142 ASN   A ND2  1 
ATOM   1108 N  N    . GLY   A 1 143 ? -23.673 35.213 7.540   1.00 51.36  ? 143 GLY   A N    1 
ATOM   1109 C  CA   . GLY   A 1 143 ? -23.362 36.584 7.874   1.00 42.82  ? 143 GLY   A CA   1 
ATOM   1110 C  C    . GLY   A 1 143 ? -21.992 36.790 8.480   1.00 48.89  ? 143 GLY   A C    1 
ATOM   1111 O  O    . GLY   A 1 143 ? -21.571 37.943 8.641   1.00 42.80  ? 143 GLY   A O    1 
ATOM   1112 N  N    . SER   A 1 144 ? -21.285 35.713 8.825   1.00 43.71  ? 144 SER   A N    1 
ATOM   1113 C  CA   . SER   A 1 144 ? -19.938 35.826 9.366   1.00 44.44  ? 144 SER   A CA   1 
ATOM   1114 C  C    . SER   A 1 144 ? -18.917 36.256 8.321   1.00 35.83  ? 144 SER   A C    1 
ATOM   1115 O  O    . SER   A 1 144 ? -17.778 36.568 8.682   1.00 37.51  ? 144 SER   A O    1 
ATOM   1116 C  CB   . SER   A 1 144 ? -19.513 34.491 9.988   1.00 45.45  ? 144 SER   A CB   1 
ATOM   1117 O  OG   . SER   A 1 144 ? -19.484 33.454 9.016   1.00 45.96  ? 144 SER   A OG   1 
ATOM   1118 N  N    . CYS   A 1 145 ? -19.294 36.281 7.048   1.00 34.20  ? 145 CYS   A N    1 
ATOM   1119 C  CA   . CYS   A 1 145 ? -18.361 36.648 5.992   1.00 41.68  ? 145 CYS   A CA   1 
ATOM   1120 C  C    . CYS   A 1 145 ? -17.756 38.023 6.260   1.00 40.75  ? 145 CYS   A C    1 
ATOM   1121 O  O    . CYS   A 1 145 ? -18.460 38.971 6.617   1.00 39.45  ? 145 CYS   A O    1 
ATOM   1122 C  CB   . CYS   A 1 145 ? -19.077 36.627 4.641   1.00 38.90  ? 145 CYS   A CB   1 
ATOM   1123 S  SG   . CYS   A 1 145 ? -17.972 36.770 3.239   1.00 67.63  ? 145 CYS   A SG   1 
ATOM   1124 N  N    . GLY   A 1 146 ? -16.437 38.126 6.088   1.00 35.23  ? 146 GLY   A N    1 
ATOM   1125 C  CA   . GLY   A 1 146 ? -15.687 39.310 6.443   1.00 36.50  ? 146 GLY   A CA   1 
ATOM   1126 C  C    . GLY   A 1 146 ? -14.949 39.222 7.770   1.00 38.04  ? 146 GLY   A C    1 
ATOM   1127 O  O    . GLY   A 1 146 ? -14.059 40.045 8.027   1.00 33.13  ? 146 GLY   A O    1 
ATOM   1128 N  N    . SER   A 1 147 ? -15.297 38.260 8.621   1.00 39.25  ? 147 SER   A N    1 
ATOM   1129 C  CA   . SER   A 1 147 ? -14.597 38.103 9.891   1.00 38.94  ? 147 SER   A CA   1 
ATOM   1130 C  C    . SER   A 1 147 ? -13.107 37.877 9.644   1.00 34.01  ? 147 SER   A C    1 
ATOM   1131 O  O    . SER   A 1 147 ? -12.702 37.360 8.601   1.00 34.71  ? 147 SER   A O    1 
ATOM   1132 C  CB   . SER   A 1 147 ? -15.192 36.937 10.675  1.00 35.83  ? 147 SER   A CB   1 
ATOM   1133 O  OG   . SER   A 1 147 ? -16.485 37.258 11.162  1.00 40.25  ? 147 SER   A OG   1 
ATOM   1134 N  N    . VAL   A 1 148 ? -12.282 38.276 10.610  1.00 33.37  ? 148 VAL   A N    1 
ATOM   1135 C  CA   . VAL   A 1 148 ? -10.838 38.286 10.409  1.00 34.24  ? 148 VAL   A CA   1 
ATOM   1136 C  C    . VAL   A 1 148 ? -10.158 37.462 11.492  1.00 38.04  ? 148 VAL   A C    1 
ATOM   1137 O  O    . VAL   A 1 148 ? -10.637 37.362 12.626  1.00 33.04  ? 148 VAL   A O    1 
ATOM   1138 C  CB   . VAL   A 1 148 ? -10.273 39.724 10.378  1.00 42.83  ? 148 VAL   A CB   1 
ATOM   1139 C  CG1  . VAL   A 1 148 ? -10.883 40.511 9.211   1.00 34.42  ? 148 VAL   A CG1  1 
ATOM   1140 C  CG2  . VAL   A 1 148 ? -10.509 40.428 11.698  1.00 26.48  ? 148 VAL   A CG2  1 
ATOM   1141 N  N    . GLY   A 1 149 ? -9.034  36.852 11.117  1.00 38.56  ? 149 GLY   A N    1 
ATOM   1142 C  CA   . GLY   A 1 149 ? -8.185  36.134 12.048  1.00 32.10  ? 149 GLY   A CA   1 
ATOM   1143 C  C    . GLY   A 1 149 ? -6.903  36.907 12.283  1.00 39.52  ? 149 GLY   A C    1 
ATOM   1144 O  O    . GLY   A 1 149 ? -6.505  37.711 11.435  1.00 33.24  ? 149 GLY   A O    1 
ATOM   1145 N  N    . PHE   A 1 150 ? -6.238  36.687 13.413  1.00 33.24  ? 150 PHE   A N    1 
ATOM   1146 C  CA   . PHE   A 1 150 ? -5.128  37.557 13.765  1.00 33.36  ? 150 PHE   A CA   1 
ATOM   1147 C  C    . PHE   A 1 150 ? -4.304  36.935 14.882  1.00 40.12  ? 150 PHE   A C    1 
ATOM   1148 O  O    . PHE   A 1 150 ? -4.790  36.108 15.658  1.00 35.18  ? 150 PHE   A O    1 
ATOM   1149 C  CB   . PHE   A 1 150 ? -5.637  38.927 14.208  1.00 28.92  ? 150 PHE   A CB   1 
ATOM   1150 C  CG   . PHE   A 1 150 ? -6.533  38.864 15.401  1.00 35.04  ? 150 PHE   A CG   1 
ATOM   1151 C  CD1  . PHE   A 1 150 ? -7.882  38.589 15.255  1.00 40.38  ? 150 PHE   A CD1  1 
ATOM   1152 C  CD2  . PHE   A 1 150 ? -6.025  39.058 16.679  1.00 41.60  ? 150 PHE   A CD2  1 
ATOM   1153 C  CE1  . PHE   A 1 150 ? -8.714  38.516 16.363  1.00 32.44  ? 150 PHE   A CE1  1 
ATOM   1154 C  CE2  . PHE   A 1 150 ? -6.848  38.990 17.786  1.00 37.62  ? 150 PHE   A CE2  1 
ATOM   1155 C  CZ   . PHE   A 1 150 ? -8.193  38.719 17.630  1.00 39.65  ? 150 PHE   A CZ   1 
ATOM   1156 N  N    . ASN   A 1 151 ? -3.051  37.373 14.961  1.00 39.44  ? 151 ASN   A N    1 
ATOM   1157 C  CA   . ASN   A 1 151 ? -2.199  37.140 16.113  1.00 42.87  ? 151 ASN   A CA   1 
ATOM   1158 C  C    . ASN   A 1 151 ? -1.754  38.491 16.659  1.00 48.57  ? 151 ASN   A C    1 
ATOM   1159 O  O    . ASN   A 1 151 ? -1.787  39.506 15.956  1.00 37.45  ? 151 ASN   A O    1 
ATOM   1160 C  CB   . ASN   A 1 151 ? -0.991  36.271 15.742  1.00 36.53  ? 151 ASN   A CB   1 
ATOM   1161 C  CG   . ASN   A 1 151 ? -1.362  34.808 15.569  1.00 46.42  ? 151 ASN   A CG   1 
ATOM   1162 O  OD1  . ASN   A 1 151 ? -1.889  34.179 16.486  1.00 49.82  ? 151 ASN   A OD1  1 
ATOM   1163 N  ND2  . ASN   A 1 151 ? -1.103  34.264 14.383  1.00 38.56  ? 151 ASN   A ND2  1 
ATOM   1164 N  N    . ILE   A 1 152 ? -1.354  38.514 17.928  1.00 41.78  ? 152 ILE   A N    1 
ATOM   1165 C  CA   . ILE   A 1 152 ? -0.946  39.750 18.586  1.00 52.24  ? 152 ILE   A CA   1 
ATOM   1166 C  C    . ILE   A 1 152 ? 0.453   39.562 19.152  1.00 55.57  ? 152 ILE   A C    1 
ATOM   1167 O  O    . ILE   A 1 152 ? 0.703   38.618 19.910  1.00 59.79  ? 152 ILE   A O    1 
ATOM   1168 C  CB   . ILE   A 1 152 ? -1.934  40.172 19.687  1.00 44.31  ? 152 ILE   A CB   1 
ATOM   1169 C  CG1  . ILE   A 1 152 ? -3.243  40.659 19.066  1.00 52.08  ? 152 ILE   A CG1  1 
ATOM   1170 C  CG2  . ILE   A 1 152 ? -1.340  41.298 20.509  1.00 44.49  ? 152 ILE   A CG2  1 
ATOM   1171 C  CD1  . ILE   A 1 152 ? -4.232  41.195 20.081  1.00 50.20  ? 152 ILE   A CD1  1 
ATOM   1172 N  N    . ASP   A 1 153 ? 1.357   40.470 18.792  1.00 62.64  ? 153 ASP   A N    1 
ATOM   1173 C  CA   . ASP   A 1 153 ? 2.776   40.365 19.141  1.00 76.04  ? 153 ASP   A CA   1 
ATOM   1174 C  C    . ASP   A 1 153 ? 3.230   41.742 19.626  1.00 82.84  ? 153 ASP   A C    1 
ATOM   1175 O  O    . ASP   A 1 153 ? 3.607   42.603 18.826  1.00 86.01  ? 153 ASP   A O    1 
ATOM   1176 C  CB   . ASP   A 1 153 ? 3.590   39.872 17.947  1.00 82.67  ? 153 ASP   A CB   1 
ATOM   1177 C  CG   . ASP   A 1 153 ? 5.042   40.309 17.998  1.00 97.48  ? 153 ASP   A CG   1 
ATOM   1178 O  OD1  . ASP   A 1 153 ? 5.669   40.180 19.070  1.00 106.89 ? 153 ASP   A OD1  1 
ATOM   1179 O  OD2  . ASP   A 1 153 ? 5.558   40.784 16.964  1.00 102.61 ? 153 ASP   A OD2  1 
ATOM   1180 N  N    . TYR   A 1 154 ? 3.166   41.947 20.941  1.00 81.13  ? 154 TYR   A N    1 
ATOM   1181 C  CA   . TYR   A 1 154 ? 3.616   43.180 21.586  1.00 76.54  ? 154 TYR   A CA   1 
ATOM   1182 C  C    . TYR   A 1 154 ? 2.936   44.407 20.965  1.00 74.90  ? 154 TYR   A C    1 
ATOM   1183 O  O    . TYR   A 1 154 ? 3.557   45.253 20.318  1.00 71.50  ? 154 TYR   A O    1 
ATOM   1184 C  CB   . TYR   A 1 154 ? 5.147   43.284 21.533  1.00 81.11  ? 154 TYR   A CB   1 
ATOM   1185 C  CG   . TYR   A 1 154 ? 5.880   42.172 22.276  1.00 89.55  ? 154 TYR   A CG   1 
ATOM   1186 C  CD1  . TYR   A 1 154 ? 5.780   40.847 21.863  1.00 95.98  ? 154 TYR   A CD1  1 
ATOM   1187 C  CD2  . TYR   A 1 154 ? 6.662   42.446 23.396  1.00 92.88  ? 154 TYR   A CD2  1 
ATOM   1188 C  CE1  . TYR   A 1 154 ? 6.443   39.825 22.538  1.00 93.11  ? 154 TYR   A CE1  1 
ATOM   1189 C  CE2  . TYR   A 1 154 ? 7.334   41.427 24.076  1.00 86.62  ? 154 TYR   A CE2  1 
ATOM   1190 C  CZ   . TYR   A 1 154 ? 7.217   40.119 23.641  1.00 95.52  ? 154 TYR   A CZ   1 
ATOM   1191 O  OH   . TYR   A 1 154 ? 7.874   39.106 24.309  1.00 91.85  ? 154 TYR   A OH   1 
ATOM   1192 N  N    . ASP   A 1 155 ? 1.619   44.475 21.191  1.00 63.34  ? 155 ASP   A N    1 
ATOM   1193 C  CA   . ASP   A 1 155 ? 0.826   45.631 20.775  1.00 73.71  ? 155 ASP   A CA   1 
ATOM   1194 C  C    . ASP   A 1 155 ? 0.485   45.638 19.288  1.00 64.55  ? 155 ASP   A C    1 
ATOM   1195 O  O    . ASP   A 1 155 ? -0.420  46.365 18.859  1.00 62.59  ? 155 ASP   A O    1 
ATOM   1196 C  CB   . ASP   A 1 155 ? 1.559   46.929 21.126  1.00 70.92  ? 155 ASP   A CB   1 
ATOM   1197 C  CG   . ASP   A 1 155 ? 0.851   47.731 22.192  1.00 85.27  ? 155 ASP   A CG   1 
ATOM   1198 O  OD1  . ASP   A 1 155 ? -0.089  47.196 22.809  1.00 93.55  ? 155 ASP   A OD1  1 
ATOM   1199 O  OD2  . ASP   A 1 155 ? 1.217   48.907 22.381  1.00 90.41  ? 155 ASP   A OD2  1 
ATOM   1200 N  N    . CYS   A 1 156 ? 1.215   44.868 18.490  1.00 59.73  ? 156 CYS   A N    1 
ATOM   1201 C  CA   . CYS   A 1 156 ? 1.044   44.873 17.044  1.00 62.16  ? 156 CYS   A CA   1 
ATOM   1202 C  C    . CYS   A 1 156 ? 0.131   43.729 16.619  1.00 52.14  ? 156 CYS   A C    1 
ATOM   1203 O  O    . CYS   A 1 156 ? 0.396   42.565 16.933  1.00 50.81  ? 156 CYS   A O    1 
ATOM   1204 C  CB   . CYS   A 1 156 ? 2.397   44.769 16.342  1.00 53.25  ? 156 CYS   A CB   1 
ATOM   1205 S  SG   . CYS   A 1 156 ? 2.283   44.714 14.531  1.00 57.00  ? 156 CYS   A SG   1 
ATOM   1206 N  N    . VAL   A 1 157 ? -0.934  44.062 15.898  1.00 42.69  ? 157 VAL   A N    1 
ATOM   1207 C  CA   . VAL   A 1 157 ? -1.894  43.071 15.428  1.00 43.15  ? 157 VAL   A CA   1 
ATOM   1208 C  C    . VAL   A 1 157 ? -1.462  42.589 14.047  1.00 42.99  ? 157 VAL   A C    1 
ATOM   1209 O  O    . VAL   A 1 157 ? -1.457  43.358 13.082  1.00 41.28  ? 157 VAL   A O    1 
ATOM   1210 C  CB   . VAL   A 1 157 ? -3.316  43.639 15.387  1.00 42.86  ? 157 VAL   A CB   1 
ATOM   1211 C  CG1  . VAL   A 1 157 ? -4.268  42.594 14.817  1.00 35.16  ? 157 VAL   A CG1  1 
ATOM   1212 C  CG2  . VAL   A 1 157 ? -3.756  44.066 16.777  1.00 47.18  ? 157 VAL   A CG2  1 
ATOM   1213 N  N    . SER   A 1 158 ? -1.121  41.308 13.948  1.00 37.90  ? 158 SER   A N    1 
ATOM   1214 C  CA   . SER   A 1 158 ? -0.813  40.677 12.667  1.00 38.70  ? 158 SER   A CA   1 
ATOM   1215 C  C    . SER   A 1 158 ? -2.095  40.048 12.136  1.00 35.63  ? 158 SER   A C    1 
ATOM   1216 O  O    . SER   A 1 158 ? -2.494  38.966 12.574  1.00 33.67  ? 158 SER   A O    1 
ATOM   1217 C  CB   . SER   A 1 158 ? 0.291   39.638 12.827  1.00 33.37  ? 158 SER   A CB   1 
ATOM   1218 O  OG   . SER   A 1 158 ? 1.567   40.237 12.729  1.00 52.12  ? 158 SER   A OG   1 
ATOM   1219 N  N    . PHE   A 1 159 ? -2.757  40.732 11.204  1.00 35.63  ? 159 PHE   A N    1 
ATOM   1220 C  CA   . PHE   A 1 159 ? -3.920  40.154 10.542  1.00 34.09  ? 159 PHE   A CA   1 
ATOM   1221 C  C    . PHE   A 1 159 ? -3.472  39.115 9.528   1.00 42.37  ? 159 PHE   A C    1 
ATOM   1222 O  O    . PHE   A 1 159 ? -2.556  39.361 8.736   1.00 35.09  ? 159 PHE   A O    1 
ATOM   1223 C  CB   . PHE   A 1 159 ? -4.740  41.226 9.837   1.00 36.18  ? 159 PHE   A CB   1 
ATOM   1224 C  CG   . PHE   A 1 159 ? -5.352  42.218 10.760  1.00 34.64  ? 159 PHE   A CG   1 
ATOM   1225 C  CD1  . PHE   A 1 159 ? -6.520  41.920 11.440  1.00 31.76  ? 159 PHE   A CD1  1 
ATOM   1226 C  CD2  . PHE   A 1 159 ? -4.766  43.454 10.946  1.00 32.74  ? 159 PHE   A CD2  1 
ATOM   1227 C  CE1  . PHE   A 1 159 ? -7.091  42.843 12.294  1.00 28.56  ? 159 PHE   A CE1  1 
ATOM   1228 C  CE2  . PHE   A 1 159 ? -5.330  44.379 11.797  1.00 40.04  ? 159 PHE   A CE2  1 
ATOM   1229 C  CZ   . PHE   A 1 159 ? -6.495  44.072 12.474  1.00 35.32  ? 159 PHE   A CZ   1 
ATOM   1230 N  N    . CYS   A 1 160 ? -4.130  37.960 9.539   1.00 35.31  ? 160 CYS   A N    1 
ATOM   1231 C  CA   . CYS   A 1 160 ? -3.702  36.869 8.680   1.00 30.82  ? 160 CYS   A CA   1 
ATOM   1232 C  C    . CYS   A 1 160 ? -4.830  36.137 7.969   1.00 36.68  ? 160 CYS   A C    1 
ATOM   1233 O  O    . CYS   A 1 160 ? -4.533  35.306 7.108   1.00 40.25  ? 160 CYS   A O    1 
ATOM   1234 C  CB   . CYS   A 1 160 ? -2.890  35.855 9.498   1.00 35.20  ? 160 CYS   A CB   1 
ATOM   1235 S  SG   . CYS   A 1 160 ? -3.882  34.962 10.724  1.00 42.06  ? 160 CYS   A SG   1 
ATOM   1236 N  N    . TYR   A 1 161 ? -6.096  36.402 8.278   1.00 33.60  ? 161 TYR   A N    1 
ATOM   1237 C  CA   . TYR   A 1 161 ? -7.178  35.634 7.682   1.00 32.93  ? 161 TYR   A CA   1 
ATOM   1238 C  C    . TYR   A 1 161 ? -8.419  36.501 7.555   1.00 36.72  ? 161 TYR   A C    1 
ATOM   1239 O  O    . TYR   A 1 161 ? -8.755  37.255 8.472   1.00 39.17  ? 161 TYR   A O    1 
ATOM   1240 C  CB   . TYR   A 1 161 ? -7.492  34.387 8.514   1.00 30.06  ? 161 TYR   A CB   1 
ATOM   1241 C  CG   . TYR   A 1 161 ? -8.646  33.567 7.981   1.00 38.42  ? 161 TYR   A CG   1 
ATOM   1242 C  CD1  . TYR   A 1 161 ? -8.467  32.709 6.908   1.00 37.42  ? 161 TYR   A CD1  1 
ATOM   1243 C  CD2  . TYR   A 1 161 ? -9.907  33.640 8.559   1.00 36.09  ? 161 TYR   A CD2  1 
ATOM   1244 C  CE1  . TYR   A 1 161 ? -9.508  31.953 6.416   1.00 36.12  ? 161 TYR   A CE1  1 
ATOM   1245 C  CE2  . TYR   A 1 161 ? -10.958 32.881 8.076   1.00 28.48  ? 161 TYR   A CE2  1 
ATOM   1246 C  CZ   . TYR   A 1 161 ? -10.750 32.038 7.003   1.00 33.32  ? 161 TYR   A CZ   1 
ATOM   1247 O  OH   . TYR   A 1 161 ? -11.780 31.273 6.501   1.00 35.17  ? 161 TYR   A OH   1 
ATOM   1248 N  N    . MET   A 1 162 ? -9.097  36.388 6.415   1.00 37.15  ? 162 MET   A N    1 
ATOM   1249 C  CA   . MET   A 1 162 ? -10.403 37.006 6.224   1.00 39.91  ? 162 MET   A CA   1 
ATOM   1250 C  C    . MET   A 1 162 ? -11.353 35.917 5.755   1.00 40.89  ? 162 MET   A C    1 
ATOM   1251 O  O    . MET   A 1 162 ? -11.129 35.305 4.705   1.00 37.77  ? 162 MET   A O    1 
ATOM   1252 C  CB   . MET   A 1 162 ? -10.351 38.163 5.218   1.00 31.41  ? 162 MET   A CB   1 
ATOM   1253 C  CG   . MET   A 1 162 ? -11.721 38.755 4.883   1.00 34.01  ? 162 MET   A CG   1 
ATOM   1254 S  SD   . MET   A 1 162 ? -11.664 40.317 3.958   1.00 54.31  ? 162 MET   A SD   1 
ATOM   1255 C  CE   . MET   A 1 162 ? -11.195 41.467 5.248   1.00 44.98  ? 162 MET   A CE   1 
ATOM   1256 N  N    . HIS   A 1 163 ? -12.397 35.669 6.541   1.00 33.31  ? 163 HIS   A N    1 
ATOM   1257 C  CA   . HIS   A 1 163 ? -13.321 34.580 6.256   1.00 37.69  ? 163 HIS   A CA   1 
ATOM   1258 C  C    . HIS   A 1 163 ? -14.174 34.891 5.032   1.00 41.83  ? 163 HIS   A C    1 
ATOM   1259 O  O    . HIS   A 1 163 ? -14.645 36.016 4.854   1.00 38.68  ? 163 HIS   A O    1 
ATOM   1260 C  CB   . HIS   A 1 163 ? -14.212 34.327 7.468   1.00 35.97  ? 163 HIS   A CB   1 
ATOM   1261 C  CG   . HIS   A 1 163 ? -15.167 33.191 7.289   1.00 37.64  ? 163 HIS   A CG   1 
ATOM   1262 N  ND1  . HIS   A 1 163 ? -14.792 31.981 6.748   1.00 35.35  ? 163 HIS   A ND1  1 
ATOM   1263 C  CD2  . HIS   A 1 163 ? -16.484 33.080 7.584   1.00 41.07  ? 163 HIS   A CD2  1 
ATOM   1264 C  CE1  . HIS   A 1 163 ? -15.838 31.176 6.711   1.00 44.64  ? 163 HIS   A CE1  1 
ATOM   1265 N  NE2  . HIS   A 1 163 ? -16.876 31.817 7.216   1.00 46.54  ? 163 HIS   A NE2  1 
ATOM   1266 N  N    . HIS   A 1 164 ? -14.379 33.880 4.189   1.00 40.38  ? 164 HIS   A N    1 
ATOM   1267 C  CA   . HIS   A 1 164 ? -15.183 34.039 2.985   1.00 44.48  ? 164 HIS   A CA   1 
ATOM   1268 C  C    . HIS   A 1 164 ? -16.376 33.101 2.934   1.00 53.53  ? 164 HIS   A C    1 
ATOM   1269 O  O    . HIS   A 1 164 ? -17.501 33.560 2.703   1.00 51.69  ? 164 HIS   A O    1 
ATOM   1270 C  CB   . HIS   A 1 164 ? -14.322 33.841 1.728   1.00 45.71  ? 164 HIS   A CB   1 
ATOM   1271 C  CG   . HIS   A 1 164 ? -13.606 35.079 1.290   1.00 42.74  ? 164 HIS   A CG   1 
ATOM   1272 N  ND1  . HIS   A 1 164 ? -12.617 35.673 2.043   1.00 41.44  ? 164 HIS   A ND1  1 
ATOM   1273 C  CD2  . HIS   A 1 164 ? -13.756 35.853 0.189   1.00 41.56  ? 164 HIS   A CD2  1 
ATOM   1274 C  CE1  . HIS   A 1 164 ? -12.176 36.750 1.417   1.00 39.85  ? 164 HIS   A CE1  1 
ATOM   1275 N  NE2  . HIS   A 1 164 ? -12.853 36.883 0.290   1.00 45.06  ? 164 HIS   A NE2  1 
ATOM   1276 N  N    . MET   A 1 165 ? -16.178 31.801 3.143   1.00 47.66  ? 165 MET   A N    1 
ATOM   1277 C  CA   . MET   A 1 165 ? -17.237 30.869 2.781   1.00 54.88  ? 165 MET   A CA   1 
ATOM   1278 C  C    . MET   A 1 165 ? -17.117 29.588 3.589   1.00 44.34  ? 165 MET   A C    1 
ATOM   1279 O  O    . MET   A 1 165 ? -16.061 29.273 4.146   1.00 51.22  ? 165 MET   A O    1 
ATOM   1280 C  CB   . MET   A 1 165 ? -17.185 30.547 1.287   1.00 52.74  ? 165 MET   A CB   1 
ATOM   1281 C  CG   . MET   A 1 165 ? -15.933 29.785 0.914   1.00 50.99  ? 165 MET   A CG   1 
ATOM   1282 S  SD   . MET   A 1 165 ? -15.370 30.145 -0.749  1.00 66.70  ? 165 MET   A SD   1 
ATOM   1283 C  CE   . MET   A 1 165 ? -14.679 28.557 -1.206  1.00 57.74  ? 165 MET   A CE   1 
ATOM   1284 N  N    . GLU   A 1 166 ? -18.223 28.850 3.632   1.00 49.11  ? 166 GLU   A N    1 
ATOM   1285 C  CA   . GLU   A 1 166 ? -18.279 27.518 4.211   1.00 50.49  ? 166 GLU   A CA   1 
ATOM   1286 C  C    . GLU   A 1 166 ? -18.306 26.489 3.087   1.00 49.69  ? 166 GLU   A C    1 
ATOM   1287 O  O    . GLU   A 1 166 ? -18.826 26.747 1.999   1.00 50.37  ? 166 GLU   A O    1 
ATOM   1288 C  CB   . GLU   A 1 166 ? -19.518 27.357 5.096   1.00 46.88  ? 166 GLU   A CB   1 
ATOM   1289 C  CG   . GLU   A 1 166 ? -19.663 25.973 5.729   1.00 55.39  ? 166 GLU   A CG   1 
ATOM   1290 C  CD   . GLU   A 1 166 ? -20.669 25.941 6.873   1.00 65.08  ? 166 GLU   A CD   1 
ATOM   1291 O  OE1  . GLU   A 1 166 ? -21.842 25.583 6.623   1.00 78.42  ? 166 GLU   A OE1  1 
ATOM   1292 O  OE2  . GLU   A 1 166 ? -20.296 26.296 8.013   1.00 61.24  ? 166 GLU   A OE2  1 
ATOM   1293 N  N    . LEU   A 1 167 ? -17.740 25.326 3.352   1.00 53.14  ? 167 LEU   A N    1 
ATOM   1294 C  CA   . LEU   A 1 167 ? -17.685 24.287 2.337   1.00 51.74  ? 167 LEU   A CA   1 
ATOM   1295 C  C    . LEU   A 1 167 ? -18.706 23.199 2.622   1.00 54.77  ? 167 LEU   A C    1 
ATOM   1296 O  O    . LEU   A 1 167 ? -19.254 23.117 3.725   1.00 56.70  ? 167 LEU   A O    1 
ATOM   1297 C  CB   . LEU   A 1 167 ? -16.280 23.677 2.276   1.00 56.19  ? 167 LEU   A CB   1 
ATOM   1298 C  CG   . LEU   A 1 167 ? -15.180 24.635 1.817   1.00 59.47  ? 167 LEU   A CG   1 
ATOM   1299 C  CD1  . LEU   A 1 167 ? -13.850 23.906 1.723   1.00 56.03  ? 167 LEU   A CD1  1 
ATOM   1300 C  CD2  . LEU   A 1 167 ? -15.551 25.273 0.487   1.00 49.60  ? 167 LEU   A CD2  1 
ATOM   1301 N  N    . PRO   A 1 168 ? -18.999 22.346 1.639   1.00 56.31  ? 168 PRO   A N    1 
ATOM   1302 C  CA   . PRO   A 1 168 ? -19.987 21.282 1.873   1.00 52.30  ? 168 PRO   A CA   1 
ATOM   1303 C  C    . PRO   A 1 168 ? -19.651 20.392 3.058   1.00 57.49  ? 168 PRO   A C    1 
ATOM   1304 O  O    . PRO   A 1 168 ? -20.567 19.874 3.710   1.00 62.86  ? 168 PRO   A O    1 
ATOM   1305 C  CB   . PRO   A 1 168 ? -19.973 20.500 0.553   1.00 54.70  ? 168 PRO   A CB   1 
ATOM   1306 C  CG   . PRO   A 1 168 ? -19.556 21.508 -0.467  1.00 56.65  ? 168 PRO   A CG   1 
ATOM   1307 C  CD   . PRO   A 1 168 ? -18.557 22.395 0.235   1.00 58.96  ? 168 PRO   A CD   1 
ATOM   1308 N  N    . THR   A 1 169 ? -18.367 20.197 3.362   1.00 50.19  ? 169 THR   A N    1 
ATOM   1309 C  CA   . THR   A 1 169 ? -17.972 19.366 4.493   1.00 58.30  ? 169 THR   A CA   1 
ATOM   1310 C  C    . THR   A 1 169 ? -18.111 20.079 5.831   1.00 61.57  ? 169 THR   A C    1 
ATOM   1311 O  O    . THR   A 1 169 ? -17.849 19.466 6.871   1.00 64.40  ? 169 THR   A O    1 
ATOM   1312 C  CB   . THR   A 1 169 ? -16.525 18.885 4.329   1.00 48.83  ? 169 THR   A CB   1 
ATOM   1313 O  OG1  . THR   A 1 169 ? -15.666 20.009 4.096   1.00 56.97  ? 169 THR   A OG1  1 
ATOM   1314 C  CG2  . THR   A 1 169 ? -16.411 17.911 3.165   1.00 51.13  ? 169 THR   A CG2  1 
ATOM   1315 N  N    . GLY   A 1 170 ? -18.513 21.346 5.836   1.00 58.52  ? 170 GLY   A N    1 
ATOM   1316 C  CA   . GLY   A 1 170 ? -18.638 22.096 7.064   1.00 51.68  ? 170 GLY   A CA   1 
ATOM   1317 C  C    . GLY   A 1 170 ? -17.387 22.821 7.505   1.00 52.21  ? 170 GLY   A C    1 
ATOM   1318 O  O    . GLY   A 1 170 ? -17.390 23.417 8.589   1.00 51.31  ? 170 GLY   A O    1 
ATOM   1319 N  N    . VAL   A 1 171 ? -16.316 22.783 6.712   1.00 53.24  ? 171 VAL   A N    1 
ATOM   1320 C  CA   . VAL   A 1 171 ? -15.106 23.537 7.019   1.00 40.93  ? 171 VAL   A CA   1 
ATOM   1321 C  C    . VAL   A 1 171 ? -15.197 24.894 6.334   1.00 50.38  ? 171 VAL   A C    1 
ATOM   1322 O  O    . VAL   A 1 171 ? -16.109 25.140 5.538   1.00 47.98  ? 171 VAL   A O    1 
ATOM   1323 C  CB   . VAL   A 1 171 ? -13.838 22.777 6.591   1.00 51.32  ? 171 VAL   A CB   1 
ATOM   1324 C  CG1  . VAL   A 1 171 ? -13.787 21.410 7.261   1.00 52.01  ? 171 VAL   A CG1  1 
ATOM   1325 C  CG2  . VAL   A 1 171 ? -13.783 22.639 5.077   1.00 54.88  ? 171 VAL   A CG2  1 
ATOM   1326 N  N    . HIS   A 1 172 ? -14.250 25.776 6.630   1.00 43.32  ? 172 HIS   A N    1 
ATOM   1327 C  CA   . HIS   A 1 172 ? -14.307 27.162 6.200   1.00 45.90  ? 172 HIS   A CA   1 
ATOM   1328 C  C    . HIS   A 1 172 ? -13.061 27.529 5.404   1.00 42.52  ? 172 HIS   A C    1 
ATOM   1329 O  O    . HIS   A 1 172 ? -11.975 26.982 5.624   1.00 34.28  ? 172 HIS   A O    1 
ATOM   1330 C  CB   . HIS   A 1 172 ? -14.470 28.084 7.415   1.00 37.76  ? 172 HIS   A CB   1 
ATOM   1331 C  CG   . HIS   A 1 172 ? -15.678 27.769 8.239   1.00 50.81  ? 172 HIS   A CG   1 
ATOM   1332 N  ND1  . HIS   A 1 172 ? -15.612 27.054 9.415   1.00 41.16  ? 172 HIS   A ND1  1 
ATOM   1333 C  CD2  . HIS   A 1 172 ? -16.989 28.053 8.043   1.00 45.19  ? 172 HIS   A CD2  1 
ATOM   1334 C  CE1  . HIS   A 1 172 ? -16.828 26.920 9.915   1.00 45.10  ? 172 HIS   A CE1  1 
ATOM   1335 N  NE2  . HIS   A 1 172 ? -17.682 27.517 9.101   1.00 55.08  ? 172 HIS   A NE2  1 
ATOM   1336 N  N    . ALA   A 1 173 ? -13.231 28.461 4.469   1.00 41.38  ? 173 ALA   A N    1 
ATOM   1337 C  CA   . ALA   A 1 173 ? -12.147 28.896 3.605   1.00 35.91  ? 173 ALA   A CA   1 
ATOM   1338 C  C    . ALA   A 1 173 ? -12.128 30.415 3.537   1.00 40.58  ? 173 ALA   A C    1 
ATOM   1339 O  O    . ALA   A 1 173 ? -13.161 31.072 3.687   1.00 40.09  ? 173 ALA   A O    1 
ATOM   1340 C  CB   . ALA   A 1 173 ? -12.278 28.306 2.196   1.00 33.18  ? 173 ALA   A CB   1 
ATOM   1341 N  N    . GLY   A 1 174 ? -10.941 30.962 3.309   1.00 35.03  ? 174 GLY   A N    1 
ATOM   1342 C  CA   . GLY   A 1 174 ? -10.791 32.396 3.193   1.00 32.63  ? 174 GLY   A CA   1 
ATOM   1343 C  C    . GLY   A 1 174 ? -9.453  32.755 2.588   1.00 38.82  ? 174 GLY   A C    1 
ATOM   1344 O  O    . GLY   A 1 174 ? -8.762  31.912 2.011   1.00 36.13  ? 174 GLY   A O    1 
ATOM   1345 N  N    . THR   A 1 175 ? -9.091  34.029 2.740   1.00 30.83  ? 175 THR   A N    1 
ATOM   1346 C  CA   . THR   A 1 175 ? -7.892  34.592 2.137   1.00 34.80  ? 175 THR   A CA   1 
ATOM   1347 C  C    . THR   A 1 175 ? -7.075  35.332 3.184   1.00 39.49  ? 175 THR   A C    1 
ATOM   1348 O  O    . THR   A 1 175 ? -7.521  35.564 4.312   1.00 32.14  ? 175 THR   A O    1 
ATOM   1349 C  CB   . THR   A 1 175 ? -8.230  35.576 1.011   1.00 43.49  ? 175 THR   A CB   1 
ATOM   1350 O  OG1  . THR   A 1 175 ? -8.794  36.760 1.589   1.00 30.50  ? 175 THR   A OG1  1 
ATOM   1351 C  CG2  . THR   A 1 175 ? -9.227  34.965 0.029   1.00 38.33  ? 175 THR   A CG2  1 
ATOM   1352 N  N    . ASP   A 1 176 ? -5.872  35.733 2.780   1.00 31.47  ? 176 ASP   A N    1 
ATOM   1353 C  CA   . ASP   A 1 176 ? -5.105  36.678 3.573   1.00 35.71  ? 176 ASP   A CA   1 
ATOM   1354 C  C    . ASP   A 1 176 ? -5.614  38.093 3.297   1.00 40.29  ? 176 ASP   A C    1 
ATOM   1355 O  O    . ASP   A 1 176 ? -6.469  38.320 2.433   1.00 36.92  ? 176 ASP   A O    1 
ATOM   1356 C  CB   . ASP   A 1 176 ? -3.611  36.536 3.282   1.00 40.89  ? 176 ASP   A CB   1 
ATOM   1357 C  CG   . ASP   A 1 176 ? -3.264  36.776 1.819   1.00 38.85  ? 176 ASP   A CG   1 
ATOM   1358 O  OD1  . ASP   A 1 176 ? -3.920  37.616 1.163   1.00 46.03  ? 176 ASP   A OD1  1 
ATOM   1359 O  OD2  . ASP   A 1 176 ? -2.316  36.129 1.323   1.00 45.98  ? 176 ASP   A OD2  1 
ATOM   1360 N  N    . LEU   A 1 177 ? -5.084  39.065 4.033   1.00 37.11  ? 177 LEU   A N    1 
ATOM   1361 C  CA   . LEU   A 1 177 ? -5.588  40.424 3.890   1.00 38.53  ? 177 LEU   A CA   1 
ATOM   1362 C  C    . LEU   A 1 177 ? -5.190  41.071 2.570   1.00 43.72  ? 177 LEU   A C    1 
ATOM   1363 O  O    . LEU   A 1 177 ? -5.632  42.192 2.300   1.00 41.47  ? 177 LEU   A O    1 
ATOM   1364 C  CB   . LEU   A 1 177 ? -5.121  41.284 5.065   1.00 37.72  ? 177 LEU   A CB   1 
ATOM   1365 C  CG   . LEU   A 1 177 ? -6.098  41.310 6.245   1.00 39.85  ? 177 LEU   A CG   1 
ATOM   1366 C  CD1  . LEU   A 1 177 ? -7.314  42.163 5.926   1.00 50.07  ? 177 LEU   A CD1  1 
ATOM   1367 C  CD2  . LEU   A 1 177 ? -6.525  39.902 6.619   1.00 49.40  ? 177 LEU   A CD2  1 
ATOM   1368 N  N    . GLU   A 1 178 ? -4.379  40.400 1.754   1.00 48.04  ? 178 GLU   A N    1 
ATOM   1369 C  CA   . GLU   A 1 178 ? -4.045  40.849 0.409   1.00 38.47  ? 178 GLU   A CA   1 
ATOM   1370 C  C    . GLU   A 1 178 ? -5.034  40.353 -0.641  1.00 43.62  ? 178 GLU   A C    1 
ATOM   1371 O  O    . GLU   A 1 178 ? -4.882  40.685 -1.822  1.00 38.75  ? 178 GLU   A O    1 
ATOM   1372 C  CB   . GLU   A 1 178 ? -2.638  40.373 0.030   1.00 50.65  ? 178 GLU   A CB   1 
ATOM   1373 C  CG   . GLU   A 1 178 ? -1.529  40.904 0.920   1.00 60.14  ? 178 GLU   A CG   1 
ATOM   1374 C  CD   . GLU   A 1 178 ? -1.499  42.418 0.986   1.00 67.55  ? 178 GLU   A CD   1 
ATOM   1375 O  OE1  . GLU   A 1 178 ? -0.811  42.956 1.879   1.00 70.93  ? 178 GLU   A OE1  1 
ATOM   1376 O  OE2  . GLU   A 1 178 ? -2.143  43.070 0.135   1.00 65.96  ? 178 GLU   A OE2  1 
ATOM   1377 N  N    . GLY   A 1 179 ? -6.026  39.556 -0.248  1.00 33.68  ? 179 GLY   A N    1 
ATOM   1378 C  CA   . GLY   A 1 179 ? -6.988  39.001 -1.179  1.00 41.45  ? 179 GLY   A CA   1 
ATOM   1379 C  C    . GLY   A 1 179 ? -6.607  37.672 -1.799  1.00 45.40  ? 179 GLY   A C    1 
ATOM   1380 O  O    . GLY   A 1 179 ? -7.352  37.168 -2.650  1.00 41.39  ? 179 GLY   A O    1 
ATOM   1381 N  N    . ASN   A 1 180 ? -5.483  37.083 -1.404  1.00 40.31  ? 180 ASN   A N    1 
ATOM   1382 C  CA   . ASN   A 1 180 ? -5.033  35.822 -1.979  1.00 39.13  ? 180 ASN   A CA   1 
ATOM   1383 C  C    . ASN   A 1 180 ? -5.574  34.669 -1.141  1.00 33.66  ? 180 ASN   A C    1 
ATOM   1384 O  O    . ASN   A 1 180 ? -5.267  34.563 0.051   1.00 36.67  ? 180 ASN   A O    1 
ATOM   1385 C  CB   . ASN   A 1 180 ? -3.509  35.785 -2.056  1.00 38.83  ? 180 ASN   A CB   1 
ATOM   1386 C  CG   . ASN   A 1 180 ? -2.938  36.970 -2.815  1.00 43.07  ? 180 ASN   A CG   1 
ATOM   1387 O  OD1  . ASN   A 1 180 ? -3.093  37.071 -4.029  1.00 48.70  ? 180 ASN   A OD1  1 
ATOM   1388 N  ND2  . ASN   A 1 180 ? -2.289  37.880 -2.099  1.00 45.81  ? 180 ASN   A ND2  1 
ATOM   1389 N  N    . PHE   A 1 181 ? -6.374  33.811 -1.767  1.00 31.39  ? 181 PHE   A N    1 
ATOM   1390 C  CA   . PHE   A 1 181 ? -7.023  32.720 -1.054  1.00 35.20  ? 181 PHE   A CA   1 
ATOM   1391 C  C    . PHE   A 1 181 ? -5.999  31.784 -0.420  1.00 36.53  ? 181 PHE   A C    1 
ATOM   1392 O  O    . PHE   A 1 181 ? -4.872  31.634 -0.898  1.00 31.81  ? 181 PHE   A O    1 
ATOM   1393 C  CB   . PHE   A 1 181 ? -7.925  31.926 -2.006  1.00 32.31  ? 181 PHE   A CB   1 
ATOM   1394 C  CG   . PHE   A 1 181 ? -9.386  32.208 -1.824  1.00 36.15  ? 181 PHE   A CG   1 
ATOM   1395 C  CD1  . PHE   A 1 181 ? -10.105 31.605 -0.805  1.00 32.03  ? 181 PHE   A CD1  1 
ATOM   1396 C  CD2  . PHE   A 1 181 ? -10.035 33.109 -2.656  1.00 38.77  ? 181 PHE   A CD2  1 
ATOM   1397 C  CE1  . PHE   A 1 181 ? -11.450 31.878 -0.631  1.00 35.97  ? 181 PHE   A CE1  1 
ATOM   1398 C  CE2  . PHE   A 1 181 ? -11.375 33.389 -2.485  1.00 37.54  ? 181 PHE   A CE2  1 
ATOM   1399 C  CZ   . PHE   A 1 181 ? -12.085 32.771 -1.472  1.00 42.45  ? 181 PHE   A CZ   1 
ATOM   1400 N  N    . TYR   A 1 182 ? -6.405  31.155 0.676   1.00 35.55  ? 182 TYR   A N    1 
ATOM   1401 C  CA   . TYR   A 1 182 ? -5.681  30.020 1.229   1.00 30.87  ? 182 TYR   A CA   1 
ATOM   1402 C  C    . TYR   A 1 182 ? -6.203  28.754 0.552   1.00 33.29  ? 182 TYR   A C    1 
ATOM   1403 O  O    . TYR   A 1 182 ? -7.391  28.432 0.662   1.00 38.95  ? 182 TYR   A O    1 
ATOM   1404 C  CB   . TYR   A 1 182 ? -5.860  29.944 2.745   1.00 38.29  ? 182 TYR   A CB   1 
ATOM   1405 C  CG   . TYR   A 1 182 ? -5.055  30.957 3.547   1.00 37.77  ? 182 TYR   A CG   1 
ATOM   1406 C  CD1  . TYR   A 1 182 ? -3.681  30.806 3.717   1.00 34.35  ? 182 TYR   A CD1  1 
ATOM   1407 C  CD2  . TYR   A 1 182 ? -5.674  32.046 4.160   1.00 37.48  ? 182 TYR   A CD2  1 
ATOM   1408 C  CE1  . TYR   A 1 182 ? -2.943  31.716 4.463   1.00 36.07  ? 182 TYR   A CE1  1 
ATOM   1409 C  CE2  . TYR   A 1 182 ? -4.940  32.964 4.910   1.00 36.59  ? 182 TYR   A CE2  1 
ATOM   1410 C  CZ   . TYR   A 1 182 ? -3.575  32.793 5.055   1.00 43.80  ? 182 TYR   A CZ   1 
ATOM   1411 O  OH   . TYR   A 1 182 ? -2.837  33.699 5.792   1.00 36.35  ? 182 TYR   A OH   1 
ATOM   1412 N  N    . GLY   A 1 183 ? -5.330  28.055 -0.168  1.00 34.38  ? 183 GLY   A N    1 
ATOM   1413 C  CA   . GLY   A 1 183 ? -5.713  26.830 -0.834  1.00 38.24  ? 183 GLY   A CA   1 
ATOM   1414 C  C    . GLY   A 1 183 ? -6.341  27.059 -2.195  1.00 45.73  ? 183 GLY   A C    1 
ATOM   1415 O  O    . GLY   A 1 183 ? -6.428  28.190 -2.683  1.00 36.39  ? 183 GLY   A O    1 
ATOM   1416 N  N    . PRO   A 1 184 ? -6.813  25.974 -2.838  1.00 42.76  ? 184 PRO   A N    1 
ATOM   1417 C  CA   . PRO   A 1 184 ? -7.286  26.041 -4.223  1.00 45.94  ? 184 PRO   A CA   1 
ATOM   1418 C  C    . PRO   A 1 184 ? -8.764  26.407 -4.349  1.00 50.69  ? 184 PRO   A C    1 
ATOM   1419 O  O    . PRO   A 1 184 ? -9.529  25.753 -5.063  1.00 60.55  ? 184 PRO   A O    1 
ATOM   1420 C  CB   . PRO   A 1 184 ? -7.026  24.620 -4.735  1.00 39.62  ? 184 PRO   A CB   1 
ATOM   1421 C  CG   . PRO   A 1 184 ? -7.274  23.766 -3.509  1.00 40.57  ? 184 PRO   A CG   1 
ATOM   1422 C  CD   . PRO   A 1 184 ? -6.922  24.610 -2.292  1.00 42.30  ? 184 PRO   A CD   1 
ATOM   1423 N  N    . PHE   A 1 185 ? -9.178  27.459 -3.650  1.00 47.85  ? 185 PHE   A N    1 
ATOM   1424 C  CA   . PHE   A 1 185 ? -10.567 27.890 -3.651  1.00 43.84  ? 185 PHE   A CA   1 
ATOM   1425 C  C    . PHE   A 1 185 ? -10.714 29.233 -4.352  1.00 47.16  ? 185 PHE   A C    1 
ATOM   1426 O  O    . PHE   A 1 185 ? -9.753  29.991 -4.510  1.00 41.97  ? 185 PHE   A O    1 
ATOM   1427 C  CB   . PHE   A 1 185 ? -11.108 27.973 -2.221  1.00 44.00  ? 185 PHE   A CB   1 
ATOM   1428 C  CG   . PHE   A 1 185 ? -10.831 26.745 -1.412  1.00 50.84  ? 185 PHE   A CG   1 
ATOM   1429 C  CD1  . PHE   A 1 185 ? -11.457 25.546 -1.713  1.00 43.81  ? 185 PHE   A CD1  1 
ATOM   1430 C  CD2  . PHE   A 1 185 ? -9.920  26.778 -0.372  1.00 38.10  ? 185 PHE   A CD2  1 
ATOM   1431 C  CE1  . PHE   A 1 185 ? -11.194 24.409 -0.976  1.00 45.77  ? 185 PHE   A CE1  1 
ATOM   1432 C  CE2  . PHE   A 1 185 ? -9.651  25.644 0.365   1.00 45.14  ? 185 PHE   A CE2  1 
ATOM   1433 C  CZ   . PHE   A 1 185 ? -10.286 24.457 0.062   1.00 39.97  ? 185 PHE   A CZ   1 
ATOM   1434 N  N    . VAL   A 1 186 ? -11.943 29.512 -4.788  1.00 47.34  ? 186 VAL   A N    1 
ATOM   1435 C  CA   . VAL   A 1 186 ? -12.282 30.773 -5.432  1.00 48.16  ? 186 VAL   A CA   1 
ATOM   1436 C  C    . VAL   A 1 186 ? -13.574 31.297 -4.825  1.00 50.95  ? 186 VAL   A C    1 
ATOM   1437 O  O    . VAL   A 1 186 ? -14.353 30.554 -4.223  1.00 45.58  ? 186 VAL   A O    1 
ATOM   1438 C  CB   . VAL   A 1 186 ? -12.427 30.636 -6.965  1.00 51.24  ? 186 VAL   A CB   1 
ATOM   1439 C  CG1  . VAL   A 1 186 ? -11.103 30.229 -7.587  1.00 42.00  ? 186 VAL   A CG1  1 
ATOM   1440 C  CG2  . VAL   A 1 186 ? -13.522 29.637 -7.312  1.00 47.27  ? 186 VAL   A CG2  1 
ATOM   1441 N  N    . ASP   A 1 187 ? -13.850 32.577 -5.155  1.00 45.87  ? 187 ASP   A N    1 
ATOM   1442 C  CA   . ASP   A 1 187 ? -15.098 33.271 -4.760  1.00 51.58  ? 187 ASP   A CA   1 
ATOM   1443 C  C    . ASP   A 1 187 ? -16.251 33.165 -5.781  1.00 55.03  ? 187 ASP   A C    1 
ATOM   1444 O  O    . ASP   A 1 187 ? -16.428 34.056 -6.564  1.00 45.98  ? 187 ASP   A O    1 
ATOM   1445 C  CB   . ASP   A 1 187 ? -14.860 34.685 -4.207  1.00 44.79  ? 187 ASP   A CB   1 
ATOM   1446 C  CG   . ASP   A 1 187 ? -13.890 35.507 -5.017  1.00 53.75  ? 187 ASP   A CG   1 
ATOM   1447 O  OD1  . ASP   A 1 187 ? -13.511 35.140 -6.142  1.00 55.26  ? 187 ASP   A OD1  1 
ATOM   1448 O  OD2  . ASP   A 1 187 ? -13.520 36.570 -4.506  1.00 54.82  ? 187 ASP   A OD2  1 
ATOM   1449 N  N    . ARG   A 1 188 ? -16.844 31.980 -5.802  1.00 48.17  ? 188 ARG   A N    1 
ATOM   1450 C  CA   . ARG   A 1 188 ? -17.955 31.717 -6.680  1.00 67.21  ? 188 ARG   A CA   1 
ATOM   1451 C  C    . ARG   A 1 188 ? -18.814 30.791 -5.864  1.00 73.74  ? 188 ARG   A C    1 
ATOM   1452 O  O    . ARG   A 1 188 ? -18.280 29.915 -5.203  1.00 68.23  ? 188 ARG   A O    1 
ATOM   1453 C  CB   . ARG   A 1 188 ? -17.527 31.025 -7.962  1.00 30.00  ? 188 ARG   A CB   1 
ATOM   1454 C  CG   . ARG   A 1 188 ? -16.974 31.949 -9.025  1.00 30.00  ? 188 ARG   A CG   1 
ATOM   1455 C  CD   . ARG   A 1 188 ? -16.631 31.176 -10.280 1.00 30.00  ? 188 ARG   A CD   1 
ATOM   1456 N  NE   . ARG   A 1 188 ? -17.827 30.641 -10.919 1.00 30.00  ? 188 ARG   A NE   1 
ATOM   1457 C  CZ   . ARG   A 1 188 ? -17.952 29.386 -11.332 1.00 30.00  ? 188 ARG   A CZ   1 
ATOM   1458 N  NH1  . ARG   A 1 188 ? -16.955 28.530 -11.168 1.00 30.00  ? 188 ARG   A NH1  1 
ATOM   1459 N  NH2  . ARG   A 1 188 ? -19.076 28.985 -11.906 1.00 30.00  ? 188 ARG   A NH2  1 
ATOM   1460 N  N    . GLN   A 1 189 ? -20.114 30.995 -5.884  1.00 81.54  ? 189 GLN   A N    1 
ATOM   1461 C  CA   . GLN   A 1 189 ? -21.111 30.195 -5.124  1.00 77.53  ? 189 GLN   A CA   1 
ATOM   1462 C  C    . GLN   A 1 189 ? -21.299 28.822 -5.764  1.00 79.43  ? 189 GLN   A C    1 
ATOM   1463 O  O    . GLN   A 1 189 ? -22.452 28.404 -5.916  1.00 85.55  ? 189 GLN   A O    1 
ATOM   1464 C  CB   . GLN   A 1 189 ? -22.430 30.958 -4.991  1.00 84.49  ? 189 GLN   A CB   1 
ATOM   1465 C  CG   . GLN   A 1 189 ? -23.345 30.392 -3.917  1.00 87.41  ? 189 GLN   A CG   1 
ATOM   1466 C  CD   . GLN   A 1 189 ? -24.327 31.415 -3.405  1.00 88.96  ? 189 GLN   A CD   1 
ATOM   1467 O  OE1  . GLN   A 1 189 ? -24.789 32.282 -4.142  1.00 84.41  ? 189 GLN   A OE1  1 
ATOM   1468 N  NE2  . GLN   A 1 189 ? -24.654 31.319 -2.128  1.00 90.83  ? 189 GLN   A NE2  1 
ATOM   1469 N  N    . THR   A 1 190 ? -20.210 28.161 -6.137  1.00 83.18  ? 190 THR   A N    1 
ATOM   1470 C  CA   . THR   A 1 190 ? -20.288 26.794 -6.622  1.00 84.29  ? 190 THR   A CA   1 
ATOM   1471 C  C    . THR   A 1 190 ? -19.730 25.865 -5.554  1.00 87.60  ? 190 THR   A C    1 
ATOM   1472 O  O    . THR   A 1 190 ? -18.978 26.284 -4.669  1.00 81.90  ? 190 THR   A O    1 
ATOM   1473 C  CB   . THR   A 1 190 ? -19.519 26.615 -7.941  1.00 81.09  ? 190 THR   A CB   1 
ATOM   1474 O  OG1  . THR   A 1 190 ? -18.142 26.323 -7.659  1.00 83.60  ? 190 THR   A OG1  1 
ATOM   1475 C  CG2  . THR   A 1 190 ? -19.607 27.885 -8.773  1.00 80.67  ? 190 THR   A CG2  1 
ATOM   1476 N  N    . ALA   A 1 191 ? -20.119 24.596 -5.632  1.00 86.48  ? 191 ALA   A N    1 
ATOM   1477 C  CA   . ALA   A 1 191 ? -19.650 23.613 -4.666  1.00 75.43  ? 191 ALA   A CA   1 
ATOM   1478 C  C    . ALA   A 1 191 ? -18.182 23.299 -4.924  1.00 72.56  ? 191 ALA   A C    1 
ATOM   1479 O  O    . ALA   A 1 191 ? -17.820 22.837 -6.011  1.00 77.96  ? 191 ALA   A O    1 
ATOM   1480 C  CB   . ALA   A 1 191 ? -20.497 22.344 -4.743  1.00 71.22  ? 191 ALA   A CB   1 
ATOM   1481 N  N    . GLN   A 1 192 ? -17.335 23.563 -3.935  1.00 66.74  ? 192 GLN   A N    1 
ATOM   1482 C  CA   . GLN   A 1 192 ? -15.924 23.215 -4.001  1.00 59.84  ? 192 GLN   A CA   1 
ATOM   1483 C  C    . GLN   A 1 192 ? -15.577 22.334 -2.814  1.00 63.50  ? 192 GLN   A C    1 
ATOM   1484 O  O    . GLN   A 1 192 ? -16.101 22.524 -1.712  1.00 74.56  ? 192 GLN   A O    1 
ATOM   1485 C  CB   . GLN   A 1 192 ? -15.023 24.457 -4.008  1.00 52.92  ? 192 GLN   A CB   1 
ATOM   1486 C  CG   . GLN   A 1 192 ? -15.600 25.644 -4.746  1.00 62.50  ? 192 GLN   A CG   1 
ATOM   1487 C  CD   . GLN   A 1 192 ? -14.817 26.913 -4.492  1.00 59.00  ? 192 GLN   A CD   1 
ATOM   1488 O  OE1  . GLN   A 1 192 ? -13.594 26.938 -4.633  1.00 57.22  ? 192 GLN   A OE1  1 
ATOM   1489 N  NE2  . GLN   A 1 192 ? -15.518 27.980 -4.125  1.00 57.66  ? 192 GLN   A NE2  1 
ATOM   1490 N  N    . ALA   A 1 193 ? -14.690 21.375 -3.041  1.00 61.39  ? 193 ALA   A N    1 
ATOM   1491 C  CA   . ALA   A 1 193 ? -14.315 20.412 -2.022  1.00 61.01  ? 193 ALA   A CA   1 
ATOM   1492 C  C    . ALA   A 1 193 ? -12.867 20.622 -1.602  1.00 59.00  ? 193 ALA   A C    1 
ATOM   1493 O  O    . ALA   A 1 193 ? -12.017 21.022 -2.403  1.00 58.46  ? 193 ALA   A O    1 
ATOM   1494 C  CB   . ALA   A 1 193 ? -14.516 18.979 -2.521  1.00 46.80  ? 193 ALA   A CB   1 
ATOM   1495 N  N    . ALA   A 1 194 ? -12.597 20.356 -0.331  1.00 63.84  ? 194 ALA   A N    1 
ATOM   1496 C  CA   . ALA   A 1 194 ? -11.239 20.424 0.178   1.00 53.65  ? 194 ALA   A CA   1 
ATOM   1497 C  C    . ALA   A 1 194 ? -10.499 19.124 -0.110  1.00 55.18  ? 194 ALA   A C    1 
ATOM   1498 O  O    . ALA   A 1 194 ? -11.091 18.041 -0.152  1.00 51.59  ? 194 ALA   A O    1 
ATOM   1499 C  CB   . ALA   A 1 194 ? -11.244 20.701 1.681   1.00 50.64  ? 194 ALA   A CB   1 
ATOM   1500 N  N    . GLY   A 1 195 ? -9.194  19.242 -0.329  1.00 50.33  ? 195 GLY   A N    1 
ATOM   1501 C  CA   . GLY   A 1 195 ? -8.351  18.067 -0.411  1.00 54.38  ? 195 GLY   A CA   1 
ATOM   1502 C  C    . GLY   A 1 195 ? -8.357  17.289 0.893   1.00 56.55  ? 195 GLY   A C    1 
ATOM   1503 O  O    . GLY   A 1 195 ? -8.875  17.727 1.921   1.00 56.73  ? 195 GLY   A O    1 
ATOM   1504 N  N    . THR   A 1 196 ? -7.773  16.095 0.844   1.00 56.24  ? 196 THR   A N    1 
ATOM   1505 C  CA   . THR   A 1 196 ? -7.678  15.273 2.044   1.00 65.71  ? 196 THR   A CA   1 
ATOM   1506 C  C    . THR   A 1 196 ? -6.786  15.959 3.075   1.00 57.15  ? 196 THR   A C    1 
ATOM   1507 O  O    . THR   A 1 196 ? -5.776  16.578 2.731   1.00 58.58  ? 196 THR   A O    1 
ATOM   1508 C  CB   . THR   A 1 196 ? -7.128  13.885 1.709   1.00 68.08  ? 196 THR   A CB   1 
ATOM   1509 O  OG1  . THR   A 1 196 ? -5.903  14.019 0.979   1.00 69.64  ? 196 THR   A OG1  1 
ATOM   1510 C  CG2  . THR   A 1 196 ? -8.130  13.097 0.864   1.00 54.49  ? 196 THR   A CG2  1 
ATOM   1511 N  N    . ASP   A 1 197 ? -7.167  15.854 4.344   1.00 57.33  ? 197 ASP   A N    1 
ATOM   1512 C  CA   . ASP   A 1 197 ? -6.439  16.507 5.421   1.00 60.07  ? 197 ASP   A CA   1 
ATOM   1513 C  C    . ASP   A 1 197 ? -5.486  15.535 6.111   1.00 57.95  ? 197 ASP   A C    1 
ATOM   1514 O  O    . ASP   A 1 197 ? -5.637  14.313 6.038   1.00 54.35  ? 197 ASP   A O    1 
ATOM   1515 C  CB   . ASP   A 1 197 ? -7.406  17.108 6.446   1.00 58.37  ? 197 ASP   A CB   1 
ATOM   1516 C  CG   . ASP   A 1 197 ? -6.769  18.216 7.271   1.00 60.40  ? 197 ASP   A CG   1 
ATOM   1517 O  OD1  . ASP   A 1 197 ? -5.804  18.849 6.782   1.00 52.85  ? 197 ASP   A OD1  1 
ATOM   1518 O  OD2  . ASP   A 1 197 ? -7.235  18.458 8.406   1.00 55.17  ? 197 ASP   A OD2  1 
ATOM   1519 N  N    . THR   A 1 198 ? -4.496  16.106 6.793   1.00 54.59  ? 198 THR   A N    1 
ATOM   1520 C  CA   . THR   A 1 198 ? -3.475  15.358 7.508   1.00 51.59  ? 198 THR   A CA   1 
ATOM   1521 C  C    . THR   A 1 198 ? -3.367  15.899 8.927   1.00 52.43  ? 198 THR   A C    1 
ATOM   1522 O  O    . THR   A 1 198 ? -3.913  16.955 9.258   1.00 48.85  ? 198 THR   A O    1 
ATOM   1523 C  CB   . THR   A 1 198 ? -2.115  15.447 6.797   1.00 54.55  ? 198 THR   A CB   1 
ATOM   1524 O  OG1  . THR   A 1 198 ? -2.265  15.057 5.428   1.00 63.55  ? 198 THR   A OG1  1 
ATOM   1525 C  CG2  . THR   A 1 198 ? -1.096  14.530 7.458   1.00 61.27  ? 198 THR   A CG2  1 
ATOM   1526 N  N    . THR   A 1 199 ? -2.652  15.166 9.771   1.00 44.42  ? 199 THR   A N    1 
ATOM   1527 C  CA   . THR   A 1 199 ? -2.417  15.570 11.148  1.00 42.73  ? 199 THR   A CA   1 
ATOM   1528 C  C    . THR   A 1 199 ? -1.075  16.286 11.243  1.00 42.55  ? 199 THR   A C    1 
ATOM   1529 O  O    . THR   A 1 199 ? -0.082  15.839 10.657  1.00 44.00  ? 199 THR   A O    1 
ATOM   1530 C  CB   . THR   A 1 199 ? -2.457  14.358 12.079  1.00 51.84  ? 199 THR   A CB   1 
ATOM   1531 O  OG1  . THR   A 1 199 ? -3.722  13.700 11.937  1.00 43.70  ? 199 THR   A OG1  1 
ATOM   1532 C  CG2  . THR   A 1 199 ? -2.282  14.787 13.527  1.00 44.51  ? 199 THR   A CG2  1 
ATOM   1533 N  N    . ILE   A 1 200 ? -1.053  17.401 11.971  1.00 37.53  ? 200 ILE   A N    1 
ATOM   1534 C  CA   . ILE   A 1 200 ? 0.146   18.226 12.107  1.00 47.27  ? 200 ILE   A CA   1 
ATOM   1535 C  C    . ILE   A 1 200 ? 1.030   17.575 13.169  1.00 43.41  ? 200 ILE   A C    1 
ATOM   1536 O  O    . ILE   A 1 200 ? 0.827   17.766 14.369  1.00 34.95  ? 200 ILE   A O    1 
ATOM   1537 C  CB   . ILE   A 1 200 ? -0.197  19.676 12.458  1.00 46.15  ? 200 ILE   A CB   1 
ATOM   1538 C  CG1  . ILE   A 1 200 ? -1.281  20.203 11.513  1.00 44.24  ? 200 ILE   A CG1  1 
ATOM   1539 C  CG2  . ILE   A 1 200 ? 1.046   20.556 12.371  1.00 36.73  ? 200 ILE   A CG2  1 
ATOM   1540 C  CD1  . ILE   A 1 200 ? -2.241  21.192 12.153  1.00 43.24  ? 200 ILE   A CD1  1 
ATOM   1541 N  N    . THR   A 1 201 ? 2.025   16.804 12.724  1.00 38.89  ? 201 THR   A N    1 
ATOM   1542 C  CA   . THR   A 1 201 ? 2.834   16.018 13.651  1.00 40.18  ? 201 THR   A CA   1 
ATOM   1543 C  C    . THR   A 1 201 ? 3.515   16.904 14.687  1.00 41.30  ? 201 THR   A C    1 
ATOM   1544 O  O    . THR   A 1 201 ? 3.412   16.660 15.895  1.00 37.47  ? 201 THR   A O    1 
ATOM   1545 C  CB   . THR   A 1 201 ? 3.875   15.209 12.879  1.00 49.37  ? 201 THR   A CB   1 
ATOM   1546 O  OG1  . THR   A 1 201 ? 3.239   14.529 11.790  1.00 46.53  ? 201 THR   A OG1  1 
ATOM   1547 C  CG2  . THR   A 1 201 ? 4.538   14.186 13.792  1.00 40.46  ? 201 THR   A CG2  1 
ATOM   1548 N  N    . VAL   A 1 202 ? 4.230   17.935 14.231  1.00 37.50  ? 202 VAL   A N    1 
ATOM   1549 C  CA   . VAL   A 1 202 ? 4.974   18.782 15.159  1.00 43.09  ? 202 VAL   A CA   1 
ATOM   1550 C  C    . VAL   A 1 202 ? 4.054   19.328 16.241  1.00 41.78  ? 202 VAL   A C    1 
ATOM   1551 O  O    . VAL   A 1 202 ? 4.434   19.420 17.413  1.00 43.64  ? 202 VAL   A O    1 
ATOM   1552 C  CB   . VAL   A 1 202 ? 5.687   19.915 14.398  1.00 51.55  ? 202 VAL   A CB   1 
ATOM   1553 C  CG1  . VAL   A 1 202 ? 4.671   20.902 13.837  1.00 45.85  ? 202 VAL   A CG1  1 
ATOM   1554 C  CG2  . VAL   A 1 202 ? 6.673   20.616 15.313  1.00 56.27  ? 202 VAL   A CG2  1 
ATOM   1555 N  N    . ASN   A 1 203 ? 2.824   19.692 15.872  1.00 43.20  ? 203 ASN   A N    1 
ATOM   1556 C  CA   . ASN   A 1 203 ? 1.891   20.210 16.866  1.00 39.50  ? 203 ASN   A CA   1 
ATOM   1557 C  C    . ASN   A 1 203 ? 1.549   19.148 17.902  1.00 38.03  ? 203 ASN   A C    1 
ATOM   1558 O  O    . ASN   A 1 203 ? 1.430   19.450 19.095  1.00 28.57  ? 203 ASN   A O    1 
ATOM   1559 C  CB   . ASN   A 1 203 ? 0.621   20.720 16.185  1.00 36.44  ? 203 ASN   A CB   1 
ATOM   1560 C  CG   . ASN   A 1 203 ? 0.818   22.071 15.529  1.00 45.34  ? 203 ASN   A CG   1 
ATOM   1561 O  OD1  . ASN   A 1 203 ? 1.928   22.605 15.511  1.00 40.86  ? 203 ASN   A OD1  1 
ATOM   1562 N  ND2  . ASN   A 1 203 ? -0.256  22.627 14.975  1.00 35.15  ? 203 ASN   A ND2  1 
ATOM   1563 N  N    . VAL   A 1 204 ? 1.369   17.899 17.464  1.00 35.42  ? 204 VAL   A N    1 
ATOM   1564 C  CA   . VAL   A 1 204 ? 1.087   16.821 18.407  1.00 31.70  ? 204 VAL   A CA   1 
ATOM   1565 C  C    . VAL   A 1 204 ? 2.207   16.720 19.435  1.00 36.67  ? 204 VAL   A C    1 
ATOM   1566 O  O    . VAL   A 1 204 ? 1.966   16.726 20.648  1.00 35.28  ? 204 VAL   A O    1 
ATOM   1567 C  CB   . VAL   A 1 204 ? 0.884   15.488 17.662  1.00 44.16  ? 204 VAL   A CB   1 
ATOM   1568 C  CG1  . VAL   A 1 204 ? 0.790   14.335 18.654  1.00 35.88  ? 204 VAL   A CG1  1 
ATOM   1569 C  CG2  . VAL   A 1 204 ? -0.359  15.541 16.775  1.00 33.04  ? 204 VAL   A CG2  1 
ATOM   1570 N  N    . LEU   A 1 205 ? 3.454   16.643 18.963  1.00 35.07  ? 205 LEU   A N    1 
ATOM   1571 C  CA   . LEU   A 1 205 ? 4.579   16.545 19.886  1.00 44.87  ? 205 LEU   A CA   1 
ATOM   1572 C  C    . LEU   A 1 205 ? 4.611   17.728 20.846  1.00 40.12  ? 205 LEU   A C    1 
ATOM   1573 O  O    . LEU   A 1 205 ? 4.873   17.557 22.042  1.00 32.22  ? 205 LEU   A O    1 
ATOM   1574 C  CB   . LEU   A 1 205 ? 5.897   16.435 19.114  1.00 34.13  ? 205 LEU   A CB   1 
ATOM   1575 C  CG   . LEU   A 1 205 ? 6.082   15.207 18.217  1.00 35.89  ? 205 LEU   A CG   1 
ATOM   1576 C  CD1  . LEU   A 1 205 ? 7.253   15.408 17.268  1.00 37.49  ? 205 LEU   A CD1  1 
ATOM   1577 C  CD2  . LEU   A 1 205 ? 6.251   13.923 19.038  1.00 40.27  ? 205 LEU   A CD2  1 
ATOM   1578 N  N    . ALA   A 1 206 ? 4.353   18.939 20.344  1.00 33.13  ? 206 ALA   A N    1 
ATOM   1579 C  CA   . ALA   A 1 206 ? 4.326   20.097 21.230  1.00 34.25  ? 206 ALA   A CA   1 
ATOM   1580 C  C    . ALA   A 1 206 ? 3.268   19.924 22.312  1.00 36.72  ? 206 ALA   A C    1 
ATOM   1581 O  O    . ALA   A 1 206 ? 3.495   20.261 23.480  1.00 35.25  ? 206 ALA   A O    1 
ATOM   1582 C  CB   . ALA   A 1 206 ? 4.078   21.374 20.427  1.00 34.89  ? 206 ALA   A CB   1 
ATOM   1583 N  N    . TRP   A 1 207 ? 2.110   19.385 21.940  1.00 30.23  ? 207 TRP   A N    1 
ATOM   1584 C  CA   . TRP   A 1 207 ? 1.057   19.130 22.912  1.00 31.97  ? 207 TRP   A CA   1 
ATOM   1585 C  C    . TRP   A 1 207 ? 1.482   18.063 23.918  1.00 42.62  ? 207 TRP   A C    1 
ATOM   1586 O  O    . TRP   A 1 207 ? 1.178   18.169 25.111  1.00 34.54  ? 207 TRP   A O    1 
ATOM   1587 C  CB   . TRP   A 1 207 ? -0.212  18.734 22.164  1.00 36.78  ? 207 TRP   A CB   1 
ATOM   1588 C  CG   . TRP   A 1 207 ? -1.366  18.334 22.992  1.00 30.47  ? 207 TRP   A CG   1 
ATOM   1589 C  CD1  . TRP   A 1 207 ? -2.166  19.145 23.744  1.00 33.06  ? 207 TRP   A CD1  1 
ATOM   1590 C  CD2  . TRP   A 1 207 ? -1.891  17.013 23.125  1.00 41.82  ? 207 TRP   A CD2  1 
ATOM   1591 N  NE1  . TRP   A 1 207 ? -3.151  18.402 24.350  1.00 34.31  ? 207 TRP   A NE1  1 
ATOM   1592 C  CE2  . TRP   A 1 207 ? -3.003  17.089 23.985  1.00 41.52  ? 207 TRP   A CE2  1 
ATOM   1593 C  CE3  . TRP   A 1 207 ? -1.523  15.769 22.603  1.00 36.14  ? 207 TRP   A CE3  1 
ATOM   1594 C  CZ2  . TRP   A 1 207 ? -3.751  15.970 24.334  1.00 34.73  ? 207 TRP   A CZ2  1 
ATOM   1595 C  CZ3  . TRP   A 1 207 ? -2.265  14.659 22.953  1.00 41.00  ? 207 TRP   A CZ3  1 
ATOM   1596 C  CH2  . TRP   A 1 207 ? -3.366  14.767 23.810  1.00 38.52  ? 207 TRP   A CH2  1 
ATOM   1597 N  N    . LEU   A 1 208 ? 2.205   17.035 23.462  1.00 39.71  ? 208 LEU   A N    1 
ATOM   1598 C  CA   . LEU   A 1 208 ? 2.725   16.045 24.400  1.00 46.29  ? 208 LEU   A CA   1 
ATOM   1599 C  C    . LEU   A 1 208 ? 3.703   16.685 25.377  1.00 44.13  ? 208 LEU   A C    1 
ATOM   1600 O  O    . LEU   A 1 208 ? 3.672   16.393 26.578  1.00 44.03  ? 208 LEU   A O    1 
ATOM   1601 C  CB   . LEU   A 1 208 ? 3.387   14.891 23.645  1.00 38.56  ? 208 LEU   A CB   1 
ATOM   1602 C  CG   . LEU   A 1 208 ? 2.428   13.957 22.896  1.00 46.15  ? 208 LEU   A CG   1 
ATOM   1603 C  CD1  . LEU   A 1 208 ? 3.173   12.820 22.200  1.00 37.80  ? 208 LEU   A CD1  1 
ATOM   1604 C  CD2  . LEU   A 1 208 ? 1.357   13.414 23.835  1.00 38.40  ? 208 LEU   A CD2  1 
ATOM   1605 N  N    . TYR   A 1 209 ? 4.569   17.574 24.885  1.00 42.58  ? 209 TYR   A N    1 
ATOM   1606 C  CA   . TYR   A 1 209 ? 5.473   18.285 25.781  1.00 41.44  ? 209 TYR   A CA   1 
ATOM   1607 C  C    . TYR   A 1 209 ? 4.701   19.131 26.783  1.00 48.74  ? 209 TYR   A C    1 
ATOM   1608 O  O    . TYR   A 1 209 ? 5.081   19.218 27.956  1.00 40.34  ? 209 TYR   A O    1 
ATOM   1609 C  CB   . TYR   A 1 209 ? 6.432   19.160 24.984  1.00 42.62  ? 209 TYR   A CB   1 
ATOM   1610 C  CG   . TYR   A 1 209 ? 7.658   18.428 24.506  1.00 48.78  ? 209 TYR   A CG   1 
ATOM   1611 C  CD1  . TYR   A 1 209 ? 8.651   18.035 25.395  1.00 47.77  ? 209 TYR   A CD1  1 
ATOM   1612 C  CD2  . TYR   A 1 209 ? 7.822   18.131 23.165  1.00 44.81  ? 209 TYR   A CD2  1 
ATOM   1613 C  CE1  . TYR   A 1 209 ? 9.774   17.363 24.952  1.00 52.42  ? 209 TYR   A CE1  1 
ATOM   1614 C  CE2  . TYR   A 1 209 ? 8.937   17.464 22.713  1.00 53.68  ? 209 TYR   A CE2  1 
ATOM   1615 C  CZ   . TYR   A 1 209 ? 9.909   17.081 23.606  1.00 48.25  ? 209 TYR   A CZ   1 
ATOM   1616 O  OH   . TYR   A 1 209 ? 11.017  16.416 23.142  1.00 58.05  ? 209 TYR   A OH   1 
ATOM   1617 N  N    . ALA   A 1 210 ? 3.619   19.776 26.337  1.00 39.44  ? 210 ALA   A N    1 
ATOM   1618 C  CA   . ALA   A 1 210 ? 2.793   20.535 27.268  1.00 39.82  ? 210 ALA   A CA   1 
ATOM   1619 C  C    . ALA   A 1 210 ? 2.281   19.644 28.389  1.00 39.73  ? 210 ALA   A C    1 
ATOM   1620 O  O    . ALA   A 1 210 ? 2.247   20.053 29.554  1.00 48.43  ? 210 ALA   A O    1 
ATOM   1621 C  CB   . ALA   A 1 210 ? 1.625   21.191 26.534  1.00 35.55  ? 210 ALA   A CB   1 
ATOM   1622 N  N    . ALA   A 1 211 ? 1.875   18.419 28.053  1.00 39.54  ? 211 ALA   A N    1 
ATOM   1623 C  CA   . ALA   A 1 211 ? 1.408   17.487 29.071  1.00 50.18  ? 211 ALA   A CA   1 
ATOM   1624 C  C    . ALA   A 1 211 ? 2.502   17.206 30.095  1.00 47.79  ? 211 ALA   A C    1 
ATOM   1625 O  O    . ALA   A 1 211 ? 2.272   17.291 31.306  1.00 46.17  ? 211 ALA   A O    1 
ATOM   1626 C  CB   . ALA   A 1 211 ? 0.930   16.193 28.412  1.00 44.26  ? 211 ALA   A CB   1 
ATOM   1627 N  N    . VAL   A 1 212 ? 3.709   16.883 29.623  1.00 42.90  ? 212 VAL   A N    1 
ATOM   1628 C  CA   . VAL   A 1 212 ? 4.810   16.598 30.540  1.00 52.71  ? 212 VAL   A CA   1 
ATOM   1629 C  C    . VAL   A 1 212 ? 5.048   17.777 31.475  1.00 54.22  ? 212 VAL   A C    1 
ATOM   1630 O  O    . VAL   A 1 212 ? 5.217   17.604 32.689  1.00 53.84  ? 212 VAL   A O    1 
ATOM   1631 C  CB   . VAL   A 1 212 ? 6.083   16.238 29.752  1.00 49.50  ? 212 VAL   A CB   1 
ATOM   1632 C  CG1  . VAL   A 1 212 ? 7.279   16.140 30.690  1.00 41.38  ? 212 VAL   A CG1  1 
ATOM   1633 C  CG2  . VAL   A 1 212 ? 5.886   14.940 28.980  1.00 46.36  ? 212 VAL   A CG2  1 
ATOM   1634 N  N    . ILE   A 1 213 ? 5.059   18.996 30.928  1.00 49.93  ? 213 ILE   A N    1 
ATOM   1635 C  CA   . ILE   A 1 213 ? 5.300   20.177 31.752  1.00 51.77  ? 213 ILE   A CA   1 
ATOM   1636 C  C    . ILE   A 1 213 ? 4.213   20.338 32.803  1.00 57.66  ? 213 ILE   A C    1 
ATOM   1637 O  O    . ILE   A 1 213 ? 4.466   20.871 33.891  1.00 56.41  ? 213 ILE   A O    1 
ATOM   1638 C  CB   . ILE   A 1 213 ? 5.410   21.434 30.869  1.00 54.72  ? 213 ILE   A CB   1 
ATOM   1639 C  CG1  . ILE   A 1 213 ? 6.617   21.331 29.936  1.00 58.87  ? 213 ILE   A CG1  1 
ATOM   1640 C  CG2  . ILE   A 1 213 ? 5.507   22.685 31.730  1.00 60.53  ? 213 ILE   A CG2  1 
ATOM   1641 C  CD1  . ILE   A 1 213 ? 6.760   22.518 28.998  1.00 50.60  ? 213 ILE   A CD1  1 
ATOM   1642 N  N    . ASN   A 1 214 ? 2.996   19.887 32.507  1.00 46.12  ? 214 ASN   A N    1 
ATOM   1643 C  CA   . ASN   A 1 214 ? 1.881   19.991 33.438  1.00 53.66  ? 214 ASN   A CA   1 
ATOM   1644 C  C    . ASN   A 1 214 ? 1.699   18.741 34.297  1.00 60.90  ? 214 ASN   A C    1 
ATOM   1645 O  O    . ASN   A 1 214 ? 0.649   18.590 34.929  1.00 63.83  ? 214 ASN   A O    1 
ATOM   1646 C  CB   . ASN   A 1 214 ? 0.583   20.293 32.684  1.00 52.22  ? 214 ASN   A CB   1 
ATOM   1647 C  CG   . ASN   A 1 214 ? 0.420   21.770 32.369  1.00 62.27  ? 214 ASN   A CG   1 
ATOM   1648 O  OD1  . ASN   A 1 214 ? -0.597  22.379 32.700  1.00 56.38  ? 214 ASN   A OD1  1 
ATOM   1649 N  ND2  . ASN   A 1 214 ? 1.422   22.351 31.718  1.00 66.31  ? 214 ASN   A ND2  1 
ATOM   1650 N  N    . GLY   A 1 215 ? 2.683   17.842 34.326  1.00 57.86  ? 215 GLY   A N    1 
ATOM   1651 C  CA   . GLY   A 1 215 ? 2.714   16.757 35.289  1.00 67.50  ? 215 GLY   A CA   1 
ATOM   1652 C  C    . GLY   A 1 215 ? 2.345   15.387 34.760  1.00 68.41  ? 215 GLY   A C    1 
ATOM   1653 O  O    . GLY   A 1 215 ? 2.507   14.404 35.494  1.00 85.52  ? 215 GLY   A O    1 
ATOM   1654 N  N    . ASP   A 1 216 ? 1.858   15.276 33.528  1.00 77.29  ? 216 ASP   A N    1 
ATOM   1655 C  CA   . ASP   A 1 216 ? 1.472   13.986 32.970  1.00 79.17  ? 216 ASP   A CA   1 
ATOM   1656 C  C    . ASP   A 1 216 ? 2.667   13.303 32.315  1.00 79.86  ? 216 ASP   A C    1 
ATOM   1657 O  O    . ASP   A 1 216 ? 3.471   13.947 31.635  1.00 77.93  ? 216 ASP   A O    1 
ATOM   1658 C  CB   . ASP   A 1 216 ? 0.343   14.154 31.954  1.00 75.84  ? 216 ASP   A CB   1 
ATOM   1659 C  CG   . ASP   A 1 216 ? -0.803  13.195 32.196  1.00 82.54  ? 216 ASP   A CG   1 
ATOM   1660 O  OD1  . ASP   A 1 216 ? -0.635  12.263 33.009  1.00 84.68  ? 216 ASP   A OD1  1 
ATOM   1661 O  OD2  . ASP   A 1 216 ? -1.871  13.373 31.570  1.00 83.31  ? 216 ASP   A OD2  1 
ATOM   1662 N  N    . ARG   A 1 217 ? 2.773   11.985 32.522  1.00 74.42  ? 217 ARG   A N    1 
ATOM   1663 C  CA   . ARG   A 1 217 ? 3.913   11.237 32.002  1.00 58.11  ? 217 ARG   A CA   1 
ATOM   1664 C  C    . ARG   A 1 217 ? 3.603   9.782  31.671  1.00 55.96  ? 217 ARG   A C    1 
ATOM   1665 O  O    . ARG   A 1 217 ? 4.518   9.064  31.261  1.00 63.06  ? 217 ARG   A O    1 
ATOM   1666 C  CB   . ARG   A 1 217 ? 5.077   11.296 33.007  1.00 63.65  ? 217 ARG   A CB   1 
ATOM   1667 C  CG   . ARG   A 1 217 ? 5.807   12.631 33.042  1.00 63.64  ? 217 ARG   A CG   1 
ATOM   1668 C  CD   . ARG   A 1 217 ? 6.930   12.651 34.079  1.00 55.55  ? 217 ARG   A CD   1 
ATOM   1669 N  NE   . ARG   A 1 217 ? 8.079   11.862 33.651  1.00 51.92  ? 217 ARG   A NE   1 
ATOM   1670 C  CZ   . ARG   A 1 217 ? 9.229   12.381 33.238  1.00 52.31  ? 217 ARG   A CZ   1 
ATOM   1671 N  NH1  . ARG   A 1 217 ? 9.407   13.692 33.145  1.00 55.94  ? 217 ARG   A NH1  1 
ATOM   1672 N  NH2  . ARG   A 1 217 ? 10.223  11.566 32.899  1.00 53.88  ? 217 ARG   A NH2  1 
ATOM   1673 N  N    . TRP   A 1 218 ? 2.360   9.318  31.826  1.00 56.56  ? 218 TRP   A N    1 
ATOM   1674 C  CA   . TRP   A 1 218 ? 2.066   7.899  31.643  1.00 55.53  ? 218 TRP   A CA   1 
ATOM   1675 C  C    . TRP   A 1 218 ? 2.403   7.420  30.237  1.00 62.39  ? 218 TRP   A C    1 
ATOM   1676 O  O    . TRP   A 1 218 ? 2.775   6.256  30.054  1.00 66.47  ? 218 TRP   A O    1 
ATOM   1677 C  CB   . TRP   A 1 218 ? 0.593   7.625  31.955  1.00 59.08  ? 218 TRP   A CB   1 
ATOM   1678 C  CG   . TRP   A 1 218 ? -0.368  8.220  30.960  1.00 65.02  ? 218 TRP   A CG   1 
ATOM   1679 C  CD1  . TRP   A 1 218 ? -0.997  9.428  31.051  1.00 57.81  ? 218 TRP   A CD1  1 
ATOM   1680 C  CD2  . TRP   A 1 218 ? -0.812  7.630  29.730  1.00 57.83  ? 218 TRP   A CD2  1 
ATOM   1681 N  NE1  . TRP   A 1 218 ? -1.803  9.629  29.955  1.00 60.48  ? 218 TRP   A NE1  1 
ATOM   1682 C  CE2  . TRP   A 1 218 ? -1.707  8.540  29.129  1.00 64.12  ? 218 TRP   A CE2  1 
ATOM   1683 C  CE3  . TRP   A 1 218 ? -0.539  6.424  29.078  1.00 61.19  ? 218 TRP   A CE3  1 
ATOM   1684 C  CZ2  . TRP   A 1 218 ? -2.328  8.282  27.908  1.00 62.61  ? 218 TRP   A CZ2  1 
ATOM   1685 C  CZ3  . TRP   A 1 218 ? -1.158  6.168  27.867  1.00 64.49  ? 218 TRP   A CZ3  1 
ATOM   1686 C  CH2  . TRP   A 1 218 ? -2.042  7.094  27.294  1.00 64.45  ? 218 TRP   A CH2  1 
ATOM   1687 N  N    . PHE   A 1 219 ? 2.280   8.295  29.238  1.00 53.79  ? 219 PHE   A N    1 
ATOM   1688 C  CA   . PHE   A 1 219 ? 2.526   7.927  27.850  1.00 54.88  ? 219 PHE   A CA   1 
ATOM   1689 C  C    . PHE   A 1 219 ? 4.007   7.848  27.503  1.00 57.07  ? 219 PHE   A C    1 
ATOM   1690 O  O    . PHE   A 1 219 ? 4.347   7.327  26.435  1.00 51.05  ? 219 PHE   A O    1 
ATOM   1691 C  CB   . PHE   A 1 219 ? 1.845   8.930  26.916  1.00 52.73  ? 219 PHE   A CB   1 
ATOM   1692 C  CG   . PHE   A 1 219 ? 2.203   10.358 27.205  1.00 46.45  ? 219 PHE   A CG   1 
ATOM   1693 C  CD1  . PHE   A 1 219 ? 3.328   10.931 26.638  1.00 41.51  ? 219 PHE   A CD1  1 
ATOM   1694 C  CD2  . PHE   A 1 219 ? 1.425   11.122 28.061  1.00 52.82  ? 219 PHE   A CD2  1 
ATOM   1695 C  CE1  . PHE   A 1 219 ? 3.664   12.244 26.906  1.00 46.72  ? 219 PHE   A CE1  1 
ATOM   1696 C  CE2  . PHE   A 1 219 ? 1.757   12.436 28.337  1.00 50.41  ? 219 PHE   A CE2  1 
ATOM   1697 C  CZ   . PHE   A 1 219 ? 2.879   12.998 27.756  1.00 46.95  ? 219 PHE   A CZ   1 
ATOM   1698 N  N    . LEU   A 1 220 ? 4.891   8.358  28.356  1.00 54.66  ? 220 LEU   A N    1 
ATOM   1699 C  CA   . LEU   A 1 220 ? 6.314   8.290  28.064  1.00 57.85  ? 220 LEU   A CA   1 
ATOM   1700 C  C    . LEU   A 1 220 ? 6.785   6.839  28.101  1.00 56.01  ? 220 LEU   A C    1 
ATOM   1701 O  O    . LEU   A 1 220 ? 6.146   5.968  28.695  1.00 60.09  ? 220 LEU   A O    1 
ATOM   1702 C  CB   . LEU   A 1 220 ? 7.111   9.133  29.059  1.00 54.80  ? 220 LEU   A CB   1 
ATOM   1703 C  CG   . LEU   A 1 220 ? 6.981   10.655 28.947  1.00 52.44  ? 220 LEU   A CG   1 
ATOM   1704 C  CD1  . LEU   A 1 220 ? 7.936   11.338 29.916  1.00 57.08  ? 220 LEU   A CD1  1 
ATOM   1705 C  CD2  . LEU   A 1 220 ? 7.219   11.129 27.522  1.00 44.84  ? 220 LEU   A CD2  1 
ATOM   1706 N  N    . ASN   A 1 221 ? 7.912   6.577  27.442  1.00 57.52  ? 221 ASN   A N    1 
ATOM   1707 C  CA   . ASN   A 1 221 ? 8.474   5.233  27.421  1.00 61.77  ? 221 ASN   A CA   1 
ATOM   1708 C  C    . ASN   A 1 221 ? 9.994   5.332  27.413  1.00 61.40  ? 221 ASN   A C    1 
ATOM   1709 O  O    . ASN   A 1 221 ? 10.570  6.424  27.387  1.00 61.25  ? 221 ASN   A O    1 
ATOM   1710 C  CB   . ASN   A 1 221 ? 7.956   4.420  26.224  1.00 68.16  ? 221 ASN   A CB   1 
ATOM   1711 C  CG   . ASN   A 1 221 ? 8.473   4.931  24.885  1.00 72.54  ? 221 ASN   A CG   1 
ATOM   1712 O  OD1  . ASN   A 1 221 ? 9.211   5.914  24.816  1.00 73.62  ? 221 ASN   A OD1  1 
ATOM   1713 N  ND2  . ASN   A 1 221 ? 8.080   4.257  23.812  1.00 77.25  ? 221 ASN   A ND2  1 
ATOM   1714 N  N    . ARG   A 1 222 ? 10.644  4.170  27.450  1.00 62.82  ? 222 ARG   A N    1 
ATOM   1715 C  CA   . ARG   A 1 222 ? 12.097  4.088  27.420  1.00 75.81  ? 222 ARG   A CA   1 
ATOM   1716 C  C    . ARG   A 1 222 ? 12.636  3.801  26.028  1.00 76.12  ? 222 ARG   A C    1 
ATOM   1717 O  O    . ARG   A 1 222 ? 13.852  3.872  25.823  1.00 73.34  ? 222 ARG   A O    1 
ATOM   1718 C  CB   . ARG   A 1 222 ? 12.588  3.009  28.396  1.00 76.31  ? 222 ARG   A CB   1 
ATOM   1719 C  CG   . ARG   A 1 222 ? 11.991  1.638  28.110  1.00 81.96  ? 222 ARG   A CG   1 
ATOM   1720 C  CD   . ARG   A 1 222 ? 12.962  0.513  28.398  1.00 87.47  ? 222 ARG   A CD   1 
ATOM   1721 N  NE   . ARG   A 1 222 ? 12.574  -0.710 27.697  1.00 88.68  ? 222 ARG   A NE   1 
ATOM   1722 C  CZ   . ARG   A 1 222 ? 13.429  -1.558 27.140  1.00 92.52  ? 222 ARG   A CZ   1 
ATOM   1723 N  NH1  . ARG   A 1 222 ? 14.735  -1.352 27.188  1.00 95.97  ? 222 ARG   A NH1  1 
ATOM   1724 N  NH2  . ARG   A 1 222 ? 12.961  -2.643 26.526  1.00 92.21  ? 222 ARG   A NH2  1 
ATOM   1725 N  N    . PHE   A 1 223 ? 11.764  3.491  25.073  1.00 77.05  ? 223 PHE   A N    1 
ATOM   1726 C  CA   . PHE   A 1 223 ? 12.185  3.184  23.718  1.00 78.17  ? 223 PHE   A CA   1 
ATOM   1727 C  C    . PHE   A 1 223 ? 12.645  4.451  22.998  1.00 72.78  ? 223 PHE   A C    1 
ATOM   1728 O  O    . PHE   A 1 223 ? 12.317  5.576  23.385  1.00 74.29  ? 223 PHE   A O    1 
ATOM   1729 C  CB   . PHE   A 1 223 ? 11.040  2.523  22.953  1.00 77.91  ? 223 PHE   A CB   1 
ATOM   1730 C  CG   . PHE   A 1 223 ? 10.752  1.121  23.398  1.00 87.25  ? 223 PHE   A CG   1 
ATOM   1731 C  CD1  . PHE   A 1 223 ? 11.743  0.151  23.387  1.00 80.67  ? 223 PHE   A CD1  1 
ATOM   1732 C  CD2  . PHE   A 1 223 ? 9.485   0.773  23.832  1.00 86.38  ? 223 PHE   A CD2  1 
ATOM   1733 C  CE1  . PHE   A 1 223 ? 11.471  -1.139 23.801  1.00 86.70  ? 223 PHE   A CE1  1 
ATOM   1734 C  CE2  . PHE   A 1 223 ? 9.209   -0.511 24.249  1.00 84.66  ? 223 PHE   A CE2  1 
ATOM   1735 C  CZ   . PHE   A 1 223 ? 10.201  -1.470 24.232  1.00 93.04  ? 223 PHE   A CZ   1 
ATOM   1736 N  N    . THR   A 1 224 ? 13.428  4.253  21.942  1.00 74.35  ? 224 THR   A N    1 
ATOM   1737 C  CA   . THR   A 1 224 ? 13.908  5.337  21.097  1.00 80.17  ? 224 THR   A CA   1 
ATOM   1738 C  C    . THR   A 1 224 ? 13.629  5.004  19.636  1.00 77.55  ? 224 THR   A C    1 
ATOM   1739 O  O    . THR   A 1 224 ? 13.512  3.837  19.253  1.00 76.45  ? 224 THR   A O    1 
ATOM   1740 C  CB   . THR   A 1 224 ? 15.410  5.598  21.299  1.00 75.81  ? 224 THR   A CB   1 
ATOM   1741 O  OG1  . THR   A 1 224 ? 15.743  6.902  20.806  1.00 80.88  ? 224 THR   A OG1  1 
ATOM   1742 C  CG2  . THR   A 1 224 ? 16.242  4.552  20.575  1.00 70.68  ? 224 THR   A CG2  1 
ATOM   1743 N  N    . THR   A 1 225 ? 13.526  6.051  18.819  1.00 70.70  ? 225 THR   A N    1 
ATOM   1744 C  CA   . THR   A 1 225 ? 13.222  5.899  17.405  1.00 74.32  ? 225 THR   A CA   1 
ATOM   1745 C  C    . THR   A 1 225 ? 14.107  6.829  16.587  1.00 76.63  ? 225 THR   A C    1 
ATOM   1746 O  O    . THR   A 1 225 ? 14.558  7.870  17.072  1.00 71.82  ? 225 THR   A O    1 
ATOM   1747 C  CB   . THR   A 1 225 ? 11.742  6.202  17.110  1.00 73.09  ? 225 THR   A CB   1 
ATOM   1748 O  OG1  . THR   A 1 225 ? 11.324  5.493  15.937  1.00 68.78  ? 225 THR   A OG1  1 
ATOM   1749 C  CG2  . THR   A 1 225 ? 11.538  7.696  16.888  1.00 68.41  ? 225 THR   A CG2  1 
ATOM   1750 N  N    . THR   A 1 226 ? 14.353  6.438  15.340  1.00 77.12  ? 226 THR   A N    1 
ATOM   1751 C  CA   . THR   A 1 226 ? 14.995  7.312  14.372  1.00 68.70  ? 226 THR   A CA   1 
ATOM   1752 C  C    . THR   A 1 226 ? 13.937  8.092  13.599  1.00 75.97  ? 226 THR   A C    1 
ATOM   1753 O  O    . THR   A 1 226 ? 12.762  7.721  13.555  1.00 70.90  ? 226 THR   A O    1 
ATOM   1754 C  CB   . THR   A 1 226 ? 15.864  6.516  13.400  1.00 73.72  ? 226 THR   A CB   1 
ATOM   1755 O  OG1  . THR   A 1 226 ? 15.074  6.117  12.274  1.00 75.23  ? 226 THR   A OG1  1 
ATOM   1756 C  CG2  . THR   A 1 226 ? 16.441  5.283  14.083  1.00 69.62  ? 226 THR   A CG2  1 
ATOM   1757 N  N    . LEU   A 1 227 ? 14.375  9.189  12.980  1.00 73.00  ? 227 LEU   A N    1 
ATOM   1758 C  CA   . LEU   A 1 227 ? 13.434  10.063 12.288  1.00 71.77  ? 227 LEU   A CA   1 
ATOM   1759 C  C    . LEU   A 1 227 ? 12.685  9.316  11.190  1.00 75.66  ? 227 LEU   A C    1 
ATOM   1760 O  O    . LEU   A 1 227 ? 11.480  9.516  11.002  1.00 69.59  ? 227 LEU   A O    1 
ATOM   1761 C  CB   . LEU   A 1 227 ? 14.172  11.272 11.712  1.00 68.95  ? 227 LEU   A CB   1 
ATOM   1762 C  CG   . LEU   A 1 227 ? 13.374  12.576 11.621  1.00 79.04  ? 227 LEU   A CG   1 
ATOM   1763 C  CD1  . LEU   A 1 227 ? 14.266  13.724 11.166  1.00 83.98  ? 227 LEU   A CD1  1 
ATOM   1764 C  CD2  . LEU   A 1 227 ? 12.176  12.420 10.701  1.00 80.08  ? 227 LEU   A CD2  1 
ATOM   1765 N  N    . ASN   A 1 228 ? 13.376  8.436  10.464  1.00 74.00  ? 228 ASN   A N    1 
ATOM   1766 C  CA   . ASN   A 1 228 ? 12.753  7.780  9.320   1.00 72.70  ? 228 ASN   A CA   1 
ATOM   1767 C  C    . ASN   A 1 228 ? 11.774  6.693  9.752   1.00 75.82  ? 228 ASN   A C    1 
ATOM   1768 O  O    . ASN   A 1 228 ? 10.640  6.643  9.263   1.00 72.05  ? 228 ASN   A O    1 
ATOM   1769 C  CB   . ASN   A 1 228 ? 13.831  7.218  8.396   1.00 69.41  ? 228 ASN   A CB   1 
ATOM   1770 C  CG   . ASN   A 1 228 ? 14.235  8.208  7.320   1.00 85.82  ? 228 ASN   A CG   1 
ATOM   1771 O  OD1  . ASN   A 1 228 ? 14.304  9.413  7.566   1.00 79.57  ? 228 ASN   A OD1  1 
ATOM   1772 N  ND2  . ASN   A 1 228 ? 14.508  7.704  6.121   1.00 85.96  ? 228 ASN   A ND2  1 
ATOM   1773 N  N    . ASP   A 1 229 ? 12.189  5.813  10.668  1.00 77.96  ? 229 ASP   A N    1 
ATOM   1774 C  CA   . ASP   A 1 229 ? 11.277  4.781  11.153  1.00 75.59  ? 229 ASP   A CA   1 
ATOM   1775 C  C    . ASP   A 1 229 ? 9.985   5.382  11.692  1.00 72.29  ? 229 ASP   A C    1 
ATOM   1776 O  O    . ASP   A 1 229 ? 8.910   4.791  11.534  1.00 70.96  ? 229 ASP   A O    1 
ATOM   1777 C  CB   . ASP   A 1 229 ? 11.960  3.933  12.224  1.00 73.29  ? 229 ASP   A CB   1 
ATOM   1778 C  CG   . ASP   A 1 229 ? 13.168  3.192  11.690  1.00 92.10  ? 229 ASP   A CG   1 
ATOM   1779 O  OD1  . ASP   A 1 229 ? 12.993  2.344  10.790  1.00 98.55  ? 229 ASP   A OD1  1 
ATOM   1780 O  OD2  . ASP   A 1 229 ? 14.292  3.457  12.168  1.00 90.69  ? 229 ASP   A OD2  1 
ATOM   1781 N  N    . PHE   A 1 230 ? 10.063  6.552  12.329  1.00 69.59  ? 230 PHE   A N    1 
ATOM   1782 C  CA   . PHE   A 1 230 ? 8.845   7.231  12.756  1.00 71.34  ? 230 PHE   A CA   1 
ATOM   1783 C  C    . PHE   A 1 230 ? 8.001   7.633  11.553  1.00 65.58  ? 230 PHE   A C    1 
ATOM   1784 O  O    . PHE   A 1 230 ? 6.786   7.409  11.526  1.00 61.31  ? 230 PHE   A O    1 
ATOM   1785 C  CB   . PHE   A 1 230 ? 9.189   8.455  13.605  1.00 59.03  ? 230 PHE   A CB   1 
ATOM   1786 C  CG   . PHE   A 1 230 ? 7.993   9.271  13.993  1.00 60.94  ? 230 PHE   A CG   1 
ATOM   1787 C  CD1  . PHE   A 1 230 ? 7.281   8.976  15.142  1.00 54.30  ? 230 PHE   A CD1  1 
ATOM   1788 C  CD2  . PHE   A 1 230 ? 7.569   10.323 13.198  1.00 58.69  ? 230 PHE   A CD2  1 
ATOM   1789 C  CE1  . PHE   A 1 230 ? 6.177   9.721  15.498  1.00 58.35  ? 230 PHE   A CE1  1 
ATOM   1790 C  CE2  . PHE   A 1 230 ? 6.465   11.069 13.548  1.00 59.40  ? 230 PHE   A CE2  1 
ATOM   1791 C  CZ   . PHE   A 1 230 ? 5.768   10.770 14.700  1.00 64.20  ? 230 PHE   A CZ   1 
ATOM   1792 N  N    . ASN   A 1 231 ? 8.638   8.225  10.539  1.00 73.46  ? 231 ASN   A N    1 
ATOM   1793 C  CA   . ASN   A 1 231 ? 7.910   8.675  9.357   1.00 70.44  ? 231 ASN   A CA   1 
ATOM   1794 C  C    . ASN   A 1 231 ? 7.189   7.525  8.668   1.00 62.25  ? 231 ASN   A C    1 
ATOM   1795 O  O    . ASN   A 1 231 ? 6.105   7.719  8.108   1.00 67.70  ? 231 ASN   A O    1 
ATOM   1796 C  CB   . ASN   A 1 231 ? 8.870   9.364  8.387   1.00 63.30  ? 231 ASN   A CB   1 
ATOM   1797 C  CG   . ASN   A 1 231 ? 9.171   10.797 8.787   1.00 67.53  ? 231 ASN   A CG   1 
ATOM   1798 O  OD1  . ASN   A 1 231 ? 8.320   11.489 9.347   1.00 63.88  ? 231 ASN   A OD1  1 
ATOM   1799 N  ND2  . ASN   A 1 231 ? 10.390  11.247 8.508   1.00 71.35  ? 231 ASN   A ND2  1 
ATOM   1800 N  N    . LEU   A 1 232 ? 7.766   6.324  8.699   1.00 58.04  ? 232 LEU   A N    1 
ATOM   1801 C  CA   . LEU   A 1 232 ? 7.093   5.179  8.101   1.00 65.86  ? 232 LEU   A CA   1 
ATOM   1802 C  C    . LEU   A 1 232 ? 5.844   4.792  8.882   1.00 72.15  ? 232 LEU   A C    1 
ATOM   1803 O  O    . LEU   A 1 232 ? 4.871   4.308  8.292   1.00 79.02  ? 232 LEU   A O    1 
ATOM   1804 C  CB   . LEU   A 1 232 ? 8.055   3.998  8.003   1.00 67.08  ? 232 LEU   A CB   1 
ATOM   1805 C  CG   . LEU   A 1 232 ? 9.050   4.105  6.846   1.00 80.88  ? 232 LEU   A CG   1 
ATOM   1806 C  CD1  . LEU   A 1 232 ? 10.228  3.161  7.045   1.00 68.85  ? 232 LEU   A CD1  1 
ATOM   1807 C  CD2  . LEU   A 1 232 ? 8.358   3.848  5.512   1.00 74.72  ? 232 LEU   A CD2  1 
ATOM   1808 N  N    . VAL   A 1 233 ? 5.850   4.995  10.200  1.00 65.68  ? 233 VAL   A N    1 
ATOM   1809 C  CA   . VAL   A 1 233 ? 4.649   4.747  10.991  1.00 67.58  ? 233 VAL   A CA   1 
ATOM   1810 C  C    . VAL   A 1 233 ? 3.648   5.881  10.816  1.00 70.55  ? 233 VAL   A C    1 
ATOM   1811 O  O    . VAL   A 1 233 ? 2.438   5.646  10.718  1.00 72.95  ? 233 VAL   A O    1 
ATOM   1812 C  CB   . VAL   A 1 233 ? 5.015   4.545  12.472  1.00 72.13  ? 233 VAL   A CB   1 
ATOM   1813 C  CG1  . VAL   A 1 233 ? 3.850   3.918  13.222  1.00 73.30  ? 233 VAL   A CG1  1 
ATOM   1814 C  CG2  . VAL   A 1 233 ? 6.263   3.687  12.601  1.00 76.15  ? 233 VAL   A CG2  1 
ATOM   1815 N  N    . ALA   A 1 234 ? 4.134   7.123  10.772  1.00 62.34  ? 234 ALA   A N    1 
ATOM   1816 C  CA   . ALA   A 1 234 ? 3.237   8.267  10.649  1.00 69.33  ? 234 ALA   A CA   1 
ATOM   1817 C  C    . ALA   A 1 234 ? 2.471   8.237  9.333   1.00 69.68  ? 234 ALA   A C    1 
ATOM   1818 O  O    . ALA   A 1 234 ? 1.268   8.523  9.300   1.00 67.45  ? 234 ALA   A O    1 
ATOM   1819 C  CB   . ALA   A 1 234 ? 4.030   9.568  10.781  1.00 71.35  ? 234 ALA   A CB   1 
ATOM   1820 N  N    . MET   A 1 235 ? 3.150   7.894  8.235   1.00 70.27  ? 235 MET   A N    1 
ATOM   1821 C  CA   . MET   A 1 235 ? 2.483   7.855  6.937   1.00 69.11  ? 235 MET   A CA   1 
ATOM   1822 C  C    . MET   A 1 235 ? 1.308   6.883  6.946   1.00 75.71  ? 235 MET   A C    1 
ATOM   1823 O  O    . MET   A 1 235 ? 0.254   7.167  6.364   1.00 75.53  ? 235 MET   A O    1 
ATOM   1824 C  CB   . MET   A 1 235 ? 3.483   7.477  5.844   1.00 78.55  ? 235 MET   A CB   1 
ATOM   1825 C  CG   . MET   A 1 235 ? 2.835   7.038  4.537   1.00 80.38  ? 235 MET   A CG   1 
ATOM   1826 S  SD   . MET   A 1 235 ? 3.059   5.278  4.203   1.00 117.77 ? 235 MET   A SD   1 
ATOM   1827 C  CE   . MET   A 1 235 ? 1.952   5.043  2.812   1.00 99.92  ? 235 MET   A CE   1 
ATOM   1828 N  N    . LYS   A 1 236 ? 1.469   5.731  7.600   1.00 77.68  ? 236 LYS   A N    1 
ATOM   1829 C  CA   . LYS   A 1 236 ? 0.392   4.750  7.651   1.00 71.99  ? 236 LYS   A CA   1 
ATOM   1830 C  C    . LYS   A 1 236 ? -0.823  5.263  8.414   1.00 71.11  ? 236 LYS   A C    1 
ATOM   1831 O  O    . LYS   A 1 236 ? -1.929  4.751  8.211   1.00 78.88  ? 236 LYS   A O    1 
ATOM   1832 C  CB   . LYS   A 1 236 ? 0.898   3.448  8.278   1.00 75.59  ? 236 LYS   A CB   1 
ATOM   1833 C  CG   . LYS   A 1 236 ? -0.102  2.763  9.200   1.00 82.48  ? 236 LYS   A CG   1 
ATOM   1834 C  CD   . LYS   A 1 236 ? -0.774  1.573  8.522   1.00 92.21  ? 236 LYS   A CD   1 
ATOM   1835 C  CE   . LYS   A 1 236 ? -1.625  0.779  9.509   1.00 88.85  ? 236 LYS   A CE   1 
ATOM   1836 N  NZ   . LYS   A 1 236 ? -2.751  1.588  10.063  1.00 79.55  ? 236 LYS   A NZ   1 
ATOM   1837 N  N    . TYR   A 1 237 ? -0.646  6.264  9.278   1.00 62.71  ? 237 TYR   A N    1 
ATOM   1838 C  CA   . TYR   A 1 237 ? -1.732  6.824  10.075  1.00 69.23  ? 237 TYR   A CA   1 
ATOM   1839 C  C    . TYR   A 1 237 ? -2.122  8.229  9.629   1.00 65.23  ? 237 TYR   A C    1 
ATOM   1840 O  O    . TYR   A 1 237 ? -2.796  8.945  10.375  1.00 59.87  ? 237 TYR   A O    1 
ATOM   1841 C  CB   . TYR   A 1 237 ? -1.356  6.836  11.556  1.00 64.41  ? 237 TYR   A CB   1 
ATOM   1842 C  CG   . TYR   A 1 237 ? -1.283  5.463  12.176  1.00 63.76  ? 237 TYR   A CG   1 
ATOM   1843 C  CD1  . TYR   A 1 237 ? -2.424  4.837  12.654  1.00 69.70  ? 237 TYR   A CD1  1 
ATOM   1844 C  CD2  . TYR   A 1 237 ? -0.074  4.793  12.281  1.00 66.65  ? 237 TYR   A CD2  1 
ATOM   1845 C  CE1  . TYR   A 1 237 ? -2.364  3.580  13.222  1.00 72.73  ? 237 TYR   A CE1  1 
ATOM   1846 C  CE2  . TYR   A 1 237 ? -0.002  3.536  12.846  1.00 72.11  ? 237 TYR   A CE2  1 
ATOM   1847 C  CZ   . TYR   A 1 237 ? -1.150  2.935  13.315  1.00 69.53  ? 237 TYR   A CZ   1 
ATOM   1848 O  OH   . TYR   A 1 237 ? -1.084  1.683  13.879  1.00 80.65  ? 237 TYR   A OH   1 
ATOM   1849 N  N    . ASN   A 1 238 ? -1.700  8.643  8.435   1.00 57.55  ? 238 ASN   A N    1 
ATOM   1850 C  CA   . ASN   A 1 238 ? -2.083  9.940  7.879   1.00 63.34  ? 238 ASN   A CA   1 
ATOM   1851 C  C    . ASN   A 1 238 ? -1.548  11.100 8.718   1.00 61.14  ? 238 ASN   A C    1 
ATOM   1852 O  O    . ASN   A 1 238 ? -2.245  12.088 8.967   1.00 53.02  ? 238 ASN   A O    1 
ATOM   1853 C  CB   . ASN   A 1 238 ? -3.598  10.045 7.717   1.00 55.71  ? 238 ASN   A CB   1 
ATOM   1854 C  CG   . ASN   A 1 238 ? -3.991  11.004 6.623   1.00 69.03  ? 238 ASN   A CG   1 
ATOM   1855 O  OD1  . ASN   A 1 238 ? -3.307  11.114 5.605   1.00 75.64  ? 238 ASN   A OD1  1 
ATOM   1856 N  ND2  . ASN   A 1 238 ? -5.095  11.715 6.827   1.00 65.87  ? 238 ASN   A ND2  1 
ATOM   1857 N  N    . TYR   A 1 239 ? -0.299  10.980 9.150   1.00 52.30  ? 239 TYR   A N    1 
ATOM   1858 C  CA   . TYR   A 1 239 ? 0.408   12.053 9.829   1.00 52.86  ? 239 TYR   A CA   1 
ATOM   1859 C  C    . TYR   A 1 239 ? 1.399   12.708 8.875   1.00 58.26  ? 239 TYR   A C    1 
ATOM   1860 O  O    . TYR   A 1 239 ? 1.986   12.051 8.012   1.00 58.28  ? 239 TYR   A O    1 
ATOM   1861 C  CB   . TYR   A 1 239 ? 1.147   11.530 11.061  1.00 49.06  ? 239 TYR   A CB   1 
ATOM   1862 C  CG   . TYR   A 1 239 ? 0.344   11.589 12.336  1.00 46.53  ? 239 TYR   A CG   1 
ATOM   1863 C  CD1  . TYR   A 1 239 ? -0.921  11.015 12.418  1.00 45.26  ? 239 TYR   A CD1  1 
ATOM   1864 C  CD2  . TYR   A 1 239 ? 0.851   12.224 13.463  1.00 47.80  ? 239 TYR   A CD2  1 
ATOM   1865 C  CE1  . TYR   A 1 239 ? -1.655  11.071 13.592  1.00 42.57  ? 239 TYR   A CE1  1 
ATOM   1866 C  CE2  . TYR   A 1 239 ? 0.131   12.285 14.635  1.00 41.38  ? 239 TYR   A CE2  1 
ATOM   1867 C  CZ   . TYR   A 1 239 ? -1.122  11.709 14.698  1.00 50.88  ? 239 TYR   A CZ   1 
ATOM   1868 O  OH   . TYR   A 1 239 ? -1.834  11.777 15.874  1.00 49.11  ? 239 TYR   A OH   1 
ATOM   1869 N  N    . GLU   A 1 240 ? 1.586   14.010 9.044   1.00 53.24  ? 240 GLU   A N    1 
ATOM   1870 C  CA   . GLU   A 1 240 ? 2.538   14.725 8.215   1.00 56.46  ? 240 GLU   A CA   1 
ATOM   1871 C  C    . GLU   A 1 240 ? 3.957   14.266 8.541   1.00 53.79  ? 240 GLU   A C    1 
ATOM   1872 O  O    . GLU   A 1 240 ? 4.281   14.031 9.710   1.00 56.72  ? 240 GLU   A O    1 
ATOM   1873 C  CB   . GLU   A 1 240 ? 2.416   16.231 8.433   1.00 57.86  ? 240 GLU   A CB   1 
ATOM   1874 C  CG   . GLU   A 1 240 ? 1.615   16.947 7.361   1.00 70.65  ? 240 GLU   A CG   1 
ATOM   1875 C  CD   . GLU   A 1 240 ? 1.956   18.419 7.269   1.00 88.09  ? 240 GLU   A CD   1 
ATOM   1876 O  OE1  . GLU   A 1 240 ? 2.193   18.906 6.139   1.00 85.49  ? 240 GLU   A OE1  1 
ATOM   1877 O  OE2  . GLU   A 1 240 ? 1.998   19.083 8.329   1.00 79.08  ? 240 GLU   A OE2  1 
ATOM   1878 N  N    . PRO   A 1 241 ? 4.823   14.130 7.539   1.00 68.04  ? 241 PRO   A N    1 
ATOM   1879 C  CA   . PRO   A 1 241 ? 6.205   13.725 7.817   1.00 65.46  ? 241 PRO   A CA   1 
ATOM   1880 C  C    . PRO   A 1 241 ? 6.910   14.739 8.705   1.00 65.39  ? 241 PRO   A C    1 
ATOM   1881 O  O    . PRO   A 1 241 ? 6.612   15.935 8.683   1.00 64.64  ? 241 PRO   A O    1 
ATOM   1882 C  CB   . PRO   A 1 241 ? 6.847   13.656 6.425   1.00 70.74  ? 241 PRO   A CB   1 
ATOM   1883 C  CG   . PRO   A 1 241 ? 5.692   13.584 5.462   1.00 60.10  ? 241 PRO   A CG   1 
ATOM   1884 C  CD   . PRO   A 1 241 ? 4.576   14.340 6.103   1.00 57.02  ? 241 PRO   A CD   1 
ATOM   1885 N  N    . LEU   A 1 242 ? 7.854   14.247 9.498   1.00 65.48  ? 242 LEU   A N    1 
ATOM   1886 C  CA   . LEU   A 1 242 ? 8.631   15.088 10.399  1.00 74.79  ? 242 LEU   A CA   1 
ATOM   1887 C  C    . LEU   A 1 242 ? 9.979   15.392 9.757   1.00 71.92  ? 242 LEU   A C    1 
ATOM   1888 O  O    . LEU   A 1 242 ? 10.743  14.474 9.442   1.00 70.31  ? 242 LEU   A O    1 
ATOM   1889 C  CB   . LEU   A 1 242 ? 8.818   14.410 11.755  1.00 71.52  ? 242 LEU   A CB   1 
ATOM   1890 C  CG   . LEU   A 1 242 ? 9.033   15.350 12.944  1.00 73.96  ? 242 LEU   A CG   1 
ATOM   1891 C  CD1  . LEU   A 1 242 ? 7.765   16.129 13.260  1.00 63.85  ? 242 LEU   A CD1  1 
ATOM   1892 C  CD2  . LEU   A 1 242 ? 9.508   14.570 14.163  1.00 64.17  ? 242 LEU   A CD2  1 
ATOM   1893 N  N    . THR   A 1 243 ? 10.261  16.675 9.558   1.00 77.13  ? 243 THR   A N    1 
ATOM   1894 C  CA   . THR   A 1 243 ? 11.529  17.104 8.989   1.00 89.26  ? 243 THR   A CA   1 
ATOM   1895 C  C    . THR   A 1 243 ? 12.548  17.332 10.097  1.00 86.48  ? 243 THR   A C    1 
ATOM   1896 O  O    . THR   A 1 243 ? 12.195  17.642 11.237  1.00 84.71  ? 243 THR   A O    1 
ATOM   1897 C  CB   . THR   A 1 243 ? 11.354  18.386 8.172   1.00 90.68  ? 243 THR   A CB   1 
ATOM   1898 O  OG1  . THR   A 1 243 ? 11.348  19.518 9.051   1.00 95.70  ? 243 THR   A OG1  1 
ATOM   1899 C  CG2  . THR   A 1 243 ? 10.047  18.351 7.392   1.00 80.06  ? 243 THR   A CG2  1 
ATOM   1900 N  N    . GLN   A 1 244 ? 13.828  17.174 9.751   1.00 92.57  ? 244 GLN   A N    1 
ATOM   1901 C  CA   . GLN   A 1 244 ? 14.872  17.438 10.735  1.00 90.86  ? 244 GLN   A CA   1 
ATOM   1902 C  C    . GLN   A 1 244 ? 14.808  18.874 11.239  1.00 92.15  ? 244 GLN   A C    1 
ATOM   1903 O  O    . GLN   A 1 244 ? 15.211  19.153 12.374  1.00 94.01  ? 244 GLN   A O    1 
ATOM   1904 C  CB   . GLN   A 1 244 ? 16.247  17.135 10.147  1.00 82.58  ? 244 GLN   A CB   1 
ATOM   1905 C  CG   . GLN   A 1 244 ? 17.405  17.477 11.071  1.00 93.15  ? 244 GLN   A CG   1 
ATOM   1906 C  CD   . GLN   A 1 244 ? 17.216  16.933 12.477  1.00 93.43  ? 244 GLN   A CD   1 
ATOM   1907 O  OE1  . GLN   A 1 244 ? 16.685  15.838 12.666  1.00 91.49  ? 244 GLN   A OE1  1 
ATOM   1908 N  NE2  . GLN   A 1 244 ? 17.654  17.697 13.471  1.00 93.60  ? 244 GLN   A NE2  1 
ATOM   1909 N  N    . ASP   A 1 245 ? 14.295  19.793 10.422  1.00 91.19  ? 245 ASP   A N    1 
ATOM   1910 C  CA   . ASP   A 1 245 ? 14.100  21.164 10.877  1.00 89.56  ? 245 ASP   A CA   1 
ATOM   1911 C  C    . ASP   A 1 245 ? 12.914  21.269 11.831  1.00 88.35  ? 245 ASP   A C    1 
ATOM   1912 O  O    . ASP   A 1 245 ? 12.967  22.025 12.808  1.00 85.38  ? 245 ASP   A O    1 
ATOM   1913 C  CB   . ASP   A 1 245 ? 13.909  22.091 9.678   1.00 100.76 ? 245 ASP   A CB   1 
ATOM   1914 C  CG   . ASP   A 1 245 ? 13.158  23.350 10.034  1.00 106.78 ? 245 ASP   A CG   1 
ATOM   1915 O  OD1  . ASP   A 1 245 ? 13.774  24.246 10.648  1.00 111.70 ? 245 ASP   A OD1  1 
ATOM   1916 O  OD2  . ASP   A 1 245 ? 11.955  23.439 9.710   1.00 105.82 ? 245 ASP   A OD2  1 
ATOM   1917 N  N    . HIS   A 1 246 ? 11.839  20.519 11.566  1.00 87.98  ? 246 HIS   A N    1 
ATOM   1918 C  CA   . HIS   A 1 246 ? 10.727  20.458 12.509  1.00 81.49  ? 246 HIS   A CA   1 
ATOM   1919 C  C    . HIS   A 1 246 ? 11.192  20.027 13.891  1.00 73.28  ? 246 HIS   A C    1 
ATOM   1920 O  O    . HIS   A 1 246 ? 10.596  20.419 14.902  1.00 73.43  ? 246 HIS   A O    1 
ATOM   1921 C  CB   . HIS   A 1 246 ? 9.656   19.492 12.004  1.00 77.34  ? 246 HIS   A CB   1 
ATOM   1922 C  CG   . HIS   A 1 246 ? 8.496   20.167 11.345  1.00 82.56  ? 246 HIS   A CG   1 
ATOM   1923 N  ND1  . HIS   A 1 246 ? 7.587   19.487 10.562  1.00 75.45  ? 246 HIS   A ND1  1 
ATOM   1924 C  CD2  . HIS   A 1 246 ? 8.097   21.461 11.348  1.00 79.02  ? 246 HIS   A CD2  1 
ATOM   1925 C  CE1  . HIS   A 1 246 ? 6.677   20.332 10.114  1.00 69.03  ? 246 HIS   A CE1  1 
ATOM   1926 N  NE2  . HIS   A 1 246 ? 6.963   21.537 10.576  1.00 74.85  ? 246 HIS   A NE2  1 
ATOM   1927 N  N    . VAL   A 1 247 ? 12.247  19.213 13.952  1.00 70.68  ? 247 VAL   A N    1 
ATOM   1928 C  CA   . VAL   A 1 247 ? 12.786  18.781 15.236  1.00 79.33  ? 247 VAL   A CA   1 
ATOM   1929 C  C    . VAL   A 1 247 ? 13.458  19.945 15.954  1.00 72.49  ? 247 VAL   A C    1 
ATOM   1930 O  O    . VAL   A 1 247 ? 13.377  20.064 17.182  1.00 72.26  ? 247 VAL   A O    1 
ATOM   1931 C  CB   . VAL   A 1 247 ? 13.759  17.605 15.031  1.00 77.72  ? 247 VAL   A CB   1 
ATOM   1932 C  CG1  . VAL   A 1 247 ? 14.807  17.586 16.130  1.00 78.87  ? 247 VAL   A CG1  1 
ATOM   1933 C  CG2  . VAL   A 1 247 ? 12.999  16.293 14.981  1.00 73.06  ? 247 VAL   A CG2  1 
ATOM   1934 N  N    . ASP   A 1 248 ? 14.135  20.817 15.207  1.00 74.08  ? 248 ASP   A N    1 
ATOM   1935 C  CA   . ASP   A 1 248 ? 14.879  21.901 15.841  1.00 72.42  ? 248 ASP   A CA   1 
ATOM   1936 C  C    . ASP   A 1 248 ? 13.949  22.869 16.563  1.00 75.06  ? 248 ASP   A C    1 
ATOM   1937 O  O    . ASP   A 1 248 ? 14.276  23.355 17.652  1.00 76.68  ? 248 ASP   A O    1 
ATOM   1938 C  CB   . ASP   A 1 248 ? 15.726  22.634 14.802  1.00 74.11  ? 248 ASP   A CB   1 
ATOM   1939 C  CG   . ASP   A 1 248 ? 16.591  21.688 13.988  1.00 88.75  ? 248 ASP   A CG   1 
ATOM   1940 O  OD1  . ASP   A 1 248 ? 16.936  20.605 14.507  1.00 94.71  ? 248 ASP   A OD1  1 
ATOM   1941 O  OD2  . ASP   A 1 248 ? 16.933  22.025 12.834  1.00 85.44  ? 248 ASP   A OD2  1 
ATOM   1942 N  N    . ILE   A 1 249 ? 12.780  23.153 15.983  1.00 70.66  ? 249 ILE   A N    1 
ATOM   1943 C  CA   . ILE   A 1 249 ? 11.859  24.090 16.620  1.00 71.19  ? 249 ILE   A CA   1 
ATOM   1944 C  C    . ILE   A 1 249 ? 11.404  23.561 17.974  1.00 66.96  ? 249 ILE   A C    1 
ATOM   1945 O  O    . ILE   A 1 249 ? 11.106  24.341 18.887  1.00 67.25  ? 249 ILE   A O    1 
ATOM   1946 C  CB   . ILE   A 1 249 ? 10.663  24.388 15.692  1.00 74.29  ? 249 ILE   A CB   1 
ATOM   1947 C  CG1  . ILE   A 1 249 ? 9.864   25.583 16.219  1.00 73.59  ? 249 ILE   A CG1  1 
ATOM   1948 C  CG2  . ILE   A 1 249 ? 9.765   23.168 15.558  1.00 62.90  ? 249 ILE   A CG2  1 
ATOM   1949 C  CD1  . ILE   A 1 249 ? 8.522   25.767 15.545  1.00 72.62  ? 249 ILE   A CD1  1 
ATOM   1950 N  N    . LEU   A 1 250 ? 11.357  22.239 18.134  1.00 62.91  ? 250 LEU   A N    1 
ATOM   1951 C  CA   . LEU   A 1 250 ? 11.000  21.614 19.402  1.00 61.16  ? 250 LEU   A CA   1 
ATOM   1952 C  C    . LEU   A 1 250 ? 12.160  21.574 20.396  1.00 56.37  ? 250 LEU   A C    1 
ATOM   1953 O  O    . LEU   A 1 250 ? 12.027  20.956 21.454  1.00 56.76  ? 250 LEU   A O    1 
ATOM   1954 C  CB   . LEU   A 1 250 ? 10.482  20.193 19.157  1.00 55.04  ? 250 LEU   A CB   1 
ATOM   1955 C  CG   . LEU   A 1 250 ? 9.149   20.052 18.421  1.00 54.20  ? 250 LEU   A CG   1 
ATOM   1956 C  CD1  . LEU   A 1 250 ? 8.943   18.630 17.924  1.00 49.37  ? 250 LEU   A CD1  1 
ATOM   1957 C  CD2  . LEU   A 1 250 ? 7.994   20.464 19.319  1.00 56.89  ? 250 LEU   A CD2  1 
ATOM   1958 N  N    . GLY   A 1 251 ? 13.285  22.213 20.085  1.00 65.99  ? 251 GLY   A N    1 
ATOM   1959 C  CA   . GLY   A 1 251 ? 14.441  22.199 20.951  1.00 60.00  ? 251 GLY   A CA   1 
ATOM   1960 C  C    . GLY   A 1 251 ? 14.163  22.760 22.332  1.00 63.07  ? 251 GLY   A C    1 
ATOM   1961 O  O    . GLY   A 1 251 ? 14.385  22.098 23.352  1.00 61.74  ? 251 GLY   A O    1 
ATOM   1962 N  N    . PRO   A 1 252 ? 13.678  24.005 22.391  1.00 67.15  ? 252 PRO   A N    1 
ATOM   1963 C  CA   . PRO   A 1 252 ? 13.382  24.611 23.702  1.00 62.78  ? 252 PRO   A CA   1 
ATOM   1964 C  C    . PRO   A 1 252 ? 12.507  23.745 24.592  1.00 58.45  ? 252 PRO   A C    1 
ATOM   1965 O  O    . PRO   A 1 252 ? 12.779  23.626 25.793  1.00 64.61  ? 252 PRO   A O    1 
ATOM   1966 C  CB   . PRO   A 1 252 ? 12.687  25.926 23.325  1.00 68.62  ? 252 PRO   A CB   1 
ATOM   1967 C  CG   . PRO   A 1 252 ? 13.186  26.238 21.956  1.00 63.15  ? 252 PRO   A CG   1 
ATOM   1968 C  CD   . PRO   A 1 252 ? 13.382  24.918 21.274  1.00 61.91  ? 252 PRO   A CD   1 
ATOM   1969 N  N    . LEU   A 1 253 ? 11.458  23.134 24.036  1.00 59.02  ? 253 LEU   A N    1 
ATOM   1970 C  CA   . LEU   A 1 253 ? 10.603  22.269 24.841  1.00 61.79  ? 253 LEU   A CA   1 
ATOM   1971 C  C    . LEU   A 1 253 ? 11.346  21.013 25.275  1.00 62.07  ? 253 LEU   A C    1 
ATOM   1972 O  O    . LEU   A 1 253 ? 11.141  20.513 26.388  1.00 57.56  ? 253 LEU   A O    1 
ATOM   1973 C  CB   . LEU   A 1 253 ? 9.342   21.903 24.059  1.00 59.98  ? 253 LEU   A CB   1 
ATOM   1974 C  CG   . LEU   A 1 253 ? 8.375   23.055 23.784  1.00 55.75  ? 253 LEU   A CG   1 
ATOM   1975 C  CD1  . LEU   A 1 253 ? 7.311   22.632 22.784  1.00 42.80  ? 253 LEU   A CD1  1 
ATOM   1976 C  CD2  . LEU   A 1 253 ? 7.735   23.542 25.075  1.00 54.03  ? 253 LEU   A CD2  1 
ATOM   1977 N  N    . SER   A 1 254 ? 12.214  20.487 24.409  1.00 59.88  ? 254 SER   A N    1 
ATOM   1978 C  CA   . SER   A 1 254 ? 12.970  19.293 24.768  1.00 59.68  ? 254 SER   A CA   1 
ATOM   1979 C  C    . SER   A 1 254 ? 13.924  19.575 25.921  1.00 57.28  ? 254 SER   A C    1 
ATOM   1980 O  O    . SER   A 1 254 ? 14.088  18.742 26.821  1.00 61.91  ? 254 SER   A O    1 
ATOM   1981 C  CB   . SER   A 1 254 ? 13.734  18.770 23.552  1.00 60.01  ? 254 SER   A CB   1 
ATOM   1982 O  OG   . SER   A 1 254 ? 14.547  17.664 23.905  1.00 62.64  ? 254 SER   A OG   1 
ATOM   1983 N  N    . ALA   A 1 255 ? 14.559  20.748 25.916  1.00 62.20  ? 255 ALA   A N    1 
ATOM   1984 C  CA   . ALA   A 1 255 ? 15.531  21.064 26.958  1.00 60.76  ? 255 ALA   A CA   1 
ATOM   1985 C  C    . ALA   A 1 255 ? 14.846  21.349 28.287  1.00 66.00  ? 255 ALA   A C    1 
ATOM   1986 O  O    . ALA   A 1 255 ? 15.304  20.889 29.340  1.00 64.77  ? 255 ALA   A O    1 
ATOM   1987 C  CB   . ALA   A 1 255 ? 16.394  22.252 26.532  1.00 55.02  ? 255 ALA   A CB   1 
ATOM   1988 N  N    . GLN   A 1 256 ? 13.745  22.101 28.260  1.00 65.12  ? 256 GLN   A N    1 
ATOM   1989 C  CA   . GLN   A 1 256 ? 13.056  22.433 29.502  1.00 61.30  ? 256 GLN   A CA   1 
ATOM   1990 C  C    . GLN   A 1 256 ? 12.492  21.193 30.187  1.00 60.16  ? 256 GLN   A C    1 
ATOM   1991 O  O    . GLN   A 1 256 ? 12.296  21.197 31.407  1.00 58.11  ? 256 GLN   A O    1 
ATOM   1992 C  CB   . GLN   A 1 256 ? 11.942  23.440 29.229  1.00 57.92  ? 256 GLN   A CB   1 
ATOM   1993 C  CG   . GLN   A 1 256 ? 11.196  23.869 30.470  1.00 58.48  ? 256 GLN   A CG   1 
ATOM   1994 C  CD   . GLN   A 1 256 ? 9.844   24.465 30.152  1.00 75.08  ? 256 GLN   A CD   1 
ATOM   1995 O  OE1  . GLN   A 1 256 ? 9.521   24.719 28.990  1.00 79.12  ? 256 GLN   A OE1  1 
ATOM   1996 N  NE2  . GLN   A 1 256 ? 9.039   24.684 31.184  1.00 74.26  ? 256 GLN   A NE2  1 
ATOM   1997 N  N    . THR   A 1 257 ? 12.216  20.129 29.428  1.00 64.87  ? 257 THR   A N    1 
ATOM   1998 C  CA   . THR   A 1 257 ? 11.696  18.892 30.001  1.00 62.06  ? 257 THR   A CA   1 
ATOM   1999 C  C    . THR   A 1 257 ? 12.735  17.783 30.102  1.00 59.45  ? 257 THR   A C    1 
ATOM   2000 O  O    . THR   A 1 257 ? 12.499  16.804 30.815  1.00 57.22  ? 257 THR   A O    1 
ATOM   2001 C  CB   . THR   A 1 257 ? 10.513  18.364 29.180  1.00 53.02  ? 257 THR   A CB   1 
ATOM   2002 O  OG1  . THR   A 1 257 ? 10.989  17.859 27.925  1.00 57.99  ? 257 THR   A OG1  1 
ATOM   2003 C  CG2  . THR   A 1 257 ? 9.490   19.465 28.934  1.00 60.82  ? 257 THR   A CG2  1 
ATOM   2004 N  N    . GLY   A 1 258 ? 13.858  17.900 29.398  1.00 65.92  ? 258 GLY   A N    1 
ATOM   2005 C  CA   . GLY   A 1 258 ? 14.851  16.844 29.404  1.00 54.71  ? 258 GLY   A CA   1 
ATOM   2006 C  C    . GLY   A 1 258 ? 14.431  15.573 28.698  1.00 65.31  ? 258 GLY   A C    1 
ATOM   2007 O  O    . GLY   A 1 258 ? 14.875  14.486 29.081  1.00 73.10  ? 258 GLY   A O    1 
ATOM   2008 N  N    . ILE   A 1 259 ? 13.586  15.673 27.675  1.00 62.02  ? 259 ILE   A N    1 
ATOM   2009 C  CA   . ILE   A 1 259 ? 13.128  14.514 26.917  1.00 61.97  ? 259 ILE   A CA   1 
ATOM   2010 C  C    . ILE   A 1 259 ? 13.523  14.722 25.462  1.00 63.76  ? 259 ILE   A C    1 
ATOM   2011 O  O    . ILE   A 1 259 ? 13.058  15.669 24.816  1.00 60.30  ? 259 ILE   A O    1 
ATOM   2012 C  CB   . ILE   A 1 259 ? 11.614  14.297 27.057  1.00 57.92  ? 259 ILE   A CB   1 
ATOM   2013 C  CG1  . ILE   A 1 259 ? 11.269  13.911 28.496  1.00 53.66  ? 259 ILE   A CG1  1 
ATOM   2014 C  CG2  . ILE   A 1 259 ? 11.144  13.206 26.108  1.00 47.06  ? 259 ILE   A CG2  1 
ATOM   2015 C  CD1  . ILE   A 1 259 ? 9.792   13.992 28.807  1.00 58.33  ? 259 ILE   A CD1  1 
ATOM   2016 N  N    . ALA   A 1 260 ? 14.388  13.845 24.955  1.00 65.52  ? 260 ALA   A N    1 
ATOM   2017 C  CA   . ALA   A 1 260 ? 14.842  13.952 23.576  1.00 65.24  ? 260 ALA   A CA   1 
ATOM   2018 C  C    . ALA   A 1 260 ? 13.655  13.917 22.623  1.00 60.72  ? 260 ALA   A C    1 
ATOM   2019 O  O    . ALA   A 1 260 ? 12.689  13.178 22.833  1.00 62.25  ? 260 ALA   A O    1 
ATOM   2020 C  CB   . ALA   A 1 260 ? 15.816  12.819 23.249  1.00 57.23  ? 260 ALA   A CB   1 
ATOM   2021 N  N    . VAL   A 1 261 ? 13.732  14.728 21.567  1.00 59.32  ? 261 VAL   A N    1 
ATOM   2022 C  CA   . VAL   A 1 261 ? 12.632  14.800 20.610  1.00 59.37  ? 261 VAL   A CA   1 
ATOM   2023 C  C    . VAL   A 1 261 ? 12.308  13.414 20.062  1.00 59.59  ? 261 VAL   A C    1 
ATOM   2024 O  O    . VAL   A 1 261 ? 11.140  13.015 20.000  1.00 56.57  ? 261 VAL   A O    1 
ATOM   2025 C  CB   . VAL   A 1 261 ? 12.965  15.799 19.486  1.00 66.85  ? 261 VAL   A CB   1 
ATOM   2026 C  CG1  . VAL   A 1 261 ? 11.835  15.855 18.467  1.00 51.60  ? 261 VAL   A CG1  1 
ATOM   2027 C  CG2  . VAL   A 1 261 ? 13.232  17.180 20.069  1.00 59.34  ? 261 VAL   A CG2  1 
ATOM   2028 N  N    . LEU   A 1 262 ? 13.332  12.650 19.673  1.00 57.95  ? 262 LEU   A N    1 
ATOM   2029 C  CA   . LEU   A 1 262 ? 13.077  11.310 19.156  1.00 65.75  ? 262 LEU   A CA   1 
ATOM   2030 C  C    . LEU   A 1 262 ? 12.531  10.371 20.222  1.00 63.14  ? 262 LEU   A C    1 
ATOM   2031 O  O    . LEU   A 1 262 ? 11.838  9.405  19.884  1.00 61.90  ? 262 LEU   A O    1 
ATOM   2032 C  CB   . LEU   A 1 262 ? 14.347  10.728 18.535  1.00 62.11  ? 262 LEU   A CB   1 
ATOM   2033 C  CG   . LEU   A 1 262 ? 14.948  11.525 17.373  1.00 79.80  ? 262 LEU   A CG   1 
ATOM   2034 C  CD1  . LEU   A 1 262 ? 13.856  11.929 16.384  1.00 68.09  ? 262 LEU   A CD1  1 
ATOM   2035 C  CD2  . LEU   A 1 262 ? 15.731  12.744 17.855  1.00 77.96  ? 262 LEU   A CD2  1 
ATOM   2036 N  N    . ASP   A 1 263 ? 12.820  10.625 21.498  1.00 62.11  ? 263 ASP   A N    1 
ATOM   2037 C  CA   . ASP   A 1 263 ? 12.163  9.860  22.550  1.00 62.94  ? 263 ASP   A CA   1 
ATOM   2038 C  C    . ASP   A 1 263 ? 10.678  10.191 22.611  1.00 60.02  ? 263 ASP   A C    1 
ATOM   2039 O  O    . ASP   A 1 263 ? 9.839   9.296  22.770  1.00 56.75  ? 263 ASP   A O    1 
ATOM   2040 C  CB   . ASP   A 1 263 ? 12.834  10.124 23.897  1.00 59.53  ? 263 ASP   A CB   1 
ATOM   2041 C  CG   . ASP   A 1 263 ? 14.224  9.521  23.981  1.00 78.74  ? 263 ASP   A CG   1 
ATOM   2042 O  OD1  . ASP   A 1 263 ? 14.473  8.510  23.288  1.00 82.41  ? 263 ASP   A OD1  1 
ATOM   2043 O  OD2  . ASP   A 1 263 ? 15.065  10.051 24.738  1.00 83.73  ? 263 ASP   A OD2  1 
ATOM   2044 N  N    . MET   A 1 264 ? 10.331  11.471 22.470  1.00 56.35  ? 264 MET   A N    1 
ATOM   2045 C  CA   . MET   A 1 264 ? 8.920   11.826 22.416  1.00 59.08  ? 264 MET   A CA   1 
ATOM   2046 C  C    . MET   A 1 264 ? 8.261   11.244 21.172  1.00 54.55  ? 264 MET   A C    1 
ATOM   2047 O  O    . MET   A 1 264 ? 7.074   10.901 21.201  1.00 54.44  ? 264 MET   A O    1 
ATOM   2048 C  CB   . MET   A 1 264 ? 8.750   13.343 22.449  1.00 47.61  ? 264 MET   A CB   1 
ATOM   2049 C  CG   . MET   A 1 264 ? 7.323   13.771 22.714  1.00 47.06  ? 264 MET   A CG   1 
ATOM   2050 S  SD   . MET   A 1 264 ? 6.839   13.287 24.386  1.00 54.89  ? 264 MET   A SD   1 
ATOM   2051 C  CE   . MET   A 1 264 ? 7.078   14.829 25.272  1.00 46.39  ? 264 MET   A CE   1 
ATOM   2052 N  N    . CYS   A 1 265 ? 9.017   11.119 20.076  1.00 52.71  ? 265 CYS   A N    1 
ATOM   2053 C  CA   . CYS   A 1 265 ? 8.496   10.441 18.894  1.00 48.32  ? 265 CYS   A CA   1 
ATOM   2054 C  C    . CYS   A 1 265 ? 8.203   8.979  19.185  1.00 56.46  ? 265 CYS   A C    1 
ATOM   2055 O  O    . CYS   A 1 265 ? 7.206   8.432  18.700  1.00 49.33  ? 265 CYS   A O    1 
ATOM   2056 C  CB   . CYS   A 1 265 ? 9.482   10.564 17.732  1.00 58.06  ? 265 CYS   A CB   1 
ATOM   2057 S  SG   . CYS   A 1 265 ? 9.699   12.237 17.092  1.00 65.57  ? 265 CYS   A SG   1 
ATOM   2058 N  N    . ALA   A 1 266 ? 9.073   8.322  19.961  1.00 53.82  ? 266 ALA   A N    1 
ATOM   2059 C  CA   . ALA   A 1 266 ? 8.827   6.933  20.328  1.00 57.62  ? 266 ALA   A CA   1 
ATOM   2060 C  C    . ALA   A 1 266 ? 7.491   6.786  21.043  1.00 56.38  ? 266 ALA   A C    1 
ATOM   2061 O  O    . ALA   A 1 266 ? 6.729   5.856  20.762  1.00 62.19  ? 266 ALA   A O    1 
ATOM   2062 C  CB   . ALA   A 1 266 ? 9.968   6.405  21.199  1.00 61.79  ? 266 ALA   A CB   1 
ATOM   2063 N  N    . SER   A 1 267 ? 7.185   7.702  21.965  1.00 57.60  ? 267 SER   A N    1 
ATOM   2064 C  CA   . SER   A 1 267 ? 5.889   7.660  22.633  1.00 56.53  ? 267 SER   A CA   1 
ATOM   2065 C  C    . SER   A 1 267 ? 4.752   7.884  21.644  1.00 57.95  ? 267 SER   A C    1 
ATOM   2066 O  O    . SER   A 1 267 ? 3.714   7.216  21.718  1.00 59.50  ? 267 SER   A O    1 
ATOM   2067 C  CB   . SER   A 1 267 ? 5.843   8.696  23.756  1.00 57.96  ? 267 SER   A CB   1 
ATOM   2068 O  OG   . SER   A 1 267 ? 6.868   8.455  24.708  1.00 74.23  ? 267 SER   A OG   1 
ATOM   2069 N  N    . LEU   A 1 268 ? 4.924   8.821  20.709  1.00 52.76  ? 268 LEU   A N    1 
ATOM   2070 C  CA   . LEU   A 1 268 ? 3.873   9.058  19.726  1.00 56.63  ? 268 LEU   A CA   1 
ATOM   2071 C  C    . LEU   A 1 268 ? 3.611   7.807  18.895  1.00 53.91  ? 268 LEU   A C    1 
ATOM   2072 O  O    . LEU   A 1 268 ? 2.455   7.431  18.673  1.00 46.15  ? 268 LEU   A O    1 
ATOM   2073 C  CB   . LEU   A 1 268 ? 4.242   10.241 18.829  1.00 52.53  ? 268 LEU   A CB   1 
ATOM   2074 C  CG   . LEU   A 1 268 ? 3.175   10.712 17.837  1.00 46.34  ? 268 LEU   A CG   1 
ATOM   2075 C  CD1  . LEU   A 1 268 ? 1.815   10.731 18.501  1.00 45.22  ? 268 LEU   A CD1  1 
ATOM   2076 C  CD2  . LEU   A 1 268 ? 3.509   12.087 17.269  1.00 45.99  ? 268 LEU   A CD2  1 
ATOM   2077 N  N    . LYS   A 1 269 ? 4.670   7.133  18.448  1.00 52.13  ? 269 LYS   A N    1 
ATOM   2078 C  CA   . LYS   A 1 269 ? 4.480   5.909  17.677  1.00 55.92  ? 269 LYS   A CA   1 
ATOM   2079 C  C    . LYS   A 1 269 ? 3.668   4.891  18.469  1.00 57.10  ? 269 LYS   A C    1 
ATOM   2080 O  O    . LYS   A 1 269 ? 2.699   4.319  17.958  1.00 56.17  ? 269 LYS   A O    1 
ATOM   2081 C  CB   . LYS   A 1 269 ? 5.832   5.328  17.261  1.00 59.71  ? 269 LYS   A CB   1 
ATOM   2082 C  CG   . LYS   A 1 269 ? 5.726   3.982  16.572  1.00 69.87  ? 269 LYS   A CG   1 
ATOM   2083 C  CD   . LYS   A 1 269 ? 7.014   3.184  16.672  1.00 69.30  ? 269 LYS   A CD   1 
ATOM   2084 C  CE   . LYS   A 1 269 ? 7.830   3.306  15.396  1.00 73.82  ? 269 LYS   A CE   1 
ATOM   2085 N  NZ   . LYS   A 1 269 ? 8.390   1.986  14.975  1.00 77.82  ? 269 LYS   A NZ   1 
ATOM   2086 N  N    . GLU   A 1 270 ? 4.031   4.667  19.734  1.00 57.69  ? 270 GLU   A N    1 
ATOM   2087 C  CA   . GLU   A 1 270 ? 3.298   3.690  20.536  1.00 68.38  ? 270 GLU   A CA   1 
ATOM   2088 C  C    . GLU   A 1 270 ? 1.856   4.129  20.765  1.00 58.79  ? 270 GLU   A C    1 
ATOM   2089 O  O    . GLU   A 1 270 ? 0.941   3.297  20.770  1.00 60.84  ? 270 GLU   A O    1 
ATOM   2090 C  CB   . GLU   A 1 270 ? 4.000   3.450  21.875  1.00 54.28  ? 270 GLU   A CB   1 
ATOM   2091 C  CG   . GLU   A 1 270 ? 5.515   3.525  21.811  1.00 70.76  ? 270 GLU   A CG   1 
ATOM   2092 C  CD   . GLU   A 1 270 ? 6.119   2.590  20.775  1.00 85.83  ? 270 GLU   A CD   1 
ATOM   2093 O  OE1  . GLU   A 1 270 ? 5.418   1.661  20.316  1.00 84.39  ? 270 GLU   A OE1  1 
ATOM   2094 O  OE2  . GLU   A 1 270 ? 7.299   2.794  20.414  1.00 81.33  ? 270 GLU   A OE2  1 
ATOM   2095 N  N    . LEU   A 1 271 ? 1.631   5.430  20.961  1.00 54.28  ? 271 LEU   A N    1 
ATOM   2096 C  CA   . LEU   A 1 271 ? 0.261   5.913  21.114  1.00 62.02  ? 271 LEU   A CA   1 
ATOM   2097 C  C    . LEU   A 1 271 ? -0.549  5.673  19.846  1.00 59.99  ? 271 LEU   A C    1 
ATOM   2098 O  O    . LEU   A 1 271 ? -1.748  5.370  19.909  1.00 57.19  ? 271 LEU   A O    1 
ATOM   2099 C  CB   . LEU   A 1 271 ? 0.254   7.397  21.480  1.00 56.61  ? 271 LEU   A CB   1 
ATOM   2100 C  CG   . LEU   A 1 271 ? 0.467   7.731  22.956  1.00 56.34  ? 271 LEU   A CG   1 
ATOM   2101 C  CD1  . LEU   A 1 271 ? 0.654   9.230  23.143  1.00 43.55  ? 271 LEU   A CD1  1 
ATOM   2102 C  CD2  . LEU   A 1 271 ? -0.682  7.211  23.809  1.00 46.35  ? 271 LEU   A CD2  1 
ATOM   2103 N  N    . LEU   A 1 272 ? 0.091   5.801  18.681  1.00 61.60  ? 272 LEU   A N    1 
ATOM   2104 C  CA   . LEU   A 1 272 ? -0.601  5.566  17.418  1.00 56.66  ? 272 LEU   A CA   1 
ATOM   2105 C  C    . LEU   A 1 272 ? -0.983  4.102  17.244  1.00 62.23  ? 272 LEU   A C    1 
ATOM   2106 O  O    . LEU   A 1 272 ? -1.973  3.799  16.569  1.00 67.88  ? 272 LEU   A O    1 
ATOM   2107 C  CB   . LEU   A 1 272 ? 0.274   6.010  16.246  1.00 57.08  ? 272 LEU   A CB   1 
ATOM   2108 C  CG   . LEU   A 1 272 ? 0.477   7.511  16.041  1.00 56.18  ? 272 LEU   A CG   1 
ATOM   2109 C  CD1  . LEU   A 1 272 ? 1.366   7.756  14.834  1.00 56.91  ? 272 LEU   A CD1  1 
ATOM   2110 C  CD2  . LEU   A 1 272 ? -0.858  8.217  15.882  1.00 60.70  ? 272 LEU   A CD2  1 
ATOM   2111 N  N    . GLN   A 1 273 ? -0.219  3.185  17.837  1.00 70.20  ? 273 GLN   A N    1 
ATOM   2112 C  CA   . GLN   A 1 273 ? -0.425  1.761  17.609  1.00 75.22  ? 273 GLN   A CA   1 
ATOM   2113 C  C    . GLN   A 1 273 ? -1.290  1.089  18.665  1.00 75.03  ? 273 GLN   A C    1 
ATOM   2114 O  O    . GLN   A 1 273 ? -1.834  0.012  18.399  1.00 80.22  ? 273 GLN   A O    1 
ATOM   2115 C  CB   . GLN   A 1 273 ? 0.924   1.038  17.530  1.00 73.21  ? 273 GLN   A CB   1 
ATOM   2116 C  CG   . GLN   A 1 273 ? 1.541   1.054  16.143  1.00 76.53  ? 273 GLN   A CG   1 
ATOM   2117 C  CD   . GLN   A 1 273 ? 3.055   1.018  16.177  1.00 79.43  ? 273 GLN   A CD   1 
ATOM   2118 O  OE1  . GLN   A 1 273 ? 3.663   0.952  17.244  1.00 73.81  ? 273 GLN   A OE1  1 
ATOM   2119 N  NE2  . GLN   A 1 273 ? 3.674   1.062  15.003  1.00 86.72  ? 273 GLN   A NE2  1 
ATOM   2120 N  N    . ASN   A 1 274 ? -1.431  1.689  19.847  1.00 74.98  ? 274 ASN   A N    1 
ATOM   2121 C  CA   . ASN   A 1 274 ? -2.222  1.111  20.927  1.00 72.50  ? 274 ASN   A CA   1 
ATOM   2122 C  C    . ASN   A 1 274 ? -3.343  2.030  21.396  1.00 76.52  ? 274 ASN   A C    1 
ATOM   2123 O  O    . ASN   A 1 274 ? -4.050  1.686  22.352  1.00 84.89  ? 274 ASN   A O    1 
ATOM   2124 C  CB   . ASN   A 1 274 ? -1.319  0.756  22.111  1.00 73.87  ? 274 ASN   A CB   1 
ATOM   2125 C  CG   . ASN   A 1 274 ? 0.030   0.224  21.675  1.00 82.40  ? 274 ASN   A CG   1 
ATOM   2126 O  OD1  . ASN   A 1 274 ? 0.138   -0.492 20.678  1.00 82.76  ? 274 ASN   A OD1  1 
ATOM   2127 N  ND2  . ASN   A 1 274 ? 1.072   0.585  22.414  1.00 78.78  ? 274 ASN   A ND2  1 
ATOM   2128 N  N    . GLY   A 1 275 ? -3.527  3.182  20.759  1.00 73.30  ? 275 GLY   A N    1 
ATOM   2129 C  CA   . GLY   A 1 275 ? -4.558  4.052  21.276  1.00 76.87  ? 275 GLY   A CA   1 
ATOM   2130 C  C    . GLY   A 1 275 ? -4.215  4.506  22.688  1.00 81.34  ? 275 GLY   A C    1 
ATOM   2131 O  O    . GLY   A 1 275 ? -3.081  4.385  23.160  1.00 69.67  ? 275 GLY   A O    1 
ATOM   2132 N  N    . MET   A 1 276 ? -5.232  5.034  23.372  1.00 91.09  ? 276 MET   A N    1 
ATOM   2133 C  CA   . MET   A 1 276 ? -5.058  5.537  24.726  1.00 92.76  ? 276 MET   A CA   1 
ATOM   2134 C  C    . MET   A 1 276 ? -5.739  4.690  25.789  1.00 96.20  ? 276 MET   A C    1 
ATOM   2135 O  O    . MET   A 1 276 ? -5.420  4.843  26.972  1.00 94.21  ? 276 MET   A O    1 
ATOM   2136 C  CB   . MET   A 1 276 ? -5.575  6.980  24.825  1.00 85.48  ? 276 MET   A CB   1 
ATOM   2137 C  CG   . MET   A 1 276 ? -4.963  7.909  23.793  1.00 81.29  ? 276 MET   A CG   1 
ATOM   2138 S  SD   . MET   A 1 276 ? -4.889  9.638  24.296  1.00 87.04  ? 276 MET   A SD   1 
ATOM   2139 C  CE   . MET   A 1 276 ? -4.902  9.487  26.081  1.00 79.92  ? 276 MET   A CE   1 
ATOM   2140 N  N    . ASN   A 1 277 ? -6.660  3.808  25.405  1.00 98.51  ? 277 ASN   A N    1 
ATOM   2141 C  CA   . ASN   A 1 277 ? -7.312  2.891  26.336  1.00 106.20 ? 277 ASN   A CA   1 
ATOM   2142 C  C    . ASN   A 1 277 ? -8.042  3.653  27.444  1.00 102.62 ? 277 ASN   A C    1 
ATOM   2143 O  O    . ASN   A 1 277 ? -7.797  3.463  28.636  1.00 106.89 ? 277 ASN   A O    1 
ATOM   2144 C  CB   . ASN   A 1 277 ? -6.298  1.904  26.926  1.00 110.61 ? 277 ASN   A CB   1 
ATOM   2145 C  CG   . ASN   A 1 277 ? -5.737  0.959  25.890  1.00 116.71 ? 277 ASN   A CG   1 
ATOM   2146 O  OD1  . ASN   A 1 277 ? -6.113  1.006  24.718  1.00 115.72 ? 277 ASN   A OD1  1 
ATOM   2147 N  ND2  . ASN   A 1 277 ? -4.832  0.088  26.317  1.00 118.55 ? 277 ASN   A ND2  1 
ATOM   2148 N  N    . GLY   A 1 278 ? -8.946  4.532  27.024  1.00 100.90 ? 278 GLY   A N    1 
ATOM   2149 C  CA   . GLY   A 1 278 ? -9.789  5.244  27.965  1.00 103.44 ? 278 GLY   A CA   1 
ATOM   2150 C  C    . GLY   A 1 278 ? -9.043  6.269  28.789  1.00 98.74  ? 278 GLY   A C    1 
ATOM   2151 O  O    . GLY   A 1 278 ? -9.656  7.065  29.509  1.00 96.48  ? 278 GLY   A O    1 
ATOM   2152 N  N    . ARG   A 1 279 ? -7.718  6.255  28.697  1.00 95.59  ? 279 ARG   A N    1 
ATOM   2153 C  CA   . ARG   A 1 279 ? -6.911  7.254  29.371  1.00 90.07  ? 279 ARG   A CA   1 
ATOM   2154 C  C    . ARG   A 1 279 ? -6.924  8.556  28.578  1.00 78.12  ? 279 ARG   A C    1 
ATOM   2155 O  O    . ARG   A 1 279 ? -7.277  8.592  27.397  1.00 78.87  ? 279 ARG   A O    1 
ATOM   2156 C  CB   . ARG   A 1 279 ? -5.479  6.755  29.564  1.00 87.04  ? 279 ARG   A CB   1 
ATOM   2157 C  CG   . ARG   A 1 279 ? -5.381  5.280  29.932  1.00 94.18  ? 279 ARG   A CG   1 
ATOM   2158 C  CD   . ARG   A 1 279 ? -4.022  4.930  30.523  1.00 90.55  ? 279 ARG   A CD   1 
ATOM   2159 N  NE   . ARG   A 1 279 ? -3.625  5.874  31.562  1.00 92.84  ? 279 ARG   A NE   1 
ATOM   2160 C  CZ   . ARG   A 1 279 ? -3.058  5.533  32.712  1.00 97.72  ? 279 ARG   A CZ   1 
ATOM   2161 N  NH1  . ARG   A 1 279 ? -2.793  4.269  33.007  1.00 98.04  ? 279 ARG   A NH1  1 
ATOM   2162 N  NH2  . ARG   A 1 279 ? -2.748  6.483  33.589  1.00 90.55  ? 279 ARG   A NH2  1 
ATOM   2163 N  N    . THR   A 1 280 ? -6.542  9.638  29.248  1.00 70.18  ? 280 THR   A N    1 
ATOM   2164 C  CA   . THR   A 1 280 ? -6.590  10.967 28.662  1.00 65.14  ? 280 THR   A CA   1 
ATOM   2165 C  C    . THR   A 1 280 ? -5.252  11.663 28.839  1.00 60.86  ? 280 THR   A C    1 
ATOM   2166 O  O    . THR   A 1 280 ? -4.475  11.352 29.746  1.00 59.02  ? 280 THR   A O    1 
ATOM   2167 C  CB   . THR   A 1 280 ? -7.684  11.833 29.293  1.00 61.47  ? 280 THR   A CB   1 
ATOM   2168 O  OG1  . THR   A 1 280 ? -7.386  12.035 30.680  1.00 64.09  ? 280 THR   A OG1  1 
ATOM   2169 C  CG2  . THR   A 1 280 ? -9.042  11.164 29.162  1.00 69.61  ? 280 THR   A CG2  1 
ATOM   2170 N  N    . ILE   A 1 281 ? -5.003  12.621 27.953  1.00 53.83  ? 281 ILE   A N    1 
ATOM   2171 C  CA   . ILE   A 1 281 ? -3.851  13.509 28.023  1.00 50.66  ? 281 ILE   A CA   1 
ATOM   2172 C  C    . ILE   A 1 281 ? -4.376  14.936 28.060  1.00 55.07  ? 281 ILE   A C    1 
ATOM   2173 O  O    . ILE   A 1 281 ? -5.036  15.385 27.113  1.00 48.15  ? 281 ILE   A O    1 
ATOM   2174 C  CB   . ILE   A 1 281 ? -2.900  13.309 26.834  1.00 46.40  ? 281 ILE   A CB   1 
ATOM   2175 C  CG1  . ILE   A 1 281 ? -2.438  11.852 26.751  1.00 48.37  ? 281 ILE   A CG1  1 
ATOM   2176 C  CG2  . ILE   A 1 281 ? -1.719  14.255 26.937  1.00 42.21  ? 281 ILE   A CG2  1 
ATOM   2177 C  CD1  . ILE   A 1 281 ? -1.356  11.618 25.709  1.00 39.70  ? 281 ILE   A CD1  1 
ATOM   2178 N  N    . LEU   A 1 282 ? -4.090  15.646 29.148  1.00 50.22  ? 282 LEU   A N    1 
ATOM   2179 C  CA   . LEU   A 1 282 ? -4.581  17.009 29.327  1.00 51.00  ? 282 LEU   A CA   1 
ATOM   2180 C  C    . LEU   A 1 282 ? -6.088  17.072 29.092  1.00 54.89  ? 282 LEU   A C    1 
ATOM   2181 O  O    . LEU   A 1 282 ? -6.601  17.951 28.397  1.00 48.49  ? 282 LEU   A O    1 
ATOM   2182 C  CB   . LEU   A 1 282 ? -3.845  17.985 28.409  1.00 48.90  ? 282 LEU   A CB   1 
ATOM   2183 C  CG   . LEU   A 1 282 ? -2.460  18.412 28.892  1.00 51.98  ? 282 LEU   A CG   1 
ATOM   2184 C  CD1  . LEU   A 1 282 ? -1.721  19.161 27.799  1.00 43.99  ? 282 LEU   A CD1  1 
ATOM   2185 C  CD2  . LEU   A 1 282 ? -2.575  19.256 30.156  1.00 48.15  ? 282 LEU   A CD2  1 
ATOM   2186 N  N    . GLY   A 1 283 ? -6.800  16.111 29.676  1.00 55.69  ? 283 GLY   A N    1 
ATOM   2187 C  CA   . GLY   A 1 283 ? -8.244  16.080 29.585  1.00 52.24  ? 283 GLY   A CA   1 
ATOM   2188 C  C    . GLY   A 1 283 ? -8.804  15.734 28.226  1.00 55.60  ? 283 GLY   A C    1 
ATOM   2189 O  O    . GLY   A 1 283 ? -10.003 15.927 28.003  1.00 58.29  ? 283 GLY   A O    1 
ATOM   2190 N  N    . SER   A 1 284 ? -7.982  15.226 27.309  1.00 60.34  ? 284 SER   A N    1 
ATOM   2191 C  CA   . SER   A 1 284 ? -8.414  14.880 25.961  1.00 56.33  ? 284 SER   A CA   1 
ATOM   2192 C  C    . SER   A 1 284 ? -8.139  13.410 25.678  1.00 56.46  ? 284 SER   A C    1 
ATOM   2193 O  O    . SER   A 1 284 ? -7.062  12.896 26.001  1.00 54.64  ? 284 SER   A O    1 
ATOM   2194 C  CB   . SER   A 1 284 ? -7.707  15.743 24.911  1.00 53.25  ? 284 SER   A CB   1 
ATOM   2195 O  OG   . SER   A 1 284 ? -8.012  15.298 23.597  1.00 54.27  ? 284 SER   A OG   1 
ATOM   2196 N  N    . ALA   A 1 285 ? -9.115  12.741 25.064  1.00 54.10  ? 285 ALA   A N    1 
ATOM   2197 C  CA   . ALA   A 1 285 ? -8.967  11.352 24.650  1.00 58.02  ? 285 ALA   A CA   1 
ATOM   2198 C  C    . ALA   A 1 285 ? -8.420  11.210 23.236  1.00 54.88  ? 285 ALA   A C    1 
ATOM   2199 O  O    . ALA   A 1 285 ? -8.175  10.083 22.793  1.00 68.68  ? 285 ALA   A O    1 
ATOM   2200 C  CB   . ALA   A 1 285 ? -10.307 10.618 24.753  1.00 52.91  ? 285 ALA   A CB   1 
ATOM   2201 N  N    . LEU   A 1 286 ? -8.236  12.315 22.522  1.00 51.87  ? 286 LEU   A N    1 
ATOM   2202 C  CA   . LEU   A 1 286 ? -7.600  12.337 21.214  1.00 48.03  ? 286 LEU   A CA   1 
ATOM   2203 C  C    . LEU   A 1 286 ? -6.253  13.037 21.307  1.00 48.84  ? 286 LEU   A C    1 
ATOM   2204 O  O    . LEU   A 1 286 ? -5.982  13.790 22.246  1.00 51.27  ? 286 LEU   A O    1 
ATOM   2205 C  CB   . LEU   A 1 286 ? -8.468  13.063 20.180  1.00 52.95  ? 286 LEU   A CB   1 
ATOM   2206 C  CG   . LEU   A 1 286 ? -9.848  12.505 19.853  1.00 64.51  ? 286 LEU   A CG   1 
ATOM   2207 C  CD1  . LEU   A 1 286 ? -10.485 13.339 18.755  1.00 58.68  ? 286 LEU   A CD1  1 
ATOM   2208 C  CD2  . LEU   A 1 286 ? -9.737  11.048 19.434  1.00 65.11  ? 286 LEU   A CD2  1 
ATOM   2209 N  N    . LEU   A 1 287 ? -5.413  12.796 20.306  1.00 43.89  ? 287 LEU   A N    1 
ATOM   2210 C  CA   . LEU   A 1 287 ? -4.162  13.529 20.178  1.00 45.97  ? 287 LEU   A CA   1 
ATOM   2211 C  C    . LEU   A 1 287 ? -4.446  14.880 19.527  1.00 52.87  ? 287 LEU   A C    1 
ATOM   2212 O  O    . LEU   A 1 287 ? -4.894  14.938 18.377  1.00 44.99  ? 287 LEU   A O    1 
ATOM   2213 C  CB   . LEU   A 1 287 ? -3.158  12.718 19.364  1.00 42.80  ? 287 LEU   A CB   1 
ATOM   2214 C  CG   . LEU   A 1 287 ? -2.893  11.322 19.944  1.00 42.89  ? 287 LEU   A CG   1 
ATOM   2215 C  CD1  . LEU   A 1 287 ? -2.211  10.430 18.924  1.00 42.70  ? 287 LEU   A CD1  1 
ATOM   2216 C  CD2  . LEU   A 1 287 ? -2.065  11.423 21.214  1.00 52.21  ? 287 LEU   A CD2  1 
ATOM   2217 N  N    . GLU   A 1 288 ? -4.209  15.963 20.267  1.00 47.36  ? 288 GLU   A N    1 
ATOM   2218 C  CA   . GLU   A 1 288 ? -4.525  17.300 19.780  1.00 40.84  ? 288 GLU   A CA   1 
ATOM   2219 C  C    . GLU   A 1 288 ? -3.415  17.828 18.883  1.00 44.06  ? 288 GLU   A C    1 
ATOM   2220 O  O    . GLU   A 1 288 ? -2.228  17.705 19.202  1.00 41.81  ? 288 GLU   A O    1 
ATOM   2221 C  CB   . GLU   A 1 288 ? -4.742  18.258 20.951  1.00 47.79  ? 288 GLU   A CB   1 
ATOM   2222 C  CG   . GLU   A 1 288 ? -5.861  17.851 21.890  1.00 56.23  ? 288 GLU   A CG   1 
ATOM   2223 C  CD   . GLU   A 1 288 ? -7.228  18.212 21.341  1.00 71.27  ? 288 GLU   A CD   1 
ATOM   2224 O  OE1  . GLU   A 1 288 ? -7.961  17.293 20.914  1.00 73.53  ? 288 GLU   A OE1  1 
ATOM   2225 O  OE2  . GLU   A 1 288 ? -7.564  19.415 21.322  1.00 77.20  ? 288 GLU   A OE2  1 
ATOM   2226 N  N    . ASP   A 1 289 ? -3.806  18.439 17.756  1.00 42.66  ? 289 ASP   A N    1 
ATOM   2227 C  CA   . ASP   A 1 289 ? -2.822  18.927 16.796  1.00 40.81  ? 289 ASP   A CA   1 
ATOM   2228 C  C    . ASP   A 1 289 ? -3.019  20.404 16.470  1.00 44.23  ? 289 ASP   A C    1 
ATOM   2229 O  O    . ASP   A 1 289 ? -2.532  20.870 15.433  1.00 40.53  ? 289 ASP   A O    1 
ATOM   2230 C  CB   . ASP   A 1 289 ? -2.851  18.085 15.512  1.00 41.62  ? 289 ASP   A CB   1 
ATOM   2231 C  CG   . ASP   A 1 289 ? -3.978  18.475 14.565  1.00 51.31  ? 289 ASP   A CG   1 
ATOM   2232 O  OD1  . ASP   A 1 289 ? -5.094  18.793 15.033  1.00 55.06  ? 289 ASP   A OD1  1 
ATOM   2233 O  OD2  . ASP   A 1 289 ? -3.751  18.423 13.338  1.00 53.23  ? 289 ASP   A OD2  1 
ATOM   2234 N  N    . GLU   A 1 290 ? -3.702  21.159 17.335  1.00 40.60  ? 290 GLU   A N    1 
ATOM   2235 C  CA   . GLU   A 1 290 ? -3.959  22.570 17.072  1.00 42.44  ? 290 GLU   A CA   1 
ATOM   2236 C  C    . GLU   A 1 290 ? -3.222  23.492 18.042  1.00 44.73  ? 290 GLU   A C    1 
ATOM   2237 O  O    . GLU   A 1 290 ? -3.607  24.654 18.200  1.00 43.96  ? 290 GLU   A O    1 
ATOM   2238 C  CB   . GLU   A 1 290 ? -5.461  22.854 17.101  1.00 45.05  ? 290 GLU   A CB   1 
ATOM   2239 C  CG   . GLU   A 1 290 ? -6.222  22.183 15.968  1.00 46.50  ? 290 GLU   A CG   1 
ATOM   2240 C  CD   . GLU   A 1 290 ? -7.287  23.071 15.338  1.00 66.08  ? 290 GLU   A CD   1 
ATOM   2241 O  OE1  . GLU   A 1 290 ? -7.746  24.030 16.000  1.00 53.55  ? 290 GLU   A OE1  1 
ATOM   2242 O  OE2  . GLU   A 1 290 ? -7.663  22.803 14.173  1.00 53.74  ? 290 GLU   A OE2  1 
ATOM   2243 N  N    . PHE   A 1 291 ? -2.173  22.999 18.696  1.00 39.75  ? 291 PHE   A N    1 
ATOM   2244 C  CA   . PHE   A 1 291 ? -1.286  23.822 19.512  1.00 42.24  ? 291 PHE   A CA   1 
ATOM   2245 C  C    . PHE   A 1 291 ? 0.111   23.769 18.911  1.00 43.18  ? 291 PHE   A C    1 
ATOM   2246 O  O    . PHE   A 1 291 ? 0.698   22.688 18.798  1.00 40.71  ? 291 PHE   A O    1 
ATOM   2247 C  CB   . PHE   A 1 291 ? -1.250  23.344 20.968  1.00 46.50  ? 291 PHE   A CB   1 
ATOM   2248 C  CG   . PHE   A 1 291 ? -2.574  23.413 21.672  1.00 40.18  ? 291 PHE   A CG   1 
ATOM   2249 C  CD1  . PHE   A 1 291 ? -3.022  24.608 22.210  1.00 44.84  ? 291 PHE   A CD1  1 
ATOM   2250 C  CD2  . PHE   A 1 291 ? -3.350  22.276 21.836  1.00 44.66  ? 291 PHE   A CD2  1 
ATOM   2251 C  CE1  . PHE   A 1 291 ? -4.235  24.677 22.878  1.00 52.77  ? 291 PHE   A CE1  1 
ATOM   2252 C  CE2  . PHE   A 1 291 ? -4.566  22.336 22.504  1.00 47.85  ? 291 PHE   A CE2  1 
ATOM   2253 C  CZ   . PHE   A 1 291 ? -5.008  23.539 23.025  1.00 54.10  ? 291 PHE   A CZ   1 
ATOM   2254 N  N    . THR   A 1 292 ? 0.642   24.926 18.529  1.00 40.88  ? 292 THR   A N    1 
ATOM   2255 C  CA   . THR   A 1 292 ? 2.000   25.007 18.011  1.00 43.40  ? 292 THR   A CA   1 
ATOM   2256 C  C    . THR   A 1 292 ? 3.006   24.987 19.153  1.00 46.60  ? 292 THR   A C    1 
ATOM   2257 O  O    . THR   A 1 292 ? 2.650   25.137 20.325  1.00 38.61  ? 292 THR   A O    1 
ATOM   2258 C  CB   . THR   A 1 292 ? 2.186   26.284 17.200  1.00 41.85  ? 292 THR   A CB   1 
ATOM   2259 O  OG1  . THR   A 1 292 ? 2.095   27.414 18.075  1.00 46.35  ? 292 THR   A OG1  1 
ATOM   2260 C  CG2  . THR   A 1 292 ? 1.130   26.400 16.112  1.00 43.35  ? 292 THR   A CG2  1 
ATOM   2261 N  N    . PRO   A 1 293 ? 4.291   24.813 18.839  1.00 48.93  ? 293 PRO   A N    1 
ATOM   2262 C  CA   . PRO   A 1 293 ? 5.314   24.998 19.880  1.00 42.80  ? 293 PRO   A CA   1 
ATOM   2263 C  C    . PRO   A 1 293 ? 5.245   26.366 20.541  1.00 46.97  ? 293 PRO   A C    1 
ATOM   2264 O  O    . PRO   A 1 293 ? 5.460   26.476 21.756  1.00 48.38  ? 293 PRO   A O    1 
ATOM   2265 C  CB   . PRO   A 1 293 ? 6.628   24.791 19.115  1.00 46.52  ? 293 PRO   A CB   1 
ATOM   2266 C  CG   . PRO   A 1 293 ? 6.257   23.911 17.969  1.00 54.33  ? 293 PRO   A CG   1 
ATOM   2267 C  CD   . PRO   A 1 293 ? 4.863   24.319 17.574  1.00 42.48  ? 293 PRO   A CD   1 
ATOM   2268 N  N    . PHE   A 1 294 ? 4.938   27.417 19.776  1.00 49.14  ? 294 PHE   A N    1 
ATOM   2269 C  CA   . PHE   A 1 294 ? 4.865   28.754 20.359  1.00 50.39  ? 294 PHE   A CA   1 
ATOM   2270 C  C    . PHE   A 1 294 ? 3.692   28.875 21.324  1.00 56.23  ? 294 PHE   A C    1 
ATOM   2271 O  O    . PHE   A 1 294 ? 3.826   29.472 22.400  1.00 51.33  ? 294 PHE   A O    1 
ATOM   2272 C  CB   . PHE   A 1 294 ? 4.769   29.802 19.254  1.00 47.53  ? 294 PHE   A CB   1 
ATOM   2273 C  CG   . PHE   A 1 294 ? 4.424   31.179 19.748  1.00 58.79  ? 294 PHE   A CG   1 
ATOM   2274 C  CD1  . PHE   A 1 294 ? 5.400   31.995 20.295  1.00 59.00  ? 294 PHE   A CD1  1 
ATOM   2275 C  CD2  . PHE   A 1 294 ? 3.132   31.669 19.640  1.00 60.60  ? 294 PHE   A CD2  1 
ATOM   2276 C  CE1  . PHE   A 1 294 ? 5.091   33.267 20.744  1.00 61.81  ? 294 PHE   A CE1  1 
ATOM   2277 C  CE2  . PHE   A 1 294 ? 2.816   32.942 20.084  1.00 62.30  ? 294 PHE   A CE2  1 
ATOM   2278 C  CZ   . PHE   A 1 294 ? 3.800   33.741 20.639  1.00 66.81  ? 294 PHE   A CZ   1 
ATOM   2279 N  N    . ASP   A 1 295 ? 2.535   28.310 20.965  1.00 50.35  ? 295 ASP   A N    1 
ATOM   2280 C  CA   . ASP   A 1 295 ? 1.402   28.319 21.885  1.00 50.22  ? 295 ASP   A CA   1 
ATOM   2281 C  C    . ASP   A 1 295 ? 1.754   27.618 23.191  1.00 51.04  ? 295 ASP   A C    1 
ATOM   2282 O  O    . ASP   A 1 295 ? 1.346   28.058 24.272  1.00 48.51  ? 295 ASP   A O    1 
ATOM   2283 C  CB   . ASP   A 1 295 ? 0.183   27.658 21.239  1.00 46.92  ? 295 ASP   A CB   1 
ATOM   2284 C  CG   . ASP   A 1 295 ? -0.306  28.400 20.007  1.00 57.09  ? 295 ASP   A CG   1 
ATOM   2285 O  OD1  . ASP   A 1 295 ? -0.424  29.645 20.067  1.00 66.33  ? 295 ASP   A OD1  1 
ATOM   2286 O  OD2  . ASP   A 1 295 ? -0.559  27.739 18.975  1.00 51.44  ? 295 ASP   A OD2  1 
ATOM   2287 N  N    . VAL   A 1 296 ? 2.515   26.524 23.114  1.00 47.90  ? 296 VAL   A N    1 
ATOM   2288 C  CA   . VAL   A 1 296 ? 2.867   25.787 24.324  1.00 48.95  ? 296 VAL   A CA   1 
ATOM   2289 C  C    . VAL   A 1 296 ? 3.748   26.643 25.226  1.00 53.67  ? 296 VAL   A C    1 
ATOM   2290 O  O    . VAL   A 1 296 ? 3.476   26.804 26.422  1.00 48.31  ? 296 VAL   A O    1 
ATOM   2291 C  CB   . VAL   A 1 296 ? 3.554   24.457 23.965  1.00 48.59  ? 296 VAL   A CB   1 
ATOM   2292 C  CG1  . VAL   A 1 296 ? 4.147   23.819 25.215  1.00 47.18  ? 296 VAL   A CG1  1 
ATOM   2293 C  CG2  . VAL   A 1 296 ? 2.570   23.516 23.281  1.00 42.68  ? 296 VAL   A CG2  1 
ATOM   2294 N  N    . VAL   A 1 297 ? 4.756   27.289 24.666  1.00 50.70  ? 297 VAL   A N    1 
ATOM   2295 C  CA   . VAL   A 1 297 ? 5.612   28.195 25.483  1.00 56.69  ? 297 VAL   A CA   1 
ATOM   2296 C  C    . VAL   A 1 297 ? 4.783   29.373 26.023  1.00 58.44  ? 297 VAL   A C    1 
ATOM   2297 O  O    . VAL   A 1 297 ? 4.963   29.711 27.197  1.00 61.82  ? 297 VAL   A O    1 
ATOM   2298 C  CB   . VAL   A 1 297 ? 6.831   28.654 24.663  1.00 58.55  ? 297 VAL   A CB   1 
ATOM   2299 C  CG1  . VAL   A 1 297 ? 7.634   29.720 25.388  1.00 61.49  ? 297 VAL   A CG1  1 
ATOM   2300 C  CG2  . VAL   A 1 297 ? 7.716   27.482 24.277  1.00 54.40  ? 297 VAL   A CG2  1 
ATOM   2301 N  N    . ARG   A 1 298 ? 3.906   29.961 25.211  1.00 60.20  ? 298 ARG   A N    1 
ATOM   2302 C  CA   . ARG   A 1 298 ? 3.066   31.124 25.606  1.00 59.65  ? 298 ARG   A CA   1 
ATOM   2303 C  C    . ARG   A 1 298 ? 2.237   30.799 26.840  1.00 58.65  ? 298 ARG   A C    1 
ATOM   2304 O  O    . ARG   A 1 298 ? 1.914   31.734 27.577  1.00 61.81  ? 298 ARG   A O    1 
ATOM   2305 C  CB   . ARG   A 1 298 ? 2.038   31.402 24.496  1.00 63.62  ? 298 ARG   A CB   1 
ATOM   2306 C  CG   . ARG   A 1 298 ? 1.862   32.820 23.953  1.00 65.50  ? 298 ARG   A CG   1 
ATOM   2307 C  CD   . ARG   A 1 298 ? 0.624   32.941 23.089  1.00 65.68  ? 298 ARG   A CD   1 
ATOM   2308 N  NE   . ARG   A 1 298 ? -0.447  33.675 23.745  1.00 77.51  ? 298 ARG   A NE   1 
ATOM   2309 C  CZ   . ARG   A 1 298 ? -1.711  33.275 23.789  1.00 73.02  ? 298 ARG   A CZ   1 
ATOM   2310 N  NH1  . ARG   A 1 298 ? -2.063  32.136 23.219  1.00 72.45  ? 298 ARG   A NH1  1 
ATOM   2311 N  NH2  . ARG   A 1 298 ? -2.618  34.012 24.404  1.00 66.69  ? 298 ARG   A NH2  1 
ATOM   2312 N  N    . GLN   A 1 299 ? 1.934   29.525 27.087  1.00 59.71  ? 299 GLN   A N    1 
ATOM   2313 C  CA   . GLN   A 1 299 ? 0.968   29.209 28.132  1.00 58.11  ? 299 GLN   A CA   1 
ATOM   2314 C  C    . GLN   A 1 299 ? 1.593   28.511 29.327  1.00 57.73  ? 299 GLN   A C    1 
ATOM   2315 O  O    . GLN   A 1 299 ? 1.217   28.786 30.471  1.00 65.73  ? 299 GLN   A O    1 
ATOM   2316 C  CB   . GLN   A 1 299 ? -0.148  28.319 27.577  1.00 51.30  ? 299 GLN   A CB   1 
ATOM   2317 C  CG   . GLN   A 1 299 ? -1.544  28.792 27.927  1.00 54.69  ? 299 GLN   A CG   1 
ATOM   2318 C  CD   . GLN   A 1 299 ? -2.619  27.907 27.330  1.00 59.48  ? 299 GLN   A CD   1 
ATOM   2319 O  OE1  . GLN   A 1 299 ? -2.812  27.869 26.114  1.00 57.70  ? 299 GLN   A OE1  1 
ATOM   2320 N  NE2  . GLN   A 1 299 ? -3.334  27.193 28.192  1.00 57.74  ? 299 GLN   A NE2  1 
ATOM   2321 N  N    . CYS   A 1 300 ? 2.531   27.606 29.087  1.00 56.77  ? 300 CYS   A N    1 
ATOM   2322 C  CA   . CYS   A 1 300 ? 3.066   26.778 30.150  1.00 60.03  ? 300 CYS   A CA   1 
ATOM   2323 C  C    . CYS   A 1 300 ? 4.145   27.521 30.922  1.00 65.59  ? 300 CYS   A C    1 
ATOM   2324 O  O    . CYS   A 1 300 ? 4.856   28.376 30.381  1.00 64.57  ? 300 CYS   A O    1 
ATOM   2325 C  CB   . CYS   A 1 300 ? 3.625   25.479 29.576  1.00 61.03  ? 300 CYS   A CB   1 
ATOM   2326 S  SG   . CYS   A 1 300 ? 2.331   24.367 29.006  1.00 54.60  ? 300 CYS   A SG   1 
ATOM   2327 N  N    . SER   A 1 301 ? 4.248   27.196 32.209  1.00 68.41  ? 301 SER   A N    1 
ATOM   2328 C  CA   . SER   A 1 301 ? 5.298   27.763 33.040  1.00 68.38  ? 301 SER   A CA   1 
ATOM   2329 C  C    . SER   A 1 301 ? 6.657   27.513 32.404  1.00 73.31  ? 301 SER   A C    1 
ATOM   2330 O  O    . SER   A 1 301 ? 6.839   26.569 31.628  1.00 64.07  ? 301 SER   A O    1 
ATOM   2331 C  CB   . SER   A 1 301 ? 5.246   27.154 34.446  1.00 71.57  ? 301 SER   A CB   1 
ATOM   2332 O  OG   . SER   A 1 301 ? 6.400   27.483 35.202  1.00 75.38  ? 301 SER   A OG   1 
ATOM   2333 N  N    . GLY   A 1 302 ? 7.613   28.389 32.715  1.00 76.30  ? 302 GLY   A N    1 
ATOM   2334 C  CA   . GLY   A 1 302 ? 8.987   28.135 32.326  1.00 81.36  ? 302 GLY   A CA   1 
ATOM   2335 C  C    . GLY   A 1 302 ? 9.675   27.068 33.149  1.00 81.95  ? 302 GLY   A C    1 
ATOM   2336 O  O    . GLY   A 1 302 ? 10.810  26.698 32.830  1.00 89.00  ? 302 GLY   A O    1 
ATOM   2337 N  N    . VAL   A 1 303 ? 9.015   26.568 34.191  1.00 86.64  ? 303 VAL   A N    1 
ATOM   2338 C  CA   . VAL   A 1 303 ? 9.552   25.534 35.067  1.00 90.06  ? 303 VAL   A CA   1 
ATOM   2339 C  C    . VAL   A 1 303 ? 8.602   24.344 35.037  1.00 87.35  ? 303 VAL   A C    1 
ATOM   2340 O  O    . VAL   A 1 303 ? 7.395   24.498 35.261  1.00 85.77  ? 303 VAL   A O    1 
ATOM   2341 C  CB   . VAL   A 1 303 ? 9.741   26.049 36.507  1.00 91.23  ? 303 VAL   A CB   1 
ATOM   2342 C  CG1  . VAL   A 1 303 ? 10.038  24.894 37.457  1.00 85.72  ? 303 VAL   A CG1  1 
ATOM   2343 C  CG2  . VAL   A 1 303 ? 10.848  27.091 36.554  1.00 92.13  ? 303 VAL   A CG2  1 
ATOM   2344 N  N    . THR   A 1 304 ? 9.147   23.161 34.761  1.00 82.75  ? 304 THR   A N    1 
ATOM   2345 C  CA   . THR   A 1 304 ? 8.360   21.938 34.729  1.00 77.17  ? 304 THR   A CA   1 
ATOM   2346 C  C    . THR   A 1 304 ? 8.042   21.467 36.146  1.00 83.70  ? 304 THR   A C    1 
ATOM   2347 O  O    . THR   A 1 304 ? 8.658   21.894 37.128  1.00 74.53  ? 304 THR   A O    1 
ATOM   2348 C  CB   . THR   A 1 304 ? 9.106   20.832 33.981  1.00 69.45  ? 304 THR   A CB   1 
ATOM   2349 O  OG1  . THR   A 1 304 ? 9.738   21.377 32.818  1.00 67.77  ? 304 THR   A OG1  1 
ATOM   2350 C  CG2  . THR   A 1 304 ? 8.140   19.733 33.555  1.00 71.88  ? 304 THR   A CG2  1 
ATOM   2351 N  N    . PHE   A 1 305 ? 7.072   20.564 36.242  1.00 75.84  ? 305 PHE   A N    1 
ATOM   2352 C  CA   . PHE   A 1 305 ? 6.698   19.987 37.526  1.00 86.07  ? 305 PHE   A CA   1 
ATOM   2353 C  C    . PHE   A 1 305 ? 7.878   19.270 38.177  1.00 89.83  ? 305 PHE   A C    1 
ATOM   2354 O  O    . PHE   A 1 305 ? 7.824   18.066 38.431  1.00 92.12  ? 305 PHE   A O    1 
ATOM   2355 C  CB   . PHE   A 1 305 ? 5.523   19.024 37.358  1.00 83.49  ? 305 PHE   A CB   1 
ATOM   2356 C  CG   . PHE   A 1 305 ? 4.493   19.136 38.442  1.00 86.56  ? 305 PHE   A CG   1 
ATOM   2357 C  CD1  . PHE   A 1 305 ? 4.863   19.489 39.730  1.00 85.05  ? 305 PHE   A CD1  1 
ATOM   2358 C  CD2  . PHE   A 1 305 ? 3.157   18.891 38.177  1.00 84.32  ? 305 PHE   A CD2  1 
ATOM   2359 C  CE1  . PHE   A 1 305 ? 3.921   19.591 40.734  1.00 81.33  ? 305 PHE   A CE1  1 
ATOM   2360 C  CE2  . PHE   A 1 305 ? 2.208   18.993 39.177  1.00 87.44  ? 305 PHE   A CE2  1 
ATOM   2361 C  CZ   . PHE   A 1 305 ? 2.591   19.344 40.457  1.00 90.05  ? 305 PHE   A CZ   1 
HETATM 2362 C  C14  . A1EGP B 2 .   ? -23.316 29.038 8.131   1.00 65.81  ? 401 A1EGP A C14  1 
HETATM 2363 C  C15  . A1EGP B 2 .   ? -21.518 31.842 0.445   1.00 54.26  ? 401 A1EGP A C15  1 
HETATM 2364 C  C16  . A1EGP B 2 .   ? -20.329 32.443 -0.312  1.00 58.44  ? 401 A1EGP A C16  1 
HETATM 2365 C  C35  . A1EGP B 2 .   ? -23.409 35.581 1.149   1.00 63.38  ? 401 A1EGP A C35  1 
HETATM 2366 C  C36  . A1EGP B 2 .   ? -24.800 35.684 1.011   1.00 64.58  ? 401 A1EGP A C36  1 
HETATM 2367 C  C37  . A1EGP B 2 .   ? -25.448 36.919 1.256   1.00 67.04  ? 401 A1EGP A C37  1 
HETATM 2368 C  C38  . A1EGP B 2 .   ? -24.704 38.034 1.633   1.00 64.70  ? 401 A1EGP A C38  1 
HETATM 2369 C  C39  . A1EGP B 2 .   ? -23.303 37.932 1.772   1.00 64.33  ? 401 A1EGP A C39  1 
HETATM 2370 C  C40  . A1EGP B 2 .   ? -22.667 36.718 1.534   1.00 61.48  ? 401 A1EGP A C40  1 
HETATM 2371 C  C41  . A1EGP B 2 .   ? -26.824 37.377 1.211   1.00 70.81  ? 401 A1EGP A C41  1 
HETATM 2372 C  C01  . A1EGP B 2 .   ? -22.168 33.408 4.194   1.00 60.83  ? 401 A1EGP A C01  1 
HETATM 2373 C  C03  . A1EGP B 2 .   ? -22.360 33.618 1.901   1.00 59.08  ? 401 A1EGP A C03  1 
HETATM 2374 C  C05  . A1EGP B 2 .   ? -21.378 31.754 2.829   1.00 61.89  ? 401 A1EGP A C05  1 
HETATM 2375 C  C07  . A1EGP B 2 .   ? -21.152 31.474 5.186   1.00 50.98  ? 401 A1EGP A C07  1 
HETATM 2376 C  C08  . A1EGP B 2 .   ? -19.955 31.737 5.831   1.00 53.64  ? 401 A1EGP A C08  1 
HETATM 2377 C  C10  . A1EGP B 2 .   ? -20.319 30.040 7.345   1.00 51.33  ? 401 A1EGP A C10  1 
HETATM 2378 C  C11  . A1EGP B 2 .   ? -21.528 29.719 6.745   1.00 61.02  ? 401 A1EGP A C11  1 
HETATM 2379 C  C12  . A1EGP B 2 .   ? -21.958 30.444 5.644   1.00 54.40  ? 401 A1EGP A C12  1 
HETATM 2380 C  C17  . A1EGP B 2 .   ? -20.029 31.933 -1.572  1.00 64.66  ? 401 A1EGP A C17  1 
HETATM 2381 C  C18  . A1EGP B 2 .   ? -18.968 32.465 -2.288  1.00 68.34  ? 401 A1EGP A C18  1 
HETATM 2382 C  C19  . A1EGP B 2 .   ? -18.198 33.482 -1.750  1.00 64.39  ? 401 A1EGP A C19  1 
HETATM 2383 C  C20  . A1EGP B 2 .   ? -18.488 33.990 -0.497  1.00 58.71  ? 401 A1EGP A C20  1 
HETATM 2384 C  C21  . A1EGP B 2 .   ? -19.557 33.468 0.226   1.00 62.41  ? 401 A1EGP A C21  1 
HETATM 2385 C  C25  . A1EGP B 2 .   ? -20.289 29.609 -1.862  1.00 69.77  ? 401 A1EGP A C25  1 
HETATM 2386 C  C26  . A1EGP B 2 .   ? -21.118 28.626 -1.337  1.00 70.75  ? 401 A1EGP A C26  1 
HETATM 2387 C  C27  . A1EGP B 2 .   ? -20.625 27.354 -1.071  1.00 75.29  ? 401 A1EGP A C27  1 
HETATM 2388 C  C28  . A1EGP B 2 .   ? -19.297 27.048 -1.330  1.00 72.61  ? 401 A1EGP A C28  1 
HETATM 2389 C  C29  . A1EGP B 2 .   ? -18.467 28.024 -1.857  1.00 67.24  ? 401 A1EGP A C29  1 
HETATM 2390 C  C30  . A1EGP B 2 .   ? -18.962 29.295 -2.124  1.00 69.24  ? 401 A1EGP A C30  1 
HETATM 2391 C  C45  . A1EGP B 2 .   ? -27.971 39.505 1.629   1.00 66.61  ? 401 A1EGP A C45  1 
HETATM 2392 F  F23  . A1EGP B 2 .   ? -17.148 33.994 -2.458  1.00 70.93  ? 401 A1EGP A F23  1 
HETATM 2393 F  F31  . A1EGP B 2 .   ? -18.810 25.796 -1.070  1.00 67.06  ? 401 A1EGP A F31  1 
HETATM 2394 N  N02  . A1EGP B 2 .   ? -22.559 34.095 3.125   1.00 59.06  ? 401 A1EGP A N02  1 
HETATM 2395 N  N04  . A1EGP B 2 .   ? -21.757 32.436 1.754   1.00 60.79  ? 401 A1EGP A N04  1 
HETATM 2396 N  N06  . A1EGP B 2 .   ? -21.575 32.244 4.036   1.00 55.39  ? 401 A1EGP A N06  1 
HETATM 2397 N  N09  . A1EGP B 2 .   ? -19.575 31.027 6.876   1.00 51.79  ? 401 A1EGP A N09  1 
HETATM 2398 N  N32  . A1EGP B 2 .   ? -22.740 34.301 0.909   1.00 62.90  ? 401 A1EGP A N32  1 
HETATM 2399 N  N42  . A1EGP B 2 .   ? -26.800 38.648 1.545   1.00 74.18  ? 401 A1EGP A N42  1 
HETATM 2400 N  N43  . A1EGP B 2 .   ? -25.563 39.059 1.797   1.00 69.19  ? 401 A1EGP A N43  1 
HETATM 2401 O  O13  . A1EGP B 2 .   ? -22.311 28.666 7.235   1.00 62.58  ? 401 A1EGP A O13  1 
HETATM 2402 O  O24  . A1EGP B 2 .   ? -20.803 30.898 -2.133  1.00 74.77  ? 401 A1EGP A O24  1 
HETATM 2403 O  O33  . A1EGP B 2 .   ? -22.336 33.822 5.292   1.00 57.21  ? 401 A1EGP A O33  1 
HETATM 2404 O  O34  . A1EGP B 2 .   ? -20.843 30.699 2.733   1.00 54.90  ? 401 A1EGP A O34  1 
HETATM 2405 CL CL22 . A1EGP B 2 .   ? -17.467 35.311 0.150   1.00 65.23  ? 401 A1EGP A CL22 1 
HETATM 2406 CL CL44 . A1EGP B 2 .   ? -20.898 36.648 1.722   1.00 66.89  ? 401 A1EGP A CL44 1 
HETATM 2407 H  H141 . A1EGP B 2 .   ? -24.098 28.285 8.131   1.00 78.98  ? 401 A1EGP A H141 1 
HETATM 2408 H  H142 . A1EGP B 2 .   ? -23.734 29.994 7.830   1.00 78.98  ? 401 A1EGP A H142 1 
HETATM 2409 H  H143 . A1EGP B 2 .   ? -22.897 29.124 9.130   1.00 78.98  ? 401 A1EGP A H143 1 
HETATM 2410 H  H152 . A1EGP B 2 .   ? -21.333 30.782 0.582   1.00 65.11  ? 401 A1EGP A H152 1 
HETATM 2411 H  H151 . A1EGP B 2 .   ? -22.409 31.979 -0.158  1.00 65.11  ? 401 A1EGP A H151 1 
HETATM 2412 H  H361 . A1EGP B 2 .   ? -25.380 34.818 0.717   1.00 77.49  ? 401 A1EGP A H361 1 
HETATM 2413 H  H391 . A1EGP B 2 .   ? -22.723 38.800 2.064   1.00 77.19  ? 401 A1EGP A H391 1 
HETATM 2414 H  H411 . A1EGP B 2 .   ? -27.697 36.789 0.954   1.00 84.97  ? 401 A1EGP A H411 1 
HETATM 2415 H  H081 . A1EGP B 2 .   ? -19.321 32.538 5.472   1.00 64.37  ? 401 A1EGP A H081 1 
HETATM 2416 H  H101 . A1EGP B 2 .   ? -19.980 29.474 8.206   1.00 61.60  ? 401 A1EGP A H101 1 
HETATM 2417 H  H121 . A1EGP B 2 .   ? -22.897 30.211 5.155   1.00 65.28  ? 401 A1EGP A H121 1 
HETATM 2418 H  H181 . A1EGP B 2 .   ? -18.739 32.082 -3.276  1.00 82.01  ? 401 A1EGP A H181 1 
HETATM 2419 H  H211 . A1EGP B 2 .   ? -19.788 33.860 1.209   1.00 74.89  ? 401 A1EGP A H211 1 
HETATM 2420 H  H261 . A1EGP B 2 .   ? -22.157 28.852 -1.133  1.00 84.90  ? 401 A1EGP A H261 1 
HETATM 2421 H  H271 . A1EGP B 2 .   ? -21.281 26.597 -0.659  1.00 90.34  ? 401 A1EGP A H271 1 
HETATM 2422 H  H291 . A1EGP B 2 .   ? -17.428 27.796 -2.063  1.00 80.68  ? 401 A1EGP A H291 1 
HETATM 2423 H  H301 . A1EGP B 2 .   ? -18.305 30.049 -2.541  1.00 83.09  ? 401 A1EGP A H301 1 
HETATM 2424 H  H452 . A1EGP B 2 .   ? -28.806 38.938 2.029   1.00 79.93  ? 401 A1EGP A H452 1 
HETATM 2425 H  H453 . A1EGP B 2 .   ? -28.223 39.870 0.638   1.00 79.93  ? 401 A1EGP A H453 1 
HETATM 2426 H  H451 . A1EGP B 2 .   ? -27.758 40.346 2.281   1.00 79.93  ? 401 A1EGP A H451 1 
HETATM 2427 O  O    . HOH   C 3 .   ? -19.533 23.663 -7.649  1.00 75.02  ? 501 HOH   A O    1 
HETATM 2428 O  O    . HOH   C 3 .   ? -4.077  10.901 15.748  1.00 47.64  ? 502 HOH   A O    1 
HETATM 2429 O  O    . HOH   C 3 .   ? -8.995  49.289 17.940  1.00 56.17  ? 503 HOH   A O    1 
HETATM 2430 O  O    . HOH   C 3 .   ? -21.735 54.807 3.667   1.00 61.74  ? 504 HOH   A O    1 
HETATM 2431 O  O    . HOH   C 3 .   ? -6.652  43.682 22.051  1.00 45.49  ? 505 HOH   A O    1 
HETATM 2432 O  O    . HOH   C 3 .   ? -8.984  28.645 2.724   1.00 37.25  ? 506 HOH   A O    1 
HETATM 2433 O  O    . HOH   C 3 .   ? 1.754   0.528  13.294  1.00 73.80  ? 507 HOH   A O    1 
HETATM 2434 O  O    . HOH   C 3 .   ? -8.741  24.323 12.294  1.00 40.74  ? 508 HOH   A O    1 
HETATM 2435 O  O    . HOH   C 3 .   ? 15.898  14.521 20.057  1.00 70.34  ? 509 HOH   A O    1 
HETATM 2436 O  O    . HOH   C 3 .   ? -7.882  21.523 0.021   1.00 45.42  ? 510 HOH   A O    1 
HETATM 2437 O  O    . HOH   C 3 .   ? -1.393  20.523 19.288  1.00 36.57  ? 511 HOH   A O    1 
HETATM 2438 O  O    . HOH   C 3 .   ? -1.810  31.733 17.587  1.00 34.09  ? 512 HOH   A O    1 
HETATM 2439 O  O    . HOH   C 3 .   ? -19.930 32.283 15.348  1.00 56.86  ? 513 HOH   A O    1 
HETATM 2440 O  O    . HOH   C 3 .   ? 2.497   25.436 33.469  1.00 60.24  ? 514 HOH   A O    1 
HETATM 2441 O  O    . HOH   C 3 .   ? -13.292 18.644 4.690   1.00 50.77  ? 515 HOH   A O    1 
HETATM 2442 O  O    . HOH   C 3 .   ? -1.370  49.004 18.913  1.00 54.17  ? 516 HOH   A O    1 
HETATM 2443 O  O    . HOH   C 3 .   ? -23.296 49.128 5.825   1.00 53.52  ? 517 HOH   A O    1 
HETATM 2444 O  O    . HOH   C 3 .   ? -23.273 33.788 -1.810  1.00 61.53  ? 518 HOH   A O    1 
HETATM 2445 O  O    . HOH   C 3 .   ? -6.861  34.165 -4.549  1.00 41.57  ? 519 HOH   A O    1 
HETATM 2446 O  O    . HOH   C 3 .   ? -0.838  35.918 12.078  1.00 47.81  ? 520 HOH   A O    1 
HETATM 2447 O  O    . HOH   C 3 .   ? -11.068 20.126 5.803   1.00 52.29  ? 521 HOH   A O    1 
HETATM 2448 O  O    . HOH   C 3 .   ? -2.161  54.611 12.196  1.00 62.74  ? 522 HOH   A O    1 
HETATM 2449 O  O    . HOH   C 3 .   ? -10.356 28.813 21.734  1.00 49.65  ? 523 HOH   A O    1 
HETATM 2450 O  O    . HOH   C 3 .   ? -3.919  28.245 22.643  1.00 46.12  ? 524 HOH   A O    1 
HETATM 2451 O  O    . HOH   C 3 .   ? -14.847 37.838 -1.892  1.00 44.94  ? 525 HOH   A O    1 
HETATM 2452 O  O    . HOH   C 3 .   ? 4.309   18.512 11.314  1.00 43.89  ? 526 HOH   A O    1 
HETATM 2453 O  O    . HOH   C 3 .   ? 5.566   27.373 16.742  1.00 51.03  ? 527 HOH   A O    1 
HETATM 2454 O  O    . HOH   C 3 .   ? 1.841   36.400 13.005  1.00 54.87  ? 528 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   ? 1.1485 0.7651 0.5066 0.0978  -0.0786 0.0981  1   SER A N   
2    C CA  . SER A 1   ? 1.1281 0.7314 0.5043 0.1018  -0.0796 0.1129  1   SER A CA  
3    C C   . SER A 1   ? 1.1294 0.7387 0.5444 0.0894  -0.0529 0.1183  1   SER A C   
4    O O   . SER A 1   ? 0.9816 0.6026 0.4027 0.0805  -0.0302 0.1137  1   SER A O   
5    C CB  . SER A 1   ? 1.2202 0.7794 0.5397 0.1073  -0.0825 0.1335  1   SER A CB  
6    O OG  . SER A 1   ? 1.2679 0.8038 0.5958 0.1011  -0.0692 0.1528  1   SER A OG  
7    N N   . GLY A 2   ? 1.1032 0.7028 0.5427 0.0898  -0.0575 0.1277  2   GLY A N   
8    C CA  . GLY A 2   ? 0.9424 0.5490 0.4221 0.0767  -0.0382 0.1333  2   GLY A CA  
9    C C   . GLY A 2   ? 0.9583 0.5973 0.4921 0.0787  -0.0473 0.1157  2   GLY A C   
10   O O   . GLY A 2   ? 1.0411 0.7069 0.5859 0.0869  -0.0613 0.0982  2   GLY A O   
11   N N   . PHE A 3   ? 0.8907 0.5278 0.4579 0.0695  -0.0398 0.1218  3   PHE A N   
12   C CA  . PHE A 3   ? 0.8301 0.4935 0.4444 0.0713  -0.0471 0.1066  3   PHE A CA  
13   C C   . PHE A 3   ? 0.9315 0.6012 0.5794 0.0542  -0.0281 0.1138  3   PHE A C   
14   O O   . PHE A 3   ? 0.8575 0.5011 0.5001 0.0434  -0.0228 0.1326  3   PHE A O   
15   C CB  . PHE A 3   ? 0.8252 0.4717 0.4399 0.0868  -0.0733 0.1036  3   PHE A CB  
16   C CG  . PHE A 3   ? 0.9214 0.6024 0.5739 0.0965  -0.0836 0.0840  3   PHE A CG  
17   C CD1 . PHE A 3   ? 0.9622 0.6811 0.6209 0.1062  -0.0915 0.0690  3   PHE A CD1 
18   C CD2 . PHE A 3   ? 0.8907 0.5667 0.5709 0.0943  -0.0857 0.0814  3   PHE A CD2 
19   C CE1 . PHE A 3   ? 0.8719 0.6273 0.5658 0.1140  -0.0986 0.0535  3   PHE A CE1 
20   C CE2 . PHE A 3   ? 0.9033 0.6113 0.6138 0.1046  -0.0934 0.0639  3   PHE A CE2 
21   C CZ  . PHE A 3   ? 0.8845 0.6342 0.6027 0.1147  -0.0984 0.0507  3   PHE A CZ  
22   N N   . ARG A 4   ? 0.8229 0.5276 0.5055 0.0506  -0.0193 0.1002  4   ARG A N   
23   C CA  . ARG A 4   ? 0.8409 0.5589 0.5567 0.0358  -0.0007 0.1066  4   ARG A CA  
24   C C   . ARG A 4   ? 0.8191 0.5683 0.5741 0.0373  -0.0043 0.0887  4   ARG A C   
25   O O   . ARG A 4   ? 0.8345 0.6021 0.5888 0.0463  -0.0124 0.0727  4   ARG A O   
26   C CB  . ARG A 4   ? 0.8306 0.5565 0.5330 0.0293  0.0262  0.1155  4   ARG A CB  
27   C CG  . ARG A 4   ? 0.9099 0.6157 0.5960 0.0187  0.0401  0.1410  4   ARG A CG  
28   C CD  . ARG A 4   ? 0.8742 0.6066 0.5843 0.0088  0.0690  0.1509  4   ARG A CD  
29   N NE  . ARG A 4   ? 0.8412 0.5644 0.5229 0.0036  0.0897  0.1735  4   ARG A NE  
30   C CZ  . ARG A 4   ? 1.0211 0.7354 0.7103 -0.0125 0.0943  0.1983  4   ARG A CZ  
31   N NH1 . ARG A 4   ? 1.0504 0.7586 0.7727 -0.0256 0.0780  0.2027  4   ARG A NH1 
32   N NH2 . ARG A 4   ? 0.9303 0.6399 0.5904 -0.0167 0.1154  0.2199  4   ARG A NH2 
33   N N   . LYS A 5   ? 0.7717 0.5279 0.5607 0.0267  0.0007  0.0930  5   LYS A N   
34   C CA  . LYS A 5   ? 0.7959 0.5812 0.6199 0.0270  -0.0001 0.0782  5   LYS A CA  
35   C C   . LYS A 5   ? 0.7541 0.5629 0.5797 0.0262  0.0179  0.0724  5   LYS A C   
36   O O   . LYS A 5   ? 0.7589 0.5726 0.5891 0.0192  0.0382  0.0831  5   LYS A O   
37   C CB  . LYS A 5   ? 0.7201 0.5058 0.5767 0.0148  0.0003  0.0856  5   LYS A CB  
38   C CG  . LYS A 5   ? 0.8337 0.6019 0.6945 0.0203  -0.0232 0.0782  5   LYS A CG  
39   C CD  . LYS A 5   ? 0.9099 0.6598 0.7873 0.0040  -0.0274 0.0914  5   LYS A CD  
40   C CE  . LYS A 5   ? 0.9639 0.6841 0.8340 0.0119  -0.0529 0.0825  5   LYS A CE  
41   N NZ  . LYS A 5   ? 1.0619 0.7345 0.9142 0.0004  -0.0644 0.0993  5   LYS A NZ  
42   N N   . MET A 6   ? 0.6701 0.4931 0.4910 0.0336  0.0103  0.0563  6   MET A N   
43   C CA  . MET A 6   ? 0.7037 0.5372 0.5149 0.0330  0.0224  0.0493  6   MET A CA  
44   C C   . MET A 6   ? 0.6836 0.5413 0.5248 0.0305  0.0216  0.0375  6   MET A C   
45   O O   . MET A 6   ? 0.6981 0.5698 0.5535 0.0333  0.0063  0.0284  6   MET A O   
46   C CB  . MET A 6   ? 0.6972 0.5231 0.4721 0.0389  0.0118  0.0424  6   MET A CB  
47   C CG  . MET A 6   ? 0.9062 0.7188 0.6475 0.0383  0.0267  0.0429  6   MET A CG  
48   S SD  . MET A 6   ? 1.0968 0.8937 0.7884 0.0432  0.0105  0.0371  6   MET A SD  
49   C CE  . MET A 6   ? 0.8271 0.5975 0.4918 0.0482  0.0119  0.0555  6   MET A CE  
50   N N   . ALA A 7   ? 0.5526 0.4153 0.4013 0.0272  0.0388  0.0384  7   ALA A N   
51   C CA  . ALA A 7   ? 0.6088 0.4889 0.4796 0.0249  0.0389  0.0287  7   ALA A CA  
52   C C   . ALA A 7   ? 0.7090 0.5824 0.5530 0.0249  0.0395  0.0187  7   ALA A C   
53   O O   . ALA A 7   ? 0.5896 0.4434 0.3982 0.0278  0.0453  0.0198  7   ALA A O   
54   C CB  . ALA A 7   ? 0.5836 0.4722 0.4814 0.0227  0.0547  0.0365  7   ALA A CB  
55   N N   . PHE A 8   ? 0.6045 0.4914 0.4622 0.0205  0.0323  0.0092  8   PHE A N   
56   C CA  . PHE A 8   ? 0.6951 0.5706 0.5277 0.0164  0.0310  0.0006  8   PHE A CA  
57   C C   . PHE A 8   ? 0.6817 0.5374 0.5018 0.0213  0.0503  0.0024  8   PHE A C   
58   O O   . PHE A 8   ? 0.6682 0.5335 0.5147 0.0253  0.0625  0.0092  8   PHE A O   
59   C CB  . PHE A 8   ? 0.5588 0.4546 0.4104 0.0078  0.0189  -0.0069 8   PHE A CB  
60   C CG  . PHE A 8   ? 0.6720 0.5915 0.5302 0.0056  0.0007  -0.0099 8   PHE A CG  
61   C CD1 . PHE A 8   ? 0.7450 0.6625 0.5783 0.0003  -0.0116 -0.0141 8   PHE A CD1 
62   C CD2 . PHE A 8   ? 0.5936 0.5379 0.4814 0.0105  -0.0049 -0.0088 8   PHE A CD2 
63   C CE1 . PHE A 8   ? 0.6486 0.5961 0.4927 0.0007  -0.0282 -0.0155 8   PHE A CE1 
64   C CE2 . PHE A 8   ? 0.6747 0.6440 0.5683 0.0137  -0.0200 -0.0117 8   PHE A CE2 
65   C CZ  . PHE A 8   ? 0.5347 0.5094 0.4093 0.0092  -0.0311 -0.0143 8   PHE A CZ  
66   N N   . PRO A 9   ? 0.7500 0.5779 0.5287 0.0225  0.0524  -0.0036 9   PRO A N   
67   C CA  . PRO A 9   ? 0.6655 0.4715 0.4277 0.0318  0.0706  -0.0041 9   PRO A CA  
68   C C   . PRO A 9   ? 0.7597 0.5758 0.5514 0.0297  0.0714  -0.0059 9   PRO A C   
69   O O   . PRO A 9   ? 0.6871 0.5082 0.4856 0.0177  0.0560  -0.0122 9   PRO A O   
70   C CB  . PRO A 9   ? 0.6691 0.4372 0.3759 0.0306  0.0641  -0.0145 9   PRO A CB  
71   C CG  . PRO A 9   ? 0.8621 0.6359 0.5562 0.0237  0.0480  -0.0146 9   PRO A CG  
72   C CD  . PRO A 9   ? 0.6363 0.4497 0.3789 0.0165  0.0366  -0.0107 9   PRO A CD  
73   N N   . SER A 10  ? 0.6601 0.4826 0.4704 0.0411  0.0893  0.0013  10  SER A N   
74   C CA  . SER A 10  ? 0.7237 0.5592 0.5659 0.0411  0.0897  0.0021  10  SER A CA  
75   C C   . SER A 10  ? 0.6590 0.4622 0.4734 0.0489  0.0946  -0.0048 10  SER A C   
76   O O   . SER A 10  ? 0.7562 0.5657 0.5925 0.0514  0.0954  -0.0033 10  SER A O   
77   C CB  . SER A 10  ? 0.6308 0.4956 0.5137 0.0485  0.1031  0.0152  10  SER A CB  
78   O OG  . SER A 10  ? 0.6814 0.5393 0.5493 0.0643  0.1248  0.0214  10  SER A OG  
79   N N   . GLY A 11  ? 0.7477 0.5120 0.5106 0.0536  0.0962  -0.0127 11  GLY A N   
80   C CA  . GLY A 11  ? 0.7411 0.4641 0.4694 0.0642  0.1007  -0.0201 11  GLY A CA  
81   C C   . GLY A 11  ? 0.7432 0.4578 0.4797 0.0504  0.0847  -0.0243 11  GLY A C   
82   O O   . GLY A 11  ? 0.8721 0.5761 0.6138 0.0612  0.0907  -0.0231 11  GLY A O   
83   N N   . LYS A 12  ? 0.8229 0.5446 0.5609 0.0269  0.0643  -0.0278 12  LYS A N   
84   C CA  . LYS A 12  ? 0.7934 0.5081 0.5355 0.0106  0.0496  -0.0297 12  LYS A CA  
85   C C   . LYS A 12  ? 0.7547 0.5022 0.5439 0.0142  0.0542  -0.0216 12  LYS A C   
86   O O   . LYS A 12  ? 0.7206 0.4538 0.5082 0.0086  0.0481  -0.0212 12  LYS A O   
87   C CB  . LYS A 12  ? 0.7361 0.4676 0.4798 -0.0150 0.0291  -0.0319 12  LYS A CB  
88   C CG  . LYS A 12  ? 0.8463 0.5380 0.5386 -0.0250 0.0171  -0.0404 12  LYS A CG  
89   C CD  . LYS A 12  ? 0.7889 0.5033 0.4896 -0.0533 -0.0053 -0.0403 12  LYS A CD  
90   C CE  . LYS A 12  ? 1.1090 0.8035 0.7708 -0.0627 -0.0191 -0.0467 12  LYS A CE  
91   N NZ  . LYS A 12  ? 1.1457 0.7807 0.7521 -0.0458 -0.0105 -0.0547 12  LYS A NZ  
92   N N   . VAL A 13  ? 0.7141 0.5021 0.5424 0.0221  0.0628  -0.0144 13  VAL A N   
93   C CA  . VAL A 13  ? 0.7264 0.5444 0.5973 0.0243  0.0639  -0.0073 13  VAL A CA  
94   C C   . VAL A 13  ? 0.8046 0.6178 0.6841 0.0459  0.0800  -0.0018 13  VAL A C   
95   O O   . VAL A 13  ? 0.6545 0.4774 0.5564 0.0492  0.0785  0.0028  13  VAL A O   
96   C CB  . VAL A 13  ? 0.5818 0.4427 0.4895 0.0191  0.0603  -0.0027 13  VAL A CB  
97   C CG1 . VAL A 13  ? 0.5857 0.4729 0.5333 0.0236  0.0616  0.0046  13  VAL A CG1 
98   C CG2 . VAL A 13  ? 0.5856 0.4590 0.4908 0.0017  0.0441  -0.0074 13  VAL A CG2 
99   N N   . GLU A 14  ? 0.6890 0.4901 0.5504 0.0622  0.0956  -0.0014 14  GLU A N   
100  C CA  . GLU A 14  ? 0.6897 0.4956 0.5628 0.0859  0.1134  0.0053  14  GLU A CA  
101  C C   . GLU A 14  ? 0.8001 0.5720 0.6537 0.0959  0.1110  0.0015  14  GLU A C   
102  O O   . GLU A 14  ? 0.7054 0.4949 0.5878 0.1086  0.1156  0.0089  14  GLU A O   
103  C CB  . GLU A 14  ? 0.6999 0.4957 0.5471 0.1028  0.1324  0.0058  14  GLU A CB  
104  C CG  . GLU A 14  ? 0.6610 0.4988 0.5396 0.0997  0.1412  0.0169  14  GLU A CG  
105  C CD  . GLU A 14  ? 0.8029 0.6258 0.6451 0.1115  0.1577  0.0169  14  GLU A CD  
106  O OE1 . GLU A 14  ? 0.7516 0.5745 0.5824 0.0987  0.1518  0.0164  14  GLU A OE1 
107  O OE2 . GLU A 14  ? 0.7613 0.5719 0.5835 0.1357  0.1769  0.0176  14  GLU A OE2 
108  N N   . GLY A 15  ? 0.8226 0.5437 0.6265 0.0888  0.1013  -0.0093 15  GLY A N   
109  C CA  . GLY A 15  ? 0.8874 0.5633 0.6630 0.0966  0.0965  -0.0130 15  GLY A CA  
110  C C   . GLY A 15  ? 0.7765 0.4646 0.5781 0.0824  0.0824  -0.0077 15  GLY A C   
111  O O   . GLY A 15  ? 0.8933 0.5380 0.6663 0.0823  0.0742  -0.0099 15  GLY A O   
112  N N   . CYS A 16  ? 0.6727 0.4147 0.5234 0.0708  0.0788  -0.0005 16  CYS A N   
113  C CA  . CYS A 16  ? 0.7265 0.4836 0.6004 0.0594  0.0666  0.0049  16  CYS A CA  
114  C C   . CYS A 16  ? 0.6410 0.4434 0.5647 0.0708  0.0711  0.0147  16  CYS A C   
115  O O   . CYS A 16  ? 0.7375 0.5483 0.6761 0.0657  0.0614  0.0194  16  CYS A O   
116  C CB  . CYS A 16  ? 0.5733 0.3487 0.4524 0.0308  0.0523  0.0028  16  CYS A CB  
117  S SG  . CYS A 16  ? 0.8277 0.5660 0.6589 0.0118  0.0436  -0.0068 16  CYS A SG  
118  N N   . MET A 17  ? 0.5637 0.3953 0.5123 0.0843  0.0845  0.0192  17  MET A N   
119  C CA  . MET A 17  ? 0.5541 0.4305 0.5522 0.0914  0.0861  0.0300  17  MET A CA  
120  C C   . MET A 17  ? 0.6836 0.5515 0.6852 0.1143  0.0904  0.0355  17  MET A C   
121  O O   . MET A 17  ? 0.6435 0.4856 0.6204 0.1361  0.1035  0.0336  17  MET A O   
122  C CB  . MET A 17  ? 0.5680 0.4781 0.5913 0.0959  0.0991  0.0358  17  MET A CB  
123  C CG  . MET A 17  ? 0.4826 0.4062 0.5104 0.0750  0.0918  0.0329  17  MET A CG  
124  S SD  . MET A 17  ? 0.6721 0.5955 0.6986 0.0523  0.0695  0.0265  17  MET A SD  
125  C CE  . MET A 17  ? 0.5386 0.4970 0.6110 0.0533  0.0608  0.0360  17  MET A CE  
126  N N   . VAL A 18  ? 0.5791 0.4668 0.6082 0.1117  0.0788  0.0422  18  VAL A N   
127  C CA  . VAL A 18  ? 0.5869 0.4739 0.6259 0.1343  0.0800  0.0495  18  VAL A CA  
128  C C   . VAL A 18  ? 0.5745 0.5169 0.6692 0.1330  0.0735  0.0611  18  VAL A C   
129  O O   . VAL A 18  ? 0.5482 0.5170 0.6645 0.1124  0.0647  0.0614  18  VAL A O   
130  C CB  . VAL A 18  ? 0.6020 0.4424 0.6055 0.1318  0.0672  0.0465  18  VAL A CB  
131  C CG1 . VAL A 18  ? 0.7148 0.4964 0.6615 0.1285  0.0699  0.0357  18  VAL A CG1 
132  C CG2 . VAL A 18  ? 0.5551 0.4103 0.5694 0.1061  0.0495  0.0476  18  VAL A CG2 
133  N N   . GLN A 19  ? 0.5835 0.5416 0.6997 0.1563  0.0763  0.0705  19  GLN A N   
134  C CA  . GLN A 19  ? 0.5653 0.5744 0.7337 0.1553  0.0660  0.0826  19  GLN A CA  
135  C C   . GLN A 19  ? 0.5039 0.4952 0.6627 0.1540  0.0468  0.0839  19  GLN A C   
136  O O   . GLN A 19  ? 0.6167 0.5683 0.7437 0.1707  0.0475  0.0825  19  GLN A O   
137  C CB  . GLN A 19  ? 0.4829 0.5330 0.6889 0.1820  0.0807  0.0952  19  GLN A CB  
138  C CG  . GLN A 19  ? 0.5368 0.6483 0.8037 0.1757  0.0689  0.1096  19  GLN A CG  
139  C CD  . GLN A 19  ? 0.7125 0.8780 1.0243 0.1983  0.0858  0.1246  19  GLN A CD  
140  O OE1 . GLN A 19  ? 0.7770 0.9321 1.0709 0.2242  0.1084  0.1234  19  GLN A OE1 
141  N NE2 . GLN A 19  ? 0.6458 0.8705 1.0154 0.1887  0.0748  0.1393  19  GLN A NE2 
142  N N   . VAL A 20  ? 0.5311 0.5469 0.7124 0.1348  0.0290  0.0865  20  VAL A N   
143  C CA  . VAL A 20  ? 0.5486 0.5517 0.7199 0.1318  0.0099  0.0887  20  VAL A CA  
144  C C   . VAL A 20  ? 0.5700 0.6211 0.7901 0.1363  -0.0032 0.1009  20  VAL A C   
145  O O   . VAL A 20  ? 0.4932 0.5822 0.7478 0.1225  -0.0074 0.1035  20  VAL A O   
146  C CB  . VAL A 20  ? 0.5377 0.5231 0.6827 0.1051  -0.0013 0.0797  20  VAL A CB  
147  C CG1 . VAL A 20  ? 0.5555 0.5333 0.6907 0.1022  -0.0201 0.0839  20  VAL A CG1 
148  C CG2 . VAL A 20  ? 0.4770 0.4200 0.5775 0.0981  0.0090  0.0697  20  VAL A CG2 
149  N N   . THR A 21  ? 0.5492 0.5966 0.7706 0.1545  -0.0119 0.1089  21  THR A N   
150  C CA  . THR A 21  ? 0.5599 0.6543 0.8279 0.1602  -0.0273 0.1217  21  THR A CA  
151  C C   . THR A 21  ? 0.5873 0.6611 0.8346 0.1596  -0.0494 0.1241  21  THR A C   
152  O O   . THR A 21  ? 0.5836 0.6114 0.7897 0.1707  -0.0481 0.1227  21  THR A O   
153  C CB  . THR A 21  ? 0.6437 0.7706 0.9464 0.1914  -0.0147 0.1336  21  THR A CB  
154  O OG1 . THR A 21  ? 0.5001 0.6500 0.8212 0.1918  0.0074  0.1330  21  THR A OG1 
155  C CG2 . THR A 21  ? 0.5327 0.7157 0.8890 0.1952  -0.0337 0.1487  21  THR A CG2 
156  N N   . CYS A 22  ? 0.5902 0.6948 0.8627 0.1455  -0.0709 0.1284  22  CYS A N   
157  C CA  . CYS A 22  ? 0.5241 0.6172 0.7809 0.1455  -0.0944 0.1326  22  CYS A CA  
158  C C   . CYS A 22  ? 0.5179 0.6656 0.8285 0.1485  -0.1136 0.1452  22  CYS A C   
159  O O   . CYS A 22  ? 0.6593 0.8358 0.9956 0.1275  -0.1244 0.1439  22  CYS A O   
160  C CB  . CYS A 22  ? 0.5542 0.6207 0.7724 0.1204  -0.1045 0.1217  22  CYS A CB  
161  S SG  . CYS A 22  ? 0.8607 0.8942 1.0353 0.1223  -0.1252 0.1259  22  CYS A SG  
162  N N   . GLY A 23  ? 0.5408 0.7021 0.8682 0.1742  -0.1193 0.1578  23  GLY A N   
163  C CA  . GLY A 23  ? 0.6121 0.8342 0.9980 0.1787  -0.1371 0.1722  23  GLY A CA  
164  C C   . GLY A 23  ? 0.5834 0.8602 1.0253 0.1783  -0.1208 0.1786  23  GLY A C   
165  O O   . GLY A 23  ? 0.5785 0.8625 1.0295 0.2027  -0.0962 0.1820  23  GLY A O   
166  N N   . THR A 24  ? 0.6045 0.9171 1.0805 0.1507  -0.1345 0.1805  24  THR A N   
167  C CA  . THR A 24  ? 0.4641 0.8264 0.9902 0.1428  -0.1196 0.1881  24  THR A CA  
168  C C   . THR A 24  ? 0.5560 0.8917 1.0589 0.1155  -0.1105 0.1746  24  THR A C   
169  O O   . THR A 24  ? 0.4700 0.8394 1.0073 0.1056  -0.0979 0.1808  24  THR A O   
170  C CB  . THR A 24  ? 0.4972 0.9275 1.0888 0.1306  -0.1439 0.2057  24  THR A CB  
171  O OG1 . THR A 24  ? 0.6142 1.0243 1.1866 0.1085  -0.1788 0.2001  24  THR A OG1 
172  C CG2 . THR A 24  ? 0.4489 0.9160 1.0656 0.1604  -0.1398 0.2167  24  THR A CG2 
173  N N   . THR A 25  ? 0.5175 0.7966 0.9639 0.1039  -0.1163 0.1578  25  THR A N   
174  C CA  . THR A 25  ? 0.5308 0.7831 0.9519 0.0827  -0.1078 0.1443  25  THR A CA  
175  C C   . THR A 25  ? 0.5735 0.7966 0.9647 0.0966  -0.0768 0.1367  25  THR A C   
176  O O   . THR A 25  ? 0.4807 0.6704 0.8372 0.1137  -0.0702 0.1325  25  THR A O   
177  C CB  . THR A 25  ? 0.5756 0.7876 0.9516 0.0663  -0.1280 0.1305  25  THR A CB  
178  O OG1 . THR A 25  ? 0.5322 0.7644 0.9280 0.0562  -0.1595 0.1368  25  THR A OG1 
179  C CG2 . THR A 25  ? 0.5389 0.7302 0.8951 0.0465  -0.1221 0.1178  25  THR A CG2 
180  N N   . THR A 26  ? 0.5444 0.7767 0.9461 0.0880  -0.0596 0.1353  26  THR A N   
181  C CA  . THR A 26  ? 0.4945 0.7030 0.8703 0.1014  -0.0312 0.1291  26  THR A CA  
182  C C   . THR A 26  ? 0.4253 0.6163 0.7829 0.0811  -0.0241 0.1189  26  THR A C   
183  O O   . THR A 26  ? 0.4529 0.6653 0.8352 0.0616  -0.0334 0.1227  26  THR A O   
184  C CB  . THR A 26  ? 0.4573 0.7052 0.8699 0.1241  -0.0107 0.1427  26  THR A CB  
185  O OG1 . THR A 26  ? 0.5981 0.8101 0.9724 0.1442  0.0133  0.1347  26  THR A OG1 
186  C CG2 . THR A 26  ? 0.4517 0.7451 0.9077 0.1083  -0.0044 0.1531  26  THR A CG2 
187  N N   . LEU A 27  ? 0.4145 0.5645 0.7275 0.0852  -0.0096 0.1066  27  LEU A N   
188  C CA  . LEU A 27  ? 0.4409 0.5731 0.7333 0.0689  -0.0037 0.0966  27  LEU A CA  
189  C C   . LEU A 27  ? 0.4969 0.5919 0.7471 0.0787  0.0146  0.0868  27  LEU A C   
190  O O   . LEU A 27  ? 0.4401 0.5176 0.6741 0.0965  0.0214  0.0873  27  LEU A O   
191  C CB  . LEU A 27  ? 0.4208 0.5382 0.6966 0.0496  -0.0249 0.0873  27  LEU A CB  
192  C CG  . LEU A 27  ? 0.4291 0.5251 0.6776 0.0519  -0.0387 0.0819  27  LEU A CG  
193  C CD1 . LEU A 27  ? 0.4223 0.4835 0.6300 0.0598  -0.0251 0.0747  27  LEU A CD1 
194  C CD2 . LEU A 27  ? 0.4045 0.4921 0.6384 0.0356  -0.0577 0.0732  27  LEU A CD2 
195  N N   . ASN A 28  ? 0.3240 0.4037 0.5541 0.0666  0.0204  0.0781  28  ASN A N   
196  C CA  . ASN A 28  ? 0.3999 0.4467 0.5913 0.0717  0.0355  0.0691  28  ASN A CA  
197  C C   . ASN A 28  ? 0.4685 0.4828 0.6222 0.0638  0.0260  0.0587  28  ASN A C   
198  O O   . ASN A 28  ? 0.4981 0.5168 0.6518 0.0515  0.0108  0.0557  28  ASN A O   
199  C CB  . ASN A 28  ? 0.4148 0.4634 0.6027 0.0623  0.0445  0.0662  28  ASN A CB  
200  C CG  . ASN A 28  ? 0.4256 0.5086 0.6500 0.0663  0.0553  0.0792  28  ASN A CG  
201  O OD1 . ASN A 28  ? 0.5204 0.6117 0.7501 0.0846  0.0725  0.0855  28  ASN A OD1 
202  N ND2 . ASN A 28  ? 0.4780 0.5806 0.7261 0.0496  0.0453  0.0840  28  ASN A ND2 
203  N N   . GLY A 29  ? 0.4048 0.3857 0.5240 0.0704  0.0353  0.0536  29  GLY A N   
204  C CA  . GLY A 29  ? 0.4637 0.4156 0.5477 0.0596  0.0278  0.0465  29  GLY A CA  
205  C C   . GLY A 29  ? 0.5821 0.5058 0.6323 0.0546  0.0367  0.0383  29  GLY A C   
206  O O   . GLY A 29  ? 0.5147 0.4319 0.5606 0.0646  0.0498  0.0374  29  GLY A O   
207  N N   . LEU A 30  ? 0.4761 0.3852 0.5015 0.0385  0.0290  0.0330  30  LEU A N   
208  C CA  . LEU A 30  ? 0.5217 0.4076 0.5160 0.0284  0.0323  0.0256  30  LEU A CA  
209  C C   . LEU A 30  ? 0.5710 0.4178 0.5306 0.0223  0.0275  0.0261  30  LEU A C   
210  O O   . LEU A 30  ? 0.5776 0.4281 0.5338 0.0102  0.0181  0.0295  30  LEU A O   
211  C CB  . LEU A 30  ? 0.4130 0.3230 0.4122 0.0122  0.0265  0.0207  30  LEU A CB  
212  C CG  . LEU A 30  ? 0.6427 0.5398 0.6174 0.0015  0.0280  0.0139  30  LEU A CG  
213  C CD1 . LEU A 30  ? 0.4807 0.3713 0.4535 0.0121  0.0386  0.0115  30  LEU A CD1 
214  C CD2 . LEU A 30  ? 0.4490 0.3752 0.4304 -0.0121 0.0203  0.0107  30  LEU A CD2 
215  N N   . TRP A 31  ? 0.6495 0.4557 0.5795 0.0304  0.0337  0.0231  31  TRP A N   
216  C CA  . TRP A 31  ? 0.6384 0.3944 0.5292 0.0262  0.0278  0.0239  31  TRP A CA  
217  C C   . TRP A 31  ? 0.7260 0.4595 0.5849 0.0032  0.0224  0.0177  31  TRP A C   
218  O O   . TRP A 31  ? 0.6918 0.4051 0.5308 0.0074  0.0276  0.0103  31  TRP A O   
219  C CB  . TRP A 31  ? 0.6172 0.3364 0.4910 0.0537  0.0364  0.0238  31  TRP A CB  
220  C CG  . TRP A 31  ? 0.7472 0.4021 0.5739 0.0536  0.0292  0.0241  31  TRP A CG  
221  C CD1 . TRP A 31  ? 0.8069 0.4409 0.6149 0.0319  0.0155  0.0295  31  TRP A CD1 
222  C CD2 . TRP A 31  ? 0.8640 0.4632 0.6525 0.0770  0.0350  0.0195  31  TRP A CD2 
223  N NE1 . TRP A 31  ? 0.8270 0.3912 0.5870 0.0376  0.0105  0.0291  31  TRP A NE1 
224  C CE2 . TRP A 31  ? 0.8808 0.4202 0.6262 0.0671  0.0219  0.0218  31  TRP A CE2 
225  C CE3 . TRP A 31  ? 0.8267 0.4198 0.6105 0.1063  0.0508  0.0141  31  TRP A CE3 
226  C CZ2 . TRP A 31  ? 0.9555 0.4224 0.6502 0.0868  0.0220  0.0170  31  TRP A CZ2 
227  C CZ3 . TRP A 31  ? 0.9595 0.4865 0.6940 0.1287  0.0533  0.0090  31  TRP A CZ3 
228  C CH2 . TRP A 31  ? 0.9506 0.4118 0.6396 0.1195  0.0379  0.0096  31  TRP A CH2 
229  N N   . LEU A 32  ? 0.6781 0.4180 0.5320 -0.0215 0.0116  0.0217  32  LEU A N   
230  C CA  . LEU A 32  ? 0.7224 0.4474 0.5506 -0.0475 0.0036  0.0189  32  LEU A CA  
231  C C   . LEU A 32  ? 0.8343 0.5200 0.6322 -0.0654 -0.0070 0.0267  32  LEU A C   
232  O O   . LEU A 32  ? 0.7534 0.4577 0.5640 -0.0709 -0.0100 0.0360  32  LEU A O   
233  C CB  . LEU A 32  ? 0.6825 0.4656 0.5388 -0.0633 0.0014  0.0186  32  LEU A CB  
234  C CG  . LEU A 32  ? 0.6778 0.4971 0.5627 -0.0474 0.0096  0.0126  32  LEU A CG  
235  C CD1 . LEU A 32  ? 0.5151 0.3897 0.4300 -0.0545 0.0070  0.0139  32  LEU A CD1 
236  C CD2 . LEU A 32  ? 0.6153 0.4160 0.4802 -0.0478 0.0113  0.0046  32  LEU A CD2 
237  N N   . ASP A 33  ? 0.8934 0.5211 0.6476 -0.0752 -0.0138 0.0233  33  ASP A N   
238  C CA  . ASP A 33  ? 0.9567 0.5313 0.6734 -0.0933 -0.0258 0.0313  33  ASP A CA  
239  C C   . ASP A 33  ? 0.9817 0.5339 0.6973 -0.0674 -0.0220 0.0369  33  ASP A C   
240  O O   . ASP A 33  ? 0.9614 0.4993 0.6776 -0.0346 -0.0126 0.0304  33  ASP A O   
241  C CB  . ASP A 33  ? 1.0235 0.6350 0.7516 -0.1301 -0.0347 0.0418  33  ASP A CB  
242  C CG  . ASP A 33  ? 1.1688 0.8037 0.8990 -0.1535 -0.0402 0.0369  33  ASP A CG  
243  O OD1 . ASP A 33  ? 1.2152 0.8049 0.9136 -0.1534 -0.0449 0.0274  33  ASP A OD1 
244  O OD2 . ASP A 33  ? 1.1577 0.8566 0.9196 -0.1702 -0.0402 0.0424  33  ASP A OD2 
245  N N   . ASP A 34  ? 0.9448 0.4971 0.6597 -0.0796 -0.0287 0.0497  34  ASP A N   
246  C CA  . ASP A 34  ? 0.9623 0.4931 0.6746 -0.0553 -0.0281 0.0563  34  ASP A CA  
247  C C   . ASP A 34  ? 0.8940 0.4912 0.6522 -0.0479 -0.0237 0.0624  34  ASP A C   
248  O O   . ASP A 34  ? 0.9246 0.5130 0.6798 -0.0411 -0.0283 0.0725  34  ASP A O   
249  C CB  . ASP A 34  ? 0.9265 0.3916 0.5920 -0.0722 -0.0415 0.0674  34  ASP A CB  
250  C CG  . ASP A 34  ? 1.1442 0.6408 0.8161 -0.1092 -0.0483 0.0812  34  ASP A CG  
251  O OD1 . ASP A 34  ? 1.1114 0.6689 0.8128 -0.1269 -0.0445 0.0792  34  ASP A OD1 
252  O OD2 . ASP A 34  ? 1.3290 0.7899 0.9749 -0.1192 -0.0570 0.0950  34  ASP A OD2 
253  N N   . VAL A 35  ? 0.8068 0.4658 0.6032 -0.0487 -0.0167 0.0562  35  VAL A N   
254  C CA  . VAL A 35  ? 0.7307 0.4475 0.5661 -0.0414 -0.0144 0.0593  35  VAL A CA  
255  C C   . VAL A 35  ? 0.7133 0.4613 0.5824 -0.0183 -0.0053 0.0504  35  VAL A C   
256  O O   . VAL A 35  ? 0.7178 0.4654 0.5865 -0.0179 0.0007  0.0416  35  VAL A O   
257  C CB  . VAL A 35  ? 0.7131 0.4763 0.5599 -0.0670 -0.0163 0.0622  35  VAL A CB  
258  C CG1 . VAL A 35  ? 0.6449 0.4616 0.5267 -0.0550 -0.0141 0.0611  35  VAL A CG1 
259  C CG2 . VAL A 35  ? 0.6938 0.4350 0.5118 -0.0913 -0.0239 0.0754  35  VAL A CG2 
260  N N   . VAL A 36  ? 0.6684 0.4433 0.5655 -0.0010 -0.0054 0.0537  36  VAL A N   
261  C CA  . VAL A 36  ? 0.6701 0.4791 0.6034 0.0167  0.0015  0.0487  36  VAL A CA  
262  C C   . VAL A 36  ? 0.6602 0.5179 0.6215 0.0101  -0.0034 0.0488  36  VAL A C   
263  O O   . VAL A 36  ? 0.6444 0.5093 0.6068 0.0096  -0.0117 0.0552  36  VAL A O   
264  C CB  . VAL A 36  ? 0.7126 0.5110 0.6566 0.0444  0.0041  0.0532  36  VAL A CB  
265  C CG1 . VAL A 36  ? 0.5687 0.4127 0.5567 0.0572  0.0097  0.0521  36  VAL A CG1 
266  C CG2 . VAL A 36  ? 0.6564 0.4030 0.5673 0.0564  0.0106  0.0503  36  VAL A CG2 
267  N N   . TYR A 37  ? 0.5365 0.4225 0.5151 0.0061  0.0008  0.0414  37  TYR A N   
268  C CA  . TYR A 37  ? 0.4639 0.3886 0.4636 0.0025  -0.0043 0.0390  37  TYR A CA  
269  C C   . TYR A 37  ? 0.5498 0.4942 0.5822 0.0165  -0.0041 0.0388  37  TYR A C   
270  O O   . TYR A 37  ? 0.6189 0.5603 0.6606 0.0242  0.0048  0.0376  37  TYR A O   
271  C CB  . TYR A 37  ? 0.5089 0.4506 0.5043 -0.0106 -0.0019 0.0318  37  TYR A CB  
272  C CG  . TYR A 37  ? 0.5385 0.4680 0.5072 -0.0284 -0.0020 0.0338  37  TYR A CG  
273  C CD1 . TYR A 37  ? 0.5120 0.4075 0.4595 -0.0340 0.0012  0.0335  37  TYR A CD1 
274  C CD2 . TYR A 37  ? 0.5850 0.5369 0.5478 -0.0403 -0.0058 0.0368  37  TYR A CD2 
275  C CE1 . TYR A 37  ? 0.6350 0.5179 0.5584 -0.0550 -0.0020 0.0368  37  TYR A CE1 
276  C CE2 . TYR A 37  ? 0.4680 0.4152 0.4105 -0.0603 -0.0059 0.0418  37  TYR A CE2 
277  C CZ  . TYR A 37  ? 0.5667 0.4788 0.4907 -0.0697 -0.0054 0.0422  37  TYR A CZ  
278  O OH  . TYR A 37  ? 0.6521 0.5582 0.5565 -0.0942 -0.0085 0.0486  37  TYR A OH  
279  N N   . CYS A 38  ? 0.5204 0.4848 0.5682 0.0184  -0.0145 0.0408  38  CYS A N   
280  C CA  . CYS A 38  ? 0.3890 0.3742 0.4695 0.0261  -0.0184 0.0423  38  CYS A CA  
281  C C   . CYS A 38  ? 0.4594 0.4601 0.5436 0.0220  -0.0334 0.0403  38  CYS A C   
282  O O   . CYS A 38  ? 0.5243 0.5205 0.5859 0.0176  -0.0387 0.0395  38  CYS A O   
283  C CB  . CYS A 38  ? 0.5314 0.5147 0.6296 0.0406  -0.0168 0.0517  38  CYS A CB  
284  S SG  . CYS A 38  ? 0.5962 0.5742 0.6889 0.0464  -0.0316 0.0601  38  CYS A SG  
285  N N   . PRO A 39  ? 0.4856 0.5026 0.5945 0.0224  -0.0410 0.0396  39  PRO A N   
286  C CA  . PRO A 39  ? 0.4731 0.4967 0.5794 0.0195  -0.0584 0.0362  39  PRO A CA  
287  C C   . PRO A 39  ? 0.5434 0.5657 0.6474 0.0240  -0.0700 0.0435  39  PRO A C   
288  O O   . PRO A 39  ? 0.4656 0.4916 0.5893 0.0311  -0.0697 0.0532  39  PRO A O   
289  C CB  . PRO A 39  ? 0.4391 0.4742 0.5742 0.0167  -0.0654 0.0369  39  PRO A CB  
290  C CG  . PRO A 39  ? 0.4697 0.5053 0.6141 0.0168  -0.0480 0.0377  39  PRO A CG  
291  C CD  . PRO A 39  ? 0.4663 0.4930 0.6012 0.0236  -0.0341 0.0417  39  PRO A CD  
292  N N   . ARG A 40  ? 0.4590 0.4768 0.5367 0.0219  -0.0800 0.0392  40  ARG A N   
293  C CA  . ARG A 40  ? 0.6016 0.6161 0.6713 0.0259  -0.0935 0.0462  40  ARG A CA  
294  C C   . ARG A 40  ? 0.5138 0.5407 0.6132 0.0277  -0.1120 0.0507  40  ARG A C   
295  O O   . ARG A 40  ? 0.5545 0.5826 0.6573 0.0331  -0.1237 0.0594  40  ARG A O   
296  C CB  . ARG A 40  ? 0.5444 0.5532 0.5757 0.0237  -0.0989 0.0405  40  ARG A CB  
297  C CG  . ARG A 40  ? 0.4447 0.4562 0.4687 0.0234  -0.1124 0.0292  40  ARG A CG  
298  C CD  . ARG A 40  ? 0.5888 0.5961 0.5706 0.0261  -0.1157 0.0240  40  ARG A CD  
299  N NE  . ARG A 40  ? 0.6155 0.6192 0.5818 0.0298  -0.1267 0.0103  40  ARG A NE  
300  C CZ  . ARG A 40  ? 0.7321 0.7323 0.6588 0.0364  -0.1302 0.0030  40  ARG A CZ  
301  N NH1 . ARG A 40  ? 0.5345 0.5388 0.4351 0.0373  -0.1230 0.0099  40  ARG A NH1 
302  N NH2 . ARG A 40  ? 0.6107 0.6006 0.5202 0.0431  -0.1411 -0.0112 40  ARG A NH2 
303  N N   . HIS A 41  ? 0.5097 0.5459 0.6309 0.0221  -0.1163 0.0464  41  HIS A N   
304  C CA  . HIS A 41  ? 0.5571 0.6082 0.7108 0.0186  -0.1354 0.0528  41  HIS A CA  
305  C C   . HIS A 41  ? 0.4815 0.5528 0.6708 0.0265  -0.1321 0.0680  41  HIS A C   
306  O O   . HIS A 41  ? 0.5132 0.6032 0.7297 0.0252  -0.1506 0.0765  41  HIS A O   
307  C CB  . HIS A 41  ? 0.5795 0.6344 0.7514 0.0086  -0.1366 0.0487  41  HIS A CB  
308  C CG  . HIS A 41  ? 0.6533 0.7186 0.8512 -0.0016 -0.1614 0.0539  41  HIS A CG  
309  N ND1 . HIS A 41  ? 0.6862 0.7363 0.8612 -0.0059 -0.1876 0.0473  41  HIS A ND1 
310  C CD2 . HIS A 41  ? 0.6625 0.7526 0.9065 -0.0102 -0.1650 0.0660  41  HIS A CD2 
311  C CE1 . HIS A 41  ? 0.7511 0.8130 0.9569 -0.0186 -0.2089 0.0546  41  HIS A CE1 
312  N NE2 . HIS A 41  ? 0.7985 0.8881 1.0493 -0.0224 -0.1950 0.0672  41  HIS A NE2 
313  N N   . VAL A 42  ? 0.3813 0.4488 0.5695 0.0358  -0.1101 0.0714  42  VAL A N   
314  C CA  . VAL A 42  ? 0.5167 0.6006 0.7344 0.0493  -0.1043 0.0846  42  VAL A CA  
315  C C   . VAL A 42  ? 0.5846 0.6689 0.7991 0.0583  -0.1215 0.0928  42  VAL A C   
316  O O   . VAL A 42  ? 0.5148 0.6227 0.7630 0.0702  -0.1247 0.1052  42  VAL A O   
317  C CB  . VAL A 42  ? 0.4248 0.4912 0.6276 0.0592  -0.0791 0.0836  42  VAL A CB  
318  C CG1 . VAL A 42  ? 0.4590 0.4914 0.6155 0.0601  -0.0776 0.0797  42  VAL A CG1 
319  C CG2 . VAL A 42  ? 0.4455 0.5296 0.6791 0.0777  -0.0704 0.0958  42  VAL A CG2 
320  N N   . ILE A 43  ? 0.5306 0.5917 0.7047 0.0545  -0.1321 0.0873  43  ILE A N   
321  C CA  . ILE A 43  ? 0.6526 0.7096 0.8167 0.0631  -0.1491 0.0959  43  ILE A CA  
322  C C   . ILE A 43  ? 0.6158 0.6931 0.7988 0.0570  -0.1777 0.0984  43  ILE A C   
323  O O   . ILE A 43  ? 0.7017 0.7774 0.8762 0.0637  -0.1958 0.1057  43  ILE A O   
324  C CB  . ILE A 43  ? 0.6847 0.7081 0.7935 0.0611  -0.1473 0.0917  43  ILE A CB  
325  C CG1 . ILE A 43  ? 0.6581 0.6780 0.7410 0.0490  -0.1601 0.0807  43  ILE A CG1 
326  C CG2 . ILE A 43  ? 0.5584 0.5610 0.6468 0.0598  -0.1221 0.0879  43  ILE A CG2 
327  C CD1 . ILE A 43  ? 0.7204 0.7165 0.7508 0.0467  -0.1553 0.0781  43  ILE A CD1 
328  N N   . CYS A 44  ? 0.6362 0.7711 0.7142 0.0476  -0.1659 0.0896  44  CYS A N   
329  C CA  . CYS A 44  ? 0.6646 0.8354 0.7574 0.0332  -0.1899 0.0821  44  CYS A CA  
330  C C   . CYS A 44  ? 0.7374 0.9798 0.8890 0.0364  -0.1978 0.0819  44  CYS A C   
331  O O   . CYS A 44  ? 0.6911 0.9563 0.8771 0.0317  -0.1793 0.0822  44  CYS A O   
332  C CB  . CYS A 44  ? 0.6821 0.8352 0.7680 0.0005  -0.1874 0.0717  44  CYS A CB  
333  S SG  . CYS A 44  ? 0.7542 0.8362 0.7762 -0.0027 -0.1803 0.0687  44  CYS A SG  
334  N N   . THR A 45  ? 0.7390 1.0203 0.9017 0.0449  -0.2252 0.0814  45  THR A N   
335  C CA  . THR A 45  ? 0.7454 1.1069 0.9705 0.0391  -0.2365 0.0786  45  THR A CA  
336  C C   . THR A 45  ? 0.7982 1.1747 1.0396 -0.0045 -0.2437 0.0679  45  THR A C   
337  O O   . THR A 45  ? 0.8225 1.1444 1.0220 -0.0240 -0.2441 0.0617  45  THR A O   
338  C CB  . THR A 45  ? 0.8720 1.2741 1.1054 0.0649  -0.2664 0.0821  45  THR A CB  
339  O OG1 . THR A 45  ? 0.8244 1.2086 1.0228 0.0502  -0.2932 0.0759  45  THR A OG1 
340  C CG2 . THR A 45  ? 0.8086 1.1747 1.0104 0.1075  -0.2606 0.0939  45  THR A CG2 
341  N N   . SER A 46  ? 0.7589 1.2097 1.0614 -0.0197 -0.2489 0.0659  46  SER A N   
342  C CA  . SER A 46  ? 0.8301 1.2927 1.1496 -0.0656 -0.2547 0.0572  46  SER A CA  
343  C C   . SER A 46  ? 0.9815 1.4073 1.2578 -0.0824 -0.2831 0.0471  46  SER A C   
344  O O   . SER A 46  ? 0.9487 1.3257 1.1969 -0.1118 -0.2804 0.0393  46  SER A O   
345  C CB  . SER A 46  ? 0.7409 1.3009 1.1358 -0.0798 -0.2609 0.0578  46  SER A CB  
346  O OG  . SER A 46  ? 0.9166 1.5202 1.3270 -0.0906 -0.2978 0.0515  46  SER A OG  
347  N N   . GLU A 47  ? 0.8980 1.3422 1.1633 -0.0617 -0.3110 0.0469  47  GLU A N   
348  C CA  . GLU A 47  ? 0.9277 1.3402 1.1479 -0.0752 -0.3400 0.0361  47  GLU A CA  
349  C C   . GLU A 47  ? 1.0487 1.3713 1.1925 -0.0633 -0.3292 0.0348  47  GLU A C   
350  O O   . GLU A 47  ? 1.0938 1.3783 1.1928 -0.0777 -0.3463 0.0234  47  GLU A O   
351  C CB  . GLU A 47  ? 1.0636 1.5289 1.2952 -0.0555 -0.3750 0.0374  47  GLU A CB  
352  C CG  . GLU A 47  ? 0.9667 1.5340 1.2790 -0.0679 -0.3906 0.0372  47  GLU A CG  
353  C CD  . GLU A 47  ? 1.0294 1.6484 1.3940 -0.0382 -0.3675 0.0499  47  GLU A CD  
354  O OE1 . GLU A 47  ? 0.9954 1.5683 1.3282 -0.0040 -0.3466 0.0589  47  GLU A OE1 
355  O OE2 . GLU A 47  ? 1.0400 1.7459 1.4769 -0.0499 -0.3697 0.0503  47  GLU A OE2 
356  N N   . ASP A 48  ? 1.0052 1.2949 1.1328 -0.0382 -0.3013 0.0455  48  ASP A N   
357  C CA  . ASP A 48  ? 1.0671 1.2809 1.1300 -0.0291 -0.2876 0.0456  48  ASP A CA  
358  C C   . ASP A 48  ? 1.0253 1.1956 1.0771 -0.0525 -0.2657 0.0390  48  ASP A C   
359  O O   . ASP A 48  ? 0.9931 1.1061 0.9937 -0.0495 -0.2574 0.0354  48  ASP A O   
360  C CB  . ASP A 48  ? 0.9767 1.1732 1.0262 0.0054  -0.2693 0.0605  48  ASP A CB  
361  C CG  . ASP A 48  ? 1.0344 1.2609 1.0847 0.0344  -0.2908 0.0691  48  ASP A CG  
362  O OD1 . ASP A 48  ? 0.9889 1.2297 1.0242 0.0317  -0.3206 0.0636  48  ASP A OD1 
363  O OD2 . ASP A 48  ? 0.9390 1.1714 1.0017 0.0611  -0.2791 0.0811  48  ASP A OD2 
364  N N   . MET A 49  ? 1.0124 1.2101 1.1102 -0.0744 -0.2558 0.0381  49  MET A N   
365  C CA  . MET A 49  ? 1.0314 1.1859 1.1184 -0.0919 -0.2336 0.0354  49  MET A CA  
366  C C   . MET A 49  ? 1.0172 1.1263 1.0665 -0.1153 -0.2465 0.0209  49  MET A C   
367  O O   . MET A 49  ? 0.8750 0.9305 0.8935 -0.1180 -0.2308 0.0177  49  MET A O   
368  C CB  . MET A 49  ? 0.9846 1.1802 1.1263 -0.1094 -0.2199 0.0402  49  MET A CB  
369  C CG  . MET A 49  ? 0.9104 1.1516 1.0891 -0.0840 -0.2061 0.0520  49  MET A CG  
370  S SD  . MET A 49  ? 0.9210 1.1994 1.1507 -0.1006 -0.1805 0.0580  49  MET A SD  
371  C CE  . MET A 49  ? 0.6517 0.9638 0.9033 -0.0588 -0.1657 0.0682  49  MET A CE  
372  N N   . LEU A 50  ? 1.0639 1.1922 1.1133 -0.1309 -0.2763 0.0110  50  LEU A N   
373  C CA  . LEU A 50  ? 1.1060 1.1866 1.1184 -0.1559 -0.2902 -0.0051 50  LEU A CA  
374  C C   . LEU A 50  ? 1.1710 1.1903 1.1143 -0.1355 -0.2892 -0.0127 50  LEU A C   
375  O O   . LEU A 50  ? 1.1896 1.1525 1.0941 -0.1466 -0.2881 -0.0251 50  LEU A O   
376  C CB  . LEU A 50  ? 1.0812 1.2011 1.1133 -0.1814 -0.3247 -0.0147 50  LEU A CB  
377  C CG  . LEU A 50  ? 1.1474 1.3418 1.2540 -0.2039 -0.3265 -0.0074 50  LEU A CG  
378  C CD1 . LEU A 50  ? 1.0108 1.2795 1.1513 -0.1972 -0.3550 -0.0064 50  LEU A CD1 
379  C CD2 . LEU A 50  ? 1.0793 1.2557 1.1946 -0.2505 -0.3316 -0.0159 50  LEU A CD2 
380  N N   . ASN A 51  ? 1.1245 1.1522 1.0494 -0.1053 -0.2885 -0.0050 51  ASN A N   
381  C CA  . ASN A 51  ? 1.0916 1.0687 0.9511 -0.0867 -0.2854 -0.0105 51  ASN A CA  
382  C C   . ASN A 51  ? 0.9736 0.9625 0.8239 -0.0553 -0.2750 0.0055  51  ASN A C   
383  O O   . ASN A 51  ? 1.0470 1.0430 0.8701 -0.0420 -0.2934 0.0066  51  ASN A O   
384  C CB  . ASN A 51  ? 1.0354 0.9971 0.8544 -0.0970 -0.3166 -0.0277 51  ASN A CB  
385  C CG  . ASN A 51  ? 1.2591 1.1747 1.0072 -0.0752 -0.3126 -0.0331 51  ASN A CG  
386  O OD1 . ASN A 51  ? 1.3116 1.2262 1.0225 -0.0703 -0.3362 -0.0399 51  ASN A OD1 
387  N ND2 . ASN A 51  ? 1.2489 1.1293 0.9776 -0.0621 -0.2824 -0.0299 51  ASN A ND2 
388  N N   . PRO A 52  ? 1.0110 0.9981 0.8794 -0.0437 -0.2472 0.0184  52  PRO A N   
389  C CA  . PRO A 52  ? 0.9030 0.8959 0.7636 -0.0174 -0.2377 0.0346  52  PRO A CA  
390  C C   . PRO A 52  ? 0.8850 0.8343 0.6876 -0.0030 -0.2246 0.0364  52  PRO A C   
391  O O   . PRO A 52  ? 0.9215 0.8377 0.6994 -0.0085 -0.2117 0.0273  52  PRO A O   
392  C CB  . PRO A 52  ? 0.7525 0.7581 0.6563 -0.0164 -0.2139 0.0449  52  PRO A CB  
393  C CG  . PRO A 52  ? 0.8788 0.8607 0.7855 -0.0360 -0.2018 0.0351  52  PRO A CG  
394  C CD  . PRO A 52  ? 0.9472 0.9259 0.8440 -0.0561 -0.2254 0.0193  52  PRO A CD  
395  N N   . ASN A 53  ? 0.8813 0.8321 0.6619 0.0168  -0.2275 0.0494  53  ASN A N   
396  C CA  . ASN A 53  ? 0.8213 0.7377 0.5545 0.0302  -0.2087 0.0579  53  ASN A CA  
397  C C   . ASN A 53  ? 0.8255 0.7456 0.5811 0.0412  -0.1914 0.0765  53  ASN A C   
398  O O   . ASN A 53  ? 0.8706 0.7977 0.6218 0.0565  -0.2012 0.0894  53  ASN A O   
399  C CB  . ASN A 53  ? 0.9555 0.8601 0.6330 0.0416  -0.2260 0.0591  53  ASN A CB  
400  C CG  . ASN A 53  ? 1.0378 0.9068 0.6608 0.0487  -0.2042 0.0629  53  ASN A CG  
401  O OD1 . ASN A 53  ? 1.0289 0.8881 0.6557 0.0527  -0.1792 0.0763  53  ASN A OD1 
402  N ND2 . ASN A 53  ? 1.0920 0.9429 0.6631 0.0495  -0.2134 0.0508  53  ASN A ND2 
403  N N   . TYR A 54  ? 0.8487 0.7604 0.6252 0.0343  -0.1672 0.0773  54  TYR A N   
404  C CA  . TYR A 54  ? 0.7982 0.7141 0.6026 0.0406  -0.1535 0.0907  54  TYR A CA  
405  C C   . TYR A 54  ? 0.8509 0.7431 0.6200 0.0553  -0.1472 0.1078  54  TYR A C   
406  O O   . TYR A 54  ? 0.8053 0.7000 0.5862 0.0677  -0.1506 0.1192  54  TYR A O   
407  C CB  . TYR A 54  ? 0.7188 0.6275 0.5451 0.0291  -0.1310 0.0872  54  TYR A CB  
408  C CG  . TYR A 54  ? 0.7066 0.6360 0.5726 0.0152  -0.1356 0.0759  54  TYR A CG  
409  C CD1 . TYR A 54  ? 0.5963 0.5530 0.5046 0.0154  -0.1376 0.0793  54  TYR A CD1 
410  C CD2 . TYR A 54  ? 0.6480 0.5669 0.5060 0.0024  -0.1370 0.0621  54  TYR A CD2 
411  C CE1 . TYR A 54  ? 0.6527 0.6294 0.5953 -0.0004 -0.1395 0.0711  54  TYR A CE1 
412  C CE2 . TYR A 54  ? 0.6098 0.5405 0.4991 -0.0133 -0.1410 0.0540  54  TYR A CE2 
413  C CZ  . TYR A 54  ? 0.6440 0.6054 0.5760 -0.0164 -0.1417 0.0594  54  TYR A CZ  
414  O OH  . TYR A 54  ? 0.6829 0.6572 0.6443 -0.0350 -0.1435 0.0533  54  TYR A OH  
415  N N   . GLU A 55  ? 0.7752 0.6425 0.4993 0.0544  -0.1366 0.1104  55  GLU A N   
416  C CA  . GLU A 55  ? 0.8294 0.6710 0.5176 0.0639  -0.1289 0.1292  55  GLU A CA  
417  C C   . GLU A 55  ? 0.9643 0.8041 0.6239 0.0800  -0.1531 0.1372  55  GLU A C   
418  O O   . GLU A 55  ? 0.9703 0.7848 0.6006 0.0906  -0.1512 0.1554  55  GLU A O   
419  C CB  . GLU A 55  ? 0.8790 0.7015 0.5304 0.0565  -0.1072 0.1315  55  GLU A CB  
420  C CG  . GLU A 55  ? 1.1479 0.9696 0.7599 0.0576  -0.1138 0.1203  55  GLU A CG  
421  C CD  . GLU A 55  ? 1.4027 1.2018 0.9532 0.0647  -0.1096 0.1346  55  GLU A CD  
422  O OE1 . GLU A 55  ? 1.4980 1.2788 1.0364 0.0672  -0.1025 0.1551  55  GLU A OE1 
423  O OE2 . GLU A 55  ? 1.5060 1.3018 1.0162 0.0671  -0.1127 0.1253  55  GLU A OE2 
424  N N   . ASP A 56  ? 0.9522 0.8166 0.6187 0.0812  -0.1775 0.1244  56  ASP A N   
425  C CA  . ASP A 56  ? 1.0623 0.9358 0.7134 0.0979  -0.2057 0.1309  56  ASP A CA  
426  C C   . ASP A 56  ? 0.9918 0.8936 0.6943 0.1095  -0.2168 0.1351  56  ASP A C   
427  O O   . ASP A 56  ? 0.8841 0.7846 0.5742 0.1308  -0.2330 0.1478  56  ASP A O   
428  C CB  . ASP A 56  ? 0.9644 0.8554 0.6007 0.0924  -0.2301 0.1143  56  ASP A CB  
429  C CG  . ASP A 56  ? 1.1544 1.0461 0.7528 0.1102  -0.2587 0.1227  56  ASP A CG  
430  O OD1 . ASP A 56  ? 1.3017 1.1584 0.8426 0.1205  -0.2527 0.1377  56  ASP A OD1 
431  O OD2 . ASP A 56  ? 1.2034 1.1328 0.8298 0.1131  -0.2879 0.1153  56  ASP A OD2 
432  N N   . LEU A 57  ? 0.7976 0.7251 0.5553 0.0980  -0.2080 0.1249  57  LEU A N   
433  C CA  . LEU A 57  ? 0.8341 0.7921 0.6417 0.1097  -0.2131 0.1278  57  LEU A CA  
434  C C   . LEU A 57  ? 0.8548 0.7816 0.6597 0.1212  -0.1929 0.1414  57  LEU A C   
435  O O   . LEU A 57  ? 0.8343 0.7732 0.6610 0.1415  -0.1993 0.1477  57  LEU A O   
436  C CB  . LEU A 57  ? 0.7640 0.7611 0.6274 0.0909  -0.2100 0.1124  57  LEU A CB  
437  C CG  . LEU A 57  ? 0.8442 0.8579 0.7090 0.0694  -0.2234 0.0959  57  LEU A CG  
438  C CD1 . LEU A 57  ? 0.7636 0.8056 0.6807 0.0496  -0.2155 0.0854  57  LEU A CD1 
439  C CD2 . LEU A 57  ? 0.7504 0.7950 0.6125 0.0775  -0.2569 0.0939  57  LEU A CD2 
440  N N   . LEU A 58  ? 0.7606 0.6486 0.5395 0.1090  -0.1695 0.1454  58  LEU A N   
441  C CA  . LEU A 58  ? 0.8233 0.6783 0.5987 0.1142  -0.1514 0.1565  58  LEU A CA  
442  C C   . LEU A 58  ? 0.8603 0.6741 0.5880 0.1326  -0.1574 0.1756  58  LEU A C   
443  O O   . LEU A 58  ? 0.9381 0.7295 0.6670 0.1483  -0.1553 0.1847  58  LEU A O   
444  C CB  . LEU A 58  ? 0.7392 0.5743 0.5090 0.0917  -0.1261 0.1539  58  LEU A CB  
445  C CG  . LEU A 58  ? 0.8004 0.6032 0.5700 0.0906  -0.1084 0.1625  58  LEU A CG  
446  C CD1 . LEU A 58  ? 0.8261 0.6478 0.6383 0.1010  -0.1101 0.1565  58  LEU A CD1 
447  C CD2 . LEU A 58  ? 0.9191 0.7130 0.6877 0.0673  -0.0868 0.1592  58  LEU A CD2 
448  N N   . ILE A 59  ? 0.8915 0.6900 0.5717 0.1318  -0.1646 0.1820  59  ILE A N   
449  C CA  . ILE A 59  ? 0.9288 0.6852 0.5572 0.1495  -0.1724 0.2025  59  ILE A CA  
450  C C   . ILE A 59  ? 0.9487 0.7219 0.5927 0.1800  -0.1983 0.2061  59  ILE A C   
451  O O   . ILE A 59  ? 0.9992 0.7325 0.6137 0.2010  -0.2032 0.2231  59  ILE A O   
452  C CB  . ILE A 59  ? 0.9932 0.7354 0.5650 0.1431  -0.1754 0.2077  59  ILE A CB  
453  C CG1 . ILE A 59  ? 1.1370 0.8201 0.6463 0.1489  -0.1689 0.2328  59  ILE A CG1 
454  C CG2 . ILE A 59  ? 1.0764 0.8532 0.6462 0.1559  -0.2064 0.1997  59  ILE A CG2 
455  C CD1 . ILE A 59  ? 1.1412 0.7942 0.6348 0.1237  -0.1367 0.2397  59  ILE A CD1 
456  N N   . ARG A 60  ? 0.9134 0.7458 0.6049 0.1832  -0.2152 0.1906  60  ARG A N   
457  C CA  . ARG A 60  ? 1.0274 0.8916 0.7433 0.2128  -0.2406 0.1927  60  ARG A CA  
458  C C   . ARG A 60  ? 0.9055 0.7780 0.6656 0.2278  -0.2309 0.1914  60  ARG A C   
459  O O   . ARG A 60  ? 0.9453 0.8505 0.7326 0.2561  -0.2490 0.1922  60  ARG A O   
460  C CB  . ARG A 60  ? 0.9383 0.8691 0.6904 0.2066  -0.2638 0.1767  60  ARG A CB  
461  C CG  . ARG A 60  ? 0.9404 0.8636 0.6441 0.1967  -0.2792 0.1753  60  ARG A CG  
462  C CD  . ARG A 60  ? 0.9145 0.8979 0.6563 0.1820  -0.2996 0.1557  60  ARG A CD  
463  N NE  . ARG A 60  ? 0.9468 0.9160 0.6391 0.1682  -0.3103 0.1493  60  ARG A NE  
464  C CZ  . ARG A 60  ? 1.0948 1.0659 0.7479 0.1819  -0.3397 0.1536  60  ARG A CZ  
465  N NH1 . ARG A 60  ? 1.0333 1.0204 0.6913 0.2115  -0.3630 0.1662  60  ARG A NH1 
466  N NH2 . ARG A 60  ? 1.0575 1.0131 0.6625 0.1678  -0.3465 0.1447  60  ARG A NH2 
467  N N   . LYS A 61  ? 0.8769 0.7234 0.6442 0.2114  -0.2034 0.1886  61  LYS A N   
468  C CA  . LYS A 61  ? 0.8577 0.7081 0.6610 0.2237  -0.1917 0.1848  61  LYS A CA  
469  C C   . LYS A 61  ? 0.9595 0.7343 0.7186 0.2332  -0.1790 0.1990  61  LYS A C   
470  O O   . LYS A 61  ? 0.9449 0.6697 0.6566 0.2160  -0.1696 0.2093  61  LYS A O   
471  C CB  . LYS A 61  ? 0.8699 0.7501 0.7165 0.1962  -0.1721 0.1688  61  LYS A CB  
472  C CG  . LYS A 61  ? 0.8244 0.7759 0.7195 0.1855  -0.1836 0.1546  61  LYS A CG  
473  C CD  . LYS A 61  ? 0.8994 0.9045 0.8459 0.2088  -0.1919 0.1502  61  LYS A CD  
474  C CE  . LYS A 61  ? 0.8001 0.8777 0.7991 0.1902  -0.2003 0.1367  61  LYS A CE  
475  N NZ  . LYS A 61  ? 0.8633 0.9359 0.8409 0.1619  -0.2082 0.1315  61  LYS A NZ  
476  N N   . SER A 62  ? 0.9191 0.6856 0.6935 0.2598  -0.1779 0.1989  62  SER A N   
477  C CA  . SER A 62  ? 0.9731 0.6622 0.7072 0.2679  -0.1662 0.2091  62  SER A CA  
478  C C   . SER A 62  ? 1.0026 0.6943 0.7687 0.2618  -0.1460 0.1954  62  SER A C   
479  O O   . SER A 62  ? 0.9257 0.6811 0.7454 0.2581  -0.1421 0.1803  62  SER A O   
480  C CB  . SER A 62  ? 1.1650 0.8210 0.8711 0.3119  -0.1849 0.2224  62  SER A CB  
481  O OG  . SER A 62  ? 1.1957 0.9180 0.9535 0.3434  -0.1982 0.2127  62  SER A OG  
482  N N   . ASN A 63  ? 1.0326 0.6511 0.7612 0.2589  -0.1335 0.2012  63  ASN A N   
483  C CA  . ASN A 63  ? 1.0278 0.6387 0.7757 0.2520  -0.1154 0.1879  63  ASN A CA  
484  C C   . ASN A 63  ? 1.0386 0.6980 0.8309 0.2851  -0.1178 0.1755  63  ASN A C   
485  O O   . ASN A 63  ? 1.0113 0.7174 0.8456 0.2738  -0.1055 0.1608  63  ASN A O   
486  C CB  . ASN A 63  ? 1.0163 0.5337 0.7108 0.2491  -0.1074 0.1963  63  ASN A CB  
487  C CG  . ASN A 63  ? 1.1341 0.6183 0.7995 0.2060  -0.0969 0.2046  63  ASN A CG  
488  O OD1 . ASN A 63  ? 1.0703 0.6028 0.7612 0.1788  -0.0908 0.1992  63  ASN A OD1 
489  N ND2 . ASN A 63  ? 1.0845 0.4861 0.6967 0.1994  -0.0943 0.2176  63  ASN A ND2 
490  N N   . HIS A 64  ? 0.9876 0.6392 0.7711 0.3275  -0.1334 0.1820  64  HIS A N   
491  C CA  . HIS A 64  ? 0.9820 0.6823 0.8083 0.3640  -0.1340 0.1707  64  HIS A CA  
492  C C   . HIS A 64  ? 0.9140 0.7214 0.8073 0.3583  -0.1390 0.1613  64  HIS A C   
493  O O   . HIS A 64  ? 0.9317 0.7947 0.8688 0.3853  -0.1377 0.1522  64  HIS A O   
494  C CB  . HIS A 64  ? 1.0603 0.7248 0.8592 0.4150  -0.1512 0.1810  64  HIS A CB  
495  C CG  . HIS A 64  ? 1.2019 0.9026 1.0046 0.4258  -0.1761 0.1921  64  HIS A CG  
496  N ND1 . HIS A 64  ? 1.1412 0.9396 1.0018 0.4410  -0.1903 0.1866  64  HIS A ND1 
497  C CD2 . HIS A 64  ? 1.1980 0.8544 0.9556 0.4186  -0.1882 0.2071  64  HIS A CD2 
498  C CE1 . HIS A 64  ? 1.2267 1.0350 1.0742 0.4446  -0.2128 0.1973  64  HIS A CE1 
499  N NE2 . HIS A 64  ? 1.2191 0.9414 1.0029 0.4322  -0.2109 0.2101  64  HIS A NE2 
500  N N   . ASN A 65  ? 0.8733 0.7106 0.7750 0.3236  -0.1439 0.1627  65  ASN A N   
501  C CA  . ASN A 65  ? 0.8110 0.7401 0.7728 0.3097  -0.1471 0.1523  65  ASN A CA  
502  C C   . ASN A 65  ? 0.8334 0.7841 0.8241 0.2803  -0.1238 0.1392  65  ASN A C   
503  O O   . ASN A 65  ? 0.7631 0.7858 0.8037 0.2674  -0.1235 0.1307  65  ASN A O   
504  C CB  . ASN A 65  ? 0.7983 0.7441 0.7514 0.2866  -0.1639 0.1573  65  ASN A CB  
505  C CG  . ASN A 65  ? 0.9154 0.8546 0.8442 0.3160  -0.1905 0.1699  65  ASN A CG  
506  O OD1 . ASN A 65  ? 0.9544 0.8555 0.8375 0.3050  -0.1997 0.1801  65  ASN A OD1 
507  N ND2 . ASN A 65  ? 0.9454 0.9245 0.9038 0.3553  -0.2030 0.1696  65  ASN A ND2 
508  N N   . PHE A 66  ? 0.7851 0.6747 0.7443 0.2681  -0.1058 0.1379  66  PHE A N   
509  C CA  . PHE A 66  ? 0.8849 0.7862 0.8621 0.2396  -0.0856 0.1271  66  PHE A CA  
510  C C   . PHE A 66  ? 0.8380 0.7290 0.8195 0.2615  -0.0700 0.1187  66  PHE A C   
511  O O   . PHE A 66  ? 0.9338 0.7557 0.8734 0.2761  -0.0665 0.1209  66  PHE A O   
512  C CB  . PHE A 66  ? 0.7230 0.5695 0.6626 0.2064  -0.0781 0.1306  66  PHE A CB  
513  C CG  . PHE A 66  ? 0.8027 0.6596 0.7354 0.1848  -0.0891 0.1365  66  PHE A CG  
514  C CD1 . PHE A 66  ? 0.7073 0.6115 0.6704 0.1596  -0.0878 0.1290  66  PHE A CD1 
515  C CD2 . PHE A 66  ? 0.7680 0.5822 0.6585 0.1898  -0.0999 0.1494  66  PHE A CD2 
516  C CE1 . PHE A 66  ? 0.7203 0.6287 0.6717 0.1423  -0.0975 0.1320  66  PHE A CE1 
517  C CE2 . PHE A 66  ? 0.8247 0.6480 0.7038 0.1717  -0.1081 0.1534  66  PHE A CE2 
518  C CZ  . PHE A 66  ? 0.8268 0.6971 0.7363 0.1491  -0.1070 0.1435  66  PHE A CZ  
519  N N   . LEU A 67  ? 0.7325 0.6893 0.7612 0.2624  -0.0601 0.1088  67  LEU A N   
520  C CA  . LEU A 67  ? 0.7191 0.6742 0.7522 0.2815  -0.0418 0.0989  67  LEU A CA  
521  C C   . LEU A 67  ? 0.7626 0.7053 0.7899 0.2469  -0.0238 0.0919  67  LEU A C   
522  O O   . LEU A 67  ? 0.6514 0.6417 0.7090 0.2186  -0.0207 0.0905  67  LEU A O   
523  C CB  . LEU A 67  ? 0.7606 0.8022 0.8495 0.3063  -0.0398 0.0937  67  LEU A CB  
524  C CG  . LEU A 67  ? 0.9002 0.9635 1.0041 0.3195  -0.0156 0.0819  67  LEU A CG  
525  C CD1 . LEU A 67  ? 0.8531 0.8501 0.9147 0.3597  -0.0110 0.0777  67  LEU A CD1 
526  C CD2 . LEU A 67  ? 0.8149 0.9832 0.9852 0.3315  -0.0121 0.0787  67  LEU A CD2 
527  N N   . VAL A 68  ? 0.7432 0.6181 0.7283 0.2484  -0.0140 0.0879  68  VAL A N   
528  C CA  . VAL A 68  ? 0.7160 0.5744 0.6900 0.2192  0.0006  0.0811  68  VAL A CA  
529  C C   . VAL A 68  ? 0.7875 0.6422 0.7560 0.2419  0.0176  0.0690  68  VAL A C   
530  O O   . VAL A 68  ? 0.7873 0.5907 0.7234 0.2710  0.0176  0.0654  68  VAL A O   
531  C CB  . VAL A 68  ? 0.7240 0.5094 0.6524 0.1960  -0.0038 0.0855  68  VAL A CB  
532  C CG1 . VAL A 68  ? 0.7309 0.5041 0.6496 0.1689  0.0086  0.0779  68  VAL A CG1 
533  C CG2 . VAL A 68  ? 0.6944 0.4872 0.6263 0.1763  -0.0175 0.0969  68  VAL A CG2 
534  N N   . GLN A 69  ? 0.6973 0.6024 0.6931 0.2294  0.0326  0.0628  69  GLN A N   
535  C CA  . GLN A 69  ? 0.7236 0.6342 0.7141 0.2497  0.0521  0.0509  69  GLN A CA  
536  C C   . GLN A 69  ? 0.7924 0.6791 0.7594 0.2196  0.0635  0.0456  69  GLN A C   
537  O O   . GLN A 69  ? 0.7383 0.6626 0.7278 0.1893  0.0661  0.0498  69  GLN A O   
538  C CB  . GLN A 69  ? 0.7480 0.7498 0.7933 0.2659  0.0624  0.0494  69  GLN A CB  
539  C CG  . GLN A 69  ? 0.8253 0.8714 0.9069 0.2848  0.0455  0.0572  69  GLN A CG  
540  C CD  . GLN A 69  ? 0.9211 1.0598 1.0582 0.3068  0.0561  0.0541  69  GLN A CD  
541  O OE1 . GLN A 69  ? 0.9336 1.1424 1.1195 0.2943  0.0471  0.0604  69  GLN A OE1 
542  N NE2 . GLN A 69  ? 0.9221 1.0634 1.0520 0.3391  0.0755  0.0435  69  GLN A NE2 
543  N N   . ALA A 70  ? 0.8968 0.7172 0.8154 0.2280  0.0683  0.0363  70  ALA A N   
544  C CA  . ALA A 70  ? 0.9487 0.7460 0.8399 0.2062  0.0785  0.0289  70  ALA A CA  
545  C C   . ALA A 70  ? 0.9418 0.7603 0.8294 0.2334  0.1001  0.0165  70  ALA A C   
546  O O   . ALA A 70  ? 1.0440 0.8160 0.8966 0.2635  0.1041  0.0054  70  ALA A O   
547  C CB  . ALA A 70  ? 0.8984 0.6102 0.7372 0.1938  0.0679  0.0257  70  ALA A CB  
548  N N   . GLY A 71  ? 0.9329 0.8195 0.8539 0.2229  0.1148  0.0185  71  GLY A N   
549  C CA  . GLY A 71  ? 1.0244 0.9477 0.9503 0.2497  0.1387  0.0087  71  GLY A CA  
550  C C   . GLY A 71  ? 1.0879 1.0472 1.0450 0.2914  0.1394  0.0074  71  GLY A C   
551  O O   . GLY A 71  ? 1.0679 1.0847 1.0755 0.2890  0.1303  0.0179  71  GLY A O   
552  N N   . ASN A 72  ? 1.1370 1.0612 1.0623 0.3321  0.1486  -0.0063 72  ASN A N   
553  C CA  . ASN A 72  ? 1.2188 1.1645 1.1658 0.3792  0.1465  -0.0082 72  ASN A CA  
554  C C   . ASN A 72  ? 1.2350 1.0939 1.1427 0.3951  0.1237  -0.0072 72  ASN A C   
555  O O   . ASN A 72  ? 1.2664 1.1346 1.1888 0.4341  0.1163  -0.0057 72  ASN A O   
556  C CB  . ASN A 72  ? 1.3012 1.2668 1.2395 0.4222  0.1729  -0.0243 72  ASN A CB  
557  C CG  . ASN A 72  ? 1.4797 1.3805 1.3537 0.4139  0.1866  -0.0386 72  ASN A CG  
558  O OD1 . ASN A 72  ? 1.5697 1.3726 1.3835 0.4168  0.1746  -0.0466 72  ASN A OD1 
559  N ND2 . ASN A 72  ? 1.5111 1.4650 1.3950 0.4014  0.2111  -0.0414 72  ASN A ND2 
560  N N   . VAL A 73  ? 1.2044 0.9816 1.0633 0.3655  0.1121  -0.0070 73  VAL A N   
561  C CA  . VAL A 73  ? 1.1537 0.8429 0.9705 0.3733  0.0920  -0.0042 73  VAL A CA  
562  C C   . VAL A 73  ? 1.1165 0.8279 0.9648 0.3528  0.0717  0.0146  73  VAL A C   
563  O O   . VAL A 73  ? 1.0424 0.7750 0.9067 0.3102  0.0671  0.0230  73  VAL A O   
564  C CB  . VAL A 73  ? 1.1989 0.7971 0.9530 0.3465  0.0883  -0.0119 73  VAL A CB  
565  C CG1 . VAL A 73  ? 1.2465 0.7703 0.9707 0.3323  0.0657  -0.0017 73  VAL A CG1 
566  C CG2 . VAL A 73  ? 1.3270 0.8753 1.0323 0.3785  0.1025  -0.0328 73  VAL A CG2 
567  N N   . GLN A 74  ? 1.0650 0.7700 0.9188 0.3855  0.0593  0.0210  74  GLN A N   
568  C CA  . GLN A 74  ? 0.9780 0.6949 0.8510 0.3706  0.0388  0.0384  74  GLN A CA  
569  C C   . GLN A 74  ? 1.0059 0.6278 0.8249 0.3462  0.0251  0.0450  74  GLN A C   
570  O O   . GLN A 74  ? 1.2442 0.7816 1.0106 0.3631  0.0235  0.0392  74  GLN A O   
571  C CB  . GLN A 74  ? 0.9832 0.7294 0.8789 0.4171  0.0290  0.0434  74  GLN A CB  
572  C CG  . GLN A 74  ? 1.1276 0.8911 1.0410 0.4055  0.0068  0.0610  74  GLN A CG  
573  C CD  . GLN A 74  ? 1.2729 1.1131 1.2351 0.4432  -0.0015 0.0649  74  GLN A CD  
574  O OE1 . GLN A 74  ? 1.2142 1.0360 1.1669 0.4624  -0.0219 0.0763  74  GLN A OE1 
575  N NE2 . GLN A 74  ? 1.2213 1.1505 1.2358 0.4534  0.0139  0.0563  74  GLN A NE2 
576  N N   . LEU A 75  ? 0.9710 0.6061 0.8022 0.3061  0.0158  0.0569  75  LEU A N   
577  C CA  . LEU A 75  ? 0.9929 0.5534 0.7816 0.2800  0.0041  0.0660  75  LEU A CA  
578  C C   . LEU A 75  ? 1.1456 0.7037 0.9362 0.2892  -0.0130 0.0827  75  LEU A C   
579  O O   . LEU A 75  ? 1.0341 0.6639 0.8684 0.2930  -0.0182 0.0886  75  LEU A O   
580  C CB  . LEU A 75  ? 0.9435 0.5179 0.7396 0.2305  0.0067  0.0674  75  LEU A CB  
581  C CG  . LEU A 75  ? 0.9478 0.5307 0.7420 0.2174  0.0212  0.0530  75  LEU A CG  
582  C CD1 . LEU A 75  ? 0.8969 0.5225 0.7164 0.1771  0.0222  0.0569  75  LEU A CD1 
583  C CD2 . LEU A 75  ? 0.9995 0.4949 0.7368 0.2146  0.0213  0.0438  75  LEU A CD2 
584  N N   . ARG A 76  ? 1.1484 0.6210 0.8878 0.2911  -0.0224 0.0906  76  ARG A N   
585  C CA  . ARG A 76  ? 1.1220 0.5770 0.8492 0.3012  -0.0386 0.1083  76  ARG A CA  
586  C C   . ARG A 76  ? 1.1166 0.5669 0.8376 0.2551  -0.0429 0.1210  76  ARG A C   
587  O O   . ARG A 76  ? 1.0420 0.4443 0.7350 0.2227  -0.0382 0.1205  76  ARG A O   
588  C CB  . ARG A 76  ? 1.2215 0.5795 0.8907 0.3307  -0.0459 0.1120  76  ARG A CB  
589  C CG  . ARG A 76  ? 1.3840 0.7306 1.0414 0.3508  -0.0632 0.1299  76  ARG A CG  
590  C CD  . ARG A 76  ? 1.4699 0.7460 1.0847 0.3666  -0.0674 0.1283  76  ARG A CD  
591  N NE  . ARG A 76  ? 1.5681 0.7729 1.1379 0.3255  -0.0691 0.1377  76  ARG A NE  
592  C CZ  . ARG A 76  ? 1.7286 0.8709 1.2644 0.3041  -0.0622 0.1281  76  ARG A CZ  
593  N NH1 . ARG A 76  ? 1.5224 0.6566 1.0570 0.3201  -0.0529 0.1082  76  ARG A NH1 
594  N NH2 . ARG A 76  ? 1.6822 0.7720 1.1845 0.2650  -0.0644 0.1385  76  ARG A NH2 
595  N N   . VAL A 77  ? 1.0517 0.5540 0.7986 0.2529  -0.0520 0.1316  77  VAL A N   
596  C CA  . VAL A 77  ? 0.9892 0.4957 0.7317 0.2144  -0.0546 0.1427  77  VAL A CA  
597  C C   . VAL A 77  ? 1.0462 0.4794 0.7360 0.2148  -0.0640 0.1606  77  VAL A C   
598  O O   . VAL A 77  ? 1.1438 0.5634 0.8193 0.2475  -0.0766 0.1698  77  VAL A O   
599  C CB  . VAL A 77  ? 0.9431 0.5336 0.7311 0.2114  -0.0602 0.1439  77  VAL A CB  
600  C CG1 . VAL A 77  ? 0.9672 0.5566 0.7436 0.1776  -0.0623 0.1544  77  VAL A CG1 
601  C CG2 . VAL A 77  ? 0.8607 0.5174 0.6969 0.2049  -0.0497 0.1286  77  VAL A CG2 
602  N N   . ILE A 78  ? 1.0383 0.4262 0.6991 0.1778  -0.0583 0.1666  78  ILE A N   
603  C CA  . ILE A 78  ? 1.1396 0.4543 0.7470 0.1690  -0.0639 0.1855  78  ILE A CA  
604  C C   . ILE A 78  ? 1.1327 0.4735 0.7409 0.1371  -0.0624 0.1986  78  ILE A C   
605  O O   . ILE A 78  ? 1.1185 0.4233 0.6952 0.1205  -0.0625 0.2122  78  ILE A O   
606  C CB  . ILE A 78  ? 1.2267 0.4789 0.8060 0.1465  -0.0567 0.1794  78  ILE A CB  
607  C CG1 . ILE A 78  ? 1.2614 0.5255 0.8528 0.1060  -0.0463 0.1731  78  ILE A CG1 
608  C CG2 . ILE A 78  ? 1.2311 0.4521 0.8015 0.1814  -0.0581 0.1649  78  ILE A CG2 
609  C CD1 . ILE A 78  ? 1.2728 0.4839 0.8392 0.0771  -0.0422 0.1677  78  ILE A CD1 
610  N N   . GLY A 79  ? 1.0860 0.5053 0.7397 0.1249  -0.0586 0.1906  79  GLY A N   
611  C CA  . GLY A 79  ? 0.9866 0.4329 0.6401 0.0997  -0.0563 0.2003  79  GLY A CA  
612  C C   . GLY A 79  ? 0.9206 0.4472 0.6242 0.0918  -0.0532 0.1872  79  GLY A C   
613  O O   . GLY A 79  ? 0.9255 0.4799 0.6615 0.0913  -0.0480 0.1720  79  GLY A O   
614  N N   . HIS A 80  ? 0.9109 0.4707 0.6165 0.0860  -0.0565 0.1928  80  HIS A N   
615  C CA  . HIS A 80  ? 0.9019 0.5282 0.6482 0.0778  -0.0550 0.1805  80  HIS A CA  
616  C C   . HIS A 80  ? 0.8967 0.5337 0.6302 0.0545  -0.0485 0.1866  80  HIS A C   
617  O O   . HIS A 80  ? 0.9384 0.5411 0.6326 0.0488  -0.0472 0.2019  80  HIS A O   
618  C CB  . HIS A 80  ? 0.9189 0.5879 0.6885 0.1035  -0.0697 0.1753  80  HIS A CB  
619  C CG  . HIS A 80  ? 0.9632 0.6231 0.7029 0.1176  -0.0837 0.1881  80  HIS A CG  
620  N ND1 . HIS A 80  ? 1.0470 0.7206 0.7713 0.1036  -0.0845 0.1921  80  HIS A ND1 
621  C CD2 . HIS A 80  ? 0.9649 0.6026 0.6839 0.1468  -0.0983 0.1976  80  HIS A CD2 
622  C CE1 . HIS A 80  ? 1.1353 0.7947 0.8283 0.1214  -0.0992 0.2039  80  HIS A CE1 
623  N NE2 . HIS A 80  ? 1.1090 0.7469 0.7992 0.1481  -0.1088 0.2081  80  HIS A NE2 
624  N N   . SER A 81  ? 0.8293 0.5127 0.5941 0.0420  -0.0436 0.1746  81  SER A N   
625  C CA  . SER A 81  ? 0.8831 0.5828 0.6401 0.0236  -0.0354 0.1768  81  SER A CA  
626  C C   . SER A 81  ? 0.8910 0.6385 0.6841 0.0196  -0.0349 0.1608  81  SER A C   
627  O O   . SER A 81  ? 0.7968 0.5591 0.6199 0.0216  -0.0355 0.1505  81  SER A O   
628  C CB  . SER A 81  ? 0.9384 0.6147 0.6824 -0.0010 -0.0203 0.1843  81  SER A CB  
629  O OG  . SER A 81  ? 0.9787 0.6763 0.7554 -0.0139 -0.0133 0.1724  81  SER A OG  
630  N N   . MET A 82  ? 0.8615 0.6288 0.6469 0.0147  -0.0332 0.1591  82  MET A N   
631  C CA  . MET A 82  ? 0.7997 0.6025 0.6104 0.0127  -0.0348 0.1443  82  MET A CA  
632  C C   . MET A 82  ? 0.8123 0.6256 0.6258 -0.0026 -0.0197 0.1418  82  MET A C   
633  O O   . MET A 82  ? 0.8828 0.6892 0.6717 -0.0091 -0.0102 0.1508  82  MET A O   
634  C CB  . MET A 82  ? 0.8718 0.6872 0.6688 0.0232  -0.0482 0.1408  82  MET A CB  
635  C CG  . MET A 82  ? 0.9120 0.7533 0.7263 0.0193  -0.0510 0.1252  82  MET A CG  
636  S SD  . MET A 82  ? 0.9714 0.8330 0.8009 0.0292  -0.0742 0.1169  82  MET A SD  
637  C CE  . MET A 82  ? 0.8843 0.7333 0.6677 0.0408  -0.0864 0.1256  82  MET A CE  
638  N N   . GLN A 83  ? 0.7644 0.5962 0.6075 -0.0077 -0.0170 0.1308  83  GLN A N   
639  C CA  . GLN A 83  ? 0.7826 0.6312 0.6340 -0.0173 -0.0052 0.1267  83  GLN A CA  
640  C C   . GLN A 83  ? 0.7006 0.5666 0.5659 -0.0116 -0.0108 0.1126  83  GLN A C   
641  O O   . GLN A 83  ? 0.5785 0.4491 0.4669 -0.0131 -0.0141 0.1061  83  GLN A O   
642  C CB  . GLN A 83  ? 0.6680 0.5151 0.5375 -0.0296 0.0019  0.1287  83  GLN A CB  
643  C CG  . GLN A 83  ? 0.9013 0.7744 0.7910 -0.0346 0.0085  0.1211  83  GLN A CG  
644  C CD  . GLN A 83  ? 0.9354 0.8151 0.8335 -0.0506 0.0179  0.1273  83  GLN A CD  
645  O OE1 . GLN A 83  ? 0.8999 0.7601 0.7983 -0.0598 0.0160  0.1316  83  GLN A OE1 
646  N NE2 . GLN A 83  ? 0.9136 0.8221 0.8186 -0.0539 0.0278  0.1269  83  GLN A NE2 
647  N N   . ASN A 84  ? 0.6106 0.4815 0.4572 -0.0054 -0.0119 0.1078  84  ASN A N   
648  C CA  . ASN A 84  ? 0.5765 0.4531 0.4281 -0.0004 -0.0193 0.0936  84  ASN A CA  
649  C C   . ASN A 84  ? 0.6870 0.5612 0.5539 -0.0006 -0.0342 0.0904  84  ASN A C   
650  O O   . ASN A 84  ? 0.7343 0.6054 0.5930 0.0035  -0.0430 0.0957  84  ASN A O   
651  C CB  . ASN A 84  ? 0.5383 0.4253 0.4068 -0.0020 -0.0102 0.0877  84  ASN A CB  
652  C CG  . ASN A 84  ? 0.5939 0.4952 0.4548 -0.0022 0.0058  0.0924  84  ASN A CG  
653  O OD1 . ASN A 84  ? 0.7436 0.6477 0.5800 0.0048  0.0109  0.0903  84  ASN A OD1 
654  N ND2 . ASN A 84  ? 0.5685 0.4817 0.4500 -0.0111 0.0141  0.0985  84  ASN A ND2 
655  N N   . CYS A 85  ? 0.5578 0.4353 0.4470 -0.0048 -0.0370 0.0831  85  CYS A N   
656  C CA  . CYS A 85  ? 0.5958 0.4784 0.5020 -0.0076 -0.0488 0.0803  85  CYS A CA  
657  C C   . CYS A 85  ? 0.5775 0.4647 0.5040 -0.0087 -0.0451 0.0874  85  CYS A C   
658  O O   . CYS A 85  ? 0.6057 0.5042 0.5515 -0.0108 -0.0509 0.0854  85  CYS A O   
659  C CB  . CYS A 85  ? 0.5116 0.3909 0.4260 -0.0140 -0.0530 0.0700  85  CYS A CB  
660  S SG  . CYS A 85  ? 0.6381 0.5026 0.5221 -0.0096 -0.0590 0.0580  85  CYS A SG  
661  N N   . VAL A 86  ? 0.5338 0.4128 0.4553 -0.0081 -0.0353 0.0950  86  VAL A N   
662  C CA  . VAL A 86  ? 0.5614 0.4364 0.4947 -0.0079 -0.0315 0.0996  86  VAL A CA  
663  C C   . VAL A 86  ? 0.6555 0.5174 0.5730 0.0004  -0.0334 0.1086  86  VAL A C   
664  O O   . VAL A 86  ? 0.6498 0.5000 0.5449 -0.0002 -0.0306 0.1150  86  VAL A O   
665  C CB  . VAL A 86  ? 0.5837 0.4526 0.5208 -0.0161 -0.0215 0.1001  86  VAL A CB  
666  C CG1 . VAL A 86  ? 0.6198 0.4753 0.5578 -0.0156 -0.0181 0.1041  86  VAL A CG1 
667  C CG2 . VAL A 86  ? 0.5959 0.4733 0.5469 -0.0208 -0.0218 0.0929  86  VAL A CG2 
668  N N   . LEU A 87  ? 0.5783 0.4419 0.5060 0.0095  -0.0376 0.1097  87  LEU A N   
669  C CA  . LEU A 87  ? 0.6153 0.4595 0.5264 0.0218  -0.0405 0.1184  87  LEU A CA  
670  C C   . LEU A 87  ? 0.6757 0.4936 0.5811 0.0192  -0.0312 0.1209  87  LEU A C   
671  O O   . LEU A 87  ? 0.6656 0.4902 0.5877 0.0166  -0.0264 0.1143  87  LEU A O   
672  C CB  . LEU A 87  ? 0.6319 0.4959 0.5583 0.0379  -0.0516 0.1170  87  LEU A CB  
673  C CG  . LEU A 87  ? 0.7843 0.6271 0.6970 0.0574  -0.0552 0.1249  87  LEU A CG  
674  C CD1 . LEU A 87  ? 0.8038 0.6217 0.6810 0.0620  -0.0618 0.1360  87  LEU A CD1 
675  C CD2 . LEU A 87  ? 0.7736 0.6503 0.7144 0.0748  -0.0639 0.1211  87  LEU A CD2 
676  N N   . LYS A 88  ? 0.6510 0.4361 0.5291 0.0182  -0.0290 0.1305  88  LYS A N   
677  C CA  . LYS A 88  ? 0.7437 0.4947 0.6095 0.0125  -0.0225 0.1328  88  LYS A CA  
678  C C   . LYS A 88  ? 0.7843 0.5014 0.6296 0.0315  -0.0280 0.1391  88  LYS A C   
679  O O   . LYS A 88  ? 0.8315 0.5283 0.6518 0.0368  -0.0327 0.1502  88  LYS A O   
680  C CB  . LYS A 88  ? 0.7731 0.5098 0.6231 -0.0086 -0.0151 0.1395  88  LYS A CB  
681  C CG  . LYS A 88  ? 0.7828 0.5511 0.6542 -0.0235 -0.0095 0.1324  88  LYS A CG  
682  C CD  . LYS A 88  ? 0.8319 0.5915 0.6955 -0.0447 -0.0017 0.1380  88  LYS A CD  
683  C CE  . LYS A 88  ? 0.9367 0.7019 0.7849 -0.0502 0.0033  0.1479  88  LYS A CE  
684  N NZ  . LYS A 88  ? 1.1268 0.8873 0.9697 -0.0737 0.0125  0.1555  88  LYS A NZ  
685  N N   . LEU A 89  ? 0.7588 0.4678 0.6113 0.0439  -0.0270 0.1323  89  LEU A N   
686  C CA  . LEU A 89  ? 0.7936 0.4702 0.6281 0.0684  -0.0320 0.1359  89  LEU A CA  
687  C C   . LEU A 89  ? 0.8783 0.4981 0.6843 0.0613  -0.0266 0.1358  89  LEU A C   
688  O O   . LEU A 89  ? 0.9115 0.5317 0.7257 0.0558  -0.0204 0.1250  89  LEU A O   
689  C CB  . LEU A 89  ? 0.7118 0.4248 0.5756 0.0916  -0.0339 0.1268  89  LEU A CB  
690  C CG  . LEU A 89  ? 0.7419 0.5118 0.6360 0.0955  -0.0417 0.1259  89  LEU A CG  
691  C CD1 . LEU A 89  ? 0.7491 0.5614 0.6778 0.1121  -0.0404 0.1170  89  LEU A CD1 
692  C CD2 . LEU A 89  ? 0.7175 0.4782 0.5929 0.1087  -0.0550 0.1369  89  LEU A CD2 
693  N N   . LYS A 90  ? 0.8459 0.4134 0.6146 0.0600  -0.0298 0.1479  90  LYS A N   
694  C CA  . LYS A 90  ? 0.9214 0.4249 0.6572 0.0505  -0.0270 0.1484  90  LYS A CA  
695  C C   . LYS A 90  ? 0.9683 0.4370 0.6895 0.0839  -0.0305 0.1423  90  LYS A C   
696  O O   . LYS A 90  ? 1.0023 0.4601 0.7128 0.1121  -0.0384 0.1495  90  LYS A O   
697  C CB  . LYS A 90  ? 1.0300 0.4875 0.7289 0.0325  -0.0281 0.1656  90  LYS A CB  
698  C CG  . LYS A 90  ? 1.2133 0.6001 0.8763 0.0147  -0.0264 0.1671  90  LYS A CG  
699  C CD  . LYS A 90  ? 1.3080 0.6911 0.9630 -0.0264 -0.0205 0.1781  90  LYS A CD  
700  C CE  . LYS A 90  ? 1.3481 0.6580 0.9621 -0.0433 -0.0216 0.1852  90  LYS A CE  
701  N NZ  . LYS A 90  ? 1.4160 0.7367 1.0268 -0.0766 -0.0146 0.1996  90  LYS A NZ  
702  N N   . VAL A 91  ? 0.9777 0.4298 0.6965 0.0831  -0.0252 0.1285  91  VAL A N   
703  C CA  . VAL A 91  ? 1.0459 0.4655 0.7490 0.1170  -0.0255 0.1195  91  VAL A CA  
704  C C   . VAL A 91  ? 1.1611 0.4897 0.8121 0.1085  -0.0272 0.1192  91  VAL A C   
705  O O   . VAL A 91  ? 1.2465 0.5478 0.8810 0.0719  -0.0273 0.1248  91  VAL A O   
706  C CB  . VAL A 91  ? 1.0364 0.5045 0.7709 0.1273  -0.0168 0.1023  91  VAL A CB  
707  C CG1 . VAL A 91  ? 0.9409 0.4885 0.7225 0.1422  -0.0170 0.1034  91  VAL A CG1 
708  C CG2 . VAL A 91  ? 0.9655 0.4431 0.7054 0.0920  -0.0111 0.0950  91  VAL A CG2 
709  N N   . ASP A 92  ? 1.2816 0.5637 0.9067 0.1431  -0.0286 0.1119  92  ASP A N   
710  C CA  . ASP A 92  ? 1.4171 0.5997 0.9849 0.1399  -0.0322 0.1104  92  ASP A CA  
711  C C   . ASP A 92  ? 1.4501 0.6100 1.0049 0.1221  -0.0270 0.0917  92  ASP A C   
712  O O   . ASP A 92  ? 1.4814 0.5842 1.0023 0.0994  -0.0308 0.0883  92  ASP A O   
713  C CB  . ASP A 92  ? 1.5198 0.6727 1.0694 0.1861  -0.0366 0.1077  92  ASP A CB  
714  C CG  . ASP A 92  ? 1.6564 0.8322 1.2201 0.2298  -0.0294 0.0909  92  ASP A CG  
715  O OD1 . ASP A 92  ? 1.6856 0.8619 1.2477 0.2203  -0.0207 0.0737  92  ASP A OD1 
716  O OD2 . ASP A 92  ? 1.6399 0.8491 1.2232 0.2712  -0.0319 0.0937  92  ASP A OD2 
717  N N   . THR A 93  ? 1.3462 0.5708 0.9366 0.1272  -0.0184 0.0777  93  THR A N   
718  C CA  . THR A 93  ? 1.3081 0.5153 0.8833 0.1143  -0.0140 0.0593  93  THR A CA  
719  C C   . THR A 93  ? 1.2177 0.4819 0.8253 0.0737  -0.0126 0.0603  93  THR A C   
720  O O   . THR A 93  ? 1.0826 0.4237 0.7363 0.0735  -0.0085 0.0657  93  THR A O   
721  C CB  . THR A 93  ? 1.2971 0.5297 0.8803 0.1540  -0.0036 0.0425  93  THR A CB  
722  O OG1 . THR A 93  ? 1.4065 0.6153 0.9783 0.1997  -0.0046 0.0445  93  THR A OG1 
723  C CG2 . THR A 93  ? 1.3943 0.5774 0.9379 0.1482  -0.0008 0.0224  93  THR A CG2 
724  N N   . ALA A 94  ? 1.2598 0.4852 0.8426 0.0399  -0.0176 0.0548  94  ALA A N   
725  C CA  . ALA A 94  ? 1.0672 0.3455 0.6782 0.0069  -0.0176 0.0527  94  ALA A CA  
726  C C   . ALA A 94  ? 1.1179 0.4227 0.7329 0.0215  -0.0108 0.0354  94  ALA A C   
727  O O   . ALA A 94  ? 1.1473 0.4007 0.7232 0.0365  -0.0098 0.0202  94  ALA A O   
728  C CB  . ALA A 94  ? 1.1329 0.3678 0.7198 -0.0358 -0.0274 0.0536  94  ALA A CB  
729  N N   . ASN A 95  ? 1.0403 0.4209 0.6978 0.0179  -0.0055 0.0379  95  ASN A N   
730  C CA  . ASN A 95  ? 0.9610 0.3710 0.6222 0.0291  0.0026  0.0250  95  ASN A CA  
731  C C   . ASN A 95  ? 1.1101 0.4781 0.7333 0.0093  -0.0041 0.0113  95  ASN A C   
732  O O   . ASN A 95  ? 1.0820 0.4572 0.7111 -0.0247 -0.0144 0.0150  95  ASN A O   
733  C CB  . ASN A 95  ? 0.9276 0.4161 0.6362 0.0203  0.0064  0.0329  95  ASN A CB  
734  C CG  . ASN A 95  ? 0.9339 0.4532 0.6449 0.0300  0.0162  0.0232  95  ASN A CG  
735  O OD1 . ASN A 95  ? 0.9247 0.4119 0.6024 0.0447  0.0217  0.0095  95  ASN A OD1 
736  N ND2 . ASN A 95  ? 0.8780 0.4561 0.6244 0.0218  0.0191  0.0304  95  ASN A ND2 
737  N N   . PRO A 96  ? 1.1153 0.4416 0.6991 0.0301  0.0009  -0.0054 96  PRO A N   
738  C CA  . PRO A 96  ? 1.1659 0.4486 0.7072 0.0108  -0.0077 -0.0206 96  PRO A CA  
739  C C   . PRO A 96  ? 1.0927 0.4284 0.6505 -0.0065 -0.0086 -0.0222 96  PRO A C   
740  O O   . PRO A 96  ? 1.1181 0.4314 0.6521 -0.0328 -0.0220 -0.0298 96  PRO A O   
741  C CB  . PRO A 96  ? 1.1588 0.3893 0.6536 0.0461  0.0016  -0.0390 96  PRO A CB  
742  C CG  . PRO A 96  ? 1.1863 0.4288 0.7016 0.0829  0.0125  -0.0313 96  PRO A CG  
743  C CD  . PRO A 96  ? 1.0555 0.3775 0.6324 0.0738  0.0146  -0.0122 96  PRO A CD  
744  N N   . LYS A 97  ? 1.0766 0.4791 0.6721 0.0066  0.0035  -0.0150 97  LYS A N   
745  C CA  . LYS A 97  ? 1.1147 0.5626 0.7225 -0.0074 0.0026  -0.0139 97  LYS A CA  
746  C C   . LYS A 97  ? 0.9872 0.4827 0.6395 -0.0314 -0.0063 0.0020  97  LYS A C   
747  O O   . LYS A 97  ? 0.9884 0.5295 0.6607 -0.0358 -0.0048 0.0072  97  LYS A O   
748  C CB  . LYS A 97  ? 1.0220 0.5097 0.6394 0.0181  0.0220  -0.0150 97  LYS A CB  
749  C CG  . LYS A 97  ? 1.0693 0.5218 0.6515 0.0498  0.0357  -0.0299 97  LYS A CG  
750  C CD  . LYS A 97  ? 1.1483 0.6469 0.7382 0.0695  0.0566  -0.0313 97  LYS A CD  
751  C CE  . LYS A 97  ? 1.2869 0.8306 0.9209 0.0935  0.0707  -0.0227 97  LYS A CE  
752  N NZ  . LYS A 97  ? 1.4259 0.9920 1.0518 0.1226  0.0941  -0.0314 97  LYS A NZ  
753  N N   . THR A 98  ? 0.9943 0.4773 0.6589 -0.0459 -0.0147 0.0101  98  THR A N   
754  C CA  . THR A 98  ? 0.9412 0.4697 0.6462 -0.0660 -0.0212 0.0239  98  THR A CA  
755  C C   . THR A 98  ? 0.9323 0.4742 0.6351 -0.0910 -0.0349 0.0209  98  THR A C   
756  O O   . THR A 98  ? 0.9792 0.4843 0.6564 -0.1106 -0.0471 0.0136  98  THR A O   
757  C CB  . THR A 98  ? 1.0044 0.5134 0.7161 -0.0771 -0.0252 0.0331  98  THR A CB  
758  O OG1 . THR A 98  ? 1.0341 0.5345 0.7486 -0.0511 -0.0151 0.0374  98  THR A OG1 
759  C CG2 . THR A 98  ? 0.8661 0.4253 0.6174 -0.0966 -0.0295 0.0459  98  THR A CG2 
760  N N   . PRO A 99  ? 0.8938 0.4854 0.6215 -0.0916 -0.0352 0.0265  99  PRO A N   
761  C CA  . PRO A 99  ? 0.7934 0.4030 0.5221 -0.1118 -0.0506 0.0251  99  PRO A CA  
762  C C   . PRO A 99  ? 0.8312 0.4720 0.5960 -0.1320 -0.0591 0.0352  99  PRO A C   
763  O O   . PRO A 99  ? 0.8238 0.4752 0.6115 -0.1293 -0.0513 0.0444  99  PRO A O   
764  C CB  . PRO A 99  ? 0.7925 0.4372 0.5300 -0.0982 -0.0453 0.0289  99  PRO A CB  
765  C CG  . PRO A 99  ? 0.8589 0.5262 0.6262 -0.0825 -0.0305 0.0384  99  PRO A CG  
766  C CD  . PRO A 99  ? 0.8678 0.5003 0.6238 -0.0740 -0.0229 0.0348  99  PRO A CD  
767  N N   . LYS A 100 ? 0.7737 0.4325 0.5425 -0.1518 -0.0754 0.0333  100 LYS A N   
768  C CA  . LYS A 100 ? 0.8199 0.5268 0.6307 -0.1666 -0.0813 0.0433  100 LYS A CA  
769  C C   . LYS A 100 ? 0.7657 0.5142 0.6068 -0.1465 -0.0715 0.0529  100 LYS A C   
770  O O   . LYS A 100 ? 0.7657 0.5197 0.5988 -0.1307 -0.0698 0.0520  100 LYS A O   
771  C CB  . LYS A 100 ? 0.8869 0.6171 0.7014 -0.1864 -0.1020 0.0392  100 LYS A CB  
772  C CG  . LYS A 100 ? 0.9883 0.6888 0.7861 -0.2172 -0.1149 0.0321  100 LYS A CG  
773  C CD  . LYS A 100 ? 1.0963 0.7219 0.8416 -0.2132 -0.1109 0.0203  100 LYS A CD  
774  C CE  . LYS A 100 ? 1.1713 0.7553 0.8993 -0.2449 -0.1206 0.0158  100 LYS A CE  
775  N NZ  . LYS A 100 ? 1.2800 0.7844 0.9578 -0.2345 -0.1132 0.0063  100 LYS A NZ  
776  N N   . TYR A 101 ? 0.4855 0.4220 0.5804 -0.1097 0.0371  -0.0551 101 TYR A N   
777  C CA  . TYR A 101 ? 0.5321 0.4890 0.6254 -0.0898 0.0343  -0.0411 101 TYR A CA  
778  C C   . TYR A 101 ? 0.5315 0.5075 0.6603 -0.0914 0.0474  -0.0352 101 TYR A C   
779  O O   . TYR A 101 ? 0.4615 0.4273 0.6104 -0.1050 0.0663  -0.0375 101 TYR A O   
780  C CB  . TYR A 101 ? 0.5578 0.4869 0.6112 -0.0707 0.0455  -0.0285 101 TYR A CB  
781  C CG  . TYR A 101 ? 0.5770 0.4740 0.6205 -0.0689 0.0724  -0.0207 101 TYR A CG  
782  C CD1 . TYR A 101 ? 0.6374 0.4971 0.6658 -0.0773 0.0864  -0.0256 101 TYR A CD1 
783  C CD2 . TYR A 101 ? 0.6251 0.5240 0.6694 -0.0577 0.0849  -0.0082 101 TYR A CD2 
784  C CE1 . TYR A 101 ? 0.7195 0.5448 0.7351 -0.0737 0.1127  -0.0164 101 TYR A CE1 
785  C CE2 . TYR A 101 ? 0.6135 0.4788 0.6416 -0.0539 0.1100  0.0007  101 TYR A CE2 
786  C CZ  . TYR A 101 ? 0.7051 0.5338 0.7196 -0.0614 0.1241  -0.0025 101 TYR A CZ  
787  O OH  . TYR A 101 ? 0.9557 0.7462 0.9505 -0.0558 0.1505  0.0083  101 TYR A OH  
788  N N   . LYS A 102 ? 0.4407 0.4417 0.5760 -0.0774 0.0394  -0.0275 102 LYS A N   
789  C CA  . LYS A 102 ? 0.4502 0.4621 0.6058 -0.0717 0.0554  -0.0192 102 LYS A CA  
790  C C   . LYS A 102 ? 0.4444 0.4486 0.5678 -0.0504 0.0546  -0.0077 102 LYS A C   
791  O O   . LYS A 102 ? 0.4137 0.4166 0.5135 -0.0422 0.0383  -0.0070 102 LYS A O   
792  C CB  . LYS A 102 ? 0.4453 0.5005 0.6513 -0.0774 0.0456  -0.0240 102 LYS A CB  
793  C CG  . LYS A 102 ? 0.5011 0.5771 0.7403 -0.0977 0.0298  -0.0386 102 LYS A CG  
794  C CD  . LYS A 102 ? 0.5305 0.6546 0.8110 -0.0952 0.0088  -0.0414 102 LYS A CD  
795  C CE  . LYS A 102 ? 0.7156 0.8700 1.0587 -0.1068 0.0227  -0.0435 102 LYS A CE  
796  N NZ  . LYS A 102 ? 0.6754 0.8781 1.0676 -0.1158 -0.0051 -0.0539 102 LYS A NZ  
797  N N   . PHE A 103 ? 0.4148 0.4123 0.5367 -0.0424 0.0732  0.0006  103 PHE A N   
798  C CA  . PHE A 103 ? 0.3919 0.3841 0.4868 -0.0242 0.0714  0.0089  103 PHE A CA  
799  C C   . PHE A 103 ? 0.4140 0.4326 0.5371 -0.0201 0.0705  0.0086  103 PHE A C   
800  O O   . PHE A 103 ? 0.3913 0.4149 0.5388 -0.0233 0.0901  0.0099  103 PHE A O   
801  C CB  . PHE A 103 ? 0.5411 0.4994 0.6021 -0.0152 0.0925  0.0183  103 PHE A CB  
802  C CG  . PHE A 103 ? 0.5961 0.5284 0.6240 -0.0114 0.0908  0.0216  103 PHE A CG  
803  C CD1 . PHE A 103 ? 0.5622 0.5013 0.5894 -0.0148 0.0729  0.0162  103 PHE A CD1 
804  C CD2 . PHE A 103 ? 0.6872 0.5865 0.6827 -0.0023 0.1085  0.0311  103 PHE A CD2 
805  C CE1 . PHE A 103 ? 0.6077 0.5238 0.6078 -0.0090 0.0742  0.0200  103 PHE A CE1 
806  C CE2 . PHE A 103 ? 0.6795 0.5564 0.6474 0.0045  0.1070  0.0356  103 PHE A CE2 
807  C CZ  . PHE A 103 ? 0.6437 0.5303 0.6166 0.0012  0.0906  0.0299  103 PHE A CZ  
808  N N   . VAL A 104 ? 0.3612 0.3948 0.4819 -0.0123 0.0505  0.0078  104 VAL A N   
809  C CA  . VAL A 104 ? 0.3718 0.4285 0.5182 -0.0056 0.0481  0.0081  104 VAL A CA  
810  C C   . VAL A 104 ? 0.4282 0.4711 0.5424 0.0092  0.0430  0.0124  104 VAL A C   
811  O O   . VAL A 104 ? 0.5327 0.5621 0.6170 0.0115  0.0311  0.0133  104 VAL A O   
812  C CB  . VAL A 104 ? 0.4486 0.5382 0.6287 -0.0115 0.0266  0.0020  104 VAL A CB  
813  C CG1 . VAL A 104 ? 0.4414 0.5558 0.6514 -0.0012 0.0254  0.0041  104 VAL A CG1 
814  C CG2 . VAL A 104 ? 0.4329 0.5347 0.6430 -0.0297 0.0278  -0.0055 104 VAL A CG2 
815  N N   . ARG A 105 ? 0.3590 0.4048 0.4814 0.0189  0.0532  0.0145  105 ARG A N   
816  C CA  . ARG A 105 ? 0.3643 0.3953 0.4588 0.0316  0.0482  0.0163  105 ARG A CA  
817  C C   . ARG A 105 ? 0.4104 0.4633 0.5304 0.0373  0.0354  0.0156  105 ARG A C   
818  O O   . ARG A 105 ? 0.3639 0.4414 0.5237 0.0391  0.0414  0.0156  105 ARG A O   
819  C CB  . ARG A 105 ? 0.4691 0.4772 0.5428 0.0411  0.0708  0.0187  105 ARG A CB  
820  C CG  . ARG A 105 ? 0.4068 0.3906 0.4415 0.0515  0.0648  0.0179  105 ARG A CG  
821  C CD  . ARG A 105 ? 0.4607 0.4169 0.4668 0.0614  0.0877  0.0189  105 ARG A CD  
822  N NE  . ARG A 105 ? 0.4643 0.3956 0.4339 0.0702  0.0811  0.0152  105 ARG A NE  
823  C CZ  . ARG A 105 ? 0.5409 0.4476 0.4660 0.0701  0.0698  0.0128  105 ARG A CZ  
824  N NH1 . ARG A 105 ? 0.4792 0.3832 0.3896 0.0650  0.0646  0.0156  105 ARG A NH1 
825  N NH2 . ARG A 105 ? 0.5037 0.3879 0.3994 0.0755  0.0630  0.0071  105 ARG A NH2 
826  N N   . ILE A 106 ? 0.3480 0.3927 0.4472 0.0407  0.0185  0.0160  106 ILE A N   
827  C CA  . ILE A 106 ? 0.3833 0.4421 0.4988 0.0479  0.0061  0.0174  106 ILE A CA  
828  C C   . ILE A 106 ? 0.5180 0.5579 0.6201 0.0616  0.0154  0.0189  106 ILE A C   
829  O O   . ILE A 106 ? 0.4787 0.4909 0.5490 0.0634  0.0251  0.0172  106 ILE A O   
830  C CB  . ILE A 106 ? 0.4366 0.4931 0.5363 0.0439  -0.0141 0.0182  106 ILE A CB  
831  C CG1 . ILE A 106 ? 0.4333 0.4631 0.4962 0.0407  -0.0144 0.0179  106 ILE A CG1 
832  C CG2 . ILE A 106 ? 0.4456 0.5219 0.5610 0.0332  -0.0244 0.0156  106 ILE A CG2 
833  C CD1 . ILE A 106 ? 0.5659 0.5847 0.6132 0.0427  -0.0259 0.0204  106 ILE A CD1 
834  N N   . GLN A 107 ? 0.3743 0.4274 0.4985 0.0724  0.0114  0.0217  107 GLN A N   
835  C CA  . GLN A 107 ? 0.4385 0.4723 0.5531 0.0877  0.0212  0.0233  107 GLN A CA  
836  C C   . GLN A 107 ? 0.4966 0.5058 0.5816 0.0897  0.0081  0.0246  107 GLN A C   
837  O O   . GLN A 107 ? 0.4301 0.4457 0.5115 0.0822  -0.0085 0.0264  107 GLN A O   
838  C CB  . GLN A 107 ? 0.5258 0.5889 0.6857 0.1012  0.0258  0.0273  107 GLN A CB  
839  C CG  . GLN A 107 ? 0.5079 0.5940 0.7030 0.0993  0.0450  0.0262  107 GLN A CG  
840  C CD  . GLN A 107 ? 0.5778 0.6413 0.7627 0.1128  0.0730  0.0264  107 GLN A CD  
841  O OE1 . GLN A 107 ? 0.6509 0.6893 0.8147 0.1271  0.0761  0.0273  107 GLN A OE1 
842  N NE2 . GLN A 107 ? 0.5460 0.6127 0.7410 0.1085  0.0955  0.0254  107 GLN A NE2 
843  N N   . PRO A 108 ? 0.5178 0.4951 0.5793 0.0991  0.0173  0.0232  108 PRO A N   
844  C CA  . PRO A 108 ? 0.6418 0.5940 0.6808 0.1005  0.0074  0.0250  108 PRO A CA  
845  C C   . PRO A 108 ? 0.5777 0.5494 0.6399 0.1099  -0.0039 0.0337  108 PRO A C   
846  O O   . PRO A 108 ? 0.5377 0.5333 0.6321 0.1234  -0.0006 0.0378  108 PRO A O   
847  C CB  . PRO A 108 ? 0.5352 0.4496 0.5503 0.1111  0.0229  0.0208  108 PRO A CB  
848  C CG  . PRO A 108 ? 0.6257 0.5394 0.6363 0.1113  0.0390  0.0155  108 PRO A CG  
849  C CD  . PRO A 108 ? 0.5276 0.4856 0.5788 0.1086  0.0392  0.0197  108 PRO A CD  
850  N N   . GLY A 109 ? 0.5735 0.5360 0.6198 0.1035  -0.0173 0.0372  109 GLY A N   
851  C CA  . GLY A 109 ? 0.4677 0.4426 0.5244 0.1129  -0.0298 0.0464  109 GLY A CA  
852  C C   . GLY A 109 ? 0.5492 0.5575 0.6202 0.1043  -0.0451 0.0472  109 GLY A C   
853  O O   . GLY A 109 ? 0.5045 0.5147 0.5686 0.1086  -0.0582 0.0541  109 GLY A O   
854  N N   . GLN A 110 ? 0.4950 0.5248 0.5811 0.0929  -0.0429 0.0403  110 GLN A N   
855  C CA  . GLN A 110 ? 0.3749 0.4296 0.4703 0.0828  -0.0563 0.0387  110 GLN A CA  
856  C C   . GLN A 110 ? 0.5160 0.5515 0.5797 0.0704  -0.0602 0.0383  110 GLN A C   
857  O O   . GLN A 110 ? 0.4727 0.4832 0.5158 0.0658  -0.0523 0.0375  110 GLN A O   
858  C CB  . GLN A 110 ? 0.3536 0.4321 0.4751 0.0736  -0.0496 0.0317  110 GLN A CB  
859  C CG  . GLN A 110 ? 0.5348 0.6452 0.7004 0.0830  -0.0479 0.0322  110 GLN A CG  
860  C CD  . GLN A 110 ? 0.6415 0.7704 0.8336 0.0717  -0.0357 0.0259  110 GLN A CD  
861  O OE1 . GLN A 110 ? 0.6034 0.7248 0.8010 0.0753  -0.0151 0.0253  110 GLN A OE1 
862  N NE2 . GLN A 110 ? 0.6816 0.8299 0.8864 0.0578  -0.0467 0.0209  110 GLN A NE2 
863  N N   . THR A 111 ? 0.4422 0.4906 0.5035 0.0651  -0.0727 0.0384  111 THR A N   
864  C CA  . THR A 111 ? 0.4522 0.4850 0.4863 0.0555  -0.0741 0.0389  111 THR A CA  
865  C C   . THR A 111 ? 0.4109 0.4558 0.4496 0.0427  -0.0736 0.0313  111 THR A C   
866  O O   . THR A 111 ? 0.4748 0.5405 0.5367 0.0399  -0.0754 0.0259  111 THR A O   
867  C CB  . THR A 111 ? 0.5052 0.5316 0.5194 0.0619  -0.0858 0.0460  111 THR A CB  
868  O OG1 . THR A 111 ? 0.4518 0.5040 0.4809 0.0660  -0.1013 0.0438  111 THR A OG1 
869  C CG2 . THR A 111 ? 0.4891 0.4933 0.4916 0.0746  -0.0828 0.0555  111 THR A CG2 
870  N N   . PHE A 112 ? 0.4303 0.4610 0.4487 0.0350  -0.0695 0.0314  112 PHE A N   
871  C CA  . PHE A 112 ? 0.3889 0.4242 0.4059 0.0252  -0.0674 0.0255  112 PHE A CA  
872  C C   . PHE A 112 ? 0.4823 0.5024 0.4753 0.0221  -0.0645 0.0288  112 PHE A C   
873  O O   . PHE A 112 ? 0.5594 0.5665 0.5414 0.0249  -0.0618 0.0353  112 PHE A O   
874  C CB  . PHE A 112 ? 0.4669 0.5036 0.4953 0.0209  -0.0564 0.0216  112 PHE A CB  
875  C CG  . PHE A 112 ? 0.4489 0.4718 0.4690 0.0226  -0.0496 0.0243  112 PHE A CG  
876  C CD1 . PHE A 112 ? 0.4590 0.4758 0.4816 0.0292  -0.0484 0.0260  112 PHE A CD1 
877  C CD2 . PHE A 112 ? 0.5021 0.5181 0.5126 0.0178  -0.0453 0.0244  112 PHE A CD2 
878  C CE1 . PHE A 112 ? 0.6230 0.6241 0.6350 0.0284  -0.0443 0.0257  112 PHE A CE1 
879  C CE2 . PHE A 112 ? 0.4809 0.4877 0.4862 0.0178  -0.0434 0.0252  112 PHE A CE2 
880  C CZ  . PHE A 112 ? 0.4163 0.4142 0.4205 0.0218  -0.0436 0.0248  112 PHE A CZ  
881  N N   . SER A 113 ? 0.4369 0.4569 0.4230 0.0161  -0.0627 0.0242  113 SER A N   
882  C CA  . SER A 113 ? 0.5266 0.5333 0.4926 0.0143  -0.0559 0.0269  113 SER A CA  
883  C C   . SER A 113 ? 0.4975 0.5040 0.4724 0.0113  -0.0450 0.0269  113 SER A C   
884  O O   . SER A 113 ? 0.4443 0.4562 0.4307 0.0094  -0.0429 0.0227  113 SER A O   
885  C CB  . SER A 113 ? 0.3972 0.3989 0.3450 0.0117  -0.0596 0.0213  113 SER A CB  
886  O OG  . SER A 113 ? 0.5339 0.5356 0.4683 0.0161  -0.0733 0.0219  113 SER A OG  
887  N N   . VAL A 114 ? 0.3975 0.3984 0.3682 0.0114  -0.0379 0.0325  114 VAL A N   
888  C CA  . VAL A 114 ? 0.4431 0.4488 0.4258 0.0102  -0.0313 0.0335  114 VAL A CA  
889  C C   . VAL A 114 ? 0.4681 0.4704 0.4443 0.0111  -0.0211 0.0358  114 VAL A C   
890  O O   . VAL A 114 ? 0.4892 0.4840 0.4542 0.0115  -0.0157 0.0401  114 VAL A O   
891  C CB  . VAL A 114 ? 0.4792 0.4867 0.4727 0.0084  -0.0327 0.0371  114 VAL A CB  
892  C CG1 . VAL A 114 ? 0.4638 0.4809 0.4712 0.0072  -0.0296 0.0380  114 VAL A CG1 
893  C CG2 . VAL A 114 ? 0.4572 0.4634 0.4538 0.0095  -0.0396 0.0339  114 VAL A CG2 
894  N N   . LEU A 115 ? 0.4373 0.4423 0.4185 0.0131  -0.0161 0.0340  115 LEU A N   
895  C CA  . LEU A 115 ? 0.5273 0.5291 0.5056 0.0170  -0.0039 0.0367  115 LEU A CA  
896  C C   . LEU A 115 ? 0.4803 0.4985 0.4829 0.0197  -0.0020 0.0422  115 LEU A C   
897  O O   . LEU A 115 ? 0.5653 0.5887 0.5751 0.0237  -0.0046 0.0418  115 LEU A O   
898  C CB  . LEU A 115 ? 0.5141 0.5035 0.4796 0.0190  0.0010  0.0311  115 LEU A CB  
899  C CG  . LEU A 115 ? 0.5913 0.5713 0.5493 0.0256  0.0164  0.0331  115 LEU A CG  
900  C CD1 . LEU A 115 ? 0.5469 0.5132 0.4821 0.0253  0.0234  0.0329  115 LEU A CD1 
901  C CD2 . LEU A 115 ? 0.5448 0.5087 0.4924 0.0274  0.0216  0.0276  115 LEU A CD2 
902  N N   . ALA A 116 ? 0.4859 0.5123 0.5014 0.0172  0.0019  0.0475  116 ALA A N   
903  C CA  . ALA A 116 ? 0.4923 0.5400 0.5378 0.0178  0.0015  0.0518  116 ALA A CA  
904  C C   . ALA A 116 ? 0.5187 0.5726 0.5719 0.0281  0.0123  0.0552  116 ALA A C   
905  O O   . ALA A 116 ? 0.5787 0.6212 0.6199 0.0322  0.0277  0.0569  116 ALA A O   
906  C CB  . ALA A 116 ? 0.5688 0.6233 0.6309 0.0102  0.0067  0.0565  116 ALA A CB  
907  N N   . CYS A 117 ? 0.4204 0.4894 0.4898 0.0341  0.0046  0.0564  117 CYS A N   
908  C CA  A CYS A 117 ? 0.5519 0.6246 0.6274 0.0476  0.0140  0.0609  117 CYS A CA  
909  C CA  B CYS A 117 ? 0.5401 0.6128 0.6155 0.0477  0.0139  0.0608  117 CYS A CA  
910  C C   . CYS A 117 ? 0.6020 0.7072 0.7141 0.0531  0.0051  0.0663  117 CYS A C   
911  O O   . CYS A 117 ? 0.4453 0.5625 0.5655 0.0475  -0.0133 0.0637  117 CYS A O   
912  C CB  A CYS A 117 ? 0.5178 0.5681 0.5663 0.0538  0.0136  0.0575  117 CYS A CB  
913  C CB  B CYS A 117 ? 0.5139 0.5646 0.5627 0.0539  0.0131  0.0576  117 CYS A CB  
914  S SG  A CYS A 117 ? 0.6625 0.6788 0.6751 0.0487  0.0251  0.0501  117 CYS A SG  
915  S SG  B CYS A 117 ? 0.7163 0.7479 0.7527 0.0687  0.0337  0.0606  117 CYS A SG  
916  N N   . TYR A 118 ? 0.5334 0.6528 0.6673 0.0646  0.0179  0.0734  118 TYR A N   
917  C CA  . TYR A 118 ? 0.5415 0.6984 0.7175 0.0724  0.0089  0.0796  118 TYR A CA  
918  C C   . TYR A 118 ? 0.5519 0.7071 0.7286 0.0944  0.0201  0.0868  118 TYR A C   
919  O O   . TYR A 118 ? 0.5177 0.6559 0.6848 0.1013  0.0436  0.0890  118 TYR A O   
920  C CB  . TYR A 118 ? 0.3347 0.5210 0.5542 0.0631  0.0157  0.0828  118 TYR A CB  
921  C CG  . TYR A 118 ? 0.5735 0.7545 0.7893 0.0420  0.0072  0.0765  118 TYR A CG  
922  C CD1 . TYR A 118 ? 0.5666 0.7180 0.7526 0.0340  0.0211  0.0745  118 TYR A CD1 
923  C CD2 . TYR A 118 ? 0.4786 0.6808 0.7166 0.0312  -0.0157 0.0722  118 TYR A CD2 
924  C CE1 . TYR A 118 ? 0.5151 0.6581 0.6958 0.0178  0.0145  0.0704  118 TYR A CE1 
925  C CE2 . TYR A 118 ? 0.4919 0.6828 0.7236 0.0129  -0.0212 0.0662  118 TYR A CE2 
926  C CZ  . TYR A 118 ? 0.5036 0.6647 0.7075 0.0072  -0.0051 0.0663  118 TYR A CZ  
927  O OH  . TYR A 118 ? 0.5455 0.6923 0.7417 -0.0080 -0.0093 0.0622  118 TYR A OH  
928  N N   . ASN A 119 ? 0.5292 0.6968 0.7114 0.1067  0.0038  0.0906  119 ASN A N   
929  C CA  . ASN A 119 ? 0.6159 0.7795 0.7972 0.1310  0.0130  0.0995  119 ASN A CA  
930  C C   . ASN A 119 ? 0.6120 0.7260 0.7473 0.1354  0.0340  0.0970  119 ASN A C   
931  O O   . ASN A 119 ? 0.6746 0.7763 0.8079 0.1527  0.0530  0.1029  119 ASN A O   
932  C CB  . ASN A 119 ? 0.5251 0.7250 0.7569 0.1430  0.0249  0.1085  119 ASN A CB  
933  C CG  . ASN A 119 ? 0.6846 0.9382 0.9677 0.1442  0.0000  0.1124  119 ASN A CG  
934  O OD1 . ASN A 119 ? 0.7707 1.0294 1.0436 0.1485  -0.0255 0.1120  119 ASN A OD1 
935  N ND2 . ASN A 119 ? 0.7689 1.0621 1.1069 0.1396  0.0074  0.1156  119 ASN A ND2 
936  N N   . GLY A 120 ? 0.5999 0.6851 0.7000 0.1196  0.0309  0.0875  120 GLY A N   
937  C CA  . GLY A 120 ? 0.6234 0.6640 0.6833 0.1195  0.0466  0.0827  120 GLY A CA  
938  C C   . GLY A 120 ? 0.6696 0.6918 0.7169 0.1119  0.0651  0.0768  120 GLY A C   
939  O O   . GLY A 120 ? 0.7143 0.6990 0.7279 0.1094  0.0760  0.0702  120 GLY A O   
940  N N   . SER A 121 ? 0.6547 0.6997 0.7257 0.1074  0.0694  0.0784  121 SER A N   
941  C CA  . SER A 121 ? 0.6358 0.6601 0.6875 0.1020  0.0878  0.0739  121 SER A CA  
942  C C   . SER A 121 ? 0.7358 0.7663 0.7848 0.0831  0.0776  0.0690  121 SER A C   
943  O O   . SER A 121 ? 0.5803 0.6423 0.6625 0.0776  0.0691  0.0733  121 SER A O   
944  C CB  . SER A 121 ? 0.5189 0.5567 0.5951 0.1161  0.1097  0.0823  121 SER A CB  
945  O OG  . SER A 121 ? 0.7458 0.8312 0.8747 0.1203  0.1004  0.0912  121 SER A OG  
946  N N   . PRO A 122 ? 0.7400 0.7414 0.7517 0.0728  0.0770  0.0600  122 PRO A N   
947  C CA  . PRO A 122 ? 0.6306 0.6361 0.6379 0.0583  0.0665  0.0571  122 PRO A CA  
948  C C   . PRO A 122 ? 0.5789 0.5927 0.5969 0.0576  0.0807  0.0633  122 PRO A C   
949  O O   . PRO A 122 ? 0.7037 0.7072 0.7149 0.0667  0.1023  0.0664  122 PRO A O   
950  C CB  . PRO A 122 ? 0.6718 0.6451 0.6372 0.0516  0.0636  0.0468  122 PRO A CB  
951  C CG  . PRO A 122 ? 0.7552 0.7120 0.7108 0.0576  0.0666  0.0429  122 PRO A CG  
952  C CD  . PRO A 122 ? 0.6263 0.5905 0.6000 0.0735  0.0826  0.0515  122 PRO A CD  
953  N N   . SER A 123 ? 0.6135 0.6423 0.6467 0.0467  0.0709  0.0654  123 SER A N   
954  C CA  . SER A 123 ? 0.5823 0.6164 0.6267 0.0432  0.0858  0.0724  123 SER A CA  
955  C C   . SER A 123 ? 0.4872 0.5001 0.5009 0.0338  0.0823  0.0709  123 SER A C   
956  O O   . SER A 123 ? 0.5919 0.5954 0.5979 0.0331  0.1000  0.0772  123 SER A O   
957  C CB  . SER A 123 ? 0.5861 0.6589 0.6854 0.0386  0.0813  0.0785  123 SER A CB  
958  O OG  . SER A 123 ? 0.6592 0.7355 0.7628 0.0250  0.0635  0.0757  123 SER A OG  
959  N N   . GLY A 124 ? 0.5126 0.5175 0.5091 0.0281  0.0618  0.0642  124 GLY A N   
960  C CA  . GLY A 124 ? 0.4404 0.4272 0.4097 0.0225  0.0568  0.0643  124 GLY A CA  
961  C C   . GLY A 124 ? 0.5554 0.5377 0.5110 0.0196  0.0350  0.0563  124 GLY A C   
962  O O   . GLY A 124 ? 0.4575 0.4524 0.4296 0.0192  0.0244  0.0517  124 GLY A O   
963  N N   . VAL A 125 ? 0.5200 0.4841 0.4450 0.0189  0.0293  0.0558  125 VAL A N   
964  C CA  . VAL A 125 ? 0.5425 0.5058 0.4592 0.0171  0.0094  0.0494  125 VAL A CA  
965  C C   . VAL A 125 ? 0.5278 0.4834 0.4357 0.0166  0.0039  0.0554  125 VAL A C   
966  O O   . VAL A 125 ? 0.5048 0.4437 0.3915 0.0189  0.0148  0.0629  125 VAL A O   
967  C CB  . VAL A 125 ? 0.5658 0.5151 0.4523 0.0190  0.0037  0.0405  125 VAL A CB  
968  C CG1 . VAL A 125 ? 0.5678 0.4927 0.4136 0.0235  0.0126  0.0432  125 VAL A CG1 
969  C CG2 . VAL A 125 ? 0.5220 0.4777 0.4101 0.0165  -0.0167 0.0345  125 VAL A CG2 
970  N N   . TYR A 126 ? 0.4275 0.3916 0.3490 0.0149  -0.0105 0.0530  126 TYR A N   
971  C CA  . TYR A 126 ? 0.5287 0.4828 0.4424 0.0168  -0.0154 0.0590  126 TYR A CA  
972  C C   . TYR A 126 ? 0.5660 0.5297 0.4908 0.0185  -0.0315 0.0536  126 TYR A C   
973  O O   . TYR A 126 ? 0.5190 0.4974 0.4613 0.0160  -0.0359 0.0462  126 TYR A O   
974  C CB  . TYR A 126 ? 0.6195 0.5711 0.5509 0.0111  -0.0041 0.0662  126 TYR A CB  
975  C CG  . TYR A 126 ? 0.5074 0.4781 0.4734 0.0042  -0.0072 0.0611  126 TYR A CG  
976  C CD1 . TYR A 126 ? 0.5106 0.4831 0.4857 0.0034  -0.0186 0.0569  126 TYR A CD1 
977  C CD2 . TYR A 126 ? 0.5491 0.5350 0.5363 0.0004  0.0010  0.0608  126 TYR A CD2 
978  C CE1 . TYR A 126 ? 0.5965 0.5819 0.5941 -0.0020 -0.0227 0.0515  126 TYR A CE1 
979  C CE2 . TYR A 126 ? 0.5948 0.5983 0.6094 -0.0042 -0.0057 0.0564  126 TYR A CE2 
980  C CZ  . TYR A 126 ? 0.6293 0.6306 0.6456 -0.0059 -0.0181 0.0513  126 TYR A CZ  
981  O OH  . TYR A 126 ? 0.5839 0.5983 0.6187 -0.0097 -0.0260 0.0462  126 TYR A OH  
982  N N   . GLN A 127 ? 0.5180 0.4718 0.4323 0.0243  -0.0380 0.0587  127 GLN A N   
983  C CA  . GLN A 127 ? 0.6045 0.5678 0.5308 0.0290  -0.0511 0.0552  127 GLN A CA  
984  C C   . GLN A 127 ? 0.5870 0.5470 0.5310 0.0271  -0.0473 0.0564  127 GLN A C   
985  O O   . GLN A 127 ? 0.6834 0.6270 0.6232 0.0242  -0.0385 0.0625  127 GLN A O   
986  C CB  . GLN A 127 ? 0.6323 0.5878 0.5372 0.0401  -0.0622 0.0604  127 GLN A CB  
987  C CG  . GLN A 127 ? 0.6043 0.5803 0.5272 0.0458  -0.0779 0.0549  127 GLN A CG  
988  C CD  . GLN A 127 ? 0.6634 0.6589 0.5969 0.0388  -0.0845 0.0435  127 GLN A CD  
989  O OE1 . GLN A 127 ? 0.6801 0.6958 0.6341 0.0405  -0.0958 0.0382  127 GLN A OE1 
990  N NE2 . GLN A 127 ? 0.6551 0.6439 0.5768 0.0309  -0.0759 0.0400  127 GLN A NE2 
991  N N   . CYS A 128 ? 0.5642 0.5369 0.5265 0.0278  -0.0524 0.0497  128 CYS A N   
992  C CA  . CYS A 128 ? 0.6052 0.5716 0.5784 0.0264  -0.0493 0.0479  128 CYS A CA  
993  C C   . CYS A 128 ? 0.4900 0.4607 0.4713 0.0361  -0.0544 0.0461  128 CYS A C   
994  O O   . CYS A 128 ? 0.5639 0.5513 0.5523 0.0411  -0.0613 0.0445  128 CYS A O   
995  C CB  . CYS A 128 ? 0.5124 0.4881 0.4975 0.0180  -0.0464 0.0411  128 CYS A CB  
996  S SG  . CYS A 128 ? 0.9732 0.9423 0.9627 0.0069  -0.0403 0.0427  128 CYS A SG  
997  N N   . ALA A 129 ? 0.6162 0.5720 0.5986 0.0381  -0.0502 0.0453  129 ALA A N   
998  C CA  . ALA A 129 ? 0.5821 0.5394 0.5735 0.0488  -0.0501 0.0435  129 ALA A CA  
999  C C   . ALA A 129 ? 0.5939 0.5424 0.5856 0.0446  -0.0436 0.0356  129 ALA A C   
1000 O O   . ALA A 129 ? 0.5342 0.4675 0.5166 0.0352  -0.0418 0.0328  129 ALA A O   
1001 C CB  . ALA A 129 ? 0.5893 0.5270 0.5721 0.0611  -0.0498 0.0516  129 ALA A CB  
1002 N N   . MET A 130 ? 0.5238 0.4824 0.5263 0.0514  -0.0401 0.0318  130 MET A N   
1003 C CA  . MET A 130 ? 0.4703 0.4148 0.4647 0.0512  -0.0322 0.0247  130 MET A CA  
1004 C C   . MET A 130 ? 0.5109 0.4276 0.4950 0.0603  -0.0265 0.0250  130 MET A C   
1005 O O   . MET A 130 ? 0.5377 0.4581 0.5333 0.0745  -0.0227 0.0293  130 MET A O   
1006 C CB  . MET A 130 ? 0.5570 0.5195 0.5650 0.0552  -0.0257 0.0219  130 MET A CB  
1007 C CG  . MET A 130 ? 0.5482 0.4922 0.5404 0.0579  -0.0147 0.0156  130 MET A CG  
1008 S SD  . MET A 130 ? 0.7012 0.6338 0.6680 0.0459  -0.0195 0.0097  130 MET A SD  
1009 C CE  . MET A 130 ? 0.5574 0.5181 0.5405 0.0409  -0.0203 0.0130  130 MET A CE  
1010 N N   . ARG A 131 ? 0.4637 0.3523 0.4280 0.0523  -0.0262 0.0202  131 ARG A N   
1011 C CA  . ARG A 131 ? 0.4992 0.3530 0.4491 0.0591  -0.0193 0.0189  131 ARG A CA  
1012 C C   . ARG A 131 ? 0.5024 0.3464 0.4467 0.0718  -0.0079 0.0135  131 ARG A C   
1013 O O   . ARG A 131 ? 0.5069 0.3659 0.4530 0.0712  -0.0051 0.0094  131 ARG A O   
1014 C CB  . ARG A 131 ? 0.5606 0.3865 0.4923 0.0434  -0.0224 0.0120  131 ARG A CB  
1015 C CG  . ARG A 131 ? 0.6061 0.4408 0.5464 0.0299  -0.0290 0.0177  131 ARG A CG  
1016 C CD  . ARG A 131 ? 0.6003 0.4319 0.5444 0.0395  -0.0261 0.0307  131 ARG A CD  
1017 N NE  . ARG A 131 ? 0.6224 0.4171 0.5530 0.0500  -0.0177 0.0330  131 ARG A NE  
1018 C CZ  . ARG A 131 ? 0.7464 0.5320 0.6751 0.0643  -0.0148 0.0454  131 ARG A CZ  
1019 N NH1 . ARG A 131 ? 0.7034 0.5139 0.6397 0.0687  -0.0212 0.0555  131 ARG A NH1 
1020 N NH2 . ARG A 131 ? 0.5952 0.3428 0.5101 0.0756  -0.0055 0.0476  131 ARG A NH2 
1021 N N   . PRO A 132 ? 0.5922 0.4082 0.5283 0.0849  0.0016  0.0145  132 PRO A N   
1022 C CA  . PRO A 132 ? 0.6230 0.4246 0.5509 0.0986  0.0168  0.0091  132 PRO A CA  
1023 C C   . PRO A 132 ? 0.7028 0.4792 0.5978 0.0888  0.0191  -0.0045 132 PRO A C   
1024 O O   . PRO A 132 ? 0.6683 0.4389 0.5536 0.0985  0.0325  -0.0088 132 PRO A O   
1025 C CB  . PRO A 132 ? 0.5977 0.3662 0.5185 0.1141  0.0262  0.0130  132 PRO A CB  
1026 C CG  . PRO A 132 ? 0.6575 0.4408 0.5949 0.1147  0.0153  0.0256  132 PRO A CG  
1027 C CD  . PRO A 132 ? 0.5553 0.3525 0.4905 0.0918  0.0016  0.0233  132 PRO A CD  
1028 N N   . ASN A 133 ? 0.6391 0.4008 0.5165 0.0704  0.0066  -0.0114 133 ASN A N   
1029 C CA  . ASN A 133 ? 0.6811 0.4232 0.5266 0.0606  0.0025  -0.0248 133 ASN A CA  
1030 C C   . ASN A 133 ? 0.6712 0.4476 0.5244 0.0525  -0.0076 -0.0239 133 ASN A C   
1031 O O   . ASN A 133 ? 0.6554 0.4208 0.4829 0.0444  -0.0160 -0.0333 133 ASN A O   
1032 C CB  . ASN A 133 ? 0.7267 0.4358 0.5530 0.0442  -0.0076 -0.0345 133 ASN A CB  
1033 C CG  . ASN A 133 ? 0.6718 0.4069 0.5233 0.0268  -0.0224 -0.0292 133 ASN A CG  
1034 O OD1 . ASN A 133 ? 0.7223 0.4961 0.6002 0.0283  -0.0253 -0.0187 133 ASN A OD1 
1035 N ND2 . ASN A 133 ? 0.6839 0.3959 0.5276 0.0095  -0.0304 -0.0372 133 ASN A ND2 
1036 N N   . PHE A 134 ? 0.5991 0.4144 0.4847 0.0549  -0.0081 -0.0130 134 PHE A N   
1037 C CA  . PHE A 134 ? 0.5911 0.4353 0.4846 0.0506  -0.0127 -0.0107 134 PHE A CA  
1038 C C   . PHE A 134 ? 0.5814 0.4381 0.4782 0.0352  -0.0297 -0.0116 134 PHE A C   
1039 O O   . PHE A 134 ? 0.7541 0.6268 0.6496 0.0326  -0.0344 -0.0110 134 PHE A O   
1040 C CB  . PHE A 134 ? 0.5308 0.3605 0.3965 0.0574  -0.0032 -0.0163 134 PHE A CB  
1041 C CG  . PHE A 134 ? 0.6729 0.5045 0.5485 0.0726  0.0178  -0.0122 134 PHE A CG  
1042 C CD1 . PHE A 134 ? 0.5775 0.4445 0.4893 0.0750  0.0230  -0.0035 134 PHE A CD1 
1043 C CD2 . PHE A 134 ? 0.6640 0.4623 0.5155 0.0842  0.0330  -0.0178 134 PHE A CD2 
1044 C CE1 . PHE A 134 ? 0.6988 0.5741 0.6296 0.0874  0.0422  0.0001  134 PHE A CE1 
1045 C CE2 . PHE A 134 ? 0.7165 0.5211 0.5846 0.0994  0.0550  -0.0131 134 PHE A CE2 
1046 C CZ  . PHE A 134 ? 0.7410 0.5872 0.6525 0.1004  0.0591  -0.0038 134 PHE A CZ  
1047 N N   . THR A 135 ? 0.5455 0.3946 0.4481 0.0258  -0.0370 -0.0120 135 THR A N   
1048 C CA  . THR A 135 ? 0.5240 0.3922 0.4421 0.0120  -0.0492 -0.0100 135 THR A CA  
1049 C C   . THR A 135 ? 0.5355 0.4229 0.4781 0.0132  -0.0460 0.0014  135 THR A C   
1050 O O   . THR A 135 ? 0.5238 0.4086 0.4707 0.0238  -0.0384 0.0070  135 THR A O   
1051 C CB  . THR A 135 ? 0.6755 0.5223 0.5861 -0.0023 -0.0576 -0.0184 135 THR A CB  
1052 O OG1 . THR A 135 ? 0.5557 0.3808 0.4691 -0.0022 -0.0496 -0.0149 135 THR A OG1 
1053 C CG2 . THR A 135 ? 0.5908 0.4103 0.4679 -0.0024 -0.0621 -0.0320 135 THR A CG2 
1054 N N   . ILE A 136 ? 0.4877 0.3944 0.4455 0.0035  -0.0522 0.0050  136 ILE A N   
1055 C CA  . ILE A 136 ? 0.5372 0.4557 0.5098 0.0037  -0.0489 0.0150  136 ILE A CA  
1056 C C   . ILE A 136 ? 0.6211 0.5365 0.6030 -0.0101 -0.0506 0.0164  136 ILE A C   
1057 O O   . ILE A 136 ? 0.5424 0.4645 0.5309 -0.0207 -0.0578 0.0104  136 ILE A O   
1058 C CB  . ILE A 136 ? 0.5806 0.5265 0.5631 0.0075  -0.0491 0.0194  136 ILE A CB  
1059 C CG1 . ILE A 136 ? 0.6403 0.6024 0.6304 -0.0002 -0.0543 0.0179  136 ILE A CG1 
1060 C CG2 . ILE A 136 ? 0.6045 0.5544 0.5832 0.0176  -0.0455 0.0172  136 ILE A CG2 
1061 C CD1 . ILE A 136 ? 0.5566 0.5383 0.5529 0.0039  -0.0519 0.0219  136 ILE A CD1 
1062 N N   . LYS A 137 ? 0.6264 0.5316 0.6094 -0.0096 -0.0437 0.0248  137 LYS A N   
1063 C CA  . LYS A 137 ? 0.6626 0.5630 0.6563 -0.0230 -0.0398 0.0284  137 LYS A CA  
1064 C C   . LYS A 137 ? 0.6270 0.5517 0.6322 -0.0229 -0.0360 0.0365  137 LYS A C   
1065 O O   . LYS A 137 ? 0.6999 0.6170 0.6985 -0.0193 -0.0275 0.0463  137 LYS A O   
1066 C CB  . LYS A 137 ? 0.6618 0.5280 0.6432 -0.0216 -0.0307 0.0342  137 LYS A CB  
1067 C CG  . LYS A 137 ? 0.7262 0.5631 0.6916 -0.0170 -0.0314 0.0267  137 LYS A CG  
1068 C CD  . LYS A 137 ? 0.9097 0.7064 0.8660 -0.0223 -0.0216 0.0300  137 LYS A CD  
1069 C CE  . LYS A 137 ? 0.9536 0.7167 0.8890 -0.0106 -0.0186 0.0252  137 LYS A CE  
1070 N NZ  . LYS A 137 ? 1.1148 0.8433 1.0360 0.0001  -0.0067 0.0372  137 LYS A NZ  
1071 N N   . GLY A 138 ? 0.5477 0.4985 0.5660 -0.0253 -0.0419 0.0326  138 GLY A N   
1072 C CA  . GLY A 138 ? 0.5392 0.5108 0.5667 -0.0233 -0.0370 0.0387  138 GLY A CA  
1073 C C   . GLY A 138 ? 0.5539 0.5353 0.6048 -0.0352 -0.0303 0.0422  138 GLY A C   
1074 O O   . GLY A 138 ? 0.5462 0.5172 0.6079 -0.0473 -0.0290 0.0406  138 GLY A O   
1075 N N   . SER A 139 ? 0.5227 0.5237 0.5836 -0.0320 -0.0242 0.0470  139 SER A N   
1076 C CA  . SER A 139 ? 0.5900 0.6084 0.6811 -0.0410 -0.0156 0.0511  139 SER A CA  
1077 C C   . SER A 139 ? 0.6079 0.6561 0.7163 -0.0354 -0.0215 0.0490  139 SER A C   
1078 O O   . SER A 139 ? 0.4921 0.5433 0.5893 -0.0246 -0.0148 0.0526  139 SER A O   
1079 C CB  . SER A 139 ? 0.5028 0.5092 0.5852 -0.0393 0.0045  0.0620  139 SER A CB  
1080 O OG  . SER A 139 ? 0.6358 0.6638 0.7500 -0.0446 0.0169  0.0668  139 SER A OG  
1081 N N   . PHE A 140 ? 0.4172 0.4846 0.5500 -0.0422 -0.0349 0.0429  140 PHE A N   
1082 C CA  . PHE A 140 ? 0.5404 0.6339 0.6862 -0.0341 -0.0445 0.0415  140 PHE A CA  
1083 C C   . PHE A 140 ? 0.4821 0.6071 0.6730 -0.0440 -0.0516 0.0404  140 PHE A C   
1084 O O   . PHE A 140 ? 0.5246 0.6478 0.7296 -0.0597 -0.0596 0.0344  140 PHE A O   
1085 C CB  . PHE A 140 ? 0.4999 0.5838 0.6197 -0.0277 -0.0609 0.0337  140 PHE A CB  
1086 C CG  . PHE A 140 ? 0.5556 0.6200 0.6425 -0.0165 -0.0545 0.0349  140 PHE A CG  
1087 C CD1 . PHE A 140 ? 0.4601 0.5290 0.5431 -0.0066 -0.0444 0.0403  140 PHE A CD1 
1088 C CD2 . PHE A 140 ? 0.5725 0.6141 0.6345 -0.0162 -0.0580 0.0299  140 PHE A CD2 
1089 C CE1 . PHE A 140 ? 0.5001 0.5528 0.5573 0.0004  -0.0402 0.0396  140 PHE A CE1 
1090 C CE2 . PHE A 140 ? 0.5152 0.5453 0.5561 -0.0073 -0.0528 0.0307  140 PHE A CE2 
1091 C CZ  . PHE A 140 ? 0.5006 0.5370 0.5401 -0.0005 -0.0451 0.0350  140 PHE A CZ  
1092 N N   . LEU A 141 ? 0.4633 0.6174 0.6788 -0.0349 -0.0491 0.0459  141 LEU A N   
1093 C CA  . LEU A 141 ? 0.5410 0.7345 0.8066 -0.0411 -0.0593 0.0454  141 LEU A CA  
1094 C C   . LEU A 141 ? 0.5338 0.7459 0.7972 -0.0271 -0.0799 0.0433  141 LEU A C   
1095 O O   . LEU A 141 ? 0.4447 0.6363 0.6679 -0.0134 -0.0816 0.0432  141 LEU A O   
1096 C CB  . LEU A 141 ? 0.4805 0.6971 0.7855 -0.0402 -0.0365 0.0559  141 LEU A CB  
1097 C CG  . LEU A 141 ? 0.5409 0.7361 0.8447 -0.0530 -0.0134 0.0602  141 LEU A CG  
1098 C CD1 . LEU A 141 ? 0.5293 0.7403 0.8596 -0.0471 0.0144  0.0718  141 LEU A CD1 
1099 C CD2 . LEU A 141 ? 0.4718 0.6700 0.8026 -0.0765 -0.0224 0.0535  141 LEU A CD2 
1100 N N   . ASN A 142 ? 0.4962 0.7481 0.8047 -0.0307 -0.0957 0.0421  142 ASN A N   
1101 C CA  . ASN A 142 ? 0.4816 0.7524 0.7874 -0.0146 -0.1170 0.0421  142 ASN A CA  
1102 C C   . ASN A 142 ? 0.5122 0.7797 0.8048 0.0088  -0.1000 0.0534  142 ASN A C   
1103 O O   . ASN A 142 ? 0.5087 0.7855 0.8244 0.0127  -0.0766 0.0618  142 ASN A O   
1104 C CB  . ASN A 142 ? 0.5036 0.8253 0.8687 -0.0209 -0.1374 0.0404  142 ASN A CB  
1105 C CG  . ASN A 142 ? 0.7051 1.0323 1.0521 -0.0175 -0.1733 0.0314  142 ASN A CG  
1106 O OD1 . ASN A 142 ? 0.8667 1.1962 1.1924 0.0048  -0.1826 0.0369  142 ASN A OD1 
1107 N ND2 . ASN A 142 ? 0.6255 0.9500 0.9758 -0.0393 -0.1930 0.0174  142 ASN A ND2 
1108 N N   . GLY A 143 ? 0.4832 0.7329 0.7354 0.0245  -0.1097 0.0534  143 GLY A N   
1109 C CA  . GLY A 143 ? 0.3860 0.6227 0.6182 0.0452  -0.0933 0.0625  143 GLY A CA  
1110 C C   . GLY A 143 ? 0.4926 0.6858 0.6793 0.0441  -0.0749 0.0609  143 GLY A C   
1111 O O   . GLY A 143 ? 0.4288 0.6045 0.5929 0.0586  -0.0627 0.0659  143 GLY A O   
1112 N N   . SER A 144 ? 0.4370 0.6124 0.6113 0.0274  -0.0729 0.0539  144 SER A N   
1113 C CA  . SER A 144 ? 0.4709 0.6108 0.6068 0.0265  -0.0597 0.0519  144 SER A CA  
1114 C C   . SER A 144 ? 0.3820 0.4994 0.4800 0.0334  -0.0676 0.0484  144 SER A C   
1115 O O   . SER A 144 ? 0.4202 0.5129 0.4922 0.0340  -0.0568 0.0471  144 SER A O   
1116 C CB  . SER A 144 ? 0.4878 0.6163 0.6228 0.0099  -0.0565 0.0472  144 SER A CB  
1117 O OG  . SER A 144 ? 0.4947 0.6227 0.6289 0.0000  -0.0744 0.0394  144 SER A OG  
1118 N N   . CYS A 145 ? 0.3599 0.4854 0.4542 0.0385  -0.0860 0.0469  145 CYS A N   
1119 C CA  . CYS A 145 ? 0.4764 0.5769 0.5305 0.0458  -0.0904 0.0447  145 CYS A CA  
1120 C C   . CYS A 145 ? 0.4770 0.5591 0.5122 0.0583  -0.0730 0.0512  145 CYS A C   
1121 O O   . CYS A 145 ? 0.4528 0.5447 0.5013 0.0693  -0.0664 0.0588  145 CYS A O   
1122 C CB  . CYS A 145 ? 0.4392 0.5509 0.4878 0.0530  -0.1134 0.0438  145 CYS A CB  
1123 S SG  . CYS A 145 ? 0.8343 0.9096 0.8259 0.0606  -0.1175 0.0403  145 CYS A SG  
1124 N N   . GLY A 146 ? 0.4258 0.4805 0.4323 0.0563  -0.0642 0.0480  146 GLY A N   
1125 C CA  . GLY A 146 ? 0.4536 0.4880 0.4451 0.0622  -0.0465 0.0515  146 GLY A CA  
1126 C C   . GLY A 146 ? 0.4732 0.5016 0.4708 0.0519  -0.0337 0.0477  146 GLY A C   
1127 O O   . GLY A 146 ? 0.4217 0.4313 0.4060 0.0521  -0.0212 0.0471  146 GLY A O   
1128 N N   . SER A 147 ? 0.4777 0.5200 0.4937 0.0427  -0.0368 0.0453  147 SER A N   
1129 C CA  . SER A 147 ? 0.4765 0.5113 0.4917 0.0349  -0.0275 0.0423  147 SER A CA  
1130 C C   . SER A 147 ? 0.4240 0.4440 0.4242 0.0300  -0.0269 0.0370  147 SER A C   
1131 O O   . SER A 147 ? 0.4364 0.4530 0.4294 0.0302  -0.0330 0.0350  147 SER A O   
1132 C CB  . SER A 147 ? 0.4272 0.4747 0.4593 0.0269  -0.0304 0.0423  147 SER A CB  
1133 O OG  . SER A 147 ? 0.4715 0.5346 0.5233 0.0308  -0.0253 0.0478  147 SER A OG  
1134 N N   . VAL A 148 ? 0.4202 0.4318 0.4159 0.0259  -0.0197 0.0342  148 VAL A N   
1135 C CA  . VAL A 148 ? 0.4357 0.4391 0.4259 0.0218  -0.0183 0.0294  148 VAL A CA  
1136 C C   . VAL A 148 ? 0.4813 0.4886 0.4754 0.0154  -0.0227 0.0261  148 VAL A C   
1137 O O   . VAL A 148 ? 0.4183 0.4265 0.4107 0.0141  -0.0224 0.0270  148 VAL A O   
1138 C CB  . VAL A 148 ? 0.5516 0.5412 0.5347 0.0221  -0.0075 0.0280  148 VAL A CB  
1139 C CG1 . VAL A 148 ? 0.4511 0.4319 0.4249 0.0317  -0.0024 0.0337  148 VAL A CG1 
1140 C CG2 . VAL A 148 ? 0.3475 0.3314 0.3273 0.0196  -0.0027 0.0257  148 VAL A CG2 
1141 N N   . GLY A 149 ? 0.4862 0.4948 0.4839 0.0136  -0.0257 0.0233  149 GLY A N   
1142 C CA  . GLY A 149 ? 0.4014 0.4146 0.4034 0.0107  -0.0314 0.0212  149 GLY A CA  
1143 C C   . GLY A 149 ? 0.4920 0.5081 0.5014 0.0067  -0.0301 0.0159  149 GLY A C   
1144 O O   . GLY A 149 ? 0.4124 0.4248 0.4255 0.0056  -0.0219 0.0145  149 GLY A O   
1145 N N   . PHE A 150 ? 0.4098 0.4318 0.4212 0.0042  -0.0382 0.0131  150 PHE A N   
1146 C CA  . PHE A 150 ? 0.4058 0.4336 0.4280 -0.0027 -0.0399 0.0060  150 PHE A CA  
1147 C C   . PHE A 150 ? 0.4861 0.5260 0.5122 -0.0027 -0.0550 0.0037  150 PHE A C   
1148 O O   . PHE A 150 ? 0.4303 0.4659 0.4404 0.0027  -0.0616 0.0081  150 PHE A O   
1149 C CB  . PHE A 150 ? 0.3590 0.3723 0.3677 -0.0083 -0.0336 0.0017  150 PHE A CB  
1150 C CG  . PHE A 150 ? 0.4473 0.4510 0.4331 -0.0061 -0.0368 0.0025  150 PHE A CG  
1151 C CD1 . PHE A 150 ? 0.5203 0.5176 0.4963 0.0004  -0.0299 0.0098  150 PHE A CD1 
1152 C CD2 . PHE A 150 ? 0.5352 0.5366 0.5090 -0.0105 -0.0468 -0.0041 150 PHE A CD2 
1153 C CE1 . PHE A 150 ? 0.4290 0.4173 0.3862 0.0028  -0.0282 0.0117  150 PHE A CE1 
1154 C CE2 . PHE A 150 ? 0.4988 0.4862 0.4446 -0.0070 -0.0465 -0.0027 150 PHE A CE2 
1155 C CZ  . PHE A 150 ? 0.5292 0.5097 0.4678 -0.0002 -0.0349 0.0058  150 PHE A CZ  
1156 N N   . ASN A 151 ? 0.4652 0.5201 0.5133 -0.0087 -0.0602 -0.0029 151 ASN A N   
1157 C CA  . ASN A 151 ? 0.5023 0.5715 0.5549 -0.0099 -0.0787 -0.0074 151 ASN A CA  
1158 C C   . ASN A 151 ? 0.5742 0.6422 0.6289 -0.0239 -0.0823 -0.0194 151 ASN A C   
1159 O O   . ASN A 151 ? 0.4335 0.4930 0.4963 -0.0325 -0.0681 -0.0232 151 ASN A O   
1160 C CB  . ASN A 151 ? 0.4021 0.4975 0.4882 -0.0040 -0.0854 -0.0051 151 ASN A CB  
1161 C CG  . ASN A 151 ? 0.5324 0.6227 0.6087 0.0105  -0.0854 0.0054  151 ASN A CG  
1162 O OD1 . ASN A 151 ? 0.5876 0.6672 0.6382 0.0165  -0.0940 0.0099  151 ASN A OD1 
1163 N ND2 . ASN A 151 ? 0.4262 0.5194 0.5195 0.0159  -0.0738 0.0091  151 ASN A ND2 
1164 N N   . ILE A 152 ? 0.4908 0.5629 0.5338 -0.0263 -0.1016 -0.0256 152 ILE A N   
1165 C CA  . ILE A 152 ? 0.6263 0.6931 0.6656 -0.0414 -0.1084 -0.0400 152 ILE A CA  
1166 C C   . ILE A 152 ? 0.6479 0.7470 0.7163 -0.0464 -0.1328 -0.0478 152 ILE A C   
1167 O O   . ILE A 152 ? 0.7008 0.8112 0.7596 -0.0353 -0.1520 -0.0434 152 ILE A O   
1168 C CB  . ILE A 152 ? 0.5535 0.5886 0.5414 -0.0406 -0.1094 -0.0433 152 ILE A CB  
1169 C CG1 . ILE A 152 ? 0.6665 0.6752 0.6372 -0.0374 -0.0844 -0.0374 152 ILE A CG1 
1170 C CG2 . ILE A 152 ? 0.5612 0.5888 0.5406 -0.0563 -0.1214 -0.0608 152 ILE A CG2 
1171 C CD1 . ILE A 152 ? 0.6686 0.6457 0.5932 -0.0356 -0.0796 -0.0405 152 ILE A CD1 
1172 N N   . ASP A 153 ? 0.7203 0.8342 0.8255 -0.0631 -0.1321 -0.0587 153 ASP A N   
1173 C CA  . ASP A 153 ? 0.8619 1.0162 1.0111 -0.0701 -0.1547 -0.0667 153 ASP A CA  
1174 C C   . ASP A 153 ? 0.9482 1.0966 1.1028 -0.0944 -0.1616 -0.0859 153 ASP A C   
1175 O O   . ASP A 153 ? 0.9771 1.1263 1.1645 -0.1099 -0.1439 -0.0911 153 ASP A O   
1176 C CB  . ASP A 153 ? 0.9162 1.1026 1.1223 -0.0665 -0.1423 -0.0590 153 ASP A CB  
1177 C CG  . ASP A 153 ? 1.0694 1.2978 1.3367 -0.0816 -0.1550 -0.0700 153 ASP A CG  
1178 O OD1 . ASP A 153 ? 1.1787 1.4302 1.4522 -0.0837 -0.1866 -0.0782 153 ASP A OD1 
1179 O OD2 . ASP A 153 ? 1.1168 1.3555 1.4264 -0.0913 -0.1332 -0.0702 153 ASP A OD2 
1180 N N   . TYR A 154 ? 0.9425 1.0800 1.0602 -0.0976 -0.1860 -0.0967 154 TYR A N   
1181 C CA  . TYR A 154 ? 0.8882 1.0163 1.0036 -0.1216 -0.1980 -0.1182 154 TYR A CA  
1182 C C   . TYR A 154 ? 0.8858 0.9724 0.9874 -0.1346 -0.1665 -0.1227 154 TYR A C   
1183 O O   . TYR A 154 ? 0.8275 0.9195 0.9696 -0.1538 -0.1547 -0.1306 154 TYR A O   
1184 C CB  . TYR A 154 ? 0.9058 1.0856 1.0903 -0.1370 -0.2188 -0.1288 154 TYR A CB  
1185 C CG  . TYR A 154 ? 0.9943 1.2162 1.1919 -0.1224 -0.2545 -0.1251 154 TYR A CG  
1186 C CD1 . TYR A 154 ? 1.0673 1.3067 1.2730 -0.0966 -0.2502 -0.1047 154 TYR A CD1 
1187 C CD2 . TYR A 154 ? 1.0297 1.2710 1.2284 -0.1335 -0.2935 -0.1424 154 TYR A CD2 
1188 C CE1 . TYR A 154 ? 1.0163 1.2899 1.2315 -0.0801 -0.2812 -0.0993 154 TYR A CE1 
1189 C CE2 . TYR A 154 ? 0.9342 1.2143 1.1428 -0.1167 -0.3282 -0.1372 154 TYR A CE2 
1190 C CZ  . TYR A 154 ? 1.0391 1.3343 1.2560 -0.0889 -0.3206 -0.1146 154 TYR A CZ  
1191 O OH  . TYR A 154 ? 0.9787 1.3081 1.2032 -0.0693 -0.3532 -0.1076 154 TYR A OH  
1192 N N   . ASP A 155 ? 0.7730 0.8170 0.8168 -0.1225 -0.1517 -0.1164 155 ASP A N   
1193 C CA  . ASP A 155 ? 0.9264 0.9264 0.9478 -0.1296 -0.1235 -0.1194 155 ASP A CA  
1194 C C   . ASP A 155 ? 0.8017 0.8017 0.8492 -0.1233 -0.0932 -0.1042 155 ASP A C   
1195 O O   . ASP A 155 ? 0.7972 0.7606 0.8202 -0.1206 -0.0690 -0.1005 155 ASP A O   
1196 C CB  . ASP A 155 ? 0.8924 0.8790 0.9233 -0.1570 -0.1286 -0.1417 155 ASP A CB  
1197 C CG  . ASP A 155 ? 1.1121 1.0487 1.0792 -0.1607 -0.1300 -0.1553 155 ASP A CG  
1198 O OD1 . ASP A 155 ? 1.2393 1.1581 1.1572 -0.1416 -0.1304 -0.1475 155 ASP A OD1 
1199 O OD2 . ASP A 155 ? 1.1859 1.0977 1.1517 -0.1829 -0.1275 -0.1737 155 ASP A OD2 
1200 N N   . CYS A 156 ? 0.7119 0.7509 0.8066 -0.1197 -0.0941 -0.0954 156 CYS A N   
1201 C CA  . CYS A 156 ? 0.7360 0.7737 0.8520 -0.1143 -0.0666 -0.0825 156 CYS A CA  
1202 C C   . CYS A 156 ? 0.6151 0.6540 0.7118 -0.0906 -0.0618 -0.0651 156 CYS A C   
1203 O O   . CYS A 156 ? 0.5872 0.6520 0.6915 -0.0802 -0.0783 -0.0600 156 CYS A O   
1204 C CB  . CYS A 156 ? 0.5899 0.6650 0.7682 -0.1249 -0.0652 -0.0839 156 CYS A CB  
1205 S SG  . CYS A 156 ? 0.6334 0.7027 0.8298 -0.1164 -0.0295 -0.0675 156 CYS A SG  
1206 N N   . VAL A 157 ? 0.5129 0.5234 0.5858 -0.0821 -0.0401 -0.0560 157 VAL A N   
1207 C CA  . VAL A 157 ? 0.5242 0.5347 0.5807 -0.0627 -0.0357 -0.0414 157 VAL A CA  
1208 C C   . VAL A 157 ? 0.5081 0.5331 0.5922 -0.0577 -0.0234 -0.0323 157 VAL A C   
1209 O O   . VAL A 157 ? 0.4902 0.5000 0.5782 -0.0609 -0.0035 -0.0298 157 VAL A O   
1210 C CB  . VAL A 157 ? 0.5438 0.5212 0.5634 -0.0548 -0.0218 -0.0364 157 VAL A CB  
1211 C CG1 . VAL A 157 ? 0.4471 0.4301 0.4586 -0.0379 -0.0193 -0.0226 157 VAL A CG1 
1212 C CG2 . VAL A 157 ? 0.6151 0.5743 0.6030 -0.0577 -0.0302 -0.0453 157 VAL A CG2 
1213 N N   . SER A 158 ? 0.4307 0.4803 0.5288 -0.0484 -0.0334 -0.0268 158 SER A N   
1214 C CA  . SER A 158 ? 0.4322 0.4906 0.5478 -0.0405 -0.0210 -0.0183 158 SER A CA  
1215 C C   . SER A 158 ? 0.4091 0.4508 0.4938 -0.0263 -0.0164 -0.0085 158 SER A C   
1216 O O   . SER A 158 ? 0.3852 0.4331 0.4609 -0.0178 -0.0280 -0.0048 158 SER A O   
1217 C CB  . SER A 158 ? 0.3425 0.4343 0.4912 -0.0369 -0.0328 -0.0182 158 SER A CB  
1218 O OG  . SER A 158 ? 0.5589 0.6716 0.7498 -0.0497 -0.0301 -0.0252 158 SER A OG  
1219 N N   . PHE A 159 ? 0.4216 0.4415 0.4905 -0.0240 0.0000  -0.0041 159 PHE A N   
1220 C CA  . PHE A 159 ? 0.4136 0.4226 0.4590 -0.0114 0.0020  0.0043  159 PHE A CA  
1221 C C   . PHE A 159 ? 0.5135 0.5300 0.5662 -0.0040 0.0052  0.0084  159 PHE A C   
1222 O O   . PHE A 159 ? 0.4162 0.4338 0.4833 -0.0057 0.0181  0.0085  159 PHE A O   
1223 C CB  . PHE A 159 ? 0.4551 0.4397 0.4800 -0.0085 0.0158  0.0085  159 PHE A CB  
1224 C CG  . PHE A 159 ? 0.4441 0.4154 0.4569 -0.0124 0.0159  0.0051  159 PHE A CG  
1225 C CD1 . PHE A 159 ? 0.4128 0.3833 0.4106 -0.0059 0.0083  0.0074  159 PHE A CD1 
1226 C CD2 . PHE A 159 ? 0.4234 0.3804 0.4402 -0.0230 0.0260  -0.0008 159 PHE A CD2 
1227 C CE1 . PHE A 159 ? 0.3820 0.3370 0.3660 -0.0075 0.0119  0.0043  159 PHE A CE1 
1228 C CE2 . PHE A 159 ? 0.5276 0.4658 0.5281 -0.0260 0.0279  -0.0052 159 PHE A CE2 
1229 C CZ  . PHE A 159 ? 0.4742 0.4110 0.4569 -0.0169 0.0213  -0.0024 159 PHE A CZ  
1230 N N   . CYS A 160 ? 0.4272 0.4455 0.4690 0.0040  -0.0042 0.0117  160 CYS A N   
1231 C CA  . CYS A 160 ? 0.3687 0.3891 0.4132 0.0113  -0.0017 0.0139  160 CYS A CA  
1232 C C   . CYS A 160 ? 0.4558 0.4625 0.4754 0.0186  -0.0048 0.0172  160 CYS A C   
1233 O O   . CYS A 160 ? 0.5049 0.5055 0.5189 0.0245  -0.0011 0.0174  160 CYS A O   
1234 C CB  . CYS A 160 ? 0.4113 0.4502 0.4758 0.0127  -0.0122 0.0123  160 CYS A CB  
1235 S SG  . CYS A 160 ? 0.5037 0.5413 0.5531 0.0147  -0.0292 0.0144  160 CYS A SG  
1236 N N   . TYR A 161 ? 0.4229 0.4249 0.4289 0.0182  -0.0112 0.0190  161 TYR A N   
1237 C CA  . TYR A 161 ? 0.4219 0.4171 0.4122 0.0225  -0.0177 0.0207  161 TYR A CA  
1238 C C   . TYR A 161 ? 0.4741 0.4663 0.4546 0.0241  -0.0191 0.0239  161 TYR A C   
1239 O O   . TYR A 161 ? 0.5019 0.4981 0.4880 0.0215  -0.0181 0.0248  161 TYR A O   
1240 C CB  . TYR A 161 ? 0.3818 0.3827 0.3778 0.0207  -0.0280 0.0203  161 TYR A CB  
1241 C CG  . TYR A 161 ? 0.4930 0.4880 0.4787 0.0209  -0.0353 0.0203  161 TYR A CG  
1242 C CD1 . TYR A 161 ? 0.4887 0.4711 0.4619 0.0238  -0.0360 0.0170  161 TYR A CD1 
1243 C CD2 . TYR A 161 ? 0.4598 0.4617 0.4497 0.0175  -0.0409 0.0227  161 TYR A CD2 
1244 C CE1 . TYR A 161 ? 0.4772 0.4536 0.4416 0.0212  -0.0453 0.0145  161 TYR A CE1 
1245 C CE2 . TYR A 161 ? 0.3641 0.3653 0.3527 0.0149  -0.0490 0.0216  161 TYR A CE2 
1246 C CZ  . TYR A 161 ? 0.4341 0.4224 0.4095 0.0157  -0.0528 0.0167  161 TYR A CZ  
1247 O OH  . TYR A 161 ? 0.4586 0.4452 0.4325 0.0104  -0.0635 0.0130  161 TYR A OH  
1248 N N   . MET A 162 ? 0.4878 0.4721 0.4518 0.0297  -0.0219 0.0254  162 MET A N   
1249 C CA  . MET A 162 ? 0.5237 0.5104 0.4823 0.0340  -0.0272 0.0294  162 MET A CA  
1250 C C   . MET A 162 ? 0.5349 0.5272 0.4915 0.0335  -0.0420 0.0274  162 MET A C   
1251 O O   . MET A 162 ? 0.5053 0.4861 0.4439 0.0358  -0.0457 0.0239  162 MET A O   
1252 C CB  . MET A 162 ? 0.4277 0.3991 0.3665 0.0428  -0.0188 0.0340  162 MET A CB  
1253 C CG  . MET A 162 ? 0.4613 0.4367 0.3943 0.0517  -0.0266 0.0397  162 MET A CG  
1254 S SD  . MET A 162 ? 0.7350 0.6867 0.6417 0.0651  -0.0138 0.0485  162 MET A SD  
1255 C CE  . MET A 162 ? 0.6130 0.5599 0.5360 0.0590  0.0031  0.0487  162 MET A CE  
1256 N N   . HIS A 163 ? 0.4275 0.4357 0.4023 0.0297  -0.0490 0.0287  163 HIS A N   
1257 C CA  . HIS A 163 ? 0.4781 0.4944 0.4596 0.0247  -0.0627 0.0256  163 HIS A CA  
1258 C C   . HIS A 163 ? 0.5334 0.5524 0.5037 0.0314  -0.0750 0.0258  163 HIS A C   
1259 O O   . HIS A 163 ? 0.4920 0.5163 0.4613 0.0409  -0.0737 0.0321  163 HIS A O   
1260 C CB  . HIS A 163 ? 0.4417 0.4753 0.4498 0.0183  -0.0627 0.0283  163 HIS A CB  
1261 C CG  . HIS A 163 ? 0.4548 0.4979 0.4776 0.0095  -0.0745 0.0250  163 HIS A CG  
1262 N ND1 . HIS A 163 ? 0.4342 0.4628 0.4462 0.0029  -0.0808 0.0178  163 HIS A ND1 
1263 C CD2 . HIS A 163 ? 0.4817 0.5469 0.5320 0.0050  -0.0798 0.0272  163 HIS A CD2 
1264 C CE1 . HIS A 163 ? 0.5422 0.5813 0.5727 -0.0073 -0.0907 0.0147  163 HIS A CE1 
1265 N NE2 . HIS A 163 ? 0.5490 0.6133 0.6062 -0.0066 -0.0903 0.0207  163 HIS A NE2 
1266 N N   . HIS A 164 ? 0.5207 0.5337 0.4799 0.0273  -0.0880 0.0187  164 HIS A N   
1267 C CA  . HIS A 164 ? 0.5771 0.5922 0.5209 0.0333  -0.1050 0.0171  164 HIS A CA  
1268 C C   . HIS A 164 ? 0.6779 0.7121 0.6439 0.0223  -0.1248 0.0109  164 HIS A C   
1269 O O   . HIS A 164 ? 0.6409 0.6994 0.6238 0.0261  -0.1387 0.0140  164 HIS A O   
1270 C CB  . HIS A 164 ? 0.6178 0.6023 0.5169 0.0395  -0.1041 0.0122  164 HIS A CB  
1271 C CG  . HIS A 164 ? 0.5932 0.5623 0.4686 0.0531  -0.0891 0.0202  164 HIS A CG  
1272 N ND1 . HIS A 164 ? 0.5747 0.5397 0.4603 0.0528  -0.0679 0.0248  164 HIS A ND1 
1273 C CD2 . HIS A 164 ? 0.5942 0.5493 0.4357 0.0668  -0.0919 0.0248  164 HIS A CD2 
1274 C CE1 . HIS A 164 ? 0.5678 0.5162 0.4302 0.0636  -0.0562 0.0313  164 HIS A CE1 
1275 N NE2 . HIS A 164 ? 0.6463 0.5865 0.4793 0.0735  -0.0692 0.0325  164 HIS A NE2 
1276 N N   . MET A 165 ? 0.6056 0.6302 0.5752 0.0088  -0.1262 0.0025  165 MET A N   
1277 C CA  . MET A 165 ? 0.6882 0.7241 0.6728 -0.0040 -0.1466 -0.0063 165 MET A CA  
1278 C C   . MET A 165 ? 0.5519 0.5791 0.5537 -0.0204 -0.1396 -0.0111 165 MET A C   
1279 O O   . MET A 165 ? 0.6496 0.6563 0.6403 -0.0189 -0.1226 -0.0092 165 MET A O   
1280 C CB  . MET A 165 ? 0.6817 0.6971 0.6250 -0.0011 -0.1643 -0.0167 165 MET A CB  
1281 C CG  . MET A 165 ? 0.6858 0.6603 0.5911 -0.0011 -0.1523 -0.0238 165 MET A CG  
1282 S SD  . MET A 165 ? 0.9174 0.8591 0.7578 0.0142  -0.1577 -0.0287 165 MET A SD  
1283 C CE  . MET A 165 ? 0.8283 0.7278 0.6379 0.0048  -0.1546 -0.0446 165 MET A CE  
1284 N N   . GLU A 166 ? 0.5973 0.6408 0.6280 -0.0359 -0.1533 -0.0170 166 GLU A N   
1285 C CA  . GLU A 166 ? 0.6148 0.6445 0.6592 -0.0536 -0.1480 -0.0225 166 GLU A CA  
1286 C C   . GLU A 166 ? 0.6220 0.6258 0.6402 -0.0637 -0.1648 -0.0390 166 GLU A C   
1287 O O   . GLU A 166 ? 0.6324 0.6436 0.6379 -0.0623 -0.1871 -0.0468 166 GLU A O   
1288 C CB  . GLU A 166 ? 0.5400 0.6028 0.6384 -0.0672 -0.1474 -0.0180 166 GLU A CB  
1289 C CG  . GLU A 166 ? 0.6488 0.6937 0.7619 -0.0869 -0.1388 -0.0221 166 GLU A CG  
1290 C CD  . GLU A 166 ? 0.7449 0.8185 0.9095 -0.0975 -0.1271 -0.0130 166 GLU A CD  
1291 O OE1 . GLU A 166 ? 0.8921 0.9913 1.0964 -0.1138 -0.1398 -0.0187 166 GLU A OE1 
1292 O OE2 . GLU A 166 ? 0.6967 0.7680 0.8623 -0.0895 -0.1054 -0.0005 166 GLU A OE2 
1293 N N   . LEU A 167 ? 0.6808 0.6510 0.6871 -0.0726 -0.1544 -0.0445 167 LEU A N   
1294 C CA  . LEU A 167 ? 0.6846 0.6209 0.6603 -0.0822 -0.1670 -0.0617 167 LEU A CA  
1295 C C   . LEU A 167 ? 0.7112 0.6496 0.7201 -0.1083 -0.1750 -0.0706 167 LEU A C   
1296 O O   . LEU A 167 ? 0.7138 0.6737 0.7667 -0.1174 -0.1641 -0.0611 167 LEU A O   
1297 C CB  . LEU A 167 ? 0.7698 0.6599 0.7052 -0.0724 -0.1483 -0.0630 167 LEU A CB  
1298 C CG  . LEU A 167 ? 0.8239 0.7086 0.7271 -0.0493 -0.1391 -0.0566 167 LEU A CG  
1299 C CD1 . LEU A 167 ? 0.8045 0.6478 0.6765 -0.0402 -0.1205 -0.0586 167 LEU A CD1 
1300 C CD2 . LEU A 167 ? 0.7079 0.5950 0.5816 -0.0432 -0.1585 -0.0640 167 LEU A CD2 
1301 N N   . PRO A 168 ? 0.7461 0.6600 0.7336 -0.1218 -0.1931 -0.0894 168 PRO A N   
1302 C CA  . PRO A 168 ? 0.6836 0.5976 0.7060 -0.1507 -0.2008 -0.0998 168 PRO A CA  
1303 C C   . PRO A 168 ? 0.7526 0.6417 0.7900 -0.1589 -0.1727 -0.0918 168 PRO A C   
1304 O O   . PRO A 168 ? 0.8005 0.7040 0.8840 -0.1804 -0.1700 -0.0911 168 PRO A O   
1305 C CB  . PRO A 168 ? 0.7417 0.6173 0.7196 -0.1603 -0.2220 -0.1234 168 PRO A CB  
1306 C CG  . PRO A 168 ? 0.7793 0.6593 0.7139 -0.1374 -0.2353 -0.1238 168 PRO A CG  
1307 C CD  . PRO A 168 ? 0.8079 0.6939 0.7383 -0.1126 -0.2085 -0.1029 168 PRO A CD  
1308 N N   . THR A 169 ? 0.6844 0.5370 0.6855 -0.1416 -0.1512 -0.0847 169 THR A N   
1309 C CA  . THR A 169 ? 0.7935 0.6195 0.8022 -0.1447 -0.1257 -0.0749 169 THR A CA  
1310 C C   . THR A 169 ? 0.8118 0.6723 0.8552 -0.1376 -0.1098 -0.0541 169 THR A C   
1311 O O   . THR A 169 ? 0.8530 0.6932 0.9006 -0.1385 -0.0889 -0.0436 169 THR A O   
1312 C CB  . THR A 169 ? 0.7059 0.4836 0.6659 -0.1259 -0.1104 -0.0743 169 THR A CB  
1313 O OG1 . THR A 169 ? 0.8089 0.6047 0.7512 -0.1012 -0.1091 -0.0666 169 THR A OG1 
1314 C CG2 . THR A 169 ? 0.7637 0.4938 0.6852 -0.1345 -0.1196 -0.0955 169 THR A CG2 
1315 N N   . GLY A 170 ? 0.7509 0.6583 0.8142 -0.1293 -0.1182 -0.0477 170 GLY A N   
1316 C CA  . GLY A 170 ? 0.6460 0.5818 0.7356 -0.1214 -0.1026 -0.0297 170 GLY A CA  
1317 C C   . GLY A 170 ? 0.6640 0.5938 0.7258 -0.0970 -0.0905 -0.0187 170 GLY A C   
1318 O O   . GLY A 170 ? 0.6423 0.5892 0.7182 -0.0901 -0.0775 -0.0051 170 GLY A O   
1319 N N   . VAL A 171 ? 0.6979 0.6035 0.7214 -0.0843 -0.0935 -0.0247 171 VAL A N   
1320 C CA  . VAL A 171 ? 0.5483 0.4542 0.5528 -0.0630 -0.0837 -0.0157 171 VAL A CA  
1321 C C   . VAL A 171 ? 0.6592 0.5932 0.6619 -0.0535 -0.0940 -0.0161 171 VAL A C   
1322 O O   . VAL A 171 ? 0.6211 0.5707 0.6312 -0.0605 -0.1103 -0.0233 171 VAL A O   
1323 C CB  . VAL A 171 ? 0.7044 0.5711 0.6746 -0.0528 -0.0767 -0.0198 171 VAL A CB  
1324 C CG1 . VAL A 171 ? 0.7245 0.5580 0.6937 -0.0602 -0.0657 -0.0180 171 VAL A CG1 
1325 C CG2 . VAL A 171 ? 0.7640 0.6143 0.7068 -0.0531 -0.0889 -0.0349 171 VAL A CG2 
1326 N N   . HIS A 172 ? 0.5711 0.5109 0.5642 -0.0375 -0.0853 -0.0083 172 HIS A N   
1327 C CA  . HIS A 172 ? 0.5964 0.5591 0.5887 -0.0280 -0.0899 -0.0056 172 HIS A CA  
1328 C C   . HIS A 172 ? 0.5692 0.5154 0.5311 -0.0143 -0.0853 -0.0078 172 HIS A C   
1329 O O   . HIS A 172 ? 0.4747 0.4020 0.4260 -0.0087 -0.0747 -0.0071 172 HIS A O   
1330 C CB  . HIS A 172 ? 0.4783 0.4644 0.4920 -0.0242 -0.0807 0.0059  172 HIS A CB  
1331 C CG  . HIS A 172 ? 0.6281 0.6302 0.6724 -0.0361 -0.0797 0.0097  172 HIS A CG  
1332 N ND1 . HIS A 172 ? 0.5070 0.4988 0.5580 -0.0410 -0.0673 0.0157  172 HIS A ND1 
1333 C CD2 . HIS A 172 ? 0.5391 0.5672 0.6106 -0.0433 -0.0882 0.0091  172 HIS A CD2 
1334 C CE1 . HIS A 172 ? 0.5415 0.5501 0.6219 -0.0519 -0.0651 0.0188  172 HIS A CE1 
1335 N NE2 . HIS A 172 ? 0.6538 0.6877 0.7512 -0.0538 -0.0781 0.0145  172 HIS A NE2 
1336 N N   . ALA A 173 ? 0.5566 0.5100 0.5055 -0.0077 -0.0920 -0.0092 173 ALA A N   
1337 C CA  . ALA A 173 ? 0.5029 0.4394 0.4222 0.0048  -0.0845 -0.0103 173 ALA A CA  
1338 C C   . ALA A 173 ? 0.5559 0.5091 0.4768 0.0139  -0.0811 -0.0025 173 ALA A C   
1339 O O   . ALA A 173 ? 0.5380 0.5119 0.4734 0.0125  -0.0899 0.0011  173 ALA A O   
1340 C CB  . ALA A 173 ? 0.4885 0.3999 0.3725 0.0051  -0.0942 -0.0216 173 ALA A CB  
1341 N N   . GLY A 174 ? 0.4932 0.4365 0.4014 0.0232  -0.0665 0.0005  174 GLY A N   
1342 C CA  . GLY A 174 ? 0.4607 0.4119 0.3673 0.0307  -0.0597 0.0075  174 GLY A CA  
1343 C C   . GLY A 174 ? 0.5505 0.4847 0.4398 0.0388  -0.0424 0.0085  174 GLY A C   
1344 O O   . GLY A 174 ? 0.5279 0.4435 0.4013 0.0414  -0.0368 0.0034  174 GLY A O   
1345 N N   . THR A 175 ? 0.4458 0.3853 0.3402 0.0427  -0.0316 0.0152  175 THR A N   
1346 C CA  . THR A 175 ? 0.5045 0.4300 0.3878 0.0487  -0.0121 0.0175  175 THR A CA  
1347 C C   . THR A 175 ? 0.5481 0.4891 0.4631 0.0438  -0.0009 0.0208  175 THR A C   
1348 O O   . THR A 175 ? 0.4423 0.4003 0.3785 0.0378  -0.0085 0.0217  175 THR A O   
1349 C CB  . THR A 175 ? 0.6314 0.5393 0.4816 0.0580  -0.0078 0.0223  175 THR A CB  
1350 O OG1 . THR A 175 ? 0.4588 0.3780 0.3221 0.0577  -0.0086 0.0289  175 THR A OG1 
1351 C CG2 . THR A 175 ? 0.5813 0.4771 0.3980 0.0626  -0.0258 0.0181  175 THR A CG2 
1352 N N   . ASP A 176 ? 0.4482 0.3822 0.3654 0.0460  0.0179  0.0221  176 ASP A N   
1353 C CA  . ASP A 176 ? 0.4881 0.4351 0.4338 0.0395  0.0280  0.0241  176 ASP A CA  
1354 C C   . ASP A 176 ? 0.5546 0.4899 0.4864 0.0407  0.0346  0.0295  176 ASP A C   
1355 O O   . ASP A 176 ? 0.5278 0.4468 0.4281 0.0491  0.0314  0.0332  176 ASP A O   
1356 C CB  . ASP A 176 ? 0.5470 0.4962 0.5104 0.0397  0.0463  0.0233  176 ASP A CB  
1357 C CG  . ASP A 176 ? 0.5400 0.4628 0.4735 0.0482  0.0661  0.0266  176 ASP A CG  
1358 O OD1 . ASP A 176 ? 0.6474 0.5505 0.5508 0.0523  0.0694  0.0313  176 ASP A OD1 
1359 O OD2 . ASP A 176 ? 0.6296 0.5495 0.5679 0.0528  0.0799  0.0253  176 ASP A OD2 
1360 N N   . LEU A 177 ? 0.5048 0.4465 0.4588 0.0327  0.0429  0.0297  177 LEU A N   
1361 C CA  . LEU A 177 ? 0.5327 0.4584 0.4730 0.0341  0.0507  0.0349  177 LEU A CA  
1362 C C   . LEU A 177 ? 0.6163 0.5142 0.5306 0.0412  0.0716  0.0415  177 LEU A C   
1363 O O   . LEU A 177 ? 0.6004 0.4784 0.4970 0.0454  0.0799  0.0480  177 LEU A O   
1364 C CB  . LEU A 177 ? 0.5107 0.4448 0.4779 0.0217  0.0543  0.0310  177 LEU A CB  
1365 C CG  . LEU A 177 ? 0.5327 0.4776 0.5040 0.0199  0.0381  0.0287  177 LEU A CG  
1366 C CD1 . LEU A 177 ? 0.6753 0.6035 0.6234 0.0295  0.0394  0.0355  177 LEU A CD1 
1367 C CD2 . LEU A 177 ? 0.6458 0.6093 0.6220 0.0217  0.0203  0.0264  177 LEU A CD2 
1368 N N   . GLU A 178 ? 0.6747 0.5673 0.5835 0.0443  0.0824  0.0410  178 GLU A N   
1369 C CA  . GLU A 178 ? 0.5751 0.4365 0.4502 0.0534  0.1042  0.0481  178 GLU A CA  
1370 C C   . GLU A 178 ? 0.6636 0.5054 0.4884 0.0687  0.0923  0.0511  178 GLU A C   
1371 O O   . GLU A 178 ? 0.6257 0.4364 0.4104 0.0794  0.1082  0.0576  178 GLU A O   
1372 C CB  . GLU A 178 ? 0.7222 0.5864 0.6158 0.0504  0.1254  0.0461  178 GLU A CB  
1373 C CG  . GLU A 178 ? 0.8169 0.7036 0.7644 0.0346  0.1368  0.0428  178 GLU A CG  
1374 C CD  . GLU A 178 ? 0.9167 0.7857 0.8643 0.0272  0.1525  0.0476  178 GLU A CD  
1375 O OE1 . GLU A 178 ? 0.9391 0.8262 0.9296 0.0111  0.1555  0.0422  178 GLU A OE1 
1376 O OE2 . GLU A 178 ? 0.9227 0.7576 0.8259 0.0378  0.1615  0.0564  178 GLU A OE2 
1377 N N   . GLY A 179 ? 0.5320 0.3903 0.3573 0.0695  0.0650  0.0460  179 GLY A N   
1378 C CA  . GLY A 179 ? 0.6487 0.4938 0.4325 0.0808  0.0485  0.0459  179 GLY A CA  
1379 C C   . GLY A 179 ? 0.7069 0.5441 0.4740 0.0827  0.0463  0.0381  179 GLY A C   
1380 O O   . GLY A 179 ? 0.6742 0.4965 0.4020 0.0906  0.0314  0.0355  179 GLY A O   
1381 N N   . ASN A 180 ? 0.6301 0.4762 0.4253 0.0764  0.0597  0.0337  180 ASN A N   
1382 C CA  . ASN A 180 ? 0.6245 0.4585 0.4036 0.0803  0.0620  0.0267  180 ASN A CA  
1383 C C   . ASN A 180 ? 0.5411 0.3953 0.3424 0.0730  0.0385  0.0184  180 ASN A C   
1384 O O   . ASN A 180 ? 0.5557 0.4365 0.4012 0.0645  0.0357  0.0180  180 ASN A O   
1385 C CB  . ASN A 180 ? 0.6137 0.4473 0.4144 0.0806  0.0914  0.0280  180 ASN A CB  
1386 C CG  . ASN A 180 ? 0.6799 0.4927 0.4638 0.0852  0.1194  0.0372  180 ASN A CG  
1387 O OD1 . ASN A 180 ? 0.7810 0.5585 0.5109 0.0969  0.1293  0.0404  180 ASN A OD1 
1388 N ND2 . ASN A 180 ? 0.6940 0.5255 0.5212 0.0754  0.1323  0.0413  180 ASN A ND2 
1389 N N   . PHE A 181 ? 0.4615 0.4080 0.3232 0.0066  0.0460  0.0386  181 PHE A N   
1390 C CA  . PHE A 181 ? 0.4943 0.4572 0.3861 0.0046  0.0313  0.0346  181 PHE A CA  
1391 C C   . PHE A 181 ? 0.5023 0.4795 0.4063 0.0016  0.0420  0.0276  181 PHE A C   
1392 O O   . PHE A 181 ? 0.4512 0.4232 0.3341 0.0041  0.0558  0.0243  181 PHE A O   
1393 C CB  . PHE A 181 ? 0.4694 0.4148 0.3433 0.0092  0.0066  0.0325  181 PHE A CB  
1394 C CG  . PHE A 181 ? 0.5073 0.4614 0.4048 0.0089  -0.0128 0.0397  181 PHE A CG  
1395 C CD1 . PHE A 181 ? 0.4322 0.4116 0.3733 0.0032  -0.0212 0.0417  181 PHE A CD1 
1396 C CD2 . PHE A 181 ? 0.5522 0.4913 0.4295 0.0153  -0.0214 0.0463  181 PHE A CD2 
1397 C CE1 . PHE A 181 ? 0.4682 0.4623 0.4362 0.0039  -0.0370 0.0508  181 PHE A CE1 
1398 C CE2 . PHE A 181 ? 0.5235 0.4761 0.4266 0.0172  -0.0389 0.0545  181 PHE A CE2 
1399 C CZ  . PHE A 181 ? 0.5599 0.5424 0.5107 0.0115  -0.0462 0.0571  181 PHE A CZ  
1400 N N   . TYR A 182 ? 0.4718 0.4684 0.4104 -0.0027 0.0363  0.0266  182 TYR A N   
1401 C CA  . TYR A 182 ? 0.4061 0.4124 0.3546 -0.0035 0.0402  0.0200  182 TYR A CA  
1402 C C   . TYR A 182 ? 0.4480 0.4357 0.3813 -0.0004 0.0209  0.0149  182 TYR A C   
1403 O O   . TYR A 182 ? 0.5146 0.5023 0.4632 -0.0044 0.0020  0.0180  182 TYR A O   
1404 C CB  . TYR A 182 ? 0.4785 0.5100 0.4663 -0.0093 0.0435  0.0222  182 TYR A CB  
1405 C CG  . TYR A 182 ? 0.4638 0.5095 0.4619 -0.0130 0.0617  0.0241  182 TYR A CG  
1406 C CD1 . TYR A 182 ? 0.4182 0.4731 0.4138 -0.0140 0.0757  0.0203  182 TYR A CD1 
1407 C CD2 . TYR A 182 ? 0.4548 0.5043 0.4649 -0.0152 0.0637  0.0300  182 TYR A CD2 
1408 C CE1 . TYR A 182 ? 0.4323 0.4998 0.4386 -0.0206 0.0885  0.0222  182 TYR A CE1 
1409 C CE2 . TYR A 182 ? 0.4402 0.4956 0.4545 -0.0200 0.0775  0.0306  182 TYR A CE2 
1410 C CZ  . TYR A 182 ? 0.5288 0.5933 0.5420 -0.0244 0.0885  0.0266  182 TYR A CZ  
1411 O OH  . TYR A 182 ? 0.4310 0.5010 0.4493 -0.0322 0.0986  0.0273  182 TYR A OH  
1412 N N   . GLY A 183 ? 0.4778 0.4485 0.3802 0.0068  0.0254  0.0078  183 GLY A N   
1413 C CA  . GLY A 183 ? 0.5434 0.4872 0.4223 0.0106  0.0066  0.0011  183 GLY A CA  
1414 C C   . GLY A 183 ? 0.6614 0.5747 0.5016 0.0148  -0.0090 0.0005  183 GLY A C   
1415 O O   . GLY A 183 ? 0.5467 0.4595 0.3765 0.0163  -0.0032 0.0061  183 GLY A O   
1416 N N   . PRO A 184 ? 0.6423 0.5252 0.4571 0.0165  -0.0310 -0.0062 184 PRO A N   
1417 C CA  . PRO A 184 ? 0.7103 0.5572 0.4779 0.0222  -0.0482 -0.0089 184 PRO A CA  
1418 C C   . PRO A 184 ? 0.7629 0.6137 0.5496 0.0126  -0.0751 -0.0019 184 PRO A C   
1419 O O   . PRO A 184 ? 0.9039 0.7276 0.6692 0.0103  -0.1038 -0.0056 184 PRO A O   
1420 C CB  . PRO A 184 ? 0.6555 0.4646 0.3852 0.0284  -0.0605 -0.0207 184 PRO A CB  
1421 C CG  . PRO A 184 ? 0.6464 0.4743 0.4208 0.0175  -0.0659 -0.0204 184 PRO A CG  
1422 C CD  . PRO A 184 ? 0.6353 0.5115 0.4605 0.0127  -0.0425 -0.0118 184 PRO A CD  
1423 N N   . PHE A 185 ? 0.7022 0.5867 0.5291 0.0077  -0.0670 0.0085  185 PHE A N   
1424 C CA  . PHE A 185 ? 0.6386 0.5357 0.4915 0.0014  -0.0889 0.0175  185 PHE A CA  
1425 C C   . PHE A 185 ? 0.6891 0.5810 0.5218 0.0093  -0.0843 0.0240  185 PHE A C   
1426 O O   . PHE A 185 ? 0.6320 0.5191 0.4436 0.0160  -0.0597 0.0238  185 PHE A O   
1427 C CB  . PHE A 185 ? 0.6060 0.5445 0.5213 -0.0078 -0.0841 0.0258  185 PHE A CB  
1428 C CG  . PHE A 185 ? 0.6848 0.6281 0.6190 -0.0150 -0.0838 0.0211  185 PHE A CG  
1429 C CD1 . PHE A 185 ? 0.6023 0.5284 0.5338 -0.0231 -0.1103 0.0180  185 PHE A CD1 
1430 C CD2 . PHE A 185 ? 0.5116 0.4732 0.4629 -0.0141 -0.0587 0.0199  185 PHE A CD2 
1431 C CE1 . PHE A 185 ? 0.6229 0.5481 0.5681 -0.0295 -0.1099 0.0144  185 PHE A CE1 
1432 C CE2 . PHE A 185 ? 0.5954 0.5590 0.5608 -0.0189 -0.0586 0.0162  185 PHE A CE2 
1433 C CZ  . PHE A 185 ? 0.5376 0.4818 0.4991 -0.0263 -0.0833 0.0137  185 PHE A CZ  
1434 N N   . VAL A 186 ? 0.6884 0.5816 0.5288 0.0082  -0.1093 0.0308  186 VAL A N   
1435 C CA  . VAL A 186 ? 0.7066 0.5939 0.5295 0.0169  -0.1090 0.0386  186 VAL A CA  
1436 C C   . VAL A 186 ? 0.7136 0.6349 0.5876 0.0143  -0.1216 0.0511  186 VAL A C   
1437 O O   . VAL A 186 ? 0.6234 0.5685 0.5399 0.0048  -0.1372 0.0540  186 VAL A O   
1438 C CB  . VAL A 186 ? 0.7795 0.6249 0.5426 0.0244  -0.1295 0.0343  186 VAL A CB  
1439 C CG1 . VAL A 186 ? 0.6914 0.5038 0.4005 0.0313  -0.1115 0.0236  186 VAL A CG1 
1440 C CG2 . VAL A 186 ? 0.7282 0.5685 0.4992 0.0164  -0.1686 0.0325  186 VAL A CG2 
1441 N N   . ASP A 187 ? 0.6502 0.5732 0.5194 0.0238  -0.1134 0.0598  187 ASP A N   
1442 C CA  . ASP A 187 ? 0.6972 0.6516 0.6109 0.0268  -0.1223 0.0730  187 ASP A CA  
1443 C C   . ASP A 187 ? 0.7468 0.6939 0.6501 0.0307  -0.1568 0.0784  187 ASP A C   
1444 O O   . ASP A 187 ? 0.6427 0.5790 0.5254 0.0429  -0.1606 0.0855  187 ASP A O   
1445 C CB  . ASP A 187 ? 0.6108 0.5675 0.5237 0.0365  -0.0963 0.0795  187 ASP A CB  
1446 C CG  . ASP A 187 ? 0.7572 0.6741 0.6108 0.0443  -0.0858 0.0773  187 ASP A CG  
1447 O OD1 . ASP A 187 ? 0.7997 0.6887 0.6111 0.0433  -0.0931 0.0695  187 ASP A OD1 
1448 O OD2 . ASP A 187 ? 0.7751 0.6860 0.6219 0.0518  -0.0695 0.0839  187 ASP A OD2 
1449 N N   . ARG A 188 ? 0.6543 0.6053 0.5707 0.0193  -0.1839 0.0750  188 ARG A N   
1450 C CA  . ARG A 188 ? 0.8967 0.8454 0.8116 0.0183  -0.2230 0.0799  188 ARG A CA  
1451 C C   . ARG A 188 ? 0.9460 0.9326 0.9232 0.0022  -0.2433 0.0856  188 ARG A C   
1452 O O   . ARG A 188 ? 0.8720 0.8593 0.8612 -0.0102 -0.2366 0.0785  188 ARG A O   
1460 N N   . GLN A 189 ? 1.0201 1.0396 1.0383 0.0026  -0.2675 0.1000  189 GLN A N   
1461 C CA  . GLN A 189 ? 0.9311 0.9959 1.0186 -0.0134 -0.2845 0.1101  189 GLN A CA  
1462 C C   . GLN A 189 ? 0.9680 1.0092 1.0410 -0.0325 -0.3228 0.1024  189 GLN A C   
1463 O O   . GLN A 189 ? 1.0298 1.0898 1.1311 -0.0419 -0.3595 0.1116  189 GLN A O   
1464 C CB  . GLN A 189 ? 0.9844 1.0994 1.1265 -0.0047 -0.2944 0.1305  189 GLN A CB  
1465 C CG  . GLN A 189 ? 0.9742 1.1482 1.1987 -0.0174 -0.2956 0.1452  189 GLN A CG  
1466 C CD  . GLN A 189 ? 0.9564 1.1857 1.2379 -0.0039 -0.2988 0.1671  189 GLN A CD  
1467 O OE1 . GLN A 189 ? 0.9049 1.1308 1.1714 0.0091  -0.3177 0.1724  189 GLN A OE1 
1468 N NE2 . GLN A 189 ? 0.9419 1.2219 1.2873 -0.0047 -0.2790 0.1806  189 GLN A NE2 
1469 N N   . THR A 190 ? 1.0452 1.0431 1.0721 -0.0380 -0.3143 0.0853  190 THR A N   
1470 C CA  . THR A 190 ? 1.0762 1.0428 1.0836 -0.0560 -0.3451 0.0754  190 THR A CA  
1471 C C   . THR A 190 ? 1.1088 1.0804 1.1391 -0.0682 -0.3259 0.0709  190 THR A C   
1472 O O   . THR A 190 ? 1.0285 1.0144 1.0688 -0.0598 -0.2877 0.0706  190 THR A O   
1473 C CB  . THR A 190 ? 1.0883 0.9872 1.0054 -0.0471 -0.3553 0.0579  190 THR A CB  
1474 O OG1 . THR A 190 ? 1.1423 1.0123 1.0218 -0.0408 -0.3221 0.0442  190 THR A OG1 
1475 C CG2 . THR A 190 ? 1.0963 0.9878 0.9809 -0.0273 -0.3540 0.0622  190 THR A CG2 
1476 N N   . ALA A 191 ? 1.0970 1.0545 1.1343 -0.0888 -0.3545 0.0678  191 ALA A N   
1477 C CA  . ALA A 191 ? 0.9511 0.9081 1.0068 -0.1008 -0.3398 0.0644  191 ALA A CA  
1478 C C   . ALA A 191 ? 0.9551 0.8598 0.9422 -0.0886 -0.3177 0.0447  191 ALA A C   
1479 O O   . ALA A 191 ? 1.0635 0.9132 0.9854 -0.0853 -0.3360 0.0305  191 ALA A O   
1480 C CB  . ALA A 191 ? 0.8923 0.8426 0.9710 -0.1276 -0.3787 0.0674  191 ALA A CB  
1481 N N   . GLN A 192 ? 0.8710 0.7933 0.8716 -0.0805 -0.2785 0.0443  192 GLN A N   
1482 C CA  . GLN A 192 ? 0.8137 0.6979 0.7623 -0.0694 -0.2551 0.0284  192 GLN A CA  
1483 C C   . GLN A 192 ? 0.8463 0.7413 0.8252 -0.0786 -0.2408 0.0288  192 GLN A C   
1484 O O   . GLN A 192 ? 0.9505 0.8923 0.9903 -0.0861 -0.2308 0.0425  192 GLN A O   
1485 C CB  . GLN A 192 ? 0.7298 0.6218 0.6591 -0.0494 -0.2204 0.0270  192 GLN A CB  
1486 C CG  . GLN A 192 ? 0.8507 0.7508 0.7733 -0.0407 -0.2280 0.0342  192 GLN A CG  
1487 C CD  . GLN A 192 ? 0.8045 0.7171 0.7200 -0.0252 -0.1924 0.0362  192 GLN A CD  
1488 O OE1 . GLN A 192 ? 0.8020 0.6925 0.6795 -0.0163 -0.1694 0.0265  192 GLN A OE1 
1489 N NE2 . GLN A 192 ? 0.7636 0.7113 0.7158 -0.0216 -0.1880 0.0495  192 GLN A NE2 
1490 N N   . ALA A 193 ? 0.8495 0.7000 0.7830 -0.0758 -0.2391 0.0144  193 ALA A N   
1491 C CA  . ALA A 193 ? 0.8379 0.6893 0.7909 -0.0831 -0.2287 0.0138  193 ALA A CA  
1492 C C   . ALA A 193 ? 0.8209 0.6694 0.7512 -0.0650 -0.1918 0.0055  193 ALA A C   
1493 O O   . ALA A 193 ? 0.8384 0.6632 0.7196 -0.0484 -0.1807 -0.0045 193 ALA A O   
1494 C CB  . ALA A 193 ? 0.6856 0.4854 0.6073 -0.0953 -0.2594 0.0050  193 ALA A CB  
1495 N N   . ALA A 194 ? 0.8611 0.7359 0.8286 -0.0684 -0.1729 0.0110  194 ALA A N   
1496 C CA  . ALA A 194 ? 0.7370 0.6123 0.6890 -0.0533 -0.1415 0.0041  194 ALA A CA  
1497 C C   . ALA A 194 ? 0.7869 0.6144 0.6953 -0.0483 -0.1465 -0.0087 194 ALA A C   
1498 O O   . ALA A 194 ? 0.7512 0.5517 0.6571 -0.0612 -0.1706 -0.0093 194 ALA A O   
1499 C CB  . ALA A 194 ? 0.6660 0.5868 0.6713 -0.0573 -0.1206 0.0150  194 ALA A CB  
1500 N N   . GLY A 195 ? 0.7408 0.5570 0.6144 -0.0291 -0.1236 -0.0182 195 GLY A N   
1501 C CA  . GLY A 195 ? 0.8178 0.5948 0.6538 -0.0190 -0.1217 -0.0291 195 GLY A CA  
1502 C C   . GLY A 195 ? 0.8290 0.6190 0.7005 -0.0271 -0.1177 -0.0234 195 GLY A C   
1503 O O   . GLY A 195 ? 0.7995 0.6321 0.7237 -0.0386 -0.1115 -0.0111 195 GLY A O   
1504 N N   . THR A 196 ? 0.8502 0.5989 0.6877 -0.0191 -0.1207 -0.0322 196 THR A N   
1505 C CA  . THR A 196 ? 0.9598 0.7138 0.8230 -0.0244 -0.1164 -0.0269 196 THR A CA  
1506 C C   . THR A 196 ? 0.8249 0.6277 0.7189 -0.0139 -0.0849 -0.0220 196 THR A C   
1507 O O   . THR A 196 ? 0.8447 0.6591 0.7221 0.0034  -0.0651 -0.0275 196 THR A O   
1508 C CB  . THR A 196 ? 1.0266 0.7205 0.8396 -0.0139 -0.1251 -0.0383 196 THR A CB  
1509 O OG1 . THR A 196 ? 1.0668 0.7454 0.8338 0.0133  -0.1074 -0.0501 196 THR A OG1 
1510 C CG2 . THR A 196 ? 0.8819 0.5223 0.6663 -0.0295 -0.1615 -0.0425 196 THR A CG2 
1511 N N   . ASP A 197 ? 0.8030 0.6341 0.7412 -0.0252 -0.0806 -0.0107 197 ASP A N   
1512 C CA  . ASP A 197 ? 0.8134 0.6886 0.7802 -0.0176 -0.0547 -0.0057 197 ASP A CA  
1513 C C   . ASP A 197 ? 0.7952 0.6568 0.7500 -0.0051 -0.0455 -0.0088 197 ASP A C   
1514 O O   . ASP A 197 ? 0.7705 0.5907 0.7041 -0.0063 -0.0594 -0.0113 197 ASP A O   
1515 C CB  . ASP A 197 ? 0.7613 0.6768 0.7798 -0.0337 -0.0529 0.0090  197 ASP A CB  
1516 C CG  . ASP A 197 ? 0.7650 0.7241 0.8059 -0.0262 -0.0286 0.0123  197 ASP A CG  
1517 O OD1 . ASP A 197 ? 0.6735 0.6382 0.6963 -0.0135 -0.0161 0.0046  197 ASP A OD1 
1518 O OD2 . ASP A 197 ? 0.6783 0.6645 0.7534 -0.0333 -0.0221 0.0230  197 ASP A OD2 
1519 N N   . THR A 198 ? 0.7368 0.6326 0.7048 0.0068  -0.0232 -0.0081 198 THR A N   
1520 C CA  . THR A 198 ? 0.7022 0.5949 0.6631 0.0215  -0.0129 -0.0100 198 THR A CA  
1521 C C   . THR A 198 ? 0.6855 0.6211 0.6854 0.0173  0.0001  -0.0003 198 THR A C   
1522 O O   . THR A 198 ? 0.6205 0.5875 0.6481 0.0064  0.0043  0.0060  198 THR A O   
1523 C CB  . THR A 198 ? 0.7497 0.6410 0.6819 0.0446  0.0011  -0.0200 198 THR A CB  
1524 O OG1 . THR A 198 ? 0.8921 0.7408 0.7818 0.0502  -0.0098 -0.0293 198 THR A OG1 
1525 C CG2 . THR A 198 ? 0.8394 0.7253 0.7632 0.0625  0.0091  -0.0214 198 THR A CG2 
1526 N N   . THR A 199 ? 0.5854 0.5190 0.5834 0.0278  0.0059  0.0008  199 THR A N   
1527 C CA  . THR A 199 ? 0.5428 0.5115 0.5694 0.0268  0.0170  0.0088  199 THR A CA  
1528 C C   . THR A 199 ? 0.5288 0.5298 0.5580 0.0413  0.0326  0.0040  199 THR A C   
1529 O O   . THR A 199 ? 0.5573 0.5493 0.5654 0.0585  0.0366  -0.0033 199 THR A O   
1530 C CB  . THR A 199 ? 0.6664 0.6139 0.6893 0.0290  0.0127  0.0146  199 THR A CB  
1531 O OG1 . THR A 199 ? 0.5728 0.4911 0.5965 0.0119  -0.0025 0.0207  199 THR A OG1 
1532 C CG2 . THR A 199 ? 0.5544 0.5350 0.6018 0.0285  0.0233  0.0233  199 THR A CG2 
1533 N N   . ILE A 200 ? 0.4444 0.4824 0.4991 0.0346  0.0411  0.0086  200 ILE A N   
1534 C CA  . ILE A 200 ? 0.5541 0.6256 0.6164 0.0428  0.0534  0.0054  200 ILE A CA  
1535 C C   . ILE A 200 ? 0.5009 0.5820 0.5664 0.0548  0.0562  0.0074  200 ILE A C   
1536 O O   . ILE A 200 ? 0.3849 0.4787 0.4643 0.0497  0.0565  0.0135  200 ILE A O   
1537 C CB  . ILE A 200 ? 0.5239 0.6229 0.6065 0.0300  0.0587  0.0087  200 ILE A CB  
1538 C CG1 . ILE A 200 ? 0.5049 0.5913 0.5846 0.0190  0.0536  0.0089  200 ILE A CG1 
1539 C CG2 . ILE A 200 ? 0.3923 0.5217 0.4815 0.0346  0.0691  0.0054  200 ILE A CG2 
1540 C CD1 . ILE A 200 ? 0.4812 0.5816 0.5803 0.0065  0.0547  0.0158  200 ILE A CD1 
1541 N N   . THR A 201 ? 0.4511 0.5254 0.5012 0.0730  0.0585  0.0025  201 THR A N   
1542 C CA  . THR A 201 ? 0.4656 0.5450 0.5160 0.0876  0.0590  0.0049  201 THR A CA  
1543 C C   . THR A 201 ? 0.4570 0.5799 0.5322 0.0852  0.0640  0.0084  201 THR A C   
1544 O O   . THR A 201 ? 0.4063 0.5311 0.4863 0.0846  0.0605  0.0139  201 THR A O   
1545 C CB  . THR A 201 ? 0.5915 0.6618 0.6226 0.1111  0.0630  -0.0007 201 THR A CB  
1546 O OG1 . THR A 201 ? 0.5808 0.6053 0.5819 0.1126  0.0570  -0.0060 201 THR A OG1 
1547 C CG2 . THR A 201 ? 0.4814 0.5476 0.5081 0.1286  0.0610  0.0025  201 THR A CG2 
1548 N N   . VAL A 202 ? 0.3934 0.5490 0.4823 0.0831  0.0715  0.0058  202 VAL A N   
1549 C CA  . VAL A 202 ? 0.4437 0.6384 0.5549 0.0790  0.0732  0.0084  202 VAL A CA  
1550 C C   . VAL A 202 ? 0.4274 0.6173 0.5428 0.0639  0.0685  0.0124  202 VAL A C   
1551 O O   . VAL A 202 ? 0.4443 0.6481 0.5657 0.0651  0.0651  0.0153  202 VAL A O   
1552 C CB  . VAL A 202 ? 0.5358 0.7616 0.6612 0.0732  0.0814  0.0063  202 VAL A CB  
1553 C CG1 . VAL A 202 ? 0.4690 0.6821 0.5911 0.0553  0.0827  0.0052  202 VAL A CG1 
1554 C CG2 . VAL A 202 ? 0.5745 0.8404 0.7232 0.0694  0.0803  0.0088  202 VAL A CG2 
1555 N N   . ASN A 203 ? 0.4535 0.6237 0.5644 0.0512  0.0681  0.0131  203 ASN A N   
1556 C CA  . ASN A 203 ? 0.4066 0.5732 0.5212 0.0400  0.0666  0.0182  203 ASN A CA  
1557 C C   . ASN A 203 ? 0.3959 0.5460 0.5032 0.0460  0.0627  0.0245  203 ASN A C   
1558 O O   . ASN A 203 ? 0.2739 0.4298 0.3818 0.0444  0.0628  0.0289  203 ASN A O   
1559 C CB  . ASN A 203 ? 0.3725 0.5248 0.4873 0.0278  0.0673  0.0195  203 ASN A CB  
1560 C CG  . ASN A 203 ? 0.4783 0.6457 0.5985 0.0199  0.0719  0.0156  203 ASN A CG  
1561 O OD1 . ASN A 203 ? 0.4128 0.6016 0.5382 0.0213  0.0749  0.0122  203 ASN A OD1 
1562 N ND2 . ASN A 203 ? 0.3527 0.5097 0.4731 0.0111  0.0719  0.0172  203 ASN A ND2 
1563 N N   . VAL A 204 ? 0.3749 0.4999 0.4711 0.0532  0.0590  0.0253  204 VAL A N   
1564 C CA  . VAL A 204 ? 0.3375 0.4425 0.4245 0.0587  0.0554  0.0326  204 VAL A CA  
1565 C C   . VAL A 204 ? 0.3947 0.5179 0.4806 0.0714  0.0549  0.0332  204 VAL A C   
1566 O O   . VAL A 204 ? 0.3785 0.5010 0.4612 0.0708  0.0546  0.0398  204 VAL A O   
1567 C CB  . VAL A 204 ? 0.5125 0.5820 0.5834 0.0648  0.0499  0.0320  204 VAL A CB  
1568 C CG1 . VAL A 204 ? 0.4193 0.4657 0.4782 0.0717  0.0464  0.0402  204 VAL A CG1 
1569 C CG2 . VAL A 204 ? 0.3779 0.4277 0.4499 0.0494  0.0462  0.0327  204 VAL A CG2 
1570 N N   . LEU A 205 ? 0.3676 0.5089 0.4562 0.0840  0.0548  0.0271  205 LEU A N   
1571 C CA  . LEU A 205 ? 0.4829 0.6470 0.5748 0.0964  0.0517  0.0283  205 LEU A CA  
1572 C C   . LEU A 205 ? 0.4122 0.5991 0.5130 0.0852  0.0504  0.0292  205 LEU A C   
1573 O O   . LEU A 205 ? 0.3138 0.5028 0.4078 0.0907  0.0453  0.0334  205 LEU A O   
1574 C CB  . LEU A 205 ? 0.3354 0.5247 0.4366 0.1107  0.0535  0.0232  205 LEU A CB  
1575 C CG  . LEU A 205 ? 0.3717 0.5353 0.4566 0.1282  0.0551  0.0211  205 LEU A CG  
1576 C CD1 . LEU A 205 ? 0.3781 0.5719 0.4744 0.1408  0.0618  0.0165  205 LEU A CD1 
1577 C CD2 . LEU A 205 ? 0.4409 0.5807 0.5085 0.1452  0.0492  0.0264  205 LEU A CD2 
1578 N N   . ALA A 206 ? 0.3158 0.5156 0.4273 0.0704  0.0542  0.0252  206 ALA A N   
1579 C CA  . ALA A 206 ? 0.3250 0.5377 0.4385 0.0599  0.0523  0.0250  206 ALA A CA  
1580 C C   . ALA A 206 ? 0.3697 0.5584 0.4669 0.0582  0.0532  0.0317  206 ALA A C   
1581 O O   . ALA A 206 ? 0.3534 0.5451 0.4408 0.0597  0.0491  0.0332  206 ALA A O   
1582 C CB  . ALA A 206 ? 0.3271 0.5486 0.4501 0.0449  0.0571  0.0204  206 ALA A CB  
1583 N N   . TRP A 207 ? 0.2966 0.4617 0.3903 0.0551  0.0583  0.0367  207 TRP A N   
1584 C CA  . TRP A 207 ? 0.3289 0.4747 0.4113 0.0537  0.0620  0.0461  207 TRP A CA  
1585 C C   . TRP A 207 ? 0.4724 0.6073 0.5397 0.0668  0.0579  0.0522  207 TRP A C   
1586 O O   . TRP A 207 ? 0.3772 0.5053 0.4300 0.0691  0.0598  0.0585  207 TRP A O   
1587 C CB  . TRP A 207 ? 0.3934 0.5217 0.4824 0.0453  0.0665  0.0514  207 TRP A CB  
1588 C CG  . TRP A 207 ? 0.3202 0.4326 0.4047 0.0426  0.0722  0.0642  207 TRP A CG  
1589 C CD1 . TRP A 207 ? 0.3522 0.4683 0.4354 0.0388  0.0807  0.0702  207 TRP A CD1 
1590 C CD2 . TRP A 207 ? 0.4729 0.5623 0.5536 0.0434  0.0713  0.0741  207 TRP A CD2 
1591 N NE1 . TRP A 207 ? 0.3732 0.4752 0.4553 0.0377  0.0868  0.0846  207 TRP A NE1 
1592 C CE2 . TRP A 207 ? 0.4704 0.5553 0.5518 0.0386  0.0804  0.0875  207 TRP A CE2 
1593 C CE3 . TRP A 207 ? 0.4097 0.4791 0.4842 0.0484  0.0640  0.0734  207 TRP A CE3 
1594 C CZ2 . TRP A 207 ? 0.3916 0.4559 0.4720 0.0354  0.0823  0.1016  207 TRP A CZ2 
1595 C CZ3 . TRP A 207 ? 0.4819 0.5248 0.5511 0.0454  0.0640  0.0857  207 TRP A CZ3 
1596 C CH2 . TRP A 207 ? 0.4492 0.4911 0.5233 0.0374  0.0730  0.1003  207 TRP A CH2 
1597 N N   . LEU A 208 ? 0.4370 0.5680 0.5037 0.0776  0.0528  0.0507  208 LEU A N   
1598 C CA  . LEU A 208 ? 0.5293 0.6495 0.5799 0.0925  0.0478  0.0565  208 LEU A CA  
1599 C C   . LEU A 208 ? 0.4956 0.6391 0.5422 0.0987  0.0411  0.0537  208 LEU A C   
1600 O O   . LEU A 208 ? 0.5044 0.6369 0.5317 0.1057  0.0386  0.0604  208 LEU A O   
1601 C CB  . LEU A 208 ? 0.4353 0.5457 0.4842 0.1060  0.0438  0.0543  208 LEU A CB  
1602 C CG  . LEU A 208 ? 0.5455 0.6199 0.5881 0.1012  0.0460  0.0581  208 LEU A CG  
1603 C CD1 . LEU A 208 ? 0.4489 0.5064 0.4810 0.1181  0.0415  0.0545  208 LEU A CD1 
1604 C CD2 . LEU A 208 ? 0.4604 0.5076 0.4910 0.0951  0.0489  0.0715  208 LEU A CD2 
1605 N N   . TYR A 209 ? 0.4597 0.6345 0.5235 0.0951  0.0372  0.0445  209 TYR A N   
1606 C CA  . TYR A 209 ? 0.4383 0.6358 0.5006 0.0966  0.0274  0.0416  209 TYR A CA  
1607 C C   . TYR A 209 ? 0.5419 0.7252 0.5850 0.0878  0.0293  0.0434  209 TYR A C   
1608 O O   . TYR A 209 ? 0.4424 0.6237 0.4665 0.0940  0.0209  0.0450  209 TYR A O   
1609 C CB  . TYR A 209 ? 0.4326 0.6662 0.5206 0.0895  0.0239  0.0333  209 TYR A CB  
1610 C CG  . TYR A 209 ? 0.4966 0.7555 0.6014 0.1044  0.0191  0.0328  209 TYR A CG  
1611 C CD1 . TYR A 209 ? 0.4784 0.7544 0.5823 0.1178  0.0066  0.0355  209 TYR A CD1 
1612 C CD2 . TYR A 209 ? 0.4391 0.7046 0.5587 0.1072  0.0273  0.0302  209 TYR A CD2 
1613 C CE1 . TYR A 209 ? 0.5222 0.8253 0.6443 0.1345  0.0035  0.0365  209 TYR A CE1 
1614 C CE2 . TYR A 209 ? 0.5391 0.8280 0.6724 0.1245  0.0258  0.0305  209 TYR A CE2 
1615 C CZ  . TYR A 209 ? 0.4623 0.7719 0.5991 0.1385  0.0145  0.0341  209 TYR A CZ  
1616 O OH  . TYR A 209 ? 0.5719 0.9086 0.7251 0.1585  0.0143  0.0357  209 TYR A OH  
1617 N N   . ALA A 210 ? 0.4268 0.5994 0.4722 0.0754  0.0399  0.0432  210 ALA A N   
1618 C CA  . ALA A 210 ? 0.4439 0.6006 0.4685 0.0710  0.0449  0.0459  210 ALA A CA  
1619 C C   . ALA A 210 ? 0.4588 0.5921 0.4586 0.0822  0.0484  0.0572  210 ALA A C   
1620 O O   . ALA A 210 ? 0.5813 0.7044 0.5543 0.0868  0.0469  0.0588  210 ALA A O   
1621 C CB  . ALA A 210 ? 0.3887 0.5390 0.4229 0.0595  0.0573  0.0464  210 ALA A CB  
1622 N N   . ALA A 211 ? 0.4590 0.5797 0.4637 0.0867  0.0531  0.0654  211 ALA A N   
1623 C CA  . ALA A 211 ? 0.6095 0.7060 0.5911 0.0961  0.0572  0.0783  211 ALA A CA  
1624 C C   . ALA A 211 ? 0.5863 0.6838 0.5458 0.1106  0.0445  0.0775  211 ALA A C   
1625 O O   . ALA A 211 ? 0.5808 0.6630 0.5105 0.1172  0.0461  0.0837  211 ALA A O   
1626 C CB  . ALA A 211 ? 0.5369 0.6167 0.5281 0.0962  0.0610  0.0863  211 ALA A CB  
1627 N N   . VAL A 212 ? 0.5135 0.6301 0.4865 0.1172  0.0318  0.0705  212 VAL A N   
1628 C CA  . VAL A 212 ? 0.6408 0.7641 0.5978 0.1318  0.0170  0.0704  212 VAL A CA  
1629 C C   . VAL A 212 ? 0.6640 0.7932 0.6030 0.1277  0.0092  0.0650  212 VAL A C   
1630 O O   . VAL A 212 ? 0.6747 0.7894 0.5814 0.1383  0.0025  0.0696  212 VAL A O   
1631 C CB  . VAL A 212 ? 0.5818 0.7344 0.5646 0.1393  0.0060  0.0639  212 VAL A CB  
1632 C CG1 . VAL A 212 ? 0.4768 0.6457 0.4498 0.1531  -0.0121 0.0637  212 VAL A CG1 
1633 C CG2 . VAL A 212 ? 0.5460 0.6815 0.5340 0.1481  0.0124  0.0691  212 VAL A CG2 
1634 N N   . ILE A 213 ? 0.5987 0.7446 0.5537 0.1126  0.0092  0.0550  213 ILE A N   
1635 C CA  . ILE A 213 ? 0.6292 0.7744 0.5635 0.1071  -0.0002 0.0483  213 ILE A CA  
1636 C C   . ILE A 213 ? 0.7292 0.8388 0.6230 0.1117  0.0112  0.0552  213 ILE A C   
1637 O O   . ILE A 213 ? 0.7293 0.8258 0.5883 0.1161  0.0017  0.0524  213 ILE A O   
1638 C CB  . ILE A 213 ? 0.6528 0.8160 0.6104 0.0890  -0.0004 0.0375  213 ILE A CB  
1639 C CG1 . ILE A 213 ? 0.6794 0.8815 0.6757 0.0855  -0.0108 0.0323  213 ILE A CG1 
1640 C CG2 . ILE A 213 ? 0.7398 0.8910 0.6690 0.0822  -0.0098 0.0302  213 ILE A CG2 
1641 C CD1 . ILE A 213 ? 0.5611 0.7805 0.5808 0.0668  -0.0096 0.0238  213 ILE A CD1 
1642 N N   . ASN A 214 ? 0.5871 0.6810 0.4840 0.1111  0.0314  0.0648  214 ASN A N   
1643 C CA  . ASN A 214 ? 0.7031 0.7685 0.5671 0.1165  0.0468  0.0745  214 ASN A CA  
1644 C C   . ASN A 214 ? 0.8095 0.8545 0.6500 0.1309  0.0508  0.0892  214 ASN A C   
1645 O O   . ASN A 214 ? 0.8606 0.8843 0.6804 0.1351  0.0684  0.1017  214 ASN A O   
1646 C CB  . ASN A 214 ? 0.6783 0.7428 0.5631 0.1066  0.0670  0.0793  214 ASN A CB  
1647 C CG  . ASN A 214 ? 0.8034 0.8728 0.6896 0.0972  0.0678  0.0682  214 ASN A CG  
1648 O OD1 . ASN A 214 ? 0.7382 0.7940 0.6101 0.0987  0.0831  0.0726  214 ASN A OD1 
1649 N ND2 . ASN A 214 ? 0.8424 0.9311 0.7460 0.0883  0.0523  0.0547  214 ASN A ND2 
1650 N N   . GLY A 215 ? 0.7679 0.8190 0.6114 0.1395  0.0362  0.0894  215 GLY A N   
1651 C CA  . GLY A 215 ? 0.9079 0.9358 0.7209 0.1553  0.0361  0.1024  215 GLY A CA  
1652 C C   . GLY A 215 ? 0.9178 0.9350 0.7464 0.1574  0.0443  0.1144  215 GLY A C   
1653 O O   . GLY A 215 ? 1.1500 1.1459 0.9533 0.1710  0.0424  0.1254  215 GLY A O   
1654 N N   . ASP A 216 ? 1.0149 1.0416 0.8801 0.1444  0.0519  0.1126  216 ASP A N   
1655 C CA  . ASP A 216 ? 1.0404 1.0506 0.9170 0.1443  0.0573  0.1227  216 ASP A CA  
1656 C C   . ASP A 216 ? 1.0417 1.0617 0.9308 0.1538  0.0416  0.1149  216 ASP A C   
1657 O O   . ASP A 216 ? 1.0000 1.0500 0.9110 0.1515  0.0322  0.1009  216 ASP A O   
1658 C CB  . ASP A 216 ? 0.9875 1.0001 0.8940 0.1261  0.0705  0.1247  216 ASP A CB  
1659 C CG  . ASP A 216 ? 1.0830 1.0682 0.9851 0.1215  0.0844  0.1440  216 ASP A CG  
1660 O OD1 . ASP A 216 ? 1.1270 1.0876 1.0027 0.1327  0.0838  0.1554  216 ASP A OD1 
1661 O OD2 . ASP A 216 ? 1.0835 1.0722 1.0097 0.1059  0.0951  0.1487  216 ASP A OD2 
1662 N N   . ARG A 217 ? 0.9866 0.9801 0.8610 0.1653  0.0401  0.1252  217 ARG A N   
1663 C CA  . ARG A 217 ? 0.7760 0.7750 0.6570 0.1800  0.0267  0.1194  217 ARG A CA  
1664 C C   . ARG A 217 ? 0.7646 0.7253 0.6362 0.1859  0.0297  0.1295  217 ARG A C   
1665 O O   . ARG A 217 ? 0.8550 0.8143 0.7268 0.2021  0.0200  0.1256  217 ARG A O   
1666 C CB  . ARG A 217 ? 0.8487 0.8600 0.7097 0.1991  0.0112  0.1180  217 ARG A CB  
1667 C CG  . ARG A 217 ? 0.8296 0.8825 0.7060 0.1938  0.0007  0.1043  217 ARG A CG  
1668 C CD  . ARG A 217 ? 0.7296 0.7945 0.5867 0.2109  -0.0184 0.1038  217 ARG A CD  
1669 N NE  . ARG A 217 ? 0.6727 0.7550 0.5452 0.2289  -0.0307 0.1024  217 ARG A NE  
1670 C CZ  . ARG A 217 ? 0.6523 0.7806 0.5548 0.2313  -0.0444 0.0926  217 ARG A CZ  
1671 N NH1 . ARG A 217 ? 0.6823 0.8407 0.6024 0.2140  -0.0493 0.0825  217 ARG A NH1 
1672 N NH2 . ARG A 217 ? 0.6623 0.8066 0.5781 0.2517  -0.0530 0.0938  217 ARG A NH2 
1673 N N   . TRP A 218 ? 0.7855 0.7146 0.6491 0.1735  0.0425  0.1430  218 TRP A N   
1674 C CA  . TRP A 218 ? 0.7916 0.6769 0.6413 0.1770  0.0433  0.1541  218 TRP A CA  
1675 C C   . TRP A 218 ? 0.8740 0.7551 0.7412 0.1771  0.0369  0.1431  218 TRP A C   
1676 O O   . TRP A 218 ? 0.9429 0.7902 0.7923 0.1906  0.0312  0.1463  218 TRP A O   
1677 C CB  . TRP A 218 ? 0.8461 0.7054 0.6932 0.1579  0.0584  0.1715  218 TRP A CB  
1678 C CG  . TRP A 218 ? 0.9046 0.7793 0.7863 0.1338  0.0655  0.1673  218 TRP A CG  
1679 C CD1 . TRP A 218 ? 0.7972 0.7025 0.6969 0.1214  0.0750  0.1654  218 TRP A CD1 
1680 C CD2 . TRP A 218 ? 0.8137 0.6709 0.7126 0.1207  0.0622  0.1647  218 TRP A CD2 
1681 N NE1 . TRP A 218 ? 0.8187 0.7304 0.7489 0.1018  0.0778  0.1627  218 TRP A NE1 
1682 C CE2 . TRP A 218 ? 0.8747 0.7572 0.8045 0.1001  0.0691  0.1619  218 TRP A CE2 
1683 C CE3 . TRP A 218 ? 0.8728 0.6920 0.7603 0.1255  0.0529  0.1640  218 TRP A CE3 
1684 C CZ2 . TRP A 218 ? 0.8518 0.7250 0.8024 0.0832  0.0654  0.1586  218 TRP A CZ2 
1685 C CZ3 . TRP A 218 ? 0.9134 0.7190 0.8179 0.1084  0.0496  0.1597  218 TRP A CZ3 
1686 C CH2 . TRP A 218 ? 0.8928 0.7267 0.8294 0.0869  0.0550  0.1571  218 TRP A CH2 
1687 N N   . PHE A 219 ? 0.7452 0.6559 0.6425 0.1639  0.0382  0.1302  219 PHE A N   
1688 C CA  . PHE A 219 ? 0.7567 0.6619 0.6666 0.1639  0.0338  0.1194  219 PHE A CA  
1689 C C   . PHE A 219 ? 0.7770 0.7036 0.6879 0.1879  0.0245  0.1078  219 PHE A C   
1690 O O   . PHE A 219 ? 0.7040 0.6191 0.6164 0.1950  0.0219  0.1002  219 PHE A O   
1691 C CB  . PHE A 219 ? 0.7117 0.6408 0.6510 0.1421  0.0389  0.1111  219 PHE A CB  
1692 C CG  . PHE A 219 ? 0.6109 0.5871 0.5668 0.1391  0.0407  0.1033  219 PHE A CG  
1693 C CD1 . PHE A 219 ? 0.5324 0.5425 0.5023 0.1481  0.0347  0.0896  219 PHE A CD1 
1694 C CD2 . PHE A 219 ? 0.6888 0.6734 0.6446 0.1278  0.0488  0.1105  219 PHE A CD2 
1695 C CE1 . PHE A 219 ? 0.5807 0.6297 0.5647 0.1425  0.0345  0.0829  219 PHE A CE1 
1696 C CE2 . PHE A 219 ? 0.6437 0.6633 0.6085 0.1252  0.0489  0.1024  219 PHE A CE2 
1697 C CZ  . PHE A 219 ? 0.5848 0.6352 0.5638 0.1310  0.0406  0.0884  219 PHE A CZ  
1698 N N   . LEU A 220 ? 0.7361 0.6943 0.6465 0.2008  0.0193  0.1067  220 LEU A N   
1699 C CA  . LEU A 220 ? 0.7644 0.7510 0.6828 0.2232  0.0103  0.0982  220 LEU A CA  
1700 C C   . LEU A 220 ? 0.7624 0.7109 0.6549 0.2481  0.0056  0.1041  220 LEU A C   
1701 O O   . LEU A 220 ? 0.8391 0.7405 0.7034 0.2484  0.0070  0.1162  220 LEU A O   
1702 C CB  . LEU A 220 ? 0.7101 0.7380 0.6340 0.2290  0.0021  0.0972  220 LEU A CB  
1703 C CG  . LEU A 220 ? 0.6587 0.7267 0.6073 0.2085  0.0039  0.0886  220 LEU A CG  
1704 C CD1 . LEU A 220 ? 0.7054 0.8083 0.6550 0.2157  -0.0091 0.0868  220 LEU A CD1 
1705 C CD2 . LEU A 220 ? 0.5439 0.6368 0.5229 0.2012  0.0079  0.0771  220 LEU A CD2 
1706 N N   . ASN A 221 ? 0.7719 0.7401 0.6736 0.2700  0.0010  0.0965  221 ASN A N   
1707 C CA  . ASN A 221 ? 0.8463 0.7788 0.7219 0.2987  -0.0033 0.1010  221 ASN A CA  
1708 C C   . ASN A 221 ? 0.8198 0.8007 0.7124 0.3271  -0.0105 0.0967  221 ASN A C   
1709 O O   . ASN A 221 ? 0.7869 0.8274 0.7129 0.3208  -0.0127 0.0907  221 ASN A O   
1710 C CB  . ASN A 221 ? 0.9480 0.8323 0.8094 0.2974  0.0019  0.0967  221 ASN A CB  
1711 C CG  . ASN A 221 ? 0.9847 0.9013 0.8703 0.3002  0.0063  0.0825  221 ASN A CG  
1712 O OD1 . ASN A 221 ? 0.9673 0.9450 0.8849 0.3009  0.0066  0.0770  221 ASN A OD1 
1713 N ND2 . ASN A 221 ? 1.0649 0.9374 0.9328 0.3010  0.0093  0.0772  221 ASN A ND2 
1714 N N   . ARG A 222 ? 0.8542 0.8086 0.7241 0.3587  -0.0145 0.1011  222 ARG A N   
1715 C CA  . ARG A 222 ? 0.9977 0.9980 0.8849 0.3904  -0.0208 0.0996  222 ARG A CA  
1716 C C   . ARG A 222 ? 0.9960 1.0028 0.8935 0.4073  -0.0124 0.0905  222 ARG A C   
1717 O O   . ARG A 222 ? 0.9364 0.9927 0.8577 0.4315  -0.0140 0.0892  222 ARG A O   
1718 C CB  . ARG A 222 ? 1.0244 0.9957 0.8795 0.4208  -0.0306 0.1113  222 ARG A CB  
1719 C CG  . ARG A 222 ? 1.1390 1.0270 0.9480 0.4317  -0.0264 0.1159  222 ARG A CG  
1720 C CD  . ARG A 222 ? 1.2203 1.0940 1.0093 0.4603  -0.0313 0.1181  222 ARG A CD  
1721 N NE  . ARG A 222 ? 1.2725 1.0734 1.0235 0.4672  -0.0256 0.1161  222 ARG A NE  
1722 C CZ  . ARG A 222 ? 1.3275 1.1200 1.0678 0.4911  -0.0237 0.1106  222 ARG A CZ  
1723 N NH1 . ARG A 222 ? 1.3412 1.1958 1.1094 0.5107  -0.0256 0.1081  222 ARG A NH1 
1724 N NH2 . ARG A 222 ? 1.3614 1.0806 1.0615 0.4947  -0.0201 0.1081  222 ARG A NH2 
1725 N N   . PHE A 223 ? 1.0294 0.9888 0.9096 0.3943  -0.0035 0.0847  223 PHE A N   
1726 C CA  . PHE A 223 ? 1.0450 1.0003 0.9247 0.4111  0.0051  0.0754  223 PHE A CA  
1727 C C   . PHE A 223 ? 0.9376 0.9640 0.8637 0.3992  0.0121  0.0671  223 PHE A C   
1728 O O   . PHE A 223 ? 0.9352 0.9990 0.8885 0.3705  0.0103  0.0667  223 PHE A O   
1729 C CB  . PHE A 223 ? 1.0791 0.9583 0.9228 0.3970  0.0089  0.0712  223 PHE A CB  
1730 C CG  . PHE A 223 ? 1.2393 1.0417 1.0342 0.4128  0.0030  0.0789  223 PHE A CG  
1731 C CD1 . PHE A 223 ? 1.1670 0.9565 0.9416 0.4483  0.0018  0.0795  223 PHE A CD1 
1732 C CD2 . PHE A 223 ? 1.2543 1.0011 1.0265 0.3853  -0.0005 0.0856  223 PHE A CD2 
1733 C CE1 . PHE A 223 ? 1.2823 1.0007 1.0113 0.4553  -0.0035 0.0852  223 PHE A CE1 
1734 C CE2 . PHE A 223 ? 1.2721 0.9456 0.9992 0.3971  -0.0059 0.0943  223 PHE A CE2 
1735 C CZ  . PHE A 223 ? 1.3919 1.0479 1.0951 0.4333  -0.0079 0.0937  223 PHE A CZ  
1736 N N   . THR A 224 ? 0.9501 0.9925 0.8822 0.4232  0.0211  0.0613  224 THR A N   
1737 C CA  . THR A 224 ? 0.9897 1.0942 0.9620 0.4133  0.0305  0.0548  224 THR A CA  
1738 C C   . THR A 224 ? 0.9763 1.0441 0.9260 0.4176  0.0429  0.0451  224 THR A C   
1739 O O   . THR A 224 ? 0.9975 1.0033 0.9038 0.4346  0.0434  0.0428  224 THR A O   
1740 C CB  . THR A 224 ? 0.8993 1.0737 0.9075 0.4236  0.0300  0.0580  224 THR A CB  
1741 O OG1 . THR A 224 ? 0.9273 1.1654 0.9803 0.4038  0.0359  0.0550  224 THR A OG1 
1742 C CG2 . THR A 224 ? 0.8470 1.0037 0.8349 0.4515  0.0379  0.0565  224 THR A CG2 
1743 N N   . THR A 225 ? 0.8689 0.9726 0.8447 0.4004  0.0519  0.0392  225 THR A N   
1744 C CA  . THR A 225 ? 0.9330 1.0045 0.8862 0.4032  0.0632  0.0297  225 THR A CA  
1745 C C   . THR A 225 ? 0.9283 1.0655 0.9178 0.3980  0.0756  0.0277  225 THR A C   
1746 O O   . THR A 225 ? 0.8303 1.0330 0.8656 0.3818  0.0743  0.0322  225 THR A O   
1747 C CB  . THR A 225 ? 0.9391 0.9636 0.8745 0.3660  0.0588  0.0241  225 THR A CB  
1748 O OG1 . THR A 225 ? 0.9193 0.8823 0.8119 0.3753  0.0627  0.0154  225 THR A OG1 
1749 C CG2 . THR A 225 ? 0.8486 0.9269 0.8239 0.3350  0.0630  0.0222  225 THR A CG2 
1750 N N   . THR A 226 ? 0.9501 1.0647 0.9154 0.4106  0.0870  0.0216  226 THR A N   
1751 C CA  . THR A 226 ? 0.8183 0.9822 0.8099 0.4039  0.1008  0.0205  226 THR A CA  
1752 C C   . THR A 226 ? 0.9182 1.0649 0.9033 0.3822  0.1052  0.0128  226 THR A C   
1753 O O   . THR A 226 ? 0.8851 0.9718 0.8371 0.3783  0.0989  0.0068  226 THR A O   
1754 C CB  . THR A 226 ? 0.8948 1.0452 0.8612 0.4312  0.1122  0.0195  226 THR A CB  
1755 O OG1 . THR A 226 ? 0.9519 1.0376 0.8691 0.4349  0.1170  0.0093  226 THR A OG1 
1756 C CG2 . THR A 226 ? 0.8563 0.9856 0.8031 0.4582  0.1057  0.0241  226 THR A CG2 
1757 N N   . LEU A 227 ? 0.8528 1.0511 0.8699 0.3672  0.1157  0.0139  227 LEU A N   
1758 C CA  . LEU A 227 ? 0.8411 1.0302 0.8557 0.3452  0.1200  0.0077  227 LEU A CA  
1759 C C   . LEU A 227 ? 0.9340 1.0492 0.8914 0.3577  0.1231  -0.0027 227 LEU A C   
1760 O O   . LEU A 227 ? 0.8770 0.9513 0.8159 0.3343  0.1145  -0.0085 227 LEU A O   
1761 C CB  . LEU A 227 ? 0.7722 1.0225 0.8250 0.3289  0.1314  0.0118  227 LEU A CB  
1762 C CG  . LEU A 227 ? 0.8878 1.1551 0.9603 0.2969  0.1316  0.0100  227 LEU A CG  
1763 C CD1 . LEU A 227 ? 0.9186 1.2432 1.0290 0.2804  0.1411  0.0159  227 LEU A CD1 
1764 C CD2 . LEU A 227 ? 0.9355 1.1425 0.9648 0.2933  0.1329  0.0003  227 LEU A CD2 
1765 N N   . ASN A 228 ? 0.9312 1.0227 0.8578 0.3830  0.1297  -0.0041 228 ASN A N   
1766 C CA  . ASN A 228 ? 0.9587 0.9776 0.8260 0.3936  0.1310  -0.0147 228 ASN A CA  
1767 C C   . ASN A 228 ? 1.0398 0.9786 0.8626 0.3987  0.1147  -0.0210 228 ASN A C   
1768 O O   . ASN A 228 ? 1.0212 0.9042 0.8123 0.3826  0.1056  -0.0293 228 ASN A O   
1769 C CB  . ASN A 228 ? 0.9241 0.9430 0.7702 0.4194  0.1437  -0.0133 228 ASN A CB  
1770 C CG  . ASN A 228 ? 1.1143 1.1713 0.9751 0.4116  0.1597  -0.0118 228 ASN A CG  
1771 O OD1 . ASN A 228 ? 1.0001 1.1144 0.9088 0.3881  0.1633  -0.0067 228 ASN A OD1 
1772 N ND2 . ASN A 228 ? 1.1423 1.1646 0.9592 0.4310  0.1689  -0.0156 228 ASN A ND2 
1773 N N   . ASP A 229 ? 1.0704 1.0008 0.8911 0.4134  0.1076  -0.0154 229 ASP A N   
1774 C CA  . ASP A 229 ? 1.0802 0.9319 0.8599 0.4148  0.0913  -0.0188 229 ASP A CA  
1775 C C   . ASP A 229 ? 1.0351 0.8794 0.8321 0.3706  0.0770  -0.0174 229 ASP A C   
1776 O O   . ASP A 229 ? 1.0528 0.8285 0.8148 0.3545  0.0628  -0.0216 229 ASP A O   
1777 C CB  . ASP A 229 ? 1.0484 0.9047 0.8318 0.4319  0.0861  -0.0099 229 ASP A CB  
1778 C CG  . ASP A 229 ? 1.2909 1.1522 1.0563 0.4613  0.0956  -0.0089 229 ASP A CG  
1779 O OD1 . ASP A 229 ? 1.4126 1.2089 1.1231 0.4742  0.0953  -0.0167 229 ASP A OD1 
1780 O OD2 . ASP A 229 ? 1.2373 1.1662 1.0424 0.4711  0.1025  0.0001  229 ASP A OD2 
1781 N N   . PHE A 230 ? 0.9594 0.8739 0.8107 0.3480  0.0794  -0.0107 230 PHE A N   
1782 C CA  . PHE A 230 ? 0.9767 0.8889 0.8450 0.3062  0.0683  -0.0090 230 PHE A CA  
1783 C C   . PHE A 230 ? 0.9195 0.8034 0.7690 0.2882  0.0673  -0.0176 230 PHE A C   
1784 O O   . PHE A 230 ? 0.8860 0.7242 0.7195 0.2642  0.0536  -0.0190 230 PHE A O   
1785 C CB  . PHE A 230 ? 0.7769 0.7657 0.7004 0.2893  0.0719  -0.0015 230 PHE A CB  
1786 C CG  . PHE A 230 ? 0.7949 0.7850 0.7354 0.2505  0.0638  0.0003  230 PHE A CG  
1787 C CD1 . PHE A 230 ? 0.7161 0.6887 0.6584 0.2359  0.0530  0.0072  230 PHE A CD1 
1788 C CD2 . PHE A 230 ? 0.7565 0.7642 0.7091 0.2306  0.0683  -0.0039 230 PHE A CD2 
1789 C CE1 . PHE A 230 ? 0.7608 0.7371 0.7192 0.2035  0.0482  0.0101  230 PHE A CE1 
1790 C CE2 . PHE A 230 ? 0.7600 0.7692 0.7279 0.1984  0.0617  -0.0016 230 PHE A CE2 
1791 C CZ  . PHE A 230 ? 0.8241 0.8192 0.7959 0.1855  0.0523  0.0055  230 PHE A CZ  
1792 N N   . ASN A 231 ? 1.0091 0.9212 0.8609 0.2996  0.0817  -0.0222 231 ASN A N   
1793 C CA  . ASN A 231 ? 0.9859 0.8731 0.8174 0.2846  0.0809  -0.0301 231 ASN A CA  
1794 C C   . ASN A 231 ? 0.9314 0.7308 0.7030 0.2903  0.0678  -0.0389 231 ASN A C   
1795 O O   . ASN A 231 ? 1.0165 0.7827 0.7732 0.2662  0.0558  -0.0435 231 ASN A O   
1796 C CB  . ASN A 231 ? 0.8795 0.8082 0.7173 0.3018  0.1013  -0.0319 231 ASN A CB  
1797 C CG  . ASN A 231 ? 0.8885 0.8942 0.7832 0.2812  0.1096  -0.0245 231 ASN A CG  
1798 O OD1 . ASN A 231 ? 0.8316 0.8464 0.7491 0.2494  0.0995  -0.0219 231 ASN A OD1 
1799 N ND2 . ASN A 231 ? 0.9108 0.9716 0.8285 0.2994  0.1282  -0.0203 231 ASN A ND2 
1800 N N   . LEU A 232 ? 0.9033 0.6626 0.6392 0.3219  0.0683  -0.0413 232 LEU A N   
1801 C CA  . LEU A 232 ? 1.0537 0.7210 0.7277 0.3263  0.0533  -0.0502 232 LEU A CA  
1802 C C   . LEU A 232 ? 1.1444 0.7749 0.8220 0.2930  0.0312  -0.0455 232 LEU A C   
1803 O O   . LEU A 232 ? 1.2648 0.8310 0.9067 0.2771  0.0140  -0.0516 232 LEU A O   
1804 C CB  . LEU A 232 ? 1.0954 0.7257 0.7278 0.3708  0.0600  -0.0533 232 LEU A CB  
1805 C CG  . LEU A 232 ? 1.2734 0.9164 0.8831 0.4035  0.0799  -0.0593 232 LEU A CG  
1806 C CD1 . LEU A 232 ? 1.1224 0.7720 0.7215 0.4335  0.0875  -0.0535 232 LEU A CD1 
1807 C CD2 . LEU A 232 ? 1.2380 0.8120 0.7889 0.3984  0.0710  -0.0720 232 LEU A CD2 
1808 N N   . VAL A 233 ? 1.0350 0.7054 0.7550 0.2817  0.0310  -0.0338 233 VAL A N   
1809 C CA  . VAL A 233 ? 1.0644 0.7094 0.7938 0.2491  0.0141  -0.0263 233 VAL A CA  
1810 C C   . VAL A 233 ? 1.0803 0.7568 0.8434 0.2124  0.0100  -0.0246 233 VAL A C   
1811 O O   . VAL A 233 ? 1.1253 0.7646 0.8819 0.1852  -0.0061 -0.0231 233 VAL A O   
1812 C CB  . VAL A 233 ? 1.1040 0.7766 0.8600 0.2531  0.0166  -0.0140 233 VAL A CB  
1813 C CG1 . VAL A 233 ? 1.1350 0.7637 0.8863 0.2266  0.0008  -0.0052 233 VAL A CG1 
1814 C CG2 . VAL A 233 ? 1.1669 0.8282 0.8984 0.2954  0.0243  -0.0151 233 VAL A CG2 
1815 N N   . ALA A 234 ? 0.9410 0.6864 0.7414 0.2110  0.0240  -0.0238 234 ALA A N   
1816 C CA  . ALA A 234 ? 1.0089 0.7849 0.8405 0.1793  0.0215  -0.0216 234 ALA A CA  
1817 C C   . ALA A 234 ? 1.0376 0.7711 0.8387 0.1692  0.0111  -0.0306 234 ALA A C   
1818 O O   . ALA A 234 ? 1.0082 0.7332 0.8212 0.1400  -0.0017 -0.0275 234 ALA A O   
1819 C CB  . ALA A 234 ? 0.9968 0.8470 0.8673 0.1820  0.0382  -0.0198 234 ALA A CB  
1820 N N   . MET A 235 ? 1.0671 0.7746 0.8282 0.1943  0.0164  -0.0413 235 MET A N   
1821 C CA  . MET A 235 ? 1.0798 0.7422 0.8039 0.1872  0.0052  -0.0510 235 MET A CA  
1822 C C   . MET A 235 ? 1.1945 0.7890 0.8932 0.1673  -0.0206 -0.0515 235 MET A C   
1823 O O   . MET A 235 ? 1.1985 0.7761 0.8951 0.1427  -0.0364 -0.0532 235 MET A O   
1824 C CB  . MET A 235 ? 1.2236 0.8611 0.8997 0.2228  0.0168  -0.0620 235 MET A CB  
1825 C CG  . MET A 235 ? 1.2894 0.8570 0.9078 0.2214  0.0011  -0.0741 235 MET A CG  
1826 S SD  . MET A 235 ? 1.8206 1.2903 1.3639 0.2483  -0.0109 -0.0843 235 MET A SD  
1827 C CE  . MET A 235 ? 1.6395 1.0322 1.1248 0.2318  -0.0373 -0.0973 235 MET A CE  
1828 N N   . LYS A 236 ? 1.2386 0.7938 0.9189 0.1770  -0.0261 -0.0491 236 LYS A N   
1829 C CA  . LYS A 236 ? 1.1969 0.6848 0.8536 0.1559  -0.0510 -0.0479 236 LYS A CA  
1830 C C   . LYS A 236 ? 1.1584 0.6771 0.8664 0.1163  -0.0605 -0.0344 236 LYS A C   
1831 O O   . LYS A 236 ? 1.2743 0.7495 0.9732 0.0907  -0.0827 -0.0323 236 LYS A O   
1832 C CB  . LYS A 236 ? 1.2685 0.7085 0.8950 0.1758  -0.0526 -0.0462 236 LYS A CB  
1833 C CG  . LYS A 236 ? 1.3614 0.7720 1.0003 0.1473  -0.0693 -0.0339 236 LYS A CG  
1834 C CD  . LYS A 236 ? 1.5352 0.8499 1.1185 0.1384  -0.0949 -0.0406 236 LYS A CD  
1835 C CE  . LYS A 236 ? 1.4988 0.7829 1.0941 0.1117  -0.1091 -0.0258 236 LYS A CE  
1836 N NZ  . LYS A 236 ? 1.3421 0.6802 1.0001 0.0721  -0.1126 -0.0113 236 LYS A NZ  
1837 N N   . TYR A 237 ? 1.0098 0.6020 0.7708 0.1109  -0.0446 -0.0249 237 TYR A N   
1838 C CA  . TYR A 237 ? 1.0650 0.6910 0.8742 0.0784  -0.0491 -0.0112 237 TYR A CA  
1839 C C   . TYR A 237 ? 0.9864 0.6642 0.8277 0.0649  -0.0442 -0.0117 237 TYR A C   
1840 O O   . TYR A 237 ? 0.8900 0.6097 0.7752 0.0451  -0.0413 -0.0004 237 TYR A O   
1841 C CB  . TYR A 237 ? 0.9823 0.6435 0.8213 0.0824  -0.0363 0.0011  237 TYR A CB  
1842 C CG  . TYR A 237 ? 1.0004 0.6090 0.8130 0.0889  -0.0435 0.0061  237 TYR A CG  
1843 C CD1 . TYR A 237 ? 1.0837 0.6615 0.9029 0.0619  -0.0576 0.0179  237 TYR A CD1 
1844 C CD2 . TYR A 237 ? 1.0532 0.6438 0.8355 0.1224  -0.0357 0.0006  237 TYR A CD2 
1845 C CE1 . TYR A 237 ? 1.1485 0.6736 0.9411 0.0666  -0.0641 0.0238  237 TYR A CE1 
1846 C CE2 . TYR A 237 ? 1.1492 0.6870 0.9036 0.1302  -0.0425 0.0056  237 TYR A CE2 
1847 C CZ  . TYR A 237 ? 1.1271 0.6298 0.8850 0.1014  -0.0568 0.0171  237 TYR A CZ  
1848 O OH  . TYR A 237 ? 1.2968 0.7427 1.0247 0.1078  -0.0634 0.0233  237 TYR A OH  
1849 N N   . ASN A 238 ? 0.7597 0.7224 0.7045 0.0188  -0.0512 0.0193  238 ASN A N   
1850 C CA  . ASN A 238 ? 0.8305 0.8065 0.7697 -0.0019 -0.0697 0.0376  238 ASN A CA  
1851 C C   . ASN A 238 ? 0.7885 0.7847 0.7500 -0.0073 -0.0680 0.0614  238 ASN A C   
1852 O O   . ASN A 238 ? 0.6820 0.6689 0.6637 -0.0189 -0.0873 0.0744  238 ASN A O   
1853 C CB  . ASN A 238 ? 0.7377 0.6854 0.6938 -0.0123 -0.0943 0.0324  238 ASN A CB  
1854 C CG  . ASN A 238 ? 0.9133 0.8646 0.8448 -0.0286 -0.1208 0.0442  238 ASN A CG  
1855 O OD1 . ASN A 238 ? 1.0075 0.9747 0.8916 -0.0357 -0.1188 0.0484  238 ASN A OD1 
1856 N ND2 . ASN A 238 ? 0.8674 0.8053 0.8300 -0.0352 -0.1474 0.0486  238 ASN A ND2 
1857 N N   . TYR A 239 ? 0.6672 0.6921 0.6278 0.0027  -0.0470 0.0640  239 TYR A N   
1858 C CA  . TYR A 239 ? 0.6607 0.7107 0.6372 -0.0049 -0.0440 0.0846  239 TYR A CA  
1859 C C   . TYR A 239 ? 0.7273 0.8165 0.6696 -0.0211 -0.0392 0.0953  239 TYR A C   
1860 O O   . TYR A 239 ? 0.7293 0.8432 0.6421 -0.0170 -0.0259 0.0806  239 TYR A O   
1861 C CB  . TYR A 239 ? 0.6005 0.6616 0.6018 0.0145  -0.0261 0.0808  239 TYR A CB  
1862 C CG  . TYR A 239 ? 0.5665 0.5997 0.6016 0.0161  -0.0312 0.0837  239 TYR A CG  
1863 C CD1 . TYR A 239 ? 0.5598 0.5563 0.6035 0.0147  -0.0393 0.0726  239 TYR A CD1 
1864 C CD2 . TYR A 239 ? 0.5695 0.6190 0.6276 0.0158  -0.0268 0.0953  239 TYR A CD2 
1865 C CE1 . TYR A 239 ? 0.5207 0.5023 0.5944 0.0112  -0.0398 0.0724  239 TYR A CE1 
1866 C CE2 . TYR A 239 ? 0.4856 0.5164 0.5703 0.0147  -0.0288 0.0950  239 TYR A CE2 
1867 C CZ  . TYR A 239 ? 0.6139 0.6131 0.7061 0.0115  -0.0339 0.0834  239 TYR A CZ  
1868 O OH  . TYR A 239 ? 0.5859 0.5765 0.7035 0.0057  -0.0319 0.0804  239 TYR A OH  
1869 N N   . GLU A 240 ? 0.6608 0.7561 0.6061 -0.0418 -0.0498 0.1192  240 GLU A N   
1870 C CA  . GLU A 240 ? 0.7016 0.8328 0.6109 -0.0664 -0.0447 0.1338  240 GLU A CA  
1871 C C   . GLU A 240 ? 0.6449 0.8358 0.5629 -0.0561 -0.0142 0.1225  240 GLU A C   
1872 O O   . GLU A 240 ? 0.6671 0.8644 0.6235 -0.0368 -0.0062 0.1179  240 GLU A O   
1873 C CB  . GLU A 240 ? 0.7247 0.8375 0.6362 -0.0925 -0.0665 0.1631  240 GLU A CB  
1874 C CG  . GLU A 240 ? 0.9125 0.9867 0.7850 -0.1155 -0.0978 0.1804  240 GLU A CG  
1875 C CD  . GLU A 240 ? 1.1440 1.2041 0.9991 -0.1479 -0.1171 0.2125  240 GLU A CD  
1876 O OE1 . GLU A 240 ? 1.1313 1.1882 0.9286 -0.1791 -0.1270 0.2318  240 GLU A OE1 
1877 O OE2 . GLU A 240 ? 1.0201 1.0696 0.9152 -0.1446 -0.1229 0.2184  240 GLU A OE2 
1878 N N   . PRO A 241 ? 0.8207 1.0605 0.7040 -0.0685 0.0023  0.1158  241 PRO A N   
1879 C CA  . PRO A 241 ? 0.7592 1.0687 0.6594 -0.0565 0.0304  0.0994  241 PRO A CA  
1880 C C   . PRO A 241 ? 0.7413 1.0753 0.6681 -0.0721 0.0315  0.1196  241 PRO A C   
1881 O O   . PRO A 241 ? 0.7440 1.0530 0.6590 -0.1039 0.0145  0.1480  241 PRO A O   
1882 C CB  . PRO A 241 ? 0.8239 1.1867 0.6772 -0.0779 0.0467  0.0892  241 PRO A CB  
1883 C CG  . PRO A 241 ? 0.7212 1.0311 0.5312 -0.0891 0.0269  0.0937  241 PRO A CG  
1884 C CD  . PRO A 241 ? 0.7002 0.9396 0.5268 -0.0948 -0.0043 0.1205  241 PRO A CD  
1885 N N   . LEU A 242 ? 0.7149 1.0948 0.6781 -0.0480 0.0482  0.1035  242 LEU A N   
1886 C CA  . LEU A 242 ? 0.8125 1.2244 0.8047 -0.0602 0.0503  0.1173  242 LEU A CA  
1887 C C   . LEU A 242 ? 0.7489 1.2509 0.7330 -0.0834 0.0730  0.1109  242 LEU A C   
1888 O O   . LEU A 242 ? 0.7052 1.2672 0.6990 -0.0599 0.0932  0.0800  242 LEU A O   
1889 C CB  . LEU A 242 ? 0.7576 1.1654 0.7944 -0.0212 0.0504  0.1051  242 LEU A CB  
1890 C CG  . LEU A 242 ? 0.7796 1.1860 0.8447 -0.0325 0.0416  0.1233  242 LEU A CG  
1891 C CD1 . LEU A 242 ? 0.6778 1.0106 0.7376 -0.0481 0.0191  0.1439  242 LEU A CD1 
1892 C CD2 . LEU A 242 ? 0.6396 1.0585 0.7399 0.0050  0.0440  0.1092  242 LEU A CD2 
1893 N N   . THR A 243 ? 0.8171 1.3292 0.7843 -0.1303 0.0689  0.1378  243 THR A N   
1894 C CA  . THR A 243 ? 0.9439 1.5456 0.9021 -0.1639 0.0919  0.1349  243 THR A CA  
1895 C C   . THR A 243 ? 0.8723 1.5302 0.8833 -0.1568 0.0996  0.1286  243 THR A C   
1896 O O   . THR A 243 ? 0.8552 1.4685 0.8949 -0.1438 0.0819  0.1399  243 THR A O   
1897 C CB  . THR A 243 ? 0.9875 1.5657 0.8924 -0.2259 0.0814  0.1708  243 THR A CB  
1898 O OG1 . THR A 243 ? 1.0562 1.6006 0.9793 -0.2474 0.0626  0.1975  243 THR A OG1 
1899 C CG2 . THR A 243 ? 0.8963 1.3914 0.7541 -0.2284 0.0588  0.1846  243 THR A CG2 
1900 N N   . GLN A 244 ? 0.9096 1.6732 0.9346 -0.1660 0.1263  0.1073  244 GLN A N   
1901 C CA  . GLN A 244 ? 0.8489 1.6772 0.9262 -0.1625 0.1320  0.0997  244 GLN A CA  
1902 C C   . GLN A 244 ? 0.8785 1.6727 0.9499 -0.2097 0.1158  0.1362  244 GLN A C   
1903 O O   . GLN A 244 ? 0.8842 1.6901 0.9975 -0.2002 0.1082  0.1360  244 GLN A O   
1904 C CB  . GLN A 244 ? 0.6940 1.6536 0.7900 -0.1708 0.1641  0.0679  244 GLN A CB  
1905 C CG  . GLN A 244 ? 0.7819 1.8225 0.9349 -0.1722 0.1692  0.0580  244 GLN A CG  
1906 C CD  . GLN A 244 ? 0.7836 1.7841 0.9823 -0.1163 0.1477  0.0518  244 GLN A CD  
1907 O OE1 . GLN A 244 ? 0.7722 1.7287 0.9754 -0.0633 0.1397  0.0361  244 GLN A OE1 
1908 N NE2 . GLN A 244 ? 0.7717 1.7849 0.9998 -0.1314 0.1372  0.0646  244 GLN A NE2 
1909 N N   . ASP A 245 ? 0.9004 1.6466 0.9178 -0.2600 0.1067  0.1672  245 ASP A N   
1910 C CA  . ASP A 245 ? 0.9006 1.5933 0.9091 -0.3018 0.0842  0.2019  245 ASP A CA  
1911 C C   . ASP A 245 ? 0.9138 1.5052 0.9381 -0.2695 0.0535  0.2116  245 ASP A C   
1912 O O   . ASP A 245 ? 0.8752 1.4441 0.9247 -0.2769 0.0384  0.2214  245 ASP A O   
1913 C CB  . ASP A 245 ? 1.0752 1.7378 1.0153 -0.3646 0.0783  0.2339  245 ASP A CB  
1914 C CG  . ASP A 245 ? 1.1922 1.7513 1.1138 -0.3925 0.0409  0.2709  245 ASP A CG  
1915 O OD1 . ASP A 245 ? 1.2455 1.8137 1.1850 -0.4211 0.0352  0.2807  245 ASP A OD1 
1916 O OD2 . ASP A 245 ? 1.2201 1.6880 1.1126 -0.3821 0.0145  0.2856  245 ASP A OD2 
1917 N N   . HIS A 246 ? 0.9324 1.4671 0.9433 -0.2354 0.0449  0.2059  246 HIS A N   
1918 C CA  . HIS A 246 ? 0.8694 1.3250 0.9019 -0.2031 0.0214  0.2077  246 HIS A CA  
1919 C C   . HIS A 246 ? 0.7381 1.2235 0.8225 -0.1693 0.0267  0.1900  246 HIS A C   
1920 O O   . HIS A 246 ? 0.7498 1.1863 0.8540 -0.1596 0.0090  0.1949  246 HIS A O   
1921 C CB  . HIS A 246 ? 0.8373 1.2479 0.8533 -0.1716 0.0175  0.1976  246 HIS A CB  
1922 C CG  . HIS A 246 ? 0.9416 1.2735 0.9219 -0.1915 -0.0095 0.2195  246 HIS A CG  
1923 N ND1 . HIS A 246 ? 0.8712 1.1691 0.8265 -0.1767 -0.0150 0.2135  246 HIS A ND1 
1924 C CD2 . HIS A 246 ? 0.9192 1.1975 0.8858 -0.2232 -0.0365 0.2457  246 HIS A CD2 
1925 C CE1 . HIS A 246 ? 0.8206 1.0520 0.7502 -0.1971 -0.0451 0.2354  246 HIS A CE1 
1926 N NE2 . HIS A 246 ? 0.8978 1.1128 0.8334 -0.2240 -0.0597 0.2554  246 HIS A NE2 
1927 N N   . VAL A 247 ? 0.6707 1.2377 0.7771 -0.1498 0.0493  0.1672  247 VAL A N   
1928 C CA  . VAL A 247 ? 0.7553 1.3522 0.9066 -0.1173 0.0499  0.1520  247 VAL A CA  
1929 C C   . VAL A 247 ? 0.6537 1.2758 0.8248 -0.1495 0.0435  0.1635  247 VAL A C   
1930 O O   . VAL A 247 ? 0.6478 1.2529 0.8446 -0.1335 0.0316  0.1619  247 VAL A O   
1931 C CB  . VAL A 247 ? 0.7011 1.3782 0.8736 -0.0837 0.0700  0.1218  247 VAL A CB  
1932 C CG1 . VAL A 247 ? 0.6799 1.4187 0.8981 -0.0686 0.0698  0.1098  247 VAL A CG1 
1933 C CG2 . VAL A 247 ? 0.6603 1.2902 0.8256 -0.0369 0.0675  0.1072  247 VAL A CG2 
1934 N N   . ASP A 248 ? 0.6654 1.3279 0.8213 -0.1991 0.0512  0.1749  248 ASP A N   
1935 C CA  . ASP A 248 ? 0.6286 1.3192 0.8038 -0.2345 0.0457  0.1840  248 ASP A CA  
1936 C C   . ASP A 248 ? 0.6950 1.2919 0.8649 -0.2454 0.0170  0.2031  248 ASP A C   
1937 O O   . ASP A 248 ? 0.7038 1.3074 0.9024 -0.2466 0.0076  0.1998  248 ASP A O   
1938 C CB  . ASP A 248 ? 0.6389 1.3858 0.7911 -0.2937 0.0603  0.1949  248 ASP A CB  
1939 C CG  . ASP A 248 ? 0.7883 1.6371 0.9467 -0.2835 0.0917  0.1693  248 ASP A CG  
1940 O OD1 . ASP A 248 ? 0.8356 1.7297 1.0333 -0.2304 0.0993  0.1399  248 ASP A OD1 
1941 O OD2 . ASP A 248 ? 0.7525 1.6225 0.8712 -0.3235 0.1042  0.1745  248 ASP A OD2 
1942 N N   . ILE A 249 ? 0.6790 1.1910 0.8146 -0.2512 0.0012  0.2195  249 ILE A N   
1943 C CA  . ILE A 249 ? 0.7140 1.1404 0.8506 -0.2574 -0.0281 0.2314  249 ILE A CA  
1944 C C   . ILE A 249 ? 0.6528 1.0665 0.8249 -0.2129 -0.0322 0.2123  249 ILE A C   
1945 O O   . ILE A 249 ? 0.6628 1.0414 0.8511 -0.2175 -0.0498 0.2118  249 ILE A O   
1946 C CB  . ILE A 249 ? 0.7935 1.1374 0.8918 -0.2652 -0.0475 0.2485  249 ILE A CB  
1947 C CG1 . ILE A 249 ? 0.8109 1.0718 0.9135 -0.2769 -0.0818 0.2590  249 ILE A CG1 
1948 C CG2 . ILE A 249 ? 0.6545 0.9816 0.7538 -0.2195 -0.0415 0.2335  249 ILE A CG2 
1949 C CD1 . ILE A 249 ? 0.8338 1.0125 0.9128 -0.2699 -0.1073 0.2686  249 ILE A CD1 
1950 N N   . LEU A 250 ? 0.5897 1.0295 0.7711 -0.1714 -0.0168 0.1956  250 LEU A N   
1951 C CA  . LEU A 250 ? 0.5631 0.9924 0.7682 -0.1335 -0.0192 0.1807  250 LEU A CA  
1952 C C   . LEU A 250 ? 0.4714 0.9654 0.7049 -0.1284 -0.0142 0.1705  250 LEU A C   
1953 O O   . LEU A 250 ? 0.4731 0.9644 0.7192 -0.0979 -0.0163 0.1599  250 LEU A O   
1954 C CB  . LEU A 250 ? 0.4916 0.9111 0.6886 -0.0946 -0.0090 0.1702  250 LEU A CB  
1955 C CG  . LEU A 250 ? 0.5105 0.8639 0.6850 -0.0923 -0.0165 0.1751  250 LEU A CG  
1956 C CD1 . LEU A 250 ? 0.4520 0.8081 0.6155 -0.0615 -0.0038 0.1638  250 LEU A CD1 
1957 C CD2 . LEU A 250 ? 0.5601 0.8555 0.7460 -0.0865 -0.0326 0.1728  250 LEU A CD2 
1958 N N   . GLY A 251 ? 0.5709 1.1240 0.8125 -0.1601 -0.0089 0.1739  251 GLY A N   
1959 C CA  . GLY A 251 ? 0.4607 1.0852 0.7339 -0.1566 -0.0061 0.1619  251 GLY A CA  
1960 C C   . GLY A 251 ? 0.5052 1.0993 0.7918 -0.1543 -0.0236 0.1590  251 GLY A C   
1961 O O   . GLY A 251 ? 0.4770 1.0909 0.7778 -0.1228 -0.0258 0.1470  251 GLY A O   
1962 N N   . PRO A 252 ? 0.5766 1.1192 0.8558 -0.1877 -0.0386 0.1690  252 PRO A N   
1963 C CA  . PRO A 252 ? 0.5261 1.0411 0.8183 -0.1863 -0.0549 0.1603  252 PRO A CA  
1964 C C   . PRO A 252 ? 0.4824 0.9665 0.7720 -0.1448 -0.0554 0.1492  252 PRO A C   
1965 O O   . PRO A 252 ? 0.5505 1.0542 0.8504 -0.1325 -0.0598 0.1378  252 PRO A O   
1966 C CB  . PRO A 252 ? 0.6274 1.0718 0.9080 -0.2204 -0.0732 0.1710  252 PRO A CB  
1967 C CG  . PRO A 252 ? 0.5598 1.0180 0.8218 -0.2551 -0.0672 0.1901  252 PRO A CG  
1968 C CD  . PRO A 252 ? 0.5312 1.0343 0.7869 -0.2278 -0.0445 0.1877  252 PRO A CD  
1969 N N   . LEU A 253 ? 0.5109 0.9480 0.7837 -0.1267 -0.0512 0.1525  253 LEU A N   
1970 C CA  . LEU A 253 ? 0.5573 0.9662 0.8243 -0.0944 -0.0493 0.1430  253 LEU A CA  
1971 C C   . LEU A 253 ? 0.5465 0.9996 0.8124 -0.0646 -0.0404 0.1395  253 LEU A C   
1972 O O   . LEU A 253 ? 0.4937 0.9394 0.7538 -0.0466 -0.0433 0.1334  253 LEU A O   
1973 C CB  . LEU A 253 ? 0.5575 0.9114 0.8100 -0.0859 -0.0475 0.1462  253 LEU A CB  
1974 C CG  . LEU A 253 ? 0.5208 0.8205 0.7769 -0.1056 -0.0635 0.1461  253 LEU A CG  
1975 C CD1 . LEU A 253 ? 0.3749 0.6328 0.6183 -0.0973 -0.0638 0.1503  253 LEU A CD1 
1976 C CD2 . LEU A 253 ? 0.5007 0.7811 0.7711 -0.1019 -0.0718 0.1280  253 LEU A CD2 
1977 N N   . SER A 254 ? 0.5022 1.0012 0.7720 -0.0590 -0.0310 0.1422  254 SER A N   
1978 C CA  . SER A 254 ? 0.4847 1.0241 0.7588 -0.0248 -0.0280 0.1353  254 SER A CA  
1979 C C   . SER A 254 ? 0.4321 1.0200 0.7242 -0.0241 -0.0385 0.1289  254 SER A C   
1980 O O   . SER A 254 ? 0.4927 1.0814 0.7784 0.0050  -0.0464 0.1257  254 SER A O   
1981 C CB  . SER A 254 ? 0.4698 1.0587 0.7516 -0.0184 -0.0154 0.1317  254 SER A CB  
1982 O OG  . SER A 254 ? 0.4852 1.1160 0.7788 0.0196  -0.0171 0.1202  254 SER A OG  
1983 N N   . ALA A 255 ? 0.4757 1.1005 0.7870 -0.0580 -0.0415 0.1281  255 ALA A N   
1984 C CA  . ALA A 255 ? 0.4329 1.1113 0.7643 -0.0603 -0.0529 0.1197  255 ALA A CA  
1985 C C   . ALA A 255 ? 0.5196 1.1529 0.8353 -0.0590 -0.0655 0.1172  255 ALA A C   
1986 O O   . ALA A 255 ? 0.4969 1.1533 0.8108 -0.0399 -0.0764 0.1119  255 ALA A O   
1987 C CB  . ALA A 255 ? 0.3352 1.0646 0.6906 -0.1033 -0.0520 0.1188  255 ALA A CB  
1988 N N   . GLN A 256 ? 0.5329 1.1044 0.8367 -0.0785 -0.0657 0.1188  256 GLN A N   
1989 C CA  . GLN A 256 ? 0.5000 1.0377 0.7915 -0.0794 -0.0744 0.1097  256 GLN A CA  
1990 C C   . GLN A 256 ? 0.5031 1.0163 0.7665 -0.0481 -0.0717 0.1113  256 GLN A C   
1991 O O   . GLN A 256 ? 0.4843 0.9919 0.7318 -0.0465 -0.0783 0.1041  256 GLN A O   
1992 C CB  . GLN A 256 ? 0.4764 0.9561 0.7681 -0.1010 -0.0761 0.1056  256 GLN A CB  
1993 C CG  . GLN A 256 ? 0.4946 0.9482 0.7793 -0.1027 -0.0825 0.0881  256 GLN A CG  
1994 C CD  . GLN A 256 ? 0.7233 1.1182 1.0112 -0.1092 -0.0832 0.0792  256 GLN A CD  
1995 O OE1 . GLN A 256 ? 0.7814 1.1495 1.0753 -0.1157 -0.0839 0.0893  256 GLN A OE1 
1996 N NE2 . GLN A 256 ? 0.7198 1.0981 1.0035 -0.1070 -0.0840 0.0583  256 GLN A NE2 
1997 N N   . THR A 257 ? 0.5722 1.0678 0.8246 -0.0263 -0.0626 0.1205  257 THR A N   
1998 C CA  . THR A 257 ? 0.5581 1.0209 0.7790 -0.0006 -0.0620 0.1253  257 THR A CA  
1999 C C   . THR A 257 ? 0.5157 1.0098 0.7332 0.0307  -0.0705 0.1306  257 THR A C   
2000 O O   . THR A 257 ? 0.5084 0.9719 0.6939 0.0503  -0.0775 0.1373  257 THR A O   
2001 C CB  . THR A 257 ? 0.4660 0.8747 0.6739 0.0034  -0.0496 0.1295  257 THR A CB  
2002 O OG1 . THR A 257 ? 0.5206 0.9440 0.7390 0.0160  -0.0442 0.1343  257 THR A OG1 
2003 C CG2 . THR A 257 ? 0.5705 0.9509 0.7896 -0.0220 -0.0457 0.1216  257 THR A CG2 
2004 N N   . GLY A 258 ? 0.5672 1.1208 0.8166 0.0353  -0.0714 0.1267  258 GLY A N   
2005 C CA  . GLY A 258 ? 0.4108 1.0007 0.6671 0.0712  -0.0817 0.1251  258 GLY A CA  
2006 C C   . GLY A 258 ? 0.5646 1.1131 0.8039 0.1009  -0.0769 0.1290  258 GLY A C   
2007 O O   . GLY A 258 ? 0.6686 1.2115 0.8974 0.1364  -0.0924 0.1299  258 GLY A O   
2008 N N   . ILE A 259 ? 0.5356 1.0504 0.7705 0.0881  -0.0596 0.1307  259 ILE A N   
2009 C CA  . ILE A 259 ? 0.5540 1.0278 0.7727 0.1125  -0.0545 0.1315  259 ILE A CA  
2010 C C   . ILE A 259 ? 0.5545 1.0701 0.7979 0.1079  -0.0396 0.1220  259 ILE A C   
2011 O O   . ILE A 259 ? 0.5103 1.0236 0.7571 0.0752  -0.0280 0.1251  259 ILE A O   
2012 C CB  . ILE A 259 ? 0.5411 0.9340 0.7256 0.1004  -0.0481 0.1407  259 ILE A CB  
2013 C CG1 . ILE A 259 ? 0.5105 0.8661 0.6622 0.1030  -0.0602 0.1497  259 ILE A CG1 
2014 C CG2 . ILE A 259 ? 0.4216 0.7742 0.5924 0.1199  -0.0423 0.1395  259 ILE A CG2 
2015 C CD1 . ILE A 259 ? 0.5981 0.8948 0.7236 0.0803  -0.0499 0.1540  259 ILE A CD1 
2016 N N   . ALA A 260 ? 0.5590 1.1127 0.8178 0.1405  -0.0416 0.1091  260 ALA A N   
2017 C CA  . ALA A 260 ? 0.5318 1.1362 0.8109 0.1356  -0.0246 0.0959  260 ALA A CA  
2018 C C   . ALA A 260 ? 0.5034 1.0479 0.7556 0.1199  -0.0114 0.1024  260 ALA A C   
2019 O O   . ALA A 260 ? 0.5568 1.0271 0.7813 0.1328  -0.0160 0.1085  260 ALA A O   
2020 C CB  . ALA A 260 ? 0.4083 1.0575 0.7086 0.1814  -0.0298 0.0740  260 ALA A CB  
2021 N N   . VAL A 261 ? 0.4728 1.0501 0.7310 0.0889  0.0036  0.1018  261 VAL A N   
2022 C CA  . VAL A 261 ? 0.4999 1.0240 0.7318 0.0724  0.0120  0.1086  261 VAL A CA  
2023 C C   . VAL A 261 ? 0.5183 1.0107 0.7352 0.1071  0.0139  0.0964  261 VAL A C   
2024 O O   . VAL A 261 ? 0.5124 0.9323 0.7046 0.1079  0.0112  0.1029  261 VAL A O   
2025 C CB  . VAL A 261 ? 0.5796 1.1475 0.8130 0.0339  0.0246  0.1114  261 VAL A CB  
2026 C CG1 . VAL A 261 ? 0.4156 0.9268 0.6181 0.0189  0.0279  0.1193  261 VAL A CG1 
2027 C CG2 . VAL A 261 ? 0.4749 1.0594 0.7204 -0.0027 0.0186  0.1243  261 VAL A CG2 
2028 N N   . LEU A 262 ? 0.4732 1.0208 0.7080 0.1368  0.0174  0.0751  262 LEU A N   
2029 C CA  . LEU A 262 ? 0.5880 1.1007 0.8096 0.1728  0.0162  0.0592  262 LEU A CA  
2030 C C   . LEU A 262 ? 0.5867 1.0212 0.7912 0.2007  -0.0033 0.0672  262 LEU A C   
2031 O O   . LEU A 262 ? 0.5995 0.9713 0.7810 0.2172  -0.0064 0.0628  262 LEU A O   
2032 C CB  . LEU A 262 ? 0.5045 1.0999 0.7554 0.2025  0.0227  0.0279  262 LEU A CB  
2033 C CG  . LEU A 262 ? 0.6962 1.3778 0.9581 0.1704  0.0464  0.0172  262 LEU A CG  
2034 C CD1 . LEU A 262 ? 0.5774 1.2097 0.7998 0.1357  0.0568  0.0311  262 LEU A CD1 
2035 C CD2 . LEU A 262 ? 0.6414 1.3918 0.9288 0.1375  0.0495  0.0274  262 LEU A CD2 
2036 N N   . ASP A 263 ? 0.5715 1.0063 0.7821 0.2027  -0.0171 0.0793  263 ASP A N   
2037 C CA  . ASP A 263 ? 0.6187 0.9726 0.8002 0.2171  -0.0345 0.0932  263 ASP A CA  
2038 C C   . ASP A 263 ? 0.6136 0.9002 0.7666 0.1839  -0.0270 0.1096  263 ASP A C   
2039 O O   . ASP A 263 ? 0.6063 0.8198 0.7301 0.1908  -0.0322 0.1144  263 ASP A O   
2040 C CB  . ASP A 263 ? 0.5659 0.9412 0.7548 0.2230  -0.0513 0.1023  263 ASP A CB  
2041 C CG  . ASP A 263 ? 0.7802 1.2130 0.9987 0.2655  -0.0666 0.0839  263 ASP A CG  
2042 O OD1 . ASP A 263 ? 0.8280 1.2526 1.0505 0.3003  -0.0702 0.0655  263 ASP A OD1 
2043 O OD2 . ASP A 263 ? 0.8177 1.3056 1.0581 0.2658  -0.0766 0.0844  263 ASP A OD2 
2044 N N   . MET A 264 ? 0.5560 0.8662 0.7189 0.1474  -0.0164 0.1164  264 MET A N   
2045 C CA  . MET A 264 ? 0.6144 0.8704 0.7600 0.1204  -0.0112 0.1254  264 MET A CA  
2046 C C   . MET A 264 ? 0.5709 0.7974 0.7046 0.1229  -0.0042 0.1175  264 MET A C   
2047 O O   . MET A 264 ? 0.5944 0.7638 0.7103 0.1137  -0.0042 0.1208  264 MET A O   
2048 C CB  . MET A 264 ? 0.4544 0.7382 0.6165 0.0862  -0.0072 0.1312  264 MET A CB  
2049 C CG  . MET A 264 ? 0.4668 0.7011 0.6201 0.0639  -0.0067 0.1359  264 MET A CG  
2050 S SD  . MET A 264 ? 0.5839 0.7828 0.7190 0.0662  -0.0119 0.1411  264 MET A SD  
2051 C CE  . MET A 264 ? 0.4567 0.6931 0.6129 0.0427  -0.0151 0.1408  264 MET A CE  
2052 N N   . CYS A 265 ? 0.5298 0.8000 0.6729 0.1333  0.0025  0.1044  265 CYS A N   
2053 C CA  . CYS A 265 ? 0.4879 0.7326 0.6155 0.1389  0.0079  0.0930  265 CYS A CA  
2054 C C   . CYS A 265 ? 0.6171 0.8017 0.7264 0.1687  -0.0011 0.0862  265 CYS A C   
2055 O O   . CYS A 265 ? 0.5512 0.6823 0.6408 0.1638  -0.0008 0.0836  265 CYS A O   
2056 C CB  . CYS A 265 ? 0.5847 0.8982 0.7233 0.1435  0.0191  0.0765  265 CYS A CB  
2057 S SG  . CYS A 265 ? 0.6592 1.0275 0.8046 0.0978  0.0289  0.0887  265 CYS A SG  
2058 N N   . ALA A 266 ? 0.5803 0.7699 0.6948 0.1994  -0.0125 0.0833  266 ALA A N   
2059 C CA  . ALA A 266 ? 0.6600 0.7781 0.7510 0.2269  -0.0272 0.0808  266 ALA A CA  
2060 C C   . ALA A 266 ? 0.6795 0.7217 0.7409 0.2008  -0.0297 0.1004  266 ALA A C   
2061 O O   . ALA A 266 ? 0.7829 0.7595 0.8204 0.2025  -0.0333 0.0975  266 ALA A O   
2062 C CB  . ALA A 266 ? 0.7053 0.8371 0.8052 0.2631  -0.0460 0.0791  266 ALA A CB  
2063 N N   . SER A 267 ? 0.6901 0.7444 0.7542 0.1743  -0.0270 0.1172  267 SER A N   
2064 C CA  . SER A 267 ? 0.7024 0.7016 0.7438 0.1456  -0.0248 0.1302  267 SER A CA  
2065 C C   . SER A 267 ? 0.7235 0.7096 0.7687 0.1235  -0.0136 0.1222  267 SER A C   
2066 O O   . SER A 267 ? 0.7684 0.6989 0.7935 0.1107  -0.0133 0.1234  267 SER A O   
2067 C CB  . SER A 267 ? 0.7087 0.7362 0.7572 0.1235  -0.0225 0.1421  267 SER A CB  
2068 O OG  . SER A 267 ? 0.9135 0.9521 0.9548 0.1431  -0.0362 0.1500  267 SER A OG  
2069 N N   . LEU A 268 ? 0.6333 0.6694 0.7020 0.1162  -0.0061 0.1149  268 LEU A N   
2070 C CA  . LEU A 268 ? 0.6862 0.7092 0.7563 0.0974  -0.0012 0.1082  268 LEU A CA  
2071 C C   . LEU A 268 ? 0.6723 0.6535 0.7226 0.1123  -0.0033 0.0956  268 LEU A C   
2072 O O   . LEU A 268 ? 0.5910 0.5306 0.6318 0.0968  -0.0036 0.0924  268 LEU A O   
2073 C CB  . LEU A 268 ? 0.6103 0.6868 0.6987 0.0866  0.0025  0.1067  268 LEU A CB  
2074 C CG  . LEU A 268 ? 0.5360 0.6004 0.6245 0.0663  0.0012  0.1032  268 LEU A CG  
2075 C CD1 . LEU A 268 ? 0.5323 0.5597 0.6261 0.0495  -0.0017 0.1039  268 LEU A CD1 
2076 C CD2 . LEU A 268 ? 0.5139 0.6194 0.6141 0.0490  -0.0007 0.1101  268 LEU A CD2 
2077 N N   . LYS A 269 ? 0.6466 0.6407 0.6936 0.1430  -0.0058 0.0844  269 LYS A N   
2078 C CA  . LYS A 269 ? 0.7152 0.6659 0.7436 0.1608  -0.0098 0.0674  269 LYS A CA  
2079 C C   . LYS A 269 ? 0.7659 0.6346 0.7692 0.1565  -0.0191 0.0753  269 LYS A C   
2080 O O   . LYS A 269 ? 0.7739 0.5971 0.7631 0.1439  -0.0197 0.0680  269 LYS A O   
2081 C CB  . LYS A 269 ? 0.7506 0.7326 0.7855 0.2002  -0.0127 0.0488  269 LYS A CB  
2082 C CG  . LYS A 269 ? 0.9023 0.8336 0.9190 0.2249  -0.0202 0.0262  269 LYS A CG  
2083 C CD  . LYS A 269 ? 0.8876 0.8318 0.9138 0.2725  -0.0308 0.0075  269 LYS A CD  
2084 C CE  . LYS A 269 ? 0.9138 0.9333 0.9578 0.2896  -0.0180 -0.0246 269 LYS A CE  
2085 N NZ  . LYS A 269 ? 0.9736 0.9670 1.0164 0.3363  -0.0303 -0.0586 269 LYS A NZ  
2086 N N   . GLU A 270 ? 0.7831 0.6318 0.7772 0.1624  -0.0272 0.0914  270 GLU A N   
2087 C CA  . GLU A 270 ? 0.9571 0.7235 0.9174 0.1515  -0.0364 0.1035  270 GLU A CA  
2088 C C   . GLU A 270 ? 0.8398 0.5950 0.7991 0.1067  -0.0245 0.1101  270 GLU A C   
2089 O O   . GLU A 270 ? 0.8935 0.5880 0.8300 0.0890  -0.0265 0.1099  270 GLU A O   
2090 C CB  . GLU A 270 ? 0.7900 0.5392 0.7331 0.1634  -0.0496 0.1228  270 GLU A CB  
2091 C CG  . GLU A 270 ? 0.9760 0.7732 0.9394 0.2056  -0.0598 0.1147  270 GLU A CG  
2092 C CD  . GLU A 270 ? 1.1698 0.9540 1.1375 0.2452  -0.0691 0.0891  270 GLU A CD  
2093 O OE1 . GLU A 270 ? 1.1825 0.8974 1.1267 0.2430  -0.0741 0.0820  270 GLU A OE1 
2094 O OE2 . GLU A 270 ? 1.0819 0.9297 1.0786 0.2774  -0.0709 0.0727  270 GLU A OE2 
2095 N N   . LEU A 271 ? 0.7540 0.5680 0.7404 0.0876  -0.0135 0.1133  271 LEU A N   
2096 C CA  . LEU A 271 ? 0.8484 0.6632 0.8448 0.0505  -0.0038 0.1120  271 LEU A CA  
2097 C C   . LEU A 271 ? 0.8239 0.6280 0.8275 0.0438  -0.0035 0.0950  271 LEU A C   
2098 O O   . LEU A 271 ? 0.7972 0.5763 0.7993 0.0171  -0.0002 0.0903  271 LEU A O   
2099 C CB  . LEU A 271 ? 0.7484 0.6257 0.7767 0.0383  0.0029  0.1138  271 LEU A CB  
2100 C CG  . LEU A 271 ? 0.7444 0.6308 0.7653 0.0285  0.0056  0.1269  271 LEU A CG  
2101 C CD1 . LEU A 271 ? 0.5508 0.4978 0.6060 0.0226  0.0090  0.1239  271 LEU A CD1 
2102 C CD2 . LEU A 271 ? 0.6361 0.4876 0.6373 -0.0032 0.0131  0.1295  271 LEU A CD2 
2103 N N   . LEU A 272 ? 0.8340 0.6619 0.8447 0.0655  -0.0065 0.0842  272 LEU A N   
2104 C CA  . LEU A 272 ? 0.7742 0.5931 0.7854 0.0601  -0.0084 0.0676  272 LEU A CA  
2105 C C   . LEU A 272 ? 0.8771 0.6269 0.8603 0.0627  -0.0143 0.0588  272 LEU A C   
2106 O O   . LEU A 272 ? 0.9552 0.6859 0.9379 0.0458  -0.0161 0.0462  272 LEU A O   
2107 C CB  . LEU A 272 ? 0.7634 0.6262 0.7791 0.0794  -0.0086 0.0584  272 LEU A CB  
2108 C CG  . LEU A 272 ? 0.7247 0.6470 0.7629 0.0686  -0.0062 0.0665  272 LEU A CG  
2109 C CD1 . LEU A 272 ? 0.7233 0.6848 0.7544 0.0811  -0.0043 0.0584  272 LEU A CD1 
2110 C CD2 . LEU A 272 ? 0.7766 0.6981 0.8316 0.0417  -0.0111 0.0659  272 LEU A CD2 
2111 N N   . GLN A 273 ? 0.9998 0.7081 0.9595 0.0839  -0.0208 0.0646  273 GLN A N   
2112 C CA  . GLN A 273 ? 1.0990 0.7303 1.0287 0.0909  -0.0314 0.0557  273 GLN A CA  
2113 C C   . GLN A 273 ? 1.1268 0.6928 1.0312 0.0596  -0.0336 0.0718  273 GLN A C   
2114 O O   . GLN A 273 ? 1.2236 0.7210 1.1035 0.0505  -0.0417 0.0647  273 GLN A O   
2115 C CB  . GLN A 273 ? 1.0832 0.6974 1.0009 0.1369  -0.0436 0.0489  273 GLN A CB  
2116 C CG  . GLN A 273 ? 1.1077 0.7623 1.0377 0.1644  -0.0417 0.0204  273 GLN A CG  
2117 C CD  . GLN A 273 ? 1.1280 0.8209 1.0692 0.2080  -0.0457 0.0123  273 GLN A CD  
2118 O OE1 . GLN A 273 ? 1.0600 0.7442 1.0001 0.2210  -0.0540 0.0290  273 GLN A OE1 
2119 N NE2 . GLN A 273 ? 1.2005 0.9418 1.1527 0.2296  -0.0399 -0.0155 273 GLN A NE2 
2120 N N   . ASN A 274 ? 1.1190 0.7045 1.0254 0.0395  -0.0262 0.0922  274 ASN A N   
2121 C CA  . ASN A 274 ? 1.1154 0.6478 0.9917 0.0029  -0.0246 0.1089  274 ASN A CA  
2122 C C   . ASN A 274 ? 1.1403 0.7245 1.0427 -0.0392 -0.0058 0.1081  274 ASN A C   
2123 O O   . ASN A 274 ? 1.2625 0.8203 1.1426 -0.0764 0.0013  0.1196  274 ASN A O   
2124 C CB  . ASN A 274 ? 1.1553 0.6539 0.9975 0.0166  -0.0354 0.1336  274 ASN A CB  
2125 C CG  . ASN A 274 ? 1.2717 0.7510 1.1080 0.0704  -0.0552 0.1285  274 ASN A CG  
2126 O OD1 . ASN A 274 ? 1.2874 0.7349 1.1223 0.0914  -0.0643 0.1092  274 ASN A OD1 
2127 N ND2 . ASN A 274 ? 1.2174 0.7222 1.0538 0.0941  -0.0624 0.1416  274 ASN A ND2 
2128 N N   . GLY A 275 ? 0.9651 0.7657 1.0541 -0.0799 0.1098  -0.0023 275 GLY A N   
2129 C CA  . GLY A 275 ? 0.9753 0.8497 1.0957 -0.0928 0.1031  0.0103  275 GLY A CA  
2130 C C   . GLY A 275 ? 1.0178 0.9235 1.1493 -0.0743 0.1188  0.0415  275 GLY A C   
2131 O O   . GLY A 275 ? 0.8841 0.7655 0.9977 -0.0495 0.1298  0.0538  275 GLY A O   
2132 N N   . MET A 276 ? 1.1114 1.0767 1.2730 -0.0868 0.1198  0.0540  276 MET A N   
2133 C CA  . MET A 276 ? 1.1194 1.1196 1.2853 -0.0723 0.1351  0.0792  276 MET A CA  
2134 C C   . MET A 276 ? 1.1544 1.1587 1.3420 -0.0962 0.1497  0.1056  276 MET A C   
2135 O O   . MET A 276 ? 1.1261 1.1470 1.3062 -0.0857 0.1644  0.1293  276 MET A O   
2136 C CB  . MET A 276 ? 1.0008 1.0688 1.1781 -0.0598 0.1304  0.0727  276 MET A CB  
2137 C CG  . MET A 276 ? 0.9558 1.0212 1.1118 -0.0398 0.1145  0.0522  276 MET A CG  
2138 S SD  . MET A 276 ? 1.0136 1.1280 1.1657 -0.0131 0.1132  0.0523  276 MET A SD  
2139 C CE  . MET A 276 ? 0.9171 1.0498 1.0696 -0.0106 0.1373  0.0760  276 MET A CE  
2140 N N   . ASN A 277 ? 1.1802 1.1711 1.3915 -0.1313 0.1451  0.1034  277 ASN A N   
2141 C CA  . ASN A 277 ? 1.2708 1.2607 1.5036 -0.1609 0.1586  0.1321  277 ASN A CA  
2142 C C   . ASN A 277 ? 1.1897 1.2646 1.4447 -0.1602 0.1741  0.1509  277 ASN A C   
2143 O O   . ASN A 277 ? 1.2452 1.3262 1.4899 -0.1572 0.1922  0.1794  277 ASN A O   
2144 C CB  . ASN A 277 ? 1.3596 1.2766 1.5666 -0.1530 0.1688  0.1549  277 ASN A CB  
2145 C CG  . ASN A 277 ? 1.4723 1.3000 1.6622 -0.1549 0.1583  0.1354  277 ASN A CG  
2146 O OD1 . ASN A 277 ? 1.4622 1.2815 1.6531 -0.1667 0.1430  0.1032  277 ASN A OD1 
2147 N ND2 . ASN A 277 ? 1.5240 1.2842 1.6962 -0.1419 0.1666  0.1546  277 ASN A ND2 
2148 N N   . GLY A 278 ? 1.1359 1.2779 1.4200 -0.1611 0.1670  0.1343  278 GLY A N   
2149 C CA  . GLY A 278 ? 1.1310 1.3573 1.4422 -0.1585 0.1842  0.1468  278 GLY A CA  
2150 C C   . GLY A 278 ? 1.0770 1.3194 1.3551 -0.1200 0.1965  0.1478  278 GLY A C   
2151 O O   . GLY A 278 ? 1.0218 1.3302 1.3139 -0.1094 0.2116  0.1496  278 GLY A O   
2152 N N   . ARG A 279 ? 1.0713 1.2548 1.3057 -0.0994 0.1905  0.1457  279 ARG A N   
2153 C CA  . ARG A 279 ? 1.0094 1.2036 1.2094 -0.0674 0.1962  0.1444  279 ARG A CA  
2154 C C   . ARG A 279 ? 0.8510 1.0652 1.0521 -0.0442 0.1815  0.1156  279 ARG A C   
2155 O O   . ARG A 279 ? 0.8557 1.0654 1.0757 -0.0498 0.1640  0.0987  279 ARG A O   
2156 C CB  . ARG A 279 ? 1.0041 1.1383 1.1646 -0.0556 0.1933  0.1568  279 ARG A CB  
2157 C CG  . ARG A 279 ? 1.1082 1.1992 1.2710 -0.0774 0.2003  0.1847  279 ARG A CG  
2158 C CD  . ARG A 279 ? 1.0872 1.1384 1.2149 -0.0592 0.2012  0.2059  279 ARG A CD  
2159 N NE  . ARG A 279 ? 1.1114 1.2047 1.2114 -0.0425 0.2078  0.2134  279 ARG A NE  
2160 C CZ  . ARG A 279 ? 1.1820 1.2745 1.2562 -0.0409 0.2156  0.2451  279 ARG A CZ  
2161 N NH1 . ARG A 279 ? 1.1995 1.2499 1.2757 -0.0518 0.2183  0.2768  279 ARG A NH1 
2162 N NH2 . ARG A 279 ? 1.0886 1.2202 1.1317 -0.0287 0.2193  0.2453  279 ARG A NH2 
2163 N N   . THR A 280 ? 0.7520 0.9854 0.9291 -0.0198 0.1873  0.1111  280 THR A N   
2164 C CA  . THR A 280 ? 0.6835 0.9311 0.8603 0.0029  0.1746  0.0875  280 THR A CA  
2165 C C   . THR A 280 ? 0.6561 0.8702 0.7861 0.0228  0.1674  0.0836  280 THR A C   
2166 O O   . THR A 280 ? 0.6475 0.8479 0.7472 0.0229  0.1761  0.0989  280 THR A O   
2167 C CB  . THR A 280 ? 0.6090 0.9172 0.8094 0.0140  0.1890  0.0804  280 THR A CB  
2168 O OG1 . THR A 280 ? 0.6496 0.9680 0.8176 0.0210  0.2103  0.0888  280 THR A OG1 
2169 C CG2 . THR A 280 ? 0.6774 1.0344 0.9329 -0.0081 0.1967  0.0879  280 THR A CG2 
2170 N N   . ILE A 281 ? 0.5717 0.7763 0.6974 0.0372  0.1494  0.0659  281 ILE A N   
2171 C CA  . ILE A 281 ? 0.5529 0.7324 0.6397 0.0528  0.1399  0.0609  281 ILE A CA  
2172 C C   . ILE A 281 ? 0.6028 0.7984 0.6913 0.0710  0.1358  0.0434  281 ILE A C   
2173 O O   . ILE A 281 ? 0.5033 0.7081 0.6181 0.0760  0.1233  0.0334  281 ILE A O   
2174 C CB  . ILE A 281 ? 0.5140 0.6587 0.5903 0.0516  0.1219  0.0592  281 ILE A CB  
2175 C CG1 . ILE A 281 ? 0.5462 0.6679 0.6238 0.0390  0.1279  0.0731  281 ILE A CG1 
2176 C CG2 . ILE A 281 ? 0.4782 0.6060 0.5198 0.0629  0.1121  0.0579  281 ILE A CG2 
2177 C CD1 . ILE A 281 ? 0.4518 0.5419 0.5148 0.0429  0.1165  0.0700  281 ILE A CD1 
2178 N N   . LEU A 282 ? 0.5512 0.7473 0.6096 0.0812  0.1451  0.0395  282 LEU A N   
2179 C CA  . LEU A 282 ? 0.5605 0.7611 0.6161 0.1018  0.1442  0.0198  282 LEU A CA  
2180 C C   . LEU A 282 ? 0.5780 0.8225 0.6850 0.1103  0.1531  0.0133  282 LEU A C   
2181 O O   . LEU A 282 ? 0.4894 0.7354 0.6176 0.1271  0.1407  0.0019  282 LEU A O   
2182 C CB  . LEU A 282 ? 0.5522 0.7143 0.5914 0.1091  0.1187  0.0119  282 LEU A CB  
2183 C CG  . LEU A 282 ? 0.6193 0.7474 0.6083 0.1043  0.1107  0.0140  282 LEU A CG  
2184 C CD1 . LEU A 282 ? 0.5317 0.6278 0.5118 0.1040  0.0857  0.0130  282 LEU A CD1 
2185 C CD2 . LEU A 282 ? 0.5830 0.7071 0.5395 0.1144  0.1221  -0.0011 282 LEU A CD2 
2186 N N   . GLY A 283 ? 0.5672 0.8511 0.6975 0.0976  0.1739  0.0245  283 GLY A N   
2187 C CA  . GLY A 283 ? 0.4863 0.8268 0.6720 0.1020  0.1850  0.0221  283 GLY A CA  
2188 C C   . GLY A 283 ? 0.5096 0.8620 0.7411 0.0921  0.1637  0.0252  283 GLY A C   
2189 O O   . GLY A 283 ? 0.5088 0.9138 0.7922 0.0987  0.1664  0.0230  283 GLY A O   
2190 N N   . SER A 284 ? 0.5897 0.8997 0.8034 0.0768  0.1429  0.0298  284 SER A N   
2191 C CA  . SER A 284 ? 0.5270 0.8425 0.7709 0.0644  0.1205  0.0297  284 SER A CA  
2192 C C   . SER A 284 ? 0.5361 0.8320 0.7772 0.0331  0.1206  0.0398  284 SER A C   
2193 O O   . SER A 284 ? 0.5397 0.7932 0.7430 0.0285  0.1257  0.0459  284 SER A O   
2194 C CB  . SER A 284 ? 0.5087 0.7866 0.7281 0.0767  0.0944  0.0217  284 SER A CB  
2195 O OG  . SER A 284 ? 0.5149 0.7959 0.7513 0.0610  0.0725  0.0218  284 SER A OG  
2196 N N   . ALA A 285 ? 0.4823 0.8082 0.7650 0.0120  0.1133  0.0418  285 ALA A N   
2197 C CA  . ALA A 285 ? 0.5423 0.8396 0.8224 -0.0199 0.1101  0.0470  285 ALA A CA  
2198 C C   . ALA A 285 ? 0.5237 0.7804 0.7813 -0.0258 0.0847  0.0345  285 ALA A C   
2199 O O   . ALA A 285 ? 0.7143 0.9342 0.9611 -0.0488 0.0818  0.0330  285 ALA A O   
2200 C CB  . ALA A 285 ? 0.4428 0.7911 0.7765 -0.0478 0.1145  0.0552  285 ALA A CB  
2201 N N   . LEU A 286 ? 0.4877 0.7476 0.7354 -0.0060 0.0672  0.0257  286 LEU A N   
2202 C CA  . LEU A 286 ? 0.4609 0.6863 0.6777 -0.0093 0.0456  0.0156  286 LEU A CA  
2203 C C   . LEU A 286 ? 0.4984 0.6867 0.6707 0.0125  0.0481  0.0157  286 LEU A C   
2204 O O   . LEU A 286 ? 0.5292 0.7222 0.6968 0.0313  0.0591  0.0209  286 LEU A O   
2205 C CB  . LEU A 286 ? 0.5030 0.7657 0.7430 -0.0084 0.0190  0.0113  286 LEU A CB  
2206 C CG  . LEU A 286 ? 0.6163 0.9288 0.9060 -0.0328 0.0081  0.0120  286 LEU A CG  
2207 C CD1 . LEU A 286 ? 0.5253 0.8731 0.8309 -0.0275 -0.0231 0.0113  286 LEU A CD1 
2208 C CD2 . LEU A 286 ? 0.6403 0.9182 0.9155 -0.0685 0.0072  0.0044  286 LEU A CD2 
2209 N N   . LEU A 287 ? 0.4584 0.6124 0.5967 0.0081  0.0378  0.0089  287 LEU A N   
2210 C CA  . LEU A 287 ? 0.5053 0.6348 0.6065 0.0246  0.0368  0.0111  287 LEU A CA  
2211 C C   . LEU A 287 ? 0.5873 0.7332 0.6882 0.0357  0.0160  0.0118  287 LEU A C   
2212 O O   . LEU A 287 ? 0.4845 0.6398 0.5851 0.0269  -0.0036 0.0075  287 LEU A O   
2213 C CB  . LEU A 287 ? 0.4881 0.5821 0.5561 0.0176  0.0383  0.0045  287 LEU A CB  
2214 C CG  . LEU A 287 ? 0.4973 0.5648 0.5676 0.0096  0.0572  0.0051  287 LEU A CG  
2215 C CD1 . LEU A 287 ? 0.5164 0.5471 0.5589 0.0041  0.0581  -0.0084 287 LEU A CD1 
2216 C CD2 . LEU A 287 ? 0.6184 0.6809 0.6842 0.0242  0.0741  0.0209  287 LEU A CD2 
2217 N N   . GLU A 288 ? 0.5182 0.6643 0.6168 0.0541  0.0188  0.0177  288 GLU A N   
2218 C CA  . GLU A 288 ? 0.4329 0.5848 0.5339 0.0675  -0.0006 0.0207  288 GLU A CA  
2219 C C   . GLU A 288 ? 0.4964 0.6209 0.5570 0.0651  -0.0136 0.0259  288 GLU A C   
2220 O O   . GLU A 288 ? 0.4840 0.5872 0.5173 0.0634  -0.0031 0.0287  288 GLU A O   
2221 C CB  . GLU A 288 ? 0.5174 0.6702 0.6283 0.0881  0.0086  0.0209  288 GLU A CB  
2222 C CG  . GLU A 288 ? 0.5988 0.7882 0.7496 0.0926  0.0257  0.0170  288 GLU A CG  
2223 C CD  . GLU A 288 ? 0.7598 0.9910 0.9571 0.1003  0.0120  0.0174  288 GLU A CD  
2224 O OE1 . GLU A 288 ? 0.7682 1.0317 0.9940 0.0822  0.0090  0.0181  288 GLU A OE1 
2225 O OE2 . GLU A 288 ? 0.8319 1.0626 1.0387 0.1240  0.0026  0.0177  288 GLU A OE2 
2226 N N   . ASP A 289 ? 0.4771 0.6082 0.5355 0.0643  -0.0373 0.0305  289 ASP A N   
2227 C CA  . ASP A 289 ? 0.4736 0.5850 0.4920 0.0581  -0.0492 0.0389  289 ASP A CA  
2228 C C   . ASP A 289 ? 0.5206 0.6225 0.5374 0.0696  -0.0710 0.0530  289 ASP A C   
2229 O O   . ASP A 289 ? 0.4862 0.5797 0.4740 0.0613  -0.0869 0.0650  289 ASP A O   
2230 C CB  . ASP A 289 ? 0.4869 0.6080 0.4866 0.0400  -0.0572 0.0332  289 ASP A CB  
2231 C CG  . ASP A 289 ? 0.5968 0.7428 0.6099 0.0368  -0.0851 0.0379  289 ASP A CG  
2232 O OD1 . ASP A 289 ? 0.6222 0.7910 0.6789 0.0476  -0.0920 0.0399  289 ASP A OD1 
2233 O OD2 . ASP A 289 ? 0.6316 0.7795 0.6114 0.0234  -0.0998 0.0401  289 ASP A OD2 
2234 N N   . GLU A 290 ? 0.4658 0.5658 0.5109 0.0894  -0.0708 0.0525  290 GLU A N   
2235 C CA  . GLU A 290 ? 0.4952 0.5755 0.5418 0.1048  -0.0916 0.0652  290 GLU A CA  
2236 C C   . GLU A 290 ? 0.5447 0.5815 0.5732 0.1139  -0.0841 0.0641  290 GLU A C   
2237 O O   . GLU A 290 ? 0.5412 0.5518 0.5771 0.1325  -0.0961 0.0684  290 GLU A O   
2238 C CB  . GLU A 290 ? 0.5012 0.6126 0.5978 0.1252  -0.1015 0.0648  290 GLU A CB  
2239 C CG  . GLU A 290 ? 0.5000 0.6546 0.6123 0.1119  -0.1194 0.0698  290 GLU A CG  
2240 C CD  . GLU A 290 ? 0.7300 0.9054 0.8754 0.1304  -0.1481 0.0860  290 GLU A CD  
2241 O OE1 . GLU A 290 ? 0.5661 0.7297 0.7390 0.1606  -0.1472 0.0880  290 GLU A OE1 
2242 O OE2 . GLU A 290 ? 0.5656 0.7685 0.7079 0.1158  -0.1721 0.0963  290 GLU A OE2 
2243 N N   . PHE A 291 ? 0.4929 0.5197 0.4976 0.1013  -0.0660 0.0584  291 PHE A N   
2244 C CA  . PHE A 291 ? 0.5460 0.5336 0.5255 0.1009  -0.0633 0.0584  291 PHE A CA  
2245 C C   . PHE A 291 ? 0.5718 0.5516 0.5171 0.0771  -0.0675 0.0728  291 PHE A C   
2246 O O   . PHE A 291 ? 0.5338 0.5387 0.4743 0.0659  -0.0535 0.0716  291 PHE A O   
2247 C CB  . PHE A 291 ? 0.5969 0.5899 0.5801 0.1063  -0.0395 0.0421  291 PHE A CB  
2248 C CG  . PHE A 291 ? 0.5006 0.5090 0.5170 0.1296  -0.0295 0.0279  291 PHE A CG  
2249 C CD1 . PHE A 291 ? 0.5697 0.5470 0.5871 0.1511  -0.0334 0.0194  291 PHE A CD1 
2250 C CD2 . PHE A 291 ? 0.5321 0.5856 0.5792 0.1298  -0.0144 0.0227  291 PHE A CD2 
2251 C CE1 . PHE A 291 ? 0.6514 0.6511 0.7026 0.1766  -0.0196 0.0053  291 PHE A CE1 
2252 C CE2 . PHE A 291 ? 0.5520 0.6315 0.6347 0.1496  -0.0025 0.0123  291 PHE A CE2 
2253 C CZ  . PHE A 291 ? 0.6376 0.6945 0.7235 0.1751  -0.0035 0.0032  291 PHE A CZ  
2254 N N   . THR A 292 ? 0.5615 0.5065 0.4853 0.0700  -0.0855 0.0874  292 THR A N   
2255 C CA  . THR A 292 ? 0.6032 0.5478 0.4981 0.0451  -0.0884 0.1042  292 THR A CA  
2256 C C   . THR A 292 ? 0.6499 0.5875 0.5332 0.0353  -0.0771 0.0994  292 THR A C   
2257 O O   . THR A 292 ? 0.5525 0.4741 0.4404 0.0466  -0.0705 0.0831  292 THR A O   
2258 C CB  . THR A 292 ? 0.6014 0.5111 0.4778 0.0359  -0.1135 0.1265  292 THR A CB  
2259 O OG1 . THR A 292 ? 0.6777 0.5335 0.5499 0.0425  -0.1226 0.1217  292 THR A OG1 
2260 C CG2 . THR A 292 ? 0.6139 0.5321 0.5012 0.0469  -0.1296 0.1352  292 THR A CG2 
2261 N N   . PRO A 293 ? 0.6788 0.6338 0.5464 0.0136  -0.0748 0.1143  293 PRO A N   
2262 C CA  . PRO A 293 ? 0.6059 0.5571 0.4632 0.0002  -0.0715 0.1151  293 PRO A CA  
2263 C C   . PRO A 293 ? 0.6832 0.5777 0.5236 -0.0051 -0.0892 0.1118  293 PRO A C   
2264 O O   . PRO A 293 ? 0.7082 0.5901 0.5399 -0.0064 -0.0856 0.0985  293 PRO A O   
2265 C CB  . PRO A 293 ? 0.6440 0.6300 0.4937 -0.0224 -0.0700 0.1375  293 PRO A CB  
2266 C CG  . PRO A 293 ? 0.7305 0.7470 0.5867 -0.0134 -0.0600 0.1377  293 PRO A CG  
2267 C CD  . PRO A 293 ? 0.5885 0.5769 0.4485 0.0014  -0.0724 0.1296  293 PRO A CD  
2268 N N   . PHE A 294 ? 0.7268 0.5821 0.5584 -0.0082 -0.1090 0.1234  294 PHE A N   
2269 C CA  . PHE A 294 ? 0.7715 0.5584 0.5848 -0.0118 -0.1265 0.1187  294 PHE A CA  
2270 C C   . PHE A 294 ? 0.8514 0.6112 0.6737 0.0204  -0.1186 0.0886  294 PHE A C   
2271 O O   . PHE A 294 ? 0.8096 0.5285 0.6122 0.0190  -0.1200 0.0707  294 PHE A O   
2272 C CB  . PHE A 294 ? 0.7516 0.4986 0.5556 -0.0204 -0.1501 0.1427  294 PHE A CB  
2273 C CG  . PHE A 294 ? 0.9279 0.5894 0.7165 -0.0158 -0.1688 0.1357  294 PHE A CG  
2274 C CD1 . PHE A 294 ? 0.9550 0.5716 0.7153 -0.0469 -0.1815 0.1387  294 PHE A CD1 
2275 C CD2 . PHE A 294 ? 0.9579 0.5829 0.7616 0.0196  -0.1746 0.1263  294 PHE A CD2 
2276 C CE1 . PHE A 294 ? 1.0276 0.5525 0.7685 -0.0432 -0.1990 0.1284  294 PHE A CE1 
2277 C CE2 . PHE A 294 ? 1.0130 0.5514 0.8026 0.0293  -0.1900 0.1177  294 PHE A CE2 
2278 C CZ  . PHE A 294 ? 1.1004 0.5826 0.8553 -0.0025 -0.2020 0.1169  294 PHE A CZ  
2279 N N   . ASP A 295 ? 0.7587 0.5447 0.6098 0.0482  -0.1098 0.0817  295 ASP A N   
2280 C CA  . ASP A 295 ? 0.7547 0.5319 0.6215 0.0795  -0.0973 0.0549  295 ASP A CA  
2281 C C   . ASP A 295 ? 0.7611 0.5602 0.6181 0.0758  -0.0763 0.0363  295 ASP A C   
2282 O O   . ASP A 295 ? 0.7419 0.5134 0.5877 0.0898  -0.0686 0.0129  295 ASP A O   
2283 C CB  . ASP A 295 ? 0.6857 0.5053 0.5918 0.1030  -0.0915 0.0552  295 ASP A CB  
2284 C CG  . ASP A 295 ? 0.8177 0.6184 0.7331 0.1098  -0.1155 0.0752  295 ASP A CG  
2285 O OD1 . ASP A 295 ? 0.9583 0.6981 0.8637 0.1187  -0.1316 0.0775  295 ASP A OD1 
2286 O OD2 . ASP A 295 ? 0.7272 0.5705 0.6566 0.1055  -0.1196 0.0890  295 ASP A OD2 
2287 N N   . VAL A 296 ? 0.7043 0.5524 0.5632 0.0586  -0.0662 0.0467  296 VAL A N   
2288 C CA  . VAL A 296 ? 0.7123 0.5845 0.5629 0.0552  -0.0487 0.0357  296 VAL A CA  
2289 C C   . VAL A 296 ? 0.7975 0.6321 0.6098 0.0364  -0.0593 0.0298  296 VAL A C   
2290 O O   . VAL A 296 ? 0.7407 0.5608 0.5342 0.0435  -0.0507 0.0085  296 VAL A O   
2291 C CB  . VAL A 296 ? 0.6853 0.6118 0.5491 0.0441  -0.0378 0.0514  296 VAL A CB  
2292 C CG1 . VAL A 296 ? 0.6645 0.6117 0.5164 0.0376  -0.0256 0.0483  296 VAL A CG1 
2293 C CG2 . VAL A 296 ? 0.5897 0.5465 0.4854 0.0602  -0.0265 0.0499  296 VAL A CG2 
2294 N N   . VAL A 297 ? 0.7693 0.5897 0.5673 0.0092  -0.0783 0.0487  297 VAL A N   
2295 C CA  . VAL A 297 ? 0.8686 0.6546 0.6307 -0.0167 -0.0931 0.0451  297 VAL A CA  
2296 C C   . VAL A 297 ? 0.9247 0.6345 0.6614 -0.0044 -0.1007 0.0184  297 VAL A C   
2297 O O   . VAL A 297 ? 0.9891 0.6696 0.6901 -0.0152 -0.1038 -0.0010 297 VAL A O   
2298 C CB  . VAL A 297 ? 0.8922 0.6818 0.6508 -0.0510 -0.1125 0.0744  297 VAL A CB  
2299 C CG1 . VAL A 297 ? 0.9602 0.6945 0.6816 -0.0815 -0.1350 0.0698  297 VAL A CG1 
2300 C CG2 . VAL A 297 ? 0.8072 0.6743 0.5854 -0.0626 -0.1018 0.0953  297 VAL A CG2 
2301 N N   . ARG A 298 ? 0.9528 0.6288 0.7059 0.0196  -0.1044 0.0163  298 ARG A N   
2302 C CA  . ARG A 298 ? 0.9789 0.5754 0.7121 0.0371  -0.1117 -0.0079 298 ARG A CA  
2303 C C   . ARG A 298 ? 0.9654 0.5668 0.6960 0.0691  -0.0871 -0.0428 298 ARG A C   
2304 O O   . ARG A 298 ? 1.0371 0.5736 0.7380 0.0806  -0.0882 -0.0713 298 ARG A O   
2305 C CB  . ARG A 298 ? 1.0315 0.5965 0.7893 0.0568  -0.1246 0.0064  298 ARG A CB  
2306 C CG  . ARG A 298 ? 1.0619 0.5922 0.8347 0.1032  -0.1154 -0.0191 298 ARG A CG  
2307 C CD  . ARG A 298 ? 1.0711 0.5602 0.8644 0.1195  -0.1362 0.0010  298 ARG A CD  
2308 N NE  . ARG A 298 ? 1.2302 0.6759 1.0388 0.1666  -0.1302 -0.0228 298 ARG A NE  
2309 C CZ  . ARG A 298 ? 1.1409 0.6350 0.9986 0.2054  -0.1181 -0.0237 298 ARG A CZ  
2310 N NH1 . ARG A 298 ? 1.0939 0.6742 0.9846 0.1999  -0.1116 -0.0053 298 ARG A NH1 
2311 N NH2 . ARG A 298 ? 1.0679 0.5233 0.9429 0.2510  -0.1123 -0.0444 298 ARG A NH2 
2312 N N   . GLN A 299 ? 0.9452 0.6196 0.7040 0.0828  -0.0640 -0.0417 299 GLN A N   
2313 C CA  . GLN A 299 ? 0.9188 0.6098 0.6791 0.1112  -0.0375 -0.0698 299 GLN A CA  
2314 C C   . GLN A 299 ? 0.9140 0.6367 0.6426 0.0927  -0.0246 -0.0773 299 GLN A C   
2315 O O   . GLN A 299 ? 1.0312 0.7374 0.7290 0.1039  -0.0102 -0.1062 299 GLN A O   
2316 C CB  . GLN A 299 ? 0.7940 0.5455 0.6096 0.1374  -0.0204 -0.0618 299 GLN A CB  
2317 C CG  . GLN A 299 ? 0.8327 0.5756 0.6698 0.1790  -0.0046 -0.0855 299 GLN A CG  
2318 C CD  . GLN A 299 ? 0.8507 0.6618 0.7475 0.1980  0.0081  -0.0739 299 GLN A CD  
2319 O OE1 . GLN A 299 ? 0.8146 0.6354 0.7424 0.1983  -0.0087 -0.0527 299 GLN A OE1 
2320 N NE2 . GLN A 299 ? 0.8076 0.6680 0.7183 0.2109  0.0369  -0.0868 299 GLN A NE2 
2321 N N   . CYS A 300 ? 0.8841 0.6539 0.6189 0.0666  -0.0288 -0.0513 300 CYS A N   
2322 C CA  . CYS A 300 ? 0.9193 0.7290 0.6327 0.0526  -0.0176 -0.0505 300 CYS A CA  
2323 C C   . CYS A 300 ? 1.0193 0.7938 0.6789 0.0225  -0.0367 -0.0582 300 CYS A C   
2324 O O   . CYS A 300 ? 1.0236 0.7577 0.6720 0.0013  -0.0615 -0.0513 300 CYS A O   
2325 C CB  . CYS A 300 ? 0.9001 0.7723 0.6465 0.0420  -0.0142 -0.0189 300 CYS A CB  
2326 S SG  . CYS A 300 ? 0.7860 0.7026 0.5858 0.0700  0.0098  -0.0147 300 CYS A SG  
2327 N N   . SER A 301 ? 1.0615 0.8526 0.6853 0.0175  -0.0262 -0.0712 301 SER A N   
2328 C CA  . SER A 301 ? 1.0871 0.8550 0.6562 -0.0158 -0.0466 -0.0780 301 SER A CA  
2329 C C   . SER A 301 ? 1.1335 0.9319 0.7199 -0.0491 -0.0705 -0.0420 301 SER A C   
2330 O O   . SER A 301 ? 0.9832 0.8342 0.6171 -0.0436 -0.0639 -0.0129 301 SER A O   
2331 C CB  . SER A 301 ? 1.1288 0.9306 0.6599 -0.0175 -0.0314 -0.0883 301 SER A CB  
2332 O OG  . SER A 301 ? 1.1951 0.9922 0.6767 -0.0552 -0.0555 -0.0872 301 SER A OG  
2333 N N   . GLY A 302 ? 1.1954 0.9602 0.7434 -0.0844 -0.0979 -0.0454 302 GLY A N   
2334 C CA  . GLY A 302 ? 1.2391 1.0484 0.8039 -0.1192 -0.1195 -0.0100 302 GLY A CA  
2335 C C   . GLY A 302 ? 1.2221 1.1057 0.7861 -0.1290 -0.1173 0.0096  302 GLY A C   
2336 O O   . GLY A 302 ? 1.2857 1.2214 0.8747 -0.1514 -0.1319 0.0426  302 GLY A O   
2337 N N   . VAL A 303 ? 1.2869 1.1802 0.8247 -0.1117 -0.0988 -0.0071 303 VAL A N   
2338 C CA  . VAL A 303 ? 1.3100 1.2695 0.8423 -0.1185 -0.0968 0.0143  303 VAL A CA  
2339 C C   . VAL A 303 ? 1.2541 1.2464 0.8186 -0.0823 -0.0636 0.0215  303 VAL A C   
2340 O O   . VAL A 303 ? 1.2476 1.2107 0.8007 -0.0584 -0.0415 -0.0058 303 VAL A O   
2341 C CB  . VAL A 303 ? 1.3556 1.2975 0.8131 -0.1406 -0.1088 -0.0092 303 VAL A CB  
2342 C CG1 . VAL A 303 ? 1.2655 1.2763 0.7152 -0.1410 -0.1031 0.0152  303 VAL A CG1 
2343 C CG2 . VAL A 303 ? 1.3853 1.3018 0.8136 -0.1854 -0.1469 -0.0110 303 VAL A CG2 
2344 N N   . THR A 304 ? 1.1614 1.2144 0.7684 -0.0783 -0.0598 0.0584  304 THR A N   
2345 C CA  . THR A 304 ? 1.0713 1.1515 0.7092 -0.0499 -0.0315 0.0693  304 THR A CA  
2346 C C   . THR A 304 ? 1.1619 1.2603 0.7581 -0.0502 -0.0211 0.0678  304 THR A C   
2347 O O   . THR A 304 ? 1.0612 1.1640 0.6068 -0.0732 -0.0388 0.0648  304 THR A O   
2348 C CB  . THR A 304 ? 0.9392 1.0673 0.6322 -0.0443 -0.0311 0.1075  304 THR A CB  
2349 O OG1 . THR A 304 ? 0.9110 1.0335 0.6306 -0.0528 -0.0449 0.1126  304 THR A OG1 
2350 C CG2 . THR A 304 ? 0.9557 1.0898 0.6855 -0.0162 -0.0029 0.1119  304 THR A CG2 
2351 N N   . PHE A 305 ? 1.0514 1.1629 0.6672 -0.0276 0.0069  0.0714  305 PHE A N   
2352 C CA  . PHE A 305 ? 1.1854 1.3200 0.7647 -0.0280 0.0208  0.0763  305 PHE A CA  
2353 C C   . PHE A 305 ? 1.2210 1.4008 0.7913 -0.0445 0.0024  0.1153  305 PHE A C   
2354 O O   . PHE A 305 ? 1.2325 1.4439 0.8237 -0.0356 0.0139  0.1468  305 PHE A O   
2355 C CB  . PHE A 305 ? 1.1374 1.2834 0.7515 -0.0052 0.0529  0.0818  305 PHE A CB  
2356 C CG  . PHE A 305 ? 1.1895 1.3379 0.7615 -0.0007 0.0768  0.0620  305 PHE A CG  
2357 C CD1 . PHE A 305 ? 1.1911 1.3472 0.6933 -0.0175 0.0702  0.0561  305 PHE A CD1 
2358 C CD2 . PHE A 305 ? 1.1512 1.3001 0.7525 0.0190  0.1060  0.0493  305 PHE A CD2 
2359 C CE1 . PHE A 305 ? 1.1564 1.3191 0.6147 -0.0125 0.0962  0.0364  305 PHE A CE1 
2360 C CE2 . PHE A 305 ? 1.1982 1.3596 0.7646 0.0242  0.1321  0.0322  305 PHE A CE2 
2361 C CZ  . PHE A 305 ? 1.2538 1.4212 0.7464 0.0096  0.1291  0.0248  305 PHE A CZ  
# 
