data_9EXU
# 
_entry.id   9EXU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EXU         pdb_00009exu 10.2210/pdb9exu/pdb 
WWPDB D_1292137780 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        9EXU 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9EX8 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              roberto.battistutta@unipd.it 
_pdbx_contact_author.name_first         Roberto 
_pdbx_contact_author.name_last          Battistutta 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0193-0694 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Battistutta, R.' 1 ? 
'Fornasier, E.'   2 ? 
'Giachin, G.'     3 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            7 
_citation.language                  ? 
_citation.page_first                1435 
_citation.page_last                 1435 
_citation.title                     'Allostery in homodimeric SARS-CoV-2 main protease.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-024-07138-w 
_citation.pdbx_database_id_PubMed   39496839 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fornasier, E.'   1  ?                   
primary 'Fabbian, S.'     2  ?                   
primary 'Shehi, H.'       3  ?                   
primary 'Enderle, J.'     4  ?                   
primary 'Gatto, B.'       5  0000-0001-9465-6913 
primary 'Volpin, D.'      6  ?                   
primary 'Biondi, B.'      7  ?                   
primary 'Bellanda, M.'    8  0000-0002-8187-0264 
primary 'Giachin, G.'     9  0000-0001-7550-0307 
primary 'Sosic, A.'       10 ?                   
primary 'Battistutta, R.' 11 0000-0002-0193-0694 
# 
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 'Non-structural protein 7'                  33726.410 2   ? ? ? ?      
2 polymer syn THR-SER-ALA-VAL-LEU-GLN-SER-GLY-PHE-ARG-LYS 1237.406  2   ? ? ? nsp4/5 
3 water   nat water                                       18.015    331 ? ? ? ?      
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        nsp7 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRAVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSAGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRAVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSAGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
A,B ? 
2 'polypeptide(L)' no yes '(THC)SAVLQSGFRK' TSAVLQSGFRK C,D ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     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  ALA 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 ALA 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 
1 306 GLN n 
2 1   THC n 
2 2   SER n 
2 3   ALA n 
2 4   VAL n 
2 5   LEU n 
2 6   GLN n 
2 7   SER n 
2 8   GLY n 
2 9   PHE n 
2 10  ARG n 
2 11  LYS 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       11 
_pdbx_entity_src_syn.organism_scientific    'Severe acute respiratory syndrome coronavirus 2' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       2697049 
_pdbx_entity_src_syn.details                ? 
# 
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 
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 
THC 'L-peptide linking' n N-METHYLCARBONYLTHREONINE ? 'C6 H11 N O4'    161.156 
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  ALA 41  41  41  ALA ALA 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 ALA 145 145 145 ALA ALA 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 ?   ?   ?   A . n 
A 1 304 THR 304 304 ?   ?   ?   A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 THR 304 304 ?   ?   ?   B . n 
B 1 305 PHE 305 305 ?   ?   ?   B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . n 
C 2 1   THC 1   1   1   THC THR C . n 
C 2 2   SER 2   2   2   SER SER C . n 
C 2 3   ALA 3   3   3   ALA ALA C . n 
C 2 4   VAL 4   4   4   VAL VAL C . n 
C 2 5   LEU 5   5   5   LEU LEU C . n 
C 2 6   GLN 6   6   6   GLN GLN C . n 
C 2 7   SER 7   7   7   SER SER C . n 
C 2 8   GLY 8   8   8   GLY GLY C . n 
C 2 9   PHE 9   9   9   PHE PHE C . n 
C 2 10  ARG 10  10  10  ARG ARG C . n 
C 2 11  LYS 11  11  11  LYS LYS C . n 
D 2 1   THC 1   1   1   THC THR D . n 
D 2 2   SER 2   2   2   SER SER D . n 
D 2 3   ALA 3   3   3   ALA ALA D . n 
D 2 4   VAL 4   4   4   VAL VAL D . n 
D 2 5   LEU 5   5   5   LEU LEU D . n 
D 2 6   GLN 6   6   6   GLN GLN D . n 
D 2 7   SER 7   7   7   SER SER D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   PHE 9   9   9   PHE PHE D . n 
D 2 10  ARG 10  10  10  ARG ARG D . n 
D 2 11  LYS 11  11  ?   ?   ?   D . n 
# 
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 
E 3 HOH 1   401 287 HOH HOH A . 
E 3 HOH 2   402 84  HOH HOH A . 
E 3 HOH 3   403 216 HOH HOH A . 
E 3 HOH 4   404 320 HOH HOH A . 
E 3 HOH 5   405 51  HOH HOH A . 
E 3 HOH 6   406 90  HOH HOH A . 
E 3 HOH 7   407 162 HOH HOH A . 
E 3 HOH 8   408 91  HOH HOH A . 
E 3 HOH 9   409 13  HOH HOH A . 
E 3 HOH 10  410 280 HOH HOH A . 
E 3 HOH 11  411 186 HOH HOH A . 
E 3 HOH 12  412 241 HOH HOH A . 
E 3 HOH 13  413 107 HOH HOH A . 
E 3 HOH 14  414 225 HOH HOH A . 
E 3 HOH 15  415 130 HOH HOH A . 
E 3 HOH 16  416 147 HOH HOH A . 
E 3 HOH 17  417 234 HOH HOH A . 
E 3 HOH 18  418 2   HOH HOH A . 
E 3 HOH 19  419 221 HOH HOH A . 
E 3 HOH 20  420 272 HOH HOH A . 
E 3 HOH 21  421 290 HOH HOH A . 
E 3 HOH 22  422 49  HOH HOH A . 
E 3 HOH 23  423 224 HOH HOH A . 
E 3 HOH 24  424 142 HOH HOH A . 
E 3 HOH 25  425 314 HOH HOH A . 
E 3 HOH 26  426 292 HOH HOH A . 
E 3 HOH 27  427 153 HOH HOH A . 
E 3 HOH 28  428 117 HOH HOH A . 
E 3 HOH 29  429 236 HOH HOH A . 
E 3 HOH 30  430 71  HOH HOH A . 
E 3 HOH 31  431 73  HOH HOH A . 
E 3 HOH 32  432 309 HOH HOH A . 
E 3 HOH 33  433 105 HOH HOH A . 
E 3 HOH 34  434 199 HOH HOH A . 
E 3 HOH 35  435 96  HOH HOH A . 
E 3 HOH 36  436 116 HOH HOH A . 
E 3 HOH 37  437 22  HOH HOH A . 
E 3 HOH 38  438 233 HOH HOH A . 
E 3 HOH 39  439 4   HOH HOH A . 
E 3 HOH 40  440 47  HOH HOH A . 
E 3 HOH 41  441 44  HOH HOH A . 
E 3 HOH 42  442 63  HOH HOH A . 
E 3 HOH 43  443 98  HOH HOH A . 
E 3 HOH 44  444 64  HOH HOH A . 
E 3 HOH 45  445 284 HOH HOH A . 
E 3 HOH 46  446 298 HOH HOH A . 
E 3 HOH 47  447 75  HOH HOH A . 
E 3 HOH 48  448 65  HOH HOH A . 
E 3 HOH 49  449 313 HOH HOH A . 
E 3 HOH 50  450 41  HOH HOH A . 
E 3 HOH 51  451 58  HOH HOH A . 
E 3 HOH 52  452 48  HOH HOH A . 
E 3 HOH 53  453 68  HOH HOH A . 
E 3 HOH 54  454 14  HOH HOH A . 
E 3 HOH 55  455 17  HOH HOH A . 
E 3 HOH 56  456 132 HOH HOH A . 
E 3 HOH 57  457 16  HOH HOH A . 
E 3 HOH 58  458 217 HOH HOH A . 
E 3 HOH 59  459 254 HOH HOH A . 
E 3 HOH 60  460 30  HOH HOH A . 
E 3 HOH 61  461 74  HOH HOH A . 
E 3 HOH 62  462 170 HOH HOH A . 
E 3 HOH 63  463 24  HOH HOH A . 
E 3 HOH 64  464 244 HOH HOH A . 
E 3 HOH 65  465 319 HOH HOH A . 
E 3 HOH 66  466 201 HOH HOH A . 
E 3 HOH 67  467 103 HOH HOH A . 
E 3 HOH 68  468 120 HOH HOH A . 
E 3 HOH 69  469 40  HOH HOH A . 
E 3 HOH 70  470 187 HOH HOH A . 
E 3 HOH 71  471 57  HOH HOH A . 
E 3 HOH 72  472 273 HOH HOH A . 
E 3 HOH 73  473 33  HOH HOH A . 
E 3 HOH 74  474 36  HOH HOH A . 
E 3 HOH 75  475 114 HOH HOH A . 
E 3 HOH 76  476 288 HOH HOH A . 
E 3 HOH 77  477 54  HOH HOH A . 
E 3 HOH 78  478 72  HOH HOH A . 
E 3 HOH 79  479 106 HOH HOH A . 
E 3 HOH 80  480 146 HOH HOH A . 
E 3 HOH 81  481 121 HOH HOH A . 
E 3 HOH 82  482 80  HOH HOH A . 
E 3 HOH 83  483 230 HOH HOH A . 
E 3 HOH 84  484 302 HOH HOH A . 
E 3 HOH 85  485 246 HOH HOH A . 
E 3 HOH 86  486 166 HOH HOH A . 
E 3 HOH 87  487 219 HOH HOH A . 
E 3 HOH 88  488 37  HOH HOH A . 
E 3 HOH 89  489 111 HOH HOH A . 
E 3 HOH 90  490 143 HOH HOH A . 
E 3 HOH 91  491 76  HOH HOH A . 
E 3 HOH 92  492 229 HOH HOH A . 
E 3 HOH 93  493 9   HOH HOH A . 
E 3 HOH 94  494 69  HOH HOH A . 
E 3 HOH 95  495 165 HOH HOH A . 
E 3 HOH 96  496 18  HOH HOH A . 
E 3 HOH 97  497 50  HOH HOH A . 
E 3 HOH 98  498 332 HOH HOH A . 
E 3 HOH 99  499 53  HOH HOH A . 
E 3 HOH 100 500 299 HOH HOH A . 
E 3 HOH 101 501 182 HOH HOH A . 
E 3 HOH 102 502 207 HOH HOH A . 
E 3 HOH 103 503 43  HOH HOH A . 
E 3 HOH 104 504 215 HOH HOH A . 
E 3 HOH 105 505 210 HOH HOH A . 
E 3 HOH 106 506 185 HOH HOH A . 
E 3 HOH 107 507 119 HOH HOH A . 
E 3 HOH 108 508 250 HOH HOH A . 
E 3 HOH 109 509 109 HOH HOH A . 
E 3 HOH 110 510 301 HOH HOH A . 
E 3 HOH 111 511 253 HOH HOH A . 
E 3 HOH 112 512 178 HOH HOH A . 
E 3 HOH 113 513 86  HOH HOH A . 
E 3 HOH 114 514 156 HOH HOH A . 
E 3 HOH 115 515 154 HOH HOH A . 
E 3 HOH 116 516 85  HOH HOH A . 
E 3 HOH 117 517 206 HOH HOH A . 
E 3 HOH 118 518 93  HOH HOH A . 
E 3 HOH 119 519 127 HOH HOH A . 
E 3 HOH 120 520 265 HOH HOH A . 
E 3 HOH 121 521 243 HOH HOH A . 
E 3 HOH 122 522 118 HOH HOH A . 
E 3 HOH 123 523 52  HOH HOH A . 
E 3 HOH 124 524 249 HOH HOH A . 
E 3 HOH 125 525 172 HOH HOH A . 
E 3 HOH 126 526 128 HOH HOH A . 
E 3 HOH 127 527 1   HOH HOH A . 
E 3 HOH 128 528 31  HOH HOH A . 
E 3 HOH 129 529 263 HOH HOH A . 
E 3 HOH 130 530 158 HOH HOH A . 
E 3 HOH 131 531 238 HOH HOH A . 
E 3 HOH 132 532 138 HOH HOH A . 
E 3 HOH 133 533 226 HOH HOH A . 
E 3 HOH 134 534 193 HOH HOH A . 
E 3 HOH 135 535 262 HOH HOH A . 
E 3 HOH 136 536 211 HOH HOH A . 
E 3 HOH 137 537 255 HOH HOH A . 
E 3 HOH 138 538 168 HOH HOH A . 
E 3 HOH 139 539 304 HOH HOH A . 
E 3 HOH 140 540 310 HOH HOH A . 
E 3 HOH 141 541 136 HOH HOH A . 
E 3 HOH 142 542 251 HOH HOH A . 
E 3 HOH 143 543 282 HOH HOH A . 
E 3 HOH 144 544 242 HOH HOH A . 
E 3 HOH 145 545 171 HOH HOH A . 
E 3 HOH 146 546 29  HOH HOH A . 
E 3 HOH 147 547 145 HOH HOH A . 
E 3 HOH 148 548 108 HOH HOH A . 
E 3 HOH 149 549 123 HOH HOH A . 
E 3 HOH 150 550 169 HOH HOH A . 
E 3 HOH 151 551 95  HOH HOH A . 
E 3 HOH 152 552 101 HOH HOH A . 
E 3 HOH 153 553 104 HOH HOH A . 
E 3 HOH 154 554 312 HOH HOH A . 
E 3 HOH 155 555 267 HOH HOH A . 
E 3 HOH 156 556 82  HOH HOH A . 
E 3 HOH 157 557 23  HOH HOH A . 
E 3 HOH 158 558 129 HOH HOH A . 
E 3 HOH 159 559 295 HOH HOH A . 
E 3 HOH 160 560 149 HOH HOH A . 
E 3 HOH 161 561 212 HOH HOH A . 
E 3 HOH 162 562 281 HOH HOH A . 
E 3 HOH 163 563 283 HOH HOH A . 
E 3 HOH 164 564 173 HOH HOH A . 
E 3 HOH 165 565 202 HOH HOH A . 
E 3 HOH 166 566 140 HOH HOH A . 
E 3 HOH 167 567 175 HOH HOH A . 
E 3 HOH 168 568 20  HOH HOH A . 
E 3 HOH 169 569 271 HOH HOH A . 
E 3 HOH 170 570 203 HOH HOH A . 
E 3 HOH 171 571 112 HOH HOH A . 
E 3 HOH 172 572 297 HOH HOH A . 
E 3 HOH 173 573 247 HOH HOH A . 
E 3 HOH 174 574 293 HOH HOH A . 
E 3 HOH 175 575 180 HOH HOH A . 
E 3 HOH 176 576 196 HOH HOH A . 
F 3 HOH 1   401 276 HOH HOH B . 
F 3 HOH 2   402 78  HOH HOH B . 
F 3 HOH 3   403 213 HOH HOH B . 
F 3 HOH 4   404 228 HOH HOH B . 
F 3 HOH 5   405 303 HOH HOH B . 
F 3 HOH 6   406 270 HOH HOH B . 
F 3 HOH 7   407 12  HOH HOH B . 
F 3 HOH 8   408 286 HOH HOH B . 
F 3 HOH 9   409 19  HOH HOH B . 
F 3 HOH 10  410 279 HOH HOH B . 
F 3 HOH 11  411 220 HOH HOH B . 
F 3 HOH 12  412 195 HOH HOH B . 
F 3 HOH 13  413 322 HOH HOH B . 
F 3 HOH 14  414 235 HOH HOH B . 
F 3 HOH 15  415 102 HOH HOH B . 
F 3 HOH 16  416 174 HOH HOH B . 
F 3 HOH 17  417 259 HOH HOH B . 
F 3 HOH 18  418 8   HOH HOH B . 
F 3 HOH 19  419 194 HOH HOH B . 
F 3 HOH 20  420 324 HOH HOH B . 
F 3 HOH 21  421 32  HOH HOH B . 
F 3 HOH 22  422 110 HOH HOH B . 
F 3 HOH 23  423 81  HOH HOH B . 
F 3 HOH 24  424 183 HOH HOH B . 
F 3 HOH 25  425 45  HOH HOH B . 
F 3 HOH 26  426 328 HOH HOH B . 
F 3 HOH 27  427 245 HOH HOH B . 
F 3 HOH 28  428 66  HOH HOH B . 
F 3 HOH 29  429 274 HOH HOH B . 
F 3 HOH 30  430 275 HOH HOH B . 
F 3 HOH 31  431 10  HOH HOH B . 
F 3 HOH 32  432 126 HOH HOH B . 
F 3 HOH 33  433 26  HOH HOH B . 
F 3 HOH 34  434 205 HOH HOH B . 
F 3 HOH 35  435 167 HOH HOH B . 
F 3 HOH 36  436 181 HOH HOH B . 
F 3 HOH 37  437 160 HOH HOH B . 
F 3 HOH 38  438 67  HOH HOH B . 
F 3 HOH 39  439 5   HOH HOH B . 
F 3 HOH 40  440 144 HOH HOH B . 
F 3 HOH 41  441 38  HOH HOH B . 
F 3 HOH 42  442 192 HOH HOH B . 
F 3 HOH 43  443 46  HOH HOH B . 
F 3 HOH 44  444 150 HOH HOH B . 
F 3 HOH 45  445 300 HOH HOH B . 
F 3 HOH 46  446 190 HOH HOH B . 
F 3 HOH 47  447 6   HOH HOH B . 
F 3 HOH 48  448 164 HOH HOH B . 
F 3 HOH 49  449 87  HOH HOH B . 
F 3 HOH 50  450 15  HOH HOH B . 
F 3 HOH 51  451 197 HOH HOH B . 
F 3 HOH 52  452 11  HOH HOH B . 
F 3 HOH 53  453 99  HOH HOH B . 
F 3 HOH 54  454 39  HOH HOH B . 
F 3 HOH 55  455 256 HOH HOH B . 
F 3 HOH 56  456 35  HOH HOH B . 
F 3 HOH 57  457 252 HOH HOH B . 
F 3 HOH 58  458 62  HOH HOH B . 
F 3 HOH 59  459 161 HOH HOH B . 
F 3 HOH 60  460 92  HOH HOH B . 
F 3 HOH 61  461 159 HOH HOH B . 
F 3 HOH 62  462 139 HOH HOH B . 
F 3 HOH 63  463 294 HOH HOH B . 
F 3 HOH 64  464 151 HOH HOH B . 
F 3 HOH 65  465 97  HOH HOH B . 
F 3 HOH 66  466 83  HOH HOH B . 
F 3 HOH 67  467 115 HOH HOH B . 
F 3 HOH 68  468 131 HOH HOH B . 
F 3 HOH 69  469 7   HOH HOH B . 
F 3 HOH 70  470 200 HOH HOH B . 
F 3 HOH 71  471 25  HOH HOH B . 
F 3 HOH 72  472 232 HOH HOH B . 
F 3 HOH 73  473 122 HOH HOH B . 
F 3 HOH 74  474 21  HOH HOH B . 
F 3 HOH 75  475 28  HOH HOH B . 
F 3 HOH 76  476 223 HOH HOH B . 
F 3 HOH 77  477 135 HOH HOH B . 
F 3 HOH 78  478 209 HOH HOH B . 
F 3 HOH 79  479 56  HOH HOH B . 
F 3 HOH 80  480 42  HOH HOH B . 
F 3 HOH 81  481 330 HOH HOH B . 
F 3 HOH 82  482 60  HOH HOH B . 
F 3 HOH 83  483 124 HOH HOH B . 
F 3 HOH 84  484 155 HOH HOH B . 
F 3 HOH 85  485 231 HOH HOH B . 
F 3 HOH 86  486 188 HOH HOH B . 
F 3 HOH 87  487 222 HOH HOH B . 
F 3 HOH 88  488 266 HOH HOH B . 
F 3 HOH 89  489 3   HOH HOH B . 
F 3 HOH 90  490 248 HOH HOH B . 
F 3 HOH 91  491 227 HOH HOH B . 
F 3 HOH 92  492 218 HOH HOH B . 
F 3 HOH 93  493 94  HOH HOH B . 
F 3 HOH 94  494 308 HOH HOH B . 
F 3 HOH 95  495 141 HOH HOH B . 
F 3 HOH 96  496 61  HOH HOH B . 
F 3 HOH 97  497 257 HOH HOH B . 
F 3 HOH 98  498 184 HOH HOH B . 
F 3 HOH 99  499 327 HOH HOH B . 
F 3 HOH 100 500 208 HOH HOH B . 
F 3 HOH 101 501 240 HOH HOH B . 
F 3 HOH 102 502 27  HOH HOH B . 
F 3 HOH 103 503 133 HOH HOH B . 
F 3 HOH 104 504 285 HOH HOH B . 
F 3 HOH 105 505 179 HOH HOH B . 
F 3 HOH 106 506 77  HOH HOH B . 
F 3 HOH 107 507 137 HOH HOH B . 
F 3 HOH 108 508 148 HOH HOH B . 
F 3 HOH 109 509 269 HOH HOH B . 
F 3 HOH 110 510 100 HOH HOH B . 
F 3 HOH 111 511 34  HOH HOH B . 
F 3 HOH 112 512 88  HOH HOH B . 
F 3 HOH 113 513 214 HOH HOH B . 
F 3 HOH 114 514 296 HOH HOH B . 
F 3 HOH 115 515 277 HOH HOH B . 
F 3 HOH 116 516 323 HOH HOH B . 
F 3 HOH 117 517 289 HOH HOH B . 
F 3 HOH 118 518 70  HOH HOH B . 
F 3 HOH 119 519 79  HOH HOH B . 
F 3 HOH 120 520 113 HOH HOH B . 
F 3 HOH 121 521 198 HOH HOH B . 
F 3 HOH 122 522 307 HOH HOH B . 
F 3 HOH 123 523 134 HOH HOH B . 
F 3 HOH 124 524 311 HOH HOH B . 
F 3 HOH 125 525 163 HOH HOH B . 
F 3 HOH 126 526 191 HOH HOH B . 
F 3 HOH 127 527 176 HOH HOH B . 
F 3 HOH 128 528 306 HOH HOH B . 
F 3 HOH 129 529 239 HOH HOH B . 
F 3 HOH 130 530 189 HOH HOH B . 
F 3 HOH 131 531 261 HOH HOH B . 
F 3 HOH 132 532 264 HOH HOH B . 
F 3 HOH 133 533 305 HOH HOH B . 
F 3 HOH 134 534 260 HOH HOH B . 
F 3 HOH 135 535 268 HOH HOH B . 
F 3 HOH 136 536 157 HOH HOH B . 
F 3 HOH 137 537 258 HOH HOH B . 
F 3 HOH 138 538 152 HOH HOH B . 
F 3 HOH 139 539 278 HOH HOH B . 
F 3 HOH 140 540 204 HOH HOH B . 
F 3 HOH 141 541 177 HOH HOH B . 
G 3 HOH 1   201 316 HOH HOH C . 
G 3 HOH 2   202 331 HOH HOH C . 
G 3 HOH 3   203 318 HOH HOH C . 
G 3 HOH 4   204 317 HOH HOH C . 
G 3 HOH 5   205 315 HOH HOH C . 
H 3 HOH 1   201 59  HOH HOH D . 
H 3 HOH 2   202 321 HOH HOH D . 
H 3 HOH 3   203 55  HOH HOH D . 
H 3 HOH 4   204 89  HOH HOH D . 
H 3 HOH 5   205 326 HOH HOH D . 
H 3 HOH 6   206 329 HOH HOH D . 
H 3 HOH 7   207 325 HOH HOH D . 
H 3 HOH 8   208 237 HOH HOH D . 
H 3 HOH 9   209 125 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  92.220 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.100 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  108.380 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EXU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.558 
_cell.length_a_esd                 ? 
_cell.length_b                     61.356 
_cell.length_b_esd                 ? 
_cell.length_c                     67.902 
_cell.length_c_esd                 ? 
_cell.volume                       197571.596 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9EXU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            'P 1' 
_symmetry.space_group_name_H-M             'P 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                   9EXU 
_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             1.96 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.16 
_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              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M MMT (DL-malic acid, MES, and Tris base in molar ratio 1:2:2), pH 7.0, 25% PEG 1500' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8856 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          38.45 
_reflns.entry_id                                       9EXU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.78 
_reflns.d_resolution_low                               46.88 
_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                                     68784 
_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                           93.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.045 
_reflns.pdbx_Rpim_I_all                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.038 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.038 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.78 
_reflns_shell.d_res_low                                     1.81 
_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                             2308 
_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                               1.195 
_reflns_shell.pdbx_Rpim_I_all                               0.652 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.665 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.993 
_reflns_shell.pdbx_Rsym_value                               0.993 
_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                               50.66 
_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                                 9EXU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.78 
_refine.ls_d_res_low                             46.88 
_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                     68649 
_refine.ls_number_reflns_R_free                  3400 
_refine.ls_number_reflns_R_work                  65249 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.90 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1808 
_refine.ls_R_factor_R_free                       0.2039 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1795 
_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                          1.97 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 27.9331 
_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                            0.2068 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        46.88 
_refine_hist.number_atoms_solvent             331 
_refine_hist.number_atoms_total               5155 
_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        4818 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_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' ? 0.0174  ? 4959 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.4481  ? 6738 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0895  ? 761  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0208  ? 877  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.6139 ? 1773 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.78 1.80  . . 92  1533 52.97 . . . . 0.3852 . . . . . . . . . . . 0.3781 
'X-RAY DIFFRACTION' 1.80 1.83  . . 90  1914 64.25 . . . . 0.3468 . . . . . . . . . . . 0.3431 
'X-RAY DIFFRACTION' 1.83 1.86  . . 114 2183 75.63 . . . . 0.3198 . . . . . . . . . . . 0.4022 
'X-RAY DIFFRACTION' 1.86 1.89  . . 133 2654 90.93 . . . . 0.3182 . . . . . . . . . . . 0.3304 
'X-RAY DIFFRACTION' 1.89 1.92  . . 147 2764 93.60 . . . . 0.2961 . . . . . . . . . . . 0.2960 
'X-RAY DIFFRACTION' 1.92 1.95  . . 125 2769 95.23 . . . . 0.2641 . . . . . . . . . . . 0.2781 
'X-RAY DIFFRACTION' 1.95 1.99  . . 131 2886 96.48 . . . . 0.2520 . . . . . . . . . . . 0.2589 
'X-RAY DIFFRACTION' 1.99 2.03  . . 155 2806 96.58 . . . . 0.2476 . . . . . . . . . . . 0.2760 
'X-RAY DIFFRACTION' 2.03 2.08  . . 151 2818 97.06 . . . . 0.2463 . . . . . . . . . . . 0.2703 
'X-RAY DIFFRACTION' 2.08 2.13  . . 151 2890 97.31 . . . . 0.2243 . . . . . . . . . . . 0.2695 
'X-RAY DIFFRACTION' 2.13 2.18  . . 150 2818 97.18 . . . . 0.1979 . . . . . . . . . . . 0.2448 
'X-RAY DIFFRACTION' 2.18 2.24  . . 136 2860 97.69 . . . . 0.1900 . . . . . . . . . . . 0.2192 
'X-RAY DIFFRACTION' 2.24 2.30  . . 171 2834 97.60 . . . . 0.1877 . . . . . . . . . . . 0.2011 
'X-RAY DIFFRACTION' 2.30 2.38  . . 148 2834 97.20 . . . . 0.1910 . . . . . . . . . . . 0.2358 
'X-RAY DIFFRACTION' 2.38 2.46  . . 147 2872 97.89 . . . . 0.1977 . . . . . . . . . . . 0.2514 
'X-RAY DIFFRACTION' 2.46 2.56  . . 154 2884 98.16 . . . . 0.1976 . . . . . . . . . . . 0.2416 
'X-RAY DIFFRACTION' 2.56 2.68  . . 169 2856 97.90 . . . . 0.2119 . . . . . . . . . . . 0.2435 
'X-RAY DIFFRACTION' 2.68 2.82  . . 141 2889 98.28 . . . . 0.2090 . . . . . . . . . . . 0.2373 
'X-RAY DIFFRACTION' 2.82 3.00  . . 166 2836 98.30 . . . . 0.2035 . . . . . . . . . . . 0.2440 
'X-RAY DIFFRACTION' 3.00 3.23  . . 154 2896 98.10 . . . . 0.1961 . . . . . . . . . . . 0.2115 
'X-RAY DIFFRACTION' 3.23 3.55  . . 137 2861 97.72 . . . . 0.1777 . . . . . . . . . . . 0.2012 
'X-RAY DIFFRACTION' 3.55 4.06  . . 136 2859 97.94 . . . . 0.1574 . . . . . . . . . . . 0.1995 
'X-RAY DIFFRACTION' 4.07 5.12  . . 146 2892 98.16 . . . . 0.1319 . . . . . . . . . . . 0.1391 
'X-RAY DIFFRACTION' 5.12 46.88 . . 156 2841 97.56 . . . . 0.1429 . . . . . . . . . . . 0.1573 
# 
_struct.entry_id                     9EXU 
_struct.title                        
'Complex of a mutant of the SARS-CoV-2 main protease Mpro with the nsp4/5 substrate peptide (cocrystallization).' 
_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        9EXU 
_struct_keywords.text            'SARS-CoV-2, main protease, nsp5, Cys-peptidase, 3CLpro, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP R1AB_SARS2 P0DTD1 ? 1 
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
3264 
2 PDB 9EXU       9EXU   ? 2 ? 1    
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EXU A 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
2 1 9EXU B 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
3 2 9EXU C 1 ? 11  ? 9EXU   1    ? 11   ? 1 11  
4 2 9EXU D 1 ? 11  ? 9EXU   1    ? 11   ? 1 11  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EXU ALA A 41  ? UNP P0DTD1 HIS 3304 conflict 41  1 
1 9EXU ALA A 145 ? UNP P0DTD1 CYS 3408 conflict 145 2 
2 9EXU ALA B 41  ? UNP P0DTD1 HIS 3304 conflict 41  3 
2 9EXU ALA B 145 ? UNP P0DTD1 CYS 3408 conflict 145 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ALA A 41  ? CYS A 44  ? ALA A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 SER A 62  ? PHE A 66  ? SER A 62  PHE A 66  5 ? 5  
HELX_P HELX_P5  AA5 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P7  AA7 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P11 AB2 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P12 AB3 ALA B 41  ? CYS B 44  ? ALA B 41  CYS B 44  5 ? 4  
HELX_P HELX_P13 AB4 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P14 AB5 SER B 62  ? PHE B 66  ? SER B 62  PHE B 66  5 ? 5  
HELX_P HELX_P15 AB6 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P16 AB7 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P17 AB8 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P18 AB9 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P19 AC1 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P20 AC2 THR B 292 ? SER B 301 ? THR B 292 SER B 301 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? C THC 1 C ? ? ? 1_555 C SER 2 N A ? C THC 1 C SER 2 1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale2 covale both ? C THC 1 C ? ? ? 1_555 C SER 2 N B ? C THC 1 C SER 2 1_555 ? ? ? ? ? ? ? 1.323 ? ? 
covale3 covale both ? D THC 1 C ? ? ? 1_555 D SER 2 N ? ? D THC 1 D SER 2 1_555 ? ? ? ? ? ? ? 1.322 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 THC C 1 ? . . . . THC C 1 ? 1_555 . . . . . . . THR 1 THC None 'Non-standard residue' 
2 THC D 1 ? . . . . THC D 1 ? 1_555 . . . . . . . THR 1 THC None 'Non-standard residue' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 5 ? 
AA5 ? 7 ? 
AA6 ? 5 ? 
AA7 ? 3 ? 
AA8 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-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 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? 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 LEU A 67  ? ALA A 70  ? LEU A 67  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 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA2 2 LEU A 67  ? ALA A 70  ? LEU A 67  ALA A 70  
AA2 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA2 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA2 5 GLY C 8   ? PHE C 9   ? GLY C 8   PHE C 9   
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA4 2 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA4 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA4 4 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA4 5 VAL C 4   ? LEU C 5   ? VAL C 4   LEU C 5   
AA5 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA5 2 LEU B 67  ? ALA B 70  ? LEU B 67  ALA B 70  
AA5 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA5 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA5 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA5 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA5 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA6 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA6 2 LEU B 67  ? ALA B 70  ? LEU B 67  ALA B 70  
AA6 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA6 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA6 5 GLY D 8   ? PHE D 9   ? GLY D 8   PHE D 9   
AA7 1 LYS B 100 ? PHE B 103 ? LYS B 100 PHE B 103 
AA7 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA7 3 HIS B 172 ? THR B 175 ? HIS B 172 THR B 175 
AA8 1 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA8 2 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA8 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA8 4 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA8 5 VAL D 4   ? LEU D 5   ? VAL D 4   LEU D 5   
# 
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 LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 O LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA2 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA2 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA2 4 5 N THR A 26  ? N THR A 26  O GLY C 8   ? O GLY C 8   
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
AA4 1 2 O SER A 123 ? O SER A 123 N ALA A 116 ? N ALA A 116 
AA4 2 3 N SER A 113 ? N SER A 113 O PHE A 150 ? O PHE A 150 
AA4 3 4 N ASN A 151 ? N ASN A 151 O SER A 158 ? O SER A 158 
AA4 4 5 N GLU A 166 ? N GLU A 166 O VAL C 4   ? O VAL C 4   
AA5 1 2 O LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA5 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA5 3 4 N CYS B 22  ? N CYS B 22  O THR B 25  ? O THR B 25  
AA5 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA5 5 6 N CYS B 38  ? N CYS B 38  O LEU B 87  ? O LEU B 87  
AA5 6 7 O LYS B 88  ? O LYS B 88  N SER B 81  ? N SER B 81  
AA6 1 2 O LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA6 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA6 3 4 N CYS B 22  ? N CYS B 22  O THR B 25  ? O THR B 25  
AA6 4 5 N THR B 26  ? N THR B 26  O GLY D 8   ? O GLY D 8   
AA7 1 2 N LYS B 100 ? N LYS B 100 O VAL B 157 ? O VAL B 157 
AA7 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
AA8 1 2 O SER B 123 ? O SER B 123 N ALA B 116 ? N ALA B 116 
AA8 2 3 N SER B 113 ? N SER B 113 O PHE B 150 ? O PHE B 150 
AA8 3 4 N ASP B 153 ? N ASP B 153 O CYS B 156 ? O CYS B 156 
AA8 4 5 N GLU B 166 ? N GLU B 166 O VAL D 4   ? O VAL D 4   
# 
_pdbx_entry_details.entry_id                   9EXU 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O  B HOH 525 ? ? O B HOH 526 ? ? 1.86 
2 1 O  B HOH 499 ? ? O D HOH 202 ? ? 2.03 
3 1 OG A SER 62  ? ? O A HOH 401 ? ? 2.13 
4 1 O  A HOH 486 ? ? O A HOH 562 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    ILE 
_pdbx_validate_symm_contact.auth_seq_id_1     59 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NH1 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    ARG 
_pdbx_validate_symm_contact.auth_seq_id_2     217 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_665 
_pdbx_validate_symm_contact.dist              2.10 
# 
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  ? ? 53.94   -129.27 
2  1 ASP A 48  ? ? -98.68  48.10   
3  1 ASN A 84  ? ? 54.48   -123.23 
4  1 TYR A 154 ? ? 58.27   -105.32 
5  1 HIS A 164 ? ? -122.54 -51.23  
6  1 LEU B 27  ? ? -160.63 -167.28 
7  1 ASP B 33  ? ? 54.57   -129.28 
8  1 ASP B 48  ? ? -112.77 59.46   
9  1 ASN B 84  ? ? 55.43   -123.59 
10 1 TYR B 154 ? ? 58.53   -106.91 
11 1 GLN C 6   ? ? -86.95  45.02   
12 1 GLN D 6   ? ? -92.95  40.91   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     222 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.268 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 575 ? 6.09 . 
2 1 O ? A HOH 576 ? 6.35 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A VAL 303 ? A VAL 303 
2 1 Y 1 A THR 304 ? A THR 304 
3 1 Y 1 A PHE 305 ? A PHE 305 
4 1 Y 1 A GLN 306 ? A GLN 306 
5 1 Y 1 B THR 304 ? B THR 304 
6 1 Y 1 B PHE 305 ? B PHE 305 
7 1 Y 1 B GLN 306 ? B GLN 306 
8 1 Y 1 D LYS 11  ? D LYS 11  
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THC N1   N N N 304 
THC CN   C N N 305 
THC ON   O N N 306 
THC CM   C N N 307 
THC CA   C N S 308 
THC CB   C N R 309 
THC OG1  O N N 310 
THC CG2  C N N 311 
THC C    C N N 312 
THC O    O N N 313 
THC OXT  O N N 314 
THC HN   H N N 315 
THC HM1  H N N 316 
THC HM2  H N N 317 
THC HM3  H N N 318 
THC HA   H N N 319 
THC HB   H N N 320 
THC HG1  H N N 321 
THC HG21 H N N 322 
THC HG22 H N N 323 
THC HG23 H N N 324 
THC HXT  H N N 325 
THR N    N N N 326 
THR CA   C N S 327 
THR C    C N N 328 
THR O    O N N 329 
THR CB   C N R 330 
THR OG1  O N N 331 
THR CG2  C N N 332 
THR OXT  O N N 333 
THR H    H N N 334 
THR H2   H N N 335 
THR HA   H N N 336 
THR HB   H N N 337 
THR HG1  H N N 338 
THR HG21 H N N 339 
THR HG22 H N N 340 
THR HG23 H N N 341 
THR HXT  H N N 342 
TRP N    N N N 343 
TRP CA   C N S 344 
TRP C    C N N 345 
TRP O    O N N 346 
TRP CB   C N N 347 
TRP CG   C Y N 348 
TRP CD1  C Y N 349 
TRP CD2  C Y N 350 
TRP NE1  N Y N 351 
TRP CE2  C Y N 352 
TRP CE3  C Y N 353 
TRP CZ2  C Y N 354 
TRP CZ3  C Y N 355 
TRP CH2  C Y N 356 
TRP OXT  O N N 357 
TRP H    H N N 358 
TRP H2   H N N 359 
TRP HA   H N N 360 
TRP HB2  H N N 361 
TRP HB3  H N N 362 
TRP HD1  H N N 363 
TRP HE1  H N N 364 
TRP HE3  H N N 365 
TRP HZ2  H N N 366 
TRP HZ3  H N N 367 
TRP HH2  H N N 368 
TRP HXT  H N N 369 
TYR N    N N N 370 
TYR CA   C N S 371 
TYR C    C N N 372 
TYR O    O N N 373 
TYR CB   C N N 374 
TYR CG   C Y N 375 
TYR CD1  C Y N 376 
TYR CD2  C Y N 377 
TYR CE1  C Y N 378 
TYR CE2  C Y N 379 
TYR CZ   C Y N 380 
TYR OH   O N N 381 
TYR OXT  O N N 382 
TYR H    H N N 383 
TYR H2   H N N 384 
TYR HA   H N N 385 
TYR HB2  H N N 386 
TYR HB3  H N N 387 
TYR HD1  H N N 388 
TYR HD2  H N N 389 
TYR HE1  H N N 390 
TYR HE2  H N N 391 
TYR HH   H N N 392 
TYR HXT  H N N 393 
VAL N    N N N 394 
VAL CA   C N S 395 
VAL C    C N N 396 
VAL O    O N N 397 
VAL CB   C N N 398 
VAL CG1  C N N 399 
VAL CG2  C N N 400 
VAL OXT  O N N 401 
VAL H    H N N 402 
VAL H2   H N N 403 
VAL HA   H N N 404 
VAL HB   H N N 405 
VAL HG11 H N N 406 
VAL HG12 H N N 407 
VAL HG13 H N N 408 
VAL HG21 H N N 409 
VAL HG22 H N N 410 
VAL HG23 H N N 411 
VAL HXT  H N N 412 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THC N1  CN   sing N N 290 
THC N1  CA   sing N N 291 
THC N1  HN   sing N N 292 
THC CN  ON   doub N N 293 
THC CN  CM   sing N N 294 
THC CM  HM1  sing N N 295 
THC CM  HM2  sing N N 296 
THC CM  HM3  sing N N 297 
THC CA  CB   sing N N 298 
THC CA  C    sing N N 299 
THC CA  HA   sing N N 300 
THC CB  OG1  sing N N 301 
THC CB  CG2  sing N N 302 
THC CB  HB   sing N N 303 
THC OG1 HG1  sing N N 304 
THC CG2 HG21 sing N N 305 
THC CG2 HG22 sing N N 306 
THC CG2 HG23 sing N N 307 
THC C   O    doub N N 308 
THC C   OXT  sing N N 309 
THC OXT HXT  sing N N 310 
THR N   CA   sing N N 311 
THR N   H    sing N N 312 
THR N   H2   sing N N 313 
THR CA  C    sing N N 314 
THR CA  CB   sing N N 315 
THR CA  HA   sing N N 316 
THR C   O    doub N N 317 
THR C   OXT  sing N N 318 
THR CB  OG1  sing N N 319 
THR CB  CG2  sing N N 320 
THR CB  HB   sing N N 321 
THR OG1 HG1  sing N N 322 
THR CG2 HG21 sing N N 323 
THR CG2 HG22 sing N N 324 
THR CG2 HG23 sing N N 325 
THR OXT HXT  sing N N 326 
TRP N   CA   sing N N 327 
TRP N   H    sing N N 328 
TRP N   H2   sing N N 329 
TRP CA  C    sing N N 330 
TRP CA  CB   sing N N 331 
TRP CA  HA   sing N N 332 
TRP C   O    doub N N 333 
TRP C   OXT  sing N N 334 
TRP CB  CG   sing N N 335 
TRP CB  HB2  sing N N 336 
TRP CB  HB3  sing N N 337 
TRP CG  CD1  doub Y N 338 
TRP CG  CD2  sing Y N 339 
TRP CD1 NE1  sing Y N 340 
TRP CD1 HD1  sing N N 341 
TRP CD2 CE2  doub Y N 342 
TRP CD2 CE3  sing Y N 343 
TRP NE1 CE2  sing Y N 344 
TRP NE1 HE1  sing N N 345 
TRP CE2 CZ2  sing Y N 346 
TRP CE3 CZ3  doub Y N 347 
TRP CE3 HE3  sing N N 348 
TRP CZ2 CH2  doub Y N 349 
TRP CZ2 HZ2  sing N N 350 
TRP CZ3 CH2  sing Y N 351 
TRP CZ3 HZ3  sing N N 352 
TRP CH2 HH2  sing N N 353 
TRP OXT HXT  sing N N 354 
TYR N   CA   sing N N 355 
TYR N   H    sing N N 356 
TYR N   H2   sing N N 357 
TYR CA  C    sing N N 358 
TYR CA  CB   sing N N 359 
TYR CA  HA   sing N N 360 
TYR C   O    doub N N 361 
TYR C   OXT  sing N N 362 
TYR CB  CG   sing N N 363 
TYR CB  HB2  sing N N 364 
TYR CB  HB3  sing N N 365 
TYR CG  CD1  doub Y N 366 
TYR CG  CD2  sing Y N 367 
TYR CD1 CE1  sing Y N 368 
TYR CD1 HD1  sing N N 369 
TYR CD2 CE2  doub Y N 370 
TYR CD2 HD2  sing N N 371 
TYR CE1 CZ   doub Y N 372 
TYR CE1 HE1  sing N N 373 
TYR CE2 CZ   sing Y N 374 
TYR CE2 HE2  sing N N 375 
TYR CZ  OH   sing N N 376 
TYR OH  HH   sing N N 377 
TYR OXT HXT  sing N N 378 
VAL N   CA   sing N N 379 
VAL N   H    sing N N 380 
VAL N   H2   sing N N 381 
VAL CA  C    sing N N 382 
VAL CA  CB   sing N N 383 
VAL CA  HA   sing N N 384 
VAL C   O    doub N N 385 
VAL C   OXT  sing N N 386 
VAL CB  CG1  sing N N 387 
VAL CB  CG2  sing N N 388 
VAL CB  HB   sing N N 389 
VAL CG1 HG11 sing N N 390 
VAL CG1 HG12 sing N N 391 
VAL CG1 HG13 sing N N 392 
VAL CG2 HG21 sing N N 393 
VAL CG2 HG22 sing N N 394 
VAL CG2 HG23 sing N N 395 
VAL OXT HXT  sing N N 396 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7NIJ 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1' 
_space_group.name_Hall        'P 1' 
_space_group.IT_number        1 
_space_group.crystal_system   triclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EXU 
_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]   0.018671 
_atom_sites.fract_transf_matrix[1][2]   0.006204 
_atom_sites.fract_transf_matrix[1][3]   0.007542 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017174 
_atom_sites.fract_transf_matrix[2][3]   0.002753 
_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]   0.015784 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   ? -9.91100  7.86900   -16.94000 1.000 39.90742  ? 1   SER A N   1 
ATOM   2    C CA  . SER A 1 1   ? -10.49300 6.66200   -17.55700 1.000 44.65272  ? 1   SER A CA  1 
ATOM   3    C C   . SER A 1 1   ? -10.60500 5.57000   -16.55500 1.000 39.42052  ? 1   SER A C   1 
ATOM   4    O O   . SER A 1 1   ? -9.94600  5.58200   -15.46200 1.000 34.65942  ? 1   SER A O   1 
ATOM   5    C CB  . SER A 1 1   ? -9.63600  6.09900   -18.75600 1.000 42.44193  ? 1   SER A CB  1 
ATOM   6    O OG  . SER A 1 1   ? -9.66600  7.02600   -19.79100 1.000 51.17192  ? 1   SER A OG  1 
ATOM   7    N N   . GLY A 1 2   ? -11.34200 4.56000   -16.98100 1.000 38.58621  ? 2   GLY A N   1 
ATOM   8    C CA  . GLY A 1 2   ? -11.61700 3.42600   -16.12400 1.000 38.08878  ? 2   GLY A CA  1 
ATOM   9    C C   . GLY A 1 2   ? -13.04100 3.49500   -15.58300 1.000 38.74938  ? 2   GLY A C   1 
ATOM   10   O O   . GLY A 1 2   ? -13.69600 4.54200   -15.57100 1.000 42.36824  ? 2   GLY A O   1 
ATOM   11   N N   . PHE A 1 3   ? -13.54400 2.37100   -15.16300 1.000 37.09129  ? 3   PHE A N   1 
ATOM   12   C CA  . PHE A 1 3   ? -14.91500 2.40300   -14.62900 1.000 38.73886  ? 3   PHE A CA  1 
ATOM   13   C C   . PHE A 1 3   ? -15.01300 1.25800   -13.67500 1.000 38.62305  ? 3   PHE A C   1 
ATOM   14   O O   . PHE A 1 3   ? -14.82800 0.11700   -14.10900 1.000 39.97848  ? 3   PHE A O   1 
ATOM   15   C CB  . PHE A 1 3   ? -15.94200 2.27700   -15.73700 1.000 40.39958  ? 3   PHE A CB  1 
ATOM   16   C CG  . PHE A 1 3   ? -17.32800 2.66200   -15.28900 1.000 40.47327  ? 3   PHE A CG  1 
ATOM   17   C CD1 . PHE A 1 3   ? -17.63700 3.99500   -15.02300 1.000 43.84210  ? 3   PHE A CD1 1 
ATOM   18   C CD2 . PHE A 1 3   ? -18.28000 1.67800   -15.08300 1.000 42.68670  ? 3   PHE A CD2 1 
ATOM   19   C CE1 . PHE A 1 3   ? -18.91300 4.35600   -14.58100 1.000 46.96353  ? 3   PHE A CE1 1 
ATOM   20   C CE2 . PHE A 1 3   ? -19.59800 2.02000   -14.64300 1.000 41.90502  ? 3   PHE A CE2 1 
ATOM   21   C CZ  . PHE A 1 3   ? -19.89900 3.36800   -14.37700 1.000 42.08136  ? 3   PHE A CZ  1 
ATOM   22   N N   . ARG A 1 4   ? -15.24400 1.55100   -12.37500 1.000 38.46514  ? 4   ARG A N   1 
ATOM   23   C CA  . ARG A 1 4   ? -15.21500 0.52800   -11.35500 1.000 36.97549  ? 4   ARG A CA  1 
ATOM   24   C C   . ARG A 1 4   ? -16.47500 0.65700   -10.50200 1.000 34.45939  ? 4   ARG A C   1 
ATOM   25   O O   . ARG A 1 4   ? -16.94900 1.76300   -10.28400 1.000 35.01736  ? 4   ARG A O   1 
ATOM   26   C CB  . ARG A 1 4   ? -14.10200 0.69900   -10.39700 1.000 37.91770  ? 4   ARG A CB  1 
ATOM   27   C CG  . ARG A 1 4   ? -12.73100 0.64600   -11.15600 1.000 37.89139  ? 4   ARG A CG  1 
ATOM   28   C CD  . ARG A 1 4   ? -12.51100 -0.75700  -11.69200 1.000 42.59195  ? 4   ARG A CD  1 
ATOM   29   N NE  . ARG A 1 4   ? -12.81200 -1.65100  -10.61200 1.000 42.91830  ? 4   ARG A NE  1 
ATOM   30   C CZ  . ARG A 1 4   ? -11.90700 -2.04800  -9.74500  1.000 48.75585  ? 4   ARG A CZ  1 
ATOM   31   N NH1 . ARG A 1 4   ? -10.61100 -1.75500  -9.93000  1.000 43.36046  ? 4   ARG A NH1 1 
ATOM   32   N NH2 . ARG A 1 4   ? -12.31200 -2.68700  -8.64100  1.000 44.07371  ? 4   ARG A NH2 1 
ATOM   33   N N   . LYS A 1 5   ? -16.84700 -0.43400  -9.89300  1.000 33.92775  ? 5   LYS A N   1 
ATOM   34   C CA  . LYS A 1 5   ? -17.90600 -0.36200  -8.85500  1.000 36.18592  ? 5   LYS A CA  1 
ATOM   35   C C   . LYS A 1 5   ? -17.28500 0.32700   -7.63600  1.000 39.29155  ? 5   LYS A C   1 
ATOM   36   O O   . LYS A 1 5   ? -16.42500 -0.21900  -6.93900  1.000 43.74209  ? 5   LYS A O   1 
ATOM   37   C CB  . LYS A 1 5   ? -18.42400 -1.76800  -8.57400  1.000 40.26799  ? 5   LYS A CB  1 
ATOM   38   C CG  . LYS A 1 5   ? -19.93300 -1.87800  -8.30500  1.000 47.49254  ? 5   LYS A CG  1 
ATOM   39   C CD  . LYS A 1 5   ? -20.36700 -3.26100  -8.67100  1.000 54.28809  ? 5   LYS A CD  1 
ATOM   40   C CE  . LYS A 1 5   ? -21.34000 -3.22300  -9.83000  1.000 50.20865  ? 5   LYS A CE  1 
ATOM   41   N NZ  . LYS A 1 5   ? -21.63100 -4.63800  -10.13100 1.000 57.94379  ? 5   LYS A NZ  1 
ATOM   42   N N   . MET A 1 6   ? -17.65000 1.55600   -7.43400  1.000 32.44863  ? 6   MET A N   1 
ATOM   43   C CA  . MET A 1 6   ? -17.00500 2.44600   -6.48000  1.000 38.66516  ? 6   MET A CA  1 
ATOM   44   C C   . MET A 1 6   ? -17.96600 2.77600   -5.31600  1.000 41.11809  ? 6   MET A C   1 
ATOM   45   O O   . MET A 1 6   ? -19.06100 3.28400   -5.54600  1.000 43.93948  ? 6   MET A O   1 
ATOM   46   C CB  . MET A 1 6   ? -16.62000 3.71200   -7.23000  1.000 38.72833  ? 6   MET A CB  1 
ATOM   47   C CG  . MET A 1 6   ? -15.84400 4.63200   -6.40300  1.000 43.92369  ? 6   MET A CG  1 
ATOM   48   S SD  . MET A 1 6   ? -15.02400 5.83200   -7.47700  1.000 54.78025  ? 6   MET A SD  1 
ATOM   49   C CE  . MET A 1 6   ? -16.33300 6.90900   -8.10700  1.000 48.13998  ? 6   MET A CE  1 
ATOM   50   N N   . ALA A 1 7   ? -17.54900 2.50600   -4.08600  1.000 36.79389  ? 7   ALA A N   1 
ATOM   51   C CA  . ALA A 1 7   ? -18.35900 2.84200   -2.90900  1.000 39.07574  ? 7   ALA A CA  1 
ATOM   52   C C   . ALA A 1 7   ? -18.03100 4.24800   -2.45600  1.000 46.20291  ? 7   ALA A C   1 
ATOM   53   O O   . ALA A 1 7   ? -16.98500 4.81800   -2.83500  1.000 38.08615  ? 7   ALA A O   1 
ATOM   54   C CB  . ALA A 1 7   ? -18.09500 1.85100   -1.78800  1.000 40.46275  ? 7   ALA A CB  1 
ATOM   55   N N   . PHE A 1 8   ? -18.94100 4.83100   -1.67500  1.000 39.82846  ? 8   PHE A N   1 
ATOM   56   C CA  . PHE A 1 8   ? -18.60400 6.09600   -1.02300  1.000 39.39420  ? 8   PHE A CA  1 
ATOM   57   C C   . PHE A 1 8   ? -17.58500 5.85400   0.08100   1.000 40.66540  ? 8   PHE A C   1 
ATOM   58   O O   . PHE A 1 8   ? -17.49200 4.76500   0.63600   1.000 39.70739  ? 8   PHE A O   1 
ATOM   59   C CB  . PHE A 1 8   ? -19.84800 6.78200   -0.44900  1.000 41.50498  ? 8   PHE A CB  1 
ATOM   60   C CG  . PHE A 1 8   ? -20.74100 7.32100   -1.50100  1.000 44.10529  ? 8   PHE A CG  1 
ATOM   61   C CD1 . PHE A 1 8   ? -20.48800 8.54500   -2.06400  1.000 45.80812  ? 8   PHE A CD1 1 
ATOM   62   C CD2 . PHE A 1 8   ? -21.86300 6.57600   -1.94300  1.000 44.03686  ? 8   PHE A CD2 1 
ATOM   63   C CE1 . PHE A 1 8   ? -21.31500 9.05000   -3.06800  1.000 50.09548  ? 8   PHE A CE1 1 
ATOM   64   C CE2 . PHE A 1 8   ? -22.70100 7.07600   -2.94000  1.000 42.60774  ? 8   PHE A CE2 1 
ATOM   65   C CZ  . PHE A 1 8   ? -22.41800 8.31700   -3.50200  1.000 48.99535  ? 8   PHE A CZ  1 
ATOM   66   N N   . PRO A 1 9   ? -16.75100 6.84800   0.38800   1.000 42.49983  ? 9   PRO A N   1 
ATOM   67   C CA  . PRO A 1 9   ? -15.83800 6.69400   1.52300   1.000 42.42351  ? 9   PRO A CA  1 
ATOM   68   C C   . PRO A 1 9   ? -16.64400 6.48600   2.79900   1.000 42.47615  ? 9   PRO A C   1 
ATOM   69   O O   . PRO A 1 9   ? -17.62500 7.16800   3.04500   1.000 43.23150  ? 9   PRO A O   1 
ATOM   70   C CB  . PRO A 1 9   ? -15.04300 8.01000   1.52500   1.000 44.66325  ? 9   PRO A CB  1 
ATOM   71   C CG  . PRO A 1 9   ? -15.19200 8.56400   0.09600   1.000 44.61588  ? 9   PRO A CG  1 
ATOM   72   C CD  . PRO A 1 9   ? -16.68000 8.17900   -0.20800  1.000 40.52854  ? 9   PRO A CD  1 
ATOM   73   N N   . SER A 1 10  ? -16.21900 5.53100   3.61400   1.000 44.09739  ? 10  SER A N   1 
ATOM   74   C CA  . SER A 1 10  ? -17.05100 5.03500   4.69600   1.000 40.34168  ? 10  SER A CA  1 
ATOM   75   C C   . SER A 1 10  ? -16.75500 5.70500   6.00000   1.000 44.45007  ? 10  SER A C   1 
ATOM   76   O O   . SER A 1 10  ? -17.41600 5.38300   6.98000   1.000 42.32086  ? 10  SER A O   1 
ATOM   77   C CB  . SER A 1 10  ? -16.85900 3.52600   4.86300   1.000 40.95228  ? 10  SER A CB  1 
ATOM   78   O OG  . SER A 1 10  ? -15.46800 3.22700   5.07600   1.000 44.61588  ? 10  SER A OG  1 
ATOM   79   N N   . GLY A 1 11  ? -15.79900 6.64700   6.03200   1.000 40.66014  ? 11  GLY A N   1 
ATOM   80   C CA  . GLY A 1 11  ? -15.37100 7.24400   7.30300   1.000 43.38152  ? 11  GLY A CA  1 
ATOM   81   C C   . GLY A 1 11  ? -16.50500 7.77800   8.17300   1.000 44.92644  ? 11  GLY A C   1 
ATOM   82   O O   . GLY A 1 11  ? -16.55200 7.51700   9.37700   1.000 46.60559  ? 11  GLY A O   1 
ATOM   83   N N   . LYS A 1 12  ? -17.40400 8.57200   7.58700   1.000 44.58429  ? 12  LYS A N   1 
ATOM   84   C CA  . LYS A 1 12  ? -18.49200 9.17900   8.35000   1.000 50.11127  ? 12  LYS A CA  1 
ATOM   85   C C   . LYS A 1 12  ? -19.44200 8.14100   8.94100   1.000 44.59482  ? 12  LYS A C   1 
ATOM   86   O O   . LYS A 1 12  ? -20.11300 8.43400   9.93000   1.000 49.41382  ? 12  LYS A O   1 
ATOM   87   C CB  . LYS A 1 12  ? -19.27100 10.16100  7.46300   1.000 50.30866  ? 12  LYS A CB  1 
ATOM   88   C CG  . LYS A 1 12  ? -18.43600 11.33400  6.99500   1.000 54.34073  ? 12  LYS A CG  1 
ATOM   89   C CD  . LYS A 1 12  ? -19.24000 12.24700  6.12700   1.000 58.32805  ? 12  LYS A CD  1 
ATOM   90   C CE  . LYS A 1 12  ? -18.49200 13.52900  5.86900   1.000 66.82643  ? 12  LYS A CE  1 
ATOM   91   N NZ  . LYS A 1 12  ? -17.08600 13.28300  5.40200   1.000 67.59495  ? 12  LYS A NZ  1 
ATOM   92   N N   . VAL A 1 13  ? -19.51600 6.95600   8.36000   1.000 43.19465  ? 13  VAL A N   1 
ATOM   93   C CA  . VAL A 1 13  ? -20.38400 5.89000   8.88600   1.000 45.30280  ? 13  VAL A CA  1 
ATOM   94   C C   . VAL A 1 13  ? -19.67300 5.00100   9.90200   1.000 45.02645  ? 13  VAL A C   1 
ATOM   95   O O   . VAL A 1 13  ? -20.29900 4.51200   10.86700  1.000 45.01066  ? 13  VAL A O   1 
ATOM   96   C CB  . VAL A 1 13  ? -20.91000 5.05900   7.70500   1.000 42.78934  ? 13  VAL A CB  1 
ATOM   97   C CG1 . VAL A 1 13  ? -21.82100 3.93800   8.22100   1.000 43.56312  ? 13  VAL A CG1 1 
ATOM   98   C CG2 . VAL A 1 13  ? -21.64400 5.96100   6.73300   1.000 43.40520  ? 13  VAL A CG2 1 
ATOM   99   N N   . GLU A 1 14  ? -18.35700 4.77900   9.71100   1.000 44.14477  ? 14  GLU A N   1 
ATOM   100  C CA  . GLU A 1 14  ? -17.60200 3.95700   10.64900  1.000 42.53668  ? 14  GLU A CA  1 
ATOM   101  C C   . GLU A 1 14  ? -17.73500 4.49700   12.05300  1.000 44.82380  ? 14  GLU A C   1 
ATOM   102  O O   . GLU A 1 14  ? -17.80200 3.73100   13.01300  1.000 48.88218  ? 14  GLU A O   1 
ATOM   103  C CB  . GLU A 1 14  ? -16.10300 3.91000   10.25100  1.000 43.64207  ? 14  GLU A CB  1 
ATOM   104  C CG  . GLU A 1 14  ? -15.87400 3.29200   8.83900   1.000 38.33091  ? 14  GLU A CG  1 
ATOM   105  C CD  . GLU A 1 14  ? -14.39400 3.56000   8.40200   1.000 46.40820  ? 14  GLU A CD  1 
ATOM   106  O OE1 . GLU A 1 14  ? -13.46900 3.45300   9.24100   1.000 47.17671  ? 14  GLU A OE1 1 
ATOM   107  O OE2 . GLU A 1 14  ? -14.21000 3.87800   7.23600   1.000 45.06593  ? 14  GLU A OE2 1 
ATOM   108  N N   . GLY A 1 15  ? -17.78000 5.81600   12.19100  1.000 44.12634  ? 15  GLY A N   1 
ATOM   109  C CA  . GLY A 1 15  ? -17.82300 6.44300   13.46500  1.000 49.60858  ? 15  GLY A CA  1 
ATOM   110  C C   . GLY A 1 15  ? -19.16200 6.33000   14.16200  1.000 48.03207  ? 15  GLY A C   1 
ATOM   111  O O   . GLY A 1 15  ? -19.32100 6.85700   15.24700  1.000 50.49553  ? 15  GLY A O   1 
ATOM   112  N N   . CYS A 1 16  ? -20.11600 5.69700   13.52700  1.000 45.84234  ? 16  CYS A N   1 
ATOM   113  C CA  . CYS A 1 16  ? -21.45600 5.51000   14.03700  1.000 45.53967  ? 16  CYS A CA  1 
ATOM   114  C C   . CYS A 1 16  ? -21.75400 4.06900   14.40900  1.000 49.10326  ? 16  CYS A C   1 
ATOM   115  O O   . CYS A 1 16  ? -22.84900 3.80000   14.94200  1.000 46.60822  ? 16  CYS A O   1 
ATOM   116  C CB  . CYS A 1 16  ? -22.47400 5.96100   12.99100  1.000 43.26571  ? 16  CYS A CB  1 
ATOM   117  S SG  . CYS A 1 16  ? -22.36200 7.66600   12.56900  1.000 49.92967  ? 16  CYS A SG  1 
ATOM   118  N N   . MET A 1 17  ? -20.84600 3.13200   14.13600  1.000 46.17922  ? 17  MET A N   1 
ATOM   119  C CA  . MET A 1 17  ? -21.16200 1.72500   14.35100  1.000 48.44265  ? 17  MET A CA  1 
ATOM   120  C C   . MET A 1 17  ? -20.86300 1.34200   15.78900  1.000 50.74293  ? 17  MET A C   1 
ATOM   121  O O   . MET A 1 17  ? -19.79300 1.67900   16.31000  1.000 51.59829  ? 17  MET A O   1 
ATOM   122  C CB  . MET A 1 17  ? -20.39800 0.81100   13.38600  1.000 44.83959  ? 17  MET A CB  1 
ATOM   123  C CG  . MET A 1 17  ? -20.66000 1.10000   11.93700  1.000 44.58956  ? 17  MET A CG  1 
ATOM   124  S SD  . MET A 1 17  ? -22.40400 1.27400   11.46700  1.000 45.65547  ? 17  MET A SD  1 
ATOM   125  C CE  . MET A 1 17  ? -22.98300 -0.34600  11.99800  1.000 43.70787  ? 17  MET A CE  1 
ATOM   126  N N   . VAL A 1 18  ? -21.84700 0.68900   16.44000  1.000 49.93230  ? 18  VAL A N   1 
ATOM   127  C CA  . VAL A 1 18  ? -21.71500 0.16000   17.78500  1.000 49.68490  ? 18  VAL A CA  1 
ATOM   128  C C   . VAL A 1 18  ? -22.12200 -1.30500  17.76700  1.000 48.70847  ? 18  VAL A C   1 
ATOM   129  O O   . VAL A 1 18  ? -22.61200 -1.83200  16.77200  1.000 47.34252  ? 18  VAL A O   1 
ATOM   130  C CB  . VAL A 1 18  ? -22.54800 0.94000   18.80700  1.000 51.96939  ? 18  VAL A CB  1 
ATOM   131  C CG1 . VAL A 1 18  ? -22.07300 2.36200   18.82700  1.000 53.79856  ? 18  VAL A CG1 1 
ATOM   132  C CG2 . VAL A 1 18  ? -24.04300 0.85900   18.46700  1.000 50.21918  ? 18  VAL A CG2 1 
ATOM   133  N N   . GLN A 1 19  ? -21.82000 -1.97100  18.85600  1.000 52.11151  ? 19  GLN A N   1 
ATOM   134  C CA  . GLN A 1 19  ? -22.18100 -3.35700  19.06300  1.000 49.76123  ? 19  GLN A CA  1 
ATOM   135  C C   . GLN A 1 19  ? -23.34400 -3.33800  20.04000  1.000 52.45366  ? 19  GLN A C   1 
ATOM   136  O O   . GLN A 1 19  ? -23.31000 -2.60100  21.02400  1.000 56.40413  ? 19  GLN A O   1 
ATOM   137  C CB  . GLN A 1 19  ? -20.99300 -4.15300  19.62800  1.000 53.24059  ? 19  GLN A CB  1 
ATOM   138  C CG  . GLN A 1 19  ? -21.21100 -5.67300  19.78000  1.000 60.91520  ? 19  GLN A CG  1 
ATOM   139  C CD  . GLN A 1 19  ? -19.93600 -6.43800  20.23800  1.000 64.80514  ? 19  GLN A CD  1 
ATOM   140  O OE1 . GLN A 1 19  ? -18.95400 -5.83600  20.68000  1.000 66.20004  ? 19  GLN A OE1 1 
ATOM   141  N NE2 . GLN A 1 19  ? -19.97500 -7.77600  20.13400  1.000 65.62366  ? 19  GLN A NE2 1 
ATOM   142  N N   . VAL A 1 20  ? -24.38500 -4.09900  19.74400  1.000 51.04033  ? 20  VAL A N   1 
ATOM   143  C CA  . VAL A 1 20  ? -25.51900 -4.23800  20.66400  1.000 51.63514  ? 20  VAL A CA  1 
ATOM   144  C C   . VAL A 1 20  ? -25.66600 -5.71200  20.99400  1.000 53.52747  ? 20  VAL A C   1 
ATOM   145  O O   . VAL A 1 20  ? -25.78900 -6.53500  20.08300  1.000 52.04045  ? 20  VAL A O   1 
ATOM   146  C CB  . VAL A 1 20  ? -26.83900 -3.70100  20.06400  1.000 51.02454  ? 20  VAL A CB  1 
ATOM   147  C CG1 . VAL A 1 20  ? -28.03700 -3.88100  21.12100  1.000 48.92429  ? 20  VAL A CG1 1 
ATOM   148  C CG2 . VAL A 1 20  ? -26.71100 -2.26500  19.58000  1.000 52.56683  ? 20  VAL A CG2 1 
ATOM   149  N N   . THR A 1 21  ? -25.74000 -6.03900  22.29400  1.000 57.93326  ? 21  THR A N   1 
ATOM   150  C CA  . THR A 1 21  ? -25.87300 -7.42300  22.75100  1.000 60.47304  ? 21  THR A CA  1 
ATOM   151  C C   . THR A 1 21  ? -27.01800 -7.57800  23.75400  1.000 61.07048  ? 21  THR A C   1 
ATOM   152  O O   . THR A 1 21  ? -27.15400 -6.76600  24.66600  1.000 63.94451  ? 21  THR A O   1 
ATOM   153  C CB  . THR A 1 21  ? -24.55000 -7.89800  23.39000  1.000 62.90228  ? 21  THR A CB  1 
ATOM   154  O OG1 . THR A 1 21  ? -23.49300 -7.61700  22.48700  1.000 63.81818  ? 21  THR A OG1 1 
ATOM   155  C CG2 . THR A 1 21  ? -24.55300 -9.40200  23.63300  1.000 66.72905  ? 21  THR A CG2 1 
ATOM   156  N N   . CYS A 1 22  ? -27.81000 -8.64500  23.59400  1.000 59.72295  ? 22  CYS A N   1 
ATOM   157  C CA  . CYS A 1 22  ? -28.89600 -9.04100  24.49300  1.000 66.55798  ? 22  CYS A CA  1 
ATOM   158  C C   . CYS A 1 22  ? -28.71300 -10.51400 24.78200  1.000 68.55032  ? 22  CYS A C   1 
ATOM   159  O O   . CYS A 1 22  ? -28.88600 -11.33800 23.87500  1.000 65.63419  ? 22  CYS A O   1 
ATOM   160  C CB  . CYS A 1 22  ? -30.26200 -8.83400  23.85900  1.000 71.31645  ? 22  CYS A CB  1 
ATOM   161  S SG  . CYS A 1 22  ? -30.75800 -7.14800  23.76700  1.000 75.89068  ? 22  CYS A SG  1 
ATOM   162  N N   . GLY A 1 23  ? -28.30900 -10.84200 26.00200  1.000 67.57652  ? 23  GLY A N   1 
ATOM   163  C CA  . GLY A 1 23  ? -28.03000 -12.22600 26.31800  1.000 65.35257  ? 23  GLY A CA  1 
ATOM   164  C C   . GLY A 1 23  ? -26.84800 -12.69900 25.50800  1.000 67.43440  ? 23  GLY A C   1 
ATOM   165  O O   . GLY A 1 23  ? -25.77500 -12.08500 25.54600  1.000 68.19765  ? 23  GLY A O   1 
ATOM   166  N N   . THR A 1 24  ? -27.02900 -13.75200 24.71700  1.000 68.03710  ? 24  THR A N   1 
ATOM   167  C CA  . THR A 1 24  ? -25.94800 -14.19200 23.85200  1.000 64.57616  ? 24  THR A CA  1 
ATOM   168  C C   . THR A 1 24  ? -26.10400 -13.72200 22.39400  1.000 68.72929  ? 24  THR A C   1 
ATOM   169  O O   . THR A 1 24  ? -25.25500 -14.06700 21.56000  1.000 68.31082  ? 24  THR A O   1 
ATOM   170  C CB  . THR A 1 24  ? -25.79200 -15.71800 23.87900  1.000 68.34240  ? 24  THR A CB  1 
ATOM   171  O OG1 . THR A 1 24  ? -27.01500 -16.35500 23.52400  1.000 69.19251  ? 24  THR A OG1 1 
ATOM   172  C CG2 . THR A 1 24  ? -25.35600 -16.20400 25.26000  1.000 62.54434  ? 24  THR A CG2 1 
ATOM   173  N N   . THR A 1 25  ? -27.13900 -12.93700 22.07400  1.000 62.63119  ? 25  THR A N   1 
ATOM   174  C CA  . THR A 1 25  ? -27.36100 -12.44000 20.72000  1.000 61.05732  ? 25  THR A CA  1 
ATOM   175  C C   . THR A 1 25  ? -26.68300 -11.08400 20.54300  1.000 59.89139  ? 25  THR A C   1 
ATOM   176  O O   . THR A 1 25  ? -26.95800 -10.14500 21.29700  1.000 59.53872  ? 25  THR A O   1 
ATOM   177  C CB  . THR A 1 25  ? -28.85900 -12.30700 20.44600  1.000 61.39684  ? 25  THR A CB  1 
ATOM   178  O OG1 . THR A 1 25  ? -29.48500 -13.56500 20.68900  1.000 63.46550  ? 25  THR A OG1 1 
ATOM   179  C CG2 . THR A 1 25  ? -29.11500 -11.85200 18.95500  1.000 53.78803  ? 25  THR A CG2 1 
ATOM   180  N N   . THR A 1 26  ? -25.82100 -10.96500 19.53200  1.000 54.03279  ? 26  THR A N   1 
ATOM   181  C CA  . THR A 1 26  ? -25.15300 -9.71000  19.28400  1.000 53.21954  ? 26  THR A CA  1 
ATOM   182  C C   . THR A 1 26  ? -25.32500 -9.34200  17.80200  1.000 54.24335  ? 26  THR A C   1 
ATOM   183  O O   . THR A 1 26  ? -25.50100 -10.20700 16.93400  1.000 53.69328  ? 26  THR A O   1 
ATOM   184  C CB  . THR A 1 26  ? -23.65700 -9.81600  19.69700  1.000 59.11498  ? 26  THR A CB  1 
ATOM   185  O OG1 . THR A 1 26  ? -23.08300 -8.51300  19.73800  1.000 61.21260  ? 26  THR A OG1 1 
ATOM   186  C CG2 . THR A 1 26  ? -22.86200 -10.63000 18.65900  1.000 58.84390  ? 26  THR A CG2 1 
ATOM   187  N N   . LEU A 1 27  ? -25.34800 -8.04900  17.52400  1.000 47.22935  ? 27  LEU A N   1 
ATOM   188  C CA  . LEU A 1 27  ? -25.36100 -7.57100  16.16500  1.000 48.96377  ? 27  LEU A CA  1 
ATOM   189  C C   . LEU A 1 27  ? -24.87000 -6.13100  16.22000  1.000 46.42399  ? 27  LEU A C   1 
ATOM   190  O O   . LEU A 1 27  ? -24.46700 -5.65600  17.29000  1.000 49.32960  ? 27  LEU A O   1 
ATOM   191  C CB  . LEU A 1 27  ? -26.75100 -7.73500  15.54600  1.000 46.07131  ? 27  LEU A CB  1 
ATOM   192  C CG  . LEU A 1 27  ? -28.02200 -7.38300  16.32200  1.000 45.78444  ? 27  LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? -28.00300 -5.89400  16.70100  1.000 46.99774  ? 27  LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? -29.20300 -7.71600  15.36400  1.000 44.24741  ? 27  LEU A CD2 1 
ATOM   195  N N   . ASN A 1 28  ? -24.98400 -5.41400  15.10300  1.000 44.20530  ? 28  ASN A N   1 
ATOM   196  C CA  . ASN A 1 28  ? -24.50000 -4.04900  15.02400  1.000 43.02358  ? 28  ASN A CA  1 
ATOM   197  C C   . ASN A 1 28  ? -25.61800 -3.04100  15.16500  1.000 46.26344  ? 28  ASN A C   1 
ATOM   198  O O   . ASN A 1 28  ? -26.75200 -3.29300  14.74700  1.000 44.66588  ? 28  ASN A O   1 
ATOM   199  C CB  . ASN A 1 28  ? -23.79600 -3.80800  13.69800  1.000 46.53453  ? 28  ASN A CB  1 
ATOM   200  C CG  . ASN A 1 28  ? -22.69900 -4.83700  13.44400  1.000 45.48177  ? 28  ASN A CG  1 
ATOM   201  O OD1 . ASN A 1 28  ? -21.60200 -4.71500  14.00500  1.000 46.57664  ? 28  ASN A OD1 1 
ATOM   202  N ND2 . ASN A 1 28  ? -22.98300 -5.83200  12.58900  1.000 40.72067  ? 28  ASN A ND2 1 
ATOM   203  N N   . GLY A 1 29  ? -25.26500 -1.87200  15.70900  1.000 44.04739  ? 29  GLY A N   1 
ATOM   204  C CA  . GLY A 1 29  ? -26.18800 -0.76400  15.78200  1.000 46.10026  ? 29  GLY A CA  1 
ATOM   205  C C   . GLY A 1 29  ? -25.59400 0.49700   15.20100  1.000 47.42148  ? 29  GLY A C   1 
ATOM   206  O O   . GLY A 1 29  ? -24.38600 0.60300   14.96600  1.000 46.70297  ? 29  GLY A O   1 
ATOM   207  N N   . LEU A 1 30  ? -26.47300 1.45500   14.93800  1.000 48.09524  ? 30  LEU A N   1 
ATOM   208  C CA  . LEU A 1 30  ? -26.09700 2.73300   14.32400  1.000 46.20028  ? 30  LEU A CA  1 
ATOM   209  C C   . LEU A 1 30  ? -26.39700 3.84100   15.32900  1.000 49.77439  ? 30  LEU A C   1 
ATOM   210  O O   . LEU A 1 30  ? -27.55800 4.00100   15.75600  1.000 45.63968  ? 30  LEU A O   1 
ATOM   211  C CB  . LEU A 1 30  ? -26.87100 2.93400   13.01000  1.000 42.21296  ? 30  LEU A CB  1 
ATOM   212  C CG  . LEU A 1 30  ? -26.54500 4.18800   12.23700  1.000 42.64459  ? 30  LEU A CG  1 
ATOM   213  C CD1 . LEU A 1 30  ? -25.20400 3.88700   11.55700  1.000 42.71038  ? 30  LEU A CD1 1 
ATOM   214  C CD2 . LEU A 1 30  ? -27.60900 4.57500   11.20500  1.000 42.76039  ? 30  LEU A CD2 1 
ATOM   215  N N   . TRP A 1 31  ? -25.33900 4.56800   15.75500  1.000 46.60822  ? 31  TRP A N   1 
ATOM   216  C CA  . TRP A 1 31  ? -25.38000 5.53400   16.86000  1.000 45.69232  ? 31  TRP A CA  1 
ATOM   217  C C   . TRP A 1 31  ? -25.38500 6.95000   16.28500  1.000 50.83241  ? 31  TRP A C   1 
ATOM   218  O O   . TRP A 1 31  ? -24.37300 7.39800   15.71200  1.000 50.87452  ? 31  TRP A O   1 
ATOM   219  C CB  . TRP A 1 31  ? -24.18400 5.29800   17.77800  1.000 47.13197  ? 31  TRP A CB  1 
ATOM   220  C CG  . TRP A 1 31  ? -24.06600 6.20200   19.03600  1.000 52.47998  ? 31  TRP A CG  1 
ATOM   221  C CD1 . TRP A 1 31  ? -25.07700 6.89700   19.70400  1.000 56.12778  ? 31  TRP A CD1 1 
ATOM   222  C CD2 . TRP A 1 31  ? -22.85700 6.49400   19.75400  1.000 55.56719  ? 31  TRP A CD2 1 
ATOM   223  N NE1 . TRP A 1 31  ? -24.54500 7.57900   20.77300  1.000 58.81231  ? 31  TRP A NE1 1 
ATOM   224  C CE2 . TRP A 1 31  ? -23.19100 7.35700   20.82000  1.000 58.52017  ? 31  TRP A CE2 1 
ATOM   225  C CE3 . TRP A 1 31  ? -21.51500 6.10500   19.59200  1.000 58.73599  ? 31  TRP A CE3 1 
ATOM   226  C CZ2 . TRP A 1 31  ? -22.23400 7.82400   21.73200  1.000 62.83122  ? 31  TRP A CZ2 1 
ATOM   227  C CZ3 . TRP A 1 31  ? -20.56500 6.58200   20.49700  1.000 58.58334  ? 31  TRP A CZ3 1 
ATOM   228  C CH2 . TRP A 1 31  ? -20.92600 7.43700   21.53800  1.000 62.52592  ? 31  TRP A CH2 1 
ATOM   229  N N   . LEU A 1 32  ? -26.54300 7.60600   16.34100  1.000 48.41107  ? 32  LEU A N   1 
ATOM   230  C CA  . LEU A 1 32  ? -26.75100 8.95900   15.83100  1.000 52.05624  ? 32  LEU A CA  1 
ATOM   231  C C   . LEU A 1 32  ? -27.35500 9.82200   16.93000  1.000 56.89893  ? 32  LEU A C   1 
ATOM   232  O O   . LEU A 1 32  ? -28.42600 9.50600   17.48500  1.000 52.69316  ? 32  LEU A O   1 
ATOM   233  C CB  . LEU A 1 32  ? -27.64000 8.94400   14.58200  1.000 48.50318  ? 32  LEU A CB  1 
ATOM   234  C CG  . LEU A 1 32  ? -27.11300 8.10000   13.41800  1.000 45.51862  ? 32  LEU A CG  1 
ATOM   235  C CD1 . LEU A 1 32  ? -28.21200 7.95300   12.35900  1.000 46.36345  ? 32  LEU A CD1 1 
ATOM   236  C CD2 . LEU A 1 32  ? -25.78200 8.64500   12.72600  1.000 46.91089  ? 32  LEU A CD2 1 
ATOM   237  N N   . ASP A 1 33  ? -26.66700 10.91200  17.25600  1.000 58.73862  ? 33  ASP A N   1 
ATOM   238  C CA  . ASP A 1 33  ? -27.04100 11.76100  18.38500  1.000 58.38332  ? 33  ASP A CA  1 
ATOM   239  C C   . ASP A 1 33  ? -27.11700 10.80500  19.56800  1.000 59.45976  ? 33  ASP A C   1 
ATOM   240  O O   . ASP A 1 33  ? -26.20600 9.97300   19.67500  1.000 56.63574  ? 33  ASP A O   1 
ATOM   241  C CB  . ASP A 1 33  ? -28.29600 12.55000  18.05000  1.000 62.51276  ? 33  ASP A CB  1 
ATOM   242  C CG  . ASP A 1 33  ? -28.08900 13.44300  16.80900  1.000 65.39995  ? 33  ASP A CG  1 
ATOM   243  O OD1 . ASP A 1 33  ? -27.01200 14.08200  16.73400  1.000 65.78684  ? 33  ASP A OD1 1 
ATOM   244  O OD2 . ASP A 1 33  ? -28.96500 13.48900  15.90200  1.000 67.05804  ? 33  ASP A OD2 1 
ATOM   245  N N   . ASP A 1 34  ? -28.20400 10.78900  20.35900  1.000 56.85945  ? 34  ASP A N   1 
ATOM   246  C CA  . ASP A 1 34  ? -28.25800 9.92600   21.53300  1.000 60.59937  ? 34  ASP A CA  1 
ATOM   247  C C   . ASP A 1 34  ? -29.15700 8.70500   21.34300  1.000 61.71793  ? 34  ASP A C   1 
ATOM   248  O O   . ASP A 1 34  ? -29.70800 8.18200   22.30900  1.000 60.55200  ? 34  ASP A O   1 
ATOM   249  C CB  . ASP A 1 34  ? -28.70000 10.70200  22.78400  1.000 65.05254  ? 34  ASP A CB  1 
ATOM   250  C CG  . ASP A 1 34  ? -30.08900 11.31000  22.65400  1.000 69.54518  ? 34  ASP A CG  1 
ATOM   251  O OD1 . ASP A 1 34  ? -30.65200 11.31300  21.52500  1.000 67.16332  ? 34  ASP A OD1 1 
ATOM   252  O OD2 . ASP A 1 34  ? -30.62800 11.73300  23.70100  1.000 70.11893  ? 34  ASP A OD2 1 
ATOM   253  N N   . VAL A 1 35  ? -29.27100 8.20900   20.12700  1.000 57.48321  ? 35  VAL A N   1 
ATOM   254  C CA  . VAL A 1 35  ? -30.05600 7.02500   19.82100  1.000 53.76960  ? 35  VAL A CA  1 
ATOM   255  C C   . VAL A 1 35  ? -29.20000 5.99200   19.09100  1.000 53.09321  ? 35  VAL A C   1 
ATOM   256  O O   . VAL A 1 35  ? -28.45300 6.32400   18.15000  1.000 50.58501  ? 35  VAL A O   1 
ATOM   257  C CB  . VAL A 1 35  ? -31.28200 7.38800   18.96500  1.000 54.93290  ? 35  VAL A CB  1 
ATOM   258  C CG1 . VAL A 1 35  ? -32.00000 6.13100   18.55600  1.000 53.77487  ? 35  VAL A CG1 1 
ATOM   259  C CG2 . VAL A 1 35  ? -32.22100 8.32200   19.72200  1.000 56.44098  ? 35  VAL A CG2 1 
ATOM   260  N N   . VAL A 1 36  ? -29.33900 4.72700   19.49800  1.000 50.46921  ? 36  VAL A N   1 
ATOM   261  C CA  . VAL A 1 36  ? -28.75600 3.60000   18.78000  1.000 49.31907  ? 36  VAL A CA  1 
ATOM   262  C C   . VAL A 1 36  ? -29.88600 2.85000   18.08100  1.000 50.97980  ? 36  VAL A C   1 
ATOM   263  O O   . VAL A 1 36  ? -30.84100 2.40000   18.73900  1.000 49.33749  ? 36  VAL A O   1 
ATOM   264  C CB  . VAL A 1 36  ? -27.96900 2.67200   19.72400  1.000 52.85371  ? 36  VAL A CB  1 
ATOM   265  C CG1 . VAL A 1 36  ? -27.58500 1.38600   19.00800  1.000 48.20841  ? 36  VAL A CG1 1 
ATOM   266  C CG2 . VAL A 1 36  ? -26.69600 3.38500   20.28300  1.000 53.23270  ? 36  VAL A CG2 1 
ATOM   267  N N   . TYR A 1 37  ? -29.78200 2.70100   16.76000  1.000 45.75812  ? 37  TYR A N   1 
ATOM   268  C CA  . TYR A 1 37  ? -30.76900 1.98600   15.94300  1.000 41.35496  ? 37  TYR A CA  1 
ATOM   269  C C   . TYR A 1 37  ? -30.24000 0.59200   15.62300  1.000 46.30818  ? 37  TYR A C   1 
ATOM   270  O O   . TYR A 1 37  ? -29.09800 0.46000   15.18300  1.000 46.12658  ? 37  TYR A O   1 
ATOM   271  C CB  . TYR A 1 37  ? -31.05000 2.72800   14.62600  1.000 44.96329  ? 37  TYR A CB  1 
ATOM   272  C CG  . TYR A 1 37  ? -31.49000 4.15900   14.79500  1.000 47.87679  ? 37  TYR A CG  1 
ATOM   273  C CD1 . TYR A 1 37  ? -30.56800 5.16000   15.14700  1.000 50.34814  ? 37  TYR A CD1 1 
ATOM   274  C CD2 . TYR A 1 37  ? -32.82500 4.53500   14.59600  1.000 50.96664  ? 37  TYR A CD2 1 
ATOM   275  C CE1 . TYR A 1 37  ? -30.96800 6.49400   15.32400  1.000 50.38762  ? 37  TYR A CE1 1 
ATOM   276  C CE2 . TYR A 1 37  ? -33.24000 5.86600   14.75900  1.000 49.04799  ? 37  TYR A CE2 1 
ATOM   277  C CZ  . TYR A 1 37  ? -32.31700 6.82800   15.12900  1.000 51.41406  ? 37  TYR A CZ  1 
ATOM   278  O OH  . TYR A 1 37  ? -32.72800 8.12500   15.29500  1.000 50.84294  ? 37  TYR A OH  1 
ATOM   279  N N   . CYS A 1 38  ? -31.06600 -0.44700  15.76600  1.000 44.35532  ? 38  CYS A N   1 
ATOM   280  C CA  . CYS A 1 38  ? -30.56800 -1.78200  15.43700  1.000 42.32613  ? 38  CYS A CA  1 
ATOM   281  C C   . CYS A 1 38  ? -31.73500 -2.69000  15.09700  1.000 44.40532  ? 38  CYS A C   1 
ATOM   282  O O   . CYS A 1 38  ? -32.88500 -2.42900  15.51700  1.000 44.51586  ? 38  CYS A O   1 
ATOM   283  C CB  . CYS A 1 38  ? -29.73700 -2.36800  16.59900  1.000 44.25267  ? 38  CYS A CB  1 
ATOM   284  S SG  . CYS A 1 38  ? -30.62700 -2.92100  18.03200  1.000 49.54278  ? 38  CYS A SG  1 
ATOM   285  N N   . PRO A 1 39  ? -31.47300 -3.82500  14.43100  1.000 42.09978  ? 39  PRO A N   1 
ATOM   286  C CA  . PRO A 1 39  ? -32.58400 -4.76300  14.17900  1.000 45.22121  ? 39  PRO A CA  1 
ATOM   287  C C   . PRO A 1 39  ? -33.18700 -5.30600  15.47100  1.000 46.87930  ? 39  PRO A C   1 
ATOM   288  O O   . PRO A 1 39  ? -32.48200 -5.64900  16.43600  1.000 45.45282  ? 39  PRO A O   1 
ATOM   289  C CB  . PRO A 1 39  ? -31.93300 -5.88000  13.37100  1.000 40.89174  ? 39  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 39  ? -30.68000 -5.17900  12.64000  1.000 38.25985  ? 39  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 39  ? -30.21000 -4.25700  13.78400  1.000 44.49218  ? 39  PRO A CD  1 
ATOM   292  N N   . ARG A 1 40  ? -34.51900 -5.36300  15.51000  1.000 46.24502  ? 40  ARG A N   1 
ATOM   293  C CA  . ARG A 1 40  ? -35.15600 -5.88100  16.70200  1.000 47.97680  ? 40  ARG A CA  1 
ATOM   294  C C   . ARG A 1 40  ? -34.87800 -7.36200  16.91400  1.000 48.77427  ? 40  ARG A C   1 
ATOM   295  O O   . ARG A 1 40  ? -35.09400 -7.86000  18.04000  1.000 53.14058  ? 40  ARG A O   1 
ATOM   296  C CB  . ARG A 1 40  ? -36.66000 -5.62000  16.65600  1.000 48.15051  ? 40  ARG A CB  1 
ATOM   297  C CG  . ARG A 1 40  ? -37.40800 -6.36900  15.54100  1.000 48.17420  ? 40  ARG A CG  1 
ATOM   298  C CD  . ARG A 1 40  ? -38.93400 -6.06100  15.63700  1.000 44.48691  ? 40  ARG A CD  1 
ATOM   299  N NE  . ARG A 1 40  ? -39.63800 -6.70900  14.52100  1.000 46.13448  ? 40  ARG A NE  1 
ATOM   300  C CZ  . ARG A 1 40  ? -40.96100 -6.80000  14.44700  1.000 48.46107  ? 40  ARG A CZ  1 
ATOM   301  N NH1 . ARG A 1 40  ? -41.73200 -6.27800  15.38500  1.000 46.99774  ? 40  ARG A NH1 1 
ATOM   302  N NH2 . ARG A 1 40  ? -41.51400 -7.44100  13.40900  1.000 47.52149  ? 40  ARG A NH2 1 
ATOM   303  N N   . ALA A 1 41  ? -34.32800 -8.04300  15.89800  1.000 48.41370  ? 41  ALA A N   1 
ATOM   304  C CA  . ALA A 1 41  ? -33.94800 -9.43800  16.01800  1.000 49.48751  ? 41  ALA A CA  1 
ATOM   305  C C   . ALA A 1 41  ? -32.95600 -9.67500  17.15200  1.000 50.08495  ? 41  ALA A C   1 
ATOM   306  O O   . ALA A 1 41  ? -32.78100 -10.82900 17.56200  1.000 52.31417  ? 41  ALA A O   1 
ATOM   307  C CB  . ALA A 1 41  ? -33.34800 -9.91900  14.70900  1.000 51.90359  ? 41  ALA A CB  1 
ATOM   308  N N   . VAL A 1 42  ? -32.31400 -8.62200  17.66600  1.000 40.92596  ? 42  VAL A N   1 
ATOM   309  C CA  . VAL A 1 42  ? -31.36300 -8.78000  18.77200  1.000 46.47399  ? 42  VAL A CA  1 
ATOM   310  C C   . VAL A 1 42  ? -32.02900 -9.21100  20.06900  1.000 57.12527  ? 42  VAL A C   1 
ATOM   311  O O   . VAL A 1 42  ? -31.36300 -9.76700  20.95200  1.000 53.94857  ? 42  VAL A O   1 
ATOM   312  C CB  . VAL A 1 42  ? -30.57800 -7.47800  18.98400  1.000 50.15338  ? 42  VAL A CB  1 
ATOM   313  C CG1 . VAL A 1 42  ? -31.45700 -6.40700  19.57900  1.000 50.14285  ? 42  VAL A CG1 1 
ATOM   314  C CG2 . VAL A 1 42  ? -29.32000 -7.72300  19.82700  1.000 54.89342  ? 42  VAL A CG2 1 
ATOM   315  N N   . ILE A 1 43  ? -33.33100 -8.94800  20.24000  1.000 55.49613  ? 43  ILE A N   1 
ATOM   316  C CA  . ILE A 1 43  ? -33.98800 -9.40200  21.46700  1.000 59.58346  ? 43  ILE A CA  1 
ATOM   317  C C   . ILE A 1 43  ? -34.48700 -10.83400 21.39200  1.000 61.18628  ? 43  ILE A C   1 
ATOM   318  O O   . ILE A 1 43  ? -35.05700 -11.32700 22.37000  1.000 60.59411  ? 43  ILE A O   1 
ATOM   319  C CB  . ILE A 1 43  ? -35.18200 -8.52200  21.88400  1.000 54.29072  ? 43  ILE A CB  1 
ATOM   320  C CG1 . ILE A 1 43  ? -36.32000 -8.59700  20.85800  1.000 54.47758  ? 43  ILE A CG1 1 
ATOM   321  C CG2 . ILE A 1 43  ? -34.75500 -7.12100  22.19000  1.000 57.45163  ? 43  ILE A CG2 1 
ATOM   322  C CD1 . ILE A 1 43  ? -37.57800 -7.77700  21.32600  1.000 59.72558  ? 43  ILE A CD1 1 
ATOM   323  N N   . CYS A 1 44  ? -34.28300 -11.51400 20.27400  1.000 59.67294  ? 44  CYS A N   1 
ATOM   324  C CA  . CYS A 1 44  ? -34.61500 -12.91700 20.12100  1.000 64.43667  ? 44  CYS A CA  1 
ATOM   325  C C   . CYS A 1 44  ? -33.54400 -13.81800 20.71300  1.000 69.32410  ? 44  CYS A C   1 
ATOM   326  O O   . CYS A 1 44  ? -32.35700 -13.47900 20.76300  1.000 75.84857  ? 44  CYS A O   1 
ATOM   327  C CB  . CYS A 1 44  ? -34.77500 -13.26800 18.65000  1.000 70.81639  ? 44  CYS A CB  1 
ATOM   328  S SG  . CYS A 1 44  ? -36.33200 -12.71500 18.00500  1.000 79.55164  ? 44  CYS A SG  1 
ATOM   329  N N   . THR A 1 45  ? -33.98400 -14.97200 21.15400  1.000 80.61493  ? 45  THR A N   1 
ATOM   330  C CA  . THR A 1 45  ? -33.15200 -16.08100 21.58200  1.000 87.09465  ? 45  THR A CA  1 
ATOM   331  C C   . THR A 1 45  ? -33.10100 -17.10600 20.45600  1.000 92.98220  ? 45  THR A C   1 
ATOM   332  O O   . THR A 1 45  ? -33.88700 -17.05500 19.50500  1.000 93.78493  ? 45  THR A O   1 
ATOM   333  C CB  . THR A 1 45  ? -33.72500 -16.70900 22.85400  1.000 88.84486  ? 45  THR A CB  1 
ATOM   334  O OG1 . THR A 1 45  ? -35.12200 -16.38900 22.93300  1.000 92.67953  ? 45  THR A OG1 1 
ATOM   335  C CG2 . THR A 1 45  ? -32.99800 -16.18200 24.08500  1.000 80.36227  ? 45  THR A CG2 1 
ATOM   336  N N   . SER A 1 46  ? -32.16000 -18.04500 20.56300  1.000 95.68516  ? 46  SER A N   1 
ATOM   337  C CA  . SER A 1 46  ? -32.06600 -19.08900 19.54900  1.000 101.80958 ? 46  SER A CA  1 
ATOM   338  C C   . SER A 1 46  ? -33.37700 -19.85900 19.38700  1.000 109.90528 ? 46  SER A C   1 
ATOM   339  O O   . SER A 1 46  ? -33.61400 -20.42500 18.31100  1.000 111.87657 ? 46  SER A O   1 
ATOM   340  C CB  . SER A 1 46  ? -30.91800 -20.04100 19.89400  1.000 108.42089 ? 46  SER A CB  1 
ATOM   341  O OG  . SER A 1 46  ? -29.70900 -19.32100 20.11400  1.000 100.89894 ? 46  SER A OG  1 
ATOM   342  N N   . GLU A 1 47  ? -34.25000 -19.85200 20.41200  1.000 110.34744 ? 47  GLU A N   1 
ATOM   343  C CA  . GLU A 1 47  ? -35.54700 -20.52700 20.38300  1.000 112.78194 ? 47  GLU A CA  1 
ATOM   344  C C   . GLU A 1 47  ? -36.67900 -19.64000 19.86800  1.000 114.32950 ? 47  GLU A C   1 
ATOM   345  O O   . GLU A 1 47  ? -37.65800 -20.16200 19.31600  1.000 116.12445 ? 47  GLU A O   1 
ATOM   346  C CB  . GLU A 1 47  ? -35.93400 -21.03500 21.77800  1.000 116.49555 ? 47  GLU A CB  1 
ATOM   347  C CG  . GLU A 1 47  ? -34.78700 -21.58100 22.61400  1.000 121.67775 ? 47  GLU A CG  1 
ATOM   348  C CD  . GLU A 1 47  ? -34.07100 -20.49700 23.40100  1.000 124.07014 ? 47  GLU A CD  1 
ATOM   349  O OE1 . GLU A 1 47  ? -34.70600 -19.89900 24.30400  1.000 120.84870 ? 47  GLU A OE1 1 
ATOM   350  O OE2 . GLU A 1 47  ? -32.88000 -20.23800 23.09800  1.000 116.41396 ? 47  GLU A OE2 1 
ATOM   351  N N   . ASP A 1 48  ? -36.57600 -18.32100 20.01000  1.000 117.22195 ? 48  ASP A N   1 
ATOM   352  C CA  . ASP A 1 48  ? -37.64500 -17.42900 19.54600  1.000 112.89248 ? 48  ASP A CA  1 
ATOM   353  C C   . ASP A 1 48  ? -37.32100 -16.84000 18.19200  1.000 108.44458 ? 48  ASP A C   1 
ATOM   354  O O   . ASP A 1 48  ? -37.47500 -15.63800 18.01700  1.000 116.58503 ? 48  ASP A O   1 
ATOM   355  C CB  . ASP A 1 48  ? -37.85800 -16.27200 20.52300  1.000 107.76818 ? 48  ASP A CB  1 
ATOM   356  C CG  . ASP A 1 48  ? -38.37800 -16.69600 21.86600  1.000 118.18259 ? 48  ASP A CG  1 
ATOM   357  O OD1 . ASP A 1 48  ? -39.55300 -17.13600 21.92800  1.000 122.79367 ? 48  ASP A OD1 1 
ATOM   358  O OD2 . ASP A 1 48  ? -37.63500 -16.52600 22.85800  1.000 118.99848 ? 48  ASP A OD2 1 
ATOM   359  N N   . MET A 1 49  ? -36.89900 -17.63000 17.20400  1.000 96.25891  ? 49  MET A N   1 
ATOM   360  C CA  . MET A 1 49  ? -36.65000 -17.04700 15.89400  1.000 82.92573  ? 49  MET A CA  1 
ATOM   361  C C   . MET A 1 49  ? -37.64200 -17.50800 14.83300  1.000 75.87225  ? 49  MET A C   1 
ATOM   362  O O   . MET A 1 49  ? -37.79200 -16.82100 13.81500  1.000 67.71601  ? 49  MET A O   1 
ATOM   363  C CB  . MET A 1 49  ? -35.19100 -17.31000 15.45700  1.000 78.74628  ? 49  MET A CB  1 
ATOM   364  C CG  . MET A 1 49  ? -34.12500 -16.51300 16.29900  1.000 79.42268  ? 49  MET A CG  1 
ATOM   365  S SD  . MET A 1 49  ? -32.42500 -16.24200 15.61800  1.000 97.54854  ? 49  MET A SD  1 
ATOM   366  C CE  . MET A 1 49  ? -31.50300 -17.71800 16.12400  1.000 85.15231  ? 49  MET A CE  1 
ATOM   367  N N   . LEU A 1 50  ? -38.39800 -18.58300 15.08900  1.000 78.70417  ? 50  LEU A N   1 
ATOM   368  C CA  . LEU A 1 50  ? -39.33900 -19.07700 14.08600  1.000 76.20387  ? 50  LEU A CA  1 
ATOM   369  C C   . LEU A 1 50  ? -40.62800 -18.25300 14.05500  1.000 81.14394  ? 50  LEU A C   1 
ATOM   370  O O   . LEU A 1 50  ? -41.14000 -17.93900 12.97700  1.000 78.87525  ? 50  LEU A O   1 
ATOM   371  C CB  . LEU A 1 50  ? -39.64100 -20.55800 14.33100  1.000 79.60428  ? 50  LEU A CB  1 
ATOM   372  C CG  . LEU A 1 50  ? -40.59300 -21.16400 13.29500  1.000 78.07515  ? 50  LEU A CG  1 
ATOM   373  C CD1 . LEU A 1 50  ? -39.90200 -21.22500 11.88700  1.000 72.25603  ? 50  LEU A CD1 1 
ATOM   374  C CD2 . LEU A 1 50  ? -41.09100 -22.53900 13.78500  1.000 78.99895  ? 50  LEU A CD2 1 
ATOM   375  N N   . ASN A 1 51  ? -41.21800 -17.96200 15.21900  1.000 89.97395  ? 51  ASN A N   1 
ATOM   376  C CA  . ASN A 1 51  ? -42.41000 -17.10500 15.30000  1.000 104.05458 ? 51  ASN A CA  1 
ATOM   377  C C   . ASN A 1 51  ? -42.36000 -16.27500 16.57300  1.000 97.96438  ? 51  ASN A C   1 
ATOM   378  O O   . ASN A 1 51  ? -43.16300 -16.45500 17.49700  1.000 91.67678  ? 51  ASN A O   1 
ATOM   379  C CB  . ASN A 1 51  ? -43.71600 -17.90400 15.18800  1.000 115.42437 ? 51  ASN A CB  1 
ATOM   380  C CG  . ASN A 1 51  ? -44.03300 -18.32100 13.73600  1.000 128.01009 ? 51  ASN A CG  1 
ATOM   381  O OD1 . ASN A 1 51  ? -44.09500 -17.47100 12.82600  1.000 115.15328 ? 51  ASN A OD1 1 
ATOM   382  N ND2 . ASN A 1 51  ? -44.23300 -19.62200 13.51800  1.000 126.67308 ? 51  ASN A ND2 1 
ATOM   383  N N   . PRO A 1 52  ? -41.45800 -15.30900 16.62200  1.000 81.54399  ? 52  PRO A N   1 
ATOM   384  C CA  . PRO A 1 52  ? -41.33500 -14.45500 17.80300  1.000 74.58789  ? 52  PRO A CA  1 
ATOM   385  C C   . PRO A 1 52  ? -42.44900 -13.42900 17.84700  1.000 66.92908  ? 52  PRO A C   1 
ATOM   386  O O   . PRO A 1 52  ? -42.87100 -12.89000 16.82500  1.000 66.85802  ? 52  PRO A O   1 
ATOM   387  C CB  . PRO A 1 52  ? -39.98800 -13.76200 17.57600  1.000 72.09285  ? 52  PRO A CB  1 
ATOM   388  C CG  . PRO A 1 52  ? -39.91900 -13.66100 16.06400  1.000 74.51683  ? 52  PRO A CG  1 
ATOM   389  C CD  . PRO A 1 52  ? -40.58900 -14.87500 15.51400  1.000 74.34049  ? 52  PRO A CD  1 
ATOM   390  N N   . ASN A 1 53  ? -42.92400 -13.13800 19.04700  1.000 59.00971  ? 53  ASN A N   1 
ATOM   391  C CA  . ASN A 1 53  ? -43.81200 -11.99700 19.23700  1.000 58.18856  ? 53  ASN A CA  1 
ATOM   392  C C   . ASN A 1 53  ? -42.95400 -10.90800 19.83500  1.000 55.76721  ? 53  ASN A C   1 
ATOM   393  O O   . ASN A 1 53  ? -42.63100 -10.94700 21.02300  1.000 58.59650  ? 53  ASN A O   1 
ATOM   394  C CB  . ASN A 1 53  ? -45.01900 -12.29100 20.14100  1.000 60.32039  ? 53  ASN A CB  1 
ATOM   395  C CG  . ASN A 1 53  ? -45.95500 -11.10600 20.15800  1.000 64.08400  ? 53  ASN A CG  1 
ATOM   396  O OD1 . ASN A 1 53  ? -45.68900 -10.14200 20.87000  1.000 62.72331  ? 53  ASN A OD1 1 
ATOM   397  N ND2 . ASN A 1 53  ? -46.99600 -11.11600 19.31000  1.000 69.08460  ? 53  ASN A ND2 1 
ATOM   398  N N   . TYR A 1 54  ? -42.50400 -9.97900  18.99400  1.000 58.38068  ? 54  TYR A N   1 
ATOM   399  C CA  . TYR A 1 54  ? -41.52300 -9.01500  19.45900  1.000 56.90945  ? 54  TYR A CA  1 
ATOM   400  C C   . TYR A 1 54  ? -42.08400 -8.05100  20.50300  1.000 58.97286  ? 54  TYR A C   1 
ATOM   401  O O   . TYR A 1 54  ? -41.32100 -7.55100  21.34000  1.000 58.29120  ? 54  TYR A O   1 
ATOM   402  C CB  . TYR A 1 54  ? -40.97300 -8.24000  18.27900  1.000 52.69579  ? 54  TYR A CB  1 
ATOM   403  C CG  . TYR A 1 54  ? -40.06300 -9.02400  17.37500  1.000 53.79856  ? 54  TYR A CG  1 
ATOM   404  C CD1 . TYR A 1 54  ? -38.71900 -9.19700  17.69600  1.000 52.59052  ? 54  TYR A CD1 1 
ATOM   405  C CD2 . TYR A 1 54  ? -40.52300 -9.54100  16.15500  1.000 54.34599  ? 54  TYR A CD2 1 
ATOM   406  C CE1 . TYR A 1 54  ? -37.86400 -9.87200  16.86200  1.000 51.17719  ? 54  TYR A CE1 1 
ATOM   407  C CE2 . TYR A 1 54  ? -39.61800 -10.21100 15.26400  1.000 50.79030  ? 54  TYR A CE2 1 
ATOM   408  C CZ  . TYR A 1 54  ? -38.30700 -10.39100 15.67200  1.000 50.82451  ? 54  TYR A CZ  1 
ATOM   409  O OH  . TYR A 1 54  ? -37.38800 -11.03500 14.88800  1.000 53.04847  ? 54  TYR A OH  1 
ATOM   410  N N   . GLU A 1 55  ? -43.38100 -7.74400  20.45000  1.000 58.44648  ? 55  GLU A N   1 
ATOM   411  C CA  . GLU A 1 55  ? -43.97000 -6.90000  21.49400  1.000 61.80741  ? 55  GLU A CA  1 
ATOM   412  C C   . GLU A 1 55  ? -43.79200 -7.53400  22.88300  1.000 60.80203  ? 55  GLU A C   1 
ATOM   413  O O   . GLU A 1 55  ? -43.31500 -6.88200  23.82600  1.000 56.54625  ? 55  GLU A O   1 
ATOM   414  C CB  . GLU A 1 55  ? -45.43600 -6.62800  21.16100  1.000 59.84139  ? 55  GLU A CB  1 
ATOM   415  C CG  . GLU A 1 55  ? -46.06600 -5.57500  22.09000  1.000 74.31681  ? 55  GLU A CG  1 
ATOM   416  C CD  . GLU A 1 55  ? -47.51700 -5.18800  21.75900  1.000 81.93877  ? 55  GLU A CD  1 
ATOM   417  O OE1 . GLU A 1 55  ? -48.18200 -5.86700  20.93900  1.000 102.74916 ? 55  GLU A OE1 1 
ATOM   418  O OE2 . GLU A 1 55  ? -47.98400 -4.18700  22.34300  1.000 76.75920  ? 55  GLU A OE2 1 
ATOM   419  N N   . ASP A 1 56  ? -44.07600 -8.83500  22.99300  1.000 59.16236  ? 56  ASP A N   1 
ATOM   420  C CA  . ASP A 1 56  ? -43.85600 -9.60500  24.22400  1.000 64.47615  ? 56  ASP A CA  1 
ATOM   421  C C   . ASP A 1 56  ? -42.39400 -9.58300  24.65600  1.000 64.58669  ? 56  ASP A C   1 
ATOM   422  O O   . ASP A 1 56  ? -42.07000 -9.33500  25.83300  1.000 60.21775  ? 56  ASP A O   1 
ATOM   423  C CB  . ASP A 1 56  ? -44.24900 -11.06000 23.97200  1.000 67.28701  ? 56  ASP A CB  1 
ATOM   424  C CG  . ASP A 1 56  ? -45.64500 -11.39900 24.40300  1.000 69.97155  ? 56  ASP A CG  1 
ATOM   425  O OD1 . ASP A 1 56  ? -46.29100 -10.60900 25.12500  1.000 69.15303  ? 56  ASP A OD1 1 
ATOM   426  O OD2 . ASP A 1 56  ? -46.08900 -12.48200 23.97200  1.000 84.38117  ? 56  ASP A OD2 1 
ATOM   427  N N   . LEU A 1 57  ? -41.50100 -9.95000  23.73000  1.000 59.19920  ? 57  LEU A N   1 
ATOM   428  C CA  . LEU A 1 57  ? -40.08700 -10.05400 24.05600  1.000 59.62557  ? 57  LEU A CA  1 
ATOM   429  C C   . LEU A 1 57  ? -39.56300 -8.73500  24.61000  1.000 60.68886  ? 57  LEU A C   1 
ATOM   430  O O   . LEU A 1 57  ? -38.78700 -8.71500  25.58400  1.000 63.06809  ? 57  LEU A O   1 
ATOM   431  C CB  . LEU A 1 57  ? -39.32700 -10.47900 22.79000  1.000 55.24347  ? 57  LEU A CB  1 
ATOM   432  C CG  . LEU A 1 57  ? -39.69200 -11.90700 22.35800  1.000 58.33331  ? 57  LEU A CG  1 
ATOM   433  C CD1 . LEU A 1 57  ? -39.07200 -12.34700 21.01000  1.000 63.43655  ? 57  LEU A CD1 1 
ATOM   434  C CD2 . LEU A 1 57  ? -39.38100 -12.90600 23.51100  1.000 64.78145  ? 57  LEU A CD2 1 
ATOM   435  N N   . LEU A 1 58  ? -40.05000 -7.62000  24.05000  1.000 56.10410  ? 58  LEU A N   1 
ATOM   436  C CA  . LEU A 1 58  ? -39.59900 -6.29300  24.45500  1.000 59.99930  ? 58  LEU A CA  1 
ATOM   437  C C   . LEU A 1 58  ? -40.13000 -5.89100  25.82800  1.000 59.74401  ? 58  LEU A C   1 
ATOM   438  O O   . LEU A 1 58  ? -39.38500 -5.32500  26.65100  1.000 59.74401  ? 58  LEU A O   1 
ATOM   439  C CB  . LEU A 1 58  ? -40.01100 -5.27900  23.38900  1.000 54.54075  ? 58  LEU A CB  1 
ATOM   440  C CG  . LEU A 1 58  ? -39.36900 -3.92200  23.52900  1.000 58.80705  ? 58  LEU A CG  1 
ATOM   441  C CD1 . LEU A 1 58  ? -37.83900 -4.10900  23.66500  1.000 60.62043  ? 58  LEU A CD1 1 
ATOM   442  C CD2 . LEU A 1 58  ? -39.64000 -3.19600  22.19300  1.000 58.04643  ? 58  LEU A CD2 1 
ATOM   443  N N   . ILE A 1 59  ? -41.41300 -6.19200  26.12800  1.000 61.95216  ? 59  ILE A N   1 
ATOM   444  C CA  . ILE A 1 59  ? -41.91900 -5.85800  27.45800  1.000 59.92034  ? 59  ILE A CA  1 
ATOM   445  C C   . ILE A 1 59  ? -41.15600 -6.63800  28.51800  1.000 60.59411  ? 59  ILE A C   1 
ATOM   446  O O   . ILE A 1 59  ? -41.08500 -6.22200  29.67900  1.000 66.51850  ? 59  ILE A O   1 
ATOM   447  C CB  . ILE A 1 59  ? -43.44300 -6.10100  27.65000  1.000 63.18126  ? 59  ILE A CB  1 
ATOM   448  C CG1 . ILE A 1 59  ? -44.30300 -5.27100  26.70500  1.000 71.81124  ? 59  ILE A CG1 1 
ATOM   449  C CG2 . ILE A 1 59  ? -43.88300 -5.64000  29.04700  1.000 57.60164  ? 59  ILE A CG2 1 
ATOM   450  C CD1 . ILE A 1 59  ? -45.78600 -5.67000  26.81500  1.000 73.21667  ? 59  ILE A CD1 1 
ATOM   451  N N   . ARG A 1 60  ? -40.66400 -7.82000  28.18000  1.000 59.08340  ? 60  ARG A N   1 
ATOM   452  C CA  . ARG A 1 60  ? -39.92800 -8.55800  29.19000  1.000 63.61552  ? 60  ARG A CA  1 
ATOM   453  C C   . ARG A 1 60  ? -38.51500 -8.07800  29.39400  1.000 61.08101  ? 60  ARG A C   1 
ATOM   454  O O   . ARG A 1 60  ? -37.86400 -8.61600  30.30100  1.000 65.89211  ? 60  ARG A O   1 
ATOM   455  C CB  . ARG A 1 60  ? -39.90700 -10.03600 28.84900  1.000 65.35257  ? 60  ARG A CB  1 
ATOM   456  C CG  . ARG A 1 60  ? -41.26000 -10.57200 28.85500  1.000 56.95946  ? 60  ARG A CG  1 
ATOM   457  C CD  . ARG A 1 60  ? -41.32400 -11.88900 28.21100  1.000 63.79186  ? 60  ARG A CD  1 
ATOM   458  N NE  . ARG A 1 60  ? -42.68200 -12.34500 28.36500  1.000 57.89378  ? 60  ARG A NE  1 
ATOM   459  C CZ  . ARG A 1 60  ? -43.39400 -12.97600 27.44300  1.000 61.88110  ? 60  ARG A CZ  1 
ATOM   460  N NH1 . ARG A 1 60  ? -42.85300 -13.35900 26.30500  1.000 72.47185  ? 60  ARG A NH1 1 
ATOM   461  N NH2 . ARG A 1 60  ? -44.68600 -13.25000 27.70000  1.000 69.31884  ? 60  ARG A NH2 1 
ATOM   462  N N   . LYS A 1 61  ? -38.04600 -7.06500  28.66100  1.000 62.92860  ? 61  LYS A N   1 
ATOM   463  C CA  . LYS A 1 61  ? -36.71000 -6.54400  28.88600  1.000 68.38451  ? 61  LYS A CA  1 
ATOM   464  C C   . LYS A 1 61  ? -36.79300 -5.17600  29.55500  1.000 68.60296  ? 61  LYS A C   1 
ATOM   465  O O   . LYS A 1 61  ? -37.79900 -4.47800  29.46500  1.000 68.06079  ? 61  LYS A O   1 
ATOM   466  C CB  . LYS A 1 61  ? -35.90200 -6.42000  27.57900  1.000 65.02622  ? 61  LYS A CB  1 
ATOM   467  C CG  . LYS A 1 61  ? -35.81200 -7.70500  26.72800  1.000 67.90551  ? 61  LYS A CG  1 
ATOM   468  C CD  . LYS A 1 61  ? -34.39100 -8.06000  26.32700  1.000 70.21631  ? 61  LYS A CD  1 
ATOM   469  C CE  . LYS A 1 61  ? -34.21300 -9.57900  26.23100  1.000 70.43213  ? 61  LYS A CE  1 
ATOM   470  N NZ  . LYS A 1 61  ? -34.90700 -10.15000 25.02600  1.000 69.55834  ? 61  LYS A NZ  1 
ATOM   471  N N   . SER A 1 62  ? -35.68300 -4.78100  30.18100  1.000 70.70058  ? 62  SER A N   1 
ATOM   472  C CA  . SER A 1 62  ? -35.44500 -3.42500  30.67600  1.000 69.84258  ? 62  SER A CA  1 
ATOM   473  C C   . SER A 1 62  ? -34.17400 -2.87600  30.03200  1.000 69.33463  ? 62  SER A C   1 
ATOM   474  O O   . SER A 1 62  ? -33.45300 -3.59100  29.33900  1.000 69.29252  ? 62  SER A O   1 
ATOM   475  C CB  . SER A 1 62  ? -35.29700 -3.39100  32.18900  1.000 72.01916  ? 62  SER A CB  1 
ATOM   476  O OG  . SER A 1 62  ? -34.44400 -4.45800  32.54600  1.000 77.20663  ? 62  SER A OG  1 
ATOM   477  N N   . ASN A 1 63  ? -33.90800 -1.59100  30.29900  1.000 67.93709  ? 63  ASN A N   1 
ATOM   478  C CA  . ASN A 1 63  ? -32.74400 -0.91500  29.74600  1.000 67.71601  ? 63  ASN A CA  1 
ATOM   479  C C   . ASN A 1 63  ? -31.46800 -1.70500  30.00000  1.000 69.33463  ? 63  ASN A C   1 
ATOM   480  O O   . ASN A 1 63  ? -30.64500 -1.86000  29.09000  1.000 73.20878  ? 63  ASN A O   1 
ATOM   481  C CB  . ASN A 1 63  ? -32.62700 0.49200   30.34000  1.000 69.83206  ? 63  ASN A CB  1 
ATOM   482  C CG  . ASN A 1 63  ? -33.72000 1.45200   29.84300  1.000 71.22696  ? 63  ASN A CG  1 
ATOM   483  O OD1 . ASN A 1 63  ? -34.26200 1.30700   28.72700  1.000 71.50068  ? 63  ASN A OD1 1 
ATOM   484  N ND2 . ASN A 1 63  ? -34.01000 2.46700   30.64800  1.000 62.72068  ? 63  ASN A ND2 1 
ATOM   485  N N   . HIS A 1 64  ? -31.31600 -2.28500  31.19900  1.000 71.30855  ? 64  HIS A N   1 
ATOM   486  C CA  . HIS A 1 64  ? -30.06500 -2.97400  31.50900  1.000 68.15028  ? 64  HIS A CA  1 
ATOM   487  C C   . HIS A 1 64  ? -29.89700 -4.28500  30.76400  1.000 71.90862  ? 64  HIS A C   1 
ATOM   488  O O   . HIS A 1 64  ? -28.76900 -4.77700  30.68300  1.000 76.43285  ? 64  HIS A O   1 
ATOM   489  C CB  . HIS A 1 64  ? -29.90600 -3.21200  33.01100  1.000 69.83995  ? 64  HIS A CB  1 
ATOM   490  C CG  . HIS A 1 64  ? -30.82200 -4.25900  33.59400  1.000 75.01163  ? 64  HIS A CG  1 
ATOM   491  N ND1 . HIS A 1 64  ? -30.52600 -5.60900  33.59000  1.000 77.15925  ? 64  HIS A ND1 1 
ATOM   492  C CD2 . HIS A 1 64  ? -32.00600 -4.14100  34.24200  1.000 74.40366  ? 64  HIS A CD2 1 
ATOM   493  C CE1 . HIS A 1 64  ? -31.49200 -6.27800  34.19700  1.000 73.40880  ? 64  HIS A CE1 1 
ATOM   494  N NE2 . HIS A 1 64  ? -32.40300 -5.41000  34.60100  1.000 76.05912  ? 64  HIS A NE2 1 
ATOM   495  N N   . ASN A 1 65  ? -30.93300 -4.79600  30.10600  1.000 71.88230  ? 65  ASN A N   1 
ATOM   496  C CA  . ASN A 1 65  ? -30.73700 -5.98800  29.28900  1.000 73.09824  ? 65  ASN A CA  1 
ATOM   497  C C   . ASN A 1 65  ? -30.04600 -5.71000  27.96500  1.000 69.15303  ? 65  ASN A C   1 
ATOM   498  O O   . ASN A 1 65  ? -29.76400 -6.67600  27.25400  1.000 68.31082  ? 65  ASN A O   1 
ATOM   499  C CB  . ASN A 1 65  ? -32.05800 -6.70700  29.00700  1.000 70.66637  ? 65  ASN A CB  1 
ATOM   500  C CG  . ASN A 1 65  ? -32.72100 -7.20200  30.25200  1.000 72.84558  ? 65  ASN A CG  1 
ATOM   501  O OD1 . ASN A 1 65  ? -33.94500 -7.15700  30.39000  1.000 76.43285  ? 65  ASN A OD1 1 
ATOM   502  N ND2 . ASN A 1 65  ? -31.92100 -7.69500  31.18400  1.000 77.09872  ? 65  ASN A ND2 1 
ATOM   503  N N   . PHE A 1 66  ? -29.78300 -4.43400  27.61400  1.000 69.49254  ? 66  PHE A N   1 
ATOM   504  C CA  . PHE A 1 66  ? -29.12200 -4.04000  26.35900  1.000 66.67115  ? 66  PHE A CA  1 
ATOM   505  C C   . PHE A 1 66  ? -27.71400 -3.51000  26.64000  1.000 70.30580  ? 66  PHE A C   1 
ATOM   506  O O   . PHE A 1 66  ? -27.54800 -2.43200  27.22300  1.000 72.90348  ? 66  PHE A O   1 
ATOM   507  C CB  . PHE A 1 66  ? -29.93500 -2.96900  25.63000  1.000 63.64447  ? 66  PHE A CB  1 
ATOM   508  C CG  . PHE A 1 66  ? -31.29900 -3.41800  25.20300  1.000 62.94439  ? 66  PHE A CG  1 
ATOM   509  C CD1 . PHE A 1 66  ? -31.50400 -4.00500  23.97800  1.000 61.04679  ? 66  PHE A CD1 1 
ATOM   510  C CD2 . PHE A 1 66  ? -32.38100 -3.21300  26.01700  1.000 61.21260  ? 66  PHE A CD2 1 
ATOM   511  C CE1 . PHE A 1 66  ? -32.75500 -4.41000  23.57900  1.000 62.65225  ? 66  PHE A CE1 1 
ATOM   512  C CE2 . PHE A 1 66  ? -33.63900 -3.62500  25.63700  1.000 64.45510  ? 66  PHE A CE2 1 
ATOM   513  C CZ  . PHE A 1 66  ? -33.82800 -4.22400  24.41200  1.000 61.62055  ? 66  PHE A CZ  1 
ATOM   514  N N   . LEU A 1 67  ? -26.70400 -4.23800  26.20900  1.000 64.72618  ? 67  LEU A N   1 
ATOM   515  C CA  . LEU A 1 67  ? -25.32100 -3.83400  26.39500  1.000 67.57916  ? 67  LEU A CA  1 
ATOM   516  C C   . LEU A 1 67  ? -24.82900 -3.23600  25.07600  1.000 65.33678  ? 67  LEU A C   1 
ATOM   517  O O   . LEU A 1 67  ? -24.78800 -3.92600  24.05200  1.000 63.49709  ? 67  LEU A O   1 
ATOM   518  C CB  . LEU A 1 67  ? -24.51100 -5.03900  26.86700  1.000 74.66422  ? 67  LEU A CB  1 
ATOM   519  C CG  . LEU A 1 67  ? -22.98800 -4.99400  26.76300  1.000 79.33583  ? 67  LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 67  ? -22.43600 -3.96100  27.72700  1.000 81.32817  ? 67  LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 67  ? -22.40300 -6.37700  27.02300  1.000 80.10697  ? 67  LEU A CD2 1 
ATOM   522  N N   . VAL A 1 68  ? -24.54000 -1.93500  25.07500  1.000 66.26058  ? 68  VAL A N   1 
ATOM   523  C CA  . VAL A 1 68  ? -24.11500 -1.20900  23.88000  1.000 64.84198  ? 68  VAL A CA  1 
ATOM   524  C C   . VAL A 1 68  ? -22.65300 -0.78900  24.04400  1.000 68.30819  ? 68  VAL A C   1 
ATOM   525  O O   . VAL A 1 68  ? -22.27900 -0.22200  25.07900  1.000 73.98519  ? 68  VAL A O   1 
ATOM   526  C CB  . VAL A 1 68  ? -25.04300 -0.00600  23.62200  1.000 63.98662  ? 68  VAL A CB  1 
ATOM   527  C CG1 . VAL A 1 68  ? -24.63300 0.81400   22.40800  1.000 61.74425  ? 68  VAL A CG1 1 
ATOM   528  C CG2 . VAL A 1 68  ? -26.49500 -0.50300  23.46500  1.000 61.97059  ? 68  VAL A CG2 1 
ATOM   529  N N   . GLN A 1 69  ? -21.83000 -1.07300  23.03200  1.000 64.03926  ? 69  GLN A N   1 
ATOM   530  C CA  . GLN A 1 69  ? -20.39800 -0.79900  23.09600  1.000 69.05038  ? 69  GLN A CA  1 
ATOM   531  C C   . GLN A 1 69  ? -19.94500 -0.05000  21.85400  1.000 64.78145  ? 69  GLN A C   1 
ATOM   532  O O   . GLN A 1 69  ? -20.15300 -0.51700  20.72600  1.000 55.50402  ? 69  GLN A O   1 
ATOM   533  C CB  . GLN A 1 69  ? -19.59100 -2.08300  23.25000  1.000 70.11104  ? 69  GLN A CB  1 
ATOM   534  C CG  . GLN A 1 69  ? -19.89600 -2.86000  24.47400  1.000 78.32255  ? 69  GLN A CG  1 
ATOM   535  C CD  . GLN A 1 69  ? -19.26600 -4.22000  24.43000  1.000 92.99536  ? 69  GLN A CD  1 
ATOM   536  O OE1 . GLN A 1 69  ? -19.96700 -5.22800  24.38600  1.000 100.89631 ? 69  GLN A OE1 1 
ATOM   537  N NE2 . GLN A 1 69  ? -17.93000 -4.26300  24.41000  1.000 94.07444  ? 69  GLN A NE2 1 
ATOM   538  N N   . ALA A 1 70  ? -19.37900 1.13000   22.08300  1.000 62.74963  ? 70  ALA A N   1 
ATOM   539  C CA  . ALA A 1 70  ? -18.69700 1.94500   21.08300  1.000 69.51360  ? 70  ALA A CA  1 
ATOM   540  C C   . ALA A 1 70  ? -17.21700 1.69600   21.34000  1.000 72.67977  ? 70  ALA A C   1 
ATOM   541  O O   . ALA A 1 70  ? -16.60300 2.31900   22.21300  1.000 73.09824  ? 70  ALA A O   1 
ATOM   542  C CB  . ALA A 1 70  ? -19.08600 3.41500   21.20800  1.000 69.75310  ? 70  ALA A CB  1 
ATOM   543  N N   . GLY A 1 71  ? -16.67600 0.70600   20.63200  1.000 74.03256  ? 71  GLY A N   1 
ATOM   544  C CA  . GLY A 1 71  ? -15.36200 0.17500   20.92000  1.000 76.69077  ? 71  GLY A CA  1 
ATOM   545  C C   . GLY A 1 71  ? -15.43900 -0.60300  22.20900  1.000 84.56803  ? 71  GLY A C   1 
ATOM   546  O O   . GLY A 1 71  ? -16.25800 -1.52100  22.35500  1.000 82.59148  ? 71  GLY A O   1 
ATOM   547  N N   . ASN A 1 72  ? -14.62700 -0.20100  23.18000  1.000 93.33224  ? 72  ASN A N   1 
ATOM   548  C CA  . ASN A 1 72  ? -14.75900 -0.71600  24.53600  1.000 96.94847  ? 72  ASN A CA  1 
ATOM   549  C C   . ASN A 1 72  ? -15.58100 0.19200   25.43500  1.000 91.62414  ? 72  ASN A C   1 
ATOM   550  O O   . ASN A 1 72  ? -16.00400 -0.25300  26.50700  1.000 94.90875  ? 72  ASN A O   1 
ATOM   551  C CB  . ASN A 1 72  ? -13.38100 -0.92100  25.16400  1.000 101.01211 ? 72  ASN A CB  1 
ATOM   552  C CG  . ASN A 1 72  ? -12.31200 -0.15200  24.43500  1.000 106.99178 ? 72  ASN A CG  1 
ATOM   553  O OD1 . ASN A 1 72  ? -12.17300 1.05800   24.61700  1.000 114.19001 ? 72  ASN A OD1 1 
ATOM   554  N ND2 . ASN A 1 72  ? -11.54700 -0.84400  23.60000  1.000 109.73947 ? 72  ASN A ND2 1 
ATOM   555  N N   . VAL A 1 73  ? -15.79000 1.45400   25.04600  1.000 85.76555  ? 73  VAL A N   1 
ATOM   556  C CA  . VAL A 1 73  ? -16.58700 2.35100   25.87400  1.000 82.28355  ? 73  VAL A CA  1 
ATOM   557  C C   . VAL A 1 73  ? -18.01700 1.83300   25.89800  1.000 81.03866  ? 73  VAL A C   1 
ATOM   558  O O   . VAL A 1 73  ? -18.67100 1.69400   24.85600  1.000 76.91185  ? 73  VAL A O   1 
ATOM   559  C CB  . VAL A 1 73  ? -16.51300 3.79500   25.36200  1.000 79.10685  ? 73  VAL A CB  1 
ATOM   560  C CG1 . VAL A 1 73  ? -17.45200 4.68900   26.19000  1.000 78.29097  ? 73  VAL A CG1 1 
ATOM   561  C CG2 . VAL A 1 73  ? -15.09200 4.31500   25.42000  1.000 75.66170  ? 73  VAL A CG2 1 
ATOM   562  N N   . GLN A 1 74  ? -18.50400 1.52100   27.08800  1.000 83.10733  ? 74  GLN A N   1 
ATOM   563  C CA  . GLN A 1 74  ? -19.85200 1.01100   27.25400  1.000 85.23390  ? 74  GLN A CA  1 
ATOM   564  C C   . GLN A 1 74  ? -20.81800 2.18900   27.33500  1.000 84.98124  ? 74  GLN A C   1 
ATOM   565  O O   . GLN A 1 74  ? -20.58000 3.15200   28.07700  1.000 85.53131  ? 74  GLN A O   1 
ATOM   566  C CB  . GLN A 1 74  ? -19.91800 0.13900   28.50800  1.000 90.89511  ? 74  GLN A CB  1 
ATOM   567  C CG  . GLN A 1 74  ? -20.96200 -0.94700  28.49800  1.000 91.87154  ? 74  GLN A CG  1 
ATOM   568  C CD  . GLN A 1 74  ? -22.19000 -0.57300  29.30700  1.000 104.74677 ? 74  GLN A CD  1 
ATOM   569  O OE1 . GLN A 1 74  ? -22.63900 0.57100   29.25500  1.000 117.36144 ? 74  GLN A OE1 1 
ATOM   570  N NE2 . GLN A 1 74  ? -22.72700 -1.52500  30.07700  1.000 100.07779 ? 74  GLN A NE2 1 
ATOM   571  N N   . LEU A 1 75  ? -21.90300 2.10800   26.57500  1.000 79.92537  ? 75  LEU A N   1 
ATOM   572  C CA  . LEU A 1 75  ? -22.90600 3.16100   26.52800  1.000 79.14370  ? 75  LEU A CA  1 
ATOM   573  C C   . LEU A 1 75  ? -24.10900 2.74800   27.35900  1.000 80.17540  ? 75  LEU A C   1 
ATOM   574  O O   . LEU A 1 75  ? -24.60500 1.61600   27.24800  1.000 79.17002  ? 75  LEU A O   1 
ATOM   575  C CB  . LEU A 1 75  ? -23.32700 3.48300   25.08900  1.000 76.60919  ? 75  LEU A CB  1 
ATOM   576  C CG  . LEU A 1 75  ? -22.61100 4.65300   24.38400  1.000 76.05912  ? 75  LEU A CG  1 
ATOM   577  C CD1 . LEU A 1 75  ? -21.20200 4.92200   24.91700  1.000 82.02036  ? 75  LEU A CD1 1 
ATOM   578  C CD2 . LEU A 1 75  ? -22.54400 4.45900   22.88900  1.000 67.00014  ? 75  LEU A CD2 1 
ATOM   579  N N   . ARG A 1 76  ? -24.54500 3.64800   28.22200  1.000 77.99883  ? 76  ARG A N   1 
ATOM   580  C CA  . ARG A 1 76  ? -25.65300 3.35900   29.11100  1.000 75.25376  ? 76  ARG A CA  1 
ATOM   581  C C   . ARG A 1 76  ? -26.95500 3.64100   28.36700  1.000 71.10589  ? 76  ARG A C   1 
ATOM   582  O O   . ARG A 1 76  ? -27.15800 4.74500   27.85700  1.000 70.77691  ? 76  ARG A O   1 
ATOM   583  C CB  . ARG A 1 76  ? -25.50400 4.17800   30.39900  1.000 77.76196  ? 76  ARG A CB  1 
ATOM   584  C CG  . ARG A 1 76  ? -26.75900 4.87100   30.92800  1.000 78.96473  ? 76  ARG A CG  1 
ATOM   585  C CD  . ARG A 1 76  ? -26.53300 5.53200   32.28700  1.000 79.53848  ? 76  ARG A CD  1 
ATOM   586  N NE  . ARG A 1 76  ? -27.04800 4.67800   33.34400  1.000 85.41287  ? 76  ARG A NE  1 
ATOM   587  C CZ  . ARG A 1 76  ? -28.23800 4.82600   33.91500  1.000 91.31621  ? 76  ARG A CZ  1 
ATOM   588  N NH1 . ARG A 1 76  ? -29.05800 5.80100   33.56000  1.000 92.40318  ? 76  ARG A NH1 1 
ATOM   589  N NH2 . ARG A 1 76  ? -28.60500 3.98700   34.88400  1.000 95.60620  ? 76  ARG A NH2 1 
ATOM   590  N N   . VAL A 1 77  ? -27.81000 2.62600   28.27900  1.000 68.72140  ? 77  VAL A N   1 
ATOM   591  C CA  . VAL A 1 77  ? -29.14000 2.76300   27.68500  1.000 72.74293  ? 77  VAL A CA  1 
ATOM   592  C C   . VAL A 1 77  ? -30.10700 3.35300   28.71100  1.000 70.82165  ? 77  VAL A C   1 
ATOM   593  O O   . VAL A 1 77  ? -30.22200 2.86400   29.84600  1.000 69.84522  ? 77  VAL A O   1 
ATOM   594  C CB  . VAL A 1 77  ? -29.63500 1.40800   27.15100  1.000 67.93972  ? 77  VAL A CB  1 
ATOM   595  C CG1 . VAL A 1 77  ? -31.04600 1.52800   26.60700  1.000 66.56324  ? 77  VAL A CG1 1 
ATOM   596  C CG2 . VAL A 1 77  ? -28.68600 0.91200   26.04200  1.000 63.51551  ? 77  VAL A CG2 1 
ATOM   597  N N   . ILE A 1 78  ? -30.80200 4.42300   28.32200  1.000 69.08986  ? 78  ILE A N   1 
ATOM   598  C CA  . ILE A 1 78  ? -31.70300 5.12400   29.22600  1.000 70.98746  ? 78  ILE A CA  1 
ATOM   599  C C   . ILE A 1 78  ? -33.13300 5.15000   28.71600  1.000 70.14262  ? 78  ILE A C   1 
ATOM   600  O O   . ILE A 1 78  ? -33.97700 5.83700   29.29500  1.000 65.92106  ? 78  ILE A O   1 
ATOM   601  C CB  . ILE A 1 78  ? -31.19900 6.55200   29.50200  1.000 75.80383  ? 78  ILE A CB  1 
ATOM   602  C CG1 . ILE A 1 78  ? -31.09200 7.31600   28.17400  1.000 72.26393  ? 78  ILE A CG1 1 
ATOM   603  C CG2 . ILE A 1 78  ? -29.84000 6.49900   30.18600  1.000 75.51432  ? 78  ILE A CG2 1 
ATOM   604  C CD1 . ILE A 1 78  ? -30.80000 8.80700   28.31200  1.000 74.93793  ? 78  ILE A CD1 1 
ATOM   605  N N   . GLY A 1 79  ? -33.43600 4.36300   27.68700  1.000 69.23988  ? 79  GLY A N   1 
ATOM   606  C CA  . GLY A 1 79  ? -34.76600 4.27600   27.11400  1.000 63.13652  ? 79  GLY A CA  1 
ATOM   607  C C   . GLY A 1 79  ? -34.75000 3.35500   25.91300  1.000 62.15482  ? 79  GLY A C   1 
ATOM   608  O O   . GLY A 1 79  ? -33.73000 3.22900   25.21600  1.000 66.30532  ? 79  GLY A O   1 
ATOM   609  N N   . HIS A 1 80  ? -35.86900 2.70200   25.63600  1.000 62.89438  ? 80  HIS A N   1 
ATOM   610  C CA  . HIS A 1 80  ? -35.93300 1.78600   24.50700  1.000 60.17827  ? 80  HIS A CA  1 
ATOM   611  C C   . HIS A 1 80  ? -37.33800 1.80400   23.95200  1.000 60.73097  ? 80  HIS A C   1 
ATOM   612  O O   . HIS A 1 80  ? -38.31700 1.86700   24.70700  1.000 58.21751  ? 80  HIS A O   1 
ATOM   613  C CB  . HIS A 1 80  ? -35.51200 0.35200   24.89300  1.000 59.09919  ? 80  HIS A CB  1 
ATOM   614  C CG  . HIS A 1 80  ? -36.32300 -0.25300  26.01400  1.000 62.71541  ? 80  HIS A CG  1 
ATOM   615  N ND1 . HIS A 1 80  ? -35.88100 -0.25300  27.32100  1.000 63.43919  ? 80  HIS A ND1 1 
ATOM   616  C CD2 . HIS A 1 80  ? -37.52900 -0.88200  26.03000  1.000 61.94427  ? 80  HIS A CD2 1 
ATOM   617  C CE1 . HIS A 1 80  ? -36.78000 -0.84900  28.09400  1.000 68.41083  ? 80  HIS A CE1 1 
ATOM   618  N NE2 . HIS A 1 80  ? -37.77700 -1.25400  27.33000  1.000 68.89247  ? 80  HIS A NE2 1 
ATOM   619  N N   . SER A 1 81  ? -37.42700 1.66800   22.63700  1.000 53.40377  ? 81  SER A N   1 
ATOM   620  C CA  . SER A 1 81  ? -38.70900 1.56600   21.94800  1.000 55.56192  ? 81  SER A CA  1 
ATOM   621  C C   . SER A 1 81  ? -38.53400 0.77500   20.65900  1.000 56.40150  ? 81  SER A C   1 
ATOM   622  O O   . SER A 1 81  ? -37.41300 0.57200   20.15700  1.000 54.97238  ? 81  SER A O   1 
ATOM   623  C CB  . SER A 1 81  ? -39.32100 2.95200   21.65100  1.000 56.58836  ? 81  SER A CB  1 
ATOM   624  O OG  . SER A 1 81  ? -38.50400 3.73600   20.76600  1.000 59.25710  ? 81  SER A OG  1 
ATOM   625  N N   . MET A 1 82  ? -39.65800 0.33000   20.11500  1.000 53.99858  ? 82  MET A N   1 
ATOM   626  C CA  . MET A 1 82  ? -39.67000 -0.43400  18.87600  1.000 54.67761  ? 82  MET A CA  1 
ATOM   627  C C   . MET A 1 82  ? -40.47700 0.31800   17.82200  1.000 56.05672  ? 82  MET A C   1 
ATOM   628  O O   . MET A 1 82  ? -41.60400 0.73400   18.07700  1.000 54.69866  ? 82  MET A O   1 
ATOM   629  C CB  . MET A 1 82  ? -40.24600 -1.82200  19.09100  1.000 53.69854  ? 82  MET A CB  1 
ATOM   630  C CG  . MET A 1 82  ? -40.24800 -2.60300  17.86100  1.000 54.65392  ? 82  MET A CG  1 
ATOM   631  S SD  . MET A 1 82  ? -40.73500 -4.27800  18.16300  1.000 54.95659  ? 82  MET A SD  1 
ATOM   632  C CE  . MET A 1 82  ? -42.35100 -4.05500  19.00400  1.000 50.35077  ? 82  MET A CE  1 
ATOM   633  N N   . GLN A 1 83  ? -39.87100 0.54400   16.67800  1.000 48.27947  ? 83  GLN A N   1 
ATOM   634  C CA  . GLN A 1 83  ? -40.50100 1.12600   15.48800  1.000 51.89306  ? 83  GLN A CA  1 
ATOM   635  C C   . GLN A 1 83  ? -40.41700 0.10400   14.36000  1.000 50.77451  ? 83  GLN A C   1 
ATOM   636  O O   . GLN A 1 83  ? -39.33600 -0.09500  13.78700  1.000 49.51910  ? 83  GLN A O   1 
ATOM   637  C CB  . GLN A 1 83  ? -39.79400 2.44300   15.09200  1.000 54.12228  ? 83  GLN A CB  1 
ATOM   638  C CG  . GLN A 1 83  ? -40.43300 3.11300   13.89000  1.000 57.81746  ? 83  GLN A CG  1 
ATOM   639  C CD  . GLN A 1 83  ? -39.81700 4.44600   13.40700  1.000 60.38619  ? 83  GLN A CD  1 
ATOM   640  O OE1 . GLN A 1 83  ? -38.68000 4.79100   13.69500  1.000 56.34623  ? 83  GLN A OE1 1 
ATOM   641  N NE2 . GLN A 1 83  ? -40.62700 5.21200   12.69200  1.000 63.57341  ? 83  GLN A NE2 1 
ATOM   642  N N   . ASN A 1 84  ? -41.54100 -0.53700  14.01000  1.000 47.95575  ? 84  ASN A N   1 
ATOM   643  C CA  . ASN A 1 84  ? -41.57900 -1.55400  12.93900  1.000 47.45306  ? 84  ASN A CA  1 
ATOM   644  C C   . ASN A 1 84  ? -40.52100 -2.59500  13.29300  1.000 48.79796  ? 84  ASN A C   1 
ATOM   645  O O   . ASN A 1 84  ? -40.55400 -3.06600  14.43300  1.000 43.66050  ? 84  ASN A O   1 
ATOM   646  C CB  . ASN A 1 84  ? -41.42500 -0.92900  11.53900  1.000 46.54769  ? 84  ASN A CB  1 
ATOM   647  C CG  . ASN A 1 84  ? -42.51500 0.06100   11.25200  1.000 52.37470  ? 84  ASN A CG  1 
ATOM   648  O OD1 . ASN A 1 84  ? -43.70500 -0.23500  11.48100  1.000 50.66397  ? 84  ASN A OD1 1 
ATOM   649  N ND2 . ASN A 1 84  ? -42.13600 1.26000   10.85600  1.000 49.87440  ? 84  ASN A ND2 1 
ATOM   650  N N   . CYS A 1 85  ? -39.53100 -2.88300  12.41800  1.000 45.26332  ? 85  CYS A N   1 
ATOM   651  C CA  . CYS A 1 85  ? -38.57000 -3.94700  12.71900  1.000 44.72115  ? 85  CYS A CA  1 
ATOM   652  C C   . CYS A 1 85  ? -37.26300 -3.42600  13.31600  1.000 46.67139  ? 85  CYS A C   1 
ATOM   653  O O   . CYS A 1 85  ? -36.29900 -4.19800  13.42700  1.000 45.32122  ? 85  CYS A O   1 
ATOM   654  C CB  . CYS A 1 85  ? -38.27200 -4.76400  11.48600  1.000 46.53189  ? 85  CYS A CB  1 
ATOM   655  S SG  . CYS A 1 85  ? -39.77700 -5.52700  10.88800  1.000 45.36333  ? 85  CYS A SG  1 
ATOM   656  N N   . VAL A 1 86  ? -37.19900 -2.15000  13.73400  1.000 44.34216  ? 86  VAL A N   1 
ATOM   657  C CA  . VAL A 1 86  ? -35.97900 -1.69300  14.38400  1.000 43.68945  ? 86  VAL A CA  1 
ATOM   658  C C   . VAL A 1 86  ? -36.25600 -1.25700  15.81000  1.000 47.58992  ? 86  VAL A C   1 
ATOM   659  O O   . VAL A 1 86  ? -37.38200 -0.92400  16.22000  1.000 49.67438  ? 86  VAL A O   1 
ATOM   660  C CB  . VAL A 1 86  ? -35.23600 -0.56500  13.63300  1.000 41.70500  ? 86  VAL A CB  1 
ATOM   661  C CG1 . VAL A 1 86  ? -34.82700 -1.01200  12.18100  1.000 43.43416  ? 86  VAL A CG1 1 
ATOM   662  C CG2 . VAL A 1 86  ? -36.03800 0.71200   13.66300  1.000 49.45593  ? 86  VAL A CG2 1 
ATOM   663  N N   . LEU A 1 87  ? -35.22700 -1.39300  16.62100  1.000 48.59004  ? 87  LEU A N   1 
ATOM   664  C CA  . LEU A 1 87  ? -35.26100 -0.87700  17.97800  1.000 47.51096  ? 87  LEU A CA  1 
ATOM   665  C C   . LEU A 1 87  ? -34.51200 0.43700   18.00000  1.000 50.27971  ? 87  LEU A C   1 
ATOM   666  O O   . LEU A 1 87  ? -33.50600 0.59300   17.31000  1.000 48.82954  ? 87  LEU A O   1 
ATOM   667  C CB  . LEU A 1 87  ? -34.58400 -1.80400  18.95100  1.000 49.44803  ? 87  LEU A CB  1 
ATOM   668  C CG  . LEU A 1 87  ? -35.05800 -3.19100  19.22000  1.000 54.34862  ? 87  LEU A CG  1 
ATOM   669  C CD1 . LEU A 1 87  ? -34.14900 -3.70000  20.32400  1.000 56.86734  ? 87  LEU A CD1 1 
ATOM   670  C CD2 . LEU A 1 87  ? -36.55000 -3.13600  19.71200  1.000 53.50905  ? 87  LEU A CD2 1 
ATOM   671  N N   . LYS A 1 88  ? -34.98000 1.34100   18.82600  1.000 50.79293  ? 88  LYS A N   1 
ATOM   672  C CA  . LYS A 1 88  ? -34.34300 2.61000   19.13500  1.000 52.80107  ? 88  LYS A CA  1 
ATOM   673  C C   . LYS A 1 88  ? -33.94900 2.57500   20.60700  1.000 56.68048  ? 88  LYS A C   1 
ATOM   674  O O   . LYS A 1 88  ? -34.80500 2.42900   21.51100  1.000 53.30639  ? 88  LYS A O   1 
ATOM   675  C CB  . LYS A 1 88  ? -35.27600 3.77000   18.81700  1.000 54.80657  ? 88  LYS A CB  1 
ATOM   676  C CG  . LYS A 1 88  ? -35.70700 3.74700   17.36700  1.000 54.42231  ? 88  LYS A CG  1 
ATOM   677  C CD  . LYS A 1 88  ? -36.24800 5.09200   16.89100  1.000 56.07778  ? 88  LYS A CD  1 
ATOM   678  C CE  . LYS A 1 88  ? -37.71800 5.19000   17.11000  1.000 63.19968  ? 88  LYS A CE  1 
ATOM   679  N NZ  . LYS A 1 88  ? -38.17400 6.48100   16.55200  1.000 69.56360  ? 88  LYS A NZ  1 
ATOM   680  N N   . LEU A 1 89  ? -32.65100 2.56800   20.85000  1.000 52.50630  ? 89  LEU A N   1 
ATOM   681  C CA  . LEU A 1 89  ? -32.13800 2.54300   22.22200  1.000 58.15171  ? 89  LEU A CA  1 
ATOM   682  C C   . LEU A 1 89  ? -31.59900 3.93100   22.54200  1.000 59.37554  ? 89  LEU A C   1 
ATOM   683  O O   . LEU A 1 89  ? -30.59200 4.36900   21.95000  1.000 55.25399  ? 89  LEU A O   1 
ATOM   684  C CB  . LEU A 1 89  ? -31.05500 1.47600   22.36800  1.000 58.01748  ? 89  LEU A CB  1 
ATOM   685  C CG  . LEU A 1 89  ? -31.54300 0.08900   21.97100  1.000 56.80155  ? 89  LEU A CG  1 
ATOM   686  C CD1 . LEU A 1 89  ? -30.43600 -0.92700  22.00700  1.000 56.63047  ? 89  LEU A CD1 1 
ATOM   687  C CD2 . LEU A 1 89  ? -32.62100 -0.30300  22.90400  1.000 58.66230  ? 89  LEU A CD2 1 
ATOM   688  N N   . LYS A 1 90  ? -32.29900 4.63800   23.41900  1.000 59.32553  ? 90  LYS A N   1 
ATOM   689  C CA  . LYS A 1 90  ? -31.83500 5.92800   23.89700  1.000 64.73671  ? 90  LYS A CA  1 
ATOM   690  C C   . LYS A 1 90  ? -30.64900 5.71200   24.82700  1.000 66.26058  ? 90  LYS A C   1 
ATOM   691  O O   . LYS A 1 90  ? -30.68800 4.82700   25.67800  1.000 65.82105  ? 90  LYS A O   1 
ATOM   692  C CB  . LYS A 1 90  ? -32.95900 6.66400   24.61400  1.000 67.59495  ? 90  LYS A CB  1 
ATOM   693  C CG  . LYS A 1 90  ? -32.54400 8.02800   25.12800  1.000 73.01928  ? 90  LYS A CG  1 
ATOM   694  C CD  . LYS A 1 90  ? -32.32300 9.01200   23.98800  1.000 78.00409  ? 90  LYS A CD  1 
ATOM   695  C CE  . LYS A 1 90  ? -33.60200 9.81200   23.66800  1.000 93.72176  ? 90  LYS A CE  1 
ATOM   696  N NZ  . LYS A 1 90  ? -33.33400 10.88700  22.65100  1.000 90.24766  ? 90  LYS A NZ  1 
ATOM   697  N N   . VAL A 1 91  ? -29.56300 6.47000   24.61200  1.000 69.01091  ? 91  VAL A N   1 
ATOM   698  C CA  . VAL A 1 91  ? -28.34500 6.34700   25.40600  1.000 68.15554  ? 91  VAL A CA  1 
ATOM   699  C C   . VAL A 1 91  ? -28.01100 7.69600   26.04600  1.000 70.33738  ? 91  VAL A C   1 
ATOM   700  O O   . VAL A 1 91  ? -28.51000 8.74900   25.64700  1.000 68.26871  ? 91  VAL A O   1 
ATOM   701  C CB  . VAL A 1 91  ? -27.16000 5.80500   24.56400  1.000 68.77140  ? 91  VAL A CB  1 
ATOM   702  C CG1 . VAL A 1 91  ? -27.43900 4.37200   24.13800  1.000 65.54733  ? 91  VAL A CG1 1 
ATOM   703  C CG2 . VAL A 1 91  ? -26.84000 6.68500   23.35100  1.000 59.22815  ? 91  VAL A CG2 1 
ATOM   704  N N   . ASP A 1 92  ? -27.16400 7.64200   27.07800  1.000 77.00923  ? 92  ASP A N   1 
ATOM   705  C CA  . ASP A 1 92  ? -26.80700 8.81000   27.88700  1.000 77.73037  ? 92  ASP A CA  1 
ATOM   706  C C   . ASP A 1 92  ? -25.77000 9.70600   27.22200  1.000 79.54638  ? 92  ASP A C   1 
ATOM   707  O O   . ASP A 1 92  ? -25.52100 10.81400  27.72100  1.000 82.53358  ? 92  ASP A O   1 
ATOM   708  C CB  . ASP A 1 92  ? -26.29400 8.36500   29.26300  1.000 81.77296  ? 92  ASP A CB  1 
ATOM   709  C CG  . ASP A 1 92  ? -24.96600 7.62000   29.18300  1.000 81.98878  ? 92  ASP A CG  1 
ATOM   710  O OD1 . ASP A 1 92  ? -24.58200 7.14500   28.08800  1.000 81.43871  ? 92  ASP A OD1 1 
ATOM   711  O OD2 . ASP A 1 92  ? -24.33300 7.46400   30.25400  1.000 91.28200  ? 92  ASP A OD2 1 
ATOM   712  N N   . THR A 1 93  ? -25.10300 9.21000   26.17700  1.000 72.29814  ? 93  THR A N   1 
ATOM   713  C CA  . THR A 1 93  ? -24.05000 9.92100   25.45900  1.000 72.18760  ? 93  THR A CA  1 
ATOM   714  C C   . THR A 1 93  ? -24.50200 10.15800  24.02600  1.000 67.05541  ? 93  THR A C   1 
ATOM   715  O O   . THR A 1 93  ? -24.82800 9.20900   23.31600  1.000 63.77344  ? 93  THR A O   1 
ATOM   716  C CB  . THR A 1 93  ? -22.75400 9.10100   25.46400  1.000 69.19777  ? 93  THR A CB  1 
ATOM   717  O OG1 . THR A 1 93  ? -22.48600 8.65100   26.79300  1.000 77.54614  ? 93  THR A OG1 1 
ATOM   718  C CG2 . THR A 1 93  ? -21.57300 9.90600   24.93400  1.000 71.50857  ? 93  THR A CG2 1 
ATOM   719  N N   . ALA A 1 94  ? -24.49900 11.40300  23.58900  1.000 64.10505  ? 94  ALA A N   1 
ATOM   720  C CA  . ALA A 1 94  ? -24.71900 11.66300  22.18000  1.000 62.03375  ? 94  ALA A CA  1 
ATOM   721  C C   . ALA A 1 94  ? -23.41400 11.36300  21.44300  1.000 61.53106  ? 94  ALA A C   1 
ATOM   722  O O   . ALA A 1 94  ? -22.33600 11.64700  21.96500  1.000 62.71541  ? 94  ALA A O   1 
ATOM   723  C CB  . ALA A 1 94  ? -25.16800 13.11000  21.97200  1.000 60.78887  ? 94  ALA A CB  1 
ATOM   724  N N   . ASN A 1 95  ? -23.50600 10.68500  20.27000  1.000 57.14896  ? 95  ASN A N   1 
ATOM   725  C CA  . ASN A 1 95  ? -22.32500 10.36500  19.44900  1.000 58.25172  ? 95  ASN A CA  1 
ATOM   726  C C   . ASN A 1 95  ? -21.64800 11.64700  18.98300  1.000 58.27541  ? 95  ASN A C   1 
ATOM   727  O O   . ASN A 1 95  ? -22.20900 12.36400  18.15000  1.000 59.97561  ? 95  ASN A O   1 
ATOM   728  C CB  . ASN A 1 95  ? -22.73600 9.50300   18.24400  1.000 56.19358  ? 95  ASN A CB  1 
ATOM   729  C CG  . ASN A 1 95  ? -21.54900 8.99400   17.40900  1.000 56.49625  ? 95  ASN A CG  1 
ATOM   730  O OD1 . ASN A 1 95  ? -20.38800 9.41000   17.61400  1.000 56.56731  ? 95  ASN A OD1 1 
ATOM   731  N ND2 . ASN A 1 95  ? -21.85800 8.13000   16.39300  1.000 49.91388  ? 95  ASN A ND2 1 
ATOM   732  N N   . PRO A 1 96  ? -20.44400 11.96800  19.46900  1.000 57.19370  ? 96  PRO A N   1 
ATOM   733  C CA  . PRO A 1 96  ? -19.76000 13.18900  18.98200  1.000 58.28067  ? 96  PRO A CA  1 
ATOM   734  C C   . PRO A 1 96  ? -19.38500 13.14100  17.50300  1.000 58.27278  ? 96  PRO A C   1 
ATOM   735  O O   . PRO A 1 96  ? -19.16400 14.20100  16.91100  1.000 61.70213  ? 96  PRO A O   1 
ATOM   736  C CB  . PRO A 1 96  ? -18.51200 13.27200  19.86500  1.000 59.62820  ? 96  PRO A CB  1 
ATOM   737  C CG  . PRO A 1 96  ? -18.23200 11.82100  20.26300  1.000 61.57054  ? 96  PRO A CG  1 
ATOM   738  C CD  . PRO A 1 96  ? -19.63000 11.20700  20.43300  1.000 60.28618  ? 96  PRO A CD  1 
ATOM   739  N N   . LYS A 1 97  ? -19.36200 11.97300  16.86900  1.000 56.20411  ? 97  LYS A N   1 
ATOM   740  C CA  . LYS A 1 97  ? -19.03700 11.85200  15.45200  1.000 58.19645  ? 97  LYS A CA  1 
ATOM   741  C C   . LYS A 1 97  ? -20.27000 11.75100  14.55900  1.000 55.26189  ? 97  LYS A C   1 
ATOM   742  O O   . LYS A 1 97  ? -20.15600 11.31900  13.41200  1.000 54.38547  ? 97  LYS A O   1 
ATOM   743  C CB  . LYS A 1 97  ? -18.13600 10.63600  15.20700  1.000 56.83050  ? 97  LYS A CB  1 
ATOM   744  C CG  . LYS A 1 97  ? -16.69100 10.79400  15.72600  1.000 65.69209  ? 97  LYS A CG  1 
ATOM   745  C CD  . LYS A 1 97  ? -16.46500 9.87000   16.90800  1.000 76.39074  ? 97  LYS A CD  1 
ATOM   746  C CE  . LYS A 1 97  ? -15.79400 8.55500   16.53900  1.000 71.36119  ? 97  LYS A CE  1 
ATOM   747  N NZ  . LYS A 1 97  ? -14.48700 8.75100   15.87300  1.000 75.88278  ? 97  LYS A NZ  1 
ATOM   748  N N   . THR A 1 98  ? -21.43100 12.14600  15.04500  1.000 56.09620  ? 98  THR A N   1 
ATOM   749  C CA  . THR A 1 98  ? -22.63000 12.10400  14.21900  1.000 55.23294  ? 98  THR A CA  1 
ATOM   750  C C   . THR A 1 98  ? -22.47000 13.01900  13.00000  1.000 55.71984  ? 98  THR A C   1 
ATOM   751  O O   . THR A 1 98  ? -22.23700 14.23200  13.17300  1.000 51.39827  ? 98  THR A O   1 
ATOM   752  C CB  . THR A 1 98  ? -23.85700 12.53200  15.03100  1.000 55.08818  ? 98  THR A CB  1 
ATOM   753  O OG1 . THR A 1 98  ? -23.96100 11.73200  16.20600  1.000 55.65141  ? 98  THR A OG1 1 
ATOM   754  C CG2 . THR A 1 98  ? -25.10100 12.34800  14.20600  1.000 54.38547  ? 98  THR A CG2 1 
ATOM   755  N N   . PRO A 1 99  ? -22.59200 12.49500  11.77600  1.000 52.92477  ? 99  PRO A N   1 
ATOM   756  C CA  . PRO A 1 99  ? -22.54000 13.33100  10.57000  1.000 52.33785  ? 99  PRO A CA  1 
ATOM   757  C C   . PRO A 1 99  ? -23.87000 14.02000  10.33100  1.000 53.66170  ? 99  PRO A C   1 
ATOM   758  O O   . PRO A 1 99  ? -24.86000 13.71600  10.98700  1.000 51.44301  ? 99  PRO A O   1 
ATOM   759  C CB  . PRO A 1 99  ? -22.27100 12.31600  9.46400   1.000 54.63813  ? 99  PRO A CB  1 
ATOM   760  C CG  . PRO A 1 99  ? -22.95500 11.04600  9.95500   1.000 49.95336  ? 99  PRO A CG  1 
ATOM   761  C CD  . PRO A 1 99  ? -22.70800 11.05900  11.45200  1.000 51.83779  ? 99  PRO A CD  1 
ATOM   762  N N   . LYS A 1 100 ? -23.88100 14.98700  9.40500   1.000 53.87488  ? 100 LYS A N   1 
ATOM   763  C CA  . LYS A 1 100 ? -25.16800 15.43200  8.88300   1.000 56.38308  ? 100 LYS A CA  1 
ATOM   764  C C   . LYS A 1 100 ? -25.78600 14.20400  8.22300   1.000 54.48022  ? 100 LYS A C   1 
ATOM   765  O O   . LYS A 1 100 ? -25.09200 13.44200  7.54500   1.000 47.51622  ? 100 LYS A O   1 
ATOM   766  C CB  . LYS A 1 100 ? -25.02800 16.56200  7.86600   1.000 59.73348  ? 100 LYS A CB  1 
ATOM   767  C CG  . LYS A 1 100 ? -24.01300 17.60600  8.26700   1.000 80.73336  ? 100 LYS A CG  1 
ATOM   768  C CD  . LYS A 1 100 ? -23.67400 18.53400  7.08000   1.000 94.39553  ? 100 LYS A CD  1 
ATOM   769  C CE  . LYS A 1 100 ? -22.38200 19.37900  7.30300   1.000 86.14191  ? 100 LYS A CE  1 
ATOM   770  N NZ  . LYS A 1 100 ? -22.43600 20.39500  8.39700   1.000 84.54172  ? 100 LYS A NZ  1 
ATOM   771  N N   . TYR A 1 101 ? -27.04300 13.90300  8.54800   1.000 49.60595  ? 101 TYR A N   1 
ATOM   772  C CA  . TYR A 1 101 ? -27.57500 12.69500  7.95600   1.000 47.62413  ? 101 TYR A CA  1 
ATOM   773  C C   . TYR A 1 101 ? -29.06400 12.83100  7.69400   1.000 47.96365  ? 101 TYR A C   1 
ATOM   774  O O   . TYR A 1 101 ? -29.75000 13.68700  8.26900   1.000 49.86651  ? 101 TYR A O   1 
ATOM   775  C CB  . TYR A 1 101 ? -27.27500 11.48400  8.83900   1.000 47.28198  ? 101 TYR A CB  1 
ATOM   776  C CG  . TYR A 1 101 ? -28.20200 11.42700  10.04300  1.000 47.25567  ? 101 TYR A CG  1 
ATOM   777  C CD1 . TYR A 1 101 ? -29.44900 10.81600  9.96700   1.000 48.57688  ? 101 TYR A CD1 1 
ATOM   778  C CD2 . TYR A 1 101 ? -27.82700 12.01100  11.24400  1.000 47.98996  ? 101 TYR A CD2 1 
ATOM   779  C CE1 . TYR A 1 101 ? -30.30000 10.80400  11.08400  1.000 47.31883  ? 101 TYR A CE1 1 
ATOM   780  C CE2 . TYR A 1 101 ? -28.65400 11.97800  12.36100  1.000 53.10637  ? 101 TYR A CE2 1 
ATOM   781  C CZ  . TYR A 1 101 ? -29.88200 11.36700  12.26300  1.000 48.55845  ? 101 TYR A CZ  1 
ATOM   782  O OH  . TYR A 1 101 ? -30.73300 11.35400  13.35500  1.000 55.97776  ? 101 TYR A OH  1 
ATOM   783  N N   . LYS A 1 102 ? -29.57300 11.94000  6.84500   1.000 47.82416  ? 102 LYS A N   1 
ATOM   784  C CA  . LYS A 1 102 ? -31.02400 11.73100  6.81600   1.000 50.61660  ? 102 LYS A CA  1 
ATOM   785  C C   . LYS A 1 102 ? -31.31800 10.25900  6.56700   1.000 46.05552  ? 102 LYS A C   1 
ATOM   786  O O   . LYS A 1 102 ? -30.45300 9.49100   6.16300   1.000 41.62078  ? 102 LYS A O   1 
ATOM   787  C CB  . LYS A 1 102 ? -31.72600 12.62700  5.78200   1.000 51.36405  ? 102 LYS A CB  1 
ATOM   788  C CG  . LYS A 1 102 ? -31.16300 12.48400  4.37200   1.000 53.79856  ? 102 LYS A CG  1 
ATOM   789  C CD  . LYS A 1 102 ? -32.00500 13.26800  3.35100   1.000 63.75238  ? 102 LYS A CD  1 
ATOM   790  C CE  . LYS A 1 102 ? -32.16800 14.72800  3.73100   1.000 78.10410  ? 102 LYS A CE  1 
ATOM   791  N NZ  . LYS A 1 102 ? -32.57600 15.58200  2.56100   1.000 80.83338  ? 102 LYS A NZ  1 
ATOM   792  N N   . PHE A 1 103 ? -32.53900 9.85000   6.90800   1.000 42.25770  ? 103 PHE A N   1 
ATOM   793  C CA  . PHE A 1 103 ? -33.02500 8.52500   6.58100   1.000 42.29981  ? 103 PHE A CA  1 
ATOM   794  C C   . PHE A 1 103 ? -33.83100 8.63900   5.30400   1.000 44.29215  ? 103 PHE A C   1 
ATOM   795  O O   . PHE A 1 103 ? -34.77800 9.42800   5.24300   1.000 44.17898  ? 103 PHE A O   1 
ATOM   796  C CB  . PHE A 1 103 ? -33.93700 7.97400   7.70000   1.000 40.09954  ? 103 PHE A CB  1 
ATOM   797  C CG  . PHE A 1 103 ? -33.21900 7.74000   8.98900   1.000 43.57101  ? 103 PHE A CG  1 
ATOM   798  C CD1 . PHE A 1 103 ? -31.82100 7.65500   8.99600   1.000 44.91328  ? 103 PHE A CD1 1 
ATOM   799  C CD2 . PHE A 1 103 ? -33.92100 7.58700   10.17800  1.000 45.62126  ? 103 PHE A CD2 1 
ATOM   800  C CE1 . PHE A 1 103 ? -31.13700 7.40600   10.21000  1.000 44.33689  ? 103 PHE A CE1 1 
ATOM   801  C CE2 . PHE A 1 103 ? -33.25800 7.36500   11.40000  1.000 46.64770  ? 103 PHE A CE2 1 
ATOM   802  C CZ  . PHE A 1 103 ? -31.89600 7.26900   11.41400  1.000 49.11115  ? 103 PHE A CZ  1 
ATOM   803  N N   . VAL A 1 104 ? -33.54400 7.79400   4.33500   1.000 38.40987  ? 104 VAL A N   1 
ATOM   804  C CA  . VAL A 1 104 ? -34.29300 7.82200   3.07800   1.000 39.98111  ? 104 VAL A CA  1 
ATOM   805  C C   . VAL A 1 104 ? -34.71800 6.40800   2.73500   1.000 43.19992  ? 104 VAL A C   1 
ATOM   806  O O   . VAL A 1 104 ? -34.04400 5.43100   3.07400   1.000 44.92381  ? 104 VAL A O   1 
ATOM   807  C CB  . VAL A 1 104 ? -33.48400 8.40900   1.88900   1.000 43.43152  ? 104 VAL A CB  1 
ATOM   808  C CG1 . VAL A 1 104 ? -32.97500 9.79400   2.23800   1.000 46.28713  ? 104 VAL A CG1 1 
ATOM   809  C CG2 . VAL A 1 104 ? -32.36000 7.53500   1.54300   1.000 42.87619  ? 104 VAL A CG2 1 
ATOM   810  N N   . ARG A 1 105 ? -35.81900 6.29700   2.01300   1.000 38.28880  ? 105 ARG A N   1 
ATOM   811  C CA  . ARG A 1 105 ? -36.23300 5.01100   1.49200   1.000 41.83133  ? 105 ARG A CA  1 
ATOM   812  C C   . ARG A 1 105 ? -35.94800 4.98600   -0.00600  1.000 46.31345  ? 105 ARG A C   1 
ATOM   813  O O   . ARG A 1 105 ? -36.52100 5.76400   -0.76800  1.000 47.77678  ? 105 ARG A O   1 
ATOM   814  C CB  . ARG A 1 105 ? -37.71000 4.79200   1.80200   1.000 45.42913  ? 105 ARG A CB  1 
ATOM   815  C CG  . ARG A 1 105 ? -38.19700 3.45400   1.35400   1.000 46.23186  ? 105 ARG A CG  1 
ATOM   816  C CD  . ARG A 1 105 ? -39.56800 3.22700   2.02900   1.000 42.68933  ? 105 ARG A CD  1 
ATOM   817  N NE  . ARG A 1 105 ? -40.03100 1.92800   1.54600   1.000 46.78192  ? 105 ARG A NE  1 
ATOM   818  C CZ  . ARG A 1 105 ? -39.77300 0.78200   2.15600   1.000 48.59530  ? 105 ARG A CZ  1 
ATOM   819  N NH1 . ARG A 1 105 ? -39.12000 0.75100   3.31100   1.000 43.12359  ? 105 ARG A NH1 1 
ATOM   820  N NH2 . ARG A 1 105 ? -40.15500 -0.35800  1.58400   1.000 45.82918  ? 105 ARG A NH2 1 
ATOM   821  N N   . ILE A 1 106 ? -35.11400 4.09800   -0.42800  1.000 41.74448  ? 106 ILE A N   1 
ATOM   822  C CA  . ILE A 1 106 ? -34.77800 4.06800   -1.83900  1.000 45.78180  ? 106 ILE A CA  1 
ATOM   823  C C   . ILE A 1 106 ? -35.72200 3.14600   -2.58700  1.000 47.50306  ? 106 ILE A C   1 
ATOM   824  O O   . ILE A 1 106 ? -36.40000 2.30600   -1.98800  1.000 47.04511  ? 106 ILE A O   1 
ATOM   825  C CB  . ILE A 1 106 ? -33.33000 3.64100   -2.03700  1.000 43.87105  ? 106 ILE A CB  1 
ATOM   826  C CG1 . ILE A 1 106 ? -33.03500 2.29500   -1.37100  1.000 40.15218  ? 106 ILE A CG1 1 
ATOM   827  C CG2 . ILE A 1 106 ? -32.41200 4.74600   -1.60300  1.000 50.45868  ? 106 ILE A CG2 1 
ATOM   828  C CD1 . ILE A 1 106 ? -31.75400 1.70000   -2.00000  1.000 49.81913  ? 106 ILE A CD1 1 
ATOM   829  N N   . GLN A 1 107 ? -35.74200 3.29200   -3.93800  1.000 43.52627  ? 107 GLN A N   1 
ATOM   830  C CA  . GLN A 1 107 ? -36.46500 2.50200   -4.92200  1.000 46.24765  ? 107 GLN A CA  1 
ATOM   831  C C   . GLN A 1 107 ? -35.59200 1.42100   -5.48300  1.000 41.37338  ? 107 GLN A C   1 
ATOM   832  O O   . GLN A 1 107 ? -34.35600 1.56500   -5.58100  1.000 42.22085  ? 107 GLN A O   1 
ATOM   833  C CB  . GLN A 1 107 ? -36.95700 3.33100   -6.12300  1.000 52.54314  ? 107 GLN A CB  1 
ATOM   834  C CG  . GLN A 1 107 ? -37.75200 4.61100   -5.87700  1.000 64.63143  ? 107 GLN A CG  1 
ATOM   835  C CD  . GLN A 1 107 ? -37.89800 5.44700   -7.15800  1.000 83.02311  ? 107 GLN A CD  1 
ATOM   836  O OE1 . GLN A 1 107 ? -38.12600 4.91800   -8.25300  1.000 75.11690  ? 107 GLN A OE1 1 
ATOM   837  N NE2 . GLN A 1 107 ? -37.73100 6.76200   -7.02300  1.000 92.88482  ? 107 GLN A NE2 1 
ATOM   838  N N   . PRO A 1 108 ? -36.23400 0.36900   -5.97800  1.000 41.40760  ? 108 PRO A N   1 
ATOM   839  C CA  . PRO A 1 108 ? -35.52600 -0.64300  -6.75900  1.000 38.17826  ? 108 PRO A CA  1 
ATOM   840  C C   . PRO A 1 108 ? -34.79500 0.00900   -7.92600  1.000 38.63884  ? 108 PRO A C   1 
ATOM   841  O O   . PRO A 1 108 ? -35.28700 0.96100   -8.53400  1.000 37.95455  ? 108 PRO A O   1 
ATOM   842  C CB  . PRO A 1 108 ? -36.63500 -1.55200  -7.28200  1.000 42.31297  ? 108 PRO A CB  1 
ATOM   843  C CG  . PRO A 1 108 ? -37.66000 -1.46600  -6.30100  1.000 40.77594  ? 108 PRO A CG  1 
ATOM   844  C CD  . PRO A 1 108 ? -37.66400 0.00200   -5.76400  1.000 42.87883  ? 108 PRO A CD  1 
ATOM   845  N N   . GLY A 1 109 ? -33.60900 -0.49300  -8.18300  1.000 37.54134  ? 109 GLY A N   1 
ATOM   846  C CA  . GLY A 1 109 ? -32.75600 0.03500   -9.24200  1.000 33.44348  ? 109 GLY A CA  1 
ATOM   847  C C   . GLY A 1 109 ? -31.76900 1.03700   -8.72300  1.000 41.91029  ? 109 GLY A C   1 
ATOM   848  O O   . GLY A 1 109 ? -30.78900 1.33700   -9.43200  1.000 41.45497  ? 109 GLY A O   1 
ATOM   849  N N   . GLN A 1 110 ? -31.97600 1.58100   -7.51600  1.000 37.83612  ? 110 GLN A N   1 
ATOM   850  C CA  . GLN A 1 110 ? -30.99300 2.53300   -6.96600  1.000 39.32840  ? 110 GLN A CA  1 
ATOM   851  C C   . GLN A 1 110 ? -29.85100 1.79100   -6.25400  1.000 38.81255  ? 110 GLN A C   1 
ATOM   852  O O   . GLN A 1 110 ? -29.99700 0.64200   -5.83200  1.000 35.87535  ? 110 GLN A O   1 
ATOM   853  C CB  . GLN A 1 110 ? -31.64400 3.54400   -6.01600  1.000 39.54685  ? 110 GLN A CB  1 
ATOM   854  C CG  . GLN A 1 110 ? -32.56600 4.54300   -6.69600  1.000 44.57640  ? 110 GLN A CG  1 
ATOM   855  C CD  . GLN A 1 110 ? -31.87100 5.28600   -7.87600  1.000 59.33606  ? 110 GLN A CD  1 
ATOM   856  O OE1 . GLN A 1 110 ? -30.89000 6.04900   -7.67300  1.000 55.32769  ? 110 GLN A OE1 1 
ATOM   857  N NE2 . GLN A 1 110 ? -32.37100 5.05700   -9.11100  1.000 45.77654  ? 110 GLN A NE2 1 
ATOM   858  N N   . THR A 1 111 ? -28.66400 2.41100   -6.22900  1.000 36.59649  ? 111 THR A N   1 
ATOM   859  C CA  . THR A 1 111 ? -27.49200 1.78300   -5.63000  1.000 35.33055  ? 111 THR A CA  1 
ATOM   860  C C   . THR A 1 111 ? -27.13900 2.45300   -4.29900  1.000 35.67533  ? 111 THR A C   1 
ATOM   861  O O   . THR A 1 111 ? -27.53400 3.58300   -4.02000  1.000 38.47830  ? 111 THR A O   1 
ATOM   862  C CB  . THR A 1 111 ? -26.27700 1.92300   -6.59800  1.000 35.20685  ? 111 THR A CB  1 
ATOM   863  O OG1 . THR A 1 111 ? -26.25800 3.29800   -6.93800  1.000 36.62808  ? 111 THR A OG1 1 
ATOM   864  C CG2 . THR A 1 111 ? -26.57700 1.07000   -7.85300  1.000 37.24657  ? 111 THR A CG2 1 
ATOM   865  N N   . PHE A 1 112 ? -26.31200 1.77700   -3.51000  1.000 33.73562  ? 112 PHE A N   1 
ATOM   866  C CA  . PHE A 1 112 ? -25.78200 2.35900   -2.28800  1.000 35.98853  ? 112 PHE A CA  1 
ATOM   867  C C   . PHE A 1 112 ? -24.57400 1.56000   -1.83300  1.000 36.73598  ? 112 PHE A C   1 
ATOM   868  O O   . PHE A 1 112 ? -24.29700 0.45200   -2.30700  1.000 38.78360  ? 112 PHE A O   1 
ATOM   869  C CB  . PHE A 1 112 ? -26.85700 2.38500   -1.17400  1.000 36.15697  ? 112 PHE A CB  1 
ATOM   870  C CG  . PHE A 1 112 ? -27.43800 1.04800   -0.93600  1.000 37.79137  ? 112 PHE A CG  1 
ATOM   871  C CD1 . PHE A 1 112 ? -28.48600 0.60800   -1.71900  1.000 40.01006  ? 112 PHE A CD1 1 
ATOM   872  C CD2 . PHE A 1 112 ? -26.94800 0.22900   0.06300   1.000 37.81243  ? 112 PHE A CD2 1 
ATOM   873  C CE1 . PHE A 1 112 ? -29.07700 -0.63600  -1.43900  1.000 44.62114  ? 112 PHE A CE1 1 
ATOM   874  C CE2 . PHE A 1 112 ? -27.54300 -1.02700  0.33400   1.000 42.82882  ? 112 PHE A CE2 1 
ATOM   875  C CZ  . PHE A 1 112 ? -28.58700 -1.43600  -0.41000  1.000 42.16821  ? 112 PHE A CZ  1 
ATOM   876  N N   . SER A 1 113 ? -23.83000 2.16300   -0.93400  1.000 38.28091  ? 113 SER A N   1 
ATOM   877  C CA  . SER A 1 113 ? -22.66500 1.56100   -0.31400  1.000 38.94151  ? 113 SER A CA  1 
ATOM   878  C C   . SER A 1 113 ? -23.05100 0.87900   0.97300   1.000 36.50701  ? 113 SER A C   1 
ATOM   879  O O   . SER A 1 113 ? -23.79200 1.44400   1.74400   1.000 38.48619  ? 113 SER A O   1 
ATOM   880  C CB  . SER A 1 113 ? -21.61500 2.65000   -0.01100  1.000 39.75213  ? 113 SER A CB  1 
ATOM   881  O OG  . SER A 1 113 ? -21.20400 3.26500   -1.23700  1.000 37.00180  ? 113 SER A OG  1 
ATOM   882  N N   . VAL A 1 114 ? -22.47900 -0.29400  1.21600   1.000 36.83336  ? 114 VAL A N   1 
ATOM   883  C CA  . VAL A 1 114 ? -22.69300 -1.12100  2.39900   1.000 38.27827  ? 114 VAL A CA  1 
ATOM   884  C C   . VAL A 1 114 ? -21.40300 -1.10900  3.18100   1.000 39.25207  ? 114 VAL A C   1 
ATOM   885  O O   . VAL A 1 114 ? -20.33500 -1.40300  2.61200   1.000 39.29155  ? 114 VAL A O   1 
ATOM   886  C CB  . VAL A 1 114 ? -23.02900 -2.57700  2.00400   1.000 36.85968  ? 114 VAL A CB  1 
ATOM   887  C CG1 . VAL A 1 114 ? -22.94100 -3.41300  3.25400   1.000 35.81745  ? 114 VAL A CG1 1 
ATOM   888  C CG2 . VAL A 1 114 ? -24.44000 -2.67200  1.33900   1.000 38.84413  ? 114 VAL A CG2 1 
ATOM   889  N N   . LEU A 1 115 ? -21.46900 -0.72900  4.44300   1.000 33.99881  ? 115 LEU A N   1 
ATOM   890  C CA  . LEU A 1 115 ? -20.33300 -0.94100  5.35000   1.000 36.12012  ? 115 LEU A CA  1 
ATOM   891  C C   . LEU A 1 115 ? -20.60800 -2.20700  6.15600   1.000 41.19178  ? 115 LEU A C   1 
ATOM   892  O O   . LEU A 1 115 ? -21.35300 -2.17800  7.15000   1.000 39.66528  ? 115 LEU A O   1 
ATOM   893  C CB  . LEU A 1 115 ? -20.08800 0.28800   6.22500   1.000 35.53058  ? 115 LEU A CB  1 
ATOM   894  C CG  . LEU A 1 115 ? -18.97600 0.19600   7.24400   1.000 39.81530  ? 115 LEU A CG  1 
ATOM   895  C CD1 . LEU A 1 115 ? -17.61000 0.14800   6.44800   1.000 42.48404  ? 115 LEU A CD1 1 
ATOM   896  C CD2 . LEU A 1 115 ? -19.00000 1.34200   8.24100   1.000 40.78121  ? 115 LEU A CD2 1 
ATOM   897  N N   . ALA A 1 116 ? -20.02800 -3.33600  5.71300   1.000 40.14955  ? 116 ALA A N   1 
ATOM   898  C CA  . ALA A 1 116 ? -20.20600 -4.61200  6.41800   1.000 39.47579  ? 116 ALA A CA  1 
ATOM   899  C C   . ALA A 1 116 ? -19.46700 -4.57900  7.74000   1.000 42.66038  ? 116 ALA A C   1 
ATOM   900  O O   . ALA A 1 116 ? -18.30400 -4.20500  7.79700   1.000 42.59984  ? 116 ALA A O   1 
ATOM   901  C CB  . ALA A 1 116 ? -19.71400 -5.80900  5.60400   1.000 40.84700  ? 116 ALA A CB  1 
ATOM   902  N N   . CYS A 1 117 ? -20.16500 -4.91500  8.80900   1.000 40.86016  ? 117 CYS A N   1 
ATOM   903  C CA  . CYS A 1 117 ? -19.60500 -4.83200  10.15400  1.000 40.52854  ? 117 CYS A CA  1 
ATOM   904  C C   . CYS A 1 117 ? -19.87900 -6.11100  10.91000  1.000 43.62892  ? 117 CYS A C   1 
ATOM   905  O O   . CYS A 1 117 ? -20.91000 -6.76800  10.69900  1.000 44.70273  ? 117 CYS A O   1 
ATOM   906  C CB  . CYS A 1 117 ? -20.18500 -3.72700  10.97400  1.000 45.96077  ? 117 CYS A CB  1 
ATOM   907  S SG  . CYS A 1 117 ? -19.90500 -2.09700  10.36400  1.000 48.20315  ? 117 CYS A SG  1 
ATOM   908  N N   . TYR A 1 118 ? -18.97800 -6.40800  11.84700  1.000 44.66062  ? 118 TYR A N   1 
ATOM   909  C CA  . TYR A 1 118 ? -19.12500 -7.49300  12.81100  1.000 49.20590  ? 118 TYR A CA  1 
ATOM   910  C C   . TYR A 1 118 ? -18.68800 -6.97300  14.16700  1.000 48.40317  ? 118 TYR A C   1 
ATOM   911  O O   . TYR A 1 118 ? -17.66500 -6.28200  14.25700  1.000 46.95563  ? 118 TYR A O   1 
ATOM   912  C CB  . TYR A 1 118 ? -18.30500 -8.73700  12.40400  1.000 48.33211  ? 118 TYR A CB  1 
ATOM   913  C CG  . TYR A 1 118 ? -18.81100 -9.20600  11.06300  1.000 46.44767  ? 118 TYR A CG  1 
ATOM   914  C CD1 . TYR A 1 118 ? -19.96300 -10.02400 10.97900  1.000 48.20315  ? 118 TYR A CD1 1 
ATOM   915  C CD2 . TYR A 1 118 ? -18.21600 -8.76600  9.88700   1.000 44.87380  ? 118 TYR A CD2 1 
ATOM   916  C CE1 . TYR A 1 118 ? -20.47300 -10.40300 9.72900   1.000 44.94486  ? 118 TYR A CE1 1 
ATOM   917  C CE2 . TYR A 1 118 ? -18.72000 -9.10200  8.65500   1.000 44.20793  ? 118 TYR A CE2 1 
ATOM   918  C CZ  . TYR A 1 118 ? -19.81700 -9.95500  8.57800   1.000 45.40544  ? 118 TYR A CZ  1 
ATOM   919  O OH  . TYR A 1 118 ? -20.31500 -10.29100 7.35500   1.000 42.17348  ? 118 TYR A OH  1 
ATOM   920  N N   . ASN A 1 119 ? -19.51000 -7.24000  15.19200  1.000 48.74795  ? 119 ASN A N   1 
ATOM   921  C CA  . ASN A 1 119 ? -19.21700 -6.86300  16.57800  1.000 50.98769  ? 119 ASN A CA  1 
ATOM   922  C C   . ASN A 1 119 ? -18.96400 -5.36200  16.69300  1.000 48.83217  ? 119 ASN A C   1 
ATOM   923  O O   . ASN A 1 119 ? -18.10700 -4.91800  17.44400  1.000 47.95575  ? 119 ASN A O   1 
ATOM   924  C CB  . ASN A 1 119 ? -18.01800 -7.65500  17.11600  1.000 53.54589  ? 119 ASN A CB  1 
ATOM   925  C CG  . ASN A 1 119 ? -18.17700 -9.13700  16.90500  1.000 56.54625  ? 119 ASN A CG  1 
ATOM   926  O OD1 . ASN A 1 119 ? -17.43400 -9.76200  16.13500  1.000 59.91771  ? 119 ASN A OD1 1 
ATOM   927  N ND2 . ASN A 1 119 ? -19.19100 -9.69400  17.51400  1.000 55.55140  ? 119 ASN A ND2 1 
ATOM   928  N N   . GLY A 1 120 ? -19.70800 -4.56700  15.93700  1.000 47.27672  ? 120 GLY A N   1 
ATOM   929  C CA  . GLY A 1 120 ? -19.51600 -3.13200  15.97200  1.000 45.86076  ? 120 GLY A CA  1 
ATOM   930  C C   . GLY A 1 120 ? -18.30400 -2.64700  15.20100  1.000 49.16642  ? 120 GLY A C   1 
ATOM   931  O O   . GLY A 1 120 ? -18.04000 -1.43400  15.20000  1.000 48.64004  ? 120 GLY A O   1 
ATOM   932  N N   . SER A 1 121 ? -17.55200 -3.54400  14.56600  1.000 46.29766  ? 121 SER A N   1 
ATOM   933  C CA  . SER A 1 121 ? -16.29400 -3.12200  13.88700  1.000 48.71110  ? 121 SER A CA  1 
ATOM   934  C C   . SER A 1 121 ? -16.46300 -3.22800  12.39300  1.000 47.59255  ? 121 SER A C   1 
ATOM   935  O O   . SER A 1 121 ? -16.77200 -4.32000  11.89600  1.000 46.06342  ? 121 SER A O   1 
ATOM   936  C CB  . SER A 1 121 ? -15.11600 -3.96800  14.30500  1.000 47.43200  ? 121 SER A CB  1 
ATOM   937  O OG  . SER A 1 121 ? -14.77400 -3.63200  15.60900  1.000 55.20136  ? 121 SER A OG  1 
ATOM   938  N N   . PRO A 1 122 ? -16.26500 -2.14100  11.65300  1.000 50.02968  ? 122 PRO A N   1 
ATOM   939  C CA  . PRO A 1 122 ? -16.27000 -2.22400  10.18300  1.000 48.99535  ? 122 PRO A CA  1 
ATOM   940  C C   . PRO A 1 122 ? -15.26500 -3.21600  9.65000   1.000 47.12144  ? 122 PRO A C   1 
ATOM   941  O O   . PRO A 1 122 ? -14.10900 -3.22900  10.07500  1.000 47.77678  ? 122 PRO A O   1 
ATOM   942  C CB  . PRO A 1 122 ? -15.89400 -0.80800  9.75000   1.000 47.04775  ? 122 PRO A CB  1 
ATOM   943  C CG  . PRO A 1 122 ? -16.46200 0.06700   10.86300  1.000 50.89031  ? 122 PRO A CG  1 
ATOM   944  C CD  . PRO A 1 122 ? -16.25000 -0.74500  12.14400  1.000 50.32709  ? 122 PRO A CD  1 
ATOM   945  N N   . SER A 1 123 ? -15.70200 -4.05100  8.69200   1.000 45.76075  ? 123 SER A N   1 
ATOM   946  C CA  . SER A 1 123 ? -14.75900 -4.94800  8.04800   1.000 47.19513  ? 123 SER A CA  1 
ATOM   947  C C   . SER A 1 123 ? -14.55500 -4.68600  6.55100   1.000 49.12168  ? 123 SER A C   1 
ATOM   948  O O   . SER A 1 123 ? -13.49500 -5.05400  6.03100   1.000 44.78695  ? 123 SER A O   1 
ATOM   949  C CB  . SER A 1 123 ? -15.13500 -6.40600  8.25600   1.000 52.42471  ? 123 SER A CB  1 
ATOM   950  O OG  . SER A 1 123 ? -16.30100 -6.69800  7.56600   1.000 54.65919  ? 123 SER A OG  1 
ATOM   951  N N   . GLY A 1 124 ? -15.52400 -4.10000  5.83900   1.000 44.41059  ? 124 GLY A N   1 
ATOM   952  C CA  . GLY A 1 124 ? -15.33000 -3.82200  4.42100   1.000 43.53154  ? 124 GLY A CA  1 
ATOM   953  C C   . GLY A 1 124 ? -16.45500 -2.98600  3.84000   1.000 44.12371  ? 124 GLY A C   1 
ATOM   954  O O   . GLY A 1 124 ? -17.53100 -2.79400  4.44300   1.000 39.11785  ? 124 GLY A O   1 
ATOM   955  N N   . VAL A 1 125 ? -16.19700 -2.47200  2.64500   1.000 37.46239  ? 125 VAL A N   1 
ATOM   956  C CA  . VAL A 1 125 ? -17.16100 -1.58500  2.02500   1.000 38.32302  ? 125 VAL A CA  1 
ATOM   957  C C   . VAL A 1 125 ? -17.35400 -1.99200  0.57200   1.000 41.23916  ? 125 VAL A C   1 
ATOM   958  O O   . VAL A 1 125 ? -16.38500 -2.24600  -0.16600  1.000 40.16534  ? 125 VAL A O   1 
ATOM   959  C CB  . VAL A 1 125 ? -16.73800 -0.09900  2.21800   1.000 38.55199  ? 125 VAL A CB  1 
ATOM   960  C CG1 . VAL A 1 125 ? -15.43800 0.20800   1.52200   1.000 45.27385  ? 125 VAL A CG1 1 
ATOM   961  C CG2 . VAL A 1 125 ? -17.71300 0.82100   1.62100   1.000 41.25758  ? 125 VAL A CG2 1 
ATOM   962  N N   . TYR A 1 126 ? -18.60900 -2.02400  0.13300   1.000 35.23580  ? 126 TYR A N   1 
ATOM   963  C CA  . TYR A 1 126 ? -18.88100 -2.39400  -1.25600  1.000 37.12287  ? 126 TYR A CA  1 
ATOM   964  C C   . TYR A 1 126 ? -20.18900 -1.76900  -1.73700  1.000 40.89438  ? 126 TYR A C   1 
ATOM   965  O O   . TYR A 1 126 ? -21.06800 -1.41300  -0.93100  1.000 37.69926  ? 126 TYR A O   1 
ATOM   966  C CB  . TYR A 1 126 ? -18.91100 -3.92100  -1.45800  1.000 36.99654  ? 126 TYR A CB  1 
ATOM   967  C CG  . TYR A 1 126 ? -19.86800 -4.67700  -0.56400  1.000 38.09930  ? 126 TYR A CG  1 
ATOM   968  C CD1 . TYR A 1 126 ? -21.18600 -4.81900  -0.91300  1.000 43.51574  ? 126 TYR A CD1 1 
ATOM   969  C CD2 . TYR A 1 126 ? -19.43600 -5.25500  0.61800   1.000 41.27863  ? 126 TYR A CD2 1 
ATOM   970  C CE1 . TYR A 1 126 ? -22.08200 -5.51400  -0.07800  1.000 40.80226  ? 126 TYR A CE1 1 
ATOM   971  C CE2 . TYR A 1 126 ? -20.34600 -5.94000  1.48400   1.000 43.14465  ? 126 TYR A CE2 1 
ATOM   972  C CZ  . TYR A 1 126 ? -21.61900 -6.08400  1.10600   1.000 39.19944  ? 126 TYR A CZ  1 
ATOM   973  O OH  . TYR A 1 126 ? -22.50200 -6.77300  1.91100   1.000 45.71864  ? 126 TYR A OH  1 
ATOM   974  N N   . GLN A 1 127 ? -20.33300 -1.75500  -3.06100  1.000 36.66229  ? 127 GLN A N   1 
ATOM   975  C CA  . GLN A 1 127 ? -21.55100 -1.19900  -3.68800  1.000 41.08651  ? 127 GLN A CA  1 
ATOM   976  C C   . GLN A 1 127 ? -22.60500 -2.27800  -3.90700  1.000 40.64435  ? 127 GLN A C   1 
ATOM   977  O O   . GLN A 1 127 ? -22.24000 -3.40200  -4.24100  1.000 40.33905  ? 127 GLN A O   1 
ATOM   978  C CB  . GLN A 1 127 ? -21.24500 -0.57100  -5.04400  1.000 44.93960  ? 127 GLN A CB  1 
ATOM   979  C CG  . GLN A 1 127 ? -20.71300 0.83900   -4.96800  1.000 44.97645  ? 127 GLN A CG  1 
ATOM   980  C CD  . GLN A 1 127 ? -21.74800 1.82900   -4.50400  1.000 43.32888  ? 127 GLN A CD  1 
ATOM   981  O OE1 . GLN A 1 127 ? -21.76700 2.22500   -3.34600  1.000 43.86052  ? 127 GLN A OE1 1 
ATOM   982  N NE2 . GLN A 1 127 ? -22.60700 2.25500   -5.41300  1.000 43.32098  ? 127 GLN A NE2 1 
ATOM   983  N N   . CYS A 1 128 ? -23.85400 -1.86300  -3.81400  1.000 42.47615  ? 128 CYS A N   1 
ATOM   984  C CA  . CYS A 1 128 ? -24.98000 -2.79800  -3.98600  1.000 43.73682  ? 128 CYS A CA  1 
ATOM   985  C C   . CYS A 1 128 ? -26.13700 -2.06000  -4.64600  1.000 40.04164  ? 128 CYS A C   1 
ATOM   986  O O   . CYS A 1 128 ? -26.25800 -0.86500  -4.42000  1.000 39.72845  ? 128 CYS A O   1 
ATOM   987  C CB  . CYS A 1 128 ? -25.48200 -3.27300  -2.62900  1.000 38.10983  ? 128 CYS A CB  1 
ATOM   988  S SG  . CYS A 1 128 ? -24.82900 -4.88100  -2.13000  1.000 52.81160  ? 128 CYS A SG  1 
ATOM   989  N N   . ALA A 1 129 ? -26.90600 -2.75000  -5.47500  1.000 40.22324  ? 129 ALA A N   1 
ATOM   990  C CA  . ALA A 1 129 ? -28.14800 -2.17700  -5.99600  1.000 34.43308  ? 129 ALA A CA  1 
ATOM   991  C C   . ALA A 1 129 ? -29.30800 -2.85600  -5.26800  1.000 35.86746  ? 129 ALA A C   1 
ATOM   992  O O   . ALA A 1 129 ? -29.23600 -4.03500  -4.92600  1.000 39.16522  ? 129 ALA A O   1 
ATOM   993  C CB  . ALA A 1 129 ? -28.31900 -2.39900  -7.50200  1.000 35.05157  ? 129 ALA A CB  1 
ATOM   994  N N   . MET A 1 130 ? -30.37200 -2.11800  -5.07100  1.000 36.05169  ? 130 MET A N   1 
ATOM   995  C CA  . MET A 1 130 ? -31.66000 -2.70600  -4.62500  1.000 35.50952  ? 130 MET A CA  1 
ATOM   996  C C   . MET A 1 130 ? -32.26600 -3.38500  -5.86200  1.000 33.83564  ? 130 MET A C   1 
ATOM   997  O O   . MET A 1 130 ? -32.55100 -2.71000  -6.84800  1.000 38.49409  ? 130 MET A O   1 
ATOM   998  C CB  . MET A 1 130 ? -32.53600 -1.58900  -4.06400  1.000 31.06162  ? 130 MET A CB  1 
ATOM   999  C CG  . MET A 1 130 ? -34.06300 -2.01100  -3.69300  1.000 39.90742  ? 130 MET A CG  1 
ATOM   1000 S SD  . MET A 1 130 ? -34.02200 -2.68500  -2.08100  1.000 49.84019  ? 130 MET A SD  1 
ATOM   1001 C CE  . MET A 1 130 ? -33.51700 -4.20600  -2.36500  1.000 40.89174  ? 130 MET A CE  1 
ATOM   1002 N N   . ARG A 1 131 ? -32.35000 -4.72800  -5.88100  1.000 34.43834  ? 131 ARG A N   1 
ATOM   1003 C CA  . ARG A 1 131 ? -32.88200 -5.42900  -7.03200  1.000 34.52256  ? 131 ARG A CA  1 
ATOM   1004 C C   . ARG A 1 131 ? -34.36000 -5.09800  -7.24600  1.000 38.69148  ? 131 ARG A C   1 
ATOM   1005 O O   . ARG A 1 131 ? -35.04300 -4.66700  -6.31100  1.000 40.23114  ? 131 ARG A O   1 
ATOM   1006 C CB  . ARG A 1 131 ? -32.74200 -6.94000  -6.86900  1.000 38.32828  ? 131 ARG A CB  1 
ATOM   1007 C CG  . ARG A 1 131 ? -31.37400 -7.43300  -6.52400  1.000 38.87571  ? 131 ARG A CG  1 
ATOM   1008 C CD  . ARG A 1 131 ? -30.27000 -6.96800  -7.61500  1.000 37.95455  ? 131 ARG A CD  1 
ATOM   1009 N NE  . ARG A 1 131 ? -30.84500 -7.27200  -8.92100  1.000 35.00420  ? 131 ARG A NE  1 
ATOM   1010 C CZ  . ARG A 1 131 ? -30.35500 -6.82400  -10.06400 1.000 38.63621  ? 131 ARG A CZ  1 
ATOM   1011 N NH1 . ARG A 1 131 ? -29.18800 -6.14600  -10.10000 1.000 34.41465  ? 131 ARG A NH1 1 
ATOM   1012 N NH2 . ARG A 1 131 ? -31.01700 -7.09500  -11.19300 1.000 37.72821  ? 131 ARG A NH2 1 
ATOM   1013 N N   . PRO A 1 132 ? -34.89900 -5.30600  -8.47700  1.000 36.54912  ? 132 PRO A N   1 
ATOM   1014 C CA  . PRO A 1 132 ? -36.35900 -5.15000  -8.64200  1.000 41.34969  ? 132 PRO A CA  1 
ATOM   1015 C C   . PRO A 1 132 ? -37.20400 -6.00200  -7.66100  1.000 39.88899  ? 132 PRO A C   1 
ATOM   1016 O O   . PRO A 1 132 ? -38.31700 -5.58400  -7.27500  1.000 43.01305  ? 132 PRO A O   1 
ATOM   1017 C CB  . PRO A 1 132 ? -36.60700 -5.57000  -10.10000 1.000 33.75142  ? 132 PRO A CB  1 
ATOM   1018 C CG  . PRO A 1 132 ? -35.30600 -5.16700  -10.80100 1.000 37.98613  ? 132 PRO A CG  1 
ATOM   1019 C CD  . PRO A 1 132 ? -34.18000 -5.44800  -9.77600  1.000 37.83348  ? 132 PRO A CD  1 
ATOM   1020 N N   . ASN A 1 133 ? -36.72600 -7.16900  -7.20100  1.000 39.49421  ? 133 ASN A N   1 
ATOM   1021 C CA  . ASN A 1 133 ? -37.50200 -7.95000  -6.22700  1.000 40.15481  ? 133 ASN A CA  1 
ATOM   1022 C C   . ASN A 1 133 ? -37.17100 -7.57900  -4.76400  1.000 41.35759  ? 133 ASN A C   1 
ATOM   1023 O O   . ASN A 1 133 ? -37.48600 -8.35400  -3.84700  1.000 40.54960  ? 133 ASN A O   1 
ATOM   1024 C CB  . ASN A 1 133 ? -37.26500 -9.44700  -6.45000  1.000 42.04978  ? 133 ASN A CB  1 
ATOM   1025 C CG  . ASN A 1 133 ? -35.80600 -9.86900  -6.14300  1.000 40.62329  ? 133 ASN A CG  1 
ATOM   1026 O OD1 . ASN A 1 133 ? -34.96400 -9.04800  -5.72000  1.000 38.48093  ? 133 ASN A OD1 1 
ATOM   1027 N ND2 . ASN A 1 133 ? -35.50900 -11.13500 -6.35100  1.000 41.41023  ? 133 ASN A ND2 1 
ATOM   1028 N N   . PHE A 1 134 ? -36.51200 -6.43100  -4.53600  1.000 35.71218  ? 134 PHE A N   1 
ATOM   1029 C CA  . PHE A 1 134 ? -36.30100 -5.83000  -3.22400  1.000 35.52531  ? 134 PHE A CA  1 
ATOM   1030 C C   . PHE A 1 134 ? -35.30700 -6.59500  -2.36000  1.000 40.49959  ? 134 PHE A C   1 
ATOM   1031 O O   . PHE A 1 134 ? -35.23900 -6.34200  -1.14000  1.000 47.12933  ? 134 PHE A O   1 
ATOM   1032 C CB  . PHE A 1 134 ? -37.65500 -5.68200  -2.41800  1.000 38.95730  ? 134 PHE A CB  1 
ATOM   1033 C CG  . PHE A 1 134 ? -38.59900 -4.69700  -3.02900  1.000 37.20446  ? 134 PHE A CG  1 
ATOM   1034 C CD1 . PHE A 1 134 ? -38.45600 -3.36800  -2.78600  1.000 42.12084  ? 134 PHE A CD1 1 
ATOM   1035 C CD2 . PHE A 1 134 ? -39.58900 -5.12100  -3.91100  1.000 43.36573  ? 134 PHE A CD2 1 
ATOM   1036 C CE1 . PHE A 1 134 ? -39.34700 -2.45300  -3.33400  1.000 46.91878  ? 134 PHE A CE1 1 
ATOM   1037 C CE2 . PHE A 1 134 ? -40.47400 -4.22400  -4.46000  1.000 43.64207  ? 134 PHE A CE2 1 
ATOM   1038 C CZ  . PHE A 1 134 ? -40.35300 -2.88900  -4.16000  1.000 46.74245  ? 134 PHE A CZ  1 
ATOM   1039 N N   . THR A 1 135 ? -34.48900 -7.47600  -2.92300  1.000 42.14716  ? 135 THR A N   1 
ATOM   1040 C CA  . THR A 1 135 ? -33.34000 -8.04600  -2.23500  1.000 34.53572  ? 135 THR A CA  1 
ATOM   1041 C C   . THR A 1 135 ? -32.06800 -7.28500  -2.66600  1.000 37.63609  ? 135 THR A C   1 
ATOM   1042 O O   . THR A 1 135 ? -32.09600 -6.50500  -3.60000  1.000 34.18305  ? 135 THR A O   1 
ATOM   1043 C CB  . THR A 1 135 ? -33.19700 -9.53400  -2.59400  1.000 34.86734  ? 135 THR A CB  1 
ATOM   1044 O OG1 . THR A 1 135 ? -32.96300 -9.69100  -3.99900  1.000 37.04392  ? 135 THR A OG1 1 
ATOM   1045 C CG2 . THR A 1 135 ? -34.55300 -10.29700 -2.24200  1.000 37.02812  ? 135 THR A CG2 1 
ATOM   1046 N N   . ILE A 1 136 ? -30.99400 -7.50500  -1.95000  1.000 34.07514  ? 136 ILE A N   1 
ATOM   1047 C CA  . ILE A 1 136 ? -29.68800 -7.05700  -2.44500  1.000 36.66755  ? 136 ILE A CA  1 
ATOM   1048 C C   . ILE A 1 136 ? -28.77400 -8.26700  -2.51100  1.000 38.50725  ? 136 ILE A C   1 
ATOM   1049 O O   . ILE A 1 136 ? -28.87300 -9.21300  -1.72000  1.000 37.35711  ? 136 ILE A O   1 
ATOM   1050 C CB  . ILE A 1 136 ? -29.08200 -5.93100  -1.56700  1.000 41.16283  ? 136 ILE A CB  1 
ATOM   1051 C CG1 . ILE A 1 136 ? -28.69800 -6.46500  -0.19600  1.000 42.05504  ? 136 ILE A CG1 1 
ATOM   1052 C CG2 . ILE A 1 136 ? -30.12300 -4.73600  -1.39500  1.000 41.04176  ? 136 ILE A CG2 1 
ATOM   1053 C CD1 . ILE A 1 136 ? -27.95700 -5.41500  0.72600   1.000 41.97609  ? 136 ILE A CD1 1 
ATOM   1054 N N   . LYS A 1 137 ? -27.85500 -8.23300  -3.47600  1.000 38.49935  ? 137 LYS A N   1 
ATOM   1055 C CA  . LYS A 1 137 ? -26.82600 -9.26200  -3.59100  1.000 39.03626  ? 137 LYS A CA  1 
ATOM   1056 C C   . LYS A 1 137 ? -25.62300 -8.75300  -2.82700  1.000 43.57365  ? 137 LYS A C   1 
ATOM   1057 O O   . LYS A 1 137 ? -24.68600 -8.15100  -3.39700  1.000 38.19932  ? 137 LYS A O   1 
ATOM   1058 C CB  . LYS A 1 137 ? -26.49300 -9.56800  -5.05900  1.000 40.63645  ? 137 LYS A CB  1 
ATOM   1059 C CG  . LYS A 1 137 ? -27.76700 -10.01000 -5.79900  1.000 43.26308  ? 137 LYS A CG  1 
ATOM   1060 C CD  . LYS A 1 137 ? -27.56900 -10.46600 -7.22700  1.000 47.68203  ? 137 LYS A CD  1 
ATOM   1061 C CE  . LYS A 1 137 ? -28.30500 -11.79500 -7.44500  1.000 57.07000  ? 137 LYS A CE  1 
ATOM   1062 N NZ  . LYS A 1 137 ? -28.48100 -12.10600 -8.88200  1.000 63.18652  ? 137 LYS A NZ  1 
ATOM   1063 N N   . GLY A 1 138 ? -25.63000 -9.01400  -1.52000  1.000 39.60738  ? 138 GLY A N   1 
ATOM   1064 C CA  . GLY A 1 138 ? -24.57900 -8.53600  -0.64400  1.000 39.68634  ? 138 GLY A CA  1 
ATOM   1065 C C   . GLY A 1 138 ? -23.53600 -9.57900  -0.33500  1.000 38.64411  ? 138 GLY A C   1 
ATOM   1066 O O   . GLY A 1 138 ? -23.44700 -10.63500 -0.97100  1.000 44.12898  ? 138 GLY A O   1 
ATOM   1067 N N   . SER A 1 139 ? -22.76500 -9.30300  0.70100   1.000 36.93864  ? 139 SER A N   1 
ATOM   1068 C CA  . SER A 1 139 ? -21.77500 -10.23900 1.22200   1.000 37.34395  ? 139 SER A CA  1 
ATOM   1069 C C   . SER A 1 139 ? -21.83800 -10.08300 2.74400   1.000 38.69938  ? 139 SER A C   1 
ATOM   1070 O O   . SER A 1 139 ? -21.29800 -9.13600  3.34500   1.000 37.70189  ? 139 SER A O   1 
ATOM   1071 C CB  . SER A 1 139 ? -20.36500 -9.95000  0.62700   1.000 38.48093  ? 139 SER A CB  1 
ATOM   1072 O OG  . SER A 1 139 ? -19.44500 -10.87300 1.19400   1.000 37.87296  ? 139 SER A OG  1 
ATOM   1073 N N   . PHE A 1 140 ? -22.53400 -11.00400 3.35700   1.000 41.13914  ? 140 PHE A N   1 
ATOM   1074 C CA  . PHE A 1 140 ? -22.95000 -10.91500 4.75200   1.000 41.54445  ? 140 PHE A CA  1 
ATOM   1075 C C   . PHE A 1 140 ? -22.84900 -12.29300 5.40500   1.000 40.99439  ? 140 PHE A C   1 
ATOM   1076 O O   . PHE A 1 140 ? -23.33600 -13.28000 4.84100   1.000 43.97633  ? 140 PHE A O   1 
ATOM   1077 C CB  . PHE A 1 140 ? -24.38700 -10.39600 4.83000   1.000 43.02621  ? 140 PHE A CB  1 
ATOM   1078 C CG  . PHE A 1 140 ? -24.53700 -8.93300  4.49200   1.000 39.02573  ? 140 PHE A CG  1 
ATOM   1079 C CD1 . PHE A 1 140 ? -23.90300 -7.97700  5.23400   1.000 38.48619  ? 140 PHE A CD1 1 
ATOM   1080 C CD2 . PHE A 1 140 ? -25.41700 -8.52800  3.53000   1.000 40.48907  ? 140 PHE A CD2 1 
ATOM   1081 C CE1 . PHE A 1 140 ? -24.16800 -6.63200  5.01400   1.000 40.44432  ? 140 PHE A CE1 1 
ATOM   1082 C CE2 . PHE A 1 140 ? -25.59000 -7.19200  3.21900   1.000 42.81829  ? 140 PHE A CE2 1 
ATOM   1083 C CZ  . PHE A 1 140 ? -25.04700 -6.23900  3.99900   1.000 38.46777  ? 140 PHE A CZ  1 
ATOM   1084 N N   . LEU A 1 141 ? -22.27500 -12.35000 6.61900   1.000 39.35209  ? 141 LEU A N   1 
ATOM   1085 C CA  . LEU A 1 141 ? -22.17400 -13.56100 7.40500   1.000 44.90012  ? 141 LEU A CA  1 
ATOM   1086 C C   . LEU A 1 141 ? -22.97600 -13.33600 8.68300   1.000 46.13185  ? 141 LEU A C   1 
ATOM   1087 O O   . LEU A 1 141 ? -23.44200 -12.22400 8.95600   1.000 45.01856  ? 141 LEU A O   1 
ATOM   1088 C CB  . LEU A 1 141 ? -20.72500 -13.92300 7.76200   1.000 44.51586  ? 141 LEU A CB  1 
ATOM   1089 C CG  . LEU A 1 141 ? -19.77500 -14.00500 6.52800   1.000 50.95874  ? 141 LEU A CG  1 
ATOM   1090 C CD1 . LEU A 1 141 ? -18.29000 -14.17200 6.96300   1.000 54.37757  ? 141 LEU A CD1 1 
ATOM   1091 C CD2 . LEU A 1 141 ? -20.21000 -15.13600 5.61200   1.000 49.56384  ? 141 LEU A CD2 1 
ATOM   1092 N N   . ASN A 1 142 ? -23.10200 -14.37300 9.48200   1.000 47.31620  ? 142 ASN A N   1 
ATOM   1093 C CA  . ASN A 1 142 ? -23.74100 -14.18300 10.78900  1.000 48.99272  ? 142 ASN A CA  1 
ATOM   1094 C C   . ASN A 1 142 ? -22.94300 -13.15400 11.57100  1.000 44.98960  ? 142 ASN A C   1 
ATOM   1095 O O   . ASN A 1 142 ? -21.70400 -13.15700 11.55400  1.000 47.39779  ? 142 ASN A O   1 
ATOM   1096 C CB  . ASN A 1 142 ? -23.81600 -15.47300 11.58100  1.000 49.26117  ? 142 ASN A CB  1 
ATOM   1097 C CG  . ASN A 1 142 ? -24.76700 -16.45700 11.01000  1.000 49.90072  ? 142 ASN A CG  1 
ATOM   1098 O OD1 . ASN A 1 142 ? -25.74800 -16.12000 10.33600  1.000 48.48213  ? 142 ASN A OD1 1 
ATOM   1099 N ND2 . ASN A 1 142 ? -24.48300 -17.71800 11.26700  1.000 54.88290  ? 142 ASN A ND2 1 
ATOM   1100 N N   . GLY A 1 143 ? -23.65100 -12.22900 12.18700  1.000 47.44253  ? 143 GLY A N   1 
ATOM   1101 C CA  . GLY A 1 143 ? -23.08800 -11.12000 12.91300  1.000 45.44492  ? 143 GLY A CA  1 
ATOM   1102 C C   . GLY A 1 143 ? -23.17900 -9.80900  12.17700  1.000 42.28665  ? 143 GLY A C   1 
ATOM   1103 O O   . GLY A 1 143 ? -22.84400 -8.76500  12.75200  1.000 44.38427  ? 143 GLY A O   1 
ATOM   1104 N N   . SER A 1 144 ? -23.60300 -9.83200  10.92900  1.000 43.51311  ? 144 SER A N   1 
ATOM   1105 C CA  . SER A 1 144 ? -23.61500 -8.63700  10.09300  1.000 43.26308  ? 144 SER A CA  1 
ATOM   1106 C C   . SER A 1 144 ? -24.91700 -7.83200  10.20700  1.000 39.60475  ? 144 SER A C   1 
ATOM   1107 O O   . SER A 1 144 ? -24.99100 -6.67300  9.75000   1.000 38.02824  ? 144 SER A O   1 
ATOM   1108 C CB  . SER A 1 144 ? -23.37600 -9.01200  8.61800   1.000 44.86064  ? 144 SER A CB  1 
ATOM   1109 O OG  . SER A 1 144 ? -24.38400 -9.87400  8.09800   1.000 44.16582  ? 144 SER A OG  1 
ATOM   1110 N N   . ALA A 1 145 ? -25.96000 -8.41500  10.78100  1.000 44.04212  ? 145 ALA A N   1 
ATOM   1111 C CA  . ALA A 1 145 ? -27.18100 -7.65500  10.93200  1.000 41.14967  ? 145 ALA A CA  1 
ATOM   1112 C C   . ALA A 1 145 ? -26.89900 -6.34300  11.64400  1.000 36.59386  ? 145 ALA A C   1 
ATOM   1113 O O   . ALA A 1 145 ? -26.09800 -6.27900  12.57900  1.000 41.64710  ? 145 ALA A O   1 
ATOM   1114 C CB  . ALA A 1 145 ? -28.24500 -8.48500  11.73400  1.000 36.77809  ? 145 ALA A CB  1 
ATOM   1115 N N   . GLY A 1 146 ? -27.53500 -5.29100  11.16900  1.000 37.92823  ? 146 GLY A N   1 
ATOM   1116 C CA  . GLY A 1 146 ? -27.32400 -3.97000  11.69300  1.000 38.22564  ? 146 GLY A CA  1 
ATOM   1117 C C   . GLY A 1 146 ? -26.32300 -3.18100  10.85800  1.000 38.87045  ? 146 GLY A C   1 
ATOM   1118 O O   . GLY A 1 146 ? -26.23800 -1.96400  11.04100  1.000 39.66002  ? 146 GLY A O   1 
ATOM   1119 N N   . SER A 1 147 ? -25.56700 -3.83400  9.96900   1.000 37.14919  ? 147 SER A N   1 
ATOM   1120 C CA  . SER A 1 147 ? -24.74600 -3.07500  8.99700   1.000 39.29945  ? 147 SER A CA  1 
ATOM   1121 C C   . SER A 1 147 ? -25.67300 -2.23100  8.13600   1.000 42.03399  ? 147 SER A C   1 
ATOM   1122 O O   . SER A 1 147 ? -26.83200 -2.60400  7.89300   1.000 40.48117  ? 147 SER A O   1 
ATOM   1123 C CB  . SER A 1 147 ? -23.91900 -4.01300  8.08500   1.000 35.08842  ? 147 SER A CB  1 
ATOM   1124 O OG  . SER A 1 147 ? -23.18100 -4.95000  8.85900   1.000 37.39659  ? 147 SER A OG  1 
ATOM   1125 N N   . VAL A 1 148 ? -25.18900 -1.06000  7.70500   1.000 38.88361  ? 148 VAL A N   1 
ATOM   1126 C CA  . VAL A 1 148 ? -26.06900 -0.13300  7.01900   1.000 37.67294  ? 148 VAL A CA  1 
ATOM   1127 C C   . VAL A 1 148 ? -25.57800 0.14300   5.60500   1.000 39.38893  ? 148 VAL A C   1 
ATOM   1128 O O   . VAL A 1 148 ? -24.37600 -0.01100  5.24900   1.000 39.48105  ? 148 VAL A O   1 
ATOM   1129 C CB  . VAL A 1 148 ? -26.28900 1.19200   7.81000   1.000 38.30986  ? 148 VAL A CB  1 
ATOM   1130 C CG1 . VAL A 1 148 ? -26.99600 0.99100   9.16600   1.000 37.99140  ? 148 VAL A CG1 1 
ATOM   1131 C CG2 . VAL A 1 148 ? -24.96300 1.96600   7.97800   1.000 37.46765  ? 148 VAL A CG2 1 
ATOM   1132 N N   . GLY A 1 149 ? -26.54500 0.53300   4.76600   1.000 37.05444  ? 149 GLY A N   1 
ATOM   1133 C CA  . GLY A 1 149 ? -26.28300 0.97400   3.40500   1.000 41.04439  ? 149 GLY A CA  1 
ATOM   1134 C C   . GLY A 1 149 ? -26.55900 2.46900   3.36000   1.000 40.60487  ? 149 GLY A C   1 
ATOM   1135 O O   . GLY A 1 149 ? -27.44100 2.97200   4.05200   1.000 38.02298  ? 149 GLY A O   1 
ATOM   1136 N N   . PHE A 1 150 ? -25.80700 3.18100   2.55000   1.000 36.67019  ? 150 PHE A N   1 
ATOM   1137 C CA  . PHE A 1 150 ? -25.84700 4.64200   2.58000   1.000 38.42303  ? 150 PHE A CA  1 
ATOM   1138 C C   . PHE A 1 150 ? -25.34000 5.21100   1.24700   1.000 39.64949  ? 150 PHE A C   1 
ATOM   1139 O O   . PHE A 1 150 ? -24.62200 4.56300   0.49400   1.000 36.66229  ? 150 PHE A O   1 
ATOM   1140 C CB  . PHE A 1 150 ? -24.99100 5.21200   3.72100   1.000 37.51502  ? 150 PHE A CB  1 
ATOM   1141 C CG  . PHE A 1 150 ? -23.52400 4.84600   3.62200   1.000 39.71266  ? 150 PHE A CG  1 
ATOM   1142 C CD1 . PHE A 1 150 ? -23.08600 3.60500   4.10700   1.000 40.50222  ? 150 PHE A CD1 1 
ATOM   1143 C CD2 . PHE A 1 150 ? -22.61500 5.71800   3.08200   1.000 41.03650  ? 150 PHE A CD2 1 
ATOM   1144 C CE1 . PHE A 1 150 ? -21.78200 3.21700   3.99000   1.000 43.37625  ? 150 PHE A CE1 1 
ATOM   1145 C CE2 . PHE A 1 150 ? -21.25400 5.35800   2.96400   1.000 39.89689  ? 150 PHE A CE2 1 
ATOM   1146 C CZ  . PHE A 1 150 ? -20.84200 4.10400   3.40800   1.000 40.37853  ? 150 PHE A CZ  1 
ATOM   1147 N N   . ASN A 1 151 ? -25.74000 6.44900   1.00200   1.000 40.30746  ? 151 ASN A N   1 
ATOM   1148 C CA  . ASN A 1 151 ? -25.21900 7.29900   -0.02500  1.000 44.60798  ? 151 ASN A CA  1 
ATOM   1149 C C   . ASN A 1 151 ? -24.68600 8.55900   0.64400   1.000 48.30579  ? 151 ASN A C   1 
ATOM   1150 O O   . ASN A 1 151 ? -25.12200 8.91800   1.73300   1.000 45.29227  ? 151 ASN A O   1 
ATOM   1151 C CB  . ASN A 1 151 ? -26.28700 7.61600   -1.05700  1.000 39.18628  ? 151 ASN A CB  1 
ATOM   1152 C CG  . ASN A 1 151 ? -26.47800 6.44800   -2.02800  1.000 42.84987  ? 151 ASN A CG  1 
ATOM   1153 O OD1 . ASN A 1 151 ? -25.60100 6.17900   -2.83100  1.000 42.15242  ? 151 ASN A OD1 1 
ATOM   1154 N ND2 . ASN A 1 151 ? -27.59600 5.75800   -1.95100  1.000 38.70201  ? 151 ASN A ND2 1 
ATOM   1155 N N   . ILE A 1 152 ? -23.68900 9.20700   0.02700   1.000 43.80525  ? 152 ILE A N   1 
ATOM   1156 C CA  . ILE A 1 152 ? -23.20400 10.45500  0.58600   1.000 48.95850  ? 152 ILE A CA  1 
ATOM   1157 C C   . ILE A 1 152 ? -23.32700 11.53000  -0.47200  1.000 54.81184  ? 152 ILE A C   1 
ATOM   1158 O O   . ILE A 1 152 ? -22.89600 11.32600  -1.61100  1.000 57.42531  ? 152 ILE A O   1 
ATOM   1159 C CB  . ILE A 1 152 ? -21.75800 10.35100  1.08300   1.000 49.59542  ? 152 ILE A CB  1 
ATOM   1160 C CG1 . ILE A 1 152 ? -21.63000 9.23700   2.11300   1.000 49.87177  ? 152 ILE A CG1 1 
ATOM   1161 C CG2 . ILE A 1 152 ? -21.41600 11.68100  1.76400   1.000 54.95659  ? 152 ILE A CG2 1 
ATOM   1162 C CD1 . ILE A 1 152 ? -20.23700 9.13000   2.82400   1.000 50.81662  ? 152 ILE A CD1 1 
ATOM   1163 N N   . ASP A 1 153 ? -23.89100 12.66800  -0.09100  1.000 61.98112  ? 153 ASP A N   1 
ATOM   1164 C CA  . ASP A 1 153 ? -23.96500 13.86200  -0.92200  1.000 71.76124  ? 153 ASP A CA  1 
ATOM   1165 C C   . ASP A 1 153 ? -23.38300 15.03800  -0.14800  1.000 77.34348  ? 153 ASP A C   1 
ATOM   1166 O O   . ASP A 1 153 ? -23.93300 15.43700  0.88300   1.000 73.10613  ? 153 ASP A O   1 
ATOM   1167 C CB  . ASP A 1 153 ? -25.39700 14.15000  -1.34000  1.000 73.25878  ? 153 ASP A CB  1 
ATOM   1168 C CG  . ASP A 1 153 ? -25.46400 14.85700  -2.65500  1.000 85.06020  ? 153 ASP A CG  1 
ATOM   1169 O OD1 . ASP A 1 153 ? -24.89400 15.96200  -2.74700  1.000 91.40306  ? 153 ASP A OD1 1 
ATOM   1170 O OD2 . ASP A 1 153 ? -26.04900 14.29400  -3.61000  1.000 89.17385  ? 153 ASP A OD2 1 
ATOM   1171 N N   . TYR A 1 154 ? -22.29200 15.60700  -0.67600  1.000 95.57199  ? 154 TYR A N   1 
ATOM   1172 C CA  . TYR A 1 154 ? -21.45200 16.59500  0.00300   1.000 90.27398  ? 154 TYR A CA  1 
ATOM   1173 C C   . TYR A 1 154 ? -20.92600 15.99800  1.29300   1.000 91.48728  ? 154 TYR A C   1 
ATOM   1174 O O   . TYR A 1 154 ? -20.03600 15.13500  1.26900   1.000 97.93279  ? 154 TYR A O   1 
ATOM   1175 C CB  . TYR A 1 154 ? -22.19200 17.90800  0.27600   1.000 94.60345  ? 154 TYR A CB  1 
ATOM   1176 C CG  . TYR A 1 154 ? -22.96700 18.41200  -0.92200  1.000 109.39996 ? 154 TYR A CG  1 
ATOM   1177 C CD1 . TYR A 1 154 ? -22.30000 18.94000  -2.03500  1.000 109.53419 ? 154 TYR A CD1 1 
ATOM   1178 C CD2 . TYR A 1 154 ? -24.36500 18.34400  -0.95500  1.000 105.70741 ? 154 TYR A CD2 1 
ATOM   1179 C CE1 . TYR A 1 154 ? -23.00700 19.39800  -3.14600  1.000 116.02970 ? 154 TYR A CE1 1 
ATOM   1180 C CE2 . TYR A 1 154 ? -25.08500 18.80300  -2.06200  1.000 111.42125 ? 154 TYR A CE2 1 
ATOM   1181 C CZ  . TYR A 1 154 ? -24.40200 19.32600  -3.15500  1.000 121.35666 ? 154 TYR A CZ  1 
ATOM   1182 O OH  . TYR A 1 154 ? -25.11800 19.77600  -4.25000  1.000 130.05507 ? 154 TYR A OH  1 
ATOM   1183 N N   . ASP A 1 155 ? -21.48400 16.42700  2.41900   1.000 76.78026  ? 155 ASP A N   1 
ATOM   1184 C CA  . ASP A 1 155 ? -21.13200 15.82700  3.69900   1.000 77.94882  ? 155 ASP A CA  1 
ATOM   1185 C C   . ASP A 1 155 ? -22.36000 15.25500  4.39900   1.000 68.60033  ? 155 ASP A C   1 
ATOM   1186 O O   . ASP A 1 155 ? -22.28800 14.94300  5.59300   1.000 66.86854  ? 155 ASP A O   1 
ATOM   1187 C CB  . ASP A 1 155 ? -20.40800 16.84500  4.60500   1.000 82.05458  ? 155 ASP A CB  1 
ATOM   1188 C CG  . ASP A 1 155 ? -18.93900 17.13400  4.15500   1.000 89.21596  ? 155 ASP A CG  1 
ATOM   1189 O OD1 . ASP A 1 155 ? -18.21600 16.21000  3.67300   1.000 84.87070  ? 155 ASP A OD1 1 
ATOM   1190 O OD2 . ASP A 1 155 ? -18.49600 18.29800  4.32500   1.000 92.57163  ? 155 ASP A OD2 1 
ATOM   1191 N N   . CYS A 1 156 ? -23.47300 15.10500  3.67100   1.000 64.28139  ? 156 CYS A N   1 
ATOM   1192 C CA  . CYS A 1 156 ? -24.72600 14.55600  4.19400   1.000 58.03064  ? 156 CYS A CA  1 
ATOM   1193 C C   . CYS A 1 156 ? -24.81800 13.07300  3.84200   1.000 53.47220  ? 156 CYS A C   1 
ATOM   1194 O O   . CYS A 1 156 ? -24.78500 12.69600  2.65600   1.000 50.56922  ? 156 CYS A O   1 
ATOM   1195 C CB  . CYS A 1 156 ? -25.92900 15.31800  3.64400   1.000 55.20136  ? 156 CYS A CB  1 
ATOM   1196 S SG  . CYS A 1 156 ? -27.56100 14.80200  4.34500   1.000 63.75764  ? 156 CYS A SG  1 
ATOM   1197 N N   . VAL A 1 157 ? -24.91000 12.24400  4.87900   1.000 49.50330  ? 157 VAL A N   1 
ATOM   1198 C CA  . VAL A 1 157 ? -25.06100 10.80600  4.74600   1.000 44.97908  ? 157 VAL A CA  1 
ATOM   1199 C C   . VAL A 1 157 ? -26.54300 10.47200  4.67900   1.000 46.20817  ? 157 VAL A C   1 
ATOM   1200 O O   . VAL A 1 157 ? -27.26200 10.73900  5.64100   1.000 45.59231  ? 157 VAL A O   1 
ATOM   1201 C CB  . VAL A 1 157 ? -24.44900 10.08200  5.94400   1.000 44.68957  ? 157 VAL A CB  1 
ATOM   1202 C CG1 . VAL A 1 157 ? -24.67100 8.57100   5.74900   1.000 41.45234  ? 157 VAL A CG1 1 
ATOM   1203 C CG2 . VAL A 1 157 ? -22.97800 10.45500  6.10200   1.000 48.98219  ? 157 VAL A CG2 1 
ATOM   1204 N N   . SER A 1 158 ? -26.99300 9.84700   3.59700   1.000 42.55247  ? 158 SER A N   1 
ATOM   1205 C CA  . SER A 1 158 ? -28.39900 9.38600   3.51200   1.000 43.22624  ? 158 SER A CA  1 
ATOM   1206 C C   . SER A 1 158 ? -28.39500 7.89300   3.79300   1.000 40.36800  ? 158 SER A C   1 
ATOM   1207 O O   . SER A 1 158 ? -28.01200 7.08900   2.94100   1.000 39.59159  ? 158 SER A O   1 
ATOM   1208 C CB  . SER A 1 158 ? -29.00600 9.68800   2.15000   1.000 46.08447  ? 158 SER A CB  1 
ATOM   1209 O OG  . SER A 1 158 ? -29.23900 11.09200  2.02600   1.000 50.08495  ? 158 SER A OG  1 
ATOM   1210 N N   . PHE A 1 159 ? -28.78300 7.51100   5.00500   1.000 39.92058  ? 159 PHE A N   1 
ATOM   1211 C CA  . PHE A 1 159 ? -28.91100 6.09200   5.30100   1.000 39.40736  ? 159 PHE A CA  1 
ATOM   1212 C C   . PHE A 1 159 ? -30.18500 5.55000   4.66900   1.000 43.59996  ? 159 PHE A C   1 
ATOM   1213 O O   . PHE A 1 159 ? -31.28200 6.06600   4.93500   1.000 43.44995  ? 159 PHE A O   1 
ATOM   1214 C CB  . PHE A 1 159 ? -28.97600 5.85900   6.80100   1.000 42.47088  ? 159 PHE A CB  1 
ATOM   1215 C CG  . PHE A 1 159 ? -27.75500 6.26200   7.51700   1.000 40.28641  ? 159 PHE A CG  1 
ATOM   1216 C CD1 . PHE A 1 159 ? -26.62100 5.43900   7.47700   1.000 41.15230  ? 159 PHE A CD1 1 
ATOM   1217 C CD2 . PHE A 1 159 ? -27.70700 7.45500   8.21000   1.000 42.12874  ? 159 PHE A CD2 1 
ATOM   1218 C CE1 . PHE A 1 159 ? -25.43400 5.80900   8.14800   1.000 37.21236  ? 159 PHE A CE1 1 
ATOM   1219 C CE2 . PHE A 1 159 ? -26.50300 7.85000   8.87500   1.000 45.26069  ? 159 PHE A CE2 1 
ATOM   1220 C CZ  . PHE A 1 159 ? -25.40100 7.01800   8.86000   1.000 42.40772  ? 159 PHE A CZ  1 
ATOM   1221 N N   . CYS A 1 160 ? -30.05200 4.44500   3.94500   1.000 39.12311  ? 160 CYS A N   1 
ATOM   1222 C CA  . CYS A 1 160 ? -31.16600 3.84500   3.23600   1.000 43.21571  ? 160 CYS A CA  1 
ATOM   1223 C C   . CYS A 1 160 ? -31.43400 2.37100   3.54800   1.000 41.01281  ? 160 CYS A C   1 
ATOM   1224 O O   . CYS A 1 160 ? -32.47500 1.85200   3.11200   1.000 43.27361  ? 160 CYS A O   1 
ATOM   1225 C CB  . CYS A 1 160 ? -30.95500 3.97600   1.72300   1.000 41.66289  ? 160 CYS A CB  1 
ATOM   1226 S SG  . CYS A 1 160 ? -29.48600 3.19100   1.00600   1.000 38.11246  ? 160 CYS A SG  1 
ATOM   1227 N N   . TYR A 1 161 ? -30.54500 1.66500   4.23300   1.000 39.84951  ? 161 TYR A N   1 
ATOM   1228 C CA  . TYR A 1 161 ? -30.69600 0.22000   4.37400   1.000 39.88636  ? 161 TYR A CA  1 
ATOM   1229 C C   . TYR A 1 161 ? -30.09200 -0.20000  5.69400   1.000 38.04140  ? 161 TYR A C   1 
ATOM   1230 O O   . TYR A 1 161 ? -29.04200 0.29900   6.06300   1.000 38.50198  ? 161 TYR A O   1 
ATOM   1231 C CB  . TYR A 1 161 ? -30.02300 -0.51500  3.18200   1.000 37.49134  ? 161 TYR A CB  1 
ATOM   1232 C CG  . TYR A 1 161 ? -30.04500 -2.03000  3.29000   1.000 38.83097  ? 161 TYR A CG  1 
ATOM   1233 C CD1 . TYR A 1 161 ? -31.14400 -2.74500  2.84300   1.000 37.22025  ? 161 TYR A CD1 1 
ATOM   1234 C CD2 . TYR A 1 161 ? -28.98500 -2.74400  3.89900   1.000 36.46753  ? 161 TYR A CD2 1 
ATOM   1235 C CE1 . TYR A 1 161 ? -31.17700 -4.12200  2.95600   1.000 38.95467  ? 161 TYR A CE1 1 
ATOM   1236 C CE2 . TYR A 1 161 ? -28.99500 -4.10000  3.97800   1.000 37.19130  ? 161 TYR A CE2 1 
ATOM   1237 C CZ  . TYR A 1 161 ? -30.13500 -4.78600  3.55200   1.000 37.33079  ? 161 TYR A CZ  1 
ATOM   1238 O OH  . TYR A 1 161 ? -30.26000 -6.17700  3.58400   1.000 37.70715  ? 161 TYR A OH  1 
ATOM   1239 N N   . MET A 1 162 ? -30.76200 -1.09400  6.41900   1.000 36.56754  ? 162 MET A N   1 
ATOM   1240 C CA  . MET A 1 162 ? -30.14700 -1.77100  7.54900   1.000 37.19920  ? 162 MET A CA  1 
ATOM   1241 C C   . MET A 1 162 ? -30.29000 -3.25600  7.26900   1.000 39.80477  ? 162 MET A C   1 
ATOM   1242 O O   . MET A 1 162 ? -31.39000 -3.71900  6.91300   1.000 40.03901  ? 162 MET A O   1 
ATOM   1243 C CB  . MET A 1 162 ? -30.77200 -1.39000  8.90600   1.000 40.46538  ? 162 MET A CB  1 
ATOM   1244 C CG  . MET A 1 162 ? -30.13500 -2.10700  10.15100  1.000 38.09667  ? 162 MET A CG  1 
ATOM   1245 S SD  . MET A 1 162 ? -30.61000 -1.29600  11.73600  1.000 47.88206  ? 162 MET A SD  1 
ATOM   1246 C CE  . MET A 1 162 ? -29.12100 -0.22300  11.85700  1.000 46.28186  ? 162 MET A CE  1 
ATOM   1247 N N   . HIS A 1 163 ? -29.20000 -4.00600  7.44200   1.000 34.60415  ? 163 HIS A N   1 
ATOM   1248 C CA  . HIS A 1 163 ? -29.22000 -5.43400  7.13000   1.000 39.32577  ? 163 HIS A CA  1 
ATOM   1249 C C   . HIS A 1 163 ? -29.93600 -6.25300  8.21000   1.000 34.12251  ? 163 HIS A C   1 
ATOM   1250 O O   . HIS A 1 163 ? -29.71800 -6.05400  9.41400   1.000 35.94378  ? 163 HIS A O   1 
ATOM   1251 C CB  . HIS A 1 163 ? -27.81200 -5.98700  6.97300   1.000 36.75967  ? 163 HIS A CB  1 
ATOM   1252 C CG  . HIS A 1 163 ? -27.81100 -7.41000  6.51900   1.000 34.41992  ? 163 HIS A CG  1 
ATOM   1253 N ND1 . HIS A 1 163 ? -28.53300 -7.81400  5.42300   1.000 34.75154  ? 163 HIS A ND1 1 
ATOM   1254 C CD2 . HIS A 1 163 ? -27.25000 -8.52500  7.03600   1.000 35.57532  ? 163 HIS A CD2 1 
ATOM   1255 C CE1 . HIS A 1 163 ? -28.38300 -9.11200  5.24600   1.000 34.52256  ? 163 HIS A CE1 1 
ATOM   1256 N NE2 . HIS A 1 163 ? -27.59500 -9.56800  6.20100   1.000 36.79125  ? 163 HIS A NE2 1 
ATOM   1257 N N   . HIS A 1 164 ? -30.76900 -7.21900  7.78000   1.000 38.04404  ? 164 HIS A N   1 
ATOM   1258 C CA  . HIS A 1 164 ? -31.37700 -8.16000  8.72100   1.000 40.09691  ? 164 HIS A CA  1 
ATOM   1259 C C   . HIS A 1 164 ? -31.06200 -9.61000  8.39500   1.000 36.46227  ? 164 HIS A C   1 
ATOM   1260 O O   . HIS A 1 164 ? -30.63400 -10.35500 9.28300   1.000 40.72067  ? 164 HIS A O   1 
ATOM   1261 C CB  . HIS A 1 164 ? -32.92000 -7.98000  8.80300   1.000 37.54134  ? 164 HIS A CB  1 
ATOM   1262 C CG  . HIS A 1 164 ? -33.32000 -6.66600  9.42300   1.000 42.22085  ? 164 HIS A CG  1 
ATOM   1263 N ND1 . HIS A 1 164 ? -34.05800 -6.56200  10.58300  1.000 40.29694  ? 164 HIS A ND1 1 
ATOM   1264 C CD2 . HIS A 1 164 ? -33.10700 -5.39200  9.00400   1.000 41.32074  ? 164 HIS A CD2 1 
ATOM   1265 C CE1 . HIS A 1 164 ? -34.26300 -5.28600  10.87000  1.000 39.23892  ? 164 HIS A CE1 1 
ATOM   1266 N NE2 . HIS A 1 164 ? -33.71200 -4.55500  9.91100   1.000 41.88923  ? 164 HIS A NE2 1 
ATOM   1267 N N   . MET A 1 165 ? -31.27300 -10.05600 7.17000   1.000 37.25183  ? 165 MET A N   1 
ATOM   1268 C CA  . MET A 1 165 ? -31.29400 -11.50300 7.01200   1.000 41.82080  ? 165 MET A CA  1 
ATOM   1269 C C   . MET A 1 165 ? -30.80600 -11.94500 5.63900   1.000 40.92333  ? 165 MET A C   1 
ATOM   1270 O O   . MET A 1 165 ? -30.63500 -11.15900 4.68400   1.000 39.58633  ? 165 MET A O   1 
ATOM   1271 C CB  . MET A 1 165 ? -32.71500 -12.03100 7.26900   1.000 40.05217  ? 165 MET A CB  1 
ATOM   1272 C CG  . MET A 1 165 ? -33.71700 -11.47700 6.34800   1.000 35.90167  ? 165 MET A CG  1 
ATOM   1273 S SD  . MET A 1 165 ? -35.35400 -11.91800 7.10100   1.000 47.40568  ? 165 MET A SD  1 
ATOM   1274 C CE  . MET A 1 165 ? -36.35500 -11.80200 5.65600   1.000 44.95802  ? 165 MET A CE  1 
ATOM   1275 N N   . GLU A 1 166 ? -30.56300 -13.23600 5.55300   1.000 42.49720  ? 166 GLU A N   1 
ATOM   1276 C CA  . GLU A 1 166 ? -30.19600 -13.85300 4.29300   1.000 45.91603  ? 166 GLU A CA  1 
ATOM   1277 C C   . GLU A 1 166 ? -31.27800 -14.83400 3.88700   1.000 45.03435  ? 166 GLU A C   1 
ATOM   1278 O O   . GLU A 1 166 ? -31.73100 -15.65100 4.70500   1.000 44.68430  ? 166 GLU A O   1 
ATOM   1279 C CB  . GLU A 1 166 ? -28.84500 -14.56200 4.38400   1.000 43.26045  ? 166 GLU A CB  1 
ATOM   1280 C CG  . GLU A 1 166 ? -28.44500 -15.23600 3.11700   1.000 43.96317  ? 166 GLU A CG  1 
ATOM   1281 C CD  . GLU A 1 166 ? -26.98800 -15.66400 3.16000   1.000 47.15565  ? 166 GLU A CD  1 
ATOM   1282 O OE1 . GLU A 1 166 ? -26.10800 -14.79300 3.39100   1.000 46.47663  ? 166 GLU A OE1 1 
ATOM   1283 O OE2 . GLU A 1 166 ? -26.72300 -16.86800 2.96300   1.000 51.26141  ? 166 GLU A OE2 1 
ATOM   1284 N N   . LEU A 1 167 ? -31.70200 -14.73600 2.64200   1.000 44.53429  ? 167 LEU A N   1 
ATOM   1285 C CA  . LEU A 1 167 ? -32.73100 -15.61000 2.08100   1.000 42.63669  ? 167 LEU A CA  1 
ATOM   1286 C C   . LEU A 1 167 ? -32.09600 -16.88300 1.56500   1.000 50.00863  ? 167 LEU A C   1 
ATOM   1287 O O   . LEU A 1 167 ? -30.87400 -16.97800 1.48100   1.000 48.65847  ? 167 LEU A O   1 
ATOM   1288 C CB  . LEU A 1 167 ? -33.48100 -14.89400 0.97700   1.000 40.98386  ? 167 LEU A CB  1 
ATOM   1289 C CG  . LEU A 1 167 ? -34.31500 -13.75600 1.54900   1.000 42.41298  ? 167 LEU A CG  1 
ATOM   1290 C CD1 . LEU A 1 167 ? -34.93800 -12.94500 0.43200   1.000 41.26284  ? 167 LEU A CD1 1 
ATOM   1291 C CD2 . LEU A 1 167 ? -35.44300 -14.26100 2.51800   1.000 47.08986  ? 167 LEU A CD2 1 
ATOM   1292 N N   . PRO A 1 168 ? -32.90500 -17.92300 1.27900   1.000 51.61408  ? 168 PRO A N   1 
ATOM   1293 C CA  . PRO A 1 168 ? -32.31900 -19.21600 0.90600   1.000 48.15314  ? 168 PRO A CA  1 
ATOM   1294 C C   . PRO A 1 168 ? -31.51200 -19.17000 -0.36600  1.000 49.81913  ? 168 PRO A C   1 
ATOM   1295 O O   . PRO A 1 168 ? -30.59700 -19.98800 -0.50200  1.000 53.21954  ? 168 PRO A O   1 
ATOM   1296 C CB  . PRO A 1 168 ? -33.54700 -20.13300 0.77100   1.000 55.15398  ? 168 PRO A CB  1 
ATOM   1297 C CG  . PRO A 1 168 ? -34.54700 -19.55600 1.68200   1.000 54.83289  ? 168 PRO A CG  1 
ATOM   1298 C CD  . PRO A 1 168 ? -34.35200 -18.05200 1.53800   1.000 51.38248  ? 168 PRO A CD  1 
ATOM   1299 N N   . THR A 1 169 ? -31.78200 -18.24100 -1.30100  1.000 48.50055  ? 169 THR A N   1 
ATOM   1300 C CA  . THR A 1 169 ? -30.92000 -18.15900 -2.50300  1.000 48.54529  ? 169 THR A CA  1 
ATOM   1301 C C   . THR A 1 169 ? -29.56400 -17.48500 -2.26000  1.000 50.39288  ? 169 THR A C   1 
ATOM   1302 O O   . THR A 1 169 ? -28.75600 -17.37100 -3.19300  1.000 49.26380  ? 169 THR A O   1 
ATOM   1303 C CB  . THR A 1 169 ? -31.66000 -17.43100 -3.63300  1.000 49.08220  ? 169 THR A CB  1 
ATOM   1304 O OG1 . THR A 1 169 ? -32.18000 -16.19300 -3.13200  1.000 49.99284  ? 169 THR A OG1 1 
ATOM   1305 C CG2 . THR A 1 169 ? -32.84900 -18.27500 -4.16800  1.000 49.64279  ? 169 THR A CG2 1 
ATOM   1306 N N   . GLY A 1 170 ? -29.25800 -17.04800 -1.04200  1.000 44.74221  ? 170 GLY A N   1 
ATOM   1307 C CA  . GLY A 1 170 ? -27.99200 -16.41100 -0.78600  1.000 48.82691  ? 170 GLY A CA  1 
ATOM   1308 C C   . GLY A 1 170 ? -28.03600 -14.90700 -0.92900  1.000 46.65296  ? 170 GLY A C   1 
ATOM   1309 O O   . GLY A 1 170 ? -26.99700 -14.27600 -0.78400  1.000 47.25303  ? 170 GLY A O   1 
ATOM   1310 N N   . VAL A 1 171 ? -29.21400 -14.32000 -1.19200  1.000 42.43667  ? 171 VAL A N   1 
ATOM   1311 C CA  . VAL A 1 171 ? -29.36600 -12.86400 -1.28900  1.000 41.28127  ? 171 VAL A CA  1 
ATOM   1312 C C   . VAL A 1 171 ? -29.91300 -12.31400 0.02800   1.000 41.39180  ? 171 VAL A C   1 
ATOM   1313 O O   . VAL A 1 171 ? -30.22000 -13.07700 0.95100   1.000 40.70751  ? 171 VAL A O   1 
ATOM   1314 C CB  . VAL A 1 171 ? -30.25400 -12.44400 -2.47200  1.000 40.02322  ? 171 VAL A CB  1 
ATOM   1315 C CG1 . VAL A 1 171 ? -29.64400 -12.91100 -3.86000  1.000 45.20542  ? 171 VAL A CG1 1 
ATOM   1316 C CG2 . VAL A 1 171 ? -31.71400 -12.94400 -2.30000  1.000 36.41226  ? 171 VAL A CG2 1 
ATOM   1317 N N   . HIS A 1 172 ? -30.03100 -10.99500 0.13100   1.000 38.75465  ? 172 HIS A N   1 
ATOM   1318 C CA  . HIS A 1 172 ? -30.10400 -10.35500 1.43800   1.000 41.56288  ? 172 HIS A CA  1 
ATOM   1319 C C   . HIS A 1 172 ? -31.29600 -9.42000  1.46800   1.000 37.65188  ? 172 HIS A C   1 
ATOM   1320 O O   . HIS A 1 172 ? -31.78000 -8.98400  0.42000   1.000 37.78085  ? 172 HIS A O   1 
ATOM   1321 C CB  . HIS A 1 172 ? -28.76600 -9.63200  1.75400   1.000 39.45999  ? 172 HIS A CB  1 
ATOM   1322 C CG  . HIS A 1 172 ? -27.61600 -10.57900 1.78700   1.000 42.01293  ? 172 HIS A CG  1 
ATOM   1323 N ND1 . HIS A 1 172 ? -26.65800 -10.61900 0.79200   1.000 40.82595  ? 172 HIS A ND1 1 
ATOM   1324 C CD2 . HIS A 1 172 ? -27.30800 -11.58200 2.64900   1.000 40.57065  ? 172 HIS A CD2 1 
ATOM   1325 C CE1 . HIS A 1 172 ? -25.75900 -11.54200 1.08400   1.000 40.71804  ? 172 HIS A CE1 1 
ATOM   1326 N NE2 . HIS A 1 172 ? -26.11300 -12.13000 2.21500   1.000 42.33139  ? 172 HIS A NE2 1 
ATOM   1327 N N   . ALA A 1 173 ? -31.86900 -9.27600  2.65700   1.000 40.56539  ? 173 ALA A N   1 
ATOM   1328 C CA  . ALA A 1 173 ? -33.10900 -8.53900  2.85600   1.000 36.05432  ? 173 ALA A CA  1 
ATOM   1329 C C   . ALA A 1 173 ? -32.94000 -7.69000  4.09900   1.000 35.94378  ? 173 ALA A C   1 
ATOM   1330 O O   . ALA A 1 173 ? -32.33200 -8.11200  5.09500   1.000 39.23102  ? 173 ALA A O   1 
ATOM   1331 C CB  . ALA A 1 173 ? -34.32300 -9.48900  3.01100   1.000 37.25183  ? 173 ALA A CB  1 
ATOM   1332 N N   . GLY A 1 174 ? -33.48500 -6.50800  4.05600   1.000 36.63860  ? 174 GLY A N   1 
ATOM   1333 C CA  . GLY A 1 174 ? -33.39200 -5.64700  5.19700   1.000 39.56264  ? 174 GLY A CA  1 
ATOM   1334 C C   . GLY A 1 174 ? -34.42700 -4.55900  5.13700   1.000 38.50988  ? 174 GLY A C   1 
ATOM   1335 O O   . GLY A 1 174 ? -35.33400 -4.59400  4.29000   1.000 37.92823  ? 174 GLY A O   1 
ATOM   1336 N N   . THR A 1 175 ? -34.21500 -3.54300  5.97500   1.000 35.31739  ? 175 THR A N   1 
ATOM   1337 C CA  . THR A 1 175 ? -35.20800 -2.49300  6.19700   1.000 38.47303  ? 175 THR A CA  1 
ATOM   1338 C C   . THR A 1 175 ? -34.64800 -1.13500  5.81300   1.000 41.25758  ? 175 THR A C   1 
ATOM   1339 O O   . THR A 1 175 ? -33.43000 -0.96300  5.65300   1.000 38.45724  ? 175 THR A O   1 
ATOM   1340 C CB  . THR A 1 175 ? -35.66800 -2.43600  7.65700   1.000 40.90227  ? 175 THR A CB  1 
ATOM   1341 O OG1 . THR A 1 175 ? -34.57700 -2.11000  8.58000   1.000 37.43080  ? 175 THR A OG1 1 
ATOM   1342 C CG2 . THR A 1 175 ? -36.30200 -3.74400  8.04800   1.000 42.23664  ? 175 THR A CG2 1 
ATOM   1343 N N   . ASP A 1 176 ? -35.55400 -0.16800  5.67200   1.000 39.69423  ? 176 ASP A N   1 
ATOM   1344 C CA  . ASP A 1 176 ? -35.10800 1.20900   5.79800   1.000 38.47040  ? 176 ASP A CA  1 
ATOM   1345 C C   . ASP A 1 176 ? -34.82900 1.50000   7.27600   1.000 38.16247  ? 176 ASP A C   1 
ATOM   1346 O O   . ASP A 1 176 ? -34.94200 0.62100   8.15600   1.000 38.01245  ? 176 ASP A O   1 
ATOM   1347 C CB  . ASP A 1 176 ? -36.10200 2.17300   5.15300   1.000 38.68622  ? 176 ASP A CB  1 
ATOM   1348 C CG  . ASP A 1 176 ? -37.45100 2.17900   5.85300   1.000 43.00516  ? 176 ASP A CG  1 
ATOM   1349 O OD1 . ASP A 1 176 ? -37.51000 1.92100   7.05700   1.000 40.72067  ? 176 ASP A OD1 1 
ATOM   1350 O OD2 . ASP A 1 176 ? -38.44400 2.47300   5.20300   1.000 45.90287  ? 176 ASP A OD2 1 
ATOM   1351 N N   . LEU A 1 177 ? -34.37700 2.72300   7.57000   1.000 36.58070  ? 177 LEU A N   1 
ATOM   1352 C CA  . LEU A 1 177 ? -33.99300 3.06900   8.93300   1.000 40.82595  ? 177 LEU A CA  1 
ATOM   1353 C C   . LEU A 1 177 ? -35.18700 3.43300   9.82200   1.000 44.96855  ? 177 LEU A C   1 
ATOM   1354 O O   . LEU A 1 177 ? -34.97400 3.69300   10.99300  1.000 43.28414  ? 177 LEU A O   1 
ATOM   1355 C CB  . LEU A 1 177 ? -32.95300 4.21500   8.96000   1.000 41.35496  ? 177 LEU A CB  1 
ATOM   1356 C CG  . LEU A 1 177 ? -31.47900 3.72300   8.87300   1.000 40.17850  ? 177 LEU A CG  1 
ATOM   1357 C CD1 . LEU A 1 177 ? -31.10900 2.99000   10.19700  1.000 42.16295  ? 177 LEU A CD1 1 
ATOM   1358 C CD2 . LEU A 1 177 ? -31.17000 2.85300   7.62600   1.000 38.11510  ? 177 LEU A CD2 1 
ATOM   1359 N N   . GLU A 1 178 ? -36.40500 3.45200   9.28500   1.000 43.05779  ? 178 GLU A N   1 
ATOM   1360 C CA  . GLU A 1 178 ? -37.64600 3.42600   10.05700  1.000 50.15075  ? 178 GLU A CA  1 
ATOM   1361 C C   . GLU A 1 178 ? -38.13500 2.02500   10.35800  1.000 45.95025  ? 178 GLU A C   1 
ATOM   1362 O O   . GLU A 1 178 ? -39.19700 1.88000   10.95500  1.000 47.56097  ? 178 GLU A O   1 
ATOM   1363 C CB  . GLU A 1 178 ? -38.75200 4.20800   9.33300   1.000 48.82164  ? 178 GLU A CB  1 
ATOM   1364 C CG  . GLU A 1 178 ? -38.55000 5.69800   9.51700   1.000 58.37542  ? 178 GLU A CG  1 
ATOM   1365 C CD  . GLU A 1 178 ? -39.50300 6.54400   8.72100   1.000 70.70848  ? 178 GLU A CD  1 
ATOM   1366 O OE1 . GLU A 1 178 ? -40.38700 5.98600   8.02200   1.000 71.39277  ? 178 GLU A OE1 1 
ATOM   1367 O OE2 . GLU A 1 178 ? -39.42200 7.78200   8.88100   1.000 86.00242  ? 178 GLU A OE2 1 
ATOM   1368 N N   . GLY A 1 179 ? -37.39600 1.00500   9.95100   1.000 42.08399  ? 179 GLY A N   1 
ATOM   1369 C CA  . GLY A 1 179 ? -37.67700 -0.37600  10.24600  1.000 41.48392  ? 179 GLY A CA  1 
ATOM   1370 C C   . GLY A 1 179 ? -38.62600 -1.07400  9.28800   1.000 45.15541  ? 179 GLY A C   1 
ATOM   1371 O O   . GLY A 1 179 ? -39.01500 -2.21400  9.56700   1.000 42.05504  ? 179 GLY A O   1 
ATOM   1372 N N   . ASN A 1 180 ? -39.02600 -0.44500  8.17500   1.000 41.37338  ? 180 ASN A N   1 
ATOM   1373 C CA  . ASN A 1 180 ? -39.91000 -1.13500  7.22500   1.000 44.28689  ? 180 ASN A CA  1 
ATOM   1374 C C   . ASN A 1 180 ? -39.10700 -1.96500  6.24300   1.000 42.86830  ? 180 ASN A C   1 
ATOM   1375 O O   . ASN A 1 180 ? -38.18400 -1.44300  5.61400   1.000 39.12048  ? 180 ASN A O   1 
ATOM   1376 C CB  . ASN A 1 180 ? -40.76000 -0.12700  6.46800   1.000 43.49206  ? 180 ASN A CB  1 
ATOM   1377 C CG  . ASN A 1 180 ? -41.71600 0.58800   7.36500   1.000 48.10050  ? 180 ASN A CG  1 
ATOM   1378 O OD1 . ASN A 1 180 ? -42.53200 -0.01700  8.11900   1.000 47.77152  ? 180 ASN A OD1 1 
ATOM   1379 N ND2 . ASN A 1 180 ? -41.62100 1.89200   7.33000   1.000 54.91448  ? 180 ASN A ND2 1 
ATOM   1380 N N   . PHE A 1 181 ? -39.45200 -3.25300  6.09200   1.000 41.25231  ? 181 PHE A N   1 
ATOM   1381 C CA  . PHE A 1 181 ? -38.72800 -4.07000  5.13100   1.000 43.09201  ? 181 PHE A CA  1 
ATOM   1382 C C   . PHE A 1 181 ? -38.90100 -3.52500  3.73200   1.000 42.51299  ? 181 PHE A C   1 
ATOM   1383 O O   . PHE A 1 181 ? -39.98600 -3.03800  3.35800   1.000 38.53620  ? 181 PHE A O   1 
ATOM   1384 C CB  . PHE A 1 181 ? -39.18200 -5.53400  5.15200   1.000 41.20757  ? 181 PHE A CB  1 
ATOM   1385 C CG  . PHE A 1 181 ? -38.32500 -6.39800  6.01700   1.000 41.57867  ? 181 PHE A CG  1 
ATOM   1386 C CD1 . PHE A 1 181 ? -37.15800 -6.96100  5.49700   1.000 40.48643  ? 181 PHE A CD1 1 
ATOM   1387 C CD2 . PHE A 1 181 ? -38.60300 -6.51900  7.39600   1.000 39.61264  ? 181 PHE A CD2 1 
ATOM   1388 C CE1 . PHE A 1 181 ? -36.32800 -7.72200  6.32600   1.000 39.04152  ? 181 PHE A CE1 1 
ATOM   1389 C CE2 . PHE A 1 181 ? -37.79500 -7.25000  8.23300   1.000 40.59171  ? 181 PHE A CE2 1 
ATOM   1390 C CZ  . PHE A 1 181 ? -36.62600 -7.85100  7.71100   1.000 43.07622  ? 181 PHE A CZ  1 
ATOM   1391 N N   . TYR A 1 182 ? -37.79400 -3.57500  2.97300   1.000 37.42817  ? 182 TYR A N   1 
ATOM   1392 C CA  . TYR A 1 182 ? -37.90800 -3.58200  1.52900   1.000 33.08028  ? 182 TYR A CA  1 
ATOM   1393 C C   . TYR A 1 182 ? -38.44700 -4.93400  1.12100   1.000 34.86471  ? 182 TYR A C   1 
ATOM   1394 O O   . TYR A 1 182 ? -37.94100 -5.95800  1.57500   1.000 37.70452  ? 182 TYR A O   1 
ATOM   1395 C CB  . TYR A 1 182 ? -36.51400 -3.32100  0.87100   1.000 34.32254  ? 182 TYR A CB  1 
ATOM   1396 C CG  . TYR A 1 182 ? -36.04400 -1.91000  1.13400   1.000 34.01197  ? 182 TYR A CG  1 
ATOM   1397 C CD1 . TYR A 1 182 ? -36.53900 -0.84400  0.38500   1.000 38.10457  ? 182 TYR A CD1 1 
ATOM   1398 C CD2 . TYR A 1 182 ? -35.07700 -1.64700  2.11800   1.000 38.77307  ? 182 TYR A CD2 1 
ATOM   1399 C CE1 . TYR A 1 182 ? -36.09800 0.46500   0.61500   1.000 43.42100  ? 182 TYR A CE1 1 
ATOM   1400 C CE2 . TYR A 1 182 ? -34.64400 -0.34800  2.36900   1.000 36.55175  ? 182 TYR A CE2 1 
ATOM   1401 C CZ  . TYR A 1 182 ? -35.11000 0.67500   1.59300   1.000 40.19429  ? 182 TYR A CZ  1 
ATOM   1402 O OH  . TYR A 1 182 ? -34.69100 1.92000   1.85900   1.000 41.82344  ? 182 TYR A OH  1 
ATOM   1403 N N   . GLY A 1 183 ? -39.47900 -4.95400  0.29700   1.000 36.59649  ? 183 GLY A N   1 
ATOM   1404 C CA  . GLY A 1 183 ? -39.97800 -6.22200  -0.21900  1.000 38.39671  ? 183 GLY A CA  1 
ATOM   1405 C C   . GLY A 1 183 ? -40.96100 -6.87900  0.75500   1.000 39.25471  ? 183 GLY A C   1 
ATOM   1406 O O   . GLY A 1 183 ? -41.12800 -6.44100  1.88900   1.000 39.05995  ? 183 GLY A O   1 
ATOM   1407 N N   . PRO A 1 184 ? -41.53100 -8.00300  0.35100   1.000 40.83384  ? 184 PRO A N   1 
ATOM   1408 C CA  . PRO A 1 184 ? -42.57300 -8.72000  1.15300   1.000 42.43404  ? 184 PRO A CA  1 
ATOM   1409 C C   . PRO A 1 184 ? -41.95400 -9.71100  2.13700   1.000 45.70022  ? 184 PRO A C   1 
ATOM   1410 O O   . PRO A 1 184 ? -42.19900 -10.89800 2.06200   1.000 49.90335  ? 184 PRO A O   1 
ATOM   1411 C CB  . PRO A 1 184 ? -43.34000 -9.47400  0.06400   1.000 42.11294  ? 184 PRO A CB  1 
ATOM   1412 C CG  . PRO A 1 184 ? -42.19700 -9.87600  -0.92400  1.000 46.48189  ? 184 PRO A CG  1 
ATOM   1413 C CD  . PRO A 1 184 ? -41.26800 -8.67000  -0.94200  1.000 42.69196  ? 184 PRO A CD  1 
ATOM   1414 N N   . PHE A 1 185 ? -41.03400 -9.23800  2.97300   1.000 44.91328  ? 185 PHE A N   1 
ATOM   1415 C CA  . PHE A 1 185 ? -40.24700 -10.09900 3.84600   1.000 42.07873  ? 185 PHE A CA  1 
ATOM   1416 C C   . PHE A 1 185 ? -40.54300 -9.72100  5.28600   1.000 42.31297  ? 185 PHE A C   1 
ATOM   1417 O O   . PHE A 1 185 ? -40.97200 -8.60300  5.57500   1.000 43.73156  ? 185 PHE A O   1 
ATOM   1418 C CB  . PHE A 1 185 ? -38.72400 -9.95700  3.54300   1.000 40.70488  ? 185 PHE A CB  1 
ATOM   1419 C CG  . PHE A 1 185 ? -38.40100 -10.16900 2.10400   1.000 40.89701  ? 185 PHE A CG  1 
ATOM   1420 C CD1 . PHE A 1 185 ? -38.57600 -11.43900 1.52000   1.000 44.78958  ? 185 PHE A CD1 1 
ATOM   1421 C CD2 . PHE A 1 185 ? -37.95000 -9.11800  1.29800   1.000 42.81040  ? 185 PHE A CD2 1 
ATOM   1422 C CE1 . PHE A 1 185 ? -38.28400 -11.64300 0.11500   1.000 45.87392  ? 185 PHE A CE1 1 
ATOM   1423 C CE2 . PHE A 1 185 ? -37.66600 -9.32400  -0.08200  1.000 43.19465  ? 185 PHE A CE2 1 
ATOM   1424 C CZ  . PHE A 1 185 ? -37.84300 -10.57100 -0.66600  1.000 46.18448  ? 185 PHE A CZ  1 
ATOM   1425 N N   . VAL A 1 186 ? -40.27200 -10.64500 6.20500   1.000 45.13173  ? 186 VAL A N   1 
ATOM   1426 C CA  . VAL A 1 186 ? -40.47100 -10.40600 7.62700   1.000 44.61851  ? 186 VAL A CA  1 
ATOM   1427 C C   . VAL A 1 186 ? -39.28600 -10.96800 8.38900   1.000 44.81590  ? 186 VAL A C   1 
ATOM   1428 O O   . VAL A 1 186 ? -38.61900 -11.88900 7.91800   1.000 46.17922  ? 186 VAL A O   1 
ATOM   1429 C CB  . VAL A 1 186 ? -41.75800 -11.05900 8.14200   1.000 45.71338  ? 186 VAL A CB  1 
ATOM   1430 C CG1 . VAL A 1 186 ? -42.95700 -10.29200 7.62600   1.000 48.31106  ? 186 VAL A CG1 1 
ATOM   1431 C CG2 . VAL A 1 186 ? -41.76500 -12.54000 7.70600   1.000 43.33677  ? 186 VAL A CG2 1 
ATOM   1432 N N   . ASP A 1 187 ? -39.02400 -10.40600 9.57600   1.000 44.37637  ? 187 ASP A N   1 
ATOM   1433 C CA  . ASP A 1 187 ? -37.81200 -10.75300 10.33400  1.000 47.34252  ? 187 ASP A CA  1 
ATOM   1434 C C   . ASP A 1 187 ? -38.13400 -11.95200 11.23200  1.000 48.41633  ? 187 ASP A C   1 
ATOM   1435 O O   . ASP A 1 187 ? -38.23200 -11.88000 12.47700  1.000 47.42148  ? 187 ASP A O   1 
ATOM   1436 C CB  . ASP A 1 187 ? -37.26600 -9.55900  11.12100  1.000 39.81004  ? 187 ASP A CB  1 
ATOM   1437 C CG  . ASP A 1 187 ? -38.33200 -8.89900  12.01400  1.000 48.21368  ? 187 ASP A CG  1 
ATOM   1438 O OD1 . ASP A 1 187 ? -39.52100 -9.21800  11.87300  1.000 47.30830  ? 187 ASP A OD1 1 
ATOM   1439 O OD2 . ASP A 1 187 ? -37.96800 -8.05100  12.84900  1.000 47.54781  ? 187 ASP A OD2 1 
ATOM   1440 N N   . ARG A 1 188 ? -38.30200 -13.08600 10.55100  1.000 47.20829  ? 188 ARG A N   1 
ATOM   1441 C CA  . ARG A 1 188 ? -38.48500 -14.38100 11.19800  1.000 53.66696  ? 188 ARG A CA  1 
ATOM   1442 C C   . ARG A 1 188 ? -37.84000 -15.43700 10.31800  1.000 50.24550  ? 188 ARG A C   1 
ATOM   1443 O O   . ARG A 1 188 ? -37.89400 -15.33500 9.09700   1.000 50.13233  ? 188 ARG A O   1 
ATOM   1444 C CB  . ARG A 1 188 ? -39.96700 -14.68700 11.42400  1.000 30.00000  ? 188 ARG A CB  1 
ATOM   1445 C CG  . ARG A 1 188 ? -40.63300 -13.79600 12.46000  1.000 30.00000  ? 188 ARG A CG  1 
ATOM   1446 C CD  . ARG A 1 188 ? -42.09300 -14.13000 12.72000  1.000 30.00000  ? 188 ARG A CD  1 
ATOM   1447 N NE  . ARG A 1 188 ? -42.70600 -13.20500 13.66900  1.000 30.00000  ? 188 ARG A NE  1 
ATOM   1448 C CZ  . ARG A 1 188 ? -43.99400 -13.20300 13.98000  1.000 30.00000  ? 188 ARG A CZ  1 
ATOM   1449 N NH1 . ARG A 1 188 ? -44.81600 -14.08200 13.42200  1.000 30.00000  ? 188 ARG A NH1 1 
ATOM   1450 N NH2 . ARG A 1 188 ? -44.46600 -12.32300 14.85500  1.000 30.00000  ? 188 ARG A NH2 1 
ATOM   1451 N N   . GLN A 1 189 ? -37.31300 -16.49400 10.94300  1.000 54.44863  ? 189 GLN A N   1 
ATOM   1452 C CA  . GLN A 1 189 ? -36.67700 -17.59700 10.21900  1.000 56.62784  ? 189 GLN A CA  1 
ATOM   1453 C C   . GLN A 1 189 ? -37.69900 -18.60500 9.71900   1.000 58.71230  ? 189 GLN A C   1 
ATOM   1454 O O   . GLN A 1 189 ? -37.65200 -19.79800 10.02800  1.000 60.40198  ? 189 GLN A O   1 
ATOM   1455 C CB  . GLN A 1 189 ? -35.63100 -18.26800 11.08900  1.000 55.62772  ? 189 GLN A CB  1 
ATOM   1456 C CG  . GLN A 1 189 ? -34.67400 -17.24000 11.52800  1.000 56.42782  ? 189 GLN A CG  1 
ATOM   1457 C CD  . GLN A 1 189 ? -33.39100 -17.80400 12.03800  1.000 59.91245  ? 189 GLN A CD  1 
ATOM   1458 O OE1 . GLN A 1 189 ? -32.33400 -17.23700 11.80000  1.000 59.41502  ? 189 GLN A OE1 1 
ATOM   1459 N NE2 . GLN A 1 189 ? -33.46900 -18.89300 12.79900  1.000 54.76709  ? 189 GLN A NE2 1 
ATOM   1460 N N   . THR A 1 190 ? -38.65400 -18.10200 8.97400   1.000 58.40437  ? 190 THR A N   1 
ATOM   1461 C CA  . THR A 1 190 ? -39.59700 -18.90600 8.23100   1.000 57.80693  ? 190 THR A CA  1 
ATOM   1462 C C   . THR A 1 190 ? -39.14200 -19.10000 6.79300   1.000 59.34659  ? 190 THR A C   1 
ATOM   1463 O O   . THR A 1 190 ? -38.20100 -18.45100 6.30000   1.000 55.32242  ? 190 THR A O   1 
ATOM   1464 C CB  . THR A 1 190 ? -40.94500 -18.21600 8.23900   1.000 61.29419  ? 190 THR A CB  1 
ATOM   1465 O OG1 . THR A 1 190 ? -40.75300 -16.85400 7.81300   1.000 55.38296  ? 190 THR A OG1 1 
ATOM   1466 C CG2 . THR A 1 190 ? -41.52000 -18.24600 9.62100   1.000 64.36561  ? 190 THR A CG2 1 
ATOM   1467 N N   . ALA A 1 191 ? -39.86200 -19.98100 6.10600   1.000 58.90180  ? 191 ALA A N   1 
ATOM   1468 C CA  . ALA A 1 191 ? -39.64500 -20.19600 4.68200   1.000 58.79126  ? 191 ALA A CA  1 
ATOM   1469 C C   . ALA A 1 191 ? -40.13300 -18.95600 3.93800   1.000 57.44899  ? 191 ALA A C   1 
ATOM   1470 O O   . ALA A 1 191 ? -41.32800 -18.62300 3.97000   1.000 58.12013  ? 191 ALA A O   1 
ATOM   1471 C CB  . ALA A 1 191 ? -40.36900 -21.45400 4.21300   1.000 63.14441  ? 191 ALA A CB  1 
ATOM   1472 N N   . GLN A 1 192 ? -39.20600 -18.24900 3.30600   1.000 54.79078  ? 192 GLN A N   1 
ATOM   1473 C CA  . GLN A 1 192 ? -39.48100 -17.03600 2.55100   1.000 52.38786  ? 192 GLN A CA  1 
ATOM   1474 C C   . GLN A 1 192 ? -38.60100 -17.08600 1.32200   1.000 55.68562  ? 192 GLN A C   1 
ATOM   1475 O O   . GLN A 1 192 ? -37.49800 -17.64300 1.37200   1.000 53.35377  ? 192 GLN A O   1 
ATOM   1476 C CB  . GLN A 1 192 ? -39.15600 -15.74200 3.32700   1.000 50.16391  ? 192 GLN A CB  1 
ATOM   1477 C CG  . GLN A 1 192 ? -39.85900 -15.63600 4.66800   1.000 50.63502  ? 192 GLN A CG  1 
ATOM   1478 C CD  . GLN A 1 192 ? -39.52500 -14.37100 5.36400   1.000 42.07347  ? 192 GLN A CD  1 
ATOM   1479 O OE1 . GLN A 1 192 ? -39.73500 -13.27500 4.80900   1.000 43.04463  ? 192 GLN A OE1 1 
ATOM   1480 N NE2 . GLN A 1 192 ? -39.05400 -14.47600 6.58400   1.000 44.19477  ? 192 GLN A NE2 1 
ATOM   1481 N N   . ALA A 1 193 ? -39.08500 -16.49300 0.23400   1.000 50.05863  ? 193 ALA A N   1 
ATOM   1482 C CA  . ALA A 1 193 ? -38.37100 -16.56400 -1.02900  1.000 53.71170  ? 193 ALA A CA  1 
ATOM   1483 C C   . ALA A 1 193 ? -38.48500 -15.22900 -1.73400  1.000 50.96927  ? 193 ALA A C   1 
ATOM   1484 O O   . ALA A 1 193 ? -39.55100 -14.58200 -1.72800  1.000 53.61432  ? 193 ALA A O   1 
ATOM   1485 C CB  . ALA A 1 193 ? -38.91300 -17.68300 -1.95600  1.000 53.37219  ? 193 ALA A CB  1 
ATOM   1486 N N   . ALA A 1 194 ? -37.35300 -14.83100 -2.32700  1.000 53.85646  ? 194 ALA A N   1 
ATOM   1487 C CA  . ALA A 1 194 ? -37.33800 -13.66700 -3.19200  1.000 46.77666  ? 194 ALA A CA  1 
ATOM   1488 C C   . ALA A 1 194 ? -38.25700 -13.91500 -4.37800  1.000 53.48799  ? 194 ALA A C   1 
ATOM   1489 O O   . ALA A 1 194 ? -38.23900 -14.99700 -4.96900  1.000 54.51706  ? 194 ALA A O   1 
ATOM   1490 C CB  . ALA A 1 194 ? -35.93200 -13.46400 -3.68500  1.000 52.64579  ? 194 ALA A CB  1 
ATOM   1491 N N   . GLY A 1 195 ? -39.06300 -12.92400 -4.73800  1.000 53.39851  ? 195 GLY A N   1 
ATOM   1492 C CA  . GLY A 1 195 ? -39.84000 -13.04500 -5.96400  1.000 51.27720  ? 195 GLY A CA  1 
ATOM   1493 C C   . GLY A 1 195 ? -38.90000 -13.09400 -7.16700  1.000 54.83289  ? 195 GLY A C   1 
ATOM   1494 O O   . GLY A 1 195 ? -37.69000 -12.86300 -7.06700  1.000 51.36932  ? 195 GLY A O   1 
ATOM   1495 N N   . THR A 1 196 ? -39.44800 -13.39700 -8.33800  1.000 56.44624  ? 196 THR A N   1 
ATOM   1496 C CA  . THR A 1 196 ? -38.58800 -13.43200 -9.52300  1.000 54.09596  ? 196 THR A CA  1 
ATOM   1497 C C   . THR A 1 196 ? -37.96400 -12.06200 -9.77500  1.000 48.65057  ? 196 THR A C   1 
ATOM   1498 O O   . THR A 1 196 ? -38.58700 -11.01100 -9.56300  1.000 45.13962  ? 196 THR A O   1 
ATOM   1499 C CB  . THR A 1 196 ? -39.37400 -13.88800 -10.74200 1.000 56.43308  ? 196 THR A CB  1 
ATOM   1500 O OG1 . THR A 1 196 ? -40.46200 -12.97600 -10.91600 1.000 59.28079  ? 196 THR A OG1 1 
ATOM   1501 C CG2 . THR A 1 196 ? -39.93600 -15.32000 -10.52200 1.000 50.35077  ? 196 THR A CG2 1 
ATOM   1502 N N   . ASP A 1 197 ? -36.70700 -12.07100 -10.15000 1.000 49.29012  ? 197 ASP A N   1 
ATOM   1503 C CA  . ASP A 1 197 ? -36.00700 -10.80700 -10.36100 1.000 45.98183  ? 197 ASP A CA  1 
ATOM   1504 C C   . ASP A 1 197 ? -35.95600 -10.48000 -11.85000 1.000 47.92154  ? 197 ASP A C   1 
ATOM   1505 O O   . ASP A 1 197 ? -36.31500 -11.30700 -12.69700 1.000 46.31345  ? 197 ASP A O   1 
ATOM   1506 C CB  . ASP A 1 197 ? -34.61500 -10.85300 -9.79400  1.000 42.12874  ? 197 ASP A CB  1 
ATOM   1507 C CG  . ASP A 1 197 ? -34.07000 -9.43800  -9.47200  1.000 45.10541  ? 197 ASP A CG  1 
ATOM   1508 O OD1 . ASP A 1 197 ? -34.85200 -8.45800  -9.21200  1.000 41.77606  ? 197 ASP A OD1 1 
ATOM   1509 O OD2 . ASP A 1 197 ? -32.83400 -9.29600  -9.49400  1.000 42.16821  ? 197 ASP A OD2 1 
ATOM   1510 N N   . THR A 1 198 ? -35.60300 -9.22900  -12.15300 1.000 43.46311  ? 198 THR A N   1 
ATOM   1511 C CA  . THR A 1 198 ? -35.49800 -8.77400  -13.52600 1.000 39.52842  ? 198 THR A CA  1 
ATOM   1512 C C   . THR A 1 198 ? -34.25800 -7.89700  -13.61100 1.000 38.85729  ? 198 THR A C   1 
ATOM   1513 O O   . THR A 1 198 ? -33.67800 -7.49600  -12.57900 1.000 37.22815  ? 198 THR A O   1 
ATOM   1514 C CB  . THR A 1 198 ? -36.76100 -8.01900  -13.93600 1.000 43.46574  ? 198 THR A CB  1 
ATOM   1515 O OG1 . THR A 1 198 ? -36.93000 -6.94600  -13.01200 1.000 48.74532  ? 198 THR A OG1 1 
ATOM   1516 C CG2 . THR A 1 198 ? -38.01200 -8.90700  -13.74800 1.000 47.92417  ? 198 THR A CG2 1 
ATOM   1517 N N   . THR A 1 199 ? -33.86300 -7.60000  -14.82900 1.000 37.42554  ? 199 THR A N   1 
ATOM   1518 C CA  . THR A 1 199 ? -32.64900 -6.75800  -15.02000 1.000 36.03327  ? 199 THR A CA  1 
ATOM   1519 C C   . THR A 1 199 ? -33.05200 -5.29200  -15.11900 1.000 36.58333  ? 199 THR A C   1 
ATOM   1520 O O   . THR A 1 199 ? -34.05200 -4.95100  -15.78700 1.000 37.78611  ? 199 THR A O   1 
ATOM   1521 C CB  . THR A 1 199 ? -31.87900 -7.23700  -16.25700 1.000 36.52543  ? 199 THR A CB  1 
ATOM   1522 O OG1 . THR A 1 199 ? -31.43600 -8.58900  -16.02600 1.000 39.19154  ? 199 THR A OG1 1 
ATOM   1523 C CG2 . THR A 1 199 ? -30.65100 -6.38000  -16.53900 1.000 35.63322  ? 199 THR A CG2 1 
ATOM   1524 N N   . ILE A 1 200 ? -32.29200 -4.42200  -14.45100 1.000 34.65679  ? 200 ILE A N   1 
ATOM   1525 C CA  . ILE A 1 200 ? -32.58400 -2.97900  -14.45600 1.000 32.27492  ? 200 ILE A CA  1 
ATOM   1526 C C   . ILE A 1 200 ? -32.09600 -2.35400  -15.76600 1.000 36.77020  ? 200 ILE A C   1 
ATOM   1527 O O   . ILE A 1 200 ? -30.93500 -1.90500  -15.87300 1.000 34.13830  ? 200 ILE A O   1 
ATOM   1528 C CB  . ILE A 1 200 ? -31.96100 -2.28600  -13.25600 1.000 33.48296  ? 200 ILE A CB  1 
ATOM   1529 C CG1 . ILE A 1 200 ? -32.35300 -3.06700  -11.96500 1.000 35.24633  ? 200 ILE A CG1 1 
ATOM   1530 C CG2 . ILE A 1 200 ? -32.45200 -0.80400  -13.18300 1.000 37.62293  ? 200 ILE A CG2 1 
ATOM   1531 C CD1 . ILE A 1 200 ? -31.25900 -3.00700  -10.89700 1.000 32.66971  ? 200 ILE A CD1 1 
ATOM   1532 N N   . THR A 1 201 ? -33.00800 -2.21900  -16.73100 1.000 34.85418  ? 201 THR A N   1 
ATOM   1533 C CA  . THR A 1 201 ? -32.69000 -1.73500  -18.08000 1.000 35.74113  ? 201 THR A CA  1 
ATOM   1534 C C   . THR A 1 201 ? -32.01600 -0.37300  -18.08800 1.000 33.70667  ? 201 THR A C   1 
ATOM   1535 O O   . THR A 1 201 ? -31.01600 -0.16400  -18.84300 1.000 35.29371  ? 201 THR A O   1 
ATOM   1536 C CB  . THR A 1 201 ? -33.99900 -1.67500  -18.85500 1.000 36.14118  ? 201 THR A CB  1 
ATOM   1537 O OG1 . THR A 1 201 ? -34.67500 -2.94500  -18.66900 1.000 35.66217  ? 201 THR A OG1 1 
ATOM   1538 C CG2 . THR A 1 201 ? -33.76000 -1.39300  -20.34000 1.000 39.27839  ? 201 THR A CG2 1 
ATOM   1539 N N   . VAL A 1 202 ? -32.57200 0.59600   -17.34000 1.000 33.22767  ? 202 VAL A N   1 
ATOM   1540 C CA  . VAL A 1 202 ? -32.00800 1.95000   -17.42100 1.000 36.07801  ? 202 VAL A CA  1 
ATOM   1541 C C   . VAL A 1 202 ? -30.54000 1.93700   -16.98100 1.000 34.44360  ? 202 VAL A C   1 
ATOM   1542 O O   . VAL A 1 202 ? -29.68500 2.71200   -17.51300 1.000 35.89904  ? 202 VAL A O   1 
ATOM   1543 C CB  . VAL A 1 202 ? -32.87500 2.96700   -16.63200 1.000 35.24633  ? 202 VAL A CB  1 
ATOM   1544 C CG1 . VAL A 1 202 ? -32.93100 2.70100   -15.12500 1.000 31.44588  ? 202 VAL A CG1 1 
ATOM   1545 C CG2 . VAL A 1 202 ? -32.36000 4.45300   -16.97200 1.000 34.40149  ? 202 VAL A CG2 1 
ATOM   1546 N N   . ASN A 1 203 ? -30.20700 1.05800   -16.01900 1.000 33.12766  ? 203 ASN A N   1 
ATOM   1547 C CA  . ASN A 1 203 ? -28.82400 0.94200   -15.56300 1.000 37.15709  ? 203 ASN A CA  1 
ATOM   1548 C C   . ASN A 1 203 ? -27.94400 0.27700   -16.59500 1.000 35.87272  ? 203 ASN A C   1 
ATOM   1549 O O   . ASN A 1 203 ? -26.78800 0.71000   -16.77400 1.000 34.63310  ? 203 ASN A O   1 
ATOM   1550 C CB  . ASN A 1 203 ? -28.77000 0.15600   -14.25700 1.000 32.46968  ? 203 ASN A CB  1 
ATOM   1551 C CG  . ASN A 1 203 ? -29.38500 0.93100   -13.06800 1.000 31.50378  ? 203 ASN A CG  1 
ATOM   1552 O OD1 . ASN A 1 203 ? -29.88100 2.05800   -13.23600 1.000 30.39575  ? 203 ASN A OD1 1 
ATOM   1553 N ND2 . ASN A 1 203 ? -29.31000 0.34000   -11.86900 1.000 31.58537  ? 203 ASN A ND2 1 
ATOM   1554 N N   . VAL A 1 204 ? -28.43500 -0.78200  -17.28000 1.000 35.84114  ? 204 VAL A N   1 
ATOM   1555 C CA  . VAL A 1 204 ? -27.61000 -1.34300  -18.37500 1.000 35.24107  ? 204 VAL A CA  1 
ATOM   1556 C C   . VAL A 1 204 ? -27.31900 -0.28800  -19.41400 1.000 37.95192  ? 204 VAL A C   1 
ATOM   1557 O O   . VAL A 1 204 ? -26.15400 -0.15300  -19.88400 1.000 34.11198  ? 204 VAL A O   1 
ATOM   1558 C CB  . VAL A 1 204 ? -28.27400 -2.57800  -19.02200 1.000 38.79149  ? 204 VAL A CB  1 
ATOM   1559 C CG1 . VAL A 1 204 ? -27.42500 -3.14300  -20.23900 1.000 35.18580  ? 204 VAL A CG1 1 
ATOM   1560 C CG2 . VAL A 1 204 ? -28.55800 -3.63600  -17.94600 1.000 32.30651  ? 204 VAL A CG2 1 
ATOM   1561 N N   . LEU A 1 205 ? -28.34000 0.47900   -19.81200 1.000 32.71445  ? 205 LEU A N   1 
ATOM   1562 C CA  . LEU A 1 205 ? -28.07600 1.58600   -20.74500 1.000 37.22025  ? 205 LEU A CA  1 
ATOM   1563 C C   . LEU A 1 205 ? -27.05500 2.60000   -20.19500 1.000 34.87523  ? 205 LEU A C   1 
ATOM   1564 O O   . LEU A 1 205 ? -26.11300 3.00200   -20.94400 1.000 37.53871  ? 205 LEU A O   1 
ATOM   1565 C CB  . LEU A 1 205 ? -29.37800 2.28300   -21.12200 1.000 34.42781  ? 205 LEU A CB  1 
ATOM   1566 C CG  . LEU A 1 205 ? -30.35600 1.41800   -21.97700 1.000 36.02537  ? 205 LEU A CG  1 
ATOM   1567 C CD1 . LEU A 1 205 ? -31.67300 2.13600   -21.97900 1.000 34.13304  ? 205 LEU A CD1 1 
ATOM   1568 C CD2 . LEU A 1 205 ? -29.91600 1.21200   -23.46800 1.000 34.04619  ? 205 LEU A CD2 1 
ATOM   1569 N N   . ALA A 1 206 ? -27.17600 2.98800   -18.91500 1.000 33.51454  ? 206 ALA A N   1 
ATOM   1570 C CA  . ALA A 1 206 ? -26.20900 3.92400   -18.35200 1.000 35.13316  ? 206 ALA A CA  1 
ATOM   1571 C C   . ALA A 1 206 ? -24.80700 3.37400   -18.52900 1.000 32.79341  ? 206 ALA A C   1 
ATOM   1572 O O   . ALA A 1 206 ? -23.88100 4.11000   -18.89300 1.000 32.83815  ? 206 ALA A O   1 
ATOM   1573 C CB  . ALA A 1 206 ? -26.47700 4.16100   -16.86900 1.000 33.76194  ? 206 ALA A CB  1 
ATOM   1574 N N   . TRP A 1 207 ? -24.65000 2.08100   -18.25900 1.000 32.19070  ? 207 TRP A N   1 
ATOM   1575 C CA  . TRP A 1 207 ? -23.34600 1.41800   -18.29600 1.000 36.71493  ? 207 TRP A CA  1 
ATOM   1576 C C   . TRP A 1 207 ? -22.82300 1.26100   -19.71300 1.000 37.17551  ? 207 TRP A C   1 
ATOM   1577 O O   . TRP A 1 207 ? -21.59900 1.44900   -19.94300 1.000 35.70165  ? 207 TRP A O   1 
ATOM   1578 C CB  . TRP A 1 207 ? -23.45700 0.05200   -17.58100 1.000 34.53046  ? 207 TRP A CB  1 
ATOM   1579 C CG  . TRP A 1 207 ? -22.29000 -0.96500  -17.70300 1.000 36.70440  ? 207 TRP A CG  1 
ATOM   1580 C CD1 . TRP A 1 207 ? -21.14800 -1.04000  -16.91400 1.000 37.26499  ? 207 TRP A CD1 1 
ATOM   1581 C CD2 . TRP A 1 207 ? -22.22600 -2.06500  -18.59800 1.000 37.33342  ? 207 TRP A CD2 1 
ATOM   1582 N NE1 . TRP A 1 207 ? -20.40800 -2.13700  -17.28400 1.000 35.67533  ? 207 TRP A NE1 1 
ATOM   1583 C CE2 . TRP A 1 207 ? -21.01800 -2.75800  -18.33300 1.000 38.03088  ? 207 TRP A CE2 1 
ATOM   1584 C CE3 . TRP A 1 207 ? -23.07100 -2.53000  -19.62800 1.000 36.62281  ? 207 TRP A CE3 1 
ATOM   1585 C CZ2 . TRP A 1 207 ? -20.66200 -3.91900  -19.00800 1.000 37.20709  ? 207 TRP A CZ2 1 
ATOM   1586 C CZ3 . TRP A 1 207 ? -22.69400 -3.68000  -20.33200 1.000 41.89713  ? 207 TRP A CZ3 1 
ATOM   1587 C CH2 . TRP A 1 207 ? -21.49200 -4.34100  -20.02100 1.000 36.34383  ? 207 TRP A CH2 1 
ATOM   1588 N N   . LEU A 1 208 ? -23.70500 1.00400   -20.70700 1.000 35.62532  ? 208 LEU A N   1 
ATOM   1589 C CA  . LEU A 1 208 ? -23.22400 1.12200   -22.09200 1.000 34.58046  ? 208 LEU A CA  1 
ATOM   1590 C C   . LEU A 1 208 ? -22.70900 2.52000   -22.40500 1.000 37.90191  ? 208 LEU A C   1 
ATOM   1591 O O   . LEU A 1 208 ? -21.71100 2.67600   -23.16400 1.000 35.92536  ? 208 LEU A O   1 
ATOM   1592 C CB  . LEU A 1 208 ? -24.34600 0.76000   -23.08600 1.000 33.20135  ? 208 LEU A CB  1 
ATOM   1593 C CG  . LEU A 1 208 ? -24.82000 -0.71300  -22.97100 1.000 37.18867  ? 208 LEU A CG  1 
ATOM   1594 C CD1 . LEU A 1 208 ? -25.99900 -0.98100  -23.94300 1.000 37.22288  ? 208 LEU A CD1 1 
ATOM   1595 C CD2 . LEU A 1 208 ? -23.55700 -1.58800  -23.36500 1.000 39.47579  ? 208 LEU A CD2 1 
ATOM   1596 N N   . TYR A 1 209 ? -23.37200 3.55800   -21.87800 1.000 34.76206  ? 209 TYR A N   1 
ATOM   1597 C CA  . TYR A 1 209 ? -22.85600 4.91800   -22.06900 1.000 39.08627  ? 209 TYR A CA  1 
ATOM   1598 C C   . TYR A 1 209 ? -21.50500 5.10100   -21.40100 1.000 38.50462  ? 209 TYR A C   1 
ATOM   1599 O O   . TYR A 1 209 ? -20.56100 5.66400   -22.02000 1.000 37.71505  ? 209 TYR A O   1 
ATOM   1600 C CB  . TYR A 1 209 ? -23.83100 5.94900   -21.50900 1.000 34.90418  ? 209 TYR A CB  1 
ATOM   1601 C CG  . TYR A 1 209 ? -24.93300 6.27900   -22.44700 1.000 37.43080  ? 209 TYR A CG  1 
ATOM   1602 C CD1 . TYR A 1 209 ? -24.69600 7.04300   -23.57500 1.000 37.43344  ? 209 TYR A CD1 1 
ATOM   1603 C CD2 . TYR A 1 209 ? -26.25300 5.93100   -22.12000 1.000 33.17766  ? 209 TYR A CD2 1 
ATOM   1604 C CE1 . TYR A 1 209 ? -25.68400 7.35400   -24.49800 1.000 37.79137  ? 209 TYR A CE1 1 
ATOM   1605 C CE2 . TYR A 1 209 ? -27.25600 6.19200   -23.04100 1.000 36.32541  ? 209 TYR A CE2 1 
ATOM   1606 C CZ  . TYR A 1 209 ? -27.01900 6.92800   -24.15900 1.000 38.55199  ? 209 TYR A CZ  1 
ATOM   1607 O OH  . TYR A 1 209 ? -28.03600 7.23300   -25.03500 1.000 36.94654  ? 209 TYR A OH  1 
ATOM   1608 N N   . ALA A 1 210 ? -21.36700 4.61200   -20.15800 1.000 35.66217  ? 210 ALA A N   1 
ATOM   1609 C CA  . ALA A 1 210 ? -20.01700 4.59900   -19.54900 1.000 36.74388  ? 210 ALA A CA  1 
ATOM   1610 C C   . ALA A 1 210 ? -18.97800 3.93000   -20.44000 1.000 40.29694  ? 210 ALA A C   1 
ATOM   1611 O O   . ALA A 1 210 ? -17.83700 4.41600   -20.56100 1.000 38.61516  ? 210 ALA A O   1 
ATOM   1612 C CB  . ALA A 1 210 ? -20.00700 3.84400   -18.22200 1.000 34.48045  ? 210 ALA A CB  1 
ATOM   1613 N N   . ALA A 1 211 ? -19.34600 2.81200   -21.06700 1.000 37.91770  ? 211 ALA A N   1 
ATOM   1614 C CA  . ALA A 1 211 ? -18.42800 2.10800   -21.93800 1.000 40.03112  ? 211 ALA A CA  1 
ATOM   1615 C C   . ALA A 1 211 ? -18.03000 2.96400   -23.12000 1.000 43.55259  ? 211 ALA A C   1 
ATOM   1616 O O   . ALA A 1 211 ? -16.85000 3.01300   -23.46000 1.000 38.86782  ? 211 ALA A O   1 
ATOM   1617 C CB  . ALA A 1 211 ? -19.02900 0.78700   -22.43600 1.000 40.64171  ? 211 ALA A CB  1 
ATOM   1618 N N   . VAL A 1 212 ? -18.99100 3.65100   -23.75100 1.000 39.25997  ? 212 VAL A N   1 
ATOM   1619 C CA  . VAL A 1 212 ? -18.66600 4.56300   -24.84600 1.000 42.57089  ? 212 VAL A CA  1 
ATOM   1620 C C   . VAL A 1 212 ? -17.76200 5.68600   -24.37400 1.000 43.73156  ? 212 VAL A C   1 
ATOM   1621 O O   . VAL A 1 212 ? -16.77900 6.03900   -25.06500 1.000 41.94977  ? 212 VAL A O   1 
ATOM   1622 C CB  . VAL A 1 212 ? -19.93800 5.13400   -25.52000 1.000 40.02059  ? 212 VAL A CB  1 
ATOM   1623 C CG1 . VAL A 1 212 ? -19.53700 6.23900   -26.53600 1.000 41.76553  ? 212 VAL A CG1 1 
ATOM   1624 C CG2 . VAL A 1 212 ? -20.70400 4.00500   -26.28100 1.000 38.62305  ? 212 VAL A CG2 1 
ATOM   1625 N N   . ILE A 1 213 ? -18.07000 6.27700   -23.21700 1.000 41.07335  ? 213 ILE A N   1 
ATOM   1626 C CA  . ILE A 1 213 ? -17.24700 7.37100   -22.69200 1.000 42.22612  ? 213 ILE A CA  1 
ATOM   1627 C C   . ILE A 1 213 ? -15.83800 6.89000   -22.46300 1.000 44.24741  ? 213 ILE A C   1 
ATOM   1628 O O   . ILE A 1 213 ? -14.86400 7.65500   -22.65600 1.000 38.93362  ? 213 ILE A O   1 
ATOM   1629 C CB  . ILE A 1 213 ? -17.86500 7.92700   -21.40600 1.000 43.98159  ? 213 ILE A CB  1 
ATOM   1630 C CG1 . ILE A 1 213 ? -19.17300 8.66100   -21.74600 1.000 42.52615  ? 213 ILE A CG1 1 
ATOM   1631 C CG2 . ILE A 1 213 ? -16.88200 8.77800   -20.64300 1.000 45.06856  ? 213 ILE A CG2 1 
ATOM   1632 C CD1 . ILE A 1 213 ? -20.11200 8.99500   -20.49700 1.000 39.57317  ? 213 ILE A CD1 1 
ATOM   1633 N N   . ASN A 1 214 ? -15.69500 5.60300   -22.13000 1.000 39.28892  ? 214 ASN A N   1 
ATOM   1634 C CA  . ASN A 1 214 ? -14.36800 5.05300   -21.93800 1.000 47.34252  ? 214 ASN A CA  1 
ATOM   1635 C C   . ASN A 1 214 ? -13.72400 4.45100   -23.17900 1.000 45.08172  ? 214 ASN A C   1 
ATOM   1636 O O   . ASN A 1 214 ? -12.67600 3.83500   -23.02600 1.000 44.61061  ? 214 ASN A O   1 
ATOM   1637 C CB  . ASN A 1 214 ? -14.41100 3.98900   -20.85200 1.000 37.80453  ? 214 ASN A CB  1 
ATOM   1638 C CG  . ASN A 1 214 ? -14.23300 4.60700   -19.47600 1.000 47.21882  ? 214 ASN A CG  1 
ATOM   1639 O OD1 . ASN A 1 214 ? -13.10700 4.67600   -18.98700 1.000 49.93757  ? 214 ASN A OD1 1 
ATOM   1640 N ND2 . ASN A 1 214 ? -15.34600 5.12400   -18.85700 1.000 49.69017  ? 214 ASN A ND2 1 
ATOM   1641 N N   . GLY A 1 215 ? -14.32400 4.54900   -24.37100 1.000 44.00528  ? 215 GLY A N   1 
ATOM   1642 C CA  . GLY A 1 215 ? -13.73000 4.01700   -25.60100 1.000 49.14273  ? 215 GLY A CA  1 
ATOM   1643 C C   . GLY A 1 215 ? -14.22400 2.66400   -26.14500 1.000 51.21930  ? 215 GLY A C   1 
ATOM   1644 O O   . GLY A 1 215 ? -13.72300 2.21700   -27.19000 1.000 50.41920  ? 215 GLY A O   1 
ATOM   1645 N N   . ASP A 1 216 ? -15.12300 1.94500   -25.46800 1.000 44.11318  ? 216 ASP A N   1 
ATOM   1646 C CA  . ASP A 1 216 ? -15.67100 0.71000   -26.05100 1.000 45.89761  ? 216 ASP A CA  1 
ATOM   1647 C C   . ASP A 1 216 ? -16.79500 1.11700   -27.00900 1.000 50.68502  ? 216 ASP A C   1 
ATOM   1648 O O   . ASP A 1 216 ? -17.85100 1.55800   -26.54200 1.000 48.12156  ? 216 ASP A O   1 
ATOM   1649 C CB  . ASP A 1 216 ? -16.27500 -0.21800  -24.98700 1.000 49.50330  ? 216 ASP A CB  1 
ATOM   1650 C CG  . ASP A 1 216 ? -15.23200 -1.04900  -24.19600 1.000 56.36992  ? 216 ASP A CG  1 
ATOM   1651 O OD1 . ASP A 1 216 ? -14.25900 -1.51000  -24.82400 1.000 72.11128  ? 216 ASP A OD1 1 
ATOM   1652 O OD2 . ASP A 1 216 ? -15.40600 -1.20600  -22.93000 1.000 45.11594  ? 216 ASP A OD2 1 
ATOM   1653 N N   . ARG A 1 217 ? -16.63500 0.91100   -28.33200 1.000 47.38463  ? 217 ARG A N   1 
ATOM   1654 C CA  . ARG A 1 217 ? -17.67000 1.33400   -29.28000 1.000 47.05301  ? 217 ARG A CA  1 
ATOM   1655 C C   . ARG A 1 217 ? -18.14200 0.22200   -30.18700 1.000 44.17109  ? 217 ARG A C   1 
ATOM   1656 O O   . ARG A 1 217 ? -18.98600 0.46500   -31.07100 1.000 42.09189  ? 217 ARG A O   1 
ATOM   1657 C CB  . ARG A 1 217 ? -17.13000 2.46800   -30.13800 1.000 52.20100  ? 217 ARG A CB  1 
ATOM   1658 C CG  . ARG A 1 217 ? -16.88800 3.70900   -29.37900 1.000 52.91687  ? 217 ARG A CG  1 
ATOM   1659 C CD  . ARG A 1 217 ? -16.39900 4.79400   -30.37200 1.000 60.26775  ? 217 ARG A CD  1 
ATOM   1660 N NE  . ARG A 1 217 ? -17.45600 5.24100   -31.25800 1.000 53.76960  ? 217 ARG A NE  1 
ATOM   1661 C CZ  . ARG A 1 217 ? -18.27600 6.22600   -30.95300 1.000 53.65117  ? 217 ARG A CZ  1 
ATOM   1662 N NH1 . ARG A 1 217 ? -18.14800 6.88900   -29.81100 1.000 50.56659  ? 217 ARG A NH1 1 
ATOM   1663 N NH2 . ARG A 1 217 ? -19.25000 6.54600   -31.80200 1.000 49.30854  ? 217 ARG A NH2 1 
ATOM   1664 N N   . TRP A 1 218 ? -17.63700 -0.99900  -29.98100 1.000 41.61025  ? 218 TRP A N   1 
ATOM   1665 C CA  . TRP A 1 218 ? -17.86300 -2.06700  -30.93600 1.000 46.03183  ? 218 TRP A CA  1 
ATOM   1666 C C   . TRP A 1 218 ? -19.30900 -2.45800  -31.03700 1.000 48.09524  ? 218 TRP A C   1 
ATOM   1667 O O   . TRP A 1 218 ? -19.71300 -3.04900  -32.04500 1.000 44.85538  ? 218 TRP A O   1 
ATOM   1668 C CB  . TRP A 1 218 ? -17.06300 -3.29700  -30.54100 1.000 50.10601  ? 218 TRP A CB  1 
ATOM   1669 C CG  . TRP A 1 218 ? -17.38200 -3.94600  -29.18200 1.000 45.89234  ? 218 TRP A CG  1 
ATOM   1670 C CD1 . TRP A 1 218 ? -16.71200 -3.73900  -28.01200 1.000 47.71362  ? 218 TRP A CD1 1 
ATOM   1671 C CD2 . TRP A 1 218 ? -18.44200 -4.91500  -28.86200 1.000 49.73228  ? 218 TRP A CD2 1 
ATOM   1672 N NE1 . TRP A 1 218 ? -17.25200 -4.53800  -27.01100 1.000 48.83480  ? 218 TRP A NE1 1 
ATOM   1673 C CE2 . TRP A 1 218 ? -18.30100 -5.25600  -27.51200 1.000 48.13998  ? 218 TRP A CE2 1 
ATOM   1674 C CE3 . TRP A 1 218 ? -19.45900 -5.54100  -29.61000 1.000 45.72127  ? 218 TRP A CE3 1 
ATOM   1675 C CZ2 . TRP A 1 218 ? -19.14400 -6.19000  -26.88100 1.000 48.22420  ? 218 TRP A CZ2 1 
ATOM   1676 C CZ3 . TRP A 1 218 ? -20.26000 -6.45600  -29.01500 1.000 50.46921  ? 218 TRP A CZ3 1 
ATOM   1677 C CH2 . TRP A 1 218 ? -20.13300 -6.75400  -27.64200 1.000 50.03758  ? 218 TRP A CH2 1 
ATOM   1678 N N   . PHE A 1 219 ? -20.09100 -2.22600  -29.95800 1.000 41.51550  ? 219 PHE A N   1 
ATOM   1679 C CA  . PHE A 1 219 ? -21.48500 -2.61800  -29.93200 1.000 43.46047  ? 219 PHE A CA  1 
ATOM   1680 C C   . PHE A 1 219 ? -22.43300 -1.57000  -30.52600 1.000 45.79496  ? 219 PHE A C   1 
ATOM   1681 O O   . PHE A 1 219 ? -23.64800 -1.80700  -30.55000 1.000 42.84461  ? 219 PHE A O   1 
ATOM   1682 C CB  . PHE A 1 219 ? -21.89600 -2.91800  -28.46600 1.000 43.04727  ? 219 PHE A CB  1 
ATOM   1683 C CG  . PHE A 1 219 ? -21.51400 -1.81400  -27.50900 1.000 40.13376  ? 219 PHE A CG  1 
ATOM   1684 C CD1 . PHE A 1 219 ? -22.29600 -0.68900  -27.38400 1.000 40.67067  ? 219 PHE A CD1 1 
ATOM   1685 C CD2 . PHE A 1 219 ? -20.39700 -1.92300  -26.72800 1.000 37.75979  ? 219 PHE A CD2 1 
ATOM   1686 C CE1 . PHE A 1 219 ? -21.95700 0.32900   -26.47600 1.000 40.54170  ? 219 PHE A CE1 1 
ATOM   1687 C CE2 . PHE A 1 219 ? -20.01700 -0.92500  -25.84700 1.000 38.31775  ? 219 PHE A CE2 1 
ATOM   1688 C CZ  . PHE A 1 219 ? -20.76800 0.22100   -25.72700 1.000 41.83133  ? 219 PHE A CZ  1 
ATOM   1689 N N   . LEU A 1 220 ? -21.94200 -0.40800  -30.94700 1.000 40.44169  ? 220 LEU A N   1 
ATOM   1690 C CA  . LEU A 1 220 ? -22.82600 0.57700   -31.55600 1.000 45.33175  ? 220 LEU A CA  1 
ATOM   1691 C C   . LEU A 1 220 ? -23.21300 0.13600   -32.95700 1.000 47.08722  ? 220 LEU A C   1 
ATOM   1692 O O   . LEU A 1 220 ? -22.56000 -0.71900  -33.57100 1.000 46.86878  ? 220 LEU A O   1 
ATOM   1693 C CB  . LEU A 1 220 ? -22.18300 1.96300   -31.57200 1.000 43.48153  ? 220 LEU A CB  1 
ATOM   1694 C CG  . LEU A 1 220 ? -21.86000 2.50200   -30.17600 1.000 42.95515  ? 220 LEU A CG  1 
ATOM   1695 C CD1 . LEU A 1 220 ? -21.06900 3.78700   -30.23400 1.000 41.22073  ? 220 LEU A CD1 1 
ATOM   1696 C CD2 . LEU A 1 220 ? -23.17600 2.76200   -29.37700 1.000 37.03865  ? 220 LEU A CD2 1 
ATOM   1697 N N   . ASN A 1 221 ? -24.34700 0.65700   -33.43400 1.000 45.15278  ? 221 ASN A N   1 
ATOM   1698 C CA  . ASN A 1 221 ? -24.80700 0.34000   -34.78300 1.000 46.57401  ? 221 ASN A CA  1 
ATOM   1699 C C   . ASN A 1 221 ? -25.53700 1.55600   -35.32300 1.000 50.10601  ? 221 ASN A C   1 
ATOM   1700 O O   . ASN A 1 221 ? -25.74200 2.54600   -34.61800 1.000 47.07933  ? 221 ASN A O   1 
ATOM   1701 C CB  . ASN A 1 221 ? -25.66100 -0.94900  -34.84400 1.000 47.95575  ? 221 ASN A CB  1 
ATOM   1702 C CG  . ASN A 1 221 ? -26.93800 -0.89000  -33.93500 1.000 53.61169  ? 221 ASN A CG  1 
ATOM   1703 O OD1 . ASN A 1 221 ? -27.57900 0.14000   -33.82300 1.000 54.00648  ? 221 ASN A OD1 1 
ATOM   1704 N ND2 . ASN A 1 221 ? -27.24100 -1.97800  -33.25800 1.000 51.45354  ? 221 ASN A ND2 1 
ATOM   1705 N N   . ARG A 1 222 ? -25.90200 1.50800   -36.60700 1.000 50.24813  ? 222 ARG A N   1 
ATOM   1706 C CA  . ARG A 1 222 ? -26.53800 2.69100   -37.24700 1.000 55.26189  ? 222 ARG A CA  1 
ATOM   1707 C C   . ARG A 1 222 ? -28.05500 2.64100   -37.05400 1.000 53.67222  ? 222 ARG A C   1 
ATOM   1708 O O   . ARG A 1 222 ? -28.73400 3.58400   -37.50000 1.000 56.21200  ? 222 ARG A O   1 
ATOM   1709 C CB  . ARG A 1 222 ? -26.19900 2.71600   -38.74000 1.000 30.00000  ? 222 ARG A CB  1 
ATOM   1710 C CG  . ARG A 1 222 ? -26.05400 1.33300   -39.36000 1.000 30.00000  ? 222 ARG A CG  1 
ATOM   1711 C CD  . ARG A 1 222 ? -27.32500 0.85500   -40.03400 1.000 30.00000  ? 222 ARG A CD  1 
ATOM   1712 N NE  . ARG A 1 222 ? -28.17500 1.96000   -40.45200 1.000 30.00000  ? 222 ARG A NE  1 
ATOM   1713 C CZ  . ARG A 1 222 ? -29.50000 1.90900   -40.50500 1.000 30.00000  ? 222 ARG A CZ  1 
ATOM   1714 N NH1 . ARG A 1 222 ? -30.09700 1.11600   -41.37900 1.000 30.00000  ? 222 ARG A NH1 1 
ATOM   1715 N NH2 . ARG A 1 222 ? -30.22400 2.64600   -39.68300 1.000 30.00000  ? 222 ARG A NH2 1 
ATOM   1716 N N   . PHE A 1 223 ? -28.56200 1.58400   -36.41900 1.000 52.13257  ? 223 PHE A N   1 
ATOM   1717 C CA  . PHE A 1 223 ? -30.01200 1.42900   -36.26500 1.000 55.53034  ? 223 PHE A CA  1 
ATOM   1718 C C   . PHE A 1 223 ? -30.56600 2.22500   -35.09600 1.000 52.11414  ? 223 PHE A C   1 
ATOM   1719 O O   . PHE A 1 223 ? -29.89000 2.48800   -34.08900 1.000 45.98972  ? 223 PHE A O   1 
ATOM   1720 C CB  . PHE A 1 223 ? -30.38100 -0.04000  -36.05300 1.000 52.97477  ? 223 PHE A CB  1 
ATOM   1721 C CG  . PHE A 1 223 ? -29.97700 -0.92500  -37.21300 1.000 63.88134  ? 223 PHE A CG  1 
ATOM   1722 C CD1 . PHE A 1 223 ? -30.59000 -0.78000  -38.45100 1.000 62.73910  ? 223 PHE A CD1 1 
ATOM   1723 C CD2 . PHE A 1 223 ? -28.98500 -1.89300  -37.06700 1.000 64.56037  ? 223 PHE A CD2 1 
ATOM   1724 C CE1 . PHE A 1 223 ? -30.22400 -1.58700  -39.53400 1.000 70.82428  ? 223 PHE A CE1 1 
ATOM   1725 C CE2 . PHE A 1 223 ? -28.63000 -2.70600  -38.13800 1.000 66.68694  ? 223 PHE A CE2 1 
ATOM   1726 C CZ  . PHE A 1 223 ? -29.23700 -2.54600  -39.36500 1.000 70.09788  ? 223 PHE A CZ  1 
ATOM   1727 N N   . THR A 1 224 ? -31.86600 2.51300   -35.18300 1.000 48.21894  ? 224 THR A N   1 
ATOM   1728 C CA  . THR A 1 224 ? -32.57800 3.03800   -34.03500 1.000 52.92213  ? 224 THR A CA  1 
ATOM   1729 C C   . THR A 1 224 ? -33.84500 2.19600   -33.88100 1.000 51.22193  ? 224 THR A C   1 
ATOM   1730 O O   . THR A 1 224 ? -34.22000 1.43500   -34.76500 1.000 57.01473  ? 224 THR A O   1 
ATOM   1731 C CB  . THR A 1 224 ? -32.91000 4.54900   -34.17700 1.000 53.02215  ? 224 THR A CB  1 
ATOM   1732 O OG1 . THR A 1 224 ? -33.36300 5.05000   -32.90600 1.000 56.97525  ? 224 THR A OG1 1 
ATOM   1733 C CG2 . THR A 1 224 ? -34.04100 4.74000   -35.17700 1.000 56.17252  ? 224 THR A CG2 1 
ATOM   1734 N N   . THR A 1 225 ? -34.48400 2.31600   -32.74400 1.000 52.28785  ? 225 THR A N   1 
ATOM   1735 C CA  . THR A 1 225 ? -35.68500 1.52800   -32.46300 1.000 47.30041  ? 225 THR A CA  1 
ATOM   1736 C C   . THR A 1 225 ? -36.74400 2.46600   -31.90500 1.000 48.80322  ? 225 THR A C   1 
ATOM   1737 O O   . THR A 1 225 ? -36.43800 3.58800   -31.49300 1.000 47.65045  ? 225 THR A O   1 
ATOM   1738 C CB  . THR A 1 225 ? -35.34000 0.36600   -31.50100 1.000 46.11079  ? 225 THR A CB  1 
ATOM   1739 O OG1 . THR A 1 225 ? -36.49700 -0.46600  -31.17600 1.000 46.98721  ? 225 THR A OG1 1 
ATOM   1740 C CG2 . THR A 1 225 ? -34.80400 0.91600   -30.21300 1.000 44.72378  ? 225 THR A CG2 1 
ATOM   1741 N N   . THR A 1 226 ? -38.00100 2.01800   -31.91800 1.000 48.85323  ? 226 THR A N   1 
ATOM   1742 C CA  . THR A 1 226 ? -38.99600 2.73300   -31.10600 1.000 47.07670  ? 226 THR A CA  1 
ATOM   1743 C C   . THR A 1 226 ? -38.95600 2.24000   -29.65900 1.000 44.12108  ? 226 THR A C   1 
ATOM   1744 O O   . THR A 1 226 ? -38.49500 1.13600   -29.34600 1.000 43.53680  ? 226 THR A O   1 
ATOM   1745 C CB  . THR A 1 226 ? -40.41700 2.57200   -31.64600 1.000 47.62676  ? 226 THR A CB  1 
ATOM   1746 O OG1 . THR A 1 226 ? -40.78700 1.20100   -31.59800 1.000 49.61911  ? 226 THR A OG1 1 
ATOM   1747 C CG2 . THR A 1 226 ? -40.62900 3.10300   -33.07100 1.000 50.16128  ? 226 THR A CG2 1 
ATOM   1748 N N   . LEU A 1 227 ? -39.42300 3.09200   -28.74400 1.000 44.28952  ? 227 LEU A N   1 
ATOM   1749 C CA  . LEU A 1 227 ? -39.54000 2.67300   -27.36100 1.000 44.33953  ? 227 LEU A CA  1 
ATOM   1750 C C   . LEU A 1 227 ? -40.42800 1.42700   -27.25200 1.000 43.67103  ? 227 LEU A C   1 
ATOM   1751 O O   . LEU A 1 227 ? -40.08300 0.46100   -26.54300 1.000 38.78360  ? 227 LEU A O   1 
ATOM   1752 C CB  . LEU A 1 227 ? -40.06000 3.84800   -26.55800 1.000 40.83121  ? 227 LEU A CB  1 
ATOM   1753 C CG  . LEU A 1 227 ? -40.14800 3.69000   -25.06300 1.000 46.45820  ? 227 LEU A CG  1 
ATOM   1754 C CD1 . LEU A 1 227 ? -38.78700 3.32000   -24.53600 1.000 40.98386  ? 227 LEU A CD1 1 
ATOM   1755 C CD2 . LEU A 1 227 ? -40.74500 4.95100   -24.41700 1.000 45.07909  ? 227 LEU A CD2 1 
ATOM   1756 N N   . ASN A 1 228 ? -41.54300 1.40900   -27.99400 1.000 46.01604  ? 228 ASN A N   1 
ATOM   1757 C CA  . ASN A 1 228 ? -42.43700 0.25000   -27.96900 1.000 44.98960  ? 228 ASN A CA  1 
ATOM   1758 C C   . ASN A 1 228 ? -41.75100 -1.01300  -28.47700 1.000 44.73431  ? 228 ASN A C   1 
ATOM   1759 O O   . ASN A 1 228 ? -41.81200 -2.06200  -27.82100 1.000 43.67103  ? 228 ASN A O   1 
ATOM   1760 C CB  . ASN A 1 228 ? -43.69400 0.48800   -28.79100 1.000 48.40580  ? 228 ASN A CB  1 
ATOM   1761 C CG  . ASN A 1 228 ? -44.67000 1.38600   -28.09200 1.000 49.76649  ? 228 ASN A CG  1 
ATOM   1762 O OD1 . ASN A 1 228 ? -44.63700 1.48900   -26.89100 1.000 49.54805  ? 228 ASN A OD1 1 
ATOM   1763 N ND2 . ASN A 1 228 ? -45.59100 1.98300   -28.83900 1.000 55.99619  ? 228 ASN A ND2 1 
ATOM   1764 N N   . ASP A 1 229 ? -41.03200 -0.92200  -29.61000 1.000 47.14249  ? 229 ASP A N   1 
ATOM   1765 C CA  . ASP A 1 229 ? -40.34000 -2.10100  -30.12100 1.000 43.27624  ? 229 ASP A CA  1 
ATOM   1766 C C   . ASP A 1 229 ? -39.24000 -2.52600  -29.17200 1.000 42.59195  ? 229 ASP A C   1 
ATOM   1767 O O   . ASP A 1 229 ? -39.02600 -3.72400  -28.95500 1.000 43.34730  ? 229 ASP A O   1 
ATOM   1768 C CB  . ASP A 1 229 ? -39.80600 -1.85700  -31.52500 1.000 50.40341  ? 229 ASP A CB  1 
ATOM   1769 C CG  . ASP A 1 229 ? -40.93800 -1.76000  -32.56000 1.000 53.84856  ? 229 ASP A CG  1 
ATOM   1770 O OD1 . ASP A 1 229 ? -42.05900 -2.26100  -32.27500 1.000 56.61205  ? 229 ASP A OD1 1 
ATOM   1771 O OD2 . ASP A 1 229 ? -40.69700 -1.16600  -33.63600 1.000 54.63813  ? 229 ASP A OD2 1 
ATOM   1772 N N   . PHE A 1 230 ? -38.58300 -1.57000  -28.52700 1.000 41.59183  ? 230 PHE A N   1 
ATOM   1773 C CA  . PHE A 1 230 ? -37.56100 -1.96500  -27.56800 1.000 42.23138  ? 230 PHE A CA  1 
ATOM   1774 C C   . PHE A 1 230 ? -38.17800 -2.72100  -26.39800 1.000 43.27887  ? 230 PHE A C   1 
ATOM   1775 O O   . PHE A 1 230 ? -37.64800 -3.74400  -25.95900 1.000 42.64195  ? 230 PHE A O   1 
ATOM   1776 C CB  . PHE A 1 230 ? -36.77600 -0.76700  -27.06100 1.000 38.15984  ? 230 PHE A CB  1 
ATOM   1777 C CG  . PHE A 1 230 ? -35.83400 -1.14300  -25.95800 1.000 39.77582  ? 230 PHE A CG  1 
ATOM   1778 C CD1 . PHE A 1 230 ? -34.60000 -1.75500  -26.26900 1.000 40.55223  ? 230 PHE A CD1 1 
ATOM   1779 C CD2 . PHE A 1 230 ? -36.21500 -1.01000  -24.63500 1.000 40.35484  ? 230 PHE A CD2 1 
ATOM   1780 C CE1 . PHE A 1 230 ? -33.76100 -2.15800  -25.25500 1.000 39.99690  ? 230 PHE A CE1 1 
ATOM   1781 C CE2 . PHE A 1 230 ? -35.36500 -1.44600  -23.61300 1.000 45.37649  ? 230 PHE A CE2 1 
ATOM   1782 C CZ  . PHE A 1 230 ? -34.10900 -1.99400  -23.95400 1.000 41.06545  ? 230 PHE A CZ  1 
ATOM   1783 N N   . ASN A 1 231 ? -39.31000 -2.24500  -25.88300 1.000 38.50198  ? 231 ASN A N   1 
ATOM   1784 C CA  . ASN A 1 231 ? -39.89900 -2.90100  -24.72600 1.000 41.92871  ? 231 ASN A CA  1 
ATOM   1785 C C   . ASN A 1 231 ? -40.40400 -4.32100  -25.02900 1.000 40.99965  ? 231 ASN A C   1 
ATOM   1786 O O   . ASN A 1 231 ? -40.41700 -5.16100  -24.11800 1.000 43.64471  ? 231 ASN A O   1 
ATOM   1787 C CB  . ASN A 1 231 ? -40.97200 -1.97000  -24.17200 1.000 37.06234  ? 231 ASN A CB  1 
ATOM   1788 C CG  . ASN A 1 231 ? -40.33300 -0.90900  -23.28600 1.000 40.98123  ? 231 ASN A CG  1 
ATOM   1789 O OD1 . ASN A 1 231 ? -39.29600 -1.17700  -22.68000 1.000 44.11582  ? 231 ASN A OD1 1 
ATOM   1790 N ND2 . ASN A 1 231 ? -40.89800 0.27800   -23.22400 1.000 41.50234  ? 231 ASN A ND2 1 
ATOM   1791 N N   . LEU A 1 232 ? -40.80700 -4.61500  -26.27700 1.000 41.61025  ? 232 LEU A N   1 
ATOM   1792 C CA  . LEU A 1 232 ? -41.12600 -6.00600  -26.64400 1.000 43.44205  ? 232 LEU A CA  1 
ATOM   1793 C C   . LEU A 1 232 ? -39.93600 -6.92400  -26.44700 1.000 46.31345  ? 232 LEU A C   1 
ATOM   1794 O O   . LEU A 1 232 ? -40.10300 -8.07300  -26.00500 1.000 47.00300  ? 232 LEU A O   1 
ATOM   1795 C CB  . LEU A 1 232 ? -41.58800 -6.14100  -28.08600 1.000 43.62365  ? 232 LEU A CB  1 
ATOM   1796 C CG  . LEU A 1 232 ? -43.04100 -5.89500  -28.50000 1.000 51.85359  ? 232 LEU A CG  1 
ATOM   1797 C CD1 . LEU A 1 232 ? -44.03800 -5.98500  -27.33000 1.000 51.04823  ? 232 LEU A CD1 1 
ATOM   1798 C CD2 . LEU A 1 232 ? -43.23900 -4.69700  -29.39600 1.000 52.34049  ? 232 LEU A CD2 1 
ATOM   1799 N N   . VAL A 1 233 ? -38.74400 -6.46500  -26.84700 1.000 41.76553  ? 233 VAL A N   1 
ATOM   1800 C CA  . VAL A 1 233 ? -37.52700 -7.25600  -26.64900 1.000 44.46323  ? 233 VAL A CA  1 
ATOM   1801 C C   . VAL A 1 233 ? -37.12600 -7.32000  -25.17500 1.000 42.67354  ? 233 VAL A C   1 
ATOM   1802 O O   . VAL A 1 233 ? -36.80000 -8.39400  -24.66100 1.000 43.04200  ? 233 VAL A O   1 
ATOM   1803 C CB  . VAL A 1 233 ? -36.40600 -6.67800  -27.52900 1.000 45.40281  ? 233 VAL A CB  1 
ATOM   1804 C CG1 . VAL A 1 233 ? -35.08800 -7.43500  -27.30300 1.000 52.06677  ? 233 VAL A CG1 1 
ATOM   1805 C CG2 . VAL A 1 233 ? -36.85100 -6.67600  -29.02300 1.000 46.38977  ? 233 VAL A CG2 1 
ATOM   1806 N N   . ALA A 1 234 ? -37.20100 -6.19200  -24.44000 1.000 45.04487  ? 234 ALA A N   1 
ATOM   1807 C CA  . ALA A 1 234 ? -36.99200 -6.24100  -22.99400 1.000 44.00001  ? 234 ALA A CA  1 
ATOM   1808 C C   . ALA A 1 234 ? -37.87500 -7.28700  -22.31600 1.000 41.40233  ? 234 ALA A C   1 
ATOM   1809 O O   . ALA A 1 234 ? -37.41700 -8.03100  -21.45100 1.000 40.96807  ? 234 ALA A O   1 
ATOM   1810 C CB  . ALA A 1 234 ? -37.30200 -4.89500  -22.34900 1.000 44.60798  ? 234 ALA A CB  1 
ATOM   1811 N N   . MET A 1 235 ? -39.15900 -7.32100  -22.65100 1.000 43.26835  ? 235 MET A N   1 
ATOM   1812 C CA  . MET A 1 235 ? -40.03100 -8.29800  -22.01600 1.000 47.58728  ? 235 MET A CA  1 
ATOM   1813 C C   . MET A 1 235 ? -39.54200 -9.71500  -22.28700 1.000 49.73491  ? 235 MET A C   1 
ATOM   1814 O O   . MET A 1 235 ? -39.43400 -10.51400 -21.36600 1.000 44.11318  ? 235 MET A O   1 
ATOM   1815 C CB  . MET A 1 235 ? -41.47100 -8.09700  -22.49000 1.000 48.90060  ? 235 MET A CB  1 
ATOM   1816 C CG  . MET A 1 235 ? -42.48300 -8.97800  -21.80800 1.000 58.75178  ? 235 MET A CG  1 
ATOM   1817 S SD  . MET A 1 235 ? -44.14700 -8.26000  -21.98100 1.000 78.02514  ? 235 MET A SD  1 
ATOM   1818 C CE  . MET A 1 235 ? -44.21400 -7.70700  -23.74300 1.000 52.60104  ? 235 MET A CE  1 
ATOM   1819 N N   . LYS A 1 236 ? -39.09600 -9.99700  -23.52300 1.000 49.47435  ? 236 LYS A N   1 
ATOM   1820 C CA  . LYS A 1 236 ? -38.63100 -11.33900 -23.84100 1.000 46.51874  ? 236 LYS A CA  1 
ATOM   1821 C C   . LYS A 1 236 ? -37.38000 -11.72700 -23.04800 1.000 45.10541  ? 236 LYS A C   1 
ATOM   1822 O O   . LYS A 1 236 ? -37.20800 -12.90500 -22.73400 1.000 44.36321  ? 236 LYS A O   1 
ATOM   1823 C CB  . LYS A 1 236 ? -38.45800 -11.45800 -25.34700 1.000 48.74532  ? 236 LYS A CB  1 
ATOM   1824 C CG  . LYS A 1 236 ? -37.64300 -12.63500 -25.84700 1.000 58.43595  ? 236 LYS A CG  1 
ATOM   1825 C CD  . LYS A 1 236 ? -37.70900 -12.73000 -27.37700 1.000 68.06079  ? 236 LYS A CD  1 
ATOM   1826 C CE  . LYS A 1 236 ? -36.68100 -13.73500 -27.93100 1.000 71.50331  ? 236 LYS A CE  1 
ATOM   1827 N NZ  . LYS A 1 236 ? -36.85300 -15.10000 -27.35900 1.000 72.34025  ? 236 LYS A NZ  1 
ATOM   1828 N N   . TYR A 1 237 ? -36.50700 -10.77900 -22.69700 1.000 45.42387  ? 237 TYR A N   1 
ATOM   1829 C CA  . TYR A 1 237 ? -35.26400 -11.09400 -21.97900 1.000 41.44181  ? 237 TYR A CA  1 
ATOM   1830 C C   . TYR A 1 237 ? -35.37500 -10.77300 -20.49500 1.000 41.63920  ? 237 TYR A C   1 
ATOM   1831 O O   . TYR A 1 237 ? -34.36000 -10.69900 -19.81600 1.000 37.00970  ? 237 TYR A O   1 
ATOM   1832 C CB  . TYR A 1 237 ? -34.04700 -10.36900 -22.61300 1.000 38.69938  ? 237 TYR A CB  1 
ATOM   1833 C CG  . TYR A 1 237 ? -33.76500 -10.97100 -23.95700 1.000 43.96580  ? 237 TYR A CG  1 
ATOM   1834 C CD1 . TYR A 1 237 ? -32.91300 -12.06800 -24.07600 1.000 46.99511  ? 237 TYR A CD1 1 
ATOM   1835 C CD2 . TYR A 1 237 ? -34.40200 -10.50200 -25.10200 1.000 46.22396  ? 237 TYR A CD2 1 
ATOM   1836 C CE1 . TYR A 1 237 ? -32.67900 -12.66200 -25.30400 1.000 50.38762  ? 237 TYR A CE1 1 
ATOM   1837 C CE2 . TYR A 1 237 ? -34.16800 -11.08500 -26.32900 1.000 51.70620  ? 237 TYR A CE2 1 
ATOM   1838 C CZ  . TYR A 1 237 ? -33.30800 -12.16600 -26.41600 1.000 50.17444  ? 237 TYR A CZ  1 
ATOM   1839 O OH  . TYR A 1 237 ? -33.11100 -12.74700 -27.62200 1.000 54.76183  ? 237 TYR A OH  1 
ATOM   1840 N N   . ASN A 1 238 ? -36.59800 -10.62000 -19.95300 1.000 41.23652  ? 238 ASN A N   1 
ATOM   1841 C CA  . ASN A 1 238 ? -36.75000 -10.38800 -18.52200 1.000 42.06557  ? 238 ASN A CA  1 
ATOM   1842 C C   . ASN A 1 238 ? -36.04900 -9.11100  -18.03000 1.000 40.76541  ? 238 ASN A C   1 
ATOM   1843 O O   . ASN A 1 238 ? -35.44000 -9.08400  -16.94000 1.000 40.01006  ? 238 ASN A O   1 
ATOM   1844 C CB  . ASN A 1 238 ? -36.23300 -11.57900 -17.72800 1.000 43.05516  ? 238 ASN A CB  1 
ATOM   1845 C CG  . ASN A 1 238 ? -36.66000 -11.47500 -16.31400 1.000 52.04835  ? 238 ASN A CG  1 
ATOM   1846 O OD1 . ASN A 1 238 ? -37.65900 -10.81000 -16.07000 1.000 53.31166  ? 238 ASN A OD1 1 
ATOM   1847 N ND2 . ASN A 1 238 ? -35.86400 -11.99900 -15.35800 1.000 55.30926  ? 238 ASN A ND2 1 
ATOM   1848 N N   . TYR A 1 239 ? -36.07400 -8.06900  -18.85800 1.000 40.45222  ? 239 TYR A N   1 
ATOM   1849 C CA  . TYR A 1 239 ? -35.58600 -6.73500  -18.51600 1.000 39.88110  ? 239 TYR A CA  1 
ATOM   1850 C C   . TYR A 1 239 ? -36.79500 -5.87300  -18.13600 1.000 40.18903  ? 239 TYR A C   1 
ATOM   1851 O O   . TYR A 1 239 ? -37.86600 -6.00500  -18.73700 1.000 39.47315  ? 239 TYR A O   1 
ATOM   1852 C CB  . TYR A 1 239 ? -34.91900 -6.09800  -19.72100 1.000 35.33318  ? 239 TYR A CB  1 
ATOM   1853 C CG  . TYR A 1 239 ? -33.42000 -6.35500  -19.86100 1.000 36.86495  ? 239 TYR A CG  1 
ATOM   1854 C CD1 . TYR A 1 239 ? -32.89300 -7.65300  -19.78300 1.000 37.83875  ? 239 TYR A CD1 1 
ATOM   1855 C CD2 . TYR A 1 239 ? -32.52800 -5.27400  -19.96800 1.000 35.74113  ? 239 TYR A CD2 1 
ATOM   1856 C CE1 . TYR A 1 239 ? -31.50700 -7.90100  -19.85500 1.000 39.35209  ? 239 TYR A CE1 1 
ATOM   1857 C CE2 . TYR A 1 239 ? -31.15700 -5.51700  -20.12500 1.000 37.78611  ? 239 TYR A CE2 1 
ATOM   1858 C CZ  . TYR A 1 239 ? -30.66800 -6.81900  -20.05800 1.000 38.63884  ? 239 TYR A CZ  1 
ATOM   1859 O OH  . TYR A 1 239 ? -29.31200 -7.03800  -20.14000 1.000 40.92859  ? 239 TYR A OH  1 
ATOM   1860 N N   . GLU A 1 240 ? -36.60700 -4.96900  -17.18800 1.000 35.44109  ? 240 GLU A N   1 
ATOM   1861 C CA  . GLU A 1 240 ? -37.67900 -4.02500  -16.83100 1.000 40.72857  ? 240 GLU A CA  1 
ATOM   1862 C C   . GLU A 1 240 ? -38.07200 -3.17800  -18.04600 1.000 40.67856  ? 240 GLU A C   1 
ATOM   1863 O O   . GLU A 1 240 ? -37.20800 -2.78600  -18.84700 1.000 38.03088  ? 240 GLU A O   1 
ATOM   1864 C CB  . GLU A 1 240 ? -37.24900 -3.05500  -15.72300 1.000 42.98673  ? 240 GLU A CB  1 
ATOM   1865 C CG  . GLU A 1 240 ? -36.99400 -3.67000  -14.38200 1.000 46.37661  ? 240 GLU A CG  1 
ATOM   1866 C CD  . GLU A 1 240 ? -38.29200 -3.73800  -13.54400 1.000 59.47555  ? 240 GLU A CD  1 
ATOM   1867 O OE1 . GLU A 1 240 ? -38.85300 -2.66800  -13.22800 1.000 64.96832  ? 240 GLU A OE1 1 
ATOM   1868 O OE2 . GLU A 1 240 ? -38.77800 -4.86400  -13.26900 1.000 66.17899  ? 240 GLU A OE2 1 
ATOM   1869 N N   . PRO A 1 241 ? -39.34800 -2.82000  -18.16400 1.000 40.29430  ? 241 PRO A N   1 
ATOM   1870 C CA  . PRO A 1 241 ? -39.76800 -1.89100  -19.22500 1.000 35.59637  ? 241 PRO A CA  1 
ATOM   1871 C C   . PRO A 1 241 ? -39.09000 -0.54700  -19.03800 1.000 34.56467  ? 241 PRO A C   1 
ATOM   1872 O O   . PRO A 1 241 ? -38.75800 -0.13900  -17.89800 1.000 36.74651  ? 241 PRO A O   1 
ATOM   1873 C CB  . PRO A 1 241 ? -41.29900 -1.76900  -19.01800 1.000 41.77343  ? 241 PRO A CB  1 
ATOM   1874 C CG  . PRO A 1 241 ? -41.65700 -3.01600  -18.33600 1.000 39.99953  ? 241 PRO A CG  1 
ATOM   1875 C CD  . PRO A 1 241 ? -40.50700 -3.33500  -17.41300 1.000 39.22312  ? 241 PRO A CD  1 
ATOM   1876 N N   . LEU A 1 242 ? -38.74700 0.05300   -20.18300 1.000 37.65188  ? 242 LEU A N   1 
ATOM   1877 C CA  . LEU A 1 242 ? -38.09600 1.35100   -20.22300 1.000 35.98063  ? 242 LEU A CA  1 
ATOM   1878 C C   . LEU A 1 242 ? -39.18800 2.39900   -20.40000 1.000 31.36692  ? 242 LEU A C   1 
ATOM   1879 O O   . LEU A 1 242 ? -39.97300 2.33900   -21.35300 1.000 32.83288  ? 242 LEU A O   1 
ATOM   1880 C CB  . LEU A 1 242 ? -37.08100 1.40500   -21.38700 1.000 34.64626  ? 242 LEU A CB  1 
ATOM   1881 C CG  . LEU A 1 242 ? -36.17000 2.61000   -21.26500 1.000 35.43056  ? 242 LEU A CG  1 
ATOM   1882 C CD1 . LEU A 1 242 ? -35.14500 2.35100   -20.11000 1.000 36.90442  ? 242 LEU A CD1 1 
ATOM   1883 C CD2 . LEU A 1 242 ? -35.44800 2.80200   -22.57900 1.000 38.72043  ? 242 LEU A CD2 1 
ATOM   1884 N N   . THR A 1 243 ? -39.20800 3.36400   -19.51600 1.000 33.71194  ? 243 THR A N   1 
ATOM   1885 C CA  . THR A 1 243 ? -40.20300 4.43000   -19.60800 1.000 36.78336  ? 243 THR A CA  1 
ATOM   1886 C C   . THR A 1 243 ? -39.62500 5.72700   -20.13000 1.000 37.84927  ? 243 THR A C   1 
ATOM   1887 O O   . THR A 1 243 ? -38.41500 5.89300   -20.20900 1.000 37.26763  ? 243 THR A O   1 
ATOM   1888 C CB  . THR A 1 243 ? -40.85900 4.69100   -18.26300 1.000 39.51263  ? 243 THR A CB  1 
ATOM   1889 O OG1 . THR A 1 243 ? -39.96000 5.34200   -17.36800 1.000 36.13328  ? 243 THR A OG1 1 
ATOM   1890 C CG2 . THR A 1 243 ? -41.38000 3.38200   -17.64000 1.000 39.58369  ? 243 THR A CG2 1 
ATOM   1891 N N   . GLN A 1 244 ? -40.50500 6.66300   -20.48800 1.000 37.54924  ? 244 GLN A N   1 
ATOM   1892 C CA  . GLN A 1 244 ? -40.01700 7.99200   -20.88500 1.000 41.38917  ? 244 GLN A CA  1 
ATOM   1893 C C   . GLN A 1 244 ? -39.24400 8.68000   -19.74500 1.000 40.95491  ? 244 GLN A C   1 
ATOM   1894 O O   . GLN A 1 244 ? -38.25100 9.41600   -20.00700 1.000 38.39934  ? 244 GLN A O   1 
ATOM   1895 C CB  . GLN A 1 244 ? -41.19000 8.85200   -21.35000 1.000 36.47279  ? 244 GLN A CB  1 
ATOM   1896 C CG  . GLN A 1 244 ? -40.76900 10.17700  -21.98100 1.000 37.75979  ? 244 GLN A CG  1 
ATOM   1897 C CD  . GLN A 1 244 ? -39.85800 9.97700   -23.17600 1.000 45.37123  ? 244 GLN A CD  1 
ATOM   1898 O OE1 . GLN A 1 244 ? -40.13400 9.15000   -24.09100 1.000 40.76541  ? 244 GLN A OE1 1 
ATOM   1899 N NE2 . GLN A 1 244 ? -38.75100 10.76100  -23.20600 1.000 40.73120  ? 244 GLN A NE2 1 
ATOM   1900 N N   . ASP A 1 245 ? -39.60100 8.39300   -18.49800 1.000 35.27265  ? 245 ASP A N   1 
ATOM   1901 C CA  . ASP A 1 245 ? -38.84300 8.92700   -17.36400 1.000 38.88361  ? 245 ASP A CA  1 
ATOM   1902 C C   . ASP A 1 245 ? -37.39800 8.43800   -17.41300 1.000 40.19429  ? 245 ASP A C   1 
ATOM   1903 O O   . ASP A 1 245 ? -36.47300 9.21200   -17.15500 1.000 38.68359  ? 245 ASP A O   1 
ATOM   1904 C CB  . ASP A 1 245 ? -39.49300 8.57100   -16.02300 1.000 40.93122  ? 245 ASP A CB  1 
ATOM   1905 C CG  . ASP A 1 245 ? -40.61800 9.53700   -15.64200 1.000 39.65475  ? 245 ASP A CG  1 
ATOM   1906 O OD1 . ASP A 1 245 ? -41.21100 10.13100  -16.55900 1.000 38.20195  ? 245 ASP A OD1 1 
ATOM   1907 O OD2 . ASP A 1 245 ? -40.97100 9.66300   -14.44600 1.000 43.20255  ? 245 ASP A OD2 1 
ATOM   1908 N N   . HIS A 1 246 ? -37.20000 7.13900   -17.68300 1.000 38.50988  ? 246 HIS A N   1 
ATOM   1909 C CA  . HIS A 1 246 ? -35.85600 6.58300   -17.86800 1.000 37.29921  ? 246 HIS A CA  1 
ATOM   1910 C C   . HIS A 1 246 ? -35.15200 7.20900   -19.06300 1.000 39.48368  ? 246 HIS A C   1 
ATOM   1911 O O   . HIS A 1 246 ? -33.97600 7.55700   -18.96600 1.000 36.76230  ? 246 HIS A O   1 
ATOM   1912 C CB  . HIS A 1 246 ? -35.91400 5.06800   -18.05800 1.000 35.11737  ? 246 HIS A CB  1 
ATOM   1913 C CG  . HIS A 1 246 ? -36.51000 4.29900   -16.91100 1.000 39.24155  ? 246 HIS A CG  1 
ATOM   1914 N ND1 . HIS A 1 246 ? -37.37800 3.25100   -17.12500 1.000 38.37039  ? 246 HIS A ND1 1 
ATOM   1915 C CD2 . HIS A 1 246 ? -36.33400 4.37600   -15.56200 1.000 38.13878  ? 246 HIS A CD2 1 
ATOM   1916 C CE1 . HIS A 1 246 ? -37.73500 2.72600   -15.95900 1.000 35.43320  ? 246 HIS A CE1 1 
ATOM   1917 N NE2 . HIS A 1 246 ? -37.09400 3.37600   -14.99800 1.000 37.56240  ? 246 HIS A NE2 1 
ATOM   1918 N N   . VAL A 1 247 ? -35.84400 7.33900   -20.21100 1.000 38.22827  ? 247 VAL A N   1 
ATOM   1919 C CA  . VAL A 1 247 ? -35.21400 7.99900   -21.36400 1.000 37.97561  ? 247 VAL A CA  1 
ATOM   1920 C C   . VAL A 1 247 ? -34.71800 9.39900   -20.97400 1.000 42.09189  ? 247 VAL A C   1 
ATOM   1921 O O   . VAL A 1 247 ? -33.53400 9.76100   -21.24300 1.000 38.45461  ? 247 VAL A O   1 
ATOM   1922 C CB  . VAL A 1 247 ? -36.22000 8.05700   -22.53900 1.000 39.20996  ? 247 VAL A CB  1 
ATOM   1923 C CG1 . VAL A 1 247 ? -35.72600 8.88400   -23.70600 1.000 38.29407  ? 247 VAL A CG1 1 
ATOM   1924 C CG2 . VAL A 1 247 ? -36.58100 6.64400   -23.00000 1.000 37.05707  ? 247 VAL A CG2 1 
ATOM   1925 N N   . ASP A 1 248 ? -35.55100 10.15800  -20.21500 1.000 37.95455  ? 248 ASP A N   1 
ATOM   1926 C CA  . ASP A 1 248 ? -35.17600 11.52500  -19.81900 1.000 42.38666  ? 248 ASP A CA  1 
ATOM   1927 C C   . ASP A 1 248 ? -33.98800 11.53800  -18.86800 1.000 42.54984  ? 248 ASP A C   1 
ATOM   1928 O O   . ASP A 1 248 ? -33.04900 12.35900  -19.04300 1.000 43.58154  ? 248 ASP A O   1 
ATOM   1929 C CB  . ASP A 1 248 ? -36.34900 12.27000  -19.15400 1.000 40.24167  ? 248 ASP A CB  1 
ATOM   1930 C CG  . ASP A 1 248 ? -37.47000 12.57800  -20.11200 1.000 42.87356  ? 248 ASP A CG  1 
ATOM   1931 O OD1 . ASP A 1 248 ? -37.26200 12.55800  -21.34200 1.000 45.93972  ? 248 ASP A OD1 1 
ATOM   1932 O OD2 . ASP A 1 248 ? -38.56700 12.89500  -19.62700 1.000 51.48775  ? 248 ASP A OD2 1 
ATOM   1933 N N   . ILE A 1 249 ? -33.93000 10.59300  -17.92100 1.000 39.56264  ? 249 ILE A N   1 
ATOM   1934 C CA  . ILE A 1 249 ? -32.78100 10.66500  -17.00200 1.000 41.66815  ? 249 ILE A CA  1 
ATOM   1935 C C   . ILE A 1 249 ? -31.47100 10.27200  -17.70300 1.000 38.57831  ? 249 ILE A C   1 
ATOM   1936 O O   . ILE A 1 249 ? -30.38100 10.64700  -17.22000 1.000 39.78372  ? 249 ILE A O   1 
ATOM   1937 C CB  . ILE A 1 249 ? -32.85600 9.87200   -15.68900 1.000 42.34192  ? 249 ILE A CB  1 
ATOM   1938 C CG1 . ILE A 1 249 ? -32.64900 8.39600   -15.89800 1.000 46.09763  ? 249 ILE A CG1 1 
ATOM   1939 C CG2 . ILE A 1 249 ? -34.18500 10.01700  -14.92500 1.000 43.24729  ? 249 ILE A CG2 1 
ATOM   1940 C CD1 . ILE A 1 249 ? -32.99100 7.62000   -14.61300 1.000 62.79174  ? 249 ILE A CD1 1 
ATOM   1941 N N   . LEU A 1 250 ? -31.53700 9.50800   -18.78900 1.000 35.44899  ? 250 LEU A N   1 
ATOM   1942 C CA  . LEU A 1 250 ? -30.34000 9.23600   -19.63000 1.000 35.82798  ? 250 LEU A CA  1 
ATOM   1943 C C   . LEU A 1 250 ? -29.95500 10.42600  -20.49200 1.000 40.56276  ? 250 LEU A C   1 
ATOM   1944 O O   . LEU A 1 250 ? -28.91300 10.37300  -21.18500 1.000 40.09165  ? 250 LEU A O   1 
ATOM   1945 C CB  . LEU A 1 250 ? -30.58300 8.01700   -20.51800 1.000 34.83312  ? 250 LEU A CB  1 
ATOM   1946 C CG  . LEU A 1 250 ? -30.67900 6.71700   -19.69100 1.000 36.66229  ? 250 LEU A CG  1 
ATOM   1947 C CD1 . LEU A 1 250 ? -31.25300 5.56500   -20.50700 1.000 35.58058  ? 250 LEU A CD1 1 
ATOM   1948 C CD2 . LEU A 1 250 ? -29.37900 6.34400   -19.03000 1.000 37.32026  ? 250 LEU A CD2 1 
ATOM   1949 N N   . GLY A 1 251 ? -30.68700 11.52900  -20.38300 1.000 37.99403  ? 251 GLY A N   1 
ATOM   1950 C CA  . GLY A 1 251 ? -30.47700 12.69200  -21.20900 1.000 40.77594  ? 251 GLY A CA  1 
ATOM   1951 C C   . GLY A 1 251 ? -29.00600 13.16000  -21.22200 1.000 40.04954  ? 251 GLY A C   1 
ATOM   1952 O O   . GLY A 1 251 ? -28.42200 13.36900  -22.26000 1.000 39.97585  ? 251 GLY A O   1 
ATOM   1953 N N   . PRO A 1 252 ? -28.44600 13.42800  -20.05000 1.000 41.14441  ? 252 PRO A N   1 
ATOM   1954 C CA  . PRO A 1 252 ? -27.07300 13.98200  -20.02400 1.000 40.88911  ? 252 PRO A CA  1 
ATOM   1955 C C   . PRO A 1 252 ? -26.04000 13.05000  -20.63200 1.000 40.55486  ? 252 PRO A C   1 
ATOM   1956 O O   . PRO A 1 252 ? -25.11200 13.52100  -21.33500 1.000 41.20757  ? 252 PRO A O   1 
ATOM   1957 C CB  . PRO A 1 252 ? -26.86700 14.26800  -18.53200 1.000 43.00779  ? 252 PRO A CB  1 
ATOM   1958 C CG  . PRO A 1 252 ? -28.29800 14.61500  -18.02800 1.000 46.39504  ? 252 PRO A CG  1 
ATOM   1959 C CD  . PRO A 1 252 ? -29.21500 13.72400  -18.82000 1.000 43.69208  ? 252 PRO A CD  1 
ATOM   1960 N N   . LEU A 1 253 ? -26.18000 11.73300  -20.43300 1.000 36.37541  ? 253 LEU A N   1 
ATOM   1961 C CA  . LEU A 1 253 ? -25.24200 10.77200  -21.00600 1.000 41.33127  ? 253 LEU A CA  1 
ATOM   1962 C C   . LEU A 1 253 ? -25.37700 10.69100  -22.51500 1.000 42.95515  ? 253 LEU A C   1 
ATOM   1963 O O   . LEU A 1 253 ? -24.36200 10.62200  -23.24100 1.000 39.94689  ? 253 LEU A O   1 
ATOM   1964 C CB  . LEU A 1 253 ? -25.41800 9.40000   -20.35500 1.000 37.07813  ? 253 LEU A CB  1 
ATOM   1965 C CG  . LEU A 1 253 ? -24.86500 9.32100   -18.91800 1.000 37.80980  ? 253 LEU A CG  1 
ATOM   1966 C CD1 . LEU A 1 253 ? -25.26400 7.99200   -18.37400 1.000 36.91758  ? 253 LEU A CD1 1 
ATOM   1967 C CD2 . LEU A 1 253 ? -23.32800 9.44200   -18.89400 1.000 40.33115  ? 253 LEU A CD2 1 
ATOM   1968 N N   . SER A 1 254 ? -26.61600 10.73200  -22.99600 1.000 36.92022  ? 254 SER A N   1 
ATOM   1969 C CA  . SER A 1 254 ? -26.90400 10.81100  -24.42300 1.000 38.19668  ? 254 SER A CA  1 
ATOM   1970 C C   . SER A 1 254 ? -26.31300 12.07800  -25.05500 1.000 42.06294  ? 254 SER A C   1 
ATOM   1971 O O   . SER A 1 254 ? -25.71500 12.01300  -26.13800 1.000 42.66038  ? 254 SER A O   1 
ATOM   1972 C CB  . SER A 1 254 ? -28.43900 10.81500  -24.62100 1.000 41.61025  ? 254 SER A CB  1 
ATOM   1973 O OG  . SER A 1 254 ? -28.65500 10.90200  -26.00600 1.000 43.51048  ? 254 SER A OG  1 
ATOM   1974 N N   . ALA A 1 255 ? -26.45500 13.23700  -24.39700 1.000 41.17599  ? 255 ALA A N   1 
ATOM   1975 C CA  . ALA A 1 255 ? -25.87200 14.48100  -24.95000 1.000 46.11079  ? 255 ALA A CA  1 
ATOM   1976 C C   . ALA A 1 255 ? -24.34300 14.45900  -24.96700 1.000 44.62114  ? 255 ALA A C   1 
ATOM   1977 O O   . ALA A 1 255 ? -23.69000 14.93000  -25.92500 1.000 46.60559  ? 255 ALA A O   1 
ATOM   1978 C CB  . ALA A 1 255 ? -26.36200 15.66600  -24.13000 1.000 46.20028  ? 255 ALA A CB  1 
ATOM   1979 N N   . GLN A 1 256 ? -23.72900 13.93900  -23.90600 1.000 46.28713  ? 256 GLN A N   1 
ATOM   1980 C CA  . GLN A 1 256 ? -22.29300 13.92600  -23.81800 1.000 46.84509  ? 256 GLN A CA  1 
ATOM   1981 C C   . GLN A 1 256 ? -21.68300 13.01900  -24.87400 1.000 48.10840  ? 256 GLN A C   1 
ATOM   1982 O O   . GLN A 1 256 ? -20.63100 13.34400  -25.46300 1.000 45.50019  ? 256 GLN A O   1 
ATOM   1983 C CB  . GLN A 1 256 ? -21.88800 13.51400  -22.41100 1.000 46.87141  ? 256 GLN A CB  1 
ATOM   1984 C CG  . GLN A 1 256 ? -20.41700 13.40000  -22.27200 1.000 48.44791  ? 256 GLN A CG  1 
ATOM   1985 C CD  . GLN A 1 256 ? -20.05400 12.82600  -20.96000 1.000 55.57508  ? 256 GLN A CD  1 
ATOM   1986 O OE1 . GLN A 1 256 ? -20.92800 12.59000  -20.11500 1.000 59.10182  ? 256 GLN A OE1 1 
ATOM   1987 N NE2 . GLN A 1 256 ? -18.78900 12.52700  -20.78000 1.000 57.68323  ? 256 GLN A NE2 1 
ATOM   1988 N N   . THR A 1 257 ? -22.33200 11.90400  -25.16300 1.000 43.05779  ? 257 THR A N   1 
ATOM   1989 C CA  . THR A 1 257 ? -21.78500 10.95700  -26.12500 1.000 43.55259  ? 257 THR A CA  1 
ATOM   1990 C C   . THR A 1 257 ? -22.30400 11.20300  -27.51000 1.000 45.82918  ? 257 THR A C   1 
ATOM   1991 O O   . THR A 1 257 ? -21.76500 10.62400  -28.45000 1.000 45.11330  ? 257 THR A O   1 
ATOM   1992 C CB  . THR A 1 257 ? -22.12600 9.49400   -25.72400 1.000 42.54721  ? 257 THR A CB  1 
ATOM   1993 O OG1 . THR A 1 257 ? -23.57900 9.30400   -25.66400 1.000 40.28115  ? 257 THR A OG1 1 
ATOM   1994 C CG2 . THR A 1 257 ? -21.49200 9.17500   -24.37600 1.000 41.64710  ? 257 THR A CG2 1 
ATOM   1995 N N   . GLY A 1 258 ? -23.36400 12.00000  -27.64200 1.000 43.54996  ? 258 GLY A N   1 
ATOM   1996 C CA  . GLY A 1 258 ? -23.99200 12.19400  -28.93100 1.000 43.69998  ? 258 GLY A CA  1 
ATOM   1997 C C   . GLY A 1 258 ? -24.74200 10.99000  -29.46800 1.000 47.40042  ? 258 GLY A C   1 
ATOM   1998 O O   . GLY A 1 258 ? -25.05700 10.95900  -30.64900 1.000 48.55319  ? 258 GLY A O   1 
ATOM   1999 N N   . ILE A 1 259 ? -25.04800 9.99300   -28.63200 1.000 45.65811  ? 259 ILE A N   1 
ATOM   2000 C CA  . ILE A 1 259 ? -25.76000 8.79900   -29.05400 1.000 41.05492  ? 259 ILE A CA  1 
ATOM   2001 C C   . ILE A 1 259 ? -27.16100 8.90400   -28.42000 1.000 41.57867  ? 259 ILE A C   1 
ATOM   2002 O O   . ILE A 1 259 ? -27.27900 9.05600   -27.20400 1.000 38.46251  ? 259 ILE A O   1 
ATOM   2003 C CB  . ILE A 1 259 ? -25.02400 7.52900   -28.61000 1.000 42.33139  ? 259 ILE A CB  1 
ATOM   2004 C CG1 . ILE A 1 259 ? -23.57300 7.46800   -29.15700 1.000 44.80537  ? 259 ILE A CG1 1 
ATOM   2005 C CG2 . ILE A 1 259 ? -25.82000 6.22000   -28.91000 1.000 41.62604  ? 259 ILE A CG2 1 
ATOM   2006 C CD1 . ILE A 1 259 ? -22.88400 6.42600   -28.38900 1.000 40.88911  ? 259 ILE A CD1 1 
ATOM   2007 N N   . ALA A 1 260 ? -28.18300 9.01300   -29.26100 1.000 42.81040  ? 260 ALA A N   1 
ATOM   2008 C CA  . ALA A 1 260 ? -29.56900 9.11500   -28.77900 1.000 37.39922  ? 260 ALA A CA  1 
ATOM   2009 C C   . ALA A 1 260 ? -29.94400 7.88100   -27.96500 1.000 38.86519  ? 260 ALA A C   1 
ATOM   2010 O O   . ALA A 1 260 ? -29.46800 6.77400   -28.23900 1.000 38.95204  ? 260 ALA A O   1 
ATOM   2011 C CB  . ALA A 1 260 ? -30.47600 9.28600   -30.00400 1.000 41.33654  ? 260 ALA A CB  1 
ATOM   2012 N N   . VAL A 1 261 ? -30.82100 8.06500   -26.94900 1.000 41.06808  ? 261 VAL A N   1 
ATOM   2013 C CA  . VAL A 1 261 ? -31.19800 6.94500   -26.07000 1.000 38.14405  ? 261 VAL A CA  1 
ATOM   2014 C C   . VAL A 1 261 ? -31.75700 5.78900   -26.89800 1.000 36.44911  ? 261 VAL A C   1 
ATOM   2015 O O   . VAL A 1 261 ? -31.31200 4.63900   -26.76300 1.000 35.19896  ? 261 VAL A O   1 
ATOM   2016 C CB  . VAL A 1 261 ? -32.20400 7.41100   -24.99000 1.000 42.01556  ? 261 VAL A CB  1 
ATOM   2017 C CG1 . VAL A 1 261 ? -32.75300 6.22700   -24.21500 1.000 37.99403  ? 261 VAL A CG1 1 
ATOM   2018 C CG2 . VAL A 1 261 ? -31.47100 8.41200   -23.99900 1.000 41.98661  ? 261 VAL A CG2 1 
ATOM   2019 N N   . LEU A 1 262 ? -32.64600 6.08700   -27.85200 1.000 35.18053  ? 262 LEU A N   1 
ATOM   2020 C CA  . LEU A 1 262 ? -33.20100 4.98600   -28.64700 1.000 41.50234  ? 262 LEU A CA  1 
ATOM   2021 C C   . LEU A 1 262 ? -32.17400 4.40500   -29.62600 1.000 43.00516  ? 262 LEU A C   1 
ATOM   2022 O O   . LEU A 1 262 ? -32.32100 3.25900   -30.06600 1.000 42.28402  ? 262 LEU A O   1 
ATOM   2023 C CB  . LEU A 1 262 ? -34.47900 5.44400   -29.39400 1.000 38.92835  ? 262 LEU A CB  1 
ATOM   2024 C CG  . LEU A 1 262 ? -35.61800 5.75100   -28.36700 1.000 41.66815  ? 262 LEU A CG  1 
ATOM   2025 C CD1 . LEU A 1 262 ? -36.78700 6.31900   -29.07300 1.000 46.12658  ? 262 LEU A CD1 1 
ATOM   2026 C CD2 . LEU A 1 262 ? -36.06300 4.51000   -27.62000 1.000 44.07371  ? 262 LEU A CD2 1 
ATOM   2027 N N   . ASP A 1 263 ? -31.09800 5.12700   -29.90100 1.000 39.77582  ? 263 ASP A N   1 
ATOM   2028 C CA  . ASP A 1 263 ? -30.02500 4.50900   -30.71700 1.000 42.02083  ? 263 ASP A CA  1 
ATOM   2029 C C   . ASP A 1 263 ? -29.30000 3.51000   -29.81200 1.000 40.81542  ? 263 ASP A C   1 
ATOM   2030 O O   . ASP A 1 263 ? -29.04200 2.38800   -30.25400 1.000 38.77570  ? 263 ASP A O   1 
ATOM   2031 C CB  . ASP A 1 263 ? -29.11700 5.58200   -31.31700 1.000 41.37075  ? 263 ASP A CB  1 
ATOM   2032 C CG  . ASP A 1 263 ? -27.94800 5.08100   -32.14900 1.000 56.86998  ? 263 ASP A CG  1 
ATOM   2033 O OD1 . ASP A 1 263 ? -27.91900 3.88500   -32.48800 1.000 51.76673  ? 263 ASP A OD1 1 
ATOM   2034 O OD2 . ASP A 1 263 ? -27.07600 5.90700   -32.46400 1.000 55.88828  ? 263 ASP A OD2 1 
ATOM   2035 N N   . MET A 1 264 ? -29.03100 3.90800   -28.56900 1.000 35.64638  ? 264 MET A N   1 
ATOM   2036 C CA  . MET A 1 264 ? -28.38800 2.98400   -27.65500 1.000 38.31249  ? 264 MET A CA  1 
ATOM   2037 C C   . MET A 1 264 ? -29.29900 1.78300   -27.34700 1.000 38.97309  ? 264 MET A C   1 
ATOM   2038 O O   . MET A 1 264 ? -28.81400 0.65200   -27.12400 1.000 36.82284  ? 264 MET A O   1 
ATOM   2039 C CB  . MET A 1 264 ? -28.02400 3.71000   -26.35200 1.000 34.21200  ? 264 MET A CB  1 
ATOM   2040 C CG  . MET A 1 264 ? -27.13400 2.81300   -25.40600 1.000 32.48811  ? 264 MET A CG  1 
ATOM   2041 S SD  . MET A 1 264 ? -25.46600 2.53500   -26.21000 1.000 36.49911  ? 264 MET A SD  1 
ATOM   2042 C CE  . MET A 1 264 ? -24.62500 4.01700   -25.67200 1.000 41.46813  ? 264 MET A CE  1 
ATOM   2043 N N   . CYS A 1 265 ? -30.62800 2.00800   -27.31000 1.000 37.42554  ? 265 CYS A N   1 
ATOM   2044 C CA  . CYS A 1 265 ? -31.53300 0.86700   -27.14300 1.000 41.49971  ? 265 CYS A CA  1 
ATOM   2045 C C   . CYS A 1 265 ? -31.42500 -0.13400  -28.29600 1.000 41.16546  ? 265 CYS A C   1 
ATOM   2046 O O   . CYS A 1 265 ? -31.55700 -1.34700  -28.07000 1.000 39.94426  ? 265 CYS A O   1 
ATOM   2047 C CB  . CYS A 1 265 ? -33.00200 1.33600   -27.00800 1.000 40.45748  ? 265 CYS A CB  1 
ATOM   2048 S SG  . CYS A 1 265 ? -33.34500 2.17400   -25.44000 1.000 40.59960  ? 265 CYS A SG  1 
ATOM   2049 N N   . ALA A 1 266 ? -31.17900 0.33700   -29.53500 1.000 38.56515  ? 266 ALA A N   1 
ATOM   2050 C CA  . ALA A 1 266 ? -30.95900 -0.61300  -30.63900 1.000 43.33151  ? 266 ALA A CA  1 
ATOM   2051 C C   . ALA A 1 266 ? -29.67600 -1.43700  -30.41600 1.000 42.44456  ? 266 ALA A C   1 
ATOM   2052 O O   . ALA A 1 266 ? -29.65000 -2.63500  -30.72100 1.000 43.70524  ? 266 ALA A O   1 
ATOM   2053 C CB  . ALA A 1 266 ? -30.91300 0.10600   -32.00800 1.000 47.06354  ? 266 ALA A CB  1 
ATOM   2054 N N   . SER A 1 267 ? -28.63800 -0.83600  -29.82400 1.000 42.07873  ? 267 SER A N   1 
ATOM   2055 C CA  . SER A 1 267 ? -27.44100 -1.58600  -29.45000 1.000 40.38905  ? 267 SER A CA  1 
ATOM   2056 C C   . SER A 1 267 ? -27.75200 -2.65300  -28.43400 1.000 42.32350  ? 267 SER A C   1 
ATOM   2057 O O   . SER A 1 267 ? -27.31300 -3.81500  -28.57600 1.000 40.51538  ? 267 SER A O   1 
ATOM   2058 C CB  . SER A 1 267 ? -26.38400 -0.64000  -28.86200 1.000 42.27612  ? 267 SER A CB  1 
ATOM   2059 O OG  . SER A 1 267 ? -25.78800 0.08500   -29.88200 1.000 45.37649  ? 267 SER A OG  1 
ATOM   2060 N N   . LEU A 1 268 ? -28.50400 -2.26800  -27.38100 1.000 40.06007  ? 268 LEU A N   1 
ATOM   2061 C CA  . LEU A 1 268 ? -28.86800 -3.21900  -26.34200 1.000 39.80740  ? 268 LEU A CA  1 
ATOM   2062 C C   . LEU A 1 268 ? -29.67600 -4.36400  -26.92200 1.000 42.03399  ? 268 LEU A C   1 
ATOM   2063 O O   . LEU A 1 268 ? -29.40700 -5.53700  -26.63700 1.000 42.76829  ? 268 LEU A O   1 
ATOM   2064 C CB  . LEU A 1 268 ? -29.65800 -2.50600  -25.22600 1.000 37.61240  ? 268 LEU A CB  1 
ATOM   2065 C CG  . LEU A 1 268 ? -30.13000 -3.37500  -24.06500 1.000 40.04954  ? 268 LEU A CG  1 
ATOM   2066 C CD1 . LEU A 1 268 ? -28.96800 -4.28300  -23.52000 1.000 38.89414  ? 268 LEU A CD1 1 
ATOM   2067 C CD2 . LEU A 1 268 ? -30.62200 -2.44500  -22.94600 1.000 36.23592  ? 268 LEU A CD2 1 
ATOM   2068 N N   . LYS A 1 269 ? -30.65400 -4.04900  -27.76700 1.000 40.42327  ? 269 LYS A N   1 
ATOM   2069 C CA  . LYS A 1 269 ? -31.42800 -5.10400  -28.42000 1.000 43.57628  ? 269 LYS A CA  1 
ATOM   2070 C C   . LYS A 1 269 ? -30.51500 -6.09800  -29.15200 1.000 47.69519  ? 269 LYS A C   1 
ATOM   2071 O O   . LYS A 1 269 ? -30.69200 -7.32200  -29.04900 1.000 46.65033  ? 269 LYS A O   1 
ATOM   2072 C CB  . LYS A 1 269 ? -32.43100 -4.46600  -29.37500 1.000 46.93194  ? 269 LYS A CB  1 
ATOM   2073 C CG  . LYS A 1 269 ? -33.13000 -5.43300  -30.29100 1.000 51.92991  ? 269 LYS A CG  1 
ATOM   2074 C CD  . LYS A 1 269 ? -34.18800 -4.74200  -31.22300 1.000 56.85419  ? 269 LYS A CD  1 
ATOM   2075 C CE  . LYS A 1 269 ? -35.10100 -3.65700  -30.56300 1.000 51.00348  ? 269 LYS A CE  1 
ATOM   2076 N NZ  . LYS A 1 269 ? -35.96600 -3.10900  -31.66900 1.000 54.75130  ? 269 LYS A NZ  1 
ATOM   2077 N N   . GLU A 1 270 ? -29.53900 -5.58700  -29.91600 1.000 42.99200  ? 270 GLU A N   1 
ATOM   2078 C CA  . GLU A 1 270 ? -28.64900 -6.48500  -30.63900 1.000 48.70058  ? 270 GLU A CA  1 
ATOM   2079 C C   . GLU A 1 270 ? -27.85600 -7.34000  -29.64800 1.000 48.31632  ? 270 GLU A C   1 
ATOM   2080 O O   . GLU A 1 270 ? -27.77700 -8.56200  -29.80200 1.000 50.96401  ? 270 GLU A O   1 
ATOM   2081 C CB  . GLU A 1 270 ? -27.73800 -5.65300  -31.56700 1.000 47.52675  ? 270 GLU A CB  1 
ATOM   2082 C CG  . GLU A 1 270 ? -26.82000 -6.49400  -32.49800 1.000 61.64423  ? 270 GLU A CG  1 
ATOM   2083 C CD  . GLU A 1 270 ? -25.90600 -5.67100  -33.47500 1.000 83.20471  ? 270 GLU A CD  1 
ATOM   2084 O OE1 . GLU A 1 270 ? -25.38300 -4.57000  -33.13500 1.000 72.63239  ? 270 GLU A OE1 1 
ATOM   2085 O OE2 . GLU A 1 270 ? -25.72600 -6.13800  -34.62300 1.000 100.91210 ? 270 GLU A OE2 1 
ATOM   2086 N N   . LEU A 1 271 ? -27.37800 -6.73200  -28.55400 1.000 44.80011  ? 271 LEU A N   1 
ATOM   2087 C CA  . LEU A 1 271 ? -26.62300 -7.47100  -27.53800 1.000 45.39492  ? 271 LEU A CA  1 
ATOM   2088 C C   . LEU A 1 271 ? -27.46000 -8.55200  -26.88500 1.000 48.80585  ? 271 LEU A C   1 
ATOM   2089 O O   . LEU A 1 271 ? -26.96000 -9.64600  -26.60000 1.000 47.30304  ? 271 LEU A O   1 
ATOM   2090 C CB  . LEU A 1 271 ? -26.07300 -6.51000  -26.47800 1.000 44.03686  ? 271 LEU A CB  1 
ATOM   2091 C CG  . LEU A 1 271 ? -24.91900 -5.61000  -26.96600 1.000 44.89749  ? 271 LEU A CG  1 
ATOM   2092 C CD1 . LEU A 1 271 ? -24.59400 -4.52100  -25.93300 1.000 43.61312  ? 271 LEU A CD1 1 
ATOM   2093 C CD2 . LEU A 1 271 ? -23.69200 -6.48300  -27.16900 1.000 46.41346  ? 271 LEU A CD2 1 
ATOM   2094 N N   . LEU A 1 272 ? -28.74000 -8.26100  -26.61800 1.000 44.52113  ? 272 LEU A N   1 
ATOM   2095 C CA  . LEU A 1 272 ? -29.62100 -9.28300  -26.07800 1.000 47.24251  ? 272 LEU A CA  1 
ATOM   2096 C C   . LEU A 1 272 ? -29.85800 -10.41200 -27.08000 1.000 49.63490  ? 272 LEU A C   1 
ATOM   2097 O O   . LEU A 1 272 ? -29.89800 -11.58500 -26.69800 1.000 50.30866  ? 272 LEU A O   1 
ATOM   2098 C CB  . LEU A 1 272 ? -30.96800 -8.64100  -25.67800 1.000 44.84748  ? 272 LEU A CB  1 
ATOM   2099 C CG  . LEU A 1 272 ? -30.83500 -7.67800  -24.48700 1.000 44.06844  ? 272 LEU A CG  1 
ATOM   2100 C CD1 . LEU A 1 272 ? -32.18700 -7.02500  -24.13700 1.000 42.53668  ? 272 LEU A CD1 1 
ATOM   2101 C CD2 . LEU A 1 272 ? -30.35000 -8.45300  -23.30300 1.000 42.89462  ? 272 LEU A CD2 1 
ATOM   2102 N N   . GLN A 1 273 ? -30.04400 -10.08500 -28.36400 1.000 48.21894  ? 273 GLN A N   1 
ATOM   2103 C CA  . GLN A 1 273 ? -30.43500 -11.13200 -29.30700 1.000 49.49278  ? 273 GLN A CA  1 
ATOM   2104 C C   . GLN A 1 273 ? -29.25000 -11.98200 -29.74500 1.000 56.27517  ? 273 GLN A C   1 
ATOM   2105 O O   . GLN A 1 273 ? -29.42100 -13.17700 -30.03200 1.000 56.97262  ? 273 GLN A O   1 
ATOM   2106 C CB  . GLN A 1 273 ? -31.10900 -10.50700 -30.52100 1.000 49.03483  ? 273 GLN A CB  1 
ATOM   2107 C CG  . GLN A 1 273 ? -32.53000 -9.98700  -30.16500 1.000 50.67186  ? 273 GLN A CG  1 
ATOM   2108 C CD  . GLN A 1 273 ? -33.09500 -9.12100  -31.26200 1.000 56.16726  ? 273 GLN A CD  1 
ATOM   2109 O OE1 . GLN A 1 273 ? -32.36200 -8.71000  -32.17300 1.000 59.87560  ? 273 GLN A OE1 1 
ATOM   2110 N NE2 . GLN A 1 273 ? -34.38100 -8.79000  -31.16500 1.000 54.24598  ? 273 GLN A NE2 1 
ATOM   2111 N N   . ASN A 1 274 ? -28.05200 -11.39200 -29.78400 1.000 53.78540  ? 274 ASN A N   1 
ATOM   2112 C CA  . ASN A 1 274 ? -26.87700 -12.06800 -30.32200 1.000 55.71194  ? 274 ASN A CA  1 
ATOM   2113 C C   . ASN A 1 274 ? -25.77900 -12.33800 -29.32400 1.000 57.62270  ? 274 ASN A C   1 
ATOM   2114 O O   . ASN A 1 274 ? -24.89600 -13.15400 -29.62600 1.000 58.90443  ? 274 ASN A O   1 
ATOM   2115 C CB  . ASN A 1 274 ? -26.26800 -11.25500 -31.46000 1.000 54.90922  ? 274 ASN A CB  1 
ATOM   2116 C CG  . ASN A 1 274 ? -27.27300 -10.95500 -32.53100 1.000 59.82033  ? 274 ASN A CG  1 
ATOM   2117 O OD1 . ASN A 1 274 ? -27.33900 -9.84000  -33.04800 1.000 67.97394  ? 274 ASN A OD1 1 
ATOM   2118 N ND2 . ASN A 1 274 ? -28.10500 -11.92700 -32.83300 1.000 62.86017  ? 274 ASN A ND2 1 
ATOM   2119 N N   . GLY A 1 275 ? -25.78100 -11.66800 -28.17600 1.000 57.89905  ? 275 GLY A N   1 
ATOM   2120 C CA  . GLY A 1 275 ? -24.69700 -11.80900 -27.22300 1.000 52.59578  ? 275 GLY A CA  1 
ATOM   2121 C C   . GLY A 1 275 ? -23.49800 -10.97400 -27.61600 1.000 54.86447  ? 275 GLY A C   1 
ATOM   2122 O O   . GLY A 1 275 ? -23.56300 -10.10200 -28.48200 1.000 55.42507  ? 275 GLY A O   1 
ATOM   2123 N N   . MET A 1 276 ? -22.37400 -11.25900 -26.97600 1.000 55.98040  ? 276 MET A N   1 
ATOM   2124 C CA  . MET A 1 276 ? -21.18400 -10.45600 -27.22300 1.000 58.24383  ? 276 MET A CA  1 
ATOM   2125 C C   . MET A 1 276 ? -20.18300 -11.07000 -28.21600 1.000 64.41299  ? 276 MET A C   1 
ATOM   2126 O O   . MET A 1 276 ? -19.23300 -10.37300 -28.60900 1.000 59.89666  ? 276 MET A O   1 
ATOM   2127 C CB  . MET A 1 276 ? -20.48400 -10.15000 -25.89900 1.000 57.68586  ? 276 MET A CB  1 
ATOM   2128 C CG  . MET A 1 276 ? -21.28300 -9.22700  -24.98600 1.000 54.42231  ? 276 MET A CG  1 
ATOM   2129 S SD  . MET A 1 276 ? -20.26500 -8.58400  -23.64900 1.000 56.07514  ? 276 MET A SD  1 
ATOM   2130 C CE  . MET A 1 276 ? -21.62400 -8.11100  -22.54200 1.000 46.49242  ? 276 MET A CE  1 
ATOM   2131 N N   . ASN A 1 277 ? -20.36300 -12.32700 -28.63700 1.000 66.76064  ? 277 ASN A N   1 
ATOM   2132 C CA  . ASN A 1 277 ? -19.44400 -12.97500 -29.58500 1.000 76.40653  ? 277 ASN A CA  1 
ATOM   2133 C C   . ASN A 1 277 ? -18.00000 -12.89500 -29.09300 1.000 71.43225  ? 277 ASN A C   1 
ATOM   2134 O O   . ASN A 1 277 ? -17.09200 -12.50500 -29.83100 1.000 69.73204  ? 277 ASN A O   1 
ATOM   2135 C CB  . ASN A 1 277 ? -19.55300 -12.38200 -30.99900 1.000 78.51731  ? 277 ASN A CB  1 
ATOM   2136 C CG  . ASN A 1 277 ? -20.91600 -12.61200 -31.64200 1.000 87.12360  ? 277 ASN A CG  1 
ATOM   2137 O OD1 . ASN A 1 277 ? -21.17800 -13.68800 -32.19200 1.000 92.34002  ? 277 ASN A OD1 1 
ATOM   2138 N ND2 . ASN A 1 277 ? -21.77900 -11.59000 -31.60700 1.000 83.09417  ? 277 ASN A ND2 1 
ATOM   2139 N N   . GLY A 1 278 ? -17.79400 -13.22300 -27.81500 1.000 69.52149  ? 278 GLY A N   1 
ATOM   2140 C CA  . GLY A 1 278 ? -16.45500 -13.24000 -27.26100 1.000 64.15243  ? 278 GLY A CA  1 
ATOM   2141 C C   . GLY A 1 278 ? -15.85400 -11.88900 -26.94000 1.000 62.20746  ? 278 GLY A C   1 
ATOM   2142 O O   . GLY A 1 278 ? -14.70300 -11.83200 -26.49400 1.000 59.57820  ? 278 GLY A O   1 
ATOM   2143 N N   . ARG A 1 279 ? -16.57500 -10.79800 -27.13200 1.000 61.07048  ? 279 ARG A N   1 
ATOM   2144 C CA  . ARG A 1 279 ? -16.01500 -9.50800  -26.75200 1.000 55.51455  ? 279 ARG A CA  1 
ATOM   2145 C C   . ARG A 1 279 ? -16.43800 -9.14500  -25.32100 1.000 52.21152  ? 279 ARG A C   1 
ATOM   2146 O O   . ARG A 1 279 ? -17.27300 -9.80500  -24.70500 1.000 51.35616  ? 279 ARG A O   1 
ATOM   2147 C CB  . ARG A 1 279 ? -16.43100 -8.44900  -27.77800 1.000 51.86148  ? 279 ARG A CB  1 
ATOM   2148 C CG  . ARG A 1 279 ? -15.46700 -8.44100  -29.01700 1.000 59.79928  ? 279 ARG A CG  1 
ATOM   2149 C CD  . ARG A 1 279 ? -16.13700 -7.90600  -30.22900 1.000 57.58322  ? 279 ARG A CD  1 
ATOM   2150 N NE  . ARG A 1 279 ? -17.44400 -8.53600  -30.38600 1.000 64.34982  ? 279 ARG A NE  1 
ATOM   2151 C CZ  . ARG A 1 279 ? -18.30000 -8.25700  -31.36400 1.000 63.08651  ? 279 ARG A CZ  1 
ATOM   2152 N NH1 . ARG A 1 279 ? -18.00100 -7.36800  -32.31800 1.000 63.00229  ? 279 ARG A NH1 1 
ATOM   2153 N NH2 . ARG A 1 279 ? -19.47000 -8.89500  -31.40000 1.000 63.81028  ? 279 ARG A NH2 1 
ATOM   2154 N N   . THR A 1 280 ? -15.84100 -8.09500  -24.78200 1.000 51.86148  ? 280 THR A N   1 
ATOM   2155 C CA  . THR A 1 280 ? -16.19800 -7.66500  -23.44500 1.000 45.94235  ? 280 THR A CA  1 
ATOM   2156 C C   . THR A 1 280 ? -16.50000 -6.17700  -23.46500 1.000 45.31596  ? 280 THR A C   1 
ATOM   2157 O O   . THR A 1 280 ? -16.11900 -5.43900  -24.38700 1.000 41.61552  ? 280 THR A O   1 
ATOM   2158 C CB  . THR A 1 280 ? -15.10900 -7.97500  -22.40500 1.000 47.90574  ? 280 THR A CB  1 
ATOM   2159 O OG1 . THR A 1 280 ? -13.90900 -7.28500  -22.76700 1.000 46.28186  ? 280 THR A OG1 1 
ATOM   2160 C CG2 . THR A 1 280 ? -14.82000 -9.51200  -22.37600 1.000 50.12180  ? 280 THR A CG2 1 
ATOM   2161 N N   . ILE A 1 281 ? -17.28800 -5.75800  -22.47700 1.000 41.34443  ? 281 ILE A N   1 
ATOM   2162 C CA  . ILE A 1 281 ? -17.60000 -4.34800  -22.29400 1.000 38.20458  ? 281 ILE A CA  1 
ATOM   2163 C C   . ILE A 1 281 ? -17.14200 -3.94300  -20.91900 1.000 40.39432  ? 281 ILE A C   1 
ATOM   2164 O O   . ILE A 1 281 ? -17.62300 -4.48000  -19.90100 1.000 40.04954  ? 281 ILE A O   1 
ATOM   2165 C CB  . ILE A 1 281 ? -19.10300 -4.05800  -22.51200 1.000 42.63932  ? 281 ILE A CB  1 
ATOM   2166 C CG1 . ILE A 1 281 ? -19.50300 -4.45300  -23.93100 1.000 43.87631  ? 281 ILE A CG1 1 
ATOM   2167 C CG2 . ILE A 1 281 ? -19.41900 -2.61400  -22.19400 1.000 40.59697  ? 281 ILE A CG2 1 
ATOM   2168 C CD1 . ILE A 1 281 ? -21.03900 -4.20000  -24.21100 1.000 44.99750  ? 281 ILE A CD1 1 
ATOM   2169 N N   . LEU A 1 282 ? -16.24500 -2.95400  -20.86400 1.000 39.71002  ? 282 LEU A N   1 
ATOM   2170 C CA  . LEU A 1 282 ? -15.72600 -2.46600  -19.56100 1.000 41.78396  ? 282 LEU A CA  1 
ATOM   2171 C C   . LEU A 1 282 ? -15.26200 -3.62300  -18.67500 1.000 41.70237  ? 282 LEU A C   1 
ATOM   2172 O O   . LEU A 1 282 ? -15.52500 -3.64200  -17.46800 1.000 42.72618  ? 282 LEU A O   1 
ATOM   2173 C CB  . LEU A 1 282 ? -16.76500 -1.60600  -18.79200 1.000 40.82332  ? 282 LEU A CB  1 
ATOM   2174 C CG  . LEU A 1 282 ? -17.00300 -0.21300  -19.35600 1.000 39.45999  ? 282 LEU A CG  1 
ATOM   2175 C CD1 . LEU A 1 282 ? -18.09800 0.53700   -18.62800 1.000 36.55438  ? 282 LEU A CD1 1 
ATOM   2176 C CD2 . LEU A 1 282 ? -15.65700 0.54200   -19.27500 1.000 36.81494  ? 282 LEU A CD2 1 
ATOM   2177 N N   . GLY A 1 283 ? -14.63200 -4.61900  -19.29700 1.000 40.61803  ? 283 GLY A N   1 
ATOM   2178 C CA  . GLY A 1 283 ? -14.07100 -5.75600  -18.59500 1.000 44.04739  ? 283 GLY A CA  1 
ATOM   2179 C C   . GLY A 1 283 ? -15.04400 -6.86400  -18.23500 1.000 49.00324  ? 283 GLY A C   1 
ATOM   2180 O O   . GLY A 1 283 ? -14.63100 -7.82200  -17.57100 1.000 50.49553  ? 283 GLY A O   1 
ATOM   2181 N N   . SER A 1 284 ? -16.30000 -6.79700  -18.69400 1.000 44.13687  ? 284 SER A N   1 
ATOM   2182 C CA  . SER A 1 284 ? -17.34400 -7.75400  -18.34200 1.000 43.63418  ? 284 SER A CA  1 
ATOM   2183 C C   . SER A 1 284 ? -17.81300 -8.50000  -19.59000 1.000 44.64483  ? 284 SER A C   1 
ATOM   2184 O O   . SER A 1 284 ? -17.86000 -7.93300  -20.69700 1.000 43.41573  ? 284 SER A O   1 
ATOM   2185 C CB  . SER A 1 284 ? -18.52300 -7.01500  -17.63800 1.000 42.66564  ? 284 SER A CB  1 
ATOM   2186 O OG  . SER A 1 284 ? -19.61300 -7.91500  -17.41900 1.000 44.65009  ? 284 SER A OG  1 
ATOM   2187 N N   . ALA A 1 285 ? -18.10000 -9.79900  -19.43200 1.000 40.12586  ? 285 ALA A N   1 
ATOM   2188 C CA  . ALA A 1 285 ? -18.74500 -10.57500 -20.47600 1.000 43.13938  ? 285 ALA A CA  1 
ATOM   2189 C C   . ALA A 1 285 ? -20.26500 -10.61700 -20.27600 1.000 42.41561  ? 285 ALA A C   1 
ATOM   2190 O O   . ALA A 1 285 ? -20.97900 -11.22300 -21.07700 1.000 47.20040  ? 285 ALA A O   1 
ATOM   2191 C CB  . ALA A 1 285 ? -18.18300 -11.98800 -20.51200 1.000 44.61324  ? 285 ALA A CB  1 
ATOM   2192 N N   . LEU A 1 286 ? -20.75900 -9.96100  -19.25500 1.000 42.32876  ? 286 LEU A N   1 
ATOM   2193 C CA  . LEU A 1 286 ? -22.19200 -9.87700  -18.98800 1.000 43.86579  ? 286 LEU A CA  1 
ATOM   2194 C C   . LEU A 1 286 ? -22.60400 -8.42300  -19.04100 1.000 40.58381  ? 286 LEU A C   1 
ATOM   2195 O O   . LEU A 1 286 ? -21.80500 -7.52600  -18.76700 1.000 41.69447  ? 286 LEU A O   1 
ATOM   2196 C CB  . LEU A 1 286 ? -22.54400 -10.45400 -17.61800 1.000 44.82380  ? 286 LEU A CB  1 
ATOM   2197 C CG  . LEU A 1 286 ? -22.26900 -11.93400 -17.40800 1.000 49.66911  ? 286 LEU A CG  1 
ATOM   2198 C CD1 . LEU A 1 286 ? -22.65800 -12.32100 -15.98200 1.000 52.34049  ? 286 LEU A CD1 1 
ATOM   2199 C CD2 . LEU A 1 286 ? -23.06700 -12.70000 -18.44000 1.000 50.58501  ? 286 LEU A CD2 1 
ATOM   2200 N N   . LEU A 1 287 ? -23.87700 -8.18900  -19.33500 1.000 38.33354  ? 287 LEU A N   1 
ATOM   2201 C CA  . LEU A 1 287 ? -24.40800 -6.83800  -19.29600 1.000 39.07311  ? 287 LEU A CA  1 
ATOM   2202 C C   . LEU A 1 287 ? -24.61500 -6.43400  -17.84500 1.000 39.26260  ? 287 LEU A C   1 
ATOM   2203 O O   . LEU A 1 287 ? -25.38600 -7.06400  -17.10300 1.000 39.26787  ? 287 LEU A O   1 
ATOM   2204 C CB  . LEU A 1 287 ? -25.71800 -6.76200  -20.09900 1.000 39.44157  ? 287 LEU A CB  1 
ATOM   2205 C CG  . LEU A 1 287 ? -25.55700 -7.14700  -21.58000 1.000 38.92046  ? 287 LEU A CG  1 
ATOM   2206 C CD1 . LEU A 1 287 ? -26.91900 -7.34600  -22.33000 1.000 45.33175  ? 287 LEU A CD1 1 
ATOM   2207 C CD2 . LEU A 1 287 ? -24.58200 -6.18700  -22.36900 1.000 44.28426  ? 287 LEU A CD2 1 
ATOM   2208 N N   . GLU A 1 288 ? -24.01300 -5.34400  -17.43400 1.000 36.09117  ? 288 GLU A N   1 
ATOM   2209 C CA  . GLU A 1 288 ? -24.00800 -4.94500  -16.02500 1.000 36.00168  ? 288 GLU A CA  1 
ATOM   2210 C C   . GLU A 1 288 ? -25.17700 -4.01600  -15.67300 1.000 35.89904  ? 288 GLU A C   1 
ATOM   2211 O O   . GLU A 1 288 ? -25.36700 -2.99700  -16.32400 1.000 37.23868  ? 288 GLU A O   1 
ATOM   2212 C CB  . GLU A 1 288 ? -22.66200 -4.25100  -15.76200 1.000 40.32852  ? 288 GLU A CB  1 
ATOM   2213 C CG  . GLU A 1 288 ? -22.54100 -3.61300  -14.39800 1.000 42.10505  ? 288 GLU A CG  1 
ATOM   2214 C CD  . GLU A 1 288 ? -22.48200 -4.64400  -13.25400 1.000 47.56360  ? 288 GLU A CD  1 
ATOM   2215 O OE1 . GLU A 1 288 ? -21.62900 -5.58500  -13.37100 1.000 47.66887  ? 288 GLU A OE1 1 
ATOM   2216 O OE2 . GLU A 1 288 ? -23.35400 -4.52000  -12.29200 1.000 41.28127  ? 288 GLU A OE2 1 
ATOM   2217 N N   . ASP A 1 289 ? -25.98900 -4.35200  -14.64900 1.000 35.06210  ? 289 ASP A N   1 
ATOM   2218 C CA  . ASP A 1 289 ? -27.08200 -3.43200  -14.34900 1.000 36.74125  ? 289 ASP A CA  1 
ATOM   2219 C C   . ASP A 1 289 ? -27.01800 -2.79400  -12.93900 1.000 34.76996  ? 289 ASP A C   1 
ATOM   2220 O O   . ASP A 1 289 ? -28.04500 -2.35200  -12.44300 1.000 35.43320  ? 289 ASP A O   1 
ATOM   2221 C CB  . ASP A 1 289 ? -28.43700 -4.17300  -14.53600 1.000 35.31213  ? 289 ASP A CB  1 
ATOM   2222 C CG  . ASP A 1 289 ? -28.76300 -5.13100  -13.40700 1.000 38.24932  ? 289 ASP A CG  1 
ATOM   2223 O OD1 . ASP A 1 289 ? -27.86100 -5.61600  -12.66900 1.000 35.70428  ? 289 ASP A OD1 1 
ATOM   2224 O OD2 . ASP A 1 289 ? -29.96800 -5.47500  -13.29800 1.000 36.50701  ? 289 ASP A OD2 1 
ATOM   2225 N N   . GLU A 1 290 ? -25.83700 -2.67700  -12.32700 1.000 32.09859  ? 290 GLU A N   1 
ATOM   2226 C CA  . GLU A 1 290 ? -25.75400 -2.13300  -10.94000 1.000 35.52005  ? 290 GLU A CA  1 
ATOM   2227 C C   . GLU A 1 290 ? -25.12000 -0.73300  -10.92200 1.000 41.13651  ? 290 GLU A C   1 
ATOM   2228 O O   . GLU A 1 290 ? -24.61300 -0.34500  -9.86800  1.000 39.96005  ? 290 GLU A O   1 
ATOM   2229 C CB  . GLU A 1 290 ? -25.12700 -3.13900  -9.97100  1.000 36.72546  ? 290 GLU A CB  1 
ATOM   2230 C CG  . GLU A 1 290 ? -25.94700 -4.40900  -9.81300  1.000 39.30471  ? 290 GLU A CG  1 
ATOM   2231 C CD  . GLU A 1 290 ? -26.15700 -4.92300  -8.39800  1.000 43.15254  ? 290 GLU A CD  1 
ATOM   2232 O OE1 . GLU A 1 290 ? -25.48400 -4.42600  -7.48100  1.000 43.71314  ? 290 GLU A OE1 1 
ATOM   2233 O OE2 . GLU A 1 290 ? -27.00200 -5.82000  -8.21600  1.000 40.70225  ? 290 GLU A OE2 1 
ATOM   2234 N N   . PHE A 1 291 ? -25.10100 -0.03000  -12.05000 1.000 32.58812  ? 291 PHE A N   1 
ATOM   2235 C CA  . PHE A 1 291 ? -24.71200 1.37200   -12.07000 1.000 33.76984  ? 291 PHE A CA  1 
ATOM   2236 C C   . PHE A 1 291 ? -25.89000 2.20400   -12.51600 1.000 33.53560  ? 291 PHE A C   1 
ATOM   2237 O O   . PHE A 1 291 ? -26.40400 2.01100   -13.62600 1.000 34.10935  ? 291 PHE A O   1 
ATOM   2238 C CB  . PHE A 1 291 ? -23.54100 1.59200   -13.06900 1.000 34.78838  ? 291 PHE A CB  1 
ATOM   2239 C CG  . PHE A 1 291 ? -22.30800 0.87100   -12.71400 1.000 39.28629  ? 291 PHE A CG  1 
ATOM   2240 C CD1 . PHE A 1 291 ? -21.39900 1.42800   -11.80100 1.000 43.60786  ? 291 PHE A CD1 1 
ATOM   2241 C CD2 . PHE A 1 291 ? -22.00900 -0.32000  -13.30500 1.000 39.53895  ? 291 PHE A CD2 1 
ATOM   2242 C CE1 . PHE A 1 291 ? -20.17200 0.76600   -11.48600 1.000 40.06796  ? 291 PHE A CE1 1 
ATOM   2243 C CE2 . PHE A 1 291 ? -20.79800 -0.97400  -13.00600 1.000 45.15015  ? 291 PHE A CE2 1 
ATOM   2244 C CZ  . PHE A 1 291 ? -19.90100 -0.42200  -12.09000 1.000 43.12622  ? 291 PHE A CZ  1 
ATOM   2245 N N   . THR A 1 292 ? -26.29900 3.15200   -11.69600 1.000 39.61264  ? 292 THR A N   1 
ATOM   2246 C CA  . THR A 1 292 ? -27.28900 4.10500   -12.14200 1.000 37.45449  ? 292 THR A CA  1 
ATOM   2247 C C   . THR A 1 292 ? -26.65800 5.12200   -13.11700 1.000 38.12562  ? 292 THR A C   1 
ATOM   2248 O O   . THR A 1 292 ? -25.43100 5.32300   -13.13700 1.000 37.25973  ? 292 THR A O   1 
ATOM   2249 C CB  . THR A 1 292 ? -27.85900 4.86300   -10.96500 1.000 38.75728  ? 292 THR A CB  1 
ATOM   2250 O OG1 . THR A 1 292 ? -26.79900 5.63100   -10.41500 1.000 37.05707  ? 292 THR A OG1 1 
ATOM   2251 C CG2 . THR A 1 292 ? -28.50800 3.90300   -9.93100  1.000 36.54386  ? 292 THR A CG2 1 
ATOM   2252 N N   . PRO A 1 293 ? -27.50300 5.83800   -13.84900 1.000 38.39671  ? 293 PRO A N   1 
ATOM   2253 C CA  . PRO A 1 293 ? -27.04300 7.00400   -14.61500 1.000 38.13089  ? 293 PRO A CA  1 
ATOM   2254 C C   . PRO A 1 293 ? -26.25900 8.01500   -13.76500 1.000 39.78372  ? 293 PRO A C   1 
ATOM   2255 O O   . PRO A 1 293 ? -25.13800 8.40700   -14.16600 1.000 39.03626  ? 293 PRO A O   1 
ATOM   2256 C CB  . PRO A 1 293 ? -28.34200 7.58800   -15.15600 1.000 37.37027  ? 293 PRO A CB  1 
ATOM   2257 C CG  . PRO A 1 293 ? -29.26500 6.33700   -15.31400 1.000 38.26248  ? 293 PRO A CG  1 
ATOM   2258 C CD  . PRO A 1 293 ? -28.90100 5.45000   -14.14000 1.000 36.19118  ? 293 PRO A CD  1 
ATOM   2259 N N   . PHE A 1 294 ? -26.72300 8.27300   -12.54000 1.000 41.48392  ? 294 PHE A N   1 
ATOM   2260 C CA  . PHE A 1 294 ? -25.99500 9.09500   -11.57700 1.000 38.33618  ? 294 PHE A CA  1 
ATOM   2261 C C   . PHE A 1 294 ? -24.64600 8.50200   -11.25000 1.000 41.43655  ? 294 PHE A C   1 
ATOM   2262 O O   . PHE A 1 294 ? -23.66500 9.24500   -11.15100 1.000 41.58393  ? 294 PHE A O   1 
ATOM   2263 C CB  . PHE A 1 294 ? -26.78600 9.23700   -10.26000 1.000 45.15805  ? 294 PHE A CB  1 
ATOM   2264 C CG  . PHE A 1 294 ? -25.99700 9.96200   -9.16300  1.000 47.27409  ? 294 PHE A CG  1 
ATOM   2265 C CD1 . PHE A 1 294 ? -25.15800 9.25700   -8.29700  1.000 51.41932  ? 294 PHE A CD1 1 
ATOM   2266 C CD2 . PHE A 1 294 ? -26.06800 11.32600  -9.01800  1.000 53.72749  ? 294 PHE A CD2 1 
ATOM   2267 C CE1 . PHE A 1 294 ? -24.42500 9.91600   -7.30900  1.000 54.90922  ? 294 PHE A CE1 1 
ATOM   2268 C CE2 . PHE A 1 294 ? -25.35300 11.97900  -8.01300  1.000 53.57748  ? 294 PHE A CE2 1 
ATOM   2269 C CZ  . PHE A 1 294 ? -24.54400 11.27700  -7.17200  1.000 56.26464  ? 294 PHE A CZ  1 
ATOM   2270 N N   . ASP A 1 295 ? -24.55700 7.17600   -11.05600 1.000 37.48081  ? 295 ASP A N   1 
ATOM   2271 C CA  . ASP A 1 295 ? -23.25000 6.57900   -10.77100 1.000 41.27863  ? 295 ASP A CA  1 
ATOM   2272 C C   . ASP A 1 295 ? -22.28600 6.78800   -11.93600 1.000 42.41035  ? 295 ASP A C   1 
ATOM   2273 O O   . ASP A 1 295 ? -21.07400 6.99400   -11.73600 1.000 38.75991  ? 295 ASP A O   1 
ATOM   2274 C CB  . ASP A 1 295 ? -23.36000 5.08400   -10.49400 1.000 36.89390  ? 295 ASP A CB  1 
ATOM   2275 C CG  . ASP A 1 295 ? -24.20100 4.79400   -9.27800  1.000 42.38666  ? 295 ASP A CG  1 
ATOM   2276 O OD1 . ASP A 1 295 ? -24.37500 5.73800   -8.46300  1.000 40.64435  ? 295 ASP A OD1 1 
ATOM   2277 O OD2 . ASP A 1 295 ? -24.66700 3.61700   -9.16000  1.000 40.65224  ? 295 ASP A OD2 1 
ATOM   2278 N N   . VAL A 1 296 ? -22.79300 6.71100   -13.16800 1.000 38.10194  ? 296 VAL A N   1 
ATOM   2279 C CA  . VAL A 1 296 ? -21.88600 6.90400   -14.31500 1.000 38.13615  ? 296 VAL A CA  1 
ATOM   2280 C C   . VAL A 1 296 ? -21.32400 8.33300   -14.34000 1.000 41.19968  ? 296 VAL A C   1 
ATOM   2281 O O   . VAL A 1 296 ? -20.09600 8.55200   -14.50300 1.000 42.69459  ? 296 VAL A O   1 
ATOM   2282 C CB  . VAL A 1 296 ? -22.61000 6.54800   -15.63000 1.000 38.14142  ? 296 VAL A CB  1 
ATOM   2283 C CG1 . VAL A 1 296 ? -21.63700 6.90100   -16.88200 1.000 38.45987  ? 296 VAL A CG1 1 
ATOM   2284 C CG2 . VAL A 1 296 ? -23.03000 5.07600   -15.63400 1.000 34.04619  ? 296 VAL A CG2 1 
ATOM   2285 N N   . VAL A 1 297 ? -22.20600 9.32400   -14.23900 1.000 38.61252  ? 297 VAL A N   1 
ATOM   2286 C CA  . VAL A 1 297 ? -21.80700 10.72400  -14.26000 1.000 44.95802  ? 297 VAL A CA  1 
ATOM   2287 C C   . VAL A 1 297 ? -20.84600 11.04000  -13.12300 1.000 46.79245  ? 297 VAL A C   1 
ATOM   2288 O O   . VAL A 1 297 ? -19.82000 11.71000  -13.33200 1.000 48.22683  ? 297 VAL A O   1 
ATOM   2289 C CB  . VAL A 1 297 ? -23.03500 11.64300  -14.20800 1.000 46.93984  ? 297 VAL A CB  1 
ATOM   2290 C CG1 . VAL A 1 297 ? -22.59000 13.09400  -13.98800 1.000 49.42172  ? 297 VAL A CG1 1 
ATOM   2291 C CG2 . VAL A 1 297 ? -23.93500 11.51100  -15.51800 1.000 44.85538  ? 297 VAL A CG2 1 
ATOM   2292 N N   . ARG A 1 298 ? -21.14700 10.55900  -11.91600 1.000 41.74448  ? 298 ARG A N   1 
ATOM   2293 C CA  . ARG A 1 298 ? -20.28800 10.84500  -10.76700 1.000 46.03973  ? 298 ARG A CA  1 
ATOM   2294 C C   . ARG A 1 298 ? -18.87800 10.38500  -11.02700 1.000 50.14549  ? 298 ARG A C   1 
ATOM   2295 O O   . ARG A 1 298 ? -17.89900 11.05000  -10.65100 1.000 48.96113  ? 298 ARG A O   1 
ATOM   2296 C CB  . ARG A 1 298 ? -20.81900 10.16100  -9.48700  1.000 48.23999  ? 298 ARG A CB  1 
ATOM   2297 C CG  . ARG A 1 298 ? -19.63700 9.66900   -8.56200  1.000 53.83803  ? 298 ARG A CG  1 
ATOM   2298 C CD  . ARG A 1 298 ? -20.04100 9.34100   -7.06900  1.000 58.00695  ? 298 ARG A CD  1 
ATOM   2299 N NE  . ARG A 1 298 ? -20.39400 7.96500   -6.73700  1.000 61.86268  ? 298 ARG A NE  1 
ATOM   2300 C CZ  . ARG A 1 298 ? -19.76700 7.19700   -5.83600  1.000 68.24239  ? 298 ARG A CZ  1 
ATOM   2301 N NH1 . ARG A 1 298 ? -18.64400 7.59500   -5.23000  1.000 49.56384  ? 298 ARG A NH1 1 
ATOM   2302 N NH2 . ARG A 1 298 ? -20.33400 6.03300   -5.46000  1.000 59.25184  ? 298 ARG A NH2 1 
ATOM   2303 N N   . GLN A 1 299 ? -18.75600 9.24800   -11.67900 1.000 48.10577  ? 299 GLN A N   1 
ATOM   2304 C CA  . GLN A 1 299 ? -17.46600 8.62200   -11.83400 1.000 47.04511  ? 299 GLN A CA  1 
ATOM   2305 C C   . GLN A 1 299 ? -16.78200 8.99700   -13.13100 1.000 49.04272  ? 299 GLN A C   1 
ATOM   2306 O O   . GLN A 1 299 ? -15.56300 9.18500   -13.12600 1.000 53.00899  ? 299 GLN A O   1 
ATOM   2307 C CB  . GLN A 1 299 ? -17.62700 7.10500   -11.70000 1.000 46.94510  ? 299 GLN A CB  1 
ATOM   2308 C CG  . GLN A 1 299 ? -16.39400 6.41100   -11.92400 1.000 43.26308  ? 299 GLN A CG  1 
ATOM   2309 C CD  . GLN A 1 299 ? -16.39900 4.94400   -11.57800 1.000 42.97884  ? 299 GLN A CD  1 
ATOM   2310 O OE1 . GLN A 1 299 ? -15.42800 4.27100   -11.90400 1.000 37.03339  ? 299 GLN A OE1 1 
ATOM   2311 N NE2 . GLN A 1 299 ? -17.52800 4.39700   -10.98700 1.000 38.08088  ? 299 GLN A NE2 1 
ATOM   2312 N N   . CYS A 1 300 ? -17.51900 9.15400   -14.23600 1.000 45.17647  ? 300 CYS A N   1 
ATOM   2313 C CA  . CYS A 1 300 ? -16.94700 9.44500   -15.54200 1.000 54.16702  ? 300 CYS A CA  1 
ATOM   2314 C C   . CYS A 1 300 ? -16.60700 10.93900  -15.74700 1.000 60.63885  ? 300 CYS A C   1 
ATOM   2315 O O   . CYS A 1 300 ? -17.06000 11.84800  -15.04100 1.000 60.02299  ? 300 CYS A O   1 
ATOM   2316 C CB  . CYS A 1 300 ? -17.87100 8.94300   -16.65900 1.000 47.18460  ? 300 CYS A CB  1 
ATOM   2317 S SG  . CYS A 1 300 ? -17.86300 7.12200   -16.84300 1.000 48.73479  ? 300 CYS A SG  1 
ATOM   2318 N N   . SER A 1 301 ? -15.78400 11.18000  -16.76400 1.000 67.45019  ? 301 SER A N   1 
ATOM   2319 C CA  . SER A 1 301 ? -15.52700 12.55200  -17.16600 1.000 75.22481  ? 301 SER A CA  1 
ATOM   2320 C C   . SER A 1 301 ? -16.72300 13.07500  -17.96000 1.000 84.42328  ? 301 SER A C   1 
ATOM   2321 O O   . SER A 1 301 ? -17.57500 12.30000  -18.42600 1.000 83.04417  ? 301 SER A O   1 
ATOM   2322 C CB  . SER A 1 301 ? -14.22800 12.63300  -17.99200 1.000 76.24862  ? 301 SER A CB  1 
ATOM   2323 O OG  . SER A 1 301 ? -14.33500 11.89000  -19.19800 1.000 67.75549  ? 301 SER A OG  1 
ATOM   2324 N N   . GLY A 1 302 ? -16.81100 14.40900  -18.04400 1.000 78.86209  ? 302 GLY A N   1 
ATOM   2325 C CA  . GLY A 1 302 ? -17.88300 15.10600  -18.74800 1.000 74.09046  ? 302 GLY A CA  1 
ATOM   2326 C C   . GLY A 1 302 ? -17.36200 15.88800  -19.94900 1.000 73.09824  ? 302 GLY A C   1 
ATOM   2327 O O   . GLY A 1 302 ? -16.40700 15.46100  -20.61500 1.000 72.78767  ? 302 GLY A O   1 
ATOM   2328 N N   . SER B 1 1   ? -23.35700 -15.47500 3.23500   1.000 45.56073  ? 1   SER B N   1 
ATOM   2329 C CA  . SER B 1 1   ? -23.13000 -15.73900 1.80400   1.000 49.75597  ? 1   SER B CA  1 
ATOM   2330 C C   . SER B 1 1   ? -22.90300 -14.49100 0.99400   1.000 45.29227  ? 1   SER B C   1 
ATOM   2331 O O   . SER B 1 1   ? -23.21300 -13.38700 1.45700   1.000 41.38654  ? 1   SER B O   1 
ATOM   2332 C CB  . SER B 1 1   ? -24.32500 -16.47200 1.17800   1.000 46.97669  ? 1   SER B CB  1 
ATOM   2333 O OG  . SER B 1 1   ? -24.43500 -17.74900 1.78100   1.000 56.08041  ? 1   SER B OG  1 
ATOM   2334 N N   . GLY B 1 2   ? -22.45500 -14.68800 -0.25200  1.000 44.82643  ? 2   GLY B N   1 
ATOM   2335 C CA  . GLY B 1 2   ? -22.14800 -13.61400 -1.17700  1.000 41.61552  ? 2   GLY B CA  1 
ATOM   2336 C C   . GLY B 1 2   ? -20.63800 -13.41100 -1.31400  1.000 41.82080  ? 2   GLY B C   1 
ATOM   2337 O O   . GLY B 1 2   ? -19.83900 -13.75700 -0.44500  1.000 43.93158  ? 2   GLY B O   1 
ATOM   2338 N N   . PHE B 1 3   ? -20.24200 -12.83600 -2.41000  1.000 39.66791  ? 3   PHE B N   1 
ATOM   2339 C CA  . PHE B 1 3   ? -18.81300 -12.57400 -2.56000  1.000 41.49182  ? 3   PHE B CA  1 
ATOM   2340 C C   . PHE B 1 3   ? -18.68500 -11.32500 -3.38400  1.000 38.83624  ? 3   PHE B C   1 
ATOM   2341 O O   . PHE B 1 3   ? -19.12700 -11.30100 -4.53200  1.000 42.79197  ? 3   PHE B O   1 
ATOM   2342 C CB  . PHE B 1 3   ? -18.06200 -13.74500 -3.21200  1.000 44.80011  ? 3   PHE B CB  1 
ATOM   2343 C CG  . PHE B 1 3   ? -16.56400 -13.67800 -2.97000  1.000 41.78133  ? 3   PHE B CG  1 
ATOM   2344 C CD1 . PHE B 1 3   ? -16.05700 -13.90000 -1.67700  1.000 42.14453  ? 3   PHE B CD1 1 
ATOM   2345 C CD2 . PHE B 1 3   ? -15.70400 -13.33200 -3.99900  1.000 44.01580  ? 3   PHE B CD2 1 
ATOM   2346 C CE1 . PHE B 1 3   ? -14.70400 -13.83200 -1.42100  1.000 46.77403  ? 3   PHE B CE1 1 
ATOM   2347 C CE2 . PHE B 1 3   ? -14.32900 -13.26600 -3.78100  1.000 42.10242  ? 3   PHE B CE2 1 
ATOM   2348 C CZ  . PHE B 1 3   ? -13.81100 -13.48800 -2.48300  1.000 41.48392  ? 3   PHE B CZ  1 
ATOM   2349 N N   . ARG B 1 4   ? -18.11900 -10.26700 -2.80700  1.000 39.74424  ? 4   ARG B N   1 
ATOM   2350 C CA  . ARG B 1 4   ? -18.06000 -8.99200  -3.50500  1.000 40.09954  ? 4   ARG B CA  1 
ATOM   2351 C C   . ARG B 1 4   ? -16.61900 -8.47100  -3.52000  1.000 39.38630  ? 4   ARG B C   1 
ATOM   2352 O O   . ARG B 1 4   ? -15.81600 -8.78500  -2.64800  1.000 38.71517  ? 4   ARG B O   1 
ATOM   2353 C CB  . ARG B 1 4   ? -18.91200 -7.91600  -2.88100  1.000 38.95730  ? 4   ARG B CB  1 
ATOM   2354 C CG  . ARG B 1 4   ? -20.48200 -8.02900  -3.07600  1.000 45.10014  ? 4   ARG B CG  1 
ATOM   2355 C CD  . ARG B 1 4   ? -20.85600 -7.21400  -4.35700  1.000 47.26619  ? 4   ARG B CD  1 
ATOM   2356 N NE  . ARG B 1 4   ? -22.29100 -6.87000  -4.40300  1.000 47.12407  ? 4   ARG B NE  1 
ATOM   2357 C CZ  . ARG B 1 4   ? -22.90600 -6.47300  -5.52600  1.000 50.67713  ? 4   ARG B CZ  1 
ATOM   2358 N NH1 . ARG B 1 4   ? -22.21300 -6.20600  -6.62700  1.000 54.90132  ? 4   ARG B NH1 1 
ATOM   2359 N NH2 . ARG B 1 4   ? -24.25800 -6.40100  -5.57000  1.000 42.18927  ? 4   ARG B NH2 1 
ATOM   2360 N N   . LYS B 1 5   ? -16.34300 -7.63000  -4.47700  1.000 38.60200  ? 5   LYS B N   1 
ATOM   2361 C CA  . LYS B 1 5   ? -15.09400 -6.86600  -4.43700  1.000 42.42614  ? 5   LYS B CA  1 
ATOM   2362 C C   . LYS B 1 5   ? -15.23300 -5.84500  -3.29800  1.000 40.82595  ? 5   LYS B C   1 
ATOM   2363 O O   . LYS B 1 5   ? -16.08200 -4.95300  -3.32800  1.000 43.60523  ? 5   LYS B O   1 
ATOM   2364 C CB  . LYS B 1 5   ? -14.82900 -6.25300  -5.80300  1.000 43.54996  ? 5   LYS B CB  1 
ATOM   2365 C CG  . LYS B 1 5   ? -13.32500 -6.28400  -6.22200  1.000 48.49002  ? 5   LYS B CG  1 
ATOM   2366 C CD  . LYS B 1 5   ? -13.22200 -6.28900  -7.71600  1.000 51.92728  ? 5   LYS B CD  1 
ATOM   2367 C CE  . LYS B 1 5   ? -12.57300 -7.56900  -8.22800  1.000 48.60846  ? 5   LYS B CE  1 
ATOM   2368 N NZ  . LYS B 1 5   ? -12.65300 -7.47500  -9.67800  1.000 56.75417  ? 5   LYS B NZ  1 
ATOM   2369 N N   . MET B 1 6   ? -14.52700 -6.07600  -2.22200  1.000 36.86758  ? 6   MET B N   1 
ATOM   2370 C CA  . MET B 1 6   ? -14.72300 -5.36700  -0.96900  1.000 40.53644  ? 6   MET B CA  1 
ATOM   2371 C C   . MET B 1 6   ? -13.47700 -4.58700  -0.58600  1.000 39.17049  ? 6   MET B C   1 
ATOM   2372 O O   . MET B 1 6   ? -12.46000 -5.19400  -0.27500  1.000 42.63932  ? 6   MET B O   1 
ATOM   2373 C CB  . MET B 1 6   ? -15.06500 -6.36900  0.14900   1.000 39.16522  ? 6   MET B CB  1 
ATOM   2374 C CG  . MET B 1 6   ? -15.39100 -5.74700  1.40000   1.000 44.58429  ? 6   MET B CG  1 
ATOM   2375 S SD  . MET B 1 6   ? -16.27800 -6.97600  2.44100   1.000 51.67988  ? 6   MET B SD  1 
ATOM   2376 C CE  . MET B 1 6   ? -15.02100 -8.18100  2.84300   1.000 48.00839  ? 6   MET B CE  1 
ATOM   2377 N N   . ALA B 1 7   ? -13.61900 -3.28400  -0.41900  1.000 37.48871  ? 7   ALA B N   1 
ATOM   2378 C CA  . ALA B 1 7   ? -12.49200 -2.45300  0.00000   1.000 38.00719  ? 7   ALA B CA  1 
ATOM   2379 C C   . ALA B 1 7   ? -12.39300 -2.44800  1.51500   1.000 43.74735  ? 7   ALA B C   1 
ATOM   2380 O O   . ALA B 1 7   ? -13.35900 -2.78400  2.21900   1.000 40.63382  ? 7   ALA B O   1 
ATOM   2381 C CB  . ALA B 1 7   ? -12.70700 -1.04900  -0.53400  1.000 39.93900  ? 7   ALA B CB  1 
ATOM   2382 N N   . PHE B 1 8   ? -11.22800 -2.08900  2.02200   1.000 37.62820  ? 8   PHE B N   1 
ATOM   2383 C CA  . PHE B 1 8   ? -11.13800 -1.81400  3.44200   1.000 40.49959  ? 8   PHE B CA  1 
ATOM   2384 C C   . PHE B 1 8   ? -11.90400 -0.53100  3.77000   1.000 42.13137  ? 8   PHE B C   1 
ATOM   2385 O O   . PHE B 1 8   ? -12.03500 0.35500   2.92800   1.000 42.83935  ? 8   PHE B O   1 
ATOM   2386 C CB  . PHE B 1 8   ? -9.69100  -1.67300  3.91800   1.000 43.16044  ? 8   PHE B CB  1 
ATOM   2387 C CG  . PHE B 1 8   ? -8.94500  -2.96200  3.95000   1.000 46.00815  ? 8   PHE B CG  1 
ATOM   2388 C CD1 . PHE B 1 8   ? -9.10100  -3.82900  5.01600   1.000 45.68179  ? 8   PHE B CD1 1 
ATOM   2389 C CD2 . PHE B 1 8   ? -8.10800  -3.32200  2.90100   1.000 41.89713  ? 8   PHE B CD2 1 
ATOM   2390 C CE1 . PHE B 1 8   ? -8.46400  -5.04800  5.05200   1.000 47.40832  ? 8   PHE B CE1 1 
ATOM   2391 C CE2 . PHE B 1 8   ? -7.42700  -4.52700  2.91300   1.000 47.14249  ? 8   PHE B CE2 1 
ATOM   2392 C CZ  . PHE B 1 8   ? -7.60600  -5.40000  3.98900   1.000 50.41394  ? 8   PHE B CZ  1 
ATOM   2393 N N   . PRO B 1 9   ? -12.46000 -0.43200  4.98800   1.000 43.86315  ? 9   PRO B N   1 
ATOM   2394 C CA  . PRO B 1 9   ? -13.08400 0.82800   5.40400   1.000 44.06055  ? 9   PRO B CA  1 
ATOM   2395 C C   . PRO B 1 9   ? -12.02800 1.91400   5.33900   1.000 43.52627  ? 9   PRO B C   1 
ATOM   2396 O O   . PRO B 1 9   ? -10.86300 1.66900   5.66500   1.000 45.65811  ? 9   PRO B O   1 
ATOM   2397 C CB  . PRO B 1 9   ? -13.53400 0.56000   6.85100   1.000 45.00540  ? 9   PRO B CB  1 
ATOM   2398 C CG  . PRO B 1 9   ? -13.57300 -0.96900  6.99700   1.000 46.81614  ? 9   PRO B CG  1 
ATOM   2399 C CD  . PRO B 1 9   ? -12.36500 -1.39400  6.09700   1.000 41.32601  ? 9   PRO B CD  1 
ATOM   2400 N N   . SER B 1 10  ? -12.41600 3.08000   4.80700   1.000 42.75249  ? 10  SER B N   1 
ATOM   2401 C CA  . SER B 1 10  ? -11.44700 4.10000   4.36700   1.000 43.58944  ? 10  SER B CA  1 
ATOM   2402 C C   . SER B 1 10  ? -11.25800 5.23500   5.36000   1.000 43.36309  ? 10  SER B C   1 
ATOM   2403 O O   . SER B 1 10  ? -10.44000 6.13100   5.09800   1.000 45.17647  ? 10  SER B O   1 
ATOM   2404 C CB  . SER B 1 10  ? -11.89200 4.69100   3.02900   1.000 39.76793  ? 10  SER B CB  1 
ATOM   2405 O OG  . SER B 1 10  ? -13.17500 5.28600   3.20400   1.000 45.37649  ? 10  SER B OG  1 
ATOM   2406 N N   . GLY B 1 11  ? -11.98600 5.20700   6.49200   1.000 43.28677  ? 11  GLY B N   1 
ATOM   2407 C CA  . GLY B 1 11  ? -11.97000 6.31500   7.44200   1.000 43.85263  ? 11  GLY B CA  1 
ATOM   2408 C C   . GLY B 1 11  ? -10.57100 6.77200   7.83700   1.000 46.41083  ? 11  GLY B C   1 
ATOM   2409 O O   . GLY B 1 11  ? -10.29300 7.97200   7.87000   1.000 43.94211  ? 11  GLY B O   1 
ATOM   2410 N N   . LYS B 1 12  ? -9.69000  5.82200   8.17800   1.000 43.91053  ? 12  LYS B N   1 
ATOM   2411 C CA  . LYS B 1 12  ? -8.35400  6.16400   8.66300   1.000 46.97932  ? 12  LYS B CA  1 
ATOM   2412 C C   . LYS B 1 12  ? -7.52500  6.87300   7.60100   1.000 44.50534  ? 12  LYS B C   1 
ATOM   2413 O O   . LYS B 1 12  ? -6.62200  7.64700   7.94300   1.000 46.85562  ? 12  LYS B O   1 
ATOM   2414 C CB  . LYS B 1 12  ? -7.61300  4.90200   9.11400   1.000 48.64267  ? 12  LYS B CB  1 
ATOM   2415 C CG  . LYS B 1 12  ? -8.15000  4.26300   10.34900  1.000 53.94857  ? 12  LYS B CG  1 
ATOM   2416 C CD  . LYS B 1 12  ? -7.34800  3.00800   10.67500  1.000 59.80191  ? 12  LYS B CD  1 
ATOM   2417 C CE  . LYS B 1 12  ? -7.65000  2.53800   12.08600  1.000 69.38990  ? 12  LYS B CE  1 
ATOM   2418 N NZ  . LYS B 1 12  ? -9.11900  2.53400   12.30300  1.000 75.35377  ? 12  LYS B NZ  1 
ATOM   2419 N N   . VAL B 1 13  ? -7.81700  6.62800   6.32500   1.000 44.26847  ? 13  VAL B N   1 
ATOM   2420 C CA  . VAL B 1 13  ? -7.08300  7.27900   5.22500   1.000 44.28952  ? 13  VAL B CA  1 
ATOM   2421 C C   . VAL B 1 13  ? -7.71100  8.62900   4.85000   1.000 45.50282  ? 13  VAL B C   1 
ATOM   2422 O O   . VAL B 1 13  ? -6.98800  9.60000   4.57200   1.000 40.06796  ? 13  VAL B O   1 
ATOM   2423 C CB  . VAL B 1 13  ? -7.02000  6.31300   4.01800   1.000 38.55199  ? 13  VAL B CB  1 
ATOM   2424 C CG1 . VAL B 1 13  ? -6.27400  6.96300   2.75200   1.000 39.57843  ? 13  VAL B CG1 1 
ATOM   2425 C CG2 . VAL B 1 13  ? -6.27400  5.04600   4.47000   1.000 39.52842  ? 13  VAL B CG2 1 
ATOM   2426 N N   . GLU B 1 14  ? -9.04900  8.74700   4.93600   1.000 43.86315  ? 14  GLU B N   1 
ATOM   2427 C CA  . GLU B 1 14  ? -9.71500  10.00400  4.61300   1.000 39.24418  ? 14  GLU B CA  1 
ATOM   2428 C C   . GLU B 1 14  ? -9.16300  11.11900  5.45000   1.000 42.32876  ? 14  GLU B C   1 
ATOM   2429 O O   . GLU B 1 14  ? -9.07400  12.26600  4.98200   1.000 46.03447  ? 14  GLU B O   1 
ATOM   2430 C CB  . GLU B 1 14  ? -11.26100 9.90200   4.83000   1.000 40.12060  ? 14  GLU B CB  1 
ATOM   2431 C CG  . GLU B 1 14  ? -11.91400 8.84300   3.93400   1.000 37.46239  ? 14  GLU B CG  1 
ATOM   2432 C CD  . GLU B 1 14  ? -13.38000 8.56000   4.41400   1.000 44.85801  ? 14  GLU B CD  1 
ATOM   2433 O OE1 . GLU B 1 14  ? -14.08100 9.54100   4.77300   1.000 42.96831  ? 14  GLU B OE1 1 
ATOM   2434 O OE2 . GLU B 1 14  ? -13.75700 7.37300   4.49100   1.000 42.40245  ? 14  GLU B OE2 1 
ATOM   2435 N N   . GLY B 1 15  ? -8.79200  10.81900  6.69100   1.000 41.15493  ? 15  GLY B N   1 
ATOM   2436 C CA  . GLY B 1 15  ? -8.32900  11.87000  7.53500   1.000 43.49206  ? 15  GLY B CA  1 
ATOM   2437 C C   . GLY B 1 15  ? -6.93600  12.35600  7.21100   1.000 47.44779  ? 15  GLY B C   1 
ATOM   2438 O O   . GLY B 1 15  ? -6.51300  13.34900  7.79300   1.000 50.47974  ? 15  GLY B O   1 
ATOM   2439 N N   . CYS B 1 16  ? -6.25300  11.72700  6.25300   1.000 44.75273  ? 16  CYS B N   1 
ATOM   2440 C CA  . CYS B 1 16  ? -4.88600  12.07100  5.87000   1.000 44.71326  ? 16  CYS B CA  1 
ATOM   2441 C C   . CYS B 1 16  ? -4.80400  12.76400  4.53000   1.000 44.52639  ? 16  CYS B C   1 
ATOM   2442 O O   . CYS B 1 16  ? -3.69200  13.15100  4.11600   1.000 47.94785  ? 16  CYS B O   1 
ATOM   2443 C CB  . CYS B 1 16  ? -4.02400  10.80700  5.77400   1.000 44.28163  ? 16  CYS B CB  1 
ATOM   2444 S SG  . CYS B 1 16  ? -4.03300  9.90000   7.27600   1.000 49.44014  ? 16  CYS B SG  1 
ATOM   2445 N N   . MET B 1 17  ? -5.91800  12.88300  3.81300   1.000 44.60008  ? 17  MET B N   1 
ATOM   2446 C CA  . MET B 1 17  ? -5.89000  13.43000  2.47200   1.000 42.61564  ? 17  MET B CA  1 
ATOM   2447 C C   . MET B 1 17  ? -5.94700  14.93800  2.55100   1.000 45.20542  ? 17  MET B C   1 
ATOM   2448 O O   . MET B 1 17  ? -6.75200  15.51000  3.30200   1.000 43.98948  ? 17  MET B O   1 
ATOM   2449 C CB  . MET B 1 17  ? -7.04000  12.88400  1.60200   1.000 42.55510  ? 17  MET B CB  1 
ATOM   2450 C CG  . MET B 1 17  ? -7.04300  11.38200  1.43600   1.000 43.34993  ? 17  MET B CG  1 
ATOM   2451 S SD  . MET B 1 17  ? -5.44100  10.63300  1.03900   1.000 43.32625  ? 17  MET B SD  1 
ATOM   2452 C CE  . MET B 1 17  ? -5.05600  11.57500  -0.47200  1.000 40.14692  ? 17  MET B CE  1 
ATOM   2453 N N   . VAL B 1 18  ? -5.01600  15.58300  1.84500   1.000 44.72642  ? 18  VAL B N   1 
ATOM   2454 C CA  . VAL B 1 18  ? -4.95200  17.02500  1.72100   1.000 43.76314  ? 18  VAL B CA  1 
ATOM   2455 C C   . VAL B 1 18  ? -4.83100  17.38400  0.24700   1.000 40.50486  ? 18  VAL B C   1 
ATOM   2456 O O   . VAL B 1 18  ? -4.66600  16.53200  -0.61700  1.000 42.90778  ? 18  VAL B O   1 
ATOM   2457 C CB  . VAL B 1 18  ? -3.79700  17.64400  2.53900   1.000 47.60308  ? 18  VAL B CB  1 
ATOM   2458 C CG1 . VAL B 1 18  ? -4.04200  17.39900  4.03200   1.000 46.95037  ? 18  VAL B CG1 1 
ATOM   2459 C CG2 . VAL B 1 18  ? -2.43300  17.08800  2.07500   1.000 42.74723  ? 18  VAL B CG2 1 
ATOM   2460 N N   . GLN B 1 19  ? -4.99400  18.66000  -0.02700  1.000 45.58704  ? 19  GLN B N   1 
ATOM   2461 C CA  . GLN B 1 19  ? -4.87200  19.22400  -1.35400  1.000 46.62401  ? 19  GLN B CA  1 
ATOM   2462 C C   . GLN B 1 19  ? -3.55300  19.97600  -1.41100  1.000 46.37135  ? 19  GLN B C   1 
ATOM   2463 O O   . GLN B 1 19  ? -3.20900  20.66400  -0.45300  1.000 49.04009  ? 19  GLN B O   1 
ATOM   2464 C CB  . GLN B 1 19  ? -6.03000  20.17900  -1.64300  1.000 47.59781  ? 19  GLN B CB  1 
ATOM   2465 C CG  . GLN B 1 19  ? -6.00100  20.66500  -3.07900  1.000 51.74305  ? 19  GLN B CG  1 
ATOM   2466 C CD  . GLN B 1 19  ? -7.19700  21.58700  -3.43000  1.000 57.53585  ? 19  GLN B CD  1 
ATOM   2467 O OE1 . GLN B 1 19  ? -7.89100  22.10100  -2.55300  1.000 58.19908  ? 19  GLN B OE1 1 
ATOM   2468 N NE2 . GLN B 1 19  ? -7.41600  21.78800  -4.72400  1.000 59.64663  ? 19  GLN B NE2 1 
ATOM   2469 N N   . VAL B 1 20  ? -2.79500  19.79200  -2.49100  1.000 45.44229  ? 20  VAL B N   1 
ATOM   2470 C CA  . VAL B 1 20  ? -1.50000  20.45800  -2.67900  1.000 46.65296  ? 20  VAL B CA  1 
ATOM   2471 C C   . VAL B 1 20  ? -1.57800  21.18800  -3.99300  1.000 48.21104  ? 20  VAL B C   1 
ATOM   2472 O O   . VAL B 1 20  ? -1.88200  20.57200  -5.02200  1.000 45.12910  ? 20  VAL B O   1 
ATOM   2473 C CB  . VAL B 1 20  ? -0.31800  19.47400  -2.70400  1.000 44.48691  ? 20  VAL B CB  1 
ATOM   2474 C CG1 . VAL B 1 20  ? 1.00500   20.25700  -2.90100  1.000 45.52388  ? 20  VAL B CG1 1 
ATOM   2475 C CG2 . VAL B 1 20  ? -0.27300  18.64800  -1.45800  1.000 46.71086  ? 20  VAL B CG2 1 
ATOM   2476 N N   . THR B 1 21  ? -1.26900  22.48200  -3.97100  1.000 52.17204  ? 21  THR B N   1 
ATOM   2477 C CA  . THR B 1 21  ? -1.33000  23.31200  -5.16500  1.000 53.88541  ? 21  THR B CA  1 
ATOM   2478 C C   . THR B 1 21  ? -0.02600  24.06800  -5.35900  1.000 54.03279  ? 21  THR B C   1 
ATOM   2479 O O   . THR B 1 21  ? 0.50900   24.63900  -4.40800  1.000 56.91735  ? 21  THR B O   1 
ATOM   2480 C CB  . THR B 1 21  ? -2.47500  24.31700  -5.09400  1.000 57.21212  ? 21  THR B CB  1 
ATOM   2481 O OG1 . THR B 1 21  ? -3.69700  23.61500  -4.78900  1.000 57.08316  ? 21  THR B OG1 1 
ATOM   2482 C CG2 . THR B 1 21  ? -2.61900  25.03600  -6.41900  1.000 58.22277  ? 21  THR B CG2 1 
ATOM   2483 N N   . CYS B 1 22  ? 0.44200   24.08500  -6.60700  1.000 50.40604  ? 22  CYS B N   1 
ATOM   2484 C CA  . CYS B 1 22  ? 1.64100   24.85800  -6.99700  1.000 54.65129  ? 22  CYS B CA  1 
ATOM   2485 C C   . CYS B 1 22  ? 1.25800   25.61500  -8.26500  1.000 58.47280  ? 22  CYS B C   1 
ATOM   2486 O O   . CYS B 1 22  ? 1.11000   24.97400  -9.30800  1.000 54.76972  ? 22  CYS B O   1 
ATOM   2487 C CB  . CYS B 1 22  ? 2.81800   23.95600  -7.32100  1.000 59.60978  ? 22  CYS B CB  1 
ATOM   2488 S SG  . CYS B 1 22  ? 3.63000   23.30400  -5.85200  1.000 64.88410  ? 22  CYS B SG  1 
ATOM   2489 N N   . GLY B 1 23  ? 1.08500   26.93100  -8.16300  1.000 60.89941  ? 23  GLY B N   1 
ATOM   2490 C CA  . GLY B 1 23  ? 0.63000   27.71400  -9.29400  1.000 58.50175  ? 23  GLY B CA  1 
ATOM   2491 C C   . GLY B 1 23  ? -0.79100  27.32300  -9.62300  1.000 58.29120  ? 23  GLY B C   1 
ATOM   2492 O O   . GLY B 1 23  ? -1.65200  27.31600  -8.74700  1.000 59.71242  ? 23  GLY B O   1 
ATOM   2493 N N   . THR B 1 24  ? -1.02300  26.88400  -10.85500 1.000 60.32039  ? 24  THR B N   1 
ATOM   2494 C CA  . THR B 1 24  ? -2.31900  26.37000  -11.27000 1.000 60.27565  ? 24  THR B CA  1 
ATOM   2495 C C   . THR B 1 24  ? -2.39300  24.84500  -11.22500 1.000 59.37554  ? 24  THR B C   1 
ATOM   2496 O O   . THR B 1 24  ? -3.43300  24.28700  -11.58000 1.000 65.02095  ? 24  THR B O   1 
ATOM   2497 C CB  . THR B 1 24  ? -2.63800  26.82700  -12.68500 1.000 61.42579  ? 24  THR B CB  1 
ATOM   2498 O OG1 . THR B 1 24  ? -1.51400  26.50100  -13.52600 1.000 65.80526  ? 24  THR B OG1 1 
ATOM   2499 C CG2 . THR B 1 24  ? -2.90700  28.34900  -12.71600 1.000 61.38631  ? 24  THR B CG2 1 
ATOM   2500 N N   . THR B 1 25  ? -1.34000  24.16200  -10.79300 1.000 53.29586  ? 25  THR B N   1 
ATOM   2501 C CA  . THR B 1 25  ? -1.36000  22.69800  -10.73600 1.000 52.88529  ? 25  THR B CA  1 
ATOM   2502 C C   . THR B 1 25  ? -1.78600  22.23300  -9.36300  1.000 50.07442  ? 25  THR B C   1 
ATOM   2503 O O   . THR B 1 25  ? -1.21200  22.66800  -8.36000  1.000 53.68802  ? 25  THR B O   1 
ATOM   2504 C CB  . THR B 1 25  ? 0.01000   22.11500  -11.06400 1.000 53.79329  ? 25  THR B CB  1 
ATOM   2505 O OG1 . THR B 1 25  ? 0.41400   22.62500  -12.32700 1.000 56.76733  ? 25  THR B OG1 1 
ATOM   2506 C CG2 . THR B 1 25  ? -0.09000  20.57300  -11.14300 1.000 49.91388  ? 25  THR B CG2 1 
ATOM   2507 N N   . THR B 1 26  ? -2.78700  21.35300  -9.31400  1.000 46.94773  ? 26  THR B N   1 
ATOM   2508 C CA  . THR B 1 26  ? -3.22900  20.85000  -8.04100  1.000 49.15853  ? 26  THR B CA  1 
ATOM   2509 C C   . THR B 1 26  ? -3.35100  19.32200  -8.06900  1.000 46.97405  ? 26  THR B C   1 
ATOM   2510 O O   . THR B 1 26  ? -3.58900  18.71300  -9.11100  1.000 44.98434  ? 26  THR B O   1 
ATOM   2511 C CB  . THR B 1 26  ? -4.56700  21.51100  -7.68500  1.000 53.11953  ? 26  THR B CB  1 
ATOM   2512 O OG1 . THR B 1 26  ? -4.84500  21.26900  -6.31700  1.000 53.49589  ? 26  THR B OG1 1 
ATOM   2513 C CG2 . THR B 1 26  ? -5.67300  20.91800  -8.54600  1.000 54.41179  ? 26  THR B CG2 1 
ATOM   2514 N N   . LEU B 1 27  ? -3.16500  18.70500  -6.91400  1.000 42.17348  ? 27  LEU B N   1 
ATOM   2515 C CA  . LEU B 1 27  ? -3.40500  17.28700  -6.77600  1.000 42.96305  ? 27  LEU B CA  1 
ATOM   2516 C C   . LEU B 1 27  ? -3.57800  16.98200  -5.28500  1.000 42.16821  ? 27  LEU B C   1 
ATOM   2517 O O   . LEU B 1 27  ? -3.71900  17.89300  -4.45500  1.000 40.97597  ? 27  LEU B O   1 
ATOM   2518 C CB  . LEU B 1 27  ? -2.28700  16.46900  -7.44000  1.000 40.02585  ? 27  LEU B CB  1 
ATOM   2519 C CG  . LEU B 1 27  ? -0.83100  16.87500  -7.28300  1.000 41.78659  ? 27  LEU B CG  1 
ATOM   2520 C CD1 . LEU B 1 27  ? -0.40700  16.91800  -5.81200  1.000 40.84963  ? 27  LEU B CD1 1 
ATOM   2521 C CD2 . LEU B 1 27  ? 0.04200   15.83100  -8.06800  1.000 40.05743  ? 27  LEU B CD2 1 
ATOM   2522 N N   . ASN B 1 28  ? -3.54500  15.68000  -4.94400  1.000 39.10995  ? 28  ASN B N   1 
ATOM   2523 C CA  . ASN B 1 28  ? -3.75300  15.23800  -3.58200  1.000 39.86794  ? 28  ASN B CA  1 
ATOM   2524 C C   . ASN B 1 28  ? -2.45100  14.91000  -2.91000  1.000 39.82583  ? 28  ASN B C   1 
ATOM   2525 O O   . ASN B 1 28  ? -1.48100  14.47400  -3.55500  1.000 38.08088  ? 28  ASN B O   1 
ATOM   2526 C CB  . ASN B 1 28  ? -4.67000  14.00200  -3.55400  1.000 37.64662  ? 28  ASN B CB  1 
ATOM   2527 C CG  . ASN B 1 28  ? -5.92000  14.25400  -4.31700  1.000 42.03399  ? 28  ASN B CG  1 
ATOM   2528 O OD1 . ASN B 1 28  ? -6.82300  14.91500  -3.80000  1.000 40.98386  ? 28  ASN B OD1 1 
ATOM   2529 N ND2 . ASN B 1 28  ? -5.99900  13.75200  -5.56600  1.000 37.07287  ? 28  ASN B ND2 1 
ATOM   2530 N N   . GLY B 1 29  ? -2.44000  15.12100  -1.59600  1.000 39.24155  ? 29  GLY B N   1 
ATOM   2531 C CA  . GLY B 1 29  ? -1.31000  14.73000  -0.78900  1.000 42.59195  ? 29  GLY B CA  1 
ATOM   2532 C C   . GLY B 1 29  ? -1.74800  13.88000  0.38100   1.000 42.34192  ? 29  GLY B C   1 
ATOM   2533 O O   . GLY B 1 29  ? -2.92900  13.84600  0.75600   1.000 40.90227  ? 29  GLY B O   1 
ATOM   2534 N N   . LEU B 1 30  ? -0.77500  13.19500  0.96600   1.000 44.27110  ? 30  LEU B N   1 
ATOM   2535 C CA  . LEU B 1 30  ? -1.01800  12.31200  2.11000   1.000 44.81590  ? 30  LEU B CA  1 
ATOM   2536 C C   . LEU B 1 30  ? -0.29700  12.90700  3.32500   1.000 45.56862  ? 30  LEU B C   1 
ATOM   2537 O O   . LEU B 1 30  ? 0.93500   13.02500  3.31600   1.000 41.08387  ? 30  LEU B O   1 
ATOM   2538 C CB  . LEU B 1 30  ? -0.52400  10.88900  1.78300   1.000 41.72079  ? 30  LEU B CB  1 
ATOM   2539 C CG  . LEU B 1 30  ? -0.76100  9.87000   2.88300   1.000 43.91053  ? 30  LEU B CG  1 
ATOM   2540 C CD1 . LEU B 1 30  ? -2.29100  9.52200   2.96300   1.000 40.03638  ? 30  LEU B CD1 1 
ATOM   2541 C CD2 . LEU B 1 30  ? 0.10500   8.60200   2.76500   1.000 40.13902  ? 30  LEU B CD2 1 
ATOM   2542 N N   . TRP B 1 31  ? -1.06400  13.24900  4.37700   1.000 43.88684  ? 31  TRP B N   1 
ATOM   2543 C CA  . TRP B 1 31  ? -0.57500  14.01800  5.53000   1.000 46.20291  ? 31  TRP B CA  1 
ATOM   2544 C C   . TRP B 1 31  ? -0.37300  13.06000  6.70100   1.000 48.85586  ? 31  TRP B C   1 
ATOM   2545 O O   . TRP B 1 31  ? -1.34300  12.62100  7.33100   1.000 46.96879  ? 31  TRP B O   1 
ATOM   2546 C CB  . TRP B 1 31  ? -1.57500  15.10900  5.89200   1.000 45.43703  ? 31  TRP B CB  1 
ATOM   2547 C CG  . TRP B 1 31  ? -1.24300  16.05300  7.02700   1.000 47.35831  ? 31  TRP B CG  1 
ATOM   2548 C CD1 . TRP B 1 31  ? -0.00000  16.38800  7.52600   1.000 48.06366  ? 31  TRP B CD1 1 
ATOM   2549 C CD2 . TRP B 1 31  ? -2.19300  16.81300  7.78800   1.000 51.83779  ? 31  TRP B CD2 1 
ATOM   2550 N NE1 . TRP B 1 31  ? -0.14400  17.29400  8.55300   1.000 49.85071  ? 31  TRP B NE1 1 
ATOM   2551 C CE2 . TRP B 1 31  ? -1.47500  17.56000  8.73900   1.000 53.07478  ? 31  TRP B CE2 1 
ATOM   2552 C CE3 . TRP B 1 31  ? -3.60800  16.90200  7.77200   1.000 51.81674  ? 31  TRP B CE3 1 
ATOM   2553 C CZ2 . TRP B 1 31  ? -2.10300  18.42200  9.65700   1.000 55.01186  ? 31  TRP B CZ2 1 
ATOM   2554 C CZ3 . TRP B 1 31  ? -4.22700  17.76100  8.67700   1.000 54.55391  ? 31  TRP B CZ3 1 
ATOM   2555 C CH2 . TRP B 1 31  ? -3.47400  18.49800  9.61700   1.000 55.78037  ? 31  TRP B CH2 1 
ATOM   2556 N N   . LEU B 1 32  ? 0.88500   12.73300  7.00600   1.000 47.73467  ? 32  LEU B N   1 
ATOM   2557 C CA  . LEU B 1 32  ? 1.17200   11.82900  8.11700   1.000 48.19525  ? 32  LEU B CA  1 
ATOM   2558 C C   . LEU B 1 32  ? 2.14100   12.52300  9.06500   1.000 52.50103  ? 32  LEU B C   1 
ATOM   2559 O O   . LEU B 1 32  ? 3.24300   12.91700  8.65500   1.000 48.49529  ? 32  LEU B O   1 
ATOM   2560 C CB  . LEU B 1 32  ? 1.73600   10.50300  7.60800   1.000 46.66349  ? 32  LEU B CB  1 
ATOM   2561 C CG  . LEU B 1 32  ? 0.90400   9.67800   6.63700   1.000 44.16056  ? 32  LEU B CG  1 
ATOM   2562 C CD1 . LEU B 1 32  ? 1.64200   8.45400   6.06200   1.000 45.45808  ? 32  LEU B CD1 1 
ATOM   2563 C CD2 . LEU B 1 32  ? -0.45000  9.20900   7.31800   1.000 41.25758  ? 32  LEU B CD2 1 
ATOM   2564 N N   . ASP B 1 33  ? 1.74700   12.65600  10.33600  1.000 47.96891  ? 33  ASP B N   1 
ATOM   2565 C CA  . ASP B 1 33  ? 2.51000   13.45900  11.31300  1.000 50.74556  ? 33  ASP B CA  1 
ATOM   2566 C C   . ASP B 1 33  ? 2.66200   14.84800  10.68900  1.000 52.57999  ? 33  ASP B C   1 
ATOM   2567 O O   . ASP B 1 33  ? 1.66300   15.39300  10.20200  1.000 51.85885  ? 33  ASP B O   1 
ATOM   2568 C CB  . ASP B 1 33  ? 3.82200   12.75000  11.69900  1.000 56.12252  ? 33  ASP B CB  1 
ATOM   2569 C CG  . ASP B 1 33  ? 3.56800   11.36600  12.31100  1.000 61.43631  ? 33  ASP B CG  1 
ATOM   2570 O OD1 . ASP B 1 33  ? 2.66400   11.27500  13.16400  1.000 59.93087  ? 33  ASP B OD1 1 
ATOM   2571 O OD2 . ASP B 1 33  ? 4.24800   10.37200  11.93000  1.000 68.06342  ? 33  ASP B OD2 1 
ATOM   2572 N N   . ASP B 1 34  ? 3.87500   15.42900  10.61700  1.000 52.14046  ? 34  ASP B N   1 
ATOM   2573 C CA  . ASP B 1 34  ? 4.04100   16.77300  10.06700  1.000 53.24059  ? 34  ASP B CA  1 
ATOM   2574 C C   . ASP B 1 34  ? 4.65100   16.77200  8.65000   1.000 53.53273  ? 34  ASP B C   1 
ATOM   2575 O O   . ASP B 1 34  ? 5.39100   17.70400  8.28900   1.000 55.65931  ? 34  ASP B O   1 
ATOM   2576 C CB  . ASP B 1 34  ? 4.91700   17.63800  10.99100  1.000 56.07251  ? 34  ASP B CB  1 
ATOM   2577 C CG  . ASP B 1 34  ? 6.34400   17.10100  11.14200  1.000 59.49134  ? 34  ASP B CG  1 
ATOM   2578 O OD1 . ASP B 1 34  ? 6.64900   15.95700  10.72800  1.000 62.22325  ? 34  ASP B OD1 1 
ATOM   2579 O OD2 . ASP B 1 34  ? 7.20800   17.86600  11.63200  1.000 63.33917  ? 34  ASP B OD2 1 
ATOM   2580 N N   . VAL B 1 35  ? 4.39600   15.73900  7.86000   1.000 52.00887  ? 35  VAL B N   1 
ATOM   2581 C CA  . VAL B 1 35  ? 4.90900   15.61600  6.49500   1.000 50.48763  ? 35  VAL B CA  1 
ATOM   2582 C C   . VAL B 1 35  ? 3.73500   15.34200  5.57800   1.000 51.03243  ? 35  VAL B C   1 
ATOM   2583 O O   . VAL B 1 35  ? 2.86900   14.51400  5.89800   1.000 45.40018  ? 35  VAL B O   1 
ATOM   2584 C CB  . VAL B 1 35  ? 5.94300   14.47700  6.36900   1.000 49.66122  ? 35  VAL B CB  1 
ATOM   2585 C CG1 . VAL B 1 35  ? 6.45500   14.39900  4.95500   1.000 49.75333  ? 35  VAL B CG1 1 
ATOM   2586 C CG2 . VAL B 1 35  ? 7.09200   14.69600  7.32600   1.000 51.66409  ? 35  VAL B CG2 1 
ATOM   2587 N N   . VAL B 1 36  ? 3.69100   16.03400  4.44300   1.000 48.42160  ? 36  VAL B N   1 
ATOM   2588 C CA  . VAL B 1 36  ? 2.70700   15.76300  3.39300   1.000 46.23712  ? 36  VAL B CA  1 
ATOM   2589 C C   . VAL B 1 36  ? 3.45200   15.14700  2.22200   1.000 48.29000  ? 36  VAL B C   1 
ATOM   2590 O O   . VAL B 1 36  ? 4.45600   15.70300  1.78100   1.000 42.26559  ? 36  VAL B O   1 
ATOM   2591 C CB  . VAL B 1 36  ? 1.97100   17.05100  2.98600   1.000 45.65811  ? 36  VAL B CB  1 
ATOM   2592 C CG1 . VAL B 1 36  ? 1.15600   16.86300  1.68600   1.000 43.68682  ? 36  VAL B CG1 1 
ATOM   2593 C CG2 . VAL B 1 36  ? 1.10300   17.53900  4.17900   1.000 44.87907  ? 36  VAL B CG2 1 
ATOM   2594 N N   . TYR B 1 37  ? 3.00100   13.97800  1.75400   1.000 40.72330  ? 37  TYR B N   1 
ATOM   2595 C CA  . TYR B 1 37  ? 3.62800   13.26000  0.64500   1.000 43.47890  ? 37  TYR B CA  1 
ATOM   2596 C C   . TYR B 1 37  ? 2.77400   13.47900  -0.59000  1.000 43.79999  ? 37  TYR B C   1 
ATOM   2597 O O   . TYR B 1 37  ? 1.56900   13.31400  -0.51300  1.000 42.78145  ? 37  TYR B O   1 
ATOM   2598 C CB  . TYR B 1 37  ? 3.71900   11.74300  0.93200   1.000 44.25004  ? 37  TYR B CB  1 
ATOM   2599 C CG  . TYR B 1 37  ? 4.50600   11.41000  2.18100   1.000 44.53692  ? 37  TYR B CG  1 
ATOM   2600 C CD1 . TYR B 1 37  ? 3.96500   11.56800  3.44900   1.000 44.19740  ? 37  TYR B CD1 1 
ATOM   2601 C CD2 . TYR B 1 37  ? 5.85500   11.04000  2.08500   1.000 47.90574  ? 37  TYR B CD2 1 
ATOM   2602 C CE1 . TYR B 1 37  ? 4.71500   11.30600  4.57900   1.000 43.47890  ? 37  TYR B CE1 1 
ATOM   2603 C CE2 . TYR B 1 37  ? 6.61400   10.77300  3.20000   1.000 48.27158  ? 37  TYR B CE2 1 
ATOM   2604 C CZ  . TYR B 1 37  ? 6.03900   10.88400  4.43000   1.000 49.65069  ? 37  TYR B CZ  1 
ATOM   2605 O OH  . TYR B 1 37  ? 6.81800   10.63500  5.50800   1.000 49.89019  ? 37  TYR B OH  1 
ATOM   2606 N N   . CYS B 1 38  ? 3.38000   13.82500  -1.72300  1.000 40.68646  ? 38  CYS B N   1 
ATOM   2607 C CA  . CYS B 1 38  ? 2.57300   14.00000  -2.92300  1.000 40.34694  ? 38  CYS B CA  1 
ATOM   2608 C C   . CYS B 1 38  ? 3.44800   13.75500  -4.14700  1.000 39.21786  ? 38  CYS B C   1 
ATOM   2609 O O   . CYS B 1 38  ? 4.68200   13.75600  -4.03900  1.000 39.03100  ? 38  CYS B O   1 
ATOM   2610 C CB  . CYS B 1 38  ? 1.93900   15.40300  -2.96000  1.000 39.30208  ? 38  CYS B CB  1 
ATOM   2611 S SG  . CYS B 1 38  ? 3.08000   16.74100  -3.29500  1.000 41.32864  ? 38  CYS B SG  1 
ATOM   2612 N N   . PRO B 1 39  ? 2.85400   13.51300  -5.31700  1.000 38.42829  ? 39  PRO B N   1 
ATOM   2613 C CA  . PRO B 1 39  ? 3.70600   13.33400  -6.51300  1.000 38.84939  ? 39  PRO B CA  1 
ATOM   2614 C C   . PRO B 1 39  ? 4.45300   14.59800  -6.87100  1.000 39.69160  ? 39  PRO B C   1 
ATOM   2615 O O   . PRO B 1 39  ? 3.91900   15.71900  -6.82200  1.000 37.79927  ? 39  PRO B O   1 
ATOM   2616 C CB  . PRO B 1 39  ? 2.71700   12.96500  -7.62200  1.000 32.20912  ? 39  PRO B CB  1 
ATOM   2617 C CG  . PRO B 1 39  ? 1.47000   12.32200  -6.80600  1.000 35.46478  ? 39  PRO B CG  1 
ATOM   2618 C CD  . PRO B 1 39  ? 1.42200   13.22400  -5.58000  1.000 39.06521  ? 39  PRO B CD  1 
ATOM   2619 N N   . ARG B 1 40  ? 5.70900   14.42100  -7.29300  1.000 39.04942  ? 40  ARG B N   1 
ATOM   2620 C CA  . ARG B 1 40  ? 6.42700   15.61000  -7.69700  1.000 38.60200  ? 40  ARG B CA  1 
ATOM   2621 C C   . ARG B 1 40  ? 5.83700   16.24900  -8.94800  1.000 40.28378  ? 40  ARG B C   1 
ATOM   2622 O O   . ARG B 1 40  ? 6.16100   17.40400  -9.25200  1.000 44.32637  ? 40  ARG B O   1 
ATOM   2623 C CB  . ARG B 1 40  ? 7.91100   15.28100  -7.88500  1.000 38.72570  ? 40  ARG B CB  1 
ATOM   2624 C CG  . ARG B 1 40  ? 8.13800   14.29600  -9.01400  1.000 38.67832  ? 40  ARG B CG  1 
ATOM   2625 C CD  . ARG B 1 40  ? 9.66400   14.03000  -9.15900  1.000 36.79652  ? 40  ARG B CD  1 
ATOM   2626 N NE  . ARG B 1 40  ? 9.93200   13.06400  -10.22700 1.000 35.91746  ? 40  ARG B NE  1 
ATOM   2627 C CZ  . ARG B 1 40  ? 11.16000  12.74800  -10.61900 1.000 43.77630  ? 40  ARG B CZ  1 
ATOM   2628 N NH1 . ARG B 1 40  ? 12.23400  13.28400  -10.02500 1.000 42.15242  ? 40  ARG B NH1 1 
ATOM   2629 N NH2 . ARG B 1 40  ? 11.32300  11.90700  -11.64800 1.000 38.41250  ? 40  ARG B NH2 1 
ATOM   2630 N N   . ALA B 1 41  ? 4.93800   15.56900  -9.63900  1.000 41.68395  ? 41  ALA B N   1 
ATOM   2631 C CA  . ALA B 1 41  ? 4.28900   16.17600  -10.79800 1.000 44.64219  ? 41  ALA B CA  1 
ATOM   2632 C C   . ALA B 1 41  ? 3.58700   17.49300  -10.47200 1.000 44.88170  ? 41  ALA B C   1 
ATOM   2633 O O   . ALA B 1 41  ? 3.33300   18.28200  -11.38900 1.000 43.56049  ? 41  ALA B O   1 
ATOM   2634 C CB  . ALA B 1 41  ? 3.27000   15.18400  -11.37500 1.000 41.81291  ? 41  ALA B CB  1 
ATOM   2635 N N   . VAL B 1 42  ? 3.29900   17.76300  -9.19300  1.000 42.71565  ? 42  VAL B N   1 
ATOM   2636 C CA  . VAL B 1 42  ? 2.64300   19.01800  -8.82500  1.000 43.14201  ? 42  VAL B CA  1 
ATOM   2637 C C   . VAL B 1 42  ? 3.53300   20.21200  -9.11300  1.000 48.68215  ? 42  VAL B C   1 
ATOM   2638 O O   . VAL B 1 42  ? 3.02200   21.31500  -9.26500  1.000 44.68430  ? 42  VAL B O   1 
ATOM   2639 C CB  . VAL B 1 42  ? 2.26900   19.01200  -7.34600  1.000 40.84174  ? 42  VAL B CB  1 
ATOM   2640 C CG1 . VAL B 1 42  ? 3.53300   19.15800  -6.46800  1.000 44.07634  ? 42  VAL B CG1 1 
ATOM   2641 C CG2 . VAL B 1 42  ? 1.12200   20.03200  -7.03900  1.000 46.23186  ? 42  VAL B CG2 1 
ATOM   2642 N N   . ILE B 1 43  ? 4.87000   20.04500  -9.14500  1.000 45.60284  ? 43  ILE B N   1 
ATOM   2643 C CA  . ILE B 1 43  ? 5.73300   21.18800  -9.46900  1.000 50.69029  ? 43  ILE B CA  1 
ATOM   2644 C C   . ILE B 1 43  ? 5.97800   21.33100  -10.96700 1.000 51.34037  ? 43  ILE B C   1 
ATOM   2645 O O   . ILE B 1 43  ? 6.71000   22.23100  -11.38700 1.000 56.56731  ? 43  ILE B O   1 
ATOM   2646 C CB  . ILE B 1 43  ? 7.08000   21.16400  -8.73200  1.000 49.52436  ? 43  ILE B CB  1 
ATOM   2647 C CG1 . ILE B 1 43  ? 8.01700   20.07900  -9.28200  1.000 47.41884  ? 43  ILE B CG1 1 
ATOM   2648 C CG2 . ILE B 1 43  ? 6.77100   21.02800  -7.23200  1.000 51.11139  ? 43  ILE B CG2 1 
ATOM   2649 C CD1 . ILE B 1 43  ? 9.43400   20.06300  -8.60700  1.000 47.60834  ? 43  ILE B CD1 1 
ATOM   2650 N N   . CYS B 1 44  ? 5.32300   20.49800  -11.75800 1.000 52.21152  ? 44  CYS B N   1 
ATOM   2651 C CA  . CYS B 1 44  ? 5.47200   20.56800  -13.22900 1.000 53.72486  ? 44  CYS B CA  1 
ATOM   2652 C C   . CYS B 1 44  ? 4.60000   21.70500  -13.75300 1.000 61.79951  ? 44  CYS B C   1 
ATOM   2653 O O   . CYS B 1 44  ? 3.50500   21.90600  -13.21500 1.000 62.01270  ? 44  CYS B O   1 
ATOM   2654 C CB  . CYS B 1 44  ? 5.03600   19.26000  -13.87300 1.000 56.95946  ? 44  CYS B CB  1 
ATOM   2655 S SG  . CYS B 1 44  ? 6.11800   18.63800  -15.18000 1.000 68.17923  ? 44  CYS B SG  1 
ATOM   2656 N N   . THR B 1 45  ? 5.09000   22.43200  -14.75300 1.000 71.91389  ? 45  THR B N   1 
ATOM   2657 C CA  . THR B 1 45  ? 4.28800   23.47300  -15.36300 1.000 75.63538  ? 45  THR B CA  1 
ATOM   2658 C C   . THR B 1 45  ? 3.56600   22.89700  -16.56000 1.000 78.64364  ? 45  THR B C   1 
ATOM   2659 O O   . THR B 1 45  ? 4.02500   21.93200  -17.17500 1.000 73.98255  ? 45  THR B O   1 
ATOM   2660 C CB  . THR B 1 45  ? 5.14500   24.66700  -15.78400 1.000 74.93530  ? 45  THR B CB  1 
ATOM   2661 O OG1 . THR B 1 45  ? 6.54800   24.30000  -15.79500 1.000 76.65393  ? 45  THR B OG1 1 
ATOM   2662 C CG2 . THR B 1 45  ? 4.88100   25.77600  -14.80200 1.000 73.31669  ? 45  THR B CG2 1 
ATOM   2663 N N   . SER B 1 46  ? 2.44400   23.52900  -16.89700 1.000 82.53884  ? 46  SER B N   1 
ATOM   2664 C CA  . SER B 1 46  ? 1.60900   23.04800  -17.98700 1.000 91.73731  ? 46  SER B CA  1 
ATOM   2665 C C   . SER B 1 46  ? 2.32800   23.01400  -19.32300 1.000 92.89272  ? 46  SER B C   1 
ATOM   2666 O O   . SER B 1 46  ? 1.98800   22.17500  -20.16400 1.000 94.71662  ? 46  SER B O   1 
ATOM   2667 C CB  . SER B 1 46  ? 0.35400   23.91600  -18.09800 1.000 95.38249  ? 46  SER B CB  1 
ATOM   2668 O OG  . SER B 1 46  ? -0.31700  24.00100  -16.84900 1.000 93.09274  ? 46  SER B OG  1 
ATOM   2669 N N   . GLU B 1 47  ? 3.36100   23.83900  -19.51600 1.000 94.14813  ? 47  GLU B N   1 
ATOM   2670 C CA  . GLU B 1 47  ? 4.03300   23.85500  -20.80900 1.000 94.79558  ? 47  GLU B CA  1 
ATOM   2671 C C   . GLU B 1 47  ? 5.17400   22.85200  -20.89200 1.000 93.96127  ? 47  GLU B C   1 
ATOM   2672 O O   . GLU B 1 47  ? 5.46900   22.36900  -21.99100 1.000 98.06439  ? 47  GLU B O   1 
ATOM   2673 C CB  . GLU B 1 47  ? 4.53800   25.26500  -21.14400 1.000 98.89080  ? 47  GLU B CB  1 
ATOM   2674 C CG  . GLU B 1 47  ? 5.04200   26.09200  -19.96600 1.000 101.25425 ? 47  GLU B CG  1 
ATOM   2675 C CD  . GLU B 1 47  ? 3.91700   26.78900  -19.21200 1.000 103.02551 ? 47  GLU B CD  1 
ATOM   2676 O OE1 . GLU B 1 47  ? 2.73700   26.49400  -19.51400 1.000 105.67320 ? 47  GLU B OE1 1 
ATOM   2677 O OE2 . GLU B 1 47  ? 4.21000   27.62300  -18.31900 1.000 102.01223 ? 47  GLU B OE2 1 
ATOM   2678 N N   . ASP B 1 48  ? 5.82900   22.52300  -19.77300 1.000 86.71303  ? 48  ASP B N   1 
ATOM   2679 C CA  . ASP B 1 48  ? 6.90200   21.53200  -19.81400 1.000 83.59687  ? 48  ASP B CA  1 
ATOM   2680 C C   . ASP B 1 48  ? 6.56600   20.22500  -19.06400 1.000 72.05074  ? 48  ASP B C   1 
ATOM   2681 O O   . ASP B 1 48  ? 7.30400   19.81600  -18.16200 1.000 66.83433  ? 48  ASP B O   1 
ATOM   2682 C CB  . ASP B 1 48  ? 8.20900   22.16600  -19.29200 1.000 90.30556  ? 48  ASP B CB  1 
ATOM   2683 C CG  . ASP B 1 48  ? 8.68800   23.37300  -20.14400 1.000 104.63886 ? 48  ASP B CG  1 
ATOM   2684 O OD1 . ASP B 1 48  ? 9.13600   23.17300  -21.30100 1.000 111.11069 ? 48  ASP B OD1 1 
ATOM   2685 O OD2 . ASP B 1 48  ? 8.60800   24.53500  -19.66100 1.000 107.98400 ? 48  ASP B OD2 1 
ATOM   2686 N N   . MET B 1 49  ? 5.49600   19.51400  -19.46000 1.000 72.09285  ? 49  MET B N   1 
ATOM   2687 C CA  . MET B 1 49  ? 5.10100   18.23700  -18.84300 1.000 60.13353  ? 49  MET B CA  1 
ATOM   2688 C C   . MET B 1 49  ? 5.72500   17.04500  -19.56500 1.000 55.74353  ? 49  MET B C   1 
ATOM   2689 O O   . MET B 1 49  ? 5.61600   15.89400  -19.10100 1.000 50.42183  ? 49  MET B O   1 
ATOM   2690 C CB  . MET B 1 49  ? 3.55900   18.12300  -18.84100 1.000 62.50749  ? 49  MET B CB  1 
ATOM   2691 C CG  . MET B 1 49  ? 2.87600   19.15200  -17.90600 1.000 64.51563  ? 49  MET B CG  1 
ATOM   2692 S SD  . MET B 1 49  ? 1.12700   18.95400  -17.53400 1.000 74.75896  ? 49  MET B SD  1 
ATOM   2693 C CE  . MET B 1 49  ? 1.15900   17.49500  -16.53000 1.000 55.23820  ? 49  MET B CE  1 
ATOM   2694 N N   . LEU B 1 50  ? 6.35400   17.30700  -20.71500 1.000 55.14345  ? 50  LEU B N   1 
ATOM   2695 C CA  . LEU B 1 50  ? 6.98600   16.29300  -21.53200 1.000 52.83265  ? 50  LEU B CA  1 
ATOM   2696 C C   . LEU B 1 50  ? 8.39000   15.94600  -21.02700 1.000 55.14609  ? 50  LEU B C   1 
ATOM   2697 O O   . LEU B 1 50  ? 8.72000   14.75800  -20.86900 1.000 52.80107  ? 50  LEU B O   1 
ATOM   2698 C CB  . LEU B 1 50  ? 7.02900   16.77800  -22.98600 1.000 60.36250  ? 50  LEU B CB  1 
ATOM   2699 C CG  . LEU B 1 50  ? 7.64700   15.84300  -24.02900 1.000 59.19131  ? 50  LEU B CG  1 
ATOM   2700 C CD1 . LEU B 1 50  ? 6.67300   14.64000  -24.19800 1.000 57.94379  ? 50  LEU B CD1 1 
ATOM   2701 C CD2 . LEU B 1 50  ? 7.92900   16.55800  -25.34700 1.000 57.98064  ? 50  LEU B CD2 1 
ATOM   2702 N N   . ASN B 1 51  ? 9.22800   16.95400  -20.71400 1.000 54.34073  ? 51  ASN B N   1 
ATOM   2703 C CA  . ASN B 1 51  ? 10.61500  16.69000  -20.31900 1.000 52.11941  ? 51  ASN B CA  1 
ATOM   2704 C C   . ASN B 1 51  ? 10.95700  17.51000  -19.09800 1.000 50.19023  ? 51  ASN B C   1 
ATOM   2705 O O   . ASN B 1 51  ? 11.89500  18.31600  -19.09800 1.000 55.67246  ? 51  ASN B O   1 
ATOM   2706 C CB  . ASN B 1 51  ? 11.57300  16.99800  -21.48000 1.000 56.48572  ? 51  ASN B CB  1 
ATOM   2707 C CG  . ASN B 1 51  ? 11.23200  16.19800  -22.72000 1.000 57.80956  ? 51  ASN B CG  1 
ATOM   2708 O OD1 . ASN B 1 51  ? 11.08300  14.96300  -22.67400 1.000 57.03315  ? 51  ASN B OD1 1 
ATOM   2709 N ND2 . ASN B 1 51  ? 11.06900  16.90400  -23.84100 1.000 62.59435  ? 51  ASN B ND2 1 
ATOM   2710 N N   . PRO B 1 52  ? 10.30700  17.24000  -17.98000 1.000 53.12742  ? 52  PRO B N   1 
ATOM   2711 C CA  . PRO B 1 52  ? 10.62300  18.04000  -16.80200 1.000 52.11941  ? 52  PRO B CA  1 
ATOM   2712 C C   . PRO B 1 52  ? 11.95200  17.60200  -16.22000 1.000 49.73228  ? 52  PRO B C   1 
ATOM   2713 O O   . PRO B 1 52  ? 12.26800  16.40800  -16.15900 1.000 50.55869  ? 52  PRO B O   1 
ATOM   2714 C CB  . PRO B 1 52  ? 9.45200   17.72900  -15.85700 1.000 50.16917  ? 52  PRO B CB  1 
ATOM   2715 C CG  . PRO B 1 52  ? 9.04300   16.28400  -16.24000 1.000 48.00839  ? 52  PRO B CG  1 
ATOM   2716 C CD  . PRO B 1 52  ? 9.27200   16.20500  -17.71300 1.000 49.02167  ? 52  PRO B CD  1 
ATOM   2717 N N   . ASN B 1 53  ? 12.75700  18.57100  -15.78700 1.000 49.42172  ? 53  ASN B N   1 
ATOM   2718 C CA  . ASN B 1 53  ? 13.86300  18.22800  -14.90900 1.000 49.89282  ? 53  ASN B CA  1 
ATOM   2719 C C   . ASN B 1 53  ? 13.40800  18.62300  -13.51200 1.000 50.32445  ? 53  ASN B C   1 
ATOM   2720 O O   . ASN B 1 53  ? 13.41900  19.80700  -13.14400 1.000 47.47411  ? 53  ASN B O   1 
ATOM   2721 C CB  . ASN B 1 53  ? 15.18200  18.88700  -15.26500 1.000 48.07945  ? 53  ASN B CB  1 
ATOM   2722 C CG  . ASN B 1 53  ? 16.26100  18.30900  -14.43100 1.000 52.91161  ? 53  ASN B CG  1 
ATOM   2723 O OD1 . ASN B 1 53  ? 16.42200  18.71500  -13.28700 1.000 56.73575  ? 53  ASN B OD1 1 
ATOM   2724 N ND2 . ASN B 1 53  ? 16.90400  17.26200  -14.91600 1.000 55.78037  ? 53  ASN B ND2 1 
ATOM   2725 N N   . TYR B 1 54  ? 12.92400  17.63500  -12.76400 1.000 49.71912  ? 54  TYR B N   1 
ATOM   2726 C CA  . TYR B 1 54  ? 12.33200  17.95200  -11.48400 1.000 46.27134  ? 54  TYR B CA  1 
ATOM   2727 C C   . TYR B 1 54  ? 13.34300  18.50800  -10.49600 1.000 49.08220  ? 54  TYR B C   1 
ATOM   2728 O O   . TYR B 1 54  ? 12.95000  19.23300  -9.58300  1.000 50.57185  ? 54  TYR B O   1 
ATOM   2729 C CB  . TYR B 1 54  ? 11.68400  16.71600  -10.90500 1.000 43.87105  ? 54  TYR B CB  1 
ATOM   2730 C CG  . TYR B 1 54  ? 10.45900  16.34100  -11.61600 1.000 43.75788  ? 54  TYR B CG  1 
ATOM   2731 C CD1 . TYR B 1 54  ? 9.26100   16.99500  -11.32900 1.000 43.76841  ? 54  TYR B CD1 1 
ATOM   2732 C CD2 . TYR B 1 54  ? 10.43800  15.27600  -12.52900 1.000 45.96604  ? 54  TYR B CD2 1 
ATOM   2733 C CE1 . TYR B 1 54  ? 8.05600   16.61400  -11.95300 1.000 44.06055  ? 54  TYR B CE1 1 
ATOM   2734 C CE2 . TYR B 1 54  ? 9.21100   14.87200  -13.13700 1.000 41.33390  ? 54  TYR B CE2 1 
ATOM   2735 C CZ  . TYR B 1 54  ? 8.05800   15.57900  -12.87100 1.000 43.31309  ? 54  TYR B CZ  1 
ATOM   2736 O OH  . TYR B 1 54  ? 6.84300   15.19600  -13.45700 1.000 45.95814  ? 54  TYR B OH  1 
ATOM   2737 N N   . GLU B 1 55  ? 14.61900  18.13600  -10.60000 1.000 47.40042  ? 55  GLU B N   1 
ATOM   2738 C CA  . GLU B 1 55  ? 15.60700  18.72300  -9.69500  1.000 51.50091  ? 55  GLU B CA  1 
ATOM   2739 C C   . GLU B 1 55  ? 15.68700  20.24600  -9.90400  1.000 54.14333  ? 55  GLU B C   1 
ATOM   2740 O O   . GLU B 1 55  ? 15.69500  21.02900  -8.94100  1.000 51.26404  ? 55  GLU B O   1 
ATOM   2741 C CB  . GLU B 1 55  ? 16.96800  18.05300  -9.89800  1.000 56.83313  ? 55  GLU B CB  1 
ATOM   2742 C CG  . GLU B 1 55  ? 17.96600  18.41000  -8.81100  1.000 61.82847  ? 55  GLU B CG  1 
ATOM   2743 C CD  . GLU B 1 55  ? 19.31600  17.66900  -8.94500  1.000 78.36992  ? 55  GLU B CD  1 
ATOM   2744 O OE1 . GLU B 1 55  ? 19.55600  17.03100  -9.99500  1.000 79.80694  ? 55  GLU B OE1 1 
ATOM   2745 O OE2 . GLU B 1 55  ? 20.14500  17.75100  -8.00600  1.000 76.48285  ? 55  GLU B OE2 1 
ATOM   2746 N N   . ASP B 1 56  ? 15.72500  20.67500  -11.16900 1.000 48.03997  ? 56  ASP B N   1 
ATOM   2747 C CA  . ASP B 1 56  ? 15.65600  22.09900  -11.52700 1.000 52.85107  ? 56  ASP B CA  1 
ATOM   2748 C C   . ASP B 1 56  ? 14.37200  22.73600  -11.01900 1.000 55.10134  ? 56  ASP B C   1 
ATOM   2749 O O   . ASP B 1 56  ? 14.37000  23.82700  -10.42200 1.000 51.62987  ? 56  ASP B O   1 
ATOM   2750 C CB  . ASP B 1 56  ? 15.66000  22.21700  -13.04800 1.000 55.21451  ? 56  ASP B CB  1 
ATOM   2751 C CG  . ASP B 1 56  ? 17.01400  22.46000  -13.62900 1.000 59.32553  ? 56  ASP B CG  1 
ATOM   2752 O OD1 . ASP B 1 56  ? 17.94100  22.79000  -12.87700 1.000 60.68096  ? 56  ASP B OD1 1 
ATOM   2753 O OD2 . ASP B 1 56  ? 17.14300  22.29300  -14.85500 1.000 65.05517  ? 56  ASP B OD2 1 
ATOM   2754 N N   . LEU B 1 57  ? 13.24900  22.11500  -11.35500 1.000 48.24263  ? 57  LEU B N   1 
ATOM   2755 C CA  . LEU B 1 57  ? 11.98300  22.68900  -10.99200 1.000 53.46167  ? 57  LEU B CA  1 
ATOM   2756 C C   . LEU B 1 57  ? 11.90300  22.88600  -9.48600  1.000 54.19334  ? 57  LEU B C   1 
ATOM   2757 O O   . LEU B 1 57  ? 11.36400  23.89300  -9.00000  1.000 55.81985  ? 57  LEU B O   1 
ATOM   2758 C CB  . LEU B 1 57  ? 10.85300  21.76700  -11.48800 1.000 51.90622  ? 57  LEU B CB  1 
ATOM   2759 C CG  . LEU B 1 57  ? 10.66200  21.67800  -13.01700 1.000 55.03028  ? 57  LEU B CG  1 
ATOM   2760 C CD1 . LEU B 1 57  ? 9.54600   20.68200  -13.36700 1.000 51.35089  ? 57  LEU B CD1 1 
ATOM   2761 C CD2 . LEU B 1 57  ? 10.32400  23.06500  -13.60300 1.000 55.20925  ? 57  LEU B CD2 1 
ATOM   2762 N N   . LEU B 1 58  ? 12.44400  21.94000  -8.73200  1.000 51.27720  ? 58  LEU B N   1 
ATOM   2763 C CA  . LEU B 1 58  ? 12.33800  22.02700  -7.28700  1.000 51.89833  ? 58  LEU B CA  1 
ATOM   2764 C C   . LEU B 1 58  ? 13.23800  23.13200  -6.74900  1.000 53.80382  ? 58  LEU B C   1 
ATOM   2765 O O   . LEU B 1 58  ? 12.82400  23.90100  -5.86300  1.000 53.85909  ? 58  LEU B O   1 
ATOM   2766 C CB  . LEU B 1 58  ? 12.71300  20.69600  -6.64900  1.000 50.44815  ? 58  LEU B CB  1 
ATOM   2767 C CG  . LEU B 1 58  ? 12.27500  20.69400  -5.18100  1.000 56.59626  ? 58  LEU B CG  1 
ATOM   2768 C CD1 . LEU B 1 58  ? 10.83100  21.07600  -5.11300  1.000 53.22217  ? 58  LEU B CD1 1 
ATOM   2769 C CD2 . LEU B 1 58  ? 12.41500  19.29900  -4.61400  1.000 58.25698  ? 58  LEU B CD2 1 
ATOM   2770 N N   . ILE B 1 59  ? 14.46300  23.25800  -7.28900  1.000 50.32709  ? 59  ILE B N   1 
ATOM   2771 C CA  . ILE B 1 59  ? 15.31700  24.31300  -6.77900  1.000 52.69842  ? 59  ILE B CA  1 
ATOM   2772 C C   . ILE B 1 59  ? 14.64600  25.65900  -6.96500  1.000 56.79892  ? 59  ILE B C   1 
ATOM   2773 O O   . ILE B 1 59  ? 14.78900  26.53500  -6.11500  1.000 58.44122  ? 59  ILE B O   1 
ATOM   2774 C CB  . ILE B 1 59  ? 16.71800  24.31500  -7.43200  1.000 53.65117  ? 59  ILE B CB  1 
ATOM   2775 C CG1 . ILE B 1 59  ? 17.45000  23.03200  -7.08300  1.000 62.15482  ? 59  ILE B CG1 1 
ATOM   2776 C CG2 . ILE B 1 59  ? 17.58300  25.46200  -6.87300  1.000 56.29622  ? 59  ILE B CG2 1 
ATOM   2777 C CD1 . ILE B 1 59  ? 18.71000  22.83700  -7.88400  1.000 66.35269  ? 59  ILE B CD1 1 
ATOM   2778 N N   . ARG B 1 60  ? 13.85500  25.83200  -8.02200  1.000 52.70369  ? 60  ARG B N   1 
ATOM   2779 C CA  . ARG B 1 60  ? 13.25400  27.13300  -8.26800  1.000 55.76721  ? 60  ARG B CA  1 
ATOM   2780 C C   . ARG B 1 60  ? 12.04100  27.38500  -7.42400  1.000 60.59674  ? 60  ARG B C   1 
ATOM   2781 O O   . ARG B 1 60  ? 11.43000  28.45200  -7.55700  1.000 62.77068  ? 60  ARG B O   1 
ATOM   2782 C CB  . ARG B 1 60  ? 12.87300  27.26600  -9.73200  1.000 53.74855  ? 60  ARG B CB  1 
ATOM   2783 C CG  . ARG B 1 60  ? 14.01600  27.09000  -10.55800 1.000 51.63251  ? 60  ARG B CG  1 
ATOM   2784 C CD  . ARG B 1 60  ? 13.61400  26.87100  -11.96600 1.000 56.39360  ? 60  ARG B CD  1 
ATOM   2785 N NE  . ARG B 1 60  ? 14.87800  26.82900  -12.70300 1.000 50.22444  ? 60  ARG B NE  1 
ATOM   2786 C CZ  . ARG B 1 60  ? 15.08300  26.20400  -13.85300 1.000 55.19083  ? 60  ARG B CZ  1 
ATOM   2787 N NH1 . ARG B 1 60  ? 14.08500  25.62500  -14.50800 1.000 60.84677  ? 60  ARG B NH1 1 
ATOM   2788 N NH2 . ARG B 1 60  ? 16.32100  26.19200  -14.37200 1.000 59.26237  ? 60  ARG B NH2 1 
ATOM   2789 N N   . LYS B 1 61  ? 11.68800  26.46300  -6.55300  1.000 57.83588  ? 61  LYS B N   1 
ATOM   2790 C CA  . LYS B 1 61  ? 10.52300  26.67500  -5.72500  1.000 62.68383  ? 61  LYS B CA  1 
ATOM   2791 C C   . LYS B 1 61  ? 10.98300  27.04100  -4.32000  1.000 64.87094  ? 61  LYS B C   1 
ATOM   2792 O O   . LYS B 1 61  ? 12.11600  26.76000  -3.91000  1.000 58.92022  ? 61  LYS B O   1 
ATOM   2793 C CB  . LYS B 1 61  ? 9.64700   25.41300  -5.71500  1.000 57.84904  ? 61  LYS B CB  1 
ATOM   2794 C CG  . LYS B 1 61  ? 8.20900   25.57000  -6.33300  1.000 69.70573  ? 61  LYS B CG  1 
ATOM   2795 C CD  . LYS B 1 61  ? 7.97800   25.07700  -7.79600  1.000 68.43978  ? 61  LYS B CD  1 
ATOM   2796 C CE  . LYS B 1 61  ? 8.70300   25.98800  -8.82900  1.000 76.98555  ? 61  LYS B CE  1 
ATOM   2797 N NZ  . LYS B 1 61  ? 9.56000   25.26100  -9.85300  1.000 59.18604  ? 61  LYS B NZ  1 
ATOM   2798 N N   . SER B 1 62  ? 10.07700  27.67200  -3.58400  1.000 70.72690  ? 62  SER B N   1 
ATOM   2799 C CA  . SER B 1 62  ? 10.25800  27.93500  -2.17000  1.000 67.64232  ? 62  SER B CA  1 
ATOM   2800 C C   . SER B 1 62  ? 9.08600   27.33900  -1.38900  1.000 65.09201  ? 62  SER B C   1 
ATOM   2801 O O   . SER B 1 62  ? 8.05300   26.95900  -1.95500  1.000 64.23665  ? 62  SER B O   1 
ATOM   2802 C CB  . SER B 1 62  ? 10.36200  29.44000  -1.91800  1.000 71.95073  ? 62  SER B CB  1 
ATOM   2803 O OG  . SER B 1 62  ? 9.87300   29.73200  -0.63100  1.000 84.92071  ? 62  SER B OG  1 
ATOM   2804 N N   . ASN B 1 63  ? 9.22100   27.29300  -0.06200  1.000 63.28654  ? 63  ASN B N   1 
ATOM   2805 C CA  . ASN B 1 63  ? 8.12300   26.78000  0.75200   1.000 61.82847  ? 63  ASN B CA  1 
ATOM   2806 C C   . ASN B 1 63  ? 6.79500   27.46500  0.41400   1.000 61.74161  ? 63  ASN B C   1 
ATOM   2807 O O   . ASN B 1 63  ? 5.78800   26.78600  0.20200   1.000 63.38392  ? 63  ASN B O   1 
ATOM   2808 C CB  . ASN B 1 63  ? 8.46200   26.95700  2.23400   1.000 61.57317  ? 63  ASN B CB  1 
ATOM   2809 C CG  . ASN B 1 63  ? 9.53600   25.98500  2.72100   1.000 61.51001  ? 63  ASN B CG  1 
ATOM   2810 O OD1 . ASN B 1 63  ? 9.66200   24.85800  2.22400   1.000 61.61528  ? 63  ASN B OD1 1 
ATOM   2811 N ND2 . ASN B 1 63  ? 10.31100  26.41100  3.70200   1.000 58.99655  ? 63  ASN B ND2 1 
ATOM   2812 N N   . HIS B 1 64  ? 6.78900   28.79600  0.23200   1.000 64.96832  ? 64  HIS B N   1 
ATOM   2813 C CA  . HIS B 1 64  ? 5.52400   29.51600  0.02200   1.000 65.34468  ? 64  HIS B CA  1 
ATOM   2814 C C   . HIS B 1 64  ? 4.90300   29.24800  -1.34000  1.000 64.13137  ? 64  HIS B C   1 
ATOM   2815 O O   . HIS B 1 64  ? 3.73000   29.57300  -1.54000  1.000 64.98411  ? 64  HIS B O   1 
ATOM   2816 C CB  . HIS B 1 64  ? 5.70600   31.03000  0.24200   1.000 64.55774  ? 64  HIS B CB  1 
ATOM   2817 C CG  . HIS B 1 64  ? 6.54900   31.70200  -0.80700  1.000 69.75047  ? 64  HIS B CG  1 
ATOM   2818 N ND1 . HIS B 1 64  ? 7.90100   31.93100  -0.63400  1.000 72.17444  ? 64  HIS B ND1 1 
ATOM   2819 C CD2 . HIS B 1 64  ? 6.24300   32.18000  -2.03900  1.000 66.84486  ? 64  HIS B CD2 1 
ATOM   2820 C CE1 . HIS B 1 64  ? 8.38800   32.53100  -1.70900  1.000 70.51109  ? 64  HIS B CE1 1 
ATOM   2821 N NE2 . HIS B 1 64  ? 7.40500   32.68000  -2.58100  1.000 74.64579  ? 64  HIS B NE2 1 
ATOM   2822 N N   . ASN B 1 65  ? 5.61900   28.58500  -2.24300  1.000 64.36561  ? 65  ASN B N   1 
ATOM   2823 C CA  . ASN B 1 65  ? 5.05700   28.16500  -3.52200  1.000 64.45246  ? 65  ASN B CA  1 
ATOM   2824 C C   . ASN B 1 65  ? 4.16100   26.94100  -3.39300  1.000 60.98100  ? 65  ASN B C   1 
ATOM   2825 O O   . ASN B 1 65  ? 3.46500   26.59600  -4.35900  1.000 63.06019  ? 65  ASN B O   1 
ATOM   2826 C CB  . ASN B 1 65  ? 6.17800   27.86100  -4.52800  1.000 63.74185  ? 65  ASN B CB  1 
ATOM   2827 C CG  . ASN B 1 65  ? 7.06100   29.03900  -4.80200  1.000 69.37148  ? 65  ASN B CG  1 
ATOM   2828 O OD1 . ASN B 1 65  ? 6.96900   30.07300  -4.15000  1.000 76.16703  ? 65  ASN B OD1 1 
ATOM   2829 N ND2 . ASN B 1 65  ? 7.94700   28.89300  -5.76600  1.000 72.26393  ? 65  ASN B ND2 1 
ATOM   2830 N N   . PHE B 1 66  ? 4.09700   26.31700  -2.21300  1.000 60.33355  ? 66  PHE B N   1 
ATOM   2831 C CA  . PHE B 1 66  ? 3.26300   25.12900  -1.97000  1.000 57.65954  ? 66  PHE B CA  1 
ATOM   2832 C C   . PHE B 1 66  ? 2.05000   25.46900  -1.10000  1.000 61.66002  ? 66  PHE B C   1 
ATOM   2833 O O   . PHE B 1 66  ? 2.18700   25.73500  0.10200   1.000 59.55977  ? 66  PHE B O   1 
ATOM   2834 C CB  . PHE B 1 66  ? 4.08700   24.03000  -1.30900  1.000 54.30914  ? 66  PHE B CB  1 
ATOM   2835 C CG  . PHE B 1 66  ? 5.14800   23.45700  -2.18600  1.000 56.00408  ? 66  PHE B CG  1 
ATOM   2836 C CD1 . PHE B 1 66  ? 4.84900   22.43800  -3.05600  1.000 55.15661  ? 66  PHE B CD1 1 
ATOM   2837 C CD2 . PHE B 1 66  ? 6.44400   23.94900  -2.15300  1.000 54.89079  ? 66  PHE B CD2 1 
ATOM   2838 C CE1 . PHE B 1 66  ? 5.82100   21.90700  -3.87600  1.000 53.14058  ? 66  PHE B CE1 1 
ATOM   2839 C CE2 . PHE B 1 66  ? 7.40400   23.42400  -2.96700  1.000 58.60703  ? 66  PHE B CE2 1 
ATOM   2840 C CZ  . PHE B 1 66  ? 7.09300   22.40800  -3.82500  1.000 51.65619  ? 66  PHE B CZ  1 
ATOM   2841 N N   . LEU B 1 67  ? 0.86000   25.39200  -1.68000  1.000 55.69878  ? 67  LEU B N   1 
ATOM   2842 C CA  . LEU B 1 67  ? -0.37500  25.66000  -0.96800  1.000 58.92285  ? 67  LEU B CA  1 
ATOM   2843 C C   . LEU B 1 67  ? -0.96400  24.31400  -0.53400  1.000 58.36489  ? 67  LEU B C   1 
ATOM   2844 O O   . LEU B 1 67  ? -1.50200  23.57500  -1.36500  1.000 55.92513  ? 67  LEU B O   1 
ATOM   2845 C CB  . LEU B 1 67  ? -1.32000  26.40500  -1.90500  1.000 63.06019  ? 67  LEU B CB  1 
ATOM   2846 C CG  . LEU B 1 67  ? -2.01800  27.70300  -1.57400  1.000 70.17684  ? 67  LEU B CG  1 
ATOM   2847 C CD1 . LEU B 1 67  ? -3.32100  27.39700  -0.81700  1.000 72.49553  ? 67  LEU B CD1 1 
ATOM   2848 C CD2 . LEU B 1 67  ? -1.06600  28.64100  -0.80100  1.000 76.51970  ? 67  LEU B CD2 1 
ATOM   2849 N N   . VAL B 1 68  ? -0.91600  24.01300  0.76300   1.000 58.62808  ? 68  VAL B N   1 
ATOM   2850 C CA  . VAL B 1 68  ? -1.43200  22.75500  1.29800   1.000 57.75429  ? 68  VAL B CA  1 
ATOM   2851 C C   . VAL B 1 68  ? -2.67100  23.05200  2.15100   1.000 58.81231  ? 68  VAL B C   1 
ATOM   2852 O O   . VAL B 1 68  ? -2.61900  23.89100  3.05800   1.000 64.74197  ? 68  VAL B O   1 
ATOM   2853 C CB  . VAL B 1 68  ? -0.34900  22.01400  2.10600   1.000 55.69089  ? 68  VAL B CB  1 
ATOM   2854 C CG1 . VAL B 1 68  ? -0.87900  20.67600  2.64600   1.000 50.45605  ? 68  VAL B CG1 1 
ATOM   2855 C CG2 . VAL B 1 68  ? 0.87800   21.77500  1.24300   1.000 52.52998  ? 68  VAL B CG2 1 
ATOM   2856 N N   . GLN B 1 69  ? -3.76600  22.34400  1.88700   1.000 54.31178  ? 69  GLN B N   1 
ATOM   2857 C CA  . GLN B 1 69  ? -5.03700  22.59500  2.56000   1.000 57.78851  ? 69  GLN B CA  1 
ATOM   2858 C C   . GLN B 1 69  ? -5.64100  21.28800  3.04700   1.000 55.95934  ? 69  GLN B C   1 
ATOM   2859 O O   . GLN B 1 69  ? -5.83600  20.35100  2.26100   1.000 51.96413  ? 69  GLN B O   1 
ATOM   2860 C CB  . GLN B 1 69  ? -6.01000  23.31900  1.63500   1.000 62.49434  ? 69  GLN B CB  1 
ATOM   2861 C CG  . GLN B 1 69  ? -5.48200  24.64200  1.09600   1.000 70.27948  ? 69  GLN B CG  1 
ATOM   2862 C CD  . GLN B 1 69  ? -6.41200  25.26100  0.05800   1.000 80.87812  ? 69  GLN B CD  1 
ATOM   2863 O OE1 . GLN B 1 69  ? -6.06400  25.35000  -1.11600  1.000 83.35999  ? 69  GLN B OE1 1 
ATOM   2864 N NE2 . GLN B 1 69  ? -7.59400  25.71600  0.50000   1.000 79.98854  ? 69  GLN B NE2 1 
ATOM   2865 N N   . ALA B 1 70  ? -5.91300  21.22500  4.34400   1.000 58.83074  ? 70  ALA B N   1 
ATOM   2866 C CA  . ALA B 1 70  ? -6.64700  20.12400  4.95800   1.000 58.97286  ? 70  ALA B CA  1 
ATOM   2867 C C   . ALA B 1 70  ? -8.06100  20.64800  5.17200   1.000 62.16535  ? 70  ALA B C   1 
ATOM   2868 O O   . ALA B 1 70  ? -8.35500  21.30000  6.17400   1.000 60.70728  ? 70  ALA B O   1 
ATOM   2869 C CB  . ALA B 1 70  ? -5.98800  19.67700  6.25100   1.000 60.35460  ? 70  ALA B CB  1 
ATOM   2870 N N   . GLY B 1 71  ? -8.91100  20.42000  4.17600   1.000 61.03363  ? 71  GLY B N   1 
ATOM   2871 C CA  . GLY B 1 71  ? -10.22000 21.04200  4.13400   1.000 72.19550  ? 71  GLY B CA  1 
ATOM   2872 C C   . GLY B 1 71  ? -10.04200 22.51500  3.84600   1.000 76.72236  ? 71  GLY B C   1 
ATOM   2873 O O   . GLY B 1 71  ? -9.35100  22.89900  2.89300   1.000 76.74868  ? 71  GLY B O   1 
ATOM   2874 N N   . ASN B 1 72  ? -10.54900 23.35600  4.73000   1.000 80.39122  ? 72  ASN B N   1 
ATOM   2875 C CA  . ASN B 1 72  ? -10.25600 24.77200  4.59700   1.000 87.16835  ? 72  ASN B CA  1 
ATOM   2876 C C   . ASN B 1 72  ? -9.04000  25.17700  5.39400   1.000 83.45474  ? 72  ASN B C   1 
ATOM   2877 O O   . ASN B 1 72  ? -8.49600  26.25900  5.15000   1.000 100.48310 ? 72  ASN B O   1 
ATOM   2878 C CB  . ASN B 1 72  ? -11.44000 25.63500  5.05800   1.000 97.28535  ? 72  ASN B CB  1 
ATOM   2879 C CG  . ASN B 1 72  ? -12.73700 25.24800  4.38600   1.000 105.52318 ? 72  ASN B CG  1 
ATOM   2880 O OD1 . ASN B 1 72  ? -13.37300 24.25500  4.75800   1.000 104.53359 ? 72  ASN B OD1 1 
ATOM   2881 N ND2 . ASN B 1 72  ? -13.14300 26.02900  3.38700   1.000 110.01845 ? 72  ASN B ND2 1 
ATOM   2882 N N   . VAL B 1 73  ? -8.60900  24.35600  6.34900   1.000 73.68252  ? 73  VAL B N   1 
ATOM   2883 C CA  . VAL B 1 73  ? -7.45000  24.73300  7.14800   1.000 73.80095  ? 73  VAL B CA  1 
ATOM   2884 C C   . VAL B 1 73  ? -6.20600  24.74400  6.25900   1.000 69.39253  ? 73  VAL B C   1 
ATOM   2885 O O   . VAL B 1 73  ? -5.82500  23.73600  5.65500   1.000 65.34204  ? 73  VAL B O   1 
ATOM   2886 C CB  . VAL B 1 73  ? -7.29400  23.81300  8.36700   1.000 68.36872  ? 73  VAL B CB  1 
ATOM   2887 C CG1 . VAL B 1 73  ? -5.99800  24.09600  9.07700   1.000 71.10589  ? 73  VAL B CG1 1 
ATOM   2888 C CG2 . VAL B 1 73  ? -8.42800  24.05400  9.32000   1.000 70.60320  ? 73  VAL B CG2 1 
ATOM   2889 N N   . GLN B 1 74  ? -5.57700  25.89400  6.15600   1.000 69.86364  ? 74  GLN B N   1 
ATOM   2890 C CA  . GLN B 1 74  ? -4.36200  25.98000  5.37400   1.000 71.49541  ? 74  GLN B CA  1 
ATOM   2891 C C   . GLN B 1 74  ? -3.21400  25.50000  6.24800   1.000 72.25077  ? 74  GLN B C   1 
ATOM   2892 O O   . GLN B 1 74  ? -3.13900  25.86200  7.42100   1.000 73.68252  ? 74  GLN B O   1 
ATOM   2893 C CB  . GLN B 1 74  ? -4.15700  27.41200  4.89600   1.000 73.75621  ? 74  GLN B CB  1 
ATOM   2894 C CG  . GLN B 1 74  ? -2.72000  27.75400  4.56400   1.000 79.82273  ? 74  GLN B CG  1 
ATOM   2895 C CD  . GLN B 1 74  ? -2.54300  28.27000  3.14300   1.000 87.39206  ? 74  GLN B CD  1 
ATOM   2896 O OE1 . GLN B 1 74  ? -3.29800  27.89200  2.24000   1.000 88.84749  ? 74  GLN B OE1 1 
ATOM   2897 N NE2 . GLN B 1 74  ? -1.53600  29.13000  2.93500   1.000 87.24467  ? 74  GLN B NE2 1 
ATOM   2898 N N   . LEU B 1 75  ? -2.36200  24.62500  5.69900   1.000 69.65835  ? 75  LEU B N   1 
ATOM   2899 C CA  . LEU B 1 75  ? -1.17900  24.11800  6.38900   1.000 67.95815  ? 75  LEU B CA  1 
ATOM   2900 C C   . LEU B 1 75  ? 0.04600   24.83300  5.83400   1.000 70.05050  ? 75  LEU B C   1 
ATOM   2901 O O   . LEU B 1 75  ? 0.24900   24.85700  4.61700   1.000 70.62163  ? 75  LEU B O   1 
ATOM   2902 C CB  . LEU B 1 75  ? -1.02900  22.60600  6.20700   1.000 63.76028  ? 75  LEU B CB  1 
ATOM   2903 C CG  . LEU B 1 75  ? -2.13200  21.74000  6.82700   1.000 61.56791  ? 75  LEU B CG  1 
ATOM   2904 C CD1 . LEU B 1 75  ? -1.86100  20.25100  6.67800   1.000 57.18844  ? 75  LEU B CD1 1 
ATOM   2905 C CD2 . LEU B 1 75  ? -2.31800  22.11900  8.31000   1.000 65.94738  ? 75  LEU B CD2 1 
ATOM   2906 N N   . ARG B 1 76  ? 0.87200   25.39700  6.70700   1.000 69.15829  ? 76  ARG B N   1 
ATOM   2907 C CA  . ARG B 1 76  ? 2.03300   26.14300  6.23100   1.000 69.35305  ? 76  ARG B CA  1 
ATOM   2908 C C   . ARG B 1 76  ? 3.19100   25.18100  5.98500   1.000 64.48142  ? 76  ARG B C   1 
ATOM   2909 O O   . ARG B 1 76  ? 3.55000   24.38900  6.86200   1.000 64.39193  ? 76  ARG B O   1 
ATOM   2910 C CB  . ARG B 1 76  ? 2.47100   27.26700  7.19300   1.000 73.69831  ? 76  ARG B CB  1 
ATOM   2911 C CG  . ARG B 1 76  ? 1.65700   27.44800  8.49100   1.000 85.74712  ? 76  ARG B CG  1 
ATOM   2912 C CD  . ARG B 1 76  ? 0.24200   28.05300  8.31900   1.000 88.98699  ? 76  ARG B CD  1 
ATOM   2913 N NE  . ARG B 1 76  ? -0.81400  27.08300  8.62400   1.000 99.19610  ? 76  ARG B NE  1 
ATOM   2914 C CZ  . ARG B 1 76  ? -1.39700  26.92500  9.81100   1.000 96.97742  ? 76  ARG B CZ  1 
ATOM   2915 N NH1 . ARG B 1 76  ? -1.07100  27.68900  10.85000  1.000 96.71949  ? 76  ARG B NH1 1 
ATOM   2916 N NH2 . ARG B 1 76  ? -2.32500  25.97000  9.96100   1.000 86.66039  ? 76  ARG B NH2 1 
ATOM   2917 N N   . VAL B 1 77  ? 3.75800   25.24500  4.78400   1.000 64.40772  ? 77  VAL B N   1 
ATOM   2918 C CA  . VAL B 1 77  ? 4.92100   24.43600  4.43700   1.000 61.45737  ? 77  VAL B CA  1 
ATOM   2919 C C   . VAL B 1 77  ? 6.17400   25.09600  4.98600   1.000 61.62844  ? 77  VAL B C   1 
ATOM   2920 O O   . VAL B 1 77  ? 6.40400   26.30100  4.77300   1.000 60.24933  ? 77  VAL B O   1 
ATOM   2921 C CB  . VAL B 1 77  ? 5.00600   24.23500  2.91900   1.000 58.42279  ? 77  VAL B CB  1 
ATOM   2922 C CG1 . VAL B 1 77  ? 6.24500   23.43000  2.57500   1.000 54.72761  ? 77  VAL B CG1 1 
ATOM   2923 C CG2 . VAL B 1 77  ? 3.73000   23.51600  2.42900   1.000 56.50941  ? 77  VAL B CG2 1 
ATOM   2924 N N   . ILE B 1 78  ? 6.98800   24.31300  5.71700   1.000 60.63095  ? 78  ILE B N   1 
ATOM   2925 C CA  . ILE B 1 78  ? 8.19900   24.83100  6.34200   1.000 61.05995  ? 78  ILE B CA  1 
ATOM   2926 C C   . ILE B 1 78  ? 9.45700   24.09200  5.89400   1.000 60.64675  ? 78  ILE B C   1 
ATOM   2927 O O   . ILE B 1 78  ? 10.50500  24.26400  6.49400   1.000 57.01736  ? 78  ILE B O   1 
ATOM   2928 C CB  . ILE B 1 78  ? 8.11600   24.80200  7.88200   1.000 60.89941  ? 78  ILE B CB  1 
ATOM   2929 C CG1 . ILE B 1 78  ? 8.00200   23.35500  8.37800   1.000 63.48656  ? 78  ILE B CG1 1 
ATOM   2930 C CG2 . ILE B 1 78  ? 6.95300   25.68400  8.37200   1.000 60.71254  ? 78  ILE B CG2 1 
ATOM   2931 C CD1 . ILE B 1 78  ? 8.22400   23.20900  9.88400   1.000 63.73659  ? 78  ILE B CD1 1 
ATOM   2932 N N   . GLY B 1 79  ? 9.37000   23.25800  4.85800   1.000 62.29168  ? 79  GLY B N   1 
ATOM   2933 C CA  . GLY B 1 79  ? 10.52700  22.52300  4.38700   1.000 55.98040  ? 79  GLY B CA  1 
ATOM   2934 C C   . GLY B 1 79  ? 10.05400  21.64000  3.25600   1.000 56.31728  ? 79  GLY B C   1 
ATOM   2935 O O   . GLY B 1 79  ? 8.88100   21.26100  3.21600   1.000 53.79592  ? 79  GLY B O   1 
ATOM   2936 N N   . HIS B 1 80  ? 10.91900  21.35000  2.29700   1.000 54.61707  ? 80  HIS B N   1 
ATOM   2937 C CA  . HIS B 1 80  ? 10.51900  20.52800  1.16900   1.000 53.53010  ? 80  HIS B CA  1 
ATOM   2938 C C   . HIS B 1 80  ? 11.72600  19.73800  0.69200   1.000 55.65667  ? 80  HIS B C   1 
ATOM   2939 O O   . HIS B 1 80  ? 12.86600  20.21200  0.75300   1.000 53.11689  ? 80  HIS B O   1 
ATOM   2940 C CB  . HIS B 1 80  ? 9.94200   21.38900  0.03100   1.000 53.28797  ? 80  HIS B CB  1 
ATOM   2941 C CG  . HIS B 1 80  ? 10.91900  22.40200  -0.51500  1.000 56.79102  ? 80  HIS B CG  1 
ATOM   2942 N ND1 . HIS B 1 80  ? 10.94200  23.71000  -0.09300  1.000 57.84378  ? 80  HIS B ND1 1 
ATOM   2943 C CD2 . HIS B 1 80  ? 11.91700  22.28700  -1.43300  1.000 58.01485  ? 80  HIS B CD2 1 
ATOM   2944 C CE1 . HIS B 1 80  ? 11.90900  24.36700  -0.73200  1.000 62.57592  ? 80  HIS B CE1 1 
ATOM   2945 N NE2 . HIS B 1 80  ? 12.50900  23.52700  -1.56100  1.000 59.58609  ? 80  HIS B NE2 1 
ATOM   2946 N N   . SER B 1 81  ? 11.47500  18.52200  0.22900   1.000 49.96652  ? 81  SER B N   1 
ATOM   2947 C CA  . SER B 1 81  ? 12.52500  17.75000  -0.40500  1.000 49.77176  ? 81  SER B CA  1 
ATOM   2948 C C   . SER B 1 81  ? 11.87100  16.74200  -1.32800  1.000 51.12455  ? 81  SER B C   1 
ATOM   2949 O O   . SER B 1 81  ? 10.66000  16.45700  -1.23300  1.000 48.66110  ? 81  SER B O   1 
ATOM   2950 C CB  . SER B 1 81  ? 13.45000  17.04600  0.60500   1.000 53.84067  ? 81  SER B CB  1 
ATOM   2951 O OG  . SER B 1 81  ? 12.74500  16.08100  1.35400   1.000 55.97513  ? 81  SER B OG  1 
ATOM   2952 N N   . MET B 1 82  ? 12.69500  16.18900  -2.20200  1.000 47.07933  ? 82  MET B N   1 
ATOM   2953 C CA  . MET B 1 82  ? 12.24000  15.24700  -3.20200  1.000 49.03746  ? 82  MET B CA  1 
ATOM   2954 C C   . MET B 1 82  ? 12.91500  13.90600  -2.94100  1.000 49.26117  ? 82  MET B C   1 
ATOM   2955 O O   . MET B 1 82  ? 14.12400  13.86300  -2.71500  1.000 49.67701  ? 82  MET B O   1 
ATOM   2956 C CB  . MET B 1 82  ? 12.57700  15.76700  -4.59100  1.000 49.22432  ? 82  MET B CB  1 
ATOM   2957 C CG  . MET B 1 82  ? 12.15600  14.85700  -5.66400  1.000 45.72654  ? 82  MET B CG  1 
ATOM   2958 S SD  . MET B 1 82  ? 12.32400  15.61600  -7.26700  1.000 50.00600  ? 82  MET B SD  1 
ATOM   2959 C CE  . MET B 1 82  ? 14.09000  16.12400  -7.39600  1.000 49.17695  ? 82  MET B CE  1 
ATOM   2960 N N   . GLN B 1 83  ? 12.12900  12.85200  -2.84600  1.000 44.60798  ? 83  GLN B N   1 
ATOM   2961 C CA  . GLN B 1 83  ? 12.62100  11.46500  -2.80200  1.000 47.68730  ? 83  GLN B CA  1 
ATOM   2962 C C   . GLN B 1 83  ? 12.04500  10.70700  -4.00300  1.000 43.38415  ? 83  GLN B C   1 
ATOM   2963 O O   . GLN B 1 83  ? 10.85500  10.36200  -3.99900  1.000 43.51574  ? 83  GLN B O   1 
ATOM   2964 C CB  . GLN B 1 83  ? 12.21200  10.77900  -1.48300  1.000 52.30101  ? 83  GLN B CB  1 
ATOM   2965 C CG  . GLN B 1 83  ? 12.70500  9.29900   -1.32900  1.000 50.29287  ? 83  GLN B CG  1 
ATOM   2966 C CD  . GLN B 1 83  ? 12.22000  8.54800   -0.05400  1.000 58.33331  ? 83  GLN B CD  1 
ATOM   2967 O OE1 . GLN B 1 83  ? 11.24100  8.95200   0.61200   1.000 56.01198  ? 83  GLN B OE1 1 
ATOM   2968 N NE2 . GLN B 1 83  ? 12.86100  7.40000   0.23400   1.000 57.01736  ? 83  GLN B NE2 1 
ATOM   2969 N N   . ASN B 1 84  ? 12.88400  10.39800  -5.01800  1.000 39.50737  ? 84  ASN B N   1 
ATOM   2970 C CA  . ASN B 1 84  ? 12.41800  9.69300   -6.23400  1.000 44.36321  ? 84  ASN B CA  1 
ATOM   2971 C C   . ASN B 1 84  ? 11.26700  10.51800  -6.81100  1.000 45.00540  ? 84  ASN B C   1 
ATOM   2972 O O   . ASN B 1 84  ? 11.43700  11.74500  -6.92000  1.000 42.52615  ? 84  ASN B O   1 
ATOM   2973 C CB  . ASN B 1 84  ? 12.08400  8.23800   -5.91300  1.000 39.74687  ? 84  ASN B CB  1 
ATOM   2974 C CG  . ASN B 1 84  ? 13.20500  7.57000   -5.20700  1.000 50.14549  ? 84  ASN B CG  1 
ATOM   2975 O OD1 . ASN B 1 84  ? 14.33000  7.66400   -5.65900  1.000 49.87440  ? 84  ASN B OD1 1 
ATOM   2976 N ND2 . ASN B 1 84  ? 12.95600  7.04500   -3.99900  1.000 43.94737  ? 84  ASN B ND2 1 
ATOM   2977 N N   . CYS B 1 85  ? 10.05600  9.95200   -7.01200  1.000 38.08878  ? 85  CYS B N   1 
ATOM   2978 C CA  . CYS B 1 85  ? 9.01200   10.69900  -7.70100  1.000 40.03638  ? 85  CYS B CA  1 
ATOM   2979 C C   . CYS B 1 85  ? 8.01400   11.33900  -6.72800  1.000 39.26260  ? 85  CYS B C   1 
ATOM   2980 O O   . CYS B 1 85  ? 6.97200   11.84100  -7.15000  1.000 39.03100  ? 85  CYS B O   1 
ATOM   2981 C CB  . CYS B 1 85  ? 8.29800   9.78500   -8.70800  1.000 42.37087  ? 85  CYS B CB  1 
ATOM   2982 S SG  . CYS B 1 85  ? 9.44100   9.14900   -10.03800 1.000 38.37039  ? 85  CYS B SG  1 
ATOM   2983 N N   . VAL B 1 86  ? 8.33100   11.36500  -5.43300  1.000 39.47842  ? 86  VAL B N   1 
ATOM   2984 C CA  . VAL B 1 86  ? 7.46100   12.04600  -4.48800  1.000 40.41011  ? 86  VAL B CA  1 
ATOM   2985 C C   . VAL B 1 86  ? 8.18400   13.20200  -3.82200  1.000 44.01054  ? 86  VAL B C   1 
ATOM   2986 O O   . VAL B 1 86  ? 9.41900   13.24200  -3.65300  1.000 42.89462  ? 86  VAL B O   1 
ATOM   2987 C CB  . VAL B 1 86  ? 6.85500   11.11100  -3.41600  1.000 43.10780  ? 86  VAL B CB  1 
ATOM   2988 C CG1 . VAL B 1 86  ? 5.90400   10.05600  -4.04700  1.000 40.77857  ? 86  VAL B CG1 1 
ATOM   2989 C CG2 . VAL B 1 86  ? 7.93800   10.51200  -2.58600  1.000 43.41573  ? 86  VAL B CG2 1 
ATOM   2990 N N   . LEU B 1 87  ? 7.39300   14.19800  -3.50500  1.000 38.93362  ? 87  LEU B N   1 
ATOM   2991 C CA  . LEU B 1 87  ? 7.82100   15.32100  -2.70700  1.000 41.49445  ? 87  LEU B CA  1 
ATOM   2992 C C   . LEU B 1 87  ? 7.40500   15.05800  -1.27400  1.000 46.08710  ? 87  LEU B C   1 
ATOM   2993 O O   . LEU B 1 87  ? 6.33100   14.49800  -1.04100  1.000 43.60786  ? 87  LEU B O   1 
ATOM   2994 C CB  . LEU B 1 87  ? 7.16000   16.58200  -3.23900  1.000 43.41836  ? 87  LEU B CB  1 
ATOM   2995 C CG  . LEU B 1 87  ? 7.85200   17.70700  -3.93700  1.000 52.99056  ? 87  LEU B CG  1 
ATOM   2996 C CD1 . LEU B 1 87  ? 9.13100   17.17000  -4.72900  1.000 50.35604  ? 87  LEU B CD1 1 
ATOM   2997 C CD2 . LEU B 1 87  ? 6.77500   18.39000  -4.76300  1.000 45.99236  ? 87  LEU B CD2 1 
ATOM   2998 N N   . LYS B 1 88  ? 8.24200   15.48900  -0.33200  1.000 44.62377  ? 88  LYS B N   1 
ATOM   2999 C CA  . LYS B 1 88  ? 8.00000   15.47400  1.10400   1.000 46.40556  ? 88  LYS B CA  1 
ATOM   3000 C C   . LYS B 1 88  ? 7.93400   16.92700  1.54900   1.000 51.44564  ? 88  LYS B C   1 
ATOM   3001 O O   . LYS B 1 88  ? 8.95400   17.63700  1.53200   1.000 49.21380  ? 88  LYS B O   1 
ATOM   3002 C CB  . LYS B 1 88  ? 9.10200   14.72700  1.85800   1.000 47.34252  ? 88  LYS B CB  1 
ATOM   3003 C CG  . LYS B 1 88  ? 9.19600   13.27000  1.41200   1.000 50.46131  ? 88  LYS B CG  1 
ATOM   3004 C CD  . LYS B 1 88  ? 9.94700   12.33200  2.37700   1.000 53.46957  ? 88  LYS B CD  1 
ATOM   3005 C CE  . LYS B 1 88  ? 11.40500  12.08800  2.09000   1.000 66.45797  ? 88  LYS B CE  1 
ATOM   3006 N NZ  . LYS B 1 88  ? 11.81100  11.02400  3.06800   1.000 68.71087  ? 88  LYS B NZ  1 
ATOM   3007 N N   . LEU B 1 89  ? 6.72900   17.38700  1.92900   1.000 48.33474  ? 89  LEU B N   1 
ATOM   3008 C CA  . LEU B 1 89  ? 6.54800   18.78000  2.34600   1.000 49.51383  ? 89  LEU B CA  1 
ATOM   3009 C C   . LEU B 1 89  ? 6.35700   18.78100  3.84800   1.000 52.93793  ? 89  LEU B C   1 
ATOM   3010 O O   . LEU B 1 89  ? 5.33900   18.27500  4.34900   1.000 52.61157  ? 89  LEU B O   1 
ATOM   3011 C CB  . LEU B 1 89  ? 5.34700   19.41100  1.66600   1.000 47.97680  ? 89  LEU B CB  1 
ATOM   3012 C CG  . LEU B 1 89  ? 5.32500   19.32600  0.17000   1.000 47.65571  ? 89  LEU B CG  1 
ATOM   3013 C CD1 . LEU B 1 89  ? 4.03400   19.95300  -0.32500  1.000 45.91340  ? 89  LEU B CD1 1 
ATOM   3014 C CD2 . LEU B 1 89  ? 6.59200   20.01900  -0.35500  1.000 47.73993  ? 89  LEU B CD2 1 
ATOM   3015 N N   . LYS B 1 90  ? 7.34400   19.29200  4.55600   1.000 50.00863  ? 90  LYS B N   1 
ATOM   3016 C CA  . LYS B 1 90  ? 7.23700   19.44400  5.99400   1.000 55.46981  ? 90  LYS B CA  1 
ATOM   3017 C C   . LYS B 1 90  ? 6.26400   20.58700  6.29600   1.000 56.18568  ? 90  LYS B C   1 
ATOM   3018 O O   . LYS B 1 90  ? 6.31500   21.63200  5.65500   1.000 56.91998  ? 90  LYS B O   1 
ATOM   3019 C CB  . LYS B 1 90  ? 8.62800   19.72000  6.56700   1.000 58.51754  ? 90  LYS B CB  1 
ATOM   3020 C CG  . LYS B 1 90  ? 8.69500   19.83000  8.04400   1.000 63.72080  ? 90  LYS B CG  1 
ATOM   3021 C CD  . LYS B 1 90  ? 8.56400   18.48100  8.71500   1.000 67.53178  ? 90  LYS B CD  1 
ATOM   3022 C CE  . LYS B 1 90  ? 9.95200   17.87900  8.97100   1.000 73.75884  ? 90  LYS B CE  1 
ATOM   3023 N NZ  . LYS B 1 90  ? 9.91000   16.63700  9.79800   1.000 72.80873  ? 90  LYS B NZ  1 
ATOM   3024 N N   . VAL B 1 91  ? 5.30800   20.35600  7.19700   1.000 58.76231  ? 91  VAL B N   1 
ATOM   3025 C CA  . VAL B 1 91  ? 4.30600   21.34800  7.56300   1.000 58.22277  ? 91  VAL B CA  1 
ATOM   3026 C C   . VAL B 1 91  ? 4.44500   21.63000  9.06100   1.000 62.92860  ? 91  VAL B C   1 
ATOM   3027 O O   . VAL B 1 91  ? 5.13800   20.91000  9.79000   1.000 61.72056  ? 91  VAL B O   1 
ATOM   3028 C CB  . VAL B 1 91  ? 2.87900   20.89900  7.19700   1.000 59.09919  ? 91  VAL B CB  1 
ATOM   3029 C CG1 . VAL B 1 91  ? 2.69700   20.86800  5.66900   1.000 55.11187  ? 91  VAL B CG1 1 
ATOM   3030 C CG2 . VAL B 1 91  ? 2.60200   19.53200  7.77900   1.000 55.39612  ? 91  VAL B CG2 1 
ATOM   3031 N N   . ASP B 1 92  ? 3.85200   22.74700  9.51100   1.000 66.02107  ? 92  ASP B N   1 
ATOM   3032 C CA  . ASP B 1 92  ? 4.00900   23.15500  10.91300  1.000 68.31872  ? 92  ASP B CA  1 
ATOM   3033 C C   . ASP B 1 92  ? 3.10500   22.39100  11.87800  1.000 70.48477  ? 92  ASP B C   1 
ATOM   3034 O O   . ASP B 1 92  ? 3.30100   22.49500  13.09800  1.000 71.82966  ? 92  ASP B O   1 
ATOM   3035 C CB  . ASP B 1 92  ? 3.75800   24.65100  11.07300  1.000 75.68802  ? 92  ASP B CB  1 
ATOM   3036 C CG  . ASP B 1 92  ? 2.35100   25.02900  10.75400  1.000 82.86520  ? 92  ASP B CG  1 
ATOM   3037 O OD1 . ASP B 1 92  ? 1.65700   24.26100  10.03500  1.000 80.87285  ? 92  ASP B OD1 1 
ATOM   3038 O OD2 . ASP B 1 92  ? 1.93900   26.11100  11.21400  1.000 89.54231  ? 92  ASP B OD2 1 
ATOM   3039 N N   . THR B 1 93  ? 2.09100   21.69200  11.36300  1.000 65.91580  ? 93  THR B N   1 
ATOM   3040 C CA  . THR B 1 93  ? 1.09900   20.98000  12.15900  1.000 65.64208  ? 93  THR B CA  1 
ATOM   3041 C C   . THR B 1 93  ? 1.19300   19.48800  11.87800  1.000 57.81483  ? 93  THR B C   1 
ATOM   3042 O O   . THR B 1 93  ? 1.09600   19.06300  10.72300  1.000 55.65141  ? 93  THR B O   1 
ATOM   3043 C CB  . THR B 1 93  ? -0.31400  21.49700  11.83400  1.000 65.66577  ? 93  THR B CB  1 
ATOM   3044 O OG1 . THR B 1 93  ? -0.31300  22.92900  11.86800  1.000 72.69819  ? 93  THR B OG1 1 
ATOM   3045 C CG2 . THR B 1 93  ? -1.35500  20.95200  12.80200  1.000 64.99727  ? 93  THR B CG2 1 
ATOM   3046 N N   . ALA B 1 94  ? 1.34400   18.68900  12.92600  1.000 58.05696  ? 94  ALA B N   1 
ATOM   3047 C CA  . ALA B 1 94  ? 1.22500   17.25100  12.76000  1.000 55.13293  ? 94  ALA B CA  1 
ATOM   3048 C C   . ALA B 1 94  ? -0.25500  16.88100  12.67000  1.000 54.95659  ? 94  ALA B C   1 
ATOM   3049 O O   . ALA B 1 94  ? -1.08200  17.40200  13.41400  1.000 58.87548  ? 94  ALA B O   1 
ATOM   3050 C CB  . ALA B 1 94  ? 1.89700   16.52700  13.92900  1.000 55.28294  ? 94  ALA B CB  1 
ATOM   3051 N N   . ASN B 1 95  ? -0.59500  16.00900  11.72100  1.000 52.62999  ? 95  ASN B N   1 
ATOM   3052 C CA  . ASN B 1 95  ? -1.96500  15.52500  11.56600  1.000 53.14321  ? 95  ASN B CA  1 
ATOM   3053 C C   . ASN B 1 95  ? -2.42300  14.81700  12.83400  1.000 55.42770  ? 95  ASN B C   1 
ATOM   3054 O O   . ASN B 1 95  ? -1.96500  13.70700  13.10800  1.000 54.93027  ? 95  ASN B O   1 
ATOM   3055 C CB  . ASN B 1 95  ? -2.04700  14.55400  10.38800  1.000 51.16140  ? 95  ASN B CB  1 
ATOM   3056 C CG  . ASN B 1 95  ? -3.47400  14.10300  10.08500  1.000 54.84079  ? 95  ASN B CG  1 
ATOM   3057 O OD1 . ASN B 1 95  ? -4.41100  14.37800  10.85100  1.000 54.77499  ? 95  ASN B OD1 1 
ATOM   3058 N ND2 . ASN B 1 95  ? -3.62400  13.35200  8.99600   1.000 49.00851  ? 95  ASN B ND2 1 
ATOM   3059 N N   . PRO B 1 96  ? -3.37100  15.37500  13.59300  1.000 57.43057  ? 96  PRO B N   1 
ATOM   3060 C CA  . PRO B 1 96  ? -3.82200  14.69400  14.82500  1.000 59.67294  ? 96  PRO B CA  1 
ATOM   3061 C C   . PRO B 1 96  ? -4.52200  13.35400  14.55700  1.000 59.91771  ? 96  PRO B C   1 
ATOM   3062 O O   . PRO B 1 96  ? -4.71400  12.56100  15.48900  1.000 61.13891  ? 96  PRO B O   1 
ATOM   3063 C CB  . PRO B 1 96  ? -4.77100  15.71500  15.45500  1.000 56.84366  ? 96  PRO B CB  1 
ATOM   3064 C CG  . PRO B 1 96  ? -5.30700  16.48400  14.27200  1.000 58.75704  ? 96  PRO B CG  1 
ATOM   3065 C CD  . PRO B 1 96  ? -4.14900  16.60100  13.32400  1.000 58.37542  ? 96  PRO B CD  1 
ATOM   3066 N N   . LYS B 1 97  ? -4.92600  13.10000  13.31900  1.000 56.25938  ? 97  LYS B N   1 
ATOM   3067 C CA  . LYS B 1 97  ? -5.56900  11.86200  12.92100  1.000 58.82021  ? 97  LYS B CA  1 
ATOM   3068 C C   . LYS B 1 97  ? -4.62000  10.91200  12.23300  1.000 53.98279  ? 97  LYS B C   1 
ATOM   3069 O O   . LYS B 1 97  ? -5.08400  10.03600  11.50500  1.000 54.37231  ? 97  LYS B O   1 
ATOM   3070 C CB  . LYS B 1 97  ? -6.73900  12.13200  11.97300  1.000 58.89917  ? 97  LYS B CB  1 
ATOM   3071 C CG  . LYS B 1 97  ? -7.70400  13.20100  12.42900  1.000 63.00229  ? 97  LYS B CG  1 
ATOM   3072 C CD  . LYS B 1 97  ? -8.45800  13.74600  11.21600  1.000 68.22923  ? 97  LYS B CD  1 
ATOM   3073 C CE  . LYS B 1 97  ? -9.91200  13.44000  11.33200  1.000 74.59579  ? 97  LYS B CE  1 
ATOM   3074 N NZ  . LYS B 1 97  ? -10.26200 13.81500  12.71500  1.000 82.84941  ? 97  LYS B NZ  1 
ATOM   3075 N N   . THR B 1 98  ? -3.32100  11.09200  12.38400  1.000 52.26153  ? 98  THR B N   1 
ATOM   3076 C CA  . THR B 1 98  ? -2.41600  10.15100  11.77600  1.000 54.97764  ? 98  THR B CA  1 
ATOM   3077 C C   . THR B 1 98  ? -2.65300  8.75800   12.34500  1.000 52.07730  ? 98  THR B C   1 
ATOM   3078 O O   . THR B 1 98  ? -2.51600  8.56700   13.56300  1.000 54.24071  ? 98  THR B O   1 
ATOM   3079 C CB  . THR B 1 98  ? -0.94400  10.53400  12.00100  1.000 51.90359  ? 98  THR B CB  1 
ATOM   3080 O OG1 . THR B 1 98  ? -0.70500  11.86200  11.55000  1.000 51.59040  ? 98  THR B OG1 1 
ATOM   3081 C CG2 . THR B 1 98  ? -0.08400  9.62700   11.19700  1.000 51.92991  ? 98  THR B CG2 1 
ATOM   3082 N N   . PRO B 1 99  ? -2.94100  7.76600   11.52000  1.000 51.99571  ? 99  PRO B N   1 
ATOM   3083 C CA  . PRO B 1 99  ? -3.06100  6.38900   12.01100  1.000 51.14034  ? 99  PRO B CA  1 
ATOM   3084 C C   . PRO B 1 99  ? -1.70000  5.74300   12.19200  1.000 53.40640  ? 99  PRO B C   1 
ATOM   3085 O O   . PRO B 1 99  ? -0.68700  6.23100   11.68200  1.000 54.32757  ? 99  PRO B O   1 
ATOM   3086 C CB  . PRO B 1 99  ? -3.81700  5.70100   10.88500  1.000 50.00600  ? 99  PRO B CB  1 
ATOM   3087 C CG  . PRO B 1 99  ? -3.39900  6.43500   9.65500   1.000 50.86663  ? 99  PRO B CG  1 
ATOM   3088 C CD  . PRO B 1 99  ? -3.26300  7.87400   10.08300  1.000 50.59554  ? 99  PRO B CD  1 
ATOM   3089 N N   . LYS B 1 100 ? -1.68900  4.60100   12.88500  1.000 51.84569  ? 100 LYS B N   1 
ATOM   3090 C CA  . LYS B 1 100 ? -0.51900  3.73700   12.79500  1.000 56.27780  ? 100 LYS B CA  1 
ATOM   3091 C C   . LYS B 1 100 ? -0.36000  3.30700   11.35100  1.000 52.01413  ? 100 LYS B C   1 
ATOM   3092 O O   . LYS B 1 100 ? -1.33700  2.92200   10.70800  1.000 53.11953  ? 100 LYS B O   1 
ATOM   3093 C CB  . LYS B 1 100 ? -0.60800  2.50300   13.69400  1.000 64.02347  ? 100 LYS B CB  1 
ATOM   3094 C CG  . LYS B 1 100 ? -0.96500  2.78600   15.12500  1.000 77.94092  ? 100 LYS B CG  1 
ATOM   3095 C CD  . LYS B 1 100 ? -1.12400  1.49700   15.91700  1.000 93.20591  ? 100 LYS B CD  1 
ATOM   3096 C CE  . LYS B 1 100 ? -1.64800  1.78000   17.32600  1.000 104.42568 ? 100 LYS B CE  1 
ATOM   3097 N NZ  . LYS B 1 100 ? -1.28200  0.70000   18.29000  1.000 107.91820 ? 100 LYS B NZ  1 
ATOM   3098 N N   . TYR B 1 101 ? 0.84600   3.44600   10.80800  1.000 49.11115  ? 101 TYR B N   1 
ATOM   3099 C CA  . TYR B 1 101 ? 0.98400   3.14800   9.39300   1.000 46.73455  ? 101 TYR B CA  1 
ATOM   3100 C C   . TYR B 1 101 ? 2.37400   2.61200   9.06500   1.000 49.36645  ? 101 TYR B C   1 
ATOM   3101 O O   . TYR B 1 101 ? 3.31700   2.70200   9.85700   1.000 49.16642  ? 101 TYR B O   1 
ATOM   3102 C CB  . TYR B 1 101 ? 0.67700   4.38500   8.55800   1.000 46.71876  ? 101 TYR B CB  1 
ATOM   3103 C CG  . TYR B 1 101 ? 1.83100   5.37500   8.57100   1.000 45.36070  ? 101 TYR B CG  1 
ATOM   3104 C CD1 . TYR B 1 101 ? 2.89400   5.26700   7.64400   1.000 48.16104  ? 101 TYR B CD1 1 
ATOM   3105 C CD2 . TYR B 1 101 ? 1.87700   6.40700   9.50500   1.000 47.01616  ? 101 TYR B CD2 1 
ATOM   3106 C CE1 . TYR B 1 101 ? 3.95100   6.15200   7.67700   1.000 44.57903  ? 101 TYR B CE1 1 
ATOM   3107 C CE2 . TYR B 1 101 ? 2.93500   7.32400   9.51400   1.000 48.29526  ? 101 TYR B CE2 1 
ATOM   3108 C CZ  . TYR B 1 101 ? 3.96100   7.16900   8.59800   1.000 49.44540  ? 101 TYR B CZ  1 
ATOM   3109 O OH  . TYR B 1 101 ? 5.01800   8.04500   8.59800   1.000 51.55881  ? 101 TYR B OH  1 
ATOM   3110 N N   . LYS B 1 102 ? 2.48400   2.04500   7.86700   1.000 46.95300  ? 102 LYS B N   1 
ATOM   3111 C CA  . LYS B 1 102 ? 3.79100   1.79700   7.28000   1.000 51.44301  ? 102 LYS B CA  1 
ATOM   3112 C C   . LYS B 1 102 ? 3.66700   1.96300   5.78100   1.000 47.44516  ? 102 LYS B C   1 
ATOM   3113 O O   . LYS B 1 102 ? 2.56500   1.96200   5.22900   1.000 42.70249  ? 102 LYS B O   1 
ATOM   3114 C CB  . LYS B 1 102 ? 4.33300   0.41500   7.65800   1.000 54.85395  ? 102 LYS B CB  1 
ATOM   3115 C CG  . LYS B 1 102 ? 3.49200   -0.69000  7.18700   1.000 55.22241  ? 102 LYS B CG  1 
ATOM   3116 C CD  . LYS B 1 102 ? 4.07100   -2.07600  7.54400   1.000 62.68646  ? 102 LYS B CD  1 
ATOM   3117 C CE  . LYS B 1 102 ? 4.30200   -2.21500  9.04100   1.000 78.60679  ? 102 LYS B CE  1 
ATOM   3118 N NZ  . LYS B 1 102 ? 4.36500   -3.64800  9.47800   1.000 84.43907  ? 102 LYS B NZ  1 
ATOM   3119 N N   . PHE B 1 103 ? 4.82600   2.20800   5.15000   1.000 43.57628  ? 103 PHE B N   1 
ATOM   3120 C CA  . PHE B 1 103 ? 4.99300   2.24100   3.70700   1.000 44.77116  ? 103 PHE B CA  1 
ATOM   3121 C C   . PHE B 1 103 ? 5.51300   0.87800   3.29600   1.000 46.79772  ? 103 PHE B C   1 
ATOM   3122 O O   . PHE B 1 103 ? 6.45300   0.36600   3.90600   1.000 45.64758  ? 103 PHE B O   1 
ATOM   3123 C CB  . PHE B 1 103 ? 5.99300   3.34000   3.26300   1.000 41.13914  ? 103 PHE B CB  1 
ATOM   3124 C CG  . PHE B 1 103 ? 5.49900   4.74700   3.56400   1.000 43.97633  ? 103 PHE B CG  1 
ATOM   3125 C CD1 . PHE B 1 103 ? 4.15000   4.94700   3.91800   1.000 41.83396  ? 103 PHE B CD1 1 
ATOM   3126 C CD2 . PHE B 1 103 ? 6.34400   5.85000   3.49200   1.000 44.32637  ? 103 PHE B CD2 1 
ATOM   3127 C CE1 . PHE B 1 103 ? 3.64900   6.21700   4.14600   1.000 43.91316  ? 103 PHE B CE1 1 
ATOM   3128 C CE2 . PHE B 1 103 ? 5.86400   7.13900   3.75100   1.000 44.08160  ? 103 PHE B CE2 1 
ATOM   3129 C CZ  . PHE B 1 103 ? 4.51600   7.32700   4.07000   1.000 47.27672  ? 103 PHE B CZ  1 
ATOM   3130 N N   . VAL B 1 104 ? 4.84400   0.24800   2.34100   1.000 41.45760  ? 104 VAL B N   1 
ATOM   3131 C CA  . VAL B 1 104 ? 5.28400   -1.05800  1.88500   1.000 38.54410  ? 104 VAL B CA  1 
ATOM   3132 C C   . VAL B 1 104 ? 5.24100   -1.05100  0.37600   1.000 43.76841  ? 104 VAL B C   1 
ATOM   3133 O O   . VAL B 1 104 ? 4.46400   -0.31300  -0.24700  1.000 43.54996  ? 104 VAL B O   1 
ATOM   3134 C CB  . VAL B 1 104 ? 4.45200   -2.22100  2.44000   1.000 44.71852  ? 104 VAL B CB  1 
ATOM   3135 C CG1 . VAL B 1 104 ? 4.43100   -2.12300  3.97800   1.000 46.36609  ? 104 VAL B CG1 1 
ATOM   3136 C CG2 . VAL B 1 104 ? 3.07400   -2.24600  1.84400   1.000 45.17647  ? 104 VAL B CG2 1 
ATOM   3137 N N   . ARG B 1 105 ? 6.08900   -1.88000  -0.21300  1.000 36.95706  ? 105 ARG B N   1 
ATOM   3138 C CA  . ARG B 1 105 ? 6.08800   -2.08800  -1.64600  1.000 39.92321  ? 105 ARG B CA  1 
ATOM   3139 C C   . ARG B 1 105 ? 5.45200   -3.44100  -1.91000  1.000 44.34742  ? 105 ARG B C   1 
ATOM   3140 O O   . ARG B 1 105 ? 5.92900   -4.46500  -1.40900  1.000 42.68670  ? 105 ARG B O   1 
ATOM   3141 C CB  . ARG B 1 105 ? 7.50900   -2.00900  -2.21700  1.000 42.10505  ? 105 ARG B CB  1 
ATOM   3142 C CG  . ARG B 1 105 ? 7.46500   -2.12700  -3.73600  1.000 39.76793  ? 105 ARG B CG  1 
ATOM   3143 C CD  . ARG B 1 105 ? 8.79400   -1.73300  -4.29200  1.000 43.56049  ? 105 ARG B CD  1 
ATOM   3144 N NE  . ARG B 1 105 ? 8.74200   -1.83300  -5.74500  1.000 39.92321  ? 105 ARG B NE  1 
ATOM   3145 C CZ  . ARG B 1 105 ? 8.43800   -0.82400  -6.55500  1.000 40.76805  ? 105 ARG B CZ  1 
ATOM   3146 N NH1 . ARG B 1 105 ? 8.16200   0.39100   -6.07700  1.000 37.45975  ? 105 ARG B NH1 1 
ATOM   3147 N NH2 . ARG B 1 105 ? 8.47100   -1.02600  -7.87400  1.000 40.12060  ? 105 ARG B NH2 1 
ATOM   3148 N N   . ILE B 1 106 ? 4.36200   -3.45100  -2.67000  1.000 41.86291  ? 106 ILE B N   1 
ATOM   3149 C CA  . ILE B 1 106 ? 3.66000   -4.70400  -2.86400  1.000 44.28426  ? 106 ILE B CA  1 
ATOM   3150 C C   . ILE B 1 106 ? 4.18500   -5.41000  -4.09800  1.000 44.56850  ? 106 ILE B C   1 
ATOM   3151 O O   . ILE B 1 106 ? 4.83900   -4.81900  -4.97600  1.000 42.75513  ? 106 ILE B O   1 
ATOM   3152 C CB  . ILE B 1 106 ? 2.13500   -4.52800  -2.95100  1.000 41.29706  ? 106 ILE B CB  1 
ATOM   3153 C CG1 . ILE B 1 106 ? 1.73000   -3.58100  -4.05100  1.000 38.44408  ? 106 ILE B CG1 1 
ATOM   3154 C CG2 . ILE B 1 106 ? 1.55400   -4.16800  -1.60300  1.000 48.06892  ? 106 ILE B CG2 1 
ATOM   3155 C CD1 . ILE B 1 106 ? 0.31000   -3.86600  -4.42800  1.000 47.46622  ? 106 ILE B CD1 1 
ATOM   3156 N N   . GLN B 1 107 ? 3.86300   -6.74900  -4.16700  1.000 41.36022  ? 107 GLN B N   1 
ATOM   3157 C CA  . GLN B 1 107 ? 4.21400   -7.54300  -5.35000  1.000 45.42124  ? 107 GLN B CA  1 
ATOM   3158 C C   . GLN B 1 107 ? 3.04800   -7.60300  -6.31300  1.000 42.37613  ? 107 GLN B C   1 
ATOM   3159 O O   . GLN B 1 107 ? 1.87300   -7.48100  -5.91400  1.000 40.92070  ? 107 GLN B O   1 
ATOM   3160 C CB  . GLN B 1 107 ? 4.60900   -8.98500  -5.00900  1.000 49.43224  ? 107 GLN B CB  1 
ATOM   3161 C CG  . GLN B 1 107 ? 5.63400   -9.08100  -3.91200  1.000 54.82236  ? 107 GLN B CG  1 
ATOM   3162 C CD  . GLN B 1 107 ? 6.96700   -8.52600  -4.37200  1.000 54.53285  ? 107 GLN B CD  1 
ATOM   3163 O OE1 . GLN B 1 107 ? 7.43400   -8.86600  -5.46800  1.000 55.73300  ? 107 GLN B OE1 1 
ATOM   3164 N NE2 . GLN B 1 107 ? 7.55900   -7.61900  -3.57000  1.000 56.78312  ? 107 GLN B NE2 1 
ATOM   3165 N N   . PRO B 1 108 ? 3.39200   -7.83800  -7.55800  1.000 40.62066  ? 108 PRO B N   1 
ATOM   3166 C CA  . PRO B 1 108 ? 2.37700   -8.10100  -8.57100  1.000 44.51586  ? 108 PRO B CA  1 
ATOM   3167 C C   . PRO B 1 108 ? 1.47300   -9.24400  -8.13400  1.000 41.83660  ? 108 PRO B C   1 
ATOM   3168 O O   . PRO B 1 108 ? 1.90900   -10.24900 -7.56800  1.000 42.06557  ? 108 PRO B O   1 
ATOM   3169 C CB  . PRO B 1 108 ? 3.22700   -8.42700  -9.82400  1.000 45.27385  ? 108 PRO B CB  1 
ATOM   3170 C CG  . PRO B 1 108 ? 4.68600   -8.48200  -9.30300  1.000 47.65571  ? 108 PRO B CG  1 
ATOM   3171 C CD  . PRO B 1 108 ? 4.72300   -7.58100  -8.17100  1.000 45.62126  ? 108 PRO B CD  1 
ATOM   3172 N N   . GLY B 1 109 ? 0.18600   -9.06600  -8.36200  1.000 42.21032  ? 109 GLY B N   1 
ATOM   3173 C CA  . GLY B 1 109 ? -0.77900  -10.03400 -7.94800  1.000 40.08902  ? 109 GLY B CA  1 
ATOM   3174 C C   . GLY B 1 109 ? -1.42500  -9.71500  -6.62000  1.000 42.82092  ? 109 GLY B C   1 
ATOM   3175 O O   . GLY B 1 109 ? -2.52100  -10.21600 -6.35200  1.000 42.04451  ? 109 GLY B O   1 
ATOM   3176 N N   . GLN B 1 110 ? -0.80200  -8.86800  -5.78400  1.000 39.09679  ? 110 GLN B N   1 
ATOM   3177 C CA  . GLN B 1 110 ? -1.41700  -8.49400  -4.51700  1.000 43.36046  ? 110 GLN B CA  1 
ATOM   3178 C C   . GLN B 1 110 ? -2.43700  -7.36500  -4.72400  1.000 40.93912  ? 110 GLN B C   1 
ATOM   3179 O O   . GLN B 1 110 ? -2.35000  -6.58500  -5.68600  1.000 40.28115  ? 110 GLN B O   1 
ATOM   3180 C CB  . GLN B 1 110 ? -0.34200  -8.09300  -3.50600  1.000 39.55737  ? 110 GLN B CB  1 
ATOM   3181 C CG  . GLN B 1 110 ? 0.51400   -9.29800  -3.02000  1.000 46.57927  ? 110 GLN B CG  1 
ATOM   3182 C CD  . GLN B 1 110 ? -0.29900  -10.47600 -2.44100  1.000 54.98291  ? 110 GLN B CD  1 
ATOM   3183 O OE1 . GLN B 1 110 ? -0.94700  -10.36500 -1.37700  1.000 61.93374  ? 110 GLN B OE1 1 
ATOM   3184 N NE2 . GLN B 1 110 ? -0.28600  -11.60500 -3.14700  1.000 51.35089  ? 110 GLN B NE2 1 
ATOM   3185 N N   . THR B 1 111 ? -3.46900  -7.32700  -3.86400  1.000 36.22803  ? 111 THR B N   1 
ATOM   3186 C CA  . THR B 1 111 ? -4.51000  -6.32200  -4.01400  1.000 36.88337  ? 111 THR B CA  1 
ATOM   3187 C C   . THR B 1 111 ? -4.40800  -5.23700  -2.94100  1.000 37.27552  ? 111 THR B C   1 
ATOM   3188 O O   . THR B 1 111 ? -3.79400  -5.40000  -1.89500  1.000 39.77845  ? 111 THR B O   1 
ATOM   3189 C CB  . THR B 1 111 ? -5.92200  -6.97600  -3.89200  1.000 38.20458  ? 111 THR B CB  1 
ATOM   3190 O OG1 . THR B 1 111 ? -5.91400  -7.72300  -2.68900  1.000 39.17312  ? 111 THR B OG1 1 
ATOM   3191 C CG2 . THR B 1 111 ? -6.19700  -7.95400  -5.02600  1.000 37.45712  ? 111 THR B CG2 1 
ATOM   3192 N N   . PHE B 1 112 ? -5.14900  -4.15700  -3.15800  1.000 36.40963  ? 112 PHE B N   1 
ATOM   3193 C CA  . PHE B 1 112 ? -5.26800  -3.08500  -2.18500  1.000 41.08914  ? 112 PHE B CA  1 
ATOM   3194 C C   . PHE B 1 112 ? -6.47700  -2.22700  -2.51500  1.000 38.12826  ? 112 PHE B C   1 
ATOM   3195 O O   . PHE B 1 112 ? -7.01900  -2.25700  -3.62600  1.000 37.83085  ? 112 PHE B O   1 
ATOM   3196 C CB  . PHE B 1 112 ? -4.02000  -2.18500  -2.13900  1.000 38.04667  ? 112 PHE B CB  1 
ATOM   3197 C CG  . PHE B 1 112 ? -3.60100  -1.68200  -3.50200  1.000 38.23353  ? 112 PHE B CG  1 
ATOM   3198 C CD1 . PHE B 1 112 ? -2.71300  -2.41500  -4.27600  1.000 36.84652  ? 112 PHE B CD1 1 
ATOM   3199 C CD2 . PHE B 1 112 ? -4.08800  -0.46300  -3.98400  1.000 41.21547  ? 112 PHE B CD2 1 
ATOM   3200 C CE1 . PHE B 1 112 ? -2.27700  -1.91700  -5.53400  1.000 37.87559  ? 112 PHE B CE1 1 
ATOM   3201 C CE2 . PHE B 1 112 ? -3.71900  0.04800   -5.24900  1.000 39.39946  ? 112 PHE B CE2 1 
ATOM   3202 C CZ  . PHE B 1 112 ? -2.79100  -0.67800  -6.02100  1.000 35.60164  ? 112 PHE B CZ  1 
ATOM   3203 N N   . SER B 1 113 ? -6.87100  -1.43900  -1.53100  1.000 38.37302  ? 113 SER B N   1 
ATOM   3204 C CA  . SER B 1 113 ? -7.96800  -0.50400  -1.67700  1.000 38.53094  ? 113 SER B CA  1 
ATOM   3205 C C   . SER B 1 113 ? -7.42400  0.83500   -2.11500  1.000 34.89103  ? 113 SER B C   1 
ATOM   3206 O O   . SER B 1 113 ? -6.43800  1.27800   -1.56700  1.000 37.95718  ? 113 SER B O   1 
ATOM   3207 C CB  . SER B 1 113 ? -8.69700  -0.34000  -0.32700  1.000 38.34407  ? 113 SER B CB  1 
ATOM   3208 O OG  . SER B 1 113 ? -9.17500  -1.60300  0.13000   1.000 38.83624  ? 113 SER B OG  1 
ATOM   3209 N N   . VAL B 1 114 ? -8.12100  1.48200   -3.04100  1.000 34.75943  ? 114 VAL B N   1 
ATOM   3210 C CA  . VAL B 1 114 ? -7.80200  2.79600   -3.58300  1.000 37.88612  ? 114 VAL B CA  1 
ATOM   3211 C C   . VAL B 1 114 ? -8.85200  3.74000   -3.06000  1.000 37.85980  ? 114 VAL B C   1 
ATOM   3212 O O   . VAL B 1 114 ? -10.04900 3.49000   -3.25700  1.000 38.77307  ? 114 VAL B O   1 
ATOM   3213 C CB  . VAL B 1 114 ? -7.83100  2.82000   -5.14000  1.000 37.50450  ? 114 VAL B CB  1 
ATOM   3214 C CG1 . VAL B 1 114 ? -7.68500  4.30600   -5.65300  1.000 36.23856  ? 114 VAL B CG1 1 
ATOM   3215 C CG2 . VAL B 1 114 ? -6.73600  1.92300   -5.77400  1.000 35.43056  ? 114 VAL B CG2 1 
ATOM   3216 N N   . LEU B 1 115 ? -8.42200  4.82100   -2.42500  1.000 36.04380  ? 115 LEU B N   1 
ATOM   3217 C CA  . LEU B 1 115 ? -9.30700  5.92700   -2.08100  1.000 35.19369  ? 115 LEU B CA  1 
ATOM   3218 C C   . LEU B 1 115 ? -9.12000  7.00800   -3.14100  1.000 40.89174  ? 115 LEU B C   1 
ATOM   3219 O O   . LEU B 1 115 ? -8.19000  7.81100   -3.07500  1.000 40.46801  ? 115 LEU B O   1 
ATOM   3220 C CB  . LEU B 1 115 ? -9.01900  6.40600   -0.65700  1.000 34.36201  ? 115 LEU B CB  1 
ATOM   3221 C CG  . LEU B 1 115 ? -9.86300  7.56700   -0.18500  1.000 38.48356  ? 115 LEU B CG  1 
ATOM   3222 C CD1 . LEU B 1 115 ? -11.29100 6.89000   0.04500   1.000 38.11246  ? 115 LEU B CD1 1 
ATOM   3223 C CD2 . LEU B 1 115 ? -9.37500  8.22800   1.14100   1.000 40.66540  ? 115 LEU B CD2 1 
ATOM   3224 N N   . ALA B 1 116 ? -9.98000  7.00400   -4.16100  1.000 38.45987  ? 116 ALA B N   1 
ATOM   3225 C CA  . ALA B 1 116 ? -9.90600  8.04600   -5.17600  1.000 36.30962  ? 116 ALA B CA  1 
ATOM   3226 C C   . ALA B 1 116 ? -10.28200 9.40100   -4.58800  1.000 41.05229  ? 116 ALA B C   1 
ATOM   3227 O O   . ALA B 1 116 ? -11.28000 9.53300   -3.86500  1.000 40.29430  ? 116 ALA B O   1 
ATOM   3228 C CB  . ALA B 1 116 ? -10.81900 7.68900   -6.36100  1.000 39.61264  ? 116 ALA B CB  1 
ATOM   3229 N N   . CYS B 1 117 ? -9.45100  10.40600  -4.84300  1.000 36.60965  ? 117 CYS B N   1 
ATOM   3230 C CA  . CYS B 1 117 ? -9.64400  11.73900  -4.29700  1.000 38.98362  ? 117 CYS B CA  1 
ATOM   3231 C C   . CYS B 1 117 ? -9.45000  12.80300  -5.36600  1.000 43.19465  ? 117 CYS B C   1 
ATOM   3232 O O   . CYS B 1 117 ? -8.60700  12.66700  -6.27400  1.000 39.49158  ? 117 CYS B O   1 
ATOM   3233 C CB  . CYS B 1 117 ? -8.64900  12.07500  -3.18700  1.000 41.71290  ? 117 CYS B CB  1 
ATOM   3234 S SG  . CYS B 1 117 ? -8.67200  11.05100  -1.74900  1.000 47.84521  ? 117 CYS B SG  1 
ATOM   3235 N N   . TYR B 1 118 ? -10.14000 13.92100  -5.16300  1.000 41.33127  ? 118 TYR B N   1 
ATOM   3236 C CA  . TYR B 1 118 ? -10.01100 15.13700  -5.96000  1.000 44.93960  ? 118 TYR B CA  1 
ATOM   3237 C C   . TYR B 1 118 ? -9.99400  16.34600  -5.03800  1.000 45.79760  ? 118 TYR B C   1 
ATOM   3238 O O   . TYR B 1 118 ? -10.78500 16.41700  -4.07400  1.000 41.57341  ? 118 TYR B O   1 
ATOM   3239 C CB  . TYR B 1 118 ? -11.16200 15.24300  -6.98000  1.000 43.44995  ? 118 TYR B CB  1 
ATOM   3240 C CG  . TYR B 1 118 ? -11.13500 14.03900  -7.86700  1.000 42.70249  ? 118 TYR B CG  1 
ATOM   3241 C CD1 . TYR B 1 118 ? -10.32400 14.02300  -8.97700  1.000 42.39719  ? 118 TYR B CD1 1 
ATOM   3242 C CD2 . TYR B 1 118 ? -11.82800 12.87200  -7.53400  1.000 42.06031  ? 118 TYR B CD2 1 
ATOM   3243 C CE1 . TYR B 1 118 ? -10.21600 12.91600  -9.76800  1.000 40.32062  ? 118 TYR B CE1 1 
ATOM   3244 C CE2 . TYR B 1 118 ? -11.75000 11.74100  -8.34200  1.000 40.63119  ? 118 TYR B CE2 1 
ATOM   3245 C CZ  . TYR B 1 118 ? -10.90000 11.79500  -9.45400  1.000 41.41286  ? 118 TYR B CZ  1 
ATOM   3246 O OH  . TYR B 1 118 ? -10.73700 10.73400  -10.30000 1.000 39.41525  ? 118 TYR B OH  1 
ATOM   3247 N N   . ASN B 1 119 ? -9.04500  17.27000  -5.28900  1.000 44.18424  ? 119 ASN B N   1 
ATOM   3248 C CA  . ASN B 1 119 ? -8.92400  18.51300  -4.50600  1.000 47.71625  ? 119 ASN B CA  1 
ATOM   3249 C C   . ASN B 1 119 ? -8.79800  18.23900  -3.00200  1.000 46.31345  ? 119 ASN B C   1 
ATOM   3250 O O   . ASN B 1 119 ? -9.38200  18.93100  -2.14800  1.000 46.17133  ? 119 ASN B O   1 
ATOM   3251 C CB  . ASN B 1 119 ? -10.11900 19.43200  -4.77800  1.000 52.42471  ? 119 ASN B CB  1 
ATOM   3252 C CG  . ASN B 1 119 ? -10.29800 19.70800  -6.23500  1.000 53.77750  ? 119 ASN B CG  1 
ATOM   3253 O OD1 . ASN B 1 119 ? -9.46400  20.38400  -6.86600  1.000 58.98865  ? 119 ASN B OD1 1 
ATOM   3254 N ND2 . ASN B 1 119 ? -11.37000 19.19900  -6.79300  1.000 52.90898  ? 119 ASN B ND2 1 
ATOM   3255 N N   . GLY B 1 120 ? -8.09600  17.17100  -2.67100  1.000 44.33163  ? 120 GLY B N   1 
ATOM   3256 C CA  . GLY B 1 120 ? -7.97900  16.78100  -1.28400  1.000 42.92883  ? 120 GLY B CA  1 
ATOM   3257 C C   . GLY B 1 120 ? -9.23100  16.12800  -0.70800  1.000 45.22648  ? 120 GLY B C   1 
ATOM   3258 O O   . GLY B 1 120 ? -9.24800  15.86200  0.49000   1.000 43.11570  ? 120 GLY B O   1 
ATOM   3259 N N   . SER B 1 121 ? -10.29800 15.93600  -1.49000  1.000 43.05253  ? 121 SER B N   1 
ATOM   3260 C CA  . SER B 1 121 ? -11.54900 15.37800  -0.90900  1.000 45.20016  ? 121 SER B CA  1 
ATOM   3261 C C   . SER B 1 121 ? -11.75200 13.94700  -1.39600  1.000 45.75285  ? 121 SER B C   1 
ATOM   3262 O O   . SER B 1 121 ? -11.91100 13.73500  -2.61400  1.000 44.17109  ? 121 SER B O   1 
ATOM   3263 C CB  . SER B 1 121 ? -12.79800 16.19800  -1.26700  1.000 49.12694  ? 121 SER B CB  1 
ATOM   3264 O OG  . SER B 1 121 ? -12.89900 17.36900  -0.52000  1.000 56.95946  ? 121 SER B OG  1 
ATOM   3265 N N   . PRO B 1 122 ? -11.83700 12.96300  -0.49300  1.000 47.53201  ? 122 PRO B N   1 
ATOM   3266 C CA  . PRO B 1 122 ? -12.16000 11.58500  -0.92400  1.000 46.96089  ? 122 PRO B CA  1 
ATOM   3267 C C   . PRO B 1 122 ? -13.47400 11.53800  -1.66700  1.000 44.40532  ? 122 PRO B C   1 
ATOM   3268 O O   . PRO B 1 122 ? -14.48100 12.05900  -1.18500  1.000 45.09225  ? 122 PRO B O   1 
ATOM   3269 C CB  . PRO B 1 122 ? -12.23400 10.80300  0.38700   1.000 44.54481  ? 122 PRO B CB  1 
ATOM   3270 C CG  . PRO B 1 122 ? -11.26900 11.52300  1.29500   1.000 49.03746  ? 122 PRO B CG  1 
ATOM   3271 C CD  . PRO B 1 122 ? -11.42400 13.02400  0.92400   1.000 45.49493  ? 122 PRO B CD  1 
ATOM   3272 N N   . SER B 1 123 ? -13.48100 10.87500  -2.82500  1.000 42.30507  ? 123 SER B N   1 
ATOM   3273 C CA  . SER B 1 123 ? -14.70400 10.68900  -3.60500  1.000 47.92154  ? 123 SER B CA  1 
ATOM   3274 C C   . SER B 1 123 ? -15.17500 9.24400   -3.71100  1.000 45.94761  ? 123 SER B C   1 
ATOM   3275 O O   . SER B 1 123 ? -16.38200 9.00100   -3.85700  1.000 46.06079  ? 123 SER B O   1 
ATOM   3276 C CB  . SER B 1 123 ? -14.52500 11.24400  -5.00600  1.000 45.87919  ? 123 SER B CB  1 
ATOM   3277 O OG  . SER B 1 123 ? -13.62600 10.44000  -5.66900  1.000 49.52699  ? 123 SER B OG  1 
ATOM   3278 N N   . GLY B 1 124 ? -14.29800 8.25600   -3.61700  1.000 42.89988  ? 124 GLY B N   1 
ATOM   3279 C CA  . GLY B 1 124 ? -14.78500 6.88500   -3.71400  1.000 41.21547  ? 124 GLY B CA  1 
ATOM   3280 C C   . GLY B 1 124 ? -13.72800 5.87800   -3.30800  1.000 44.00528  ? 124 GLY B C   1 
ATOM   3281 O O   . GLY B 1 124 ? -12.52400 6.17500   -3.22300  1.000 40.59697  ? 124 GLY B O   1 
ATOM   3282 N N   . VAL B 1 125 ? -14.17900 4.65700   -3.08800  1.000 37.02549  ? 125 VAL B N   1 
ATOM   3283 C CA  . VAL B 1 125 ? -13.25100 3.63700   -2.65100  1.000 39.88110  ? 125 VAL B CA  1 
ATOM   3284 C C   . VAL B 1 125 ? -13.51000 2.35100   -3.44500  1.000 42.34981  ? 125 VAL B C   1 
ATOM   3285 O O   . VAL B 1 125 ? -14.67300 1.95500   -3.64900  1.000 41.89450  ? 125 VAL B O   1 
ATOM   3286 C CB  . VAL B 1 125 ? -13.32900 3.44800   -1.11800  1.000 38.17037  ? 125 VAL B CB  1 
ATOM   3287 C CG1 . VAL B 1 125 ? -14.66100 2.92300   -0.71900  1.000 43.46574  ? 125 VAL B CG1 1 
ATOM   3288 C CG2 . VAL B 1 125 ? -12.26200 2.50100   -0.62400  1.000 39.40472  ? 125 VAL B CG2 1 
ATOM   3289 N N   . TYR B 1 126 ? -12.42500 1.68700   -3.90700  1.000 33.46191  ? 126 TYR B N   1 
ATOM   3290 C CA  . TYR B 1 126 ? -12.55700 0.41800   -4.64200  1.000 37.96245  ? 126 TYR B CA  1 
ATOM   3291 C C   . TYR B 1 126 ? -11.29700 -0.40800  -4.53400  1.000 40.91543  ? 126 TYR B C   1 
ATOM   3292 O O   . TYR B 1 126 ? -10.21100 0.12300   -4.27000  1.000 37.77558  ? 126 TYR B O   1 
ATOM   3293 C CB  . TYR B 1 126 ? -12.92700 0.62500   -6.11300  1.000 34.18568  ? 126 TYR B CB  1 
ATOM   3294 C CG  . TYR B 1 126 ? -11.97300 1.52500   -6.86200  1.000 39.09153  ? 126 TYR B CG  1 
ATOM   3295 C CD1 . TYR B 1 126 ? -10.83900 1.00000   -7.43800  1.000 39.49158  ? 126 TYR B CD1 1 
ATOM   3296 C CD2 . TYR B 1 126 ? -12.20500 2.88900   -6.95500  1.000 40.21798  ? 126 TYR B CD2 1 
ATOM   3297 C CE1 . TYR B 1 126 ? -9.93500  1.85700   -8.11900  1.000 38.13352  ? 126 TYR B CE1 1 
ATOM   3298 C CE2 . TYR B 1 126 ? -11.31700 3.73600   -7.62600  1.000 39.25207  ? 126 TYR B CE2 1 
ATOM   3299 C CZ  . TYR B 1 126 ? -10.20400 3.20300   -8.21100  1.000 36.85179  ? 126 TYR B CZ  1 
ATOM   3300 O OH  . TYR B 1 126 ? -9.32600  4.06000   -8.88700  1.000 40.63645  ? 126 TYR B OH  1 
ATOM   3301 N N   . GLN B 1 127 ? -11.42700 -1.70200  -4.84300  1.000 33.16713  ? 127 GLN B N   1 
ATOM   3302 C CA  . GLN B 1 127 ? -10.29400 -2.63800  -4.81300  1.000 39.74950  ? 127 GLN B CA  1 
ATOM   3303 C C   . GLN B 1 127 ? -9.58500  -2.68900  -6.14900  1.000 38.84413  ? 127 GLN B C   1 
ATOM   3304 O O   . GLN B 1 127 ? -10.22900 -2.68100  -7.19100  1.000 41.47076  ? 127 GLN B O   1 
ATOM   3305 C CB  . GLN B 1 127 ? -10.71400 -4.08400  -4.54700  1.000 42.03925  ? 127 GLN B CB  1 
ATOM   3306 C CG  . GLN B 1 127 ? -11.09300 -4.35200  -3.16800  1.000 42.04451  ? 127 GLN B CG  1 
ATOM   3307 C CD  . GLN B 1 127 ? -9.90300  -4.22600  -2.19700  1.000 40.13902  ? 127 GLN B CD  1 
ATOM   3308 O OE1 . GLN B 1 127 ? -9.76700  -3.20300  -1.56200  1.000 42.17611  ? 127 GLN B OE1 1 
ATOM   3309 N NE2 . GLN B 1 127 ? -9.16400  -5.31000  -1.97000  1.000 39.82583  ? 127 GLN B NE2 1 
ATOM   3310 N N   . CYS B 1 128 ? -8.27300  -2.88100  -6.10200  1.000 37.04918  ? 128 CYS B N   1 
ATOM   3311 C CA  . CYS B 1 128 ? -7.42700  -3.03000  -7.29200  1.000 41.28653  ? 128 CYS B CA  1 
ATOM   3312 C C   . CYS B 1 128 ? -6.44000  -4.14000  -7.04600  1.000 38.27827  ? 128 CYS B C   1 
ATOM   3313 O O   . CYS B 1 128 ? -5.97300  -4.30400  -5.91800  1.000 42.88409  ? 128 CYS B O   1 
ATOM   3314 C CB  . CYS B 1 128 ? -6.60000  -1.75300  -7.57500  1.000 37.50450  ? 128 CYS B CB  1 
ATOM   3315 S SG  . CYS B 1 128 ? -7.53600  -0.69500  -8.58700  1.000 47.29778  ? 128 CYS B SG  1 
ATOM   3316 N N   . ALA B 1 129 ? -5.99400  -4.82000  -8.11300  1.000 43.13412  ? 129 ALA B N   1 
ATOM   3317 C CA  . ALA B 1 129 ? -4.81200  -5.66200  -7.99600  1.000 36.00958  ? 129 ALA B CA  1 
ATOM   3318 C C   . ALA B 1 129 ? -3.64400  -4.98300  -8.72300  1.000 35.68849  ? 129 ALA B C   1 
ATOM   3319 O O   . ALA B 1 129 ? -3.83700  -4.25000  -9.68700  1.000 37.87033  ? 129 ALA B O   1 
ATOM   3320 C CB  . ALA B 1 129 ? -5.00000  -7.04600  -8.61000  1.000 35.10684  ? 129 ALA B CB  1 
ATOM   3321 N N   . MET B 1 130 ? -2.44800  -5.19800  -8.22800  1.000 35.38845  ? 130 MET B N   1 
ATOM   3322 C CA  . MET B 1 130 ? -1.23400  -4.82500  -9.01200  1.000 35.49636  ? 130 MET B CA  1 
ATOM   3323 C C   . MET B 1 130 ? -1.08000  -5.90900  -10.08200 1.000 33.21188  ? 130 MET B C   1 
ATOM   3324 O O   . MET B 1 130 ? -0.84000  -7.07200  -9.75100  1.000 36.38594  ? 130 MET B O   1 
ATOM   3325 C CB  . MET B 1 130 ? -0.05400  -4.73700  -8.05800  1.000 33.69615  ? 130 MET B CB  1 
ATOM   3326 C CG  . MET B 1 130 ? 1.35400   -4.55700  -8.81700  1.000 36.44121  ? 130 MET B CG  1 
ATOM   3327 S SD  . MET B 1 130 ? 1.32100   -2.90700  -9.51100  1.000 38.78360  ? 130 MET B SD  1 
ATOM   3328 C CE  . MET B 1 130 ? 1.34500   -1.92400  -8.09100  1.000 37.10445  ? 130 MET B CE  1 
ATOM   3329 N N   . ARG B 1 131 ? -1.31800  -5.55800  -11.35700 1.000 34.04619  ? 131 ARG B N   1 
ATOM   3330 C CA  . ARG B 1 131 ? -1.18600  -6.48200  -12.46900 1.000 34.30411  ? 131 ARG B CA  1 
ATOM   3331 C C   . ARG B 1 131 ? 0.27200   -6.95100  -12.62300 1.000 38.97309  ? 131 ARG B C   1 
ATOM   3332 O O   . ARG B 1 131 ? 1.20800   -6.25800  -12.18700 1.000 36.63071  ? 131 ARG B O   1 
ATOM   3333 C CB  . ARG B 1 131 ? -1.62000  -5.81300  -13.76600 1.000 34.76733  ? 131 ARG B CB  1 
ATOM   3334 C CG  . ARG B 1 131 ? -3.00900  -5.16600  -13.75600 1.000 40.26272  ? 131 ARG B CG  1 
ATOM   3335 C CD  . ARG B 1 131 ? -4.05600  -6.19700  -13.40800 1.000 39.51000  ? 131 ARG B CD  1 
ATOM   3336 N NE  . ARG B 1 131 ? -3.87700  -7.45200  -14.11700 1.000 39.05731  ? 131 ARG B NE  1 
ATOM   3337 C CZ  . ARG B 1 131 ? -4.53700  -8.57400  -13.82000 1.000 41.28127  ? 131 ARG B CZ  1 
ATOM   3338 N NH1 . ARG B 1 131 ? -5.52200  -8.58200  -12.89900 1.000 38.23880  ? 131 ARG B NH1 1 
ATOM   3339 N NH2 . ARG B 1 131 ? -4.21200  -9.71100  -14.46300 1.000 39.37577  ? 131 ARG B NH2 1 
ATOM   3340 N N   . PRO B 1 132 ? 0.48500   -8.13100  -13.24000 1.000 41.30232  ? 132 PRO B N   1 
ATOM   3341 C CA  . PRO B 1 132 ? 1.86600   -8.58100  -13.51700 1.000 40.56276  ? 132 PRO B CA  1 
ATOM   3342 C C   . PRO B 1 132 ? 2.67800   -7.57900  -14.32500 1.000 41.01544  ? 132 PRO B C   1 
ATOM   3343 O O   . PRO B 1 132 ? 3.93800   -7.59500  -14.25600 1.000 38.61779  ? 132 PRO B O   1 
ATOM   3344 C CB  . PRO B 1 132 ? 1.67100   -9.88000  -14.29200 1.000 37.30710  ? 132 PRO B CB  1 
ATOM   3345 C CG  . PRO B 1 132 ? 0.27500   -10.43600 -13.70200 1.000 37.01760  ? 132 PRO B CG  1 
ATOM   3346 C CD  . PRO B 1 132 ? -0.54000  -9.17200  -13.49600 1.000 39.29682  ? 132 PRO B CD  1 
ATOM   3347 N N   . ASN B 1 133 ? 2.01800   -6.74000  -15.13500 1.000 37.38343  ? 133 ASN B N   1 
ATOM   3348 C CA  . ASN B 1 133 ? 2.75800   -5.71300  -15.87500 1.000 38.82044  ? 133 ASN B CA  1 
ATOM   3349 C C   . ASN B 1 133 ? 2.85900   -4.41000  -15.09300 1.000 38.71254  ? 133 ASN B C   1 
ATOM   3350 O O   . ASN B 1 133 ? 3.17200   -3.36900  -15.68200 1.000 37.58082  ? 133 ASN B O   1 
ATOM   3351 C CB  . ASN B 1 133 ? 2.10600   -5.46400  -17.25300 1.000 37.06234  ? 133 ASN B CB  1 
ATOM   3352 C CG  . ASN B 1 133 ? 0.70300   -4.82100  -17.15500 1.000 37.00444  ? 133 ASN B CG  1 
ATOM   3353 O OD1 . ASN B 1 133 ? 0.17900   -4.56400  -16.08100 1.000 37.57556  ? 133 ASN B OD1 1 
ATOM   3354 N ND2 . ASN B 1 133 ? 0.10000   -4.56700  -18.31400 1.000 39.93374  ? 133 ASN B ND2 1 
ATOM   3355 N N   . PHE B 1 134 ? 2.56400   -4.43100  -13.78700 1.000 33.14082  ? 134 PHE B N   1 
ATOM   3356 C CA  . PHE B 1 134 ? 2.79300   -3.32200  -12.85700 1.000 32.89079  ? 134 PHE B CA  1 
ATOM   3357 C C   . PHE B 1 134 ? 1.88500   -2.10800  -13.07900 1.000 36.35699  ? 134 PHE B C   1 
ATOM   3358 O O   . PHE B 1 134 ? 2.23700   -0.99000  -12.63500 1.000 42.30507  ? 134 PHE B O   1 
ATOM   3359 C CB  . PHE B 1 134 ? 4.28300   -2.84500  -12.90300 1.000 37.79927  ? 134 PHE B CB  1 
ATOM   3360 C CG  . PHE B 1 134 ? 5.21200   -3.88600  -12.41900 1.000 38.22827  ? 134 PHE B CG  1 
ATOM   3361 C CD1 . PHE B 1 134 ? 5.34100   -4.14200  -11.06300 1.000 41.51550  ? 134 PHE B CD1 1 
ATOM   3362 C CD2 . PHE B 1 134 ? 5.91400   -4.67200  -13.34000 1.000 43.47100  ? 134 PHE B CD2 1 
ATOM   3363 C CE1 . PHE B 1 134 ? 6.22600   -5.21000  -10.61400 1.000 43.36836  ? 134 PHE B CE1 1 
ATOM   3364 C CE2 . PHE B 1 134 ? 6.80100   -5.70000  -12.91300 1.000 45.83971  ? 134 PHE B CE2 1 
ATOM   3365 C CZ  . PHE B 1 134 ? 6.95200   -5.94500  -11.53900 1.000 44.51060  ? 134 PHE B CZ  1 
ATOM   3366 N N   . THR B 1 135 ? 0.77100   -2.24700  -13.78900 1.000 36.89390  ? 135 THR B N   1 
ATOM   3367 C CA  . THR B 1 135 ? -0.26700  -1.24300  -13.86600 1.000 31.60642  ? 135 THR B CA  1 
ATOM   3368 C C   . THR B 1 135 ? -1.42200  -1.67100  -12.94900 1.000 34.51203  ? 135 THR B C   1 
ATOM   3369 O O   . THR B 1 135 ? -1.47900  -2.80600  -12.47800 1.000 33.76457  ? 135 THR B O   1 
ATOM   3370 C CB  . THR B 1 135 ? -0.78700  -1.08900  -15.30500 1.000 33.05660  ? 135 THR B CB  1 
ATOM   3371 O OG1 . THR B 1 135 ? -1.39500  -2.29200  -15.79500 1.000 36.97285  ? 135 THR B OG1 1 
ATOM   3372 C CG2 . THR B 1 135 ? 0.42200   -0.70500  -16.28200 1.000 34.44097  ? 135 THR B CG2 1 
ATOM   3373 N N   . ILE B 1 136 ? -2.34300  -0.77100  -12.73200 1.000 29.92990  ? 136 ILE B N   1 
ATOM   3374 C CA  . ILE B 1 136 ? -3.60600  -1.18300  -12.06800 1.000 32.73287  ? 136 ILE B CA  1 
ATOM   3375 C C   . ILE B 1 136 ? -4.72600  -0.74600  -12.96900 1.000 37.35448  ? 136 ILE B C   1 
ATOM   3376 O O   . ILE B 1 136 ? -4.61200  0.24600   -13.68000 1.000 35.88851  ? 136 ILE B O   1 
ATOM   3377 C CB  . ILE B 1 136 ? -3.76600  -0.59600  -10.66600 1.000 37.93876  ? 136 ILE B CB  1 
ATOM   3378 C CG1 . ILE B 1 136 ? -3.91200  0.94100   -10.70700 1.000 39.17838  ? 136 ILE B CG1 1 
ATOM   3379 C CG2 . ILE B 1 136 ? -2.55200  -1.03700  -9.78000  1.000 38.80202  ? 136 ILE B CG2 1 
ATOM   3380 C CD1 . ILE B 1 136 ? -4.09300  1.59800   -9.33800  1.000 36.76757  ? 136 ILE B CD1 1 
ATOM   3381 N N   . LYS B 1 137 ? -5.85500  -1.48700  -12.92700 1.000 40.79436  ? 137 LYS B N   1 
ATOM   3382 C CA  . LYS B 1 137 ? -7.01100  -1.08200  -13.69700 1.000 37.93613  ? 137 LYS B CA  1 
ATOM   3383 C C   . LYS B 1 137 ? -7.89400  -0.30000  -12.74200 1.000 38.74149  ? 137 LYS B C   1 
ATOM   3384 O O   . LYS B 1 137 ? -8.72900  -0.86700  -12.05800 1.000 38.66516  ? 137 LYS B O   1 
ATOM   3385 C CB  . LYS B 1 137 ? -7.66200  -2.32900  -14.30300 1.000 36.84915  ? 137 LYS B CB  1 
ATOM   3386 C CG  . LYS B 1 137 ? -6.73100  -3.21000  -15.19200 1.000 45.98709  ? 137 LYS B CG  1 
ATOM   3387 C CD  . LYS B 1 137 ? -7.57700  -4.38000  -15.77500 1.000 53.38798  ? 137 LYS B CD  1 
ATOM   3388 C CE  . LYS B 1 137 ? -6.78100  -5.46700  -16.48800 1.000 56.96736  ? 137 LYS B CE  1 
ATOM   3389 N NZ  . LYS B 1 137 ? -7.67500  -6.69400  -16.57800 1.000 60.41777  ? 137 LYS B NZ  1 
ATOM   3390 N N   . GLY B 1 138 ? -7.65500  0.99400   -12.63200 1.000 38.50462  ? 138 GLY B N   1 
ATOM   3391 C CA  . GLY B 1 138 ? -8.37200  1.85400   -11.71800 1.000 39.26260  ? 138 GLY B CA  1 
ATOM   3392 C C   . GLY B 1 138 ? -9.49100  2.62500   -12.40700 1.000 35.41214  ? 138 GLY B C   1 
ATOM   3393 O O   . GLY B 1 138 ? -9.91400  2.33300   -13.53600 1.000 37.85454  ? 138 GLY B O   1 
ATOM   3394 N N   . SER B 1 139 ? -9.90700  3.66700   -11.74600 1.000 34.14620  ? 139 SER B N   1 
ATOM   3395 C CA  . SER B 1 139 ? -10.85900 4.64000   -12.25800 1.000 34.49624  ? 139 SER B CA  1 
ATOM   3396 C C   . SER B 1 139 ? -10.38900 5.99400   -11.72500 1.000 35.27265  ? 139 SER B C   1 
ATOM   3397 O O   . SER B 1 139 ? -10.52600 6.29600   -10.53000 1.000 37.26499  ? 139 SER B O   1 
ATOM   3398 C CB  . SER B 1 139 ? -12.29500 4.26000   -11.75200 1.000 34.61994  ? 139 SER B CB  1 
ATOM   3399 O OG  . SER B 1 139 ? -13.11200 5.31000   -12.23900 1.000 36.28593  ? 139 SER B OG  1 
ATOM   3400 N N   . PHE B 1 140 ? -9.74200  6.76800   -12.57300 1.000 35.11474  ? 140 PHE B N   1 
ATOM   3401 C CA  . PHE B 1 140 ? -9.01800  7.96900   -12.18800 1.000 35.82008  ? 140 PHE B CA  1 
ATOM   3402 C C   . PHE B 1 140 ? -9.23000  9.01600   -13.27200 1.000 37.63346  ? 140 PHE B C   1 
ATOM   3403 O O   . PHE B 1 140 ? -9.01100  8.72200   -14.46600 1.000 38.49672  ? 140 PHE B O   1 
ATOM   3404 C CB  . PHE B 1 140 ? -7.44300  7.67500   -12.07500 1.000 34.49887  ? 140 PHE B CB  1 
ATOM   3405 C CG  . PHE B 1 140 ? -7.05500  6.85100   -10.87000 1.000 34.26463  ? 140 PHE B CG  1 
ATOM   3406 C CD1 . PHE B 1 140 ? -7.26700  7.32700   -9.57900  1.000 38.95467  ? 140 PHE B CD1 1 
ATOM   3407 C CD2 . PHE B 1 140 ? -6.55100  5.58600   -11.01700 1.000 36.65176  ? 140 PHE B CD2 1 
ATOM   3408 C CE1 . PHE B 1 140 ? -6.89200  6.59300   -8.44200  1.000 36.78073  ? 140 PHE B CE1 1 
ATOM   3409 C CE2 . PHE B 1 140 ? -6.17700  4.81700   -9.90700  1.000 37.74137  ? 140 PHE B CE2 1 
ATOM   3410 C CZ  . PHE B 1 140 ? -6.27800  5.34900   -8.63100  1.000 37.86770  ? 140 PHE B CZ  1 
ATOM   3411 N N   . LEU B 1 141 ? -9.49300  10.26100  -12.86200 1.000 35.30950  ? 141 LEU B N   1 
ATOM   3412 C CA  . LEU B 1 141 ? -9.58100  11.37900  -13.77200 1.000 39.74424  ? 141 LEU B CA  1 
ATOM   3413 C C   . LEU B 1 141 ? -8.45800  12.37000  -13.45000 1.000 41.19968  ? 141 LEU B C   1 
ATOM   3414 O O   . LEU B 1 141 ? -7.73100  12.21100  -12.46000 1.000 40.31010  ? 141 LEU B O   1 
ATOM   3415 C CB  . LEU B 1 141 ? -10.92700 12.09500  -13.67800 1.000 40.21008  ? 141 LEU B CB  1 
ATOM   3416 C CG  . LEU B 1 141 ? -12.10400 11.13300  -13.89900 1.000 44.96592  ? 141 LEU B CG  1 
ATOM   3417 C CD1 . LEU B 1 141 ? -13.46100 11.79900  -13.56200 1.000 49.53489  ? 141 LEU B CD1 1 
ATOM   3418 C CD2 . LEU B 1 141 ? -12.08900 10.64400  -15.37000 1.000 45.00803  ? 141 LEU B CD2 1 
ATOM   3419 N N   . ASN B 1 142 ? -8.36000  13.42200  -14.25200 1.000 39.20207  ? 142 ASN B N   1 
ATOM   3420 C CA  . ASN B 1 142 ? -7.43700  14.50300  -13.90600 1.000 41.66289  ? 142 ASN B CA  1 
ATOM   3421 C C   . ASN B 1 142 ? -7.80200  15.04400  -12.51900 1.000 41.85502  ? 142 ASN B C   1 
ATOM   3422 O O   . ASN B 1 142 ? -9.00100  15.13700  -12.14000 1.000 40.24693  ? 142 ASN B O   1 
ATOM   3423 C CB  . ASN B 1 142 ? -7.46900  15.59600  -14.96300 1.000 40.31799  ? 142 ASN B CB  1 
ATOM   3424 C CG  . ASN B 1 142 ? -6.82000  15.17100  -16.30800 1.000 47.30567  ? 142 ASN B CG  1 
ATOM   3425 O OD1 . ASN B 1 142 ? -5.92300  14.32500  -16.37300 1.000 46.17133  ? 142 ASN B OD1 1 
ATOM   3426 N ND2 . ASN B 1 142 ? -7.29600  15.76300  -17.38400 1.000 51.76410  ? 142 ASN B ND2 1 
ATOM   3427 N N   . GLY B 1 143 ? -6.76200  15.25300  -11.69300 1.000 41.58657  ? 143 GLY B N   1 
ATOM   3428 C CA  . GLY B 1 143 ? -6.90700  15.64600  -10.29800 1.000 38.29407  ? 143 GLY B CA  1 
ATOM   3429 C C   . GLY B 1 143 ? -6.74200  14.51400  -9.31500  1.000 37.04918  ? 143 GLY B C   1 
ATOM   3430 O O   . GLY B 1 143 ? -6.59700  14.77000  -8.11900  1.000 40.96807  ? 143 GLY B O   1 
ATOM   3431 N N   . SER B 1 144 ? -6.69100  13.29100  -9.78800  1.000 35.95957  ? 144 SER B N   1 
ATOM   3432 C CA  . SER B 1 144 ? -6.65300  12.13000  -8.90100  1.000 40.08375  ? 144 SER B CA  1 
ATOM   3433 C C   . SER B 1 144 ? -5.23800  11.77400  -8.45700  1.000 36.63860  ? 144 SER B C   1 
ATOM   3434 O O   . SER B 1 144 ? -5.07200  11.00800  -7.48700  1.000 33.66193  ? 144 SER B O   1 
ATOM   3435 C CB  . SER B 1 144 ? -7.27200  10.90000  -9.59700  1.000 37.22288  ? 144 SER B CB  1 
ATOM   3436 O OG  . SER B 1 144 ? -6.57100  10.59800  -10.80100 1.000 37.41501  ? 144 SER B OG  1 
ATOM   3437 N N   . ALA B 1 145 ? -4.20700  12.30900  -9.13700  1.000 38.50198  ? 145 ALA B N   1 
ATOM   3438 C CA  . ALA B 1 145 ? -2.83900  12.03000  -8.71600  1.000 36.15170  ? 145 ALA B CA  1 
ATOM   3439 C C   . ALA B 1 145 ? -2.66100  12.36400  -7.23700  1.000 33.61719  ? 145 ALA B C   1 
ATOM   3440 O O   . ALA B 1 145 ? -3.25000  13.30900  -6.71900  1.000 38.73359  ? 145 ALA B O   1 
ATOM   3441 C CB  . ALA B 1 145 ? -1.82900  12.82300  -9.57700  1.000 34.95419  ? 145 ALA B CB  1 
ATOM   3442 N N   . GLY B 1 146 ? -1.95300  11.50700  -6.53500  1.000 32.54338  ? 146 GLY B N   1 
ATOM   3443 C CA  . GLY B 1 146 ? -1.78400  11.62700  -5.12300  1.000 34.79365  ? 146 GLY B CA  1 
ATOM   3444 C C   . GLY B 1 146 ? -2.79400  10.77500  -4.32400  1.000 38.05193  ? 146 GLY B C   1 
ATOM   3445 O O   . GLY B 1 146 ? -2.60500  10.62000  -3.10600  1.000 33.89354  ? 146 GLY B O   1 
ATOM   3446 N N   . SER B 1 147 ? -3.87000  10.26400  -4.95500  1.000 35.79640  ? 147 SER B N   1 
ATOM   3447 C CA  . SER B 1 147 ? -4.73500  9.27700   -4.26000  1.000 36.23856  ? 147 SER B CA  1 
ATOM   3448 C C   . SER B 1 147 ? -3.87400  8.05600   -3.94600  1.000 39.20207  ? 147 SER B C   1 
ATOM   3449 O O   . SER B 1 147 ? -2.92700  7.72700   -4.69800  1.000 36.92548  ? 147 SER B O   1 
ATOM   3450 C CB  . SER B 1 147 ? -5.93100  8.84900   -5.13300  1.000 34.31727  ? 147 SER B CB  1 
ATOM   3451 O OG  . SER B 1 147 ? -6.60100  9.99700   -5.65000  1.000 38.32302  ? 147 SER B OG  1 
ATOM   3452 N N   . VAL B 1 148 ? -4.18000  7.38000   -2.83700  1.000 34.28306  ? 148 VAL B N   1 
ATOM   3453 C CA  . VAL B 1 148 ? -3.31800  6.30800   -2.35500  1.000 33.56981  ? 148 VAL B CA  1 
ATOM   3454 C C   . VAL B 1 148 ? -4.04700  4.97600   -2.32700  1.000 37.84401  ? 148 VAL B C   1 
ATOM   3455 O O   . VAL B 1 148 ? -5.29200  4.89000   -2.25000  1.000 38.69411  ? 148 VAL B O   1 
ATOM   3456 C CB  . VAL B 1 148 ? -2.69900  6.62500   -0.97000  1.000 36.48859  ? 148 VAL B CB  1 
ATOM   3457 C CG1 . VAL B 1 148 ? -1.68200  7.85500   -1.03600  1.000 39.03100  ? 148 VAL B CG1 1 
ATOM   3458 C CG2 . VAL B 1 148 ? -3.81700  6.82800   0.11200   1.000 35.98063  ? 148 VAL B CG2 1 
ATOM   3459 N N   . GLY B 1 149 ? -3.24700  3.91100   -2.38600  1.000 35.48847  ? 149 GLY B N   1 
ATOM   3460 C CA  . GLY B 1 149 ? -3.73400  2.54700   -2.23600  1.000 36.67808  ? 149 GLY B CA  1 
ATOM   3461 C C   . GLY B 1 149 ? -3.17500  2.04000   -0.92300  1.000 38.27564  ? 149 GLY B C   1 
ATOM   3462 O O   . GLY B 1 149 ? -2.08800  2.43900   -0.51100  1.000 40.62592  ? 149 GLY B O   1 
ATOM   3463 N N   . PHE B 1 150 ? -3.93300  1.17500   -0.25300  1.000 35.77271  ? 150 PHE B N   1 
ATOM   3464 C CA  . PHE B 1 150 ? -3.58300  0.76600   1.09700   1.000 40.26009  ? 150 PHE B CA  1 
ATOM   3465 C C   . PHE B 1 150 ? -4.28100  -0.55900  1.43600   1.000 40.04691  ? 150 PHE B C   1 
ATOM   3466 O O   . PHE B 1 150 ? -5.30000  -0.92300  0.85200   1.000 35.96484  ? 150 PHE B O   1 
ATOM   3467 C CB  . PHE B 1 150 ? -3.96800  1.82800   2.12000   1.000 37.20446  ? 150 PHE B CB  1 
ATOM   3468 C CG  . PHE B 1 150 ? -5.44900  2.08800   2.17300   1.000 40.15481  ? 150 PHE B CG  1 
ATOM   3469 C CD1 . PHE B 1 150 ? -6.04500  2.95700   1.27000   1.000 41.67342  ? 150 PHE B CD1 1 
ATOM   3470 C CD2 . PHE B 1 150 ? -6.24700  1.45900   3.13400   1.000 42.95778  ? 150 PHE B CD2 1 
ATOM   3471 C CE1 . PHE B 1 150 ? -7.38700  3.18300   1.30000   1.000 40.48117  ? 150 PHE B CE1 1 
ATOM   3472 C CE2 . PHE B 1 150 ? -7.63900  1.66700   3.14000   1.000 40.63645  ? 150 PHE B CE2 1 
ATOM   3473 C CZ  . PHE B 1 150 ? -8.18500  2.53600   2.20800   1.000 40.34957  ? 150 PHE B CZ  1 
ATOM   3474 N N   . ASN B 1 151 ? -3.71800  -1.24200  2.41400   1.000 39.73108  ? 151 ASN B N   1 
ATOM   3475 C CA  . ASN B 1 151 ? -4.34000  -2.35600  3.09600   1.000 43.32098  ? 151 ASN B CA  1 
ATOM   3476 C C   . ASN B 1 151 ? -4.37400  -1.99900  4.56300   1.000 45.89498  ? 151 ASN B C   1 
ATOM   3477 O O   . ASN B 1 151 ? -3.61800  -1.14500  5.02200   1.000 44.53955  ? 151 ASN B O   1 
ATOM   3478 C CB  . ASN B 1 151 ? -3.57800  -3.66100  2.89600   1.000 41.51814  ? 151 ASN B CB  1 
ATOM   3479 C CG  . ASN B 1 151 ? -3.79900  -4.27100  1.49800   1.000 44.08423  ? 151 ASN B CG  1 
ATOM   3480 O OD1 . ASN B 1 151 ? -4.84200  -4.79700  1.23100   1.000 45.47387  ? 151 ASN B OD1 1 
ATOM   3481 N ND2 . ASN B 1 151 ? -2.78600  -4.19700  0.60800   1.000 40.02059  ? 151 ASN B ND2 1 
ATOM   3482 N N   . ILE B 1 152 ? -5.30700  -2.61000  5.29600   1.000 46.31082  ? 152 ILE B N   1 
ATOM   3483 C CA  . ILE B 1 152 ? -5.39400  -2.39600  6.72700   1.000 49.78228  ? 152 ILE B CA  1 
ATOM   3484 C C   . ILE B 1 152 ? -5.25000  -3.73100  7.43800   1.000 56.69101  ? 152 ILE B C   1 
ATOM   3485 O O   . ILE B 1 152 ? -5.82200  -4.74100  7.01500   1.000 58.45175  ? 152 ILE B O   1 
ATOM   3486 C CB  . ILE B 1 152 ? -6.69300  -1.67600  7.12800   1.000 49.85335  ? 152 ILE B CB  1 
ATOM   3487 C CG1 . ILE B 1 152 ? -6.72500  -0.32000  6.41700   1.000 47.80047  ? 152 ILE B CG1 1 
ATOM   3488 C CG2 . ILE B 1 152 ? -6.73100  -1.51500  8.64600   1.000 54.04069  ? 152 ILE B CG2 1 
ATOM   3489 C CD1 . ILE B 1 152 ? -7.84100  0.60900   6.86400   1.000 55.31716  ? 152 ILE B CD1 1 
ATOM   3490 N N   . ASP B 1 153 ? -4.42300  -3.74300  8.46400   1.000 62.34958  ? 153 ASP B N   1 
ATOM   3491 C CA  . ASP B 1 153 ? -4.26700  -4.87600  9.35100   1.000 73.03507  ? 153 ASP B CA  1 
ATOM   3492 C C   . ASP B 1 153 ? -4.45700  -4.39000  10.77500  1.000 74.11415  ? 153 ASP B C   1 
ATOM   3493 O O   . ASP B 1 153 ? -3.63800  -3.61100  11.27700  1.000 74.50630  ? 153 ASP B O   1 
ATOM   3494 C CB  . ASP B 1 153 ? -2.89400  -5.51100  9.17900   1.000 74.79055  ? 153 ASP B CB  1 
ATOM   3495 C CG  . ASP B 1 153 ? -2.90100  -6.96600  9.53900   1.000 91.59519  ? 153 ASP B CG  1 
ATOM   3496 O OD1 . ASP B 1 153 ? -4.02000  -7.52100  9.70200   1.000 92.17158  ? 153 ASP B OD1 1 
ATOM   3497 O OD2 . ASP B 1 153 ? -1.80000  -7.54700  9.68100   1.000 100.06989 ? 153 ASP B OD2 1 
ATOM   3498 N N   . TYR B 1 154 ? -5.49900  -4.88900  11.43200  1.000 78.85419  ? 154 TYR B N   1 
ATOM   3499 C CA  . TYR B 1 154 ? -5.92900  -4.43500  12.75100  1.000 80.32542  ? 154 TYR B CA  1 
ATOM   3500 C C   . TYR B 1 154 ? -6.23600  -2.95500  12.65800  1.000 76.17492  ? 154 TYR B C   1 
ATOM   3501 O O   . TYR B 1 154 ? -7.21300  -2.55300  12.02000  1.000 79.57796  ? 154 TYR B O   1 
ATOM   3502 C CB  . TYR B 1 154 ? -4.85200  -4.70200  13.79700  1.000 85.82082  ? 154 TYR B CB  1 
ATOM   3503 C CG  . TYR B 1 154 ? -4.15700  -6.02400  13.56100  1.000 101.90959 ? 154 TYR B CG  1 
ATOM   3504 C CD1 . TYR B 1 154 ? -4.81900  -7.23900  13.78000  1.000 102.12014 ? 154 TYR B CD1 1 
ATOM   3505 C CD2 . TYR B 1 154 ? -2.83500  -6.05700  13.07700  1.000 99.09872  ? 154 TYR B CD2 1 
ATOM   3506 C CE1 . TYR B 1 154 ? -4.18300  -8.45900  13.53900  1.000 107.29708 ? 154 TYR B CE1 1 
ATOM   3507 C CE2 . TYR B 1 154 ? -2.18800  -7.26600  12.83300  1.000 104.12038 ? 154 TYR B CE2 1 
ATOM   3508 C CZ  . TYR B 1 154 ? -2.86600  -8.46700  13.06800  1.000 114.17422 ? 154 TYR B CZ  1 
ATOM   3509 O OH  . TYR B 1 154 ? -2.22600  -9.67100  12.83200  1.000 121.75934 ? 154 TYR B OH  1 
ATOM   3510 N N   . ASP B 1 155 ? -5.37400  -2.12300  13.21900  1.000 74.43524  ? 155 ASP B N   1 
ATOM   3511 C CA  . ASP B 1 155 ? -5.51600  -0.68300  13.03900  1.000 75.91173  ? 155 ASP B CA  1 
ATOM   3512 C C   . ASP B 1 155 ? -4.28700  -0.06800  12.36900  1.000 68.41083  ? 155 ASP B C   1 
ATOM   3513 O O   . ASP B 1 155 ? -4.13400  1.16200   12.40800  1.000 64.87883  ? 155 ASP B O   1 
ATOM   3514 C CB  . ASP B 1 155 ? -5.81600  0.00900   14.38100  1.000 82.69676  ? 155 ASP B CB  1 
ATOM   3515 C CG  . ASP B 1 155 ? -7.28900  -0.17700  14.84700  1.000 92.34791  ? 155 ASP B CG  1 
ATOM   3516 O OD1 . ASP B 1 155 ? -8.22800  -0.15100  14.00400  1.000 84.79175  ? 155 ASP B OD1 1 
ATOM   3517 O OD2 . ASP B 1 155 ? -7.50800  -0.33400  16.07200  1.000 96.89320  ? 155 ASP B OD2 1 
ATOM   3518 N N   . CYS B 1 156 ? -3.42200  -0.90000  11.74900  1.000 63.71817  ? 156 CYS B N   1 
ATOM   3519 C CA  . CYS B 1 156 ? -2.21400  -0.46300  11.04300  1.000 57.33056  ? 156 CYS B CA  1 
ATOM   3520 C C   . CYS B 1 156 ? -2.49700  -0.35600  9.53300   1.000 54.81447  ? 156 CYS B C   1 
ATOM   3521 O O   . CYS B 1 156 ? -2.90800  -1.34500  8.89100   1.000 50.14549  ? 156 CYS B O   1 
ATOM   3522 C CB  . CYS B 1 156 ? -1.05600  -1.42700  11.32100  1.000 56.53046  ? 156 CYS B CB  1 
ATOM   3523 S SG  . CYS B 1 156 ? 0.59400   -0.87000  10.62600  1.000 62.42854  ? 156 CYS B SG  1 
ATOM   3524 N N   . VAL B 1 157 ? -2.32500  0.86200   8.98300   1.000 50.79293  ? 157 VAL B N   1 
ATOM   3525 C CA  . VAL B 1 157 ? -2.52800  1.14100   7.55400   1.000 47.10565  ? 157 VAL B CA  1 
ATOM   3526 C C   . VAL B 1 157 ? -1.20000  0.93600   6.82600   1.000 46.34766  ? 157 VAL B C   1 
ATOM   3527 O O   . VAL B 1 157 ? -0.22300  1.61700   7.12500   1.000 45.43176  ? 157 VAL B O   1 
ATOM   3528 C CB  . VAL B 1 157 ? -3.03200  2.57400   7.31000   1.000 42.17085  ? 157 VAL B CB  1 
ATOM   3529 C CG1 . VAL B 1 157 ? -3.28600  2.77900   5.80700   1.000 41.46287  ? 157 VAL B CG1 1 
ATOM   3530 C CG2 . VAL B 1 157 ? -4.35100  2.86600   8.10700   1.000 44.91854  ? 157 VAL B CG2 1 
ATOM   3531 N N   . SER B 1 158 ? -1.18200  0.05300   5.84900   1.000 43.31309  ? 158 SER B N   1 
ATOM   3532 C CA  . SER B 1 158 ? -0.00500  -0.16000  4.99700   1.000 41.76817  ? 158 SER B CA  1 
ATOM   3533 C C   . SER B 1 158 ? -0.28800  0.52500   3.68100   1.000 41.18652  ? 158 SER B C   1 
ATOM   3534 O O   . SER B 1 158 ? -1.09200  0.03500   2.88500   1.000 41.28653  ? 158 SER B O   1 
ATOM   3535 C CB  . SER B 1 158 ? 0.26200   -1.63100  4.78600   1.000 43.29203  ? 158 SER B CB  1 
ATOM   3536 O OG  . SER B 1 158 ? 0.72300   -2.16400  5.99100   1.000 49.87440  ? 158 SER B OG  1 
ATOM   3537 N N   . PHE B 1 159 ? 0.33400   1.68500   3.47700   1.000 42.18137  ? 159 PHE B N   1 
ATOM   3538 C CA  . PHE B 1 159 ? 0.22900   2.40100   2.21900   1.000 39.86004  ? 159 PHE B CA  1 
ATOM   3539 C C   . PHE B 1 159 ? 1.15100   1.73200   1.21000   1.000 42.14189  ? 159 PHE B C   1 
ATOM   3540 O O   . PHE B 1 159 ? 2.34800   1.54900   1.46800   1.000 42.03662  ? 159 PHE B O   1 
ATOM   3541 C CB  . PHE B 1 159 ? 0.60000   3.88100   2.41300   1.000 40.36800  ? 159 PHE B CB  1 
ATOM   3542 C CG  . PHE B 1 159 ? -0.32700  4.61700   3.31700   1.000 40.10218  ? 159 PHE B CG  1 
ATOM   3543 C CD1 . PHE B 1 159 ? -1.57900  5.00900   2.85500   1.000 39.37577  ? 159 PHE B CD1 1 
ATOM   3544 C CD2 . PHE B 1 159 ? 0.06100   4.94400   4.60500   1.000 41.94713  ? 159 PHE B CD2 1 
ATOM   3545 C CE1 . PHE B 1 159 ? -2.48700  5.68000   3.69700   1.000 38.89414  ? 159 PHE B CE1 1 
ATOM   3546 C CE2 . PHE B 1 159 ? -0.80800  5.61800   5.44500   1.000 42.64722  ? 159 PHE B CE2 1 
ATOM   3547 C CZ  . PHE B 1 159 ? -2.09100  5.96700   5.00400   1.000 42.40245  ? 159 PHE B CZ  1 
ATOM   3548 N N   . CYS B 1 160 ? 0.61800   1.40700   0.05300   1.000 38.24932  ? 160 CYS B N   1 
ATOM   3549 C CA  . CYS B 1 160 ? 1.41900   0.74000   -0.93400  1.000 39.87320  ? 160 CYS B CA  1 
ATOM   3550 C C   . CYS B 1 160 ? 1.43200   1.41300   -2.28000  1.000 38.71780  ? 160 CYS B C   1 
ATOM   3551 O O   . CYS B 1 160 ? 2.27800   1.05300   -3.10000  1.000 40.45222  ? 160 CYS B O   1 
ATOM   3552 C CB  . CYS B 1 160 ? 0.98700   -0.72600  -1.11000  1.000 38.25985  ? 160 CYS B CB  1 
ATOM   3553 S SG  . CYS B 1 160 ? -0.75200  -0.91600  -1.58700  1.000 40.62856  ? 160 CYS B SG  1 
ATOM   3554 N N   . TYR B 1 161 ? 0.57100   2.39500   -2.53200  1.000 35.62006  ? 161 TYR B N   1 
ATOM   3555 C CA  . TYR B 1 161 ? 0.48000   2.95200   -3.86300  1.000 35.77534  ? 161 TYR B CA  1 
ATOM   3556 C C   . TYR B 1 161 ? 0.11800   4.42200   -3.75700  1.000 37.85191  ? 161 TYR B C   1 
ATOM   3557 O O   . TYR B 1 161 ? -0.68100  4.80900   -2.90900  1.000 36.55965  ? 161 TYR B O   1 
ATOM   3558 C CB  . TYR B 1 161 ? -0.55000  2.14700   -4.67900  1.000 33.74878  ? 161 TYR B CB  1 
ATOM   3559 C CG  . TYR B 1 161 ? -0.82800  2.69700   -6.04100  1.000 33.02764  ? 161 TYR B CG  1 
ATOM   3560 C CD1 . TYR B 1 161 ? -0.01900  2.33000   -7.14300  1.000 34.09883  ? 161 TYR B CD1 1 
ATOM   3561 C CD2 . TYR B 1 161 ? -1.88100  3.61300   -6.26200  1.000 34.40412  ? 161 TYR B CD2 1 
ATOM   3562 C CE1 . TYR B 1 161 ? -0.26200  2.85300   -8.41500  1.000 34.00408  ? 161 TYR B CE1 1 
ATOM   3563 C CE2 . TYR B 1 161 ? -2.15400  4.11200   -7.53800  1.000 32.61180  ? 161 TYR B CE2 1 
ATOM   3564 C CZ  . TYR B 1 161 ? -1.27200  3.76600   -8.59300  1.000 36.22803  ? 161 TYR B CZ  1 
ATOM   3565 O OH  . TYR B 1 161 ? -1.42600  4.15700   -9.90900  1.000 34.55414  ? 161 TYR B OH  1 
ATOM   3566 N N   . MET B 1 162 ? 0.77700   5.25200   -4.55100  1.000 34.18041  ? 162 MET B N   1 
ATOM   3567 C CA  . MET B 1 162 ? 0.31300   6.61100   -4.79800  1.000 36.20960  ? 162 MET B CA  1 
ATOM   3568 C C   . MET B 1 162 ? 0.11000   6.78800   -6.29700  1.000 37.08866  ? 162 MET B C   1 
ATOM   3569 O O   . MET B 1 162 ? 1.00800   6.47300   -7.09300  1.000 35.99642  ? 162 MET B O   1 
ATOM   3570 C CB  . MET B 1 162 ? 1.26100   7.66400   -4.26300  1.000 36.99128  ? 162 MET B CB  1 
ATOM   3571 C CG  . MET B 1 162 ? 0.85900   9.15500   -4.55200  1.000 35.01736  ? 162 MET B CG  1 
ATOM   3572 S SD  . MET B 1 162 ? 1.80000   10.28100  -3.47700  1.000 44.98171  ? 162 MET B SD  1 
ATOM   3573 C CE  . MET B 1 162 ? 0.70000   10.41700  -2.01700  1.000 41.85239  ? 162 MET B CE  1 
ATOM   3574 N N   . HIS B 1 163 ? -1.04000  7.33800   -6.68200  1.000 34.55941  ? 163 HIS B N   1 
ATOM   3575 C CA  . HIS B 1 163 ? -1.38300  7.46100   -8.09700  1.000 35.93326  ? 163 HIS B CA  1 
ATOM   3576 C C   . HIS B 1 163 ? -0.63800  8.63300   -8.74600  1.000 35.38056  ? 163 HIS B C   1 
ATOM   3577 O O   . HIS B 1 163 ? -0.56500  9.72200   -8.16900  1.000 34.05145  ? 163 HIS B O   1 
ATOM   3578 C CB  . HIS B 1 163 ? -2.87200  7.69000   -8.28300  1.000 35.66480  ? 163 HIS B CB  1 
ATOM   3579 C CG  . HIS B 1 163 ? -3.25900  7.67400   -9.71700  1.000 30.16414  ? 163 HIS B CG  1 
ATOM   3580 N ND1 . HIS B 1 163 ? -2.91200  6.64200   -10.54600 1.000 31.43798  ? 163 HIS B ND1 1 
ATOM   3581 C CD2 . HIS B 1 163 ? -3.89200  8.58400   -10.48600 1.000 31.66169  ? 163 HIS B CD2 1 
ATOM   3582 C CE1 . HIS B 1 163 ? -3.29300  6.90900   -11.78400 1.000 31.68801  ? 163 HIS B CE1 1 
ATOM   3583 N NE2 . HIS B 1 163 ? -3.92400  8.06800   -11.76900 1.000 35.60953  ? 163 HIS B NE2 1 
ATOM   3584 N N   . HIS B 1 164 ? -0.12000  8.41200   -9.97300  1.000 35.01472  ? 164 HIS B N   1 
ATOM   3585 C CA  . HIS B 1 164 ? 0.51100   9.46700   -10.78700 1.000 35.06736  ? 164 HIS B CA  1 
ATOM   3586 C C   . HIS B 1 164 ? -0.15900  9.69400   -12.14000 1.000 31.70643  ? 164 HIS B C   1 
ATOM   3587 O O   . HIS B 1 164 ? -0.47800  10.84800  -12.47600 1.000 34.81733  ? 164 HIS B O   1 
ATOM   3588 C CB  . HIS B 1 164 ? 1.99600   9.17500   -11.01300 1.000 33.46191  ? 164 HIS B CB  1 
ATOM   3589 C CG  . HIS B 1 164 ? 2.80700   9.30500   -9.76600  1.000 36.24119  ? 164 HIS B CG  1 
ATOM   3590 N ND1 . HIS B 1 164 ? 3.82600   10.22600  -9.61300  1.000 36.03327  ? 164 HIS B ND1 1 
ATOM   3591 C CD2 . HIS B 1 164 ? 2.79500   8.56000   -8.64000  1.000 36.49122  ? 164 HIS B CD2 1 
ATOM   3592 C CE1 . HIS B 1 164 ? 4.37300   10.06400  -8.41800  1.000 35.65954  ? 164 HIS B CE1 1 
ATOM   3593 N NE2 . HIS B 1 164 ? 3.76200   9.05600   -7.80800  1.000 36.72546  ? 164 HIS B NE2 1 
ATOM   3594 N N   . MET B 1 165 ? -0.40400  8.64900   -12.91600 1.000 36.48332  ? 165 MET B N   1 
ATOM   3595 C CA  . MET B 1 165 ? -0.68000  8.87000   -14.32400 1.000 35.99905  ? 165 MET B CA  1 
ATOM   3596 C C   . MET B 1 165 ? -1.54900  7.77300   -14.95300 1.000 32.40915  ? 165 MET B C   1 
ATOM   3597 O O   . MET B 1 165 ? -1.74200  6.63900   -14.44400 1.000 34.90418  ? 165 MET B O   1 
ATOM   3598 C CB  . MET B 1 165 ? 0.68200   9.02700   -15.11600 1.000 35.92536  ? 165 MET B CB  1 
ATOM   3599 C CG  . MET B 1 165 ? 1.45400   7.78500   -15.02300 1.000 35.64901  ? 165 MET B CG  1 
ATOM   3600 S SD  . MET B 1 165 ? 3.10400   8.24900   -15.70400 1.000 44.47375  ? 165 MET B SD  1 
ATOM   3601 C CE  . MET B 1 165 ? 3.55100   6.67000   -16.34400 1.000 39.27839  ? 165 MET B CE  1 
ATOM   3602 N N   . GLU B 1 166 ? -2.02600  8.09600   -16.13300 1.000 34.55151  ? 166 GLU B N   1 
ATOM   3603 C CA  . GLU B 1 166 ? -2.76800  7.14600   -16.93800 1.000 38.12826  ? 166 GLU B CA  1 
ATOM   3604 C C   . GLU B 1 166 ? -2.04800  6.86400   -18.24700 1.000 39.11785  ? 166 GLU B C   1 
ATOM   3605 O O   . GLU B 1 166 ? -1.55300  7.78300   -18.89300 1.000 39.60738  ? 166 GLU B O   1 
ATOM   3606 C CB  . GLU B 1 166 ? -4.17500  7.67500   -17.21700 1.000 35.87009  ? 166 GLU B CB  1 
ATOM   3607 C CG  . GLU B 1 166 ? -4.93800  6.69600   -18.08800 1.000 37.75453  ? 166 GLU B CG  1 
ATOM   3608 C CD  . GLU B 1 166 ? -6.45000  7.10200   -18.10700 1.000 41.43128  ? 166 GLU B CD  1 
ATOM   3609 O OE1 . GLU B 1 166 ? -7.06700  7.18600   -17.01600 1.000 40.16534  ? 166 GLU B OE1 1 
ATOM   3610 O OE2 . GLU B 1 166 ? -6.97800  7.39100   -19.20900 1.000 44.92907  ? 166 GLU B OE2 1 
ATOM   3611 N N   . LEU B 1 167 ? -1.92700  5.58000   -18.58900 1.000 37.34658  ? 167 LEU B N   1 
ATOM   3612 C CA  . LEU B 1 167 ? -1.25800  5.10500   -19.78700 1.000 37.64925  ? 167 LEU B CA  1 
ATOM   3613 C C   . LEU B 1 167 ? -2.25800  5.05400   -20.91300 1.000 40.90490  ? 167 LEU B C   1 
ATOM   3614 O O   . LEU B 1 167 ? -3.49100  5.16200   -20.65600 1.000 42.04451  ? 167 LEU B O   1 
ATOM   3615 C CB  . LEU B 1 167 ? -0.62800  3.74900   -19.52000 1.000 37.49397  ? 167 LEU B CB  1 
ATOM   3616 C CG  . LEU B 1 167 ? 0.55300   3.82300   -18.55500 1.000 37.40448  ? 167 LEU B CG  1 
ATOM   3617 C CD1 . LEU B 1 167 ? 1.01200   2.39400   -18.12700 1.000 38.33881  ? 167 LEU B CD1 1 
ATOM   3618 C CD2 . LEU B 1 167 ? 1.80000   4.53900   -19.18300 1.000 42.39456  ? 167 LEU B CD2 1 
ATOM   3619 N N   . PRO B 1 168 ? -1.78300  4.94600   -22.15500 1.000 39.56001  ? 168 PRO B N   1 
ATOM   3620 C CA  . PRO B 1 168 ? -2.69500  5.05400   -23.30400 1.000 43.04463  ? 168 PRO B CA  1 
ATOM   3621 C C   . PRO B 1 168 ? -3.80700  4.01500   -23.37500 1.000 44.98434  ? 168 PRO B C   1 
ATOM   3622 O O   . PRO B 1 168 ? -4.81600  4.30800   -24.01000 1.000 44.41059  ? 168 PRO B O   1 
ATOM   3623 C CB  . PRO B 1 168 ? -1.75500  4.94900   -24.51000 1.000 47.77678  ? 168 PRO B CB  1 
ATOM   3624 C CG  . PRO B 1 168 ? -0.47000  5.58700   -24.02600 1.000 44.05528  ? 168 PRO B CG  1 
ATOM   3625 C CD  . PRO B 1 168 ? -0.34800  5.12100   -22.58900 1.000 37.86507  ? 168 PRO B CD  1 
ATOM   3626 N N   . THR B 1 169 ? -3.63100  2.81300   -22.83600 1.000 40.43116  ? 169 THR B N   1 
ATOM   3627 C CA  . THR B 1 169 ? -4.68500  1.82000   -22.83500 1.000 43.41310  ? 169 THR B CA  1 
ATOM   3628 C C   . THR B 1 169 ? -5.72200  2.09700   -21.74700 1.000 44.85801  ? 169 THR B C   1 
ATOM   3629 O O   . THR B 1 169 ? -6.68500  1.33600   -21.63400 1.000 42.46825  ? 169 THR B O   1 
ATOM   3630 C CB  . THR B 1 169 ? -4.07500  0.41000   -22.69200 1.000 40.59697  ? 169 THR B CB  1 
ATOM   3631 O OG1 . THR B 1 169 ? -3.19600  0.38200   -21.55500 1.000 44.40532  ? 169 THR B OG1 1 
ATOM   3632 C CG2 . THR B 1 169 ? -3.20900  0.03300   -23.93100 1.000 47.89258  ? 169 THR B CG2 1 
ATOM   3633 N N   . GLY B 1 170 ? -5.58100  3.16300   -20.93700 1.000 39.41525  ? 170 GLY B N   1 
ATOM   3634 C CA  . GLY B 1 170 ? -6.61000  3.48000   -19.92900 1.000 40.57855  ? 170 GLY B CA  1 
ATOM   3635 C C   . GLY B 1 170 ? -6.34600  2.84500   -18.59300 1.000 42.27349  ? 170 GLY B C   1 
ATOM   3636 O O   . GLY B 1 170 ? -7.27600  2.73400   -17.79000 1.000 46.40556  ? 170 GLY B O   1 
ATOM   3637 N N   . VAL B 1 171 ? -5.18700  2.21800   -18.42700 1.000 37.51239  ? 171 VAL B N   1 
ATOM   3638 C CA  . VAL B 1 171 ? -4.77000  1.69500   -17.13800 1.000 35.73060  ? 171 VAL B CA  1 
ATOM   3639 C C   . VAL B 1 171 ? -3.84300  2.69400   -16.43900 1.000 35.05157  ? 171 VAL B C   1 
ATOM   3640 O O   . VAL B 1 171 ? -3.40900  3.70600   -17.01000 1.000 36.15170  ? 171 VAL B O   1 
ATOM   3641 C CB  . VAL B 1 171 ? -4.10200  0.31400   -17.27800 1.000 34.31990  ? 171 VAL B CB  1 
ATOM   3642 C CG1 . VAL B 1 171 ? -5.02200  -0.65500  -17.96600 1.000 38.47040  ? 171 VAL B CG1 1 
ATOM   3643 C CG2 . VAL B 1 171 ? -2.71400  0.35500   -18.03900 1.000 30.51418  ? 171 VAL B CG2 1 
ATOM   3644 N N   . HIS B 1 172 ? -3.47100  2.38700   -15.23500 1.000 33.25662  ? 172 HIS B N   1 
ATOM   3645 C CA  . HIS B 1 172 ? -2.95200  3.41900   -14.34900 1.000 35.66480  ? 172 HIS B CA  1 
ATOM   3646 C C   . HIS B 1 172 ? -1.62300  3.01600   -13.78300 1.000 36.74651  ? 172 HIS B C   1 
ATOM   3647 O O   . HIS B 1 172 ? -1.35100  1.82500   -13.62300 1.000 38.02035  ? 172 HIS B O   1 
ATOM   3648 C CB  . HIS B 1 172 ? -3.98600  3.66800   -13.22600 1.000 34.16725  ? 172 HIS B CB  1 
ATOM   3649 C CG  . HIS B 1 172 ? -5.25200  4.20200   -13.80200 1.000 36.44648  ? 172 HIS B CG  1 
ATOM   3650 N ND1 . HIS B 1 172 ? -6.40800  3.46000   -13.87200 1.000 38.76254  ? 172 HIS B ND1 1 
ATOM   3651 C CD2 . HIS B 1 172 ? -5.49500  5.35400   -14.47100 1.000 35.76481  ? 172 HIS B CD2 1 
ATOM   3652 C CE1 . HIS B 1 172 ? -7.35200  4.18200   -14.45600 1.000 37.27815  ? 172 HIS B CE1 1 
ATOM   3653 N NE2 . HIS B 1 172 ? -6.82200  5.32300   -14.85500 1.000 40.58645  ? 172 HIS B NE2 1 
ATOM   3654 N N   . ALA B 1 173 ? -0.79200  4.00900   -13.52800 1.000 34.94630  ? 173 ALA B N   1 
ATOM   3655 C CA  . ALA B 1 173 ? 0.58400   3.77200   -13.10800 1.000 33.08291  ? 173 ALA B CA  1 
ATOM   3656 C C   . ALA B 1 173 ? 0.88500   4.70600   -11.96300 1.000 31.59853  ? 173 ALA B C   1 
ATOM   3657 O O   . ALA B 1 173 ? 0.44800   5.87400   -11.93500 1.000 33.30136  ? 173 ALA B O   1 
ATOM   3658 C CB  . ALA B 1 173 ? 1.59900   3.93900   -14.28800 1.000 35.38319  ? 173 ALA B CB  1 
ATOM   3659 N N   . GLY B 1 174 ? 1.61400   4.18800   -11.00400 1.000 32.43020  ? 174 GLY B N   1 
ATOM   3660 C CA  . GLY B 1 174 ? 1.98800   5.00500   -9.89200  1.000 32.69339  ? 174 GLY B CA  1 
ATOM   3661 C C   . GLY B 1 174 ? 3.19700   4.45000   -9.17500  1.000 32.59338  ? 174 GLY B C   1 
ATOM   3662 O O   . GLY B 1 174 ? 3.91900   3.59500   -9.70300  1.000 33.61192  ? 174 GLY B O   1 
ATOM   3663 N N   . THR B 1 175 ? 3.38800   4.94000   -7.95700  1.000 31.68011  ? 175 THR B N   1 
ATOM   3664 C CA  . THR B 1 175 ? 4.62500   4.63500   -7.22400  1.000 36.37805  ? 175 THR B CA  1 
ATOM   3665 C C   . THR B 1 175 ? 4.26600   4.01500   -5.88600  1.000 37.12814  ? 175 THR B C   1 
ATOM   3666 O O   . THR B 1 175 ? 3.11600   4.04900   -5.45800  1.000 38.83624  ? 175 THR B O   1 
ATOM   3667 C CB  . THR B 1 175 ? 5.48800   5.89500   -6.97100  1.000 36.47543  ? 175 THR B CB  1 
ATOM   3668 O OG1 . THR B 1 175 ? 4.80800   6.85800   -6.10100  1.000 36.57544  ? 175 THR B OG1 1 
ATOM   3669 C CG2 . THR B 1 175 ? 5.94900   6.54500   -8.29400  1.000 35.21738  ? 175 THR B CG2 1 
ATOM   3670 N N   . ASP B 1 176 ? 5.26000   3.44300   -5.22300  1.000 35.49373  ? 176 ASP B N   1 
ATOM   3671 C CA  . ASP B 1 176 ? 5.12900   3.27100   -3.79500  1.000 38.72833  ? 176 ASP B CA  1 
ATOM   3672 C C   . ASP B 1 176 ? 5.30700   4.62200   -3.10100  1.000 36.49911  ? 176 ASP B C   1 
ATOM   3673 O O   . ASP B 1 176 ? 5.52900   5.69400   -3.72200  1.000 37.33342  ? 176 ASP B O   1 
ATOM   3674 C CB  . ASP B 1 176 ? 6.07600   2.15300   -3.32100  1.000 38.16773  ? 176 ASP B CB  1 
ATOM   3675 C CG  . ASP B 1 176 ? 7.60000   2.50500   -3.54800  1.000 40.40221  ? 176 ASP B CG  1 
ATOM   3676 O OD1 . ASP B 1 176 ? 7.95700   3.68800   -3.55000  1.000 37.97824  ? 176 ASP B OD1 1 
ATOM   3677 O OD2 . ASP B 1 176 ? 8.38500   1.55900   -3.70500  1.000 39.24681  ? 176 ASP B OD2 1 
ATOM   3678 N N   . LEU B 1 177 ? 5.20700   4.60500   -1.78200  1.000 36.36225  ? 177 LEU B N   1 
ATOM   3679 C CA  . LEU B 1 177 ? 5.25400   5.86000   -1.05100  1.000 39.32050  ? 177 LEU B CA  1 
ATOM   3680 C C   . LEU B 1 177 ? 6.68600   6.35500   -0.84500  1.000 43.17360  ? 177 LEU B C   1 
ATOM   3681 O O   . LEU B 1 177 ? 6.86000   7.44200   -0.30800  1.000 42.38140  ? 177 LEU B O   1 
ATOM   3682 C CB  . LEU B 1 177 ? 4.51800   5.75100   0.29000   1.000 43.04727  ? 177 LEU B CB  1 
ATOM   3683 C CG  . LEU B 1 177 ? 3.01000   6.06700   0.23600   1.000 36.85968  ? 177 LEU B CG  1 
ATOM   3684 C CD1 . LEU B 1 177 ? 2.73100   7.58600   0.00700   1.000 43.24203  ? 177 LEU B CD1 1 
ATOM   3685 C CD2 . LEU B 1 177 ? 2.18200   5.21000   -0.76900  1.000 40.89701  ? 177 LEU B CD2 1 
ATOM   3686 N N   . GLU B 1 178 ? 7.68100   5.61800   -1.28600  1.000 43.28677  ? 178 GLU B N   1 
ATOM   3687 C CA  . GLU B 1 178 ? 9.04200   6.17600   -1.39200  1.000 47.00037  ? 178 GLU B CA  1 
ATOM   3688 C C   . GLU B 1 178 ? 9.29000   6.82200   -2.73500  1.000 43.29203  ? 178 GLU B C   1 
ATOM   3689 O O   . GLU B 1 178 ? 10.41000  7.29900   -2.98600  1.000 46.02394  ? 178 GLU B O   1 
ATOM   3690 C CB  . GLU B 1 178 ? 10.07600  5.07200   -1.16500  1.000 47.91627  ? 178 GLU B CB  1 
ATOM   3691 C CG  . GLU B 1 178 ? 10.13600  4.63500   0.26500   1.000 57.30687  ? 178 GLU B CG  1 
ATOM   3692 C CD  . GLU B 1 178 ? 10.93800  3.36600   0.42800   1.000 80.43070  ? 178 GLU B CD  1 
ATOM   3693 O OE1 . GLU B 1 178 ? 11.60400  2.92300   -0.56300  1.000 69.10829  ? 178 GLU B OE1 1 
ATOM   3694 O OE2 . GLU B 1 178 ? 10.82800  2.77500   1.53100   1.000 95.85623  ? 178 GLU B OE2 1 
ATOM   3695 N N   . GLY B 1 179 ? 8.29700   6.81500   -3.61400  1.000 39.24681  ? 179 GLY B N   1 
ATOM   3696 C CA  . GLY B 1 179 ? 8.35900   7.46500   -4.89200  1.000 38.98625  ? 179 GLY B CA  1 
ATOM   3697 C C   . GLY B 1 179 ? 8.93300   6.61400   -6.01100  1.000 41.89450  ? 179 GLY B C   1 
ATOM   3698 O O   . GLY B 1 179 ? 9.25600   7.15800   -7.06900  1.000 41.91029  ? 179 GLY B O   1 
ATOM   3699 N N   . ASN B 1 180 ? 9.10600   5.32300   -5.77300  1.000 39.17312  ? 180 ASN B N   1 
ATOM   3700 C CA  . ASN B 1 180 ? 9.62600   4.43700   -6.83900  1.000 38.47040  ? 180 ASN B CA  1 
ATOM   3701 C C   . ASN B 1 180 ? 8.46100   3.84700   -7.63500  1.000 38.71517  ? 180 ASN B C   1 
ATOM   3702 O O   . ASN B 1 180 ? 7.59400   3.22000   -7.02400  1.000 37.94929  ? 180 ASN B O   1 
ATOM   3703 C CB  . ASN B 1 180 ? 10.56800  3.38300   -6.26600  1.000 43.37362  ? 180 ASN B CB  1 
ATOM   3704 C CG  . ASN B 1 180 ? 11.83400  4.00000   -5.71600  1.000 50.87189  ? 180 ASN B CG  1 
ATOM   3705 O OD1 . ASN B 1 180 ? 12.56500  4.66600   -6.44200  1.000 55.20925  ? 180 ASN B OD1 1 
ATOM   3706 N ND2 . ASN B 1 180 ? 12.09000  3.79800   -4.43600  1.000 48.80322  ? 180 ASN B ND2 1 
ATOM   3707 N N   . PHE B 1 181 ? 8.47100   4.04700   -8.95000  1.000 36.50701  ? 181 PHE B N   1 
ATOM   3708 C CA  . PHE B 1 181 ? 7.37700   3.52100   -9.76800  1.000 38.95467  ? 181 PHE B CA  1 
ATOM   3709 C C   . PHE B 1 181 ? 7.31500   2.01000   -9.68100  1.000 37.06760  ? 181 PHE B C   1 
ATOM   3710 O O   . PHE B 1 181 ? 8.34500   1.33200   -9.60700  1.000 34.29622  ? 181 PHE B O   1 
ATOM   3711 C CB  . PHE B 1 181 ? 7.56100   3.89600   -11.26000 1.000 38.11246  ? 181 PHE B CB  1 
ATOM   3712 C CG  . PHE B 1 181 ? 6.81200   5.12600   -11.65900 1.000 38.18879  ? 181 PHE B CG  1 
ATOM   3713 C CD1 . PHE B 1 181 ? 5.43200   5.02800   -12.02700 1.000 35.70428  ? 181 PHE B CD1 1 
ATOM   3714 C CD2 . PHE B 1 181 ? 7.43200   6.38000   -11.55600 1.000 32.81183  ? 181 PHE B CD2 1 
ATOM   3715 C CE1 . PHE B 1 181 ? 4.73600   6.12900   -12.36900 1.000 34.40676  ? 181 PHE B CE1 1 
ATOM   3716 C CE2 . PHE B 1 181 ? 6.71600   7.53400   -11.87300 1.000 38.94151  ? 181 PHE B CE2 1 
ATOM   3717 C CZ  . PHE B 1 181 ? 5.31800   7.39900   -12.25500 1.000 34.22252  ? 181 PHE B CZ  1 
ATOM   3718 N N   . TYR B 1 182 ? 6.08800   1.48600   -9.65000  1.000 34.63836  ? 182 TYR B N   1 
ATOM   3719 C CA  . TYR B 1 182 ? 5.83400   0.13300   -10.08900 1.000 32.52495  ? 182 TYR B CA  1 
ATOM   3720 C C   . TYR B 1 182 ? 5.92900   0.10300   -11.60500 1.000 33.82774  ? 182 TYR B C   1 
ATOM   3721 O O   . TYR B 1 182 ? 5.25200   0.87300   -12.28700 1.000 37.08339  ? 182 TYR B O   1 
ATOM   3722 C CB  . TYR B 1 182 ? 4.39900   -0.28100  -9.63500  1.000 33.06712  ? 182 TYR B CB  1 
ATOM   3723 C CG  . TYR B 1 182 ? 4.28700   -0.38300  -8.12200  1.000 32.68813  ? 182 TYR B CG  1 
ATOM   3724 C CD1 . TYR B 1 182 ? 4.78000   -1.52600  -7.46600  1.000 36.14644  ? 182 TYR B CD1 1 
ATOM   3725 C CD2 . TYR B 1 182 ? 3.67400   0.64700   -7.35500  1.000 32.07490  ? 182 TYR B CD2 1 
ATOM   3726 C CE1 . TYR B 1 182 ? 4.67300   -1.65400  -6.05900  1.000 39.64160  ? 182 TYR B CE1 1 
ATOM   3727 C CE2 . TYR B 1 182 ? 3.57800   0.55300   -5.96500  1.000 35.07526  ? 182 TYR B CE2 1 
ATOM   3728 C CZ  . TYR B 1 182 ? 4.03100   -0.61800  -5.34000  1.000 38.23090  ? 182 TYR B CZ  1 
ATOM   3729 O OH  . TYR B 1 182 ? 3.92900   -0.71000  -4.01400  1.000 37.24657  ? 182 TYR B OH  1 
ATOM   3730 N N   . GLY B 1 183 ? 6.73900   -0.78300  -12.14500 1.000 35.65427  ? 183 GLY B N   1 
ATOM   3731 C CA  . GLY B 1 183 ? 6.82600   -0.94900  -13.58800 1.000 36.71756  ? 183 GLY B CA  1 
ATOM   3732 C C   . GLY B 1 183 ? 7.84700   0.02000   -14.21700 1.000 37.40712  ? 183 GLY B C   1 
ATOM   3733 O O   . GLY B 1 183 ? 8.33600   0.96400   -13.58500 1.000 38.65990  ? 183 GLY B O   1 
ATOM   3734 N N   . PRO B 1 184 ? 8.09400   -0.14400  -15.47100 1.000 38.84939  ? 184 PRO B N   1 
ATOM   3735 C CA  . PRO B 1 184 ? 9.13500   0.68300   -16.17000 1.000 39.90742  ? 184 PRO B CA  1 
ATOM   3736 C C   . PRO B 1 184 ? 8.56000   1.99000   -16.72600 1.000 37.91770  ? 184 PRO B C   1 
ATOM   3737 O O   . PRO B 1 184 ? 8.61000   2.26200   -17.94500 1.000 41.97872  ? 184 PRO B O   1 
ATOM   3738 C CB  . PRO B 1 184 ? 9.55700   -0.25900  -17.28800 1.000 37.72821  ? 184 PRO B CB  1 
ATOM   3739 C CG  . PRO B 1 184 ? 8.28500   -0.92500  -17.65400 1.000 40.89701  ? 184 PRO B CG  1 
ATOM   3740 C CD  . PRO B 1 184 ? 7.54300   -1.18200  -16.36900 1.000 37.49134  ? 184 PRO B CD  1 
ATOM   3741 N N   . PHE B 1 185 ? 7.96500   2.78600   -15.85000 1.000 34.76469  ? 185 PHE B N   1 
ATOM   3742 C CA  . PHE B 1 185 ? 7.24000   3.99300   -16.20500 1.000 35.59901  ? 185 PHE B CA  1 
ATOM   3743 C C   . PHE B 1 185 ? 7.93800   5.18300   -15.57600 1.000 36.67808  ? 185 PHE B C   1 
ATOM   3744 O O   . PHE B 1 185 ? 8.60000   5.05700   -14.54000 1.000 38.29670  ? 185 PHE B O   1 
ATOM   3745 C CB  . PHE B 1 185 ? 5.76000   3.88000   -15.72300 1.000 37.57029  ? 185 PHE B CB  1 
ATOM   3746 C CG  . PHE B 1 185 ? 5.10800   2.62800   -16.21400 1.000 39.75477  ? 185 PHE B CG  1 
ATOM   3747 C CD1 . PHE B 1 185 ? 4.94400   2.43300   -17.60800 1.000 38.07299  ? 185 PHE B CD1 1 
ATOM   3748 C CD2 . PHE B 1 185 ? 4.65600   1.65400   -15.33600 1.000 36.40436  ? 185 PHE B CD2 1 
ATOM   3749 C CE1 . PHE B 1 185 ? 4.38300   1.21800   -18.10100 1.000 38.01508  ? 185 PHE B CE1 1 
ATOM   3750 C CE2 . PHE B 1 185 ? 4.13300   0.47000   -15.84300 1.000 37.30447  ? 185 PHE B CE2 1 
ATOM   3751 C CZ  . PHE B 1 185 ? 4.01400   0.26300   -17.23600 1.000 38.85203  ? 185 PHE B CZ  1 
ATOM   3752 N N   . VAL B 1 186 ? 7.69100   6.37300   -16.13000 1.000 35.94905  ? 186 VAL B N   1 
ATOM   3753 C CA  . VAL B 1 186 ? 8.28900   7.60300   -15.61900 1.000 37.73874  ? 186 VAL B CA  1 
ATOM   3754 C C   . VAL B 1 186 ? 7.20700   8.69100   -15.58900 1.000 38.09404  ? 186 VAL B C   1 
ATOM   3755 O O   . VAL B 1 186 ? 6.23600   8.63900   -16.34600 1.000 38.85203  ? 186 VAL B O   1 
ATOM   3756 C CB  . VAL B 1 186 ? 9.49300   8.03800   -16.48900 1.000 39.24944  ? 186 VAL B CB  1 
ATOM   3757 C CG1 . VAL B 1 186 ? 10.70300  7.05400   -16.28300 1.000 34.50940  ? 186 VAL B CG1 1 
ATOM   3758 C CG2 . VAL B 1 186 ? 9.03900   8.02400   -17.92400 1.000 36.80441  ? 186 VAL B CG2 1 
ATOM   3759 N N   . ASP B 1 187 ? 7.37800   9.65000   -14.66900 1.000 37.30974  ? 187 ASP B N   1 
ATOM   3760 C CA  . ASP B 1 187 ? 6.37800   10.73000  -14.43100 1.000 40.27325  ? 187 ASP B CA  1 
ATOM   3761 C C   . ASP B 1 187 ? 6.56500   11.89600  -15.39600 1.000 40.12586  ? 187 ASP B C   1 
ATOM   3762 O O   . ASP B 1 187 ? 6.92400   12.98600  -14.94900 1.000 40.67330  ? 187 ASP B O   1 
ATOM   3763 C CB  . ASP B 1 187 ? 6.37600   11.18400  -12.97000 1.000 39.10206  ? 187 ASP B CB  1 
ATOM   3764 C CG  . ASP B 1 187 ? 7.73300   11.50800  -12.38000 1.000 39.51000  ? 187 ASP B CG  1 
ATOM   3765 O OD1 . ASP B 1 187 ? 8.74600   11.18700  -13.01400 1.000 40.23904  ? 187 ASP B OD1 1 
ATOM   3766 O OD2 . ASP B 1 187 ? 7.74900   12.07500  -11.28600 1.000 37.89139  ? 187 ASP B OD2 1 
ATOM   3767 N N   . ARG B 1 188 ? 6.32400   11.64700  -16.66700 1.000 39.93900  ? 188 ARG B N   1 
ATOM   3768 C CA  . ARG B 1 188 ? 6.35900   12.66700  -17.69400 1.000 38.84676  ? 188 ARG B CA  1 
ATOM   3769 C C   . ARG B 1 188 ? 5.46600   12.17100  -18.81200 1.000 37.47028  ? 188 ARG B C   1 
ATOM   3770 O O   . ARG B 1 188 ? 5.24400   10.96800  -18.96200 1.000 40.29694  ? 188 ARG B O   1 
ATOM   3771 C CB  . ARG B 1 188 ? 7.81200   12.86600  -18.21000 1.000 40.32852  ? 188 ARG B CB  1 
ATOM   3772 C CG  . ARG B 1 188 ? 8.30000   11.55200  -18.66700 1.000 42.47878  ? 188 ARG B CG  1 
ATOM   3773 C CD  . ARG B 1 188 ? 9.86600   11.51500  -18.71000 1.000 42.06294  ? 188 ARG B CD  1 
ATOM   3774 N NE  . ARG B 1 188 ? 10.47100  12.61700  -19.40800 1.000 46.86088  ? 188 ARG B NE  1 
ATOM   3775 C CZ  . ARG B 1 188 ? 11.77300  12.67400  -19.65800 1.000 48.26368  ? 188 ARG B CZ  1 
ATOM   3776 N NH1 . ARG B 1 188 ? 12.62200  11.83500  -19.08200 1.000 43.55785  ? 188 ARG B NH1 1 
ATOM   3777 N NH2 . ARG B 1 188 ? 12.24300  13.61500  -20.48100 1.000 51.46407  ? 188 ARG B NH2 1 
ATOM   3778 N N   . GLN B 1 189 ? 4.94500   13.09200  -19.59100 1.000 42.59458  ? 189 GLN B N   1 
ATOM   3779 C CA  . GLN B 1 189 ? 4.02000   12.74900  -20.66500 1.000 44.58956  ? 189 GLN B CA  1 
ATOM   3780 C C   . GLN B 1 189 ? 4.74200   12.40200  -21.96100 1.000 48.55319  ? 189 GLN B C   1 
ATOM   3781 O O   . GLN B 1 189 ? 4.42100   12.91500  -23.02600 1.000 48.81638  ? 189 GLN B O   1 
ATOM   3782 C CB  . GLN B 1 189 ? 3.05300   13.90600  -20.85700 1.000 44.01054  ? 189 GLN B CB  1 
ATOM   3783 C CG  . GLN B 1 189 ? 2.37100   14.22400  -19.52300 1.000 46.00552  ? 189 GLN B CG  1 
ATOM   3784 C CD  . GLN B 1 189 ? 1.09000   14.98800  -19.63500 1.000 45.90814  ? 189 GLN B CD  1 
ATOM   3785 O OE1 . GLN B 1 189 ? 0.14600   14.74700  -18.87000 1.000 45.58968  ? 189 GLN B OE1 1 
ATOM   3786 N NE2 . GLN B 1 189 ? 1.03300   15.93100  -20.56700 1.000 45.55546  ? 189 GLN B NE2 1 
ATOM   3787 N N   . THR B 1 190 ? 5.71400   11.49200  -21.88700 1.000 46.86088  ? 190 THR B N   1 
ATOM   3788 C CA  . THR B 1 190 ? 6.27800   10.91000  -23.08000 1.000 46.14237  ? 190 THR B CA  1 
ATOM   3789 C C   . THR B 1 190 ? 5.53200   9.63900   -23.43200 1.000 47.08196  ? 190 THR B C   1 
ATOM   3790 O O   . THR B 1 190 ? 4.68400   9.14000   -22.66700 1.000 45.79496  ? 190 THR B O   1 
ATOM   3791 C CB  . THR B 1 190 ? 7.76300   10.58100  -22.88700 1.000 47.66624  ? 190 THR B CB  1 
ATOM   3792 O OG1 . THR B 1 190 ? 7.89800   9.76900   -21.69500 1.000 44.50797  ? 190 THR B OG1 1 
ATOM   3793 C CG2 . THR B 1 190 ? 8.59700   11.86800  -22.76900 1.000 47.98996  ? 190 THR B CG2 1 
ATOM   3794 N N   . ALA B 1 191 ? 5.88900   9.10300   -24.59100 1.000 47.12407  ? 191 ALA B N   1 
ATOM   3795 C CA  . ALA B 1 191 ? 5.29400   7.88400   -25.13600 1.000 48.36106  ? 191 ALA B CA  1 
ATOM   3796 C C   . ALA B 1 191 ? 5.65000   6.72000   -24.23600 1.000 46.02131  ? 191 ALA B C   1 
ATOM   3797 O O   . ALA B 1 191 ? 6.82600   6.49200   -23.96700 1.000 41.71553  ? 191 ALA B O   1 
ATOM   3798 C CB  . ALA B 1 191 ? 5.81400   7.64400   -26.55900 1.000 51.27457  ? 191 ALA B CB  1 
ATOM   3799 N N   . GLN B 1 192 ? 4.64100   6.08400   -23.63200 1.000 40.63119  ? 192 GLN B N   1 
ATOM   3800 C CA  . GLN B 1 192 ? 4.88300   4.94600   -22.76700 1.000 40.09691  ? 192 GLN B CA  1 
ATOM   3801 C C   . GLN B 1 192 ? 3.71900   3.98600   -22.95300 1.000 43.85526  ? 192 GLN B C   1 
ATOM   3802 O O   . GLN B 1 192 ? 2.61600   4.42900   -23.26400 1.000 39.70476  ? 192 GLN B O   1 
ATOM   3803 C CB  . GLN B 1 192 ? 4.96300   5.34500   -21.27000 1.000 40.56802  ? 192 GLN B CB  1 
ATOM   3804 C CG  . GLN B 1 192 ? 5.99400   6.43100   -20.93900 1.000 43.50258  ? 192 GLN B CG  1 
ATOM   3805 C CD  . GLN B 1 192 ? 6.02800   6.81600   -19.47900 1.000 40.14692  ? 192 GLN B CD  1 
ATOM   3806 O OE1 . GLN B 1 192 ? 6.35100   6.00500   -18.61000 1.000 35.95168  ? 192 GLN B OE1 1 
ATOM   3807 N NE2 . GLN B 1 192 ? 5.66600   8.06200   -19.20200 1.000 39.04152  ? 192 GLN B NE2 1 
ATOM   3808 N N   . ALA B 1 193 ? 3.95800   2.68200   -22.74300 1.000 41.09966  ? 193 ALA B N   1 
ATOM   3809 C CA  . ALA B 1 193 ? 2.89000   1.70500   -22.94200 1.000 37.77821  ? 193 ALA B CA  1 
ATOM   3810 C C   . ALA B 1 193 ? 3.08000   0.60900   -21.91800 1.000 42.67880  ? 193 ALA B C   1 
ATOM   3811 O O   . ALA B 1 193 ? 4.21300   0.25400   -21.58500 1.000 41.77343  ? 193 ALA B O   1 
ATOM   3812 C CB  . ALA B 1 193 ? 2.86600   1.11000   -24.34900 1.000 42.67617  ? 193 ALA B CB  1 
ATOM   3813 N N   . ALA B 1 194 ? 1.95600   0.10800   -21.41000 1.000 36.33594  ? 194 ALA B N   1 
ATOM   3814 C CA  . ALA B 1 194 ? 1.96700   -1.02500  -20.49700 1.000 39.25997  ? 194 ALA B CA  1 
ATOM   3815 C C   . ALA B 1 194 ? 2.53900   -2.24900  -21.18700 1.000 42.01030  ? 194 ALA B C   1 
ATOM   3816 O O   . ALA B 1 194 ? 2.30700   -2.45800  -22.37600 1.000 40.76805  ? 194 ALA B O   1 
ATOM   3817 C CB  . ALA B 1 194 ? 0.50500   -1.28100  -20.04500 1.000 37.63609  ? 194 ALA B CB  1 
ATOM   3818 N N   . GLY B 1 195 ? 3.30900   -3.06600  -20.46100 1.000 40.12323  ? 195 GLY B N   1 
ATOM   3819 C CA  . GLY B 1 195 ? 3.78900   -4.31000  -21.06400 1.000 43.89737  ? 195 GLY B CA  1 
ATOM   3820 C C   . GLY B 1 195 ? 2.65400   -5.31700  -21.29200 1.000 47.08986  ? 195 GLY B C   1 
ATOM   3821 O O   . GLY B 1 195 ? 1.51300   -5.13200  -20.86500 1.000 43.14991  ? 195 GLY B O   1 
ATOM   3822 N N   . THR B 1 196 ? 2.94200   -6.42500  -21.97500 1.000 46.99511  ? 196 THR B N   1 
ATOM   3823 C CA  . THR B 1 196 ? 1.90100   -7.46700  -22.01900 1.000 47.09775  ? 196 THR B CA  1 
ATOM   3824 C C   . THR B 1 196 ? 1.63600   -7.99400  -20.60900 1.000 43.23150  ? 196 THR B C   1 
ATOM   3825 O O   . THR B 1 196 ? 2.54900   -8.15200  -19.77000 1.000 42.82882  ? 196 THR B O   1 
ATOM   3826 C CB  . THR B 1 196 ? 2.26900   -8.62700  -22.90700 1.000 51.00348  ? 196 THR B CB  1 
ATOM   3827 O OG1 . THR B 1 196 ? 3.49000   -9.18300  -22.37900 1.000 57.76482  ? 196 THR B OG1 1 
ATOM   3828 C CG2 . THR B 1 196 ? 2.53300   -8.11300  -24.34900 1.000 56.31201  ? 196 THR B CG2 1 
ATOM   3829 N N   . ASP B 1 197 ? 0.38700   -8.21000  -20.34600 1.000 41.51550  ? 197 ASP B N   1 
ATOM   3830 C CA  . ASP B 1 197 ? -0.08700  -8.65500  -19.04800 1.000 46.60296  ? 197 ASP B CA  1 
ATOM   3831 C C   . ASP B 1 197 ? -0.36400  -10.16300 -19.06500 1.000 49.33749  ? 197 ASP B C   1 
ATOM   3832 O O   . ASP B 1 197 ? -0.29100  -10.81500 -20.10800 1.000 47.86890  ? 197 ASP B O   1 
ATOM   3833 C CB  . ASP B 1 197 ? -1.33400  -7.88300  -18.67500 1.000 42.29718  ? 197 ASP B CB  1 
ATOM   3834 C CG  . ASP B 1 197 ? -1.56200  -7.81200  -17.14100 1.000 45.75549  ? 197 ASP B CG  1 
ATOM   3835 O OD1 . ASP B 1 197 ? -0.55500  -7.92100  -16.37900 1.000 41.10493  ? 197 ASP B OD1 1 
ATOM   3836 O OD2 . ASP B 1 197 ? -2.74000  -7.62500  -16.69500 1.000 40.93386  ? 197 ASP B OD2 1 
ATOM   3837 N N   . THR B 1 198 ? -0.54300  -10.73700 -17.87300 1.000 45.65811  ? 198 THR B N   1 
ATOM   3838 C CA  . THR B 1 198 ? -0.88500  -12.14500 -17.75600 1.000 45.76338  ? 198 THR B CA  1 
ATOM   3839 C C   . THR B 1 198 ? -1.92800  -12.25000 -16.64900 1.000 41.12335  ? 198 THR B C   1 
ATOM   3840 O O   . THR B 1 198 ? -2.16100  -11.29100 -15.90600 1.000 37.85717  ? 198 THR B O   1 
ATOM   3841 C CB  . THR B 1 198 ? 0.33700   -12.99800 -17.47700 1.000 47.74783  ? 198 THR B CB  1 
ATOM   3842 O OG1 . THR B 1 198 ? 0.92300   -12.50100 -16.28800 1.000 55.64878  ? 198 THR B OG1 1 
ATOM   3843 C CG2 . THR B 1 198 ? 1.41600   -12.79100 -18.55600 1.000 55.73037  ? 198 THR B CG2 1 
ATOM   3844 N N   . THR B 1 199 ? -2.56300  -13.40900 -16.54900 1.000 42.63669  ? 199 THR B N   1 
ATOM   3845 C CA  . THR B 1 199 ? -3.62700  -13.57500 -15.54000 1.000 36.25435  ? 199 THR B CA  1 
ATOM   3846 C C   . THR B 1 199 ? -2.98900  -14.14000 -14.29000 1.000 39.18891  ? 199 THR B C   1 
ATOM   3847 O O   . THR B 1 199 ? -2.09100  -14.96900 -14.39100 1.000 40.48380  ? 199 THR B O   1 
ATOM   3848 C CB  . THR B 1 199 ? -4.70300  -14.47500 -16.12500 1.000 37.52818  ? 199 THR B CB  1 
ATOM   3849 O OG1 . THR B 1 199 ? -5.20400  -13.77000 -17.26100 1.000 39.51000  ? 199 THR B OG1 1 
ATOM   3850 C CG2 . THR B 1 199 ? -5.88900  -14.77300 -15.11800 1.000 41.84975  ? 199 THR B CG2 1 
ATOM   3851 N N   . ILE B 1 200 ? -3.42700  -13.66900 -13.11500 1.000 37.59135  ? 200 ILE B N   1 
ATOM   3852 C CA  . ILE B 1 200 ? -2.84100  -14.12900 -11.84500 1.000 34.81733  ? 200 ILE B CA  1 
ATOM   3853 C C   . ILE B 1 200 ? -3.46400  -15.47000 -11.46700 1.000 40.11534  ? 200 ILE B C   1 
ATOM   3854 O O   . ILE B 1 200 ? -4.55900  -15.51300 -10.84200 1.000 36.01221  ? 200 ILE B O   1 
ATOM   3855 C CB  . ILE B 1 200 ? -3.01000  -13.09200 -10.74400 1.000 36.19381  ? 200 ILE B CB  1 
ATOM   3856 C CG1 . ILE B 1 200 ? -2.41200  -11.72900 -11.25500 1.000 37.98877  ? 200 ILE B CG1 1 
ATOM   3857 C CG2 . ILE B 1 200 ? -2.36400  -13.59800 -9.44700  1.000 37.94139  ? 200 ILE B CG2 1 
ATOM   3858 C CD1 . ILE B 1 200 ? -3.25500  -10.55900 -10.74800 1.000 35.59374  ? 200 ILE B CD1 1 
ATOM   3859 N N   . THR B 1 201 ? -2.75500  -16.56100 -11.78900 1.000 38.88624  ? 201 THR B N   1 
ATOM   3860 C CA  . THR B 1 201 ? -3.29900  -17.91600 -11.60700 1.000 39.99164  ? 201 THR B CA  1 
ATOM   3861 C C   . THR B 1 201 ? -3.70400  -18.21300 -10.16300 1.000 39.87847  ? 201 THR B C   1 
ATOM   3862 O O   . THR B 1 201 ? -4.80500  -18.73400 -9.92900  1.000 40.07059  ? 201 THR B O   1 
ATOM   3863 C CB  . THR B 1 201 ? -2.28700  -18.93900 -12.06700 1.000 41.96556  ? 201 THR B CB  1 
ATOM   3864 O OG1 . THR B 1 201 ? -1.84400  -18.59900 -13.39300 1.000 39.23628  ? 201 THR B OG1 1 
ATOM   3865 C CG2 . THR B 1 201 ? -2.90600  -20.36300 -12.07300 1.000 39.22312  ? 201 THR B CG2 1 
ATOM   3866 N N   . VAL B 1 202 ? -2.81200  -17.96600 -9.18900  1.000 38.13615  ? 202 VAL B N   1 
ATOM   3867 C CA  . VAL B 1 202 ? -3.13000  -18.27300 -7.79400  1.000 40.92596  ? 202 VAL B CA  1 
ATOM   3868 C C   . VAL B 1 202 ? -4.41700  -17.57200 -7.33400  1.000 38.96783  ? 202 VAL B C   1 
ATOM   3869 O O   . VAL B 1 202 ? -5.22000  -18.15900 -6.56200  1.000 38.77570  ? 202 VAL B O   1 
ATOM   3870 C CB  . VAL B 1 202 ? -1.94200  -17.90000 -6.88300  1.000 39.05468  ? 202 VAL B CB  1 
ATOM   3871 C CG1 . VAL B 1 202 ? -1.62700  -16.36000 -6.94400  1.000 42.06294  ? 202 VAL B CG1 1 
ATOM   3872 C CG2 . VAL B 1 202 ? -2.26000  -18.33400 -5.42000  1.000 40.70488  ? 202 VAL B CG2 1 
ATOM   3873 N N   . ASN B 1 203 ? -4.67600  -16.35600 -7.83200  1.000 37.59135  ? 203 ASN B N   1 
ATOM   3874 C CA  . ASN B 1 203 ? -5.89900  -15.63000 -7.50300  1.000 39.20996  ? 203 ASN B CA  1 
ATOM   3875 C C   . ASN B 1 203 ? -7.11100  -16.24400 -8.17000  1.000 37.46239  ? 203 ASN B C   1 
ATOM   3876 O O   . ASN B 1 203 ? -8.21900  -16.25500 -7.57700  1.000 38.13352  ? 203 ASN B O   1 
ATOM   3877 C CB  . ASN B 1 203 ? -5.80800  -14.15300 -7.91300  1.000 36.22013  ? 203 ASN B CB  1 
ATOM   3878 C CG  . ASN B 1 203 ? -4.81900  -13.34200 -7.02100  1.000 36.09380  ? 203 ASN B CG  1 
ATOM   3879 O OD1 . ASN B 1 203 ? -4.18500  -13.90900 -6.13600  1.000 34.53835  ? 203 ASN B OD1 1 
ATOM   3880 N ND2 . ASN B 1 203 ? -4.66200  -12.02800 -7.30400  1.000 38.49672  ? 203 ASN B ND2 1 
ATOM   3881 N N   . VAL B 1 204 ? -6.98600  -16.67500 -9.43200  1.000 37.69399  ? 204 VAL B N   1 
ATOM   3882 C CA  . VAL B 1 204 ? -8.14800  -17.35900 -10.02300 1.000 38.67569  ? 204 VAL B CA  1 
ATOM   3883 C C   . VAL B 1 204 ? -8.52100  -18.58600 -9.20200  1.000 41.36285  ? 204 VAL B C   1 
ATOM   3884 O O   . VAL B 1 204 ? -9.72600  -18.84000 -8.91800  1.000 38.64937  ? 204 VAL B O   1 
ATOM   3885 C CB  . VAL B 1 204 ? -7.89400  -17.73100 -11.48900 1.000 38.15721  ? 204 VAL B CB  1 
ATOM   3886 C CG1 . VAL B 1 204 ? -9.07000  -18.54500 -12.03700 1.000 37.52818  ? 204 VAL B CG1 1 
ATOM   3887 C CG2 . VAL B 1 204 ? -7.69100  -16.46300 -12.31300 1.000 36.88074  ? 204 VAL B CG2 1 
ATOM   3888 N N   . LEU B 1 205 ? -7.50900  -19.39200 -8.83900  1.000 37.47028  ? 205 LEU B N   1 
ATOM   3889 C CA  . LEU B 1 205 ? -7.78200  -20.53300 -7.95800  1.000 42.84198  ? 205 LEU B CA  1 
ATOM   3890 C C   . LEU B 1 205 ? -8.41600  -20.08500 -6.63800  1.000 39.31524  ? 205 LEU B C   1 
ATOM   3891 O O   . LEU B 1 205 ? -9.34500  -20.74600 -6.14000  1.000 38.45461  ? 205 LEU B O   1 
ATOM   3892 C CB  . LEU B 1 205 ? -6.48400  -21.32800 -7.71700  1.000 38.58357  ? 205 LEU B CB  1 
ATOM   3893 C CG  . LEU B 1 205 ? -5.92900  -22.06600 -8.94600  1.000 38.61779  ? 205 LEU B CG  1 
ATOM   3894 C CD1 . LEU B 1 205 ? -4.52100  -22.62900 -8.68000  1.000 42.40772  ? 205 LEU B CD1 1 
ATOM   3895 C CD2 . LEU B 1 205 ? -6.85000  -23.20200 -9.43900  1.000 41.85502  ? 205 LEU B CD2 1 
ATOM   3896 N N   . ALA B 1 206 ? -7.92500  -18.98200 -6.03900  1.000 37.59661  ? 206 ALA B N   1 
ATOM   3897 C CA  . ALA B 1 206 ? -8.52900  -18.51100 -4.78000  1.000 39.50737  ? 206 ALA B CA  1 
ATOM   3898 C C   . ALA B 1 206 ? -10.01200 -18.22700 -4.95800  1.000 38.15457  ? 206 ALA B C   1 
ATOM   3899 O O   . ALA B 1 206 ? -10.86600 -18.61900 -4.11400  1.000 40.09428  ? 206 ALA B O   1 
ATOM   3900 C CB  . ALA B 1 206 ? -7.79500  -17.25600 -4.27000  1.000 38.42566  ? 206 ALA B CB  1 
ATOM   3901 N N   . TRP B 1 207 ? -10.34900 -17.60100 -6.08100  1.000 37.39659  ? 207 TRP B N   1 
ATOM   3902 C CA  . TRP B 1 207 ? -11.73100 -17.22200 -6.36800  1.000 40.37326  ? 207 TRP B CA  1 
ATOM   3903 C C   . TRP B 1 207 ? -12.59500 -18.44500 -6.68700  1.000 40.50222  ? 207 TRP B C   1 
ATOM   3904 O O   . TRP B 1 207 ? -13.77700 -18.48400 -6.30900  1.000 36.71756  ? 207 TRP B O   1 
ATOM   3905 C CB  . TRP B 1 207 ? -11.69400 -16.18300 -7.48800  1.000 36.84389  ? 207 TRP B CB  1 
ATOM   3906 C CG  . TRP B 1 207 ? -12.99900 -15.81700 -8.15300  1.000 38.30459  ? 207 TRP B CG  1 
ATOM   3907 C CD1 . TRP B 1 207 ? -13.95100 -14.87500 -7.75900  1.000 37.55450  ? 207 TRP B CD1 1 
ATOM   3908 C CD2 . TRP B 1 207 ? -13.47100 -16.38400 -9.36100  1.000 40.60487  ? 207 TRP B CD2 1 
ATOM   3909 N NE1 . TRP B 1 207 ? -14.95600 -14.81500 -8.72600  1.000 38.22564  ? 207 TRP B NE1 1 
ATOM   3910 C CE2 . TRP B 1 207 ? -14.72600 -15.77800 -9.66600  1.000 36.77283  ? 207 TRP B CE2 1 
ATOM   3911 C CE3 . TRP B 1 207 ? -12.95800 -17.36400 -10.21600 1.000 39.50474  ? 207 TRP B CE3 1 
ATOM   3912 C CZ2 . TRP B 1 207 ? -15.40800 -16.05800 -10.83100 1.000 37.67031  ? 207 TRP B CZ2 1 
ATOM   3913 C CZ3 . TRP B 1 207 ? -13.67100 -17.66700 -11.38000 1.000 42.42088  ? 207 TRP B CZ3 1 
ATOM   3914 C CH2 . TRP B 1 207 ? -14.87500 -17.03700 -11.66100 1.000 36.54649  ? 207 TRP B CH2 1 
ATOM   3915 N N   . LEU B 1 208 ? -12.03800 -19.46300 -7.36000  1.000 36.35699  ? 208 LEU B N   1 
ATOM   3916 C CA  . LEU B 1 208 ? -12.75600 -20.72800 -7.45300  1.000 37.12550  ? 208 LEU B CA  1 
ATOM   3917 C C   . LEU B 1 208 ? -13.05200 -21.30400 -6.06500  1.000 40.71804  ? 208 LEU B C   1 
ATOM   3918 O O   . LEU B 1 208 ? -14.11800 -21.89300 -5.85600  1.000 38.73886  ? 208 LEU B O   1 
ATOM   3919 C CB  . LEU B 1 208 ? -11.97500 -21.75600 -8.29600  1.000 33.14082  ? 208 LEU B CB  1 
ATOM   3920 C CG  . LEU B 1 208 ? -11.86000 -21.35400 -9.79600  1.000 39.53369  ? 208 LEU B CG  1 
ATOM   3921 C CD1 . LEU B 1 208 ? -10.99600 -22.38700 -10.58200 1.000 40.58381  ? 208 LEU B CD1 1 
ATOM   3922 C CD2 . LEU B 1 208 ? -13.26000 -21.15100 -10.47300 1.000 39.53895  ? 208 LEU B CD2 1 
ATOM   3923 N N   . TYR B 1 209 ? -12.11900 -21.18400 -5.10300  1.000 37.39396  ? 209 TYR B N   1 
ATOM   3924 C CA  . TYR B 1 209 ? -12.44000 -21.68400 -3.76800  1.000 40.13113  ? 209 TYR B CA  1 
ATOM   3925 C C   . TYR B 1 209 ? -13.55000 -20.88900 -3.10600  1.000 40.76805  ? 209 TYR B C   1 
ATOM   3926 O O   . TYR B 1 209 ? -14.43400 -21.47600 -2.44400  1.000 41.67605  ? 209 TYR B O   1 
ATOM   3927 C CB  . TYR B 1 209 ? -11.23400 -21.65900 -2.87400  1.000 38.25195  ? 209 TYR B CB  1 
ATOM   3928 C CG  . TYR B 1 209 ? -10.34900 -22.83500 -3.10100  1.000 43.08148  ? 209 TYR B CG  1 
ATOM   3929 C CD1 . TYR B 1 209 ? -10.73100 -24.08700 -2.69400  1.000 44.53692  ? 209 TYR B CD1 1 
ATOM   3930 C CD2 . TYR B 1 209 ? -9.08300  -22.67100 -3.69900  1.000 40.92333  ? 209 TYR B CD2 1 
ATOM   3931 C CE1 . TYR B 1 209 ? -9.92600  -25.18400 -2.87800  1.000 45.17647  ? 209 TYR B CE1 1 
ATOM   3932 C CE2 . TYR B 1 209 ? -8.28800  -23.74800 -3.89500  1.000 42.91304  ? 209 TYR B CE2 1 
ATOM   3933 C CZ  . TYR B 1 209 ? -8.71300  -24.99200 -3.49400  1.000 45.83707  ? 209 TYR B CZ  1 
ATOM   3934 O OH  . TYR B 1 209 ? -7.91100  -26.07400 -3.68100  1.000 45.02645  ? 209 TYR B OH  1 
ATOM   3935 N N   . ALA B 1 210 ? -13.48600 -19.56400 -3.23300  1.000 38.34144  ? 210 ALA B N   1 
ATOM   3936 C CA  . ALA B 1 210 ? -14.57100 -18.70700 -2.78200  1.000 41.22336  ? 210 ALA B CA  1 
ATOM   3937 C C   . ALA B 1 210 ? -15.89200 -19.15600 -3.37000  1.000 41.52077  ? 210 ALA B C   1 
ATOM   3938 O O   . ALA B 1 210 ? -16.89400 -19.22900 -2.66100  1.000 43.21308  ? 210 ALA B O   1 
ATOM   3939 C CB  . ALA B 1 210 ? -14.30700 -17.27300 -3.21900  1.000 37.78874  ? 210 ALA B CB  1 
ATOM   3940 N N   . ALA B 1 211 ? -15.89300 -19.50400 -4.66400  1.000 37.98877  ? 211 ALA B N   1 
ATOM   3941 C CA  . ALA B 1 211 ? -17.12100 -19.94800 -5.32300  1.000 41.63131  ? 211 ALA B CA  1 
ATOM   3942 C C   . ALA B 1 211 ? -17.68600 -21.21200 -4.68500  1.000 45.47387  ? 211 ALA B C   1 
ATOM   3943 O O   . ALA B 1 211 ? -18.89200 -21.28800 -4.43800  1.000 40.99439  ? 211 ALA B O   1 
ATOM   3944 C CB  . ALA B 1 211 ? -16.88100 -20.17500 -6.81600  1.000 40.25483  ? 211 ALA B CB  1 
ATOM   3945 N N   . VAL B 1 212 ? -16.82600 -22.19100 -4.39000  1.000 44.90802  ? 212 VAL B N   1 
ATOM   3946 C CA  . VAL B 1 212 ? -17.23000 -23.42700 -3.71700  1.000 43.68155  ? 212 VAL B CA  1 
ATOM   3947 C C   . VAL B 1 212 ? -17.76500 -23.14900 -2.32700  1.000 47.20566  ? 212 VAL B C   1 
ATOM   3948 O O   . VAL B 1 212 ? -18.77200 -23.75900 -1.89500  1.000 45.54230  ? 212 VAL B O   1 
ATOM   3949 C CB  . VAL B 1 212 ? -16.04900 -24.42300 -3.66100  1.000 42.33666  ? 212 VAL B CB  1 
ATOM   3950 C CG1 . VAL B 1 212 ? -16.42500 -25.66600 -2.75700  1.000 46.22133  ? 212 VAL B CG1 1 
ATOM   3951 C CG2 . VAL B 1 212 ? -15.74200 -24.95100 -5.09400  1.000 39.94163  ? 212 VAL B CG2 1 
ATOM   3952 N N   . ILE B 1 213 ? -17.08600 -22.27400 -1.58500  1.000 44.08423  ? 213 ILE B N   1 
ATOM   3953 C CA  . ILE B 1 213 ? -17.51900 -21.89200 -0.23400  1.000 46.25028  ? 213 ILE B CA  1 
ATOM   3954 C C   . ILE B 1 213 ? -18.90500 -21.27900 -0.31100  1.000 49.19800  ? 213 ILE B C   1 
ATOM   3955 O O   . ILE B 1 213 ? -19.75800 -21.51800 0.55900   1.000 47.35831  ? 213 ILE B O   1 
ATOM   3956 C CB  . ILE B 1 213 ? -16.48700 -20.92400 0.40800   1.000 48.87428  ? 213 ILE B CB  1 
ATOM   3957 C CG1 . ILE B 1 213 ? -15.13000 -21.59500 0.66900   1.000 44.36321  ? 213 ILE B CG1 1 
ATOM   3958 C CG2 . ILE B 1 213 ? -16.99500 -20.26900 1.70400   1.000 45.87392  ? 213 ILE B CG2 1 
ATOM   3959 C CD1 . ILE B 1 213 ? -13.96600 -20.57600 1.00500   1.000 45.13173  ? 213 ILE B CD1 1 
ATOM   3960 N N   . ASN B 1 214 ? -19.20200 -20.59500 -1.40700  1.000 45.24753  ? 214 ASN B N   1 
ATOM   3961 C CA  . ASN B 1 214 ? -20.51600 -20.00500 -1.58500  1.000 47.88732  ? 214 ASN B CA  1 
ATOM   3962 C C   . ASN B 1 214 ? -21.52400 -20.89900 -2.30000  1.000 46.94247  ? 214 ASN B C   1 
ATOM   3963 O O   . ASN B 1 214 ? -22.53900 -20.36500 -2.76200  1.000 50.06390  ? 214 ASN B O   1 
ATOM   3964 C CB  . ASN B 1 214 ? -20.41000 -18.69600 -2.34100  1.000 44.64746  ? 214 ASN B CB  1 
ATOM   3965 C CG  . ASN B 1 214 ? -20.10100 -17.57600 -1.41800  1.000 52.05098  ? 214 ASN B CG  1 
ATOM   3966 O OD1 . ASN B 1 214 ? -21.02100 -16.93800 -0.90300  1.000 56.94630  ? 214 ASN B OD1 1 
ATOM   3967 N ND2 . ASN B 1 214 ? -18.79700 -17.35900 -1.13200  1.000 52.58262  ? 214 ASN B ND2 1 
ATOM   3968 N N   . GLY B 1 215 ? -21.22300 -22.18600 -2.53000  1.000 47.57939  ? 215 GLY B N   1 
ATOM   3969 C CA  . GLY B 1 215 ? -22.16000 -23.12300 -3.14000  1.000 48.96640  ? 215 GLY B CA  1 
ATOM   3970 C C   . GLY B 1 215 ? -22.03800 -23.32400 -4.65800  1.000 50.10601  ? 215 GLY B C   1 
ATOM   3971 O O   . GLY B 1 215 ? -22.78600 -24.13100 -5.21400  1.000 49.88493  ? 215 GLY B O   1 
ATOM   3972 N N   . ASP B 1 216 ? -21.19100 -22.58900 -5.37800  1.000 43.63944  ? 216 ASP B N   1 
ATOM   3973 C CA  . ASP B 1 216 ? -21.03200 -22.88400 -6.80800  1.000 48.70584  ? 216 ASP B CA  1 
ATOM   3974 C C   . ASP B 1 216 ? -20.10900 -24.10800 -6.93100  1.000 52.14573  ? 216 ASP B C   1 
ATOM   3975 O O   . ASP B 1 216 ? -18.93100 -24.03300 -6.57700  1.000 47.26093  ? 216 ASP B O   1 
ATOM   3976 C CB  . ASP B 1 216 ? -20.42800 -21.70600 -7.58300  1.000 50.17180  ? 216 ASP B CB  1 
ATOM   3977 C CG  . ASP B 1 216 ? -21.45900 -20.61300 -7.98200  1.000 58.10960  ? 216 ASP B CG  1 
ATOM   3978 O OD1 . ASP B 1 216 ? -22.61900 -20.97000 -8.31300  1.000 66.06845  ? 216 ASP B OD1 1 
ATOM   3979 O OD2 . ASP B 1 216 ? -21.08600 -19.39400 -7.97400  1.000 46.41083  ? 216 ASP B OD2 1 
ATOM   3980 N N   . ARG B 1 217 ? -20.61800 -25.25300 -7.41900  1.000 47.55570  ? 217 ARG B N   1 
ATOM   3981 C CA  . ARG B 1 217 ? -19.78500 -26.43400 -7.52200  1.000 46.32924  ? 217 ARG B CA  1 
ATOM   3982 C C   . ARG B 1 217 ? -19.77200 -27.04900 -8.90000  1.000 45.30543  ? 217 ARG B C   1 
ATOM   3983 O O   . ARG B 1 217 ? -19.14500 -28.10700 -9.07600  1.000 44.57640  ? 217 ARG B O   1 
ATOM   3984 C CB  . ARG B 1 217 ? -20.22400 -27.53700 -6.55000  1.000 50.25866  ? 217 ARG B CB  1 
ATOM   3985 C CG  . ARG B 1 217 ? -19.97500 -27.32700 -5.08800  1.000 53.25112  ? 217 ARG B CG  1 
ATOM   3986 C CD  . ARG B 1 217 ? -20.22900 -28.69200 -4.31200  1.000 52.94582  ? 217 ARG B CD  1 
ATOM   3987 N NE  . ARG B 1 217 ? -19.11400 -29.00300 -3.39900  1.000 55.45665  ? 217 ARG B NE  1 
ATOM   3988 C CZ  . ARG B 1 217 ? -18.24900 -30.00100 -3.56100  1.000 58.99918  ? 217 ARG B CZ  1 
ATOM   3989 N NH1 . ARG B 1 217 ? -18.27800 -30.78100 -4.61100  1.000 61.81267  ? 217 ARG B NH1 1 
ATOM   3990 N NH2 . ARG B 1 217 ? -17.31900 -30.22100 -2.64000  1.000 66.75274  ? 217 ARG B NH2 1 
ATOM   3991 N N   . TRP B 1 218 ? -20.45400 -26.43300 -9.86800  1.000 41.93398  ? 218 TRP B N   1 
ATOM   3992 C CA  . TRP B 1 218 ? -20.68000 -27.08900 -11.14300 1.000 45.20016  ? 218 TRP B CA  1 
ATOM   3993 C C   . TRP B 1 218 ? -19.39100 -27.31800 -11.91300 1.000 48.83480  ? 218 TRP B C   1 
ATOM   3994 O O   . TRP B 1 218 ? -19.34600 -28.20100 -12.77200 1.000 48.26368  ? 218 TRP B O   1 
ATOM   3995 C CB  . TRP B 1 218 ? -21.63900 -26.25400 -12.00600 1.000 48.50318  ? 218 TRP B CB  1 
ATOM   3996 C CG  . TRP B 1 218 ? -21.12500 -24.85000 -12.41000 1.000 47.03985  ? 218 TRP B CG  1 
ATOM   3997 C CD1 . TRP B 1 218 ? -21.45100 -23.66600 -11.80500 1.000 48.05050  ? 218 TRP B CD1 1 
ATOM   3998 C CD2 . TRP B 1 218 ? -20.20600 -24.50500 -13.49300 1.000 46.20291  ? 218 TRP B CD2 1 
ATOM   3999 N NE1 . TRP B 1 218 ? -20.82000 -22.63400 -12.44400 1.000 46.96879  ? 218 TRP B NE1 1 
ATOM   4000 C CE2 . TRP B 1 218 ? -20.06500 -23.11200 -13.48300 1.000 48.65057  ? 218 TRP B CE2 1 
ATOM   4001 C CE3 . TRP B 1 218 ? -19.54200 -25.23900 -14.48600 1.000 47.46622  ? 218 TRP B CE3 1 
ATOM   4002 C CZ2 . TRP B 1 218 ? -19.22600 -22.41700 -14.40400 1.000 49.05851  ? 218 TRP B CZ2 1 
ATOM   4003 C CZ3 . TRP B 1 218 ? -18.73300 -24.56300 -15.41500 1.000 51.05612  ? 218 TRP B CZ3 1 
ATOM   4004 C CH2 . TRP B 1 218 ? -18.56700 -23.16100 -15.35300 1.000 48.45055  ? 218 TRP B CH2 1 
ATOM   4005 N N   . PHE B 1 219 ? -18.36200 -26.49300 -11.66300 1.000 42.25507  ? 219 PHE B N   1 
ATOM   4006 C CA  . PHE B 1 219 ? -17.11200 -26.60100 -12.39900 1.000 46.41346  ? 219 PHE B CA  1 
ATOM   4007 C C   . PHE B 1 219 ? -16.18100 -27.64100 -11.79900 1.000 46.55821  ? 219 PHE B C   1 
ATOM   4008 O O   . PHE B 1 219 ? -15.10200 -27.88200 -12.35900 1.000 42.69196  ? 219 PHE B O   1 
ATOM   4009 C CB  . PHE B 1 219 ? -16.42200 -25.23400 -12.43700 1.000 42.23138  ? 219 PHE B CB  1 
ATOM   4010 C CG  . PHE B 1 219 ? -16.29500 -24.61500 -11.09300 1.000 40.41274  ? 219 PHE B CG  1 
ATOM   4011 C CD1 . PHE B 1 219 ? -15.26500 -24.98600 -10.26400 1.000 40.16008  ? 219 PHE B CD1 1 
ATOM   4012 C CD2 . PHE B 1 219 ? -17.27700 -23.72900 -10.62900 1.000 42.56563  ? 219 PHE B CD2 1 
ATOM   4013 C CE1 . PHE B 1 219 ? -15.15000 -24.44300 -8.99500  1.000 43.74209  ? 219 PHE B CE1 1 
ATOM   4014 C CE2 . PHE B 1 219 ? -17.21000 -23.18500 -9.34400  1.000 42.41561  ? 219 PHE B CE2 1 
ATOM   4015 C CZ  . PHE B 1 219 ? -16.12200 -23.53500 -8.51100  1.000 41.07071  ? 219 PHE B CZ  1 
ATOM   4016 N N   . LEU B 1 220 ? -16.54400 -28.27000 -10.67400 1.000 43.36836  ? 220 LEU B N   1 
ATOM   4017 C CA  . LEU B 1 220 ? -15.65300 -29.29700 -10.12700 1.000 46.15027  ? 220 LEU B CA  1 
ATOM   4018 C C   . LEU B 1 220 ? -15.70100 -30.57700 -10.96800 1.000 47.01090  ? 220 LEU B C   1 
ATOM   4019 O O   . LEU B 1 220 ? -16.64300 -30.83700 -11.72000 1.000 47.54781  ? 220 LEU B O   1 
ATOM   4020 C CB  . LEU B 1 220 ? -15.97900 -29.56700 -8.65500  1.000 46.65033  ? 220 LEU B CB  1 
ATOM   4021 C CG  . LEU B 1 220 ? -15.75000 -28.33500 -7.76400  1.000 45.42650  ? 220 LEU B CG  1 
ATOM   4022 C CD1 . LEU B 1 220 ? -16.31000 -28.67900 -6.40300  1.000 47.73467  ? 220 LEU B CD1 1 
ATOM   4023 C CD2 . LEU B 1 220 ? -14.21300 -27.93800 -7.63600  1.000 41.51550  ? 220 LEU B CD2 1 
ATOM   4024 N N   . ASN B 1 221 ? -14.62600 -31.36500 -10.89000 1.000 49.90598  ? 221 ASN B N   1 
ATOM   4025 C CA  . ASN B 1 221 ? -14.60300 -32.63700 -11.59000 1.000 48.20841  ? 221 ASN B CA  1 
ATOM   4026 C C   . ASN B 1 221 ? -13.80800 -33.61300 -10.74600 1.000 50.11390  ? 221 ASN B C   1 
ATOM   4027 O O   . ASN B 1 221 ? -13.17700 -33.23900 -9.75800  1.000 44.87907  ? 221 ASN B O   1 
ATOM   4028 C CB  . ASN B 1 221 ? -14.03900 -32.53600 -13.01900 1.000 50.37972  ? 221 ASN B CB  1 
ATOM   4029 C CG  . ASN B 1 221 ? -12.60900 -32.01700 -13.04700 1.000 53.56695  ? 221 ASN B CG  1 
ATOM   4030 O OD1 . ASN B 1 221 ? -11.81700 -32.31000 -12.15500 1.000 53.30113  ? 221 ASN B OD1 1 
ATOM   4031 N ND2 . ASN B 1 221 ? -12.30900 -31.16300 -14.01800 1.000 53.78803  ? 221 ASN B ND2 1 
ATOM   4032 N N   . ARG B 1 222 ? -13.85100 -34.87600 -11.13000 1.000 50.88242  ? 222 ARG B N   1 
ATOM   4033 C CA  . ARG B 1 222 ? -13.17600 -35.88300 -10.33000 1.000 52.10625  ? 222 ARG B CA  1 
ATOM   4034 C C   . ARG B 1 222 ? -11.69600 -36.02500 -10.67100 1.000 53.41430  ? 222 ARG B C   1 
ATOM   4035 O O   . ARG B 1 222 ? -11.03500 -36.89200 -10.10500 1.000 54.50654  ? 222 ARG B O   1 
ATOM   4036 C CB  . ARG B 1 222 ? -13.82800 -37.21600 -10.53300 1.000 57.96221  ? 222 ARG B CB  1 
ATOM   4037 C CG  . ARG B 1 222 ? -14.39100 -37.34500 -11.91000 1.000 64.34193  ? 222 ARG B CG  1 
ATOM   4038 C CD  . ARG B 1 222 ? -13.73000 -38.43300 -12.65000 1.000 67.77655  ? 222 ARG B CD  1 
ATOM   4039 N NE  . ARG B 1 222 ? -14.49500 -39.01100 -13.75600 1.000 58.48333  ? 222 ARG B NE  1 
ATOM   4040 C CZ  . ARG B 1 222 ? -14.05800 -40.07300 -14.41700 1.000 67.84498  ? 222 ARG B CZ  1 
ATOM   4041 N NH1 . ARG B 1 222 ? -13.06000 -40.81000 -13.95500 1.000 69.72678  ? 222 ARG B NH1 1 
ATOM   4042 N NH2 . ARG B 1 222 ? -14.63300 -40.41500 -15.57000 1.000 76.54076  ? 222 ARG B NH2 1 
ATOM   4043 N N   . PHE B 1 223 ? -11.20800 -35.26100 -11.63100 1.000 52.99583  ? 223 PHE B N   1 
ATOM   4044 C CA  . PHE B 1 223 ? -9.83400  -35.37500 -12.09800 1.000 53.15111  ? 223 PHE B CA  1 
ATOM   4045 C C   . PHE B 1 223 ? -8.87100  -34.58200 -11.24100 1.000 52.62999  ? 223 PHE B C   1 
ATOM   4046 O O   . PHE B 1 223 ? -9.21000  -33.61500 -10.56000 1.000 51.99834  ? 223 PHE B O   1 
ATOM   4047 C CB  . PHE B 1 223 ? -9.70500  -34.91100 -13.54800 1.000 51.42195  ? 223 PHE B CB  1 
ATOM   4048 C CG  . PHE B 1 223 ? -10.53400 -35.72200 -14.49400 1.000 57.16475  ? 223 PHE B CG  1 
ATOM   4049 C CD1 . PHE B 1 223 ? -10.25200 -37.05500 -14.70800 1.000 59.75716  ? 223 PHE B CD1 1 
ATOM   4050 C CD2 . PHE B 1 223 ? -11.61700 -35.16000 -15.14900 1.000 60.94415  ? 223 PHE B CD2 1 
ATOM   4051 C CE1 . PHE B 1 223 ? -11.03500 -37.81200 -15.57700 1.000 64.74460  ? 223 PHE B CE1 1 
ATOM   4052 C CE2 . PHE B 1 223 ? -12.37500 -35.89800 -16.01500 1.000 58.45964  ? 223 PHE B CE2 1 
ATOM   4053 C CZ  . PHE B 1 223 ? -12.08900 -37.23000 -16.22000 1.000 61.37841  ? 223 PHE B CZ  1 
ATOM   4054 N N   . THR B 1 224 ? -7.62700  -34.97000 -11.34900 1.000 52.10098  ? 224 THR B N   1 
ATOM   4055 C CA  . THR B 1 224 ? -6.53800  -34.21700 -10.76500 1.000 55.45402  ? 224 THR B CA  1 
ATOM   4056 C C   . THR B 1 224 ? -5.45200  -34.09900 -11.83500 1.000 55.39085  ? 224 THR B C   1 
ATOM   4057 O O   . THR B 1 224 ? -5.46000  -34.81800 -12.83400 1.000 58.14381  ? 224 THR B O   1 
ATOM   4058 C CB  . THR B 1 224 ? -6.04100  -34.92700 -9.49400  1.000 59.51766  ? 224 THR B CB  1 
ATOM   4059 O OG1 . THR B 1 224 ? -5.10100  -34.07800 -8.80100  1.000 62.52329  ? 224 THR B OG1 1 
ATOM   4060 C CG2 . THR B 1 224 ? -5.36100  -36.26600 -9.85900  1.000 57.34109  ? 224 THR B CG2 1 
ATOM   4061 N N   . THR B 1 225 ? -4.51700  -33.19700 -11.61400 1.000 58.88601  ? 225 THR B N   1 
ATOM   4062 C CA  . THR B 1 225 ? -3.45000  -32.93800 -12.56800 1.000 57.00420  ? 225 THR B CA  1 
ATOM   4063 C C   . THR B 1 225 ? -2.14400  -32.83000 -11.79600 1.000 56.42519  ? 225 THR B C   1 
ATOM   4064 O O   . THR B 1 225 ? -2.14000  -32.56500 -10.59500 1.000 53.56958  ? 225 THR B O   1 
ATOM   4065 C CB  . THR B 1 225 ? -3.73700  -31.65100 -13.34800 1.000 55.24873  ? 225 THR B CB  1 
ATOM   4066 O OG1 . THR B 1 225 ? -2.64900  -31.37600 -14.26500 1.000 57.73587  ? 225 THR B OG1 1 
ATOM   4067 C CG2 . THR B 1 225 ? -3.83100  -30.49300 -12.40300 1.000 52.68000  ? 225 THR B CG2 1 
ATOM   4068 N N   . THR B 1 226 ? -1.01400  -32.97200 -12.49600 1.000 59.05182  ? 226 THR B N   1 
ATOM   4069 C CA  . THR B 1 226 ? 0.25100   -32.62400 -11.86700 1.000 56.40413  ? 226 THR B CA  1 
ATOM   4070 C C   . THR B 1 226 ? 0.52000   -31.13200 -11.99700 1.000 56.07514  ? 226 THR B C   1 
ATOM   4071 O O   . THR B 1 226 ? 0.02700   -30.47100 -12.91200 1.000 56.93577  ? 226 THR B O   1 
ATOM   4072 C CB  . THR B 1 226 ? 1.42600   -33.39300 -12.50300 1.000 62.39695  ? 226 THR B CB  1 
ATOM   4073 O OG1 . THR B 1 226 ? 1.53600   -33.03100 -13.88400 1.000 62.46802  ? 226 THR B OG1 1 
ATOM   4074 C CG2 . THR B 1 226 ? 1.25200   -34.91400 -12.36800 1.000 61.41526  ? 226 THR B CG2 1 
ATOM   4075 N N   . LEU B 1 227 ? 1.33500   -30.59500 -11.08700 1.000 55.32505  ? 227 LEU B N   1 
ATOM   4076 C CA  . LEU B 1 227 ? 1.67600   -29.18000 -11.18600 1.000 56.94104  ? 227 LEU B CA  1 
ATOM   4077 C C   . LEU B 1 227 ? 2.30400   -28.84600 -12.53900 1.000 59.83349  ? 227 LEU B C   1 
ATOM   4078 O O   . LEU B 1 227 ? 1.97800   -27.81200 -13.15500 1.000 52.35628  ? 227 LEU B O   1 
ATOM   4079 C CB  . LEU B 1 227 ? 2.60800   -28.79500 -10.03400 1.000 54.21176  ? 227 LEU B CB  1 
ATOM   4080 C CG  . LEU B 1 227 ? 2.94400   -27.33100 -9.85400  1.000 56.81471  ? 227 LEU B CG  1 
ATOM   4081 C CD1 . LEU B 1 227 ? 1.68400   -26.47000 -9.67000  1.000 51.12455  ? 227 LEU B CD1 1 
ATOM   4082 C CD2 . LEU B 1 227 ? 3.92800   -27.15600 -8.68400  1.000 58.50175  ? 227 LEU B CD2 1 
ATOM   4083 N N   . ASN B 1 228 ? 3.20900   -29.71500 -13.01300 1.000 58.85706  ? 228 ASN B N   1 
ATOM   4084 C CA  . ASN B 1 228 ? 3.87500   -29.48900 -14.29000 1.000 61.32577  ? 228 ASN B CA  1 
ATOM   4085 C C   . ASN B 1 228 ? 2.90400   -29.54100 -15.46100 1.000 59.60188  ? 228 ASN B C   1 
ATOM   4086 O O   . ASN B 1 228 ? 2.95800   -28.68000 -16.34700 1.000 57.80693  ? 228 ASN B O   1 
ATOM   4087 C CB  . ASN B 1 228 ? 5.01800   -30.49600 -14.47100 1.000 67.83445  ? 228 ASN B CB  1 
ATOM   4088 C CG  . ASN B 1 228 ? 6.18600   -30.19000 -13.54100 1.000 75.53537  ? 228 ASN B CG  1 
ATOM   4089 O OD1 . ASN B 1 228 ? 6.37200   -29.04100 -13.11400 1.000 82.65465  ? 228 ASN B OD1 1 
ATOM   4090 N ND2 . ASN B 1 228 ? 6.98000   -31.20200 -13.23400 1.000 78.84366  ? 228 ASN B ND2 1 
ATOM   4091 N N   . ASP B 1 229 ? 1.99700   -30.52900 -15.48000 1.000 58.40700  ? 229 ASP B N   1 
ATOM   4092 C CA  . ASP B 1 229 ? 1.00100   -30.57600 -16.54900 1.000 57.68586  ? 229 ASP B CA  1 
ATOM   4093 C C   . ASP B 1 229 ? 0.05300   -29.38200 -16.49200 1.000 57.35688  ? 229 ASP B C   1 
ATOM   4094 O O   . ASP B 1 229 ? -0.40000  -28.89400 -17.54100 1.000 55.97250  ? 229 ASP B O   1 
ATOM   4095 C CB  . ASP B 1 229 ? 0.21400   -31.87800 -16.51700 1.000 64.39193  ? 229 ASP B CB  1 
ATOM   4096 C CG  . ASP B 1 229 ? 1.05400   -33.07400 -16.97600 1.000 69.90838  ? 229 ASP B CG  1 
ATOM   4097 O OD1 . ASP B 1 229 ? 2.10200   -32.87200 -17.65900 1.000 66.39480  ? 229 ASP B OD1 1 
ATOM   4098 O OD2 . ASP B 1 229 ? 0.63200   -34.20700 -16.67700 1.000 66.66589  ? 229 ASP B OD2 1 
ATOM   4099 N N   . PHE B 1 230 ? -0.26500  -28.89800 -15.28900 1.000 55.13819  ? 230 PHE B N   1 
ATOM   4100 C CA  . PHE B 1 230 ? -1.09600  -27.69800 -15.21900 1.000 52.85107  ? 230 PHE B CA  1 
ATOM   4101 C C   . PHE B 1 230 ? -0.36900  -26.48900 -15.76800 1.000 53.68012  ? 230 PHE B C   1 
ATOM   4102 O O   . PHE B 1 230 ? -0.94800  -25.71100 -16.53300 1.000 51.03243  ? 230 PHE B O   1 
ATOM   4103 C CB  . PHE B 1 230 ? -1.54000  -27.40900 -13.80700 1.000 51.01928  ? 230 PHE B CB  1 
ATOM   4104 C CG  . PHE B 1 230 ? -2.24300  -26.09400 -13.68500 1.000 48.99535  ? 230 PHE B CG  1 
ATOM   4105 C CD1 . PHE B 1 230 ? -3.56200  -25.95700 -14.15300 1.000 48.19788  ? 230 PHE B CD1 1 
ATOM   4106 C CD2 . PHE B 1 230 ? -1.63000  -25.02700 -13.08000 1.000 44.85275  ? 230 PHE B CD2 1 
ATOM   4107 C CE1 . PHE B 1 230 ? -4.22200  -24.74300 -14.04000 1.000 47.39516  ? 230 PHE B CE1 1 
ATOM   4108 C CE2 . PHE B 1 230 ? -2.29200  -23.79600 -12.96000 1.000 47.35831  ? 230 PHE B CE2 1 
ATOM   4109 C CZ  . PHE B 1 230 ? -3.58000  -23.66400 -13.45500 1.000 48.53477  ? 230 PHE B CZ  1 
ATOM   4110 N N   . ASN B 1 231 ? 0.91000   -26.30900 -15.39500 1.000 51.42985  ? 231 ASN B N   1 
ATOM   4111 C CA  . ASN B 1 231 ? 1.62600   -25.13100 -15.87600 1.000 52.12204  ? 231 ASN B CA  1 
ATOM   4112 C C   . ASN B 1 231 ? 1.78500   -25.17700 -17.39000 1.000 53.95647  ? 231 ASN B C   1 
ATOM   4113 O O   . ASN B 1 231 ? 1.80100   -24.13200 -18.04400 1.000 55.91986  ? 231 ASN B O   1 
ATOM   4114 C CB  . ASN B 1 231 ? 2.97000   -25.01200 -15.14100 1.000 50.94558  ? 231 ASN B CB  1 
ATOM   4115 C CG  . ASN B 1 231 ? 2.78400   -24.41500 -13.75700 1.000 54.58549  ? 231 ASN B CG  1 
ATOM   4116 O OD1 . ASN B 1 231 ? 1.86600   -23.58000 -13.55900 1.000 53.24323  ? 231 ASN B OD1 1 
ATOM   4117 N ND2 . ASN B 1 231 ? 3.58500   -24.86500 -12.77900 1.000 51.66672  ? 231 ASN B ND2 1 
ATOM   4118 N N   . LEU B 1 232 ? 1.81800   -26.37300 -17.96800 1.000 55.48823  ? 232 LEU B N   1 
ATOM   4119 C CA  . LEU B 1 232 ? 1.82100   -26.48900 -19.42200 1.000 56.01461  ? 232 LEU B CA  1 
ATOM   4120 C C   . LEU B 1 232 ? 0.59100   -25.82400 -20.01900 1.000 55.46454  ? 232 LEU B C   1 
ATOM   4121 O O   . LEU B 1 232 ? 0.70500   -24.97200 -20.91200 1.000 52.89318  ? 232 LEU B O   1 
ATOM   4122 C CB  . LEU B 1 232 ? 1.89200   -27.96600 -19.80600 1.000 59.04392  ? 232 LEU B CB  1 
ATOM   4123 C CG  . LEU B 1 232 ? 3.34400   -28.51700 -19.74200 1.000 56.66206  ? 232 LEU B CG  1 
ATOM   4124 C CD1 . LEU B 1 232 ? 3.33900   -29.87200 -20.36300 1.000 58.24646  ? 232 LEU B CD1 1 
ATOM   4125 C CD2 . LEU B 1 232 ? 4.41200   -27.57900 -20.38500 1.000 55.52245  ? 232 LEU B CD2 1 
ATOM   4126 N N   . VAL B 1 233 ? -0.58500  -26.10200 -19.43900 1.000 55.97776  ? 233 VAL B N   1 
ATOM   4127 C CA  . VAL B 1 233 ? -1.81700  -25.46800 -19.89200 1.000 52.82475  ? 233 VAL B CA  1 
ATOM   4128 C C   . VAL B 1 233 ? -1.84000  -23.98600 -19.57000 1.000 51.02980  ? 233 VAL B C   1 
ATOM   4129 O O   . VAL B 1 233 ? -2.30700  -23.17300 -20.38100 1.000 49.81387  ? 233 VAL B O   1 
ATOM   4130 C CB  . VAL B 1 233 ? -3.01600  -26.19800 -19.26500 1.000 53.11953  ? 233 VAL B CB  1 
ATOM   4131 C CG1 . VAL B 1 233 ? -4.32800  -25.51000 -19.67300 1.000 54.19860  ? 233 VAL B CG1 1 
ATOM   4132 C CG2 . VAL B 1 233 ? -2.98700  -27.65500 -19.69500 1.000 59.47029  ? 233 VAL B CG2 1 
ATOM   4133 N N   . ALA B 1 234 ? -1.37600  -23.60200 -18.36600 1.000 52.10625  ? 234 ALA B N   1 
ATOM   4134 C CA  . ALA B 1 234 ? -1.32200  -22.19100 -17.97900 1.000 52.52998  ? 234 ALA B CA  1 
ATOM   4135 C C   . ALA B 1 234 ? -0.53600  -21.35000 -18.98600 1.000 50.89294  ? 234 ALA B C   1 
ATOM   4136 O O   . ALA B 1 234 ? -0.96700  -20.26300 -19.37300 1.000 48.52424  ? 234 ALA B O   1 
ATOM   4137 C CB  . ALA B 1 234 ? -0.69000  -22.03200 -16.58500 1.000 51.31142  ? 234 ALA B CB  1 
ATOM   4138 N N   . MET B 1 235 ? 0.62100   -21.82800 -19.41100 1.000 53.46957  ? 235 MET B N   1 
ATOM   4139 C CA  . MET B 1 235 ? 1.40900   -21.05400 -20.38200 1.000 55.01449  ? 235 MET B CA  1 
ATOM   4140 C C   . MET B 1 235 ? 0.60300   -20.80700 -21.65200 1.000 52.80107  ? 235 MET B C   1 
ATOM   4141 O O   . MET B 1 235 ? 0.45300   -19.66400 -22.08700 1.000 53.09847  ? 235 MET B O   1 
ATOM   4142 C CB  . MET B 1 235 ? 2.70300   -21.80800 -20.69600 1.000 57.31740  ? 235 MET B CB  1 
ATOM   4143 C CG  . MET B 1 235 ? 3.72300   -21.04800 -21.53100 1.000 61.82583  ? 235 MET B CG  1 
ATOM   4144 S SD  . MET B 1 235 ? 5.30400   -21.87900 -21.23200 1.000 74.75896  ? 235 MET B SD  1 
ATOM   4145 C CE  . MET B 1 235 ? 5.37500   -21.79700 -19.42700 1.000 71.03483  ? 235 MET B CE  1 
ATOM   4146 N N   . LYS B 1 236 ? -0.09300  -21.83900 -22.12900 1.000 54.73551  ? 236 LYS B N   1 
ATOM   4147 C CA  . LYS B 1 236 ? -0.85300  -21.71800 -23.36100 1.000 52.65631  ? 236 LYS B CA  1 
ATOM   4148 C C   . LYS B 1 236 ? -1.93700  -20.65300 -23.26100 1.000 54.68287  ? 236 LYS B C   1 
ATOM   4149 O O   . LYS B 1 236 ? -2.22500  -19.98400 -24.25900 1.000 55.34874  ? 236 LYS B O   1 
ATOM   4150 C CB  . LYS B 1 236 ? -1.41800  -23.10200 -23.74100 1.000 53.70907  ? 236 LYS B CB  1 
ATOM   4151 C CG  . LYS B 1 236 ? -2.43500  -23.09800 -24.84700 1.000 60.10194  ? 236 LYS B CG  1 
ATOM   4152 C CD  . LYS B 1 236 ? -2.79200  -24.52100 -25.31800 1.000 71.13484  ? 236 LYS B CD  1 
ATOM   4153 C CE  . LYS B 1 236 ? -4.00800  -24.50600 -26.26700 1.000 84.60488  ? 236 LYS B CE  1 
ATOM   4154 N NZ  . LYS B 1 236 ? -3.82000  -23.63000 -27.47600 1.000 92.17158  ? 236 LYS B NZ  1 
ATOM   4155 N N   . TYR B 1 237 ? -2.53200  -20.43700 -22.07200 1.000 50.87452  ? 237 TYR B N   1 
ATOM   4156 C CA  . TYR B 1 237 ? -3.59300  -19.44400 -21.91900 1.000 51.68514  ? 237 TYR B CA  1 
ATOM   4157 C C   . TYR B 1 237 ? -3.09600  -18.15600 -21.27400 1.000 51.24035  ? 237 TYR B C   1 
ATOM   4158 O O   . TYR B 1 237 ? -3.91500  -17.36500 -20.80800 1.000 48.39264  ? 237 TYR B O   1 
ATOM   4159 C CB  . TYR B 1 237 ? -4.77000  -20.01100 -21.11400 1.000 50.04547  ? 237 TYR B CB  1 
ATOM   4160 C CG  . TYR B 1 237 ? -5.50400  -21.04800 -21.91300 1.000 52.28258  ? 237 TYR B CG  1 
ATOM   4161 C CD1 . TYR B 1 237 ? -6.54900  -20.68600 -22.76400 1.000 48.45581  ? 237 TYR B CD1 1 
ATOM   4162 C CD2 . TYR B 1 237 ? -5.10300  -22.38900 -21.87900 1.000 50.37972  ? 237 TYR B CD2 1 
ATOM   4163 C CE1 . TYR B 1 237 ? -7.18800  -21.65000 -23.55600 1.000 52.80107  ? 237 TYR B CE1 1 
ATOM   4164 C CE2 . TYR B 1 237 ? -5.76200  -23.35300 -22.65000 1.000 52.53525  ? 237 TYR B CE2 1 
ATOM   4165 C CZ  . TYR B 1 237 ? -6.77900  -22.97100 -23.48300 1.000 51.34300  ? 237 TYR B CZ  1 
ATOM   4166 O OH  . TYR B 1 237 ? -7.40700  -23.90800 -24.23500 1.000 59.16499  ? 237 TYR B OH  1 
ATOM   4167 N N   . ASN B 1 238 ? -1.77400  -17.91700 -21.27800 1.000 50.32182  ? 238 ASN B N   1 
ATOM   4168 C CA  . ASN B 1 238 ? -1.21000  -16.66000 -20.77500 1.000 48.22683  ? 238 ASN B CA  1 
ATOM   4169 C C   . ASN B 1 238 ? -1.53900  -16.45600 -19.27800 1.000 50.13496  ? 238 ASN B C   1 
ATOM   4170 O O   . ASN B 1 238 ? -1.95200  -15.37300 -18.83300 1.000 47.28725  ? 238 ASN B O   1 
ATOM   4171 C CB  . ASN B 1 238 ? -1.71500  -15.49000 -21.61500 1.000 50.51922  ? 238 ASN B CB  1 
ATOM   4172 C CG  . ASN B 1 238 ? -0.97200  -14.22400 -21.31800 1.000 56.92261  ? 238 ASN B CG  1 
ATOM   4173 O OD1 . ASN B 1 238 ? 0.16900   -14.27500 -20.86100 1.000 61.39947  ? 238 ASN B OD1 1 
ATOM   4174 N ND2 . ASN B 1 238 ? -1.63200  -13.07500 -21.50700 1.000 55.04081  ? 238 ASN B ND2 1 
ATOM   4175 N N   . TYR B 1 239 ? -1.39800  -17.54600 -18.53600 1.000 44.85011  ? 239 TYR B N   1 
ATOM   4176 C CA  . TYR B 1 239 ? -1.58700  -17.47800 -17.07800 1.000 44.43691  ? 239 TYR B CA  1 
ATOM   4177 C C   . TYR B 1 239 ? -0.20400  -17.58800 -16.45000 1.000 46.77666  ? 239 TYR B C   1 
ATOM   4178 O O   . TYR B 1 239 ? 0.64000   -18.30100 -16.99600 1.000 47.85047  ? 239 TYR B O   1 
ATOM   4179 C CB  . TYR B 1 239 ? -2.44200  -18.64900 -16.60300 1.000 41.33390  ? 239 TYR B CB  1 
ATOM   4180 C CG  . TYR B 1 239 ? -3.92400  -18.40400 -16.51700 1.000 44.73957  ? 239 TYR B CG  1 
ATOM   4181 C CD1 . TYR B 1 239 ? -4.63400  -17.89000 -17.58700 1.000 45.52125  ? 239 TYR B CD1 1 
ATOM   4182 C CD2 . TYR B 1 239 ? -4.62200  -18.71600 -15.36400 1.000 43.93685  ? 239 TYR B CD2 1 
ATOM   4183 C CE1 . TYR B 1 239 ? -5.99900  -17.67400 -17.50700 1.000 42.44983  ? 239 TYR B CE1 1 
ATOM   4184 C CE2 . TYR B 1 239 ? -5.98600  -18.51000 -15.26800 1.000 43.20781  ? 239 TYR B CE2 1 
ATOM   4185 C CZ  . TYR B 1 239 ? -6.67600  -17.98800 -16.34300 1.000 43.07885  ? 239 TYR B CZ  1 
ATOM   4186 O OH  . TYR B 1 239 ? -8.02300  -17.78100 -16.24200 1.000 42.89462  ? 239 TYR B OH  1 
ATOM   4187 N N   . GLU B 1 240 ? 0.01700   -16.89700 -15.34400 1.000 45.35807  ? 240 GLU B N   1 
ATOM   4188 C CA  . GLU B 1 240 ? 1.28300   -16.98500 -14.62000 1.000 44.91591  ? 240 GLU B CA  1 
ATOM   4189 C C   . GLU B 1 240 ? 1.52400   -18.44100 -14.24400 1.000 47.40568  ? 240 GLU B C   1 
ATOM   4190 O O   . GLU B 1 240 ? 0.56800   -19.20000 -14.02500 1.000 43.51838  ? 240 GLU B O   1 
ATOM   4191 C CB  . GLU B 1 240 ? 1.26300   -16.16500 -13.32300 1.000 44.53166  ? 240 GLU B CB  1 
ATOM   4192 C CG  . GLU B 1 240 ? 1.13700   -14.68900 -13.48200 1.000 52.13520  ? 240 GLU B CG  1 
ATOM   4193 C CD  . GLU B 1 240 ? 2.47600   -14.01500 -13.57500 1.000 64.13664  ? 240 GLU B CD  1 
ATOM   4194 O OE1 . GLU B 1 240 ? 3.21600   -14.08100 -12.56500 1.000 72.02443  ? 240 GLU B OE1 1 
ATOM   4195 O OE2 . GLU B 1 240 ? 2.81700   -13.49300 -14.66700 1.000 67.66601  ? 240 GLU B OE2 1 
ATOM   4196 N N   . PRO B 1 241 ? 2.77600   -18.86500 -14.18000 1.000 49.90072  ? 241 PRO B N   1 
ATOM   4197 C CA  . PRO B 1 241 ? 3.06000   -20.21700 -13.67400 1.000 45.80286  ? 241 PRO B CA  1 
ATOM   4198 C C   . PRO B 1 241 ? 2.63200   -20.35200 -12.22100 1.000 49.94809  ? 241 PRO B C   1 
ATOM   4199 O O   . PRO B 1 241 ? 2.67300   -19.38700 -11.44200 1.000 51.13245  ? 241 PRO B O   1 
ATOM   4200 C CB  . PRO B 1 241 ? 4.58000   -20.35200 -13.83900 1.000 53.75118  ? 241 PRO B CB  1 
ATOM   4201 C CG  . PRO B 1 241 ? 4.92900   -19.33600 -14.94200 1.000 49.69806  ? 241 PRO B CG  1 
ATOM   4202 C CD  . PRO B 1 241 ? 3.98700   -18.17800 -14.70600 1.000 48.99798  ? 241 PRO B CD  1 
ATOM   4203 N N   . LEU B 1 242 ? 2.15900   -21.54400 -11.87200 1.000 48.48213  ? 242 LEU B N   1 
ATOM   4204 C CA  . LEU B 1 242 ? 1.77500   -21.83700 -10.50500 1.000 50.87978  ? 242 LEU B CA  1 
ATOM   4205 C C   . LEU B 1 242 ? 2.93500   -22.53300 -9.81100  1.000 51.73778  ? 242 LEU B C   1 
ATOM   4206 O O   . LEU B 1 242 ? 3.38100   -23.59800 -10.24600 1.000 50.98243  ? 242 LEU B O   1 
ATOM   4207 C CB  . LEU B 1 242 ? 0.51900   -22.72200 -10.45500 1.000 45.54230  ? 242 LEU B CB  1 
ATOM   4208 C CG  . LEU B 1 242 ? -0.03900  -22.77800 -9.04000  1.000 46.83719  ? 242 LEU B CG  1 
ATOM   4209 C CD1 . LEU B 1 242 ? -0.74700  -21.45900 -8.75600  1.000 46.67139  ? 242 LEU B CD1 1 
ATOM   4210 C CD2 . LEU B 1 242 ? -1.02000  -23.97300 -8.91300  1.000 44.34742  ? 242 LEU B CD2 1 
ATOM   4211 N N   . THR B 1 243 ? 3.37700   -21.96300 -8.71000  1.000 50.42710  ? 243 THR B N   1 
ATOM   4212 C CA  . THR B 1 243 ? 4.51900   -22.49600 -7.99100  1.000 53.32745  ? 243 THR B CA  1 
ATOM   4213 C C   . THR B 1 243 ? 4.06800   -23.27900 -6.77400  1.000 56.87787  ? 243 THR B C   1 
ATOM   4214 O O   . THR B 1 243 ? 2.92700   -23.15300 -6.29000  1.000 49.95862  ? 243 THR B O   1 
ATOM   4215 C CB  . THR B 1 243 ? 5.41500   -21.35300 -7.56900  1.000 54.47232  ? 243 THR B CB  1 
ATOM   4216 O OG1 . THR B 1 243 ? 4.75500   -20.63300 -6.52100  1.000 53.26691  ? 243 THR B OG1 1 
ATOM   4217 C CG2 . THR B 1 243 ? 5.61800   -20.41700 -8.75200  1.000 54.73814  ? 243 THR B CG2 1 
ATOM   4218 N N   . GLN B 1 244 ? 5.01200   -24.05100 -6.23100  1.000 53.79066  ? 244 GLN B N   1 
ATOM   4219 C CA  . GLN B 1 244 ? 4.72400   -24.76000 -4.99000  1.000 57.49110  ? 244 GLN B CA  1 
ATOM   4220 C C   . GLN B 1 244 ? 4.40700   -23.77300 -3.87100  1.000 55.93302  ? 244 GLN B C   1 
ATOM   4221 O O   . GLN B 1 244 ? 3.55400   -24.05200 -3.01900  1.000 56.03040  ? 244 GLN B O   1 
ATOM   4222 C CB  . GLN B 1 244 ? 5.90100   -25.68600 -4.61600  1.000 56.65679  ? 244 GLN B CB  1 
ATOM   4223 C CG  . GLN B 1 244 ? 5.60900   -26.58500 -3.41100  1.000 58.18856  ? 244 GLN B CG  1 
ATOM   4224 C CD  . GLN B 1 244 ? 4.36500   -27.45200 -3.59100  1.000 60.45462  ? 244 GLN B CD  1 
ATOM   4225 O OE1 . GLN B 1 244 ? 3.59200   -27.64700 -2.64200  1.000 63.02071  ? 244 GLN B OE1 1 
ATOM   4226 N NE2 . GLN B 1 244 ? 4.15900   -27.98400 -4.80100  1.000 60.52831  ? 244 GLN B NE2 1 
ATOM   4227 N N   . ASP B 1 245 ? 5.00900   -22.58300 -3.90300  1.000 54.31441  ? 245 ASP B N   1 
ATOM   4228 C CA  . ASP B 1 245 ? 4.66900   -21.60400 -2.88200  1.000 54.90132  ? 245 ASP B CA  1 
ATOM   4229 C C   . ASP B 1 245 ? 3.19700   -21.19700 -2.96600  1.000 56.56994  ? 245 ASP B C   1 
ATOM   4230 O O   . ASP B 1 245 ? 2.53300   -21.06700 -1.93700  1.000 56.00672  ? 245 ASP B O   1 
ATOM   4231 C CB  . ASP B 1 245 ? 5.58100   -20.38000 -2.99300  1.000 59.65715  ? 245 ASP B CB  1 
ATOM   4232 C CG  . ASP B 1 245 ? 5.45800   -19.43800 -1.78500  1.000 66.45270  ? 245 ASP B CG  1 
ATOM   4233 O OD1 . ASP B 1 245 ? 5.22300   -19.91900 -0.65000  1.000 68.71877  ? 245 ASP B OD1 1 
ATOM   4234 O OD2 . ASP B 1 245 ? 5.59000   -18.20800 -1.97200  1.000 80.97287  ? 245 ASP B OD2 1 
ATOM   4235 N N   . HIS B 1 246 ? 2.69000   -20.96900 -4.18700  1.000 53.67222  ? 246 HIS B N   1 
ATOM   4236 C CA  . HIS B 1 246 ? 1.27300   -20.70300 -4.40400  1.000 51.65356  ? 246 HIS B CA  1 
ATOM   4237 C C   . HIS B 1 246 ? 0.41700   -21.85200 -3.89800  1.000 52.84581  ? 246 HIS B C   1 
ATOM   4238 O O   . HIS B 1 246 ? -0.61800  -21.61300 -3.26600  1.000 47.27409  ? 246 HIS B O   1 
ATOM   4239 C CB  . HIS B 1 246 ? 0.97900   -20.45800 -5.88600  1.000 47.80836  ? 246 HIS B CB  1 
ATOM   4240 C CG  . HIS B 1 246 ? 1.62300   -19.22800 -6.46500  1.000 51.37195  ? 246 HIS B CG  1 
ATOM   4241 N ND1 . HIS B 1 246 ? 2.13800   -19.19300 -7.74700  1.000 50.80083  ? 246 HIS B ND1 1 
ATOM   4242 C CD2 . HIS B 1 246 ? 1.80200   -17.97900 -5.95900  1.000 51.67725  ? 246 HIS B CD2 1 
ATOM   4243 C CE1 . HIS B 1 246 ? 2.61300   -17.98200 -8.00300  1.000 49.97704  ? 246 HIS B CE1 1 
ATOM   4244 N NE2 . HIS B 1 246 ? 2.41600   -17.22300 -6.93600  1.000 47.81626  ? 246 HIS B NE2 1 
ATOM   4245 N N   . VAL B 1 247 ? 0.80800   -23.10500 -4.19000  1.000 52.96425  ? 247 VAL B N   1 
ATOM   4246 C CA  . VAL B 1 247 ? 0.04600   -24.23800 -3.67000  1.000 52.17994  ? 247 VAL B CA  1 
ATOM   4247 C C   . VAL B 1 247 ? -0.02300  -24.16300 -2.14300  1.000 54.62760  ? 247 VAL B C   1 
ATOM   4248 O O   . VAL B 1 247 ? -1.07700  -24.38700 -1.53500  1.000 49.60068  ? 247 VAL B O   1 
ATOM   4249 C CB  . VAL B 1 247 ? 0.64100   -25.58000 -4.15400  1.000 53.81435  ? 247 VAL B CB  1 
ATOM   4250 C CG1 . VAL B 1 247 ? -0.08600  -26.76100 -3.46700  1.000 51.24825  ? 247 VAL B CG1 1 
ATOM   4251 C CG2 . VAL B 1 247 ? 0.58700   -25.71200 -5.65600  1.000 49.58489  ? 247 VAL B CG2 1 
ATOM   4252 N N   . ASP B 1 248 ? 1.09500   -23.81200 -1.49500  1.000 53.58011  ? 248 ASP B N   1 
ATOM   4253 C CA  . ASP B 1 248 ? 1.12100   -23.75000 -0.02900  1.000 53.78276  ? 248 ASP B CA  1 
ATOM   4254 C C   . ASP B 1 248 ? 0.23700   -22.62500 0.49200   1.000 50.45079  ? 248 ASP B C   1 
ATOM   4255 O O   . ASP B 1 248 ? -0.43600  -22.77900 1.51500   1.000 55.44086  ? 248 ASP B O   1 
ATOM   4256 C CB  . ASP B 1 248 ? 2.56100   -23.55600 0.45800   1.000 56.25675  ? 248 ASP B CB  1 
ATOM   4257 C CG  . ASP B 1 248 ? 3.45800   -24.76100 0.17500   1.000 58.76494  ? 248 ASP B CG  1 
ATOM   4258 O OD1 . ASP B 1 248 ? 2.92000   -25.87500 0.02100   1.000 62.29694  ? 248 ASP B OD1 1 
ATOM   4259 O OD2 . ASP B 1 248 ? 4.70300   -24.57900 0.07600   1.000 64.26823  ? 248 ASP B OD2 1 
ATOM   4260 N N   . ILE B 1 249 ? 0.19800   -21.49200 -0.21000  1.000 51.22719  ? 249 ILE B N   1 
ATOM   4261 C CA  . ILE B 1 249 ? -0.63000  -20.37100 0.24300   1.000 51.12981  ? 249 ILE B CA  1 
ATOM   4262 C C   . ILE B 1 249 ? -2.10600  -20.71400 0.10400   1.000 50.62975  ? 249 ILE B C   1 
ATOM   4263 O O   . ILE B 1 249 ? -2.94800  -20.26600 0.90900   1.000 53.84856  ? 249 ILE B O   1 
ATOM   4264 C CB  . ILE B 1 249 ? -0.25500  -19.09400 -0.54900  1.000 49.59279  ? 249 ILE B CB  1 
ATOM   4265 C CG1 . ILE B 1 249 ? 1.10000   -18.54000 -0.06900  1.000 51.71936  ? 249 ILE B CG1 1 
ATOM   4266 C CG2 . ILE B 1 249 ? -1.28600  -18.04700 -0.39700  1.000 49.40066  ? 249 ILE B CG2 1 
ATOM   4267 C CD1 . ILE B 1 249 ? 1.86900   -17.80600 -1.14200  1.000 55.59614  ? 249 ILE B CD1 1 
ATOM   4268 N N   . LEU B 1 250 ? -2.42800  -21.61400 -0.81700  1.000 50.75082  ? 250 LEU B N   1 
ATOM   4269 C CA  . LEU B 1 250 ? -3.83800  -22.04100 -1.02100  1.000 47.26883  ? 250 LEU B CA  1 
ATOM   4270 C C   . LEU B 1 250 ? -4.23000  -23.13900 -0.02000  1.000 52.27995  ? 250 LEU B C   1 
ATOM   4271 O O   . LEU B 1 250 ? -5.38200  -23.58700 -0.08000  1.000 51.35879  ? 250 LEU B O   1 
ATOM   4272 C CB  . LEU B 1 250 ? -3.94400  -22.54800 -2.45700  1.000 45.88708  ? 250 LEU B CB  1 
ATOM   4273 C CG  . LEU B 1 250 ? -4.80200  -21.75200 -3.43600  1.000 48.89270  ? 250 LEU B CG  1 
ATOM   4274 C CD1 . LEU B 1 250 ? -5.27800  -20.44300 -2.83700  1.000 43.21571  ? 250 LEU B CD1 1 
ATOM   4275 C CD2 . LEU B 1 250 ? -4.04800  -21.51400 -4.73100  1.000 42.15505  ? 250 LEU B CD2 1 
ATOM   4276 N N   . GLY B 1 251 ? -3.33100  -23.54200 0.88500   1.000 51.50091  ? 251 GLY B N   1 
ATOM   4277 C CA  . GLY B 1 251 ? -3.59200  -24.63200 1.81400   1.000 50.83504  ? 251 GLY B CA  1 
ATOM   4278 C C   . GLY B 1 251 ? -4.82100  -24.45000 2.67600   1.000 51.43248  ? 251 GLY B C   1 
ATOM   4279 O O   . GLY B 1 251 ? -5.68100  -25.34800 2.78000   1.000 58.11223  ? 251 GLY B O   1 
ATOM   4280 N N   . PRO B 1 252 ? -4.93300  -23.31200 3.37400   1.000 51.85622  ? 252 PRO B N   1 
ATOM   4281 C CA  . PRO B 1 252 ? -6.11700  -23.15600 4.24100   1.000 52.52472  ? 252 PRO B CA  1 
ATOM   4282 C C   . PRO B 1 252 ? -7.42600  -23.27900 3.46700   1.000 53.62748  ? 252 PRO B C   1 
ATOM   4283 O O   . PRO B 1 252 ? -8.39200  -23.89900 3.96500   1.000 53.19059  ? 252 PRO B O   1 
ATOM   4284 C CB  . PRO B 1 252 ? -5.91600  -21.76700 4.85400   1.000 51.33510  ? 252 PRO B CB  1 
ATOM   4285 C CG  . PRO B 1 252 ? -4.35900  -21.60100 4.86000   1.000 52.95372  ? 252 PRO B CG  1 
ATOM   4286 C CD  . PRO B 1 252 ? -3.89900  -22.29200 3.63100   1.000 52.93529  ? 252 PRO B CD  1 
ATOM   4287 N N   . LEU B 1 253 ? -7.44900  -22.78300 2.22700   1.000 52.78264  ? 253 LEU B N   1 
ATOM   4288 C CA  . LEU B 1 253 ? -8.67400  -22.85700 1.38200   1.000 48.00312  ? 253 LEU B CA  1 
ATOM   4289 C C   . LEU B 1 253 ? -8.94800  -24.30600 0.97500   1.000 50.06127  ? 253 LEU B C   1 
ATOM   4290 O O   . LEU B 1 253 ? -10.10500 -24.72100 1.07300   1.000 48.60056  ? 253 LEU B O   1 
ATOM   4291 C CB  . LEU B 1 253 ? -8.50000  -21.96200 0.15500   1.000 48.28210  ? 253 LEU B CB  1 
ATOM   4292 C CG  . LEU B 1 253 ? -9.35200  -20.69400 0.11600   1.000 53.62485  ? 253 LEU B CG  1 
ATOM   4293 C CD1 . LEU B 1 253 ? -9.88600  -20.34000 1.49200   1.000 51.02717  ? 253 LEU B CD1 1 
ATOM   4294 C CD2 . LEU B 1 253 ? -8.56700  -19.53100 -0.46800  1.000 41.74974  ? 253 LEU B CD2 1 
ATOM   4295 N N   . SER B 1 254 ? -7.93600  -25.02800 0.50000   1.000 48.12156  ? 254 SER B N   1 
ATOM   4296 C CA  . SER B 1 254 ? -8.13200  -26.45000 0.21100   1.000 52.13783  ? 254 SER B CA  1 
ATOM   4297 C C   . SER B 1 254 ? -8.60500  -27.17900 1.43800   1.000 53.01162  ? 254 SER B C   1 
ATOM   4298 O O   . SER B 1 254 ? -9.41400  -28.08700 1.33800   1.000 53.20112  ? 254 SER B O   1 
ATOM   4299 C CB  . SER B 1 254 ? -6.86300  -27.16800 -0.25500  1.000 47.04775  ? 254 SER B CB  1 
ATOM   4300 O OG  . SER B 1 254 ? -5.79400  -26.26500 -0.25700  1.000 59.96772  ? 254 SER B OG  1 
ATOM   4301 N N   . ALA B 1 255 ? -8.05300  -26.83200 2.60000   1.000 53.88278  ? 255 ALA B N   1 
ATOM   4302 C CA  . ALA B 1 255 ? -8.41000  -27.53500 3.82700   1.000 55.85143  ? 255 ALA B CA  1 
ATOM   4303 C C   . ALA B 1 255 ? -9.87000  -27.30000 4.19800   1.000 52.48787  ? 255 ALA B C   1 
ATOM   4304 O O   . ALA B 1 255 ? -10.59600 -28.24700 4.52100   1.000 53.51431  ? 255 ALA B O   1 
ATOM   4305 C CB  . ALA B 1 255 ? -7.48500  -27.07500 4.95100   1.000 51.93781  ? 255 ALA B CB  1 
ATOM   4306 N N   . GLN B 1 256 ? -10.34100 -26.06000 4.08800   1.000 53.96436  ? 256 GLN B N   1 
ATOM   4307 C CA  . GLN B 1 256 ? -11.71200 -25.75500 4.45900   1.000 50.99822  ? 256 GLN B CA  1 
ATOM   4308 C C   . GLN B 1 256 ? -12.71700 -26.40100 3.51200   1.000 52.19836  ? 256 GLN B C   1 
ATOM   4309 O O   . GLN B 1 256 ? -13.74800 -26.91700 3.95700   1.000 50.65871  ? 256 GLN B O   1 
ATOM   4310 C CB  . GLN B 1 256 ? -11.90000 -24.24600 4.48700   1.000 53.33008  ? 256 GLN B CB  1 
ATOM   4311 C CG  . GLN B 1 256 ? -13.30900 -23.86700 4.76000   1.000 53.14321  ? 256 GLN B CG  1 
ATOM   4312 C CD  . GLN B 1 256 ? -13.52900 -22.40400 4.58400   1.000 58.04907  ? 256 GLN B CD  1 
ATOM   4313 O OE1 . GLN B 1 256 ? -12.57200 -21.64600 4.32000   1.000 61.43368  ? 256 GLN B OE1 1 
ATOM   4314 N NE2 . GLN B 1 256 ? -14.79100 -21.97800 4.69100   1.000 54.69603  ? 256 GLN B NE2 1 
ATOM   4315 N N   . THR B 1 257 ? -12.42600 -26.42700 2.20900   1.000 50.97716  ? 257 THR B N   1 
ATOM   4316 C CA  . THR B 1 257 ? -13.35200 -26.98500 1.23800   1.000 44.56850  ? 257 THR B CA  1 
ATOM   4317 C C   . THR B 1 257 ? -13.13600 -28.46400 1.00500   1.000 49.88230  ? 257 THR B C   1 
ATOM   4318 O O   . THR B 1 257 ? -13.97700 -29.09700 0.36700   1.000 52.24047  ? 257 THR B O   1 
ATOM   4319 C CB  . THR B 1 257 ? -13.22800 -26.29200 -0.11700  1.000 48.86639  ? 257 THR B CB  1 
ATOM   4320 O OG1 . THR B 1 257 ? -11.88800 -26.47500 -0.62300  1.000 48.91376  ? 257 THR B OG1 1 
ATOM   4321 C CG2 . THR B 1 257 ? -13.57400 -24.80200 -0.01100  1.000 46.69770  ? 257 THR B CG2 1 
ATOM   4322 N N   . GLY B 1 258 ? -12.01400 -29.01400 1.45100   1.000 50.79030  ? 258 GLY B N   1 
ATOM   4323 C CA  . GLY B 1 258 ? -11.72500 -30.40000 1.15600   1.000 52.41418  ? 258 GLY B CA  1 
ATOM   4324 C C   . GLY B 1 258 ? -11.35700 -30.68800 -0.28000  1.000 53.03004  ? 258 GLY B C   1 
ATOM   4325 O O   . GLY B 1 258 ? -11.35300 -31.85400 -0.67400  1.000 52.20626  ? 258 GLY B O   1 
ATOM   4326 N N   . ILE B 1 259 ? -11.01600 -29.67300 -1.06300  1.000 50.12180  ? 259 ILE B N   1 
ATOM   4327 C CA  . ILE B 1 259 ? -10.64800 -29.83000 -2.46700  1.000 49.12431  ? 259 ILE B CA  1 
ATOM   4328 C C   . ILE B 1 259 ? -9.13500  -29.61000 -2.55500  1.000 51.39037  ? 259 ILE B C   1 
ATOM   4329 O O   . ILE B 1 259 ? -8.64500  -28.50200 -2.28600  1.000 50.90347  ? 259 ILE B O   1 
ATOM   4330 C CB  . ILE B 1 259 ? -11.37700 -28.81500 -3.36700  1.000 50.82451  ? 259 ILE B CB  1 
ATOM   4331 C CG1 . ILE B 1 259 ? -12.91300 -28.82800 -3.17700  1.000 53.37482  ? 259 ILE B CG1 1 
ATOM   4332 C CG2 . ILE B 1 259 ? -11.03400 -29.05300 -4.83200  1.000 50.26392  ? 259 ILE B CG2 1 
ATOM   4333 C CD1 . ILE B 1 259 ? -13.57600 -29.85400 -3.91200  1.000 53.89067  ? 259 ILE B CD1 1 
ATOM   4334 N N   . ALA B 1 260 ? -8.38000  -30.64900 -2.90200  1.000 50.51922  ? 260 ALA B N   1 
ATOM   4335 C CA  . ALA B 1 260 ? -6.93400  -30.47400 -3.06800  1.000 46.13185  ? 260 ALA B CA  1 
ATOM   4336 C C   . ALA B 1 260 ? -6.64900  -29.40900 -4.11600  1.000 47.48464  ? 260 ALA B C   1 
ATOM   4337 O O   . ALA B 1 260 ? -7.41700  -29.23200 -5.07200  1.000 46.57664  ? 260 ALA B O   1 
ATOM   4338 C CB  . ALA B 1 260 ? -6.31100  -31.80600 -3.48900  1.000 50.50869  ? 260 ALA B CB  1 
ATOM   4339 N N   . VAL B 1 261 ? -5.54000  -28.66700 -3.93300  1.000 47.46359  ? 261 VAL B N   1 
ATOM   4340 C CA  . VAL B 1 261 ? -5.19200  -27.61200 -4.88400  1.000 46.05026  ? 261 VAL B CA  1 
ATOM   4341 C C   . VAL B 1 261 ? -5.06300  -28.19100 -6.29600  1.000 46.20817  ? 261 VAL B C   1 
ATOM   4342 O O   . VAL B 1 261 ? -5.57700  -27.62300 -7.26700  1.000 44.98434  ? 261 VAL B O   1 
ATOM   4343 C CB  . VAL B 1 261 ? -3.88200  -26.89900 -4.46800  1.000 49.07957  ? 261 VAL B CB  1 
ATOM   4344 C CG1 . VAL B 1 261 ? -3.48100  -25.91600 -5.54500  1.000 43.70524  ? 261 VAL B CG1 1 
ATOM   4345 C CG2 . VAL B 1 261 ? -4.06300  -26.15000 -3.16500  1.000 49.41119  ? 261 VAL B CG2 1 
ATOM   4346 N N   . LEU B 1 262 ? -4.36000  -29.31700 -6.44400  1.000 46.83983  ? 262 LEU B N   1 
ATOM   4347 C CA  . LEU B 1 262 ? -4.22800  -29.85600 -7.79800  1.000 49.04535  ? 262 LEU B CA  1 
ATOM   4348 C C   . LEU B 1 262 ? -5.52900  -30.45300 -8.33600  1.000 49.86124  ? 262 LEU B C   1 
ATOM   4349 O O   . LEU B 1 262 ? -5.66100  -30.63700 -9.55100  1.000 47.83205  ? 262 LEU B O   1 
ATOM   4350 C CB  . LEU B 1 262 ? -3.08100  -30.87700 -7.86500  1.000 52.08256  ? 262 LEU B CB  1 
ATOM   4351 C CG  . LEU B 1 262 ? -1.66900  -30.30900 -7.68000  1.000 51.92991  ? 262 LEU B CG  1 
ATOM   4352 C CD1 . LEU B 1 262 ? -0.74100  -31.43700 -7.70900  1.000 54.72498  ? 262 LEU B CD1 1 
ATOM   4353 C CD2 . LEU B 1 262 ? -1.34500  -29.35700 -8.79900  1.000 51.48775  ? 262 LEU B CD2 1 
ATOM   4354 N N   . ASP B 1 263 ? -6.50800  -30.67600 -7.45500  1.000 48.94008  ? 263 ASP B N   1 
ATOM   4355 C CA  . ASP B 1 263 ? -7.84400  -31.11900 -7.93800  1.000 47.32936  ? 263 ASP B CA  1 
ATOM   4356 C C   . ASP B 1 263 ? -8.52300  -29.88200 -8.53400  1.000 47.28988  ? 263 ASP B C   1 
ATOM   4357 O O   . ASP B 1 263 ? -9.10400  -29.99600 -9.62900  1.000 46.66086  ? 263 ASP B O   1 
ATOM   4358 C CB  . ASP B 1 263 ? -8.64400  -31.78200 -6.81200  1.000 54.08543  ? 263 ASP B CB  1 
ATOM   4359 C CG  . ASP B 1 263 ? -10.10200 -32.05800 -7.14300  1.000 65.79210  ? 263 ASP B CG  1 
ATOM   4360 O OD1 . ASP B 1 263 ? -10.39900 -32.34700 -8.31700  1.000 57.49110  ? 263 ASP B OD1 1 
ATOM   4361 O OD2 . ASP B 1 263 ? -10.92900 -32.00000 -6.21400  1.000 75.43536  ? 263 ASP B OD2 1 
ATOM   4362 N N   . MET B 1 264 ? -8.44000  -28.74100 -7.84300  1.000 43.81052  ? 264 MET B N   1 
ATOM   4363 C CA  . MET B 1 264 ? -8.98300  -27.49000 -8.37800  1.000 43.56838  ? 264 MET B CA  1 
ATOM   4364 C C   . MET B 1 264 ? -8.22900  -27.03100 -9.64700  1.000 45.78180  ? 264 MET B C   1 
ATOM   4365 O O   . MET B 1 264 ? -8.80500  -26.33700 -10.51500 1.000 42.33666  ? 264 MET B O   1 
ATOM   4366 C CB  . MET B 1 264 ? -8.92200  -26.39800 -7.31500  1.000 37.25447  ? 264 MET B CB  1 
ATOM   4367 C CG  . MET B 1 264 ? -9.63800  -25.06500 -7.69900  1.000 38.88887  ? 264 MET B CG  1 
ATOM   4368 S SD  . MET B 1 264 ? -11.44400 -25.43000 -7.66600  1.000 42.61564  ? 264 MET B SD  1 
ATOM   4369 C CE  . MET B 1 264 ? -11.67200 -25.07200 -5.92400  1.000 43.81052  ? 264 MET B CE  1 
ATOM   4370 N N   . CYS B 1 265 ? -6.92700  -27.32800 -9.74100  1.000 45.84760  ? 265 CYS B N   1 
ATOM   4371 C CA  . CYS B 1 265 ? -6.22600  -26.98700 -10.97800 1.000 45.48703  ? 265 CYS B CA  1 
ATOM   4372 C C   . CYS B 1 265 ? -6.82100  -27.75200 -12.15300 1.000 44.40269  ? 265 CYS B C   1 
ATOM   4373 O O   . CYS B 1 265 ? -6.90500  -27.22100 -13.26500 1.000 46.54769  ? 265 CYS B O   1 
ATOM   4374 C CB  . CYS B 1 265 ? -4.71400  -27.28100 -10.84100 1.000 45.55809  ? 265 CYS B CB  1 
ATOM   4375 S SG  . CYS B 1 265 ? -3.87100  -26.16700 -9.75400  1.000 46.76350  ? 265 CYS B SG  1 
ATOM   4376 N N   . ALA B 1 266 ? -7.27500  -28.98900 -11.92200 1.000 45.35017  ? 266 ALA B N   1 
ATOM   4377 C CA  . ALA B 1 266 ? -7.95300  -29.74100 -12.97600 1.000 48.24526  ? 266 ALA B CA  1 
ATOM   4378 C C   . ALA B 1 266 ? -9.26200  -29.06500 -13.39400 1.000 47.20303  ? 266 ALA B C   1 
ATOM   4379 O O   . ALA B 1 266 ? -9.63600  -29.08600 -14.57200 1.000 48.17157  ? 266 ALA B O   1 
ATOM   4380 C CB  . ALA B 1 266 ? -8.22100  -31.18600 -12.52000 1.000 50.48500  ? 266 ALA B CB  1 
ATOM   4381 N N   . SER B 1 267 ? -9.98100  -28.45400 -12.44900 1.000 46.42662  ? 267 SER B N   1 
ATOM   4382 C CA  . SER B 1 267 ? -11.14700 -27.68700 -12.83500 1.000 45.35281  ? 267 SER B CA  1 
ATOM   4383 C C   . SER B 1 267 ? -10.77200 -26.45900 -13.64200 1.000 45.06330  ? 267 SER B C   1 
ATOM   4384 O O   . SER B 1 267 ? -11.44500 -26.12500 -14.63800 1.000 43.10254  ? 267 SER B O   1 
ATOM   4385 C CB  . SER B 1 267 ? -11.95100 -27.27800 -11.59700 1.000 45.59231  ? 267 SER B CB  1 
ATOM   4386 O OG  . SER B 1 267 ? -12.52500 -28.43200 -11.09900 1.000 49.89282  ? 267 SER B OG  1 
ATOM   4387 N N   . LEU B 1 268 ? -9.75000  -25.72700 -13.18500 1.000 43.80525  ? 268 LEU B N   1 
ATOM   4388 C CA  . LEU B 1 268 ? -9.31300  -24.55500 -13.94900 1.000 45.19752  ? 268 LEU B CA  1 
ATOM   4389 C C   . LEU B 1 268 ? -8.89200  -24.94500 -15.36000 1.000 45.18963  ? 268 LEU B C   1 
ATOM   4390 O O   . LEU B 1 268 ? -9.30600  -24.30500 -16.33600 1.000 43.53680  ? 268 LEU B O   1 
ATOM   4391 C CB  . LEU B 1 268 ? -8.19000  -23.82200 -13.21800 1.000 42.94725  ? 268 LEU B CB  1 
ATOM   4392 C CG  . LEU B 1 268 ? -7.61600  -22.52000 -13.82600 1.000 42.46825  ? 268 LEU B CG  1 
ATOM   4393 C CD1 . LEU B 1 268 ? -8.75100  -21.58000 -14.23600 1.000 41.81554  ? 268 LEU B CD1 1 
ATOM   4394 C CD2 . LEU B 1 268 ? -6.72200  -21.85100 -12.77900 1.000 37.90981  ? 268 LEU B CD2 1 
ATOM   4395 N N   . LYS B 1 269 ? -8.12600  -26.02800 -15.49800 1.000 45.17647  ? 269 LYS B N   1 
ATOM   4396 C CA  . LYS B 1 269 ? -7.75400  -26.50700 -16.82600 1.000 46.81088  ? 269 LYS B CA  1 
ATOM   4397 C C   . LYS B 1 269 ? -8.98100  -26.69800 -17.72500 1.000 51.57197  ? 269 LYS B C   1 
ATOM   4398 O O   . LYS B 1 269 ? -9.00600  -26.22200 -18.86600 1.000 53.04320  ? 269 LYS B O   1 
ATOM   4399 C CB  . LYS B 1 269 ? -6.97300  -27.82100 -16.67400 1.000 48.26631  ? 269 LYS B CB  1 
ATOM   4400 C CG  . LYS B 1 269 ? -6.76500  -28.56500 -17.97200 1.000 55.65667  ? 269 LYS B CG  1 
ATOM   4401 C CD  . LYS B 1 269 ? -5.97700  -29.89800 -17.79600 1.000 62.99176  ? 269 LYS B CD  1 
ATOM   4402 C CE  . LYS B 1 269 ? -4.80500  -29.82100 -16.81300 1.000 62.65225  ? 269 LYS B CE  1 
ATOM   4403 N NZ  . LYS B 1 269 ? -4.16300  -31.17400 -16.70100 1.000 64.33140  ? 269 LYS B NZ  1 
ATOM   4404 N N   . GLU B 1 270 ? -10.02700 -27.38500 -17.21700 1.000 49.66385  ? 270 GLU B N   1 
ATOM   4405 C CA  . GLU B 1 270 ? -11.23000 -27.63100 -18.01600 1.000 53.48273  ? 270 GLU B CA  1 
ATOM   4406 C C   . GLU B 1 270 ? -11.93400 -26.31600 -18.36400 1.000 51.98781  ? 270 GLU B C   1 
ATOM   4407 O O   . GLU B 1 270 ? -12.42000 -26.14300 -19.49200 1.000 52.78001  ? 270 GLU B O   1 
ATOM   4408 C CB  . GLU B 1 270 ? -12.17000 -28.60600 -17.26400 1.000 55.34348  ? 270 GLU B CB  1 
ATOM   4409 C CG  . GLU B 1 270 ? -13.39300 -29.06300 -18.04300 1.000 66.34480  ? 270 GLU B CG  1 
ATOM   4410 C CD  . GLU B 1 270 ? -14.32000 -30.07900 -17.27900 1.000 84.19431  ? 270 GLU B CD  1 
ATOM   4411 O OE1 . GLU B 1 270 ? -14.47200 -30.03000 -16.02300 1.000 72.39815  ? 270 GLU B OE1 1 
ATOM   4412 O OE2 . GLU B 1 270 ? -14.92800 -30.92900 -17.96900 1.000 99.02766  ? 270 GLU B OE2 1 
ATOM   4413 N N   . LEU B 1 271 ? -11.98600 -25.37500 -17.40900 1.000 45.21595  ? 271 LEU B N   1 
ATOM   4414 C CA  . LEU B 1 271 ? -12.56000 -24.06200 -17.68000 1.000 46.88194  ? 271 LEU B CA  1 
ATOM   4415 C C   . LEU B 1 271 ? -11.76900 -23.30500 -18.73000 1.000 50.91400  ? 271 LEU B C   1 
ATOM   4416 O O   . LEU B 1 271 ? -12.35500 -22.61000 -19.56400 1.000 47.74520  ? 271 LEU B O   1 
ATOM   4417 C CB  . LEU B 1 271 ? -12.62600 -23.23100 -16.41600 1.000 45.91603  ? 271 LEU B CB  1 
ATOM   4418 C CG  . LEU B 1 271 ? -13.67100 -23.74700 -15.41100 1.000 43.10517  ? 271 LEU B CG  1 
ATOM   4419 C CD1 . LEU B 1 271 ? -13.45200 -22.92800 -14.16700 1.000 42.93146  ? 271 LEU B CD1 1 
ATOM   4420 C CD2 . LEU B 1 271 ? -15.07800 -23.60100 -15.92500 1.000 50.38762  ? 271 LEU B CD2 1 
ATOM   4421 N N   . LEU B 1 272 ? -10.43000 -23.40700 -18.69900 1.000 46.00288  ? 272 LEU B N   1 
ATOM   4422 C CA  . LEU B 1 272 ? -9.64000  -22.76400 -19.73300 1.000 49.54805  ? 272 LEU B CA  1 
ATOM   4423 C C   . LEU B 1 272 ? -9.87300  -23.43500 -21.08600 1.000 53.01688  ? 272 LEU B C   1 
ATOM   4424 O O   . LEU B 1 272 ? -9.95200  -22.75000 -22.10800 1.000 55.58298  ? 272 LEU B O   1 
ATOM   4425 C CB  . LEU B 1 272 ? -8.13800  -22.80400 -19.36000 1.000 44.35795  ? 272 LEU B CB  1 
ATOM   4426 C CG  . LEU B 1 272 ? -7.72500  -21.96400 -18.15800 1.000 45.47914  ? 272 LEU B CG  1 
ATOM   4427 C CD1 . LEU B 1 272 ? -6.23500  -22.11100 -17.90500 1.000 45.83181  ? 272 LEU B CD1 1 
ATOM   4428 C CD2 . LEU B 1 272 ? -8.06300  -20.49000 -18.39500 1.000 45.88971  ? 272 LEU B CD2 1 
ATOM   4429 N N   . GLN B 1 273 ? -9.98100  -24.77400 -21.12100 1.000 49.82966  ? 273 GLN B N   1 
ATOM   4430 C CA  . GLN B 1 273 ? -10.05200 -25.46600 -22.40500 1.000 54.44337  ? 273 GLN B CA  1 
ATOM   4431 C C   . GLN B 1 273 ? -11.44100 -25.38300 -23.03600 1.000 59.03339  ? 273 GLN B C   1 
ATOM   4432 O O   . GLN B 1 273 ? -11.55000 -25.37500 -24.26800 1.000 58.63335  ? 273 GLN B O   1 
ATOM   4433 C CB  . GLN B 1 273 ? -9.63500  -26.92900 -22.23800 1.000 54.33020  ? 273 GLN B CB  1 
ATOM   4434 C CG  . GLN B 1 273 ? -8.13000  -27.10200 -22.00000 1.000 56.16463  ? 273 GLN B CG  1 
ATOM   4435 C CD  . GLN B 1 273 ? -7.70700  -28.53100 -21.58200 1.000 61.60739  ? 273 GLN B CD  1 
ATOM   4436 O OE1 . GLN B 1 273 ? -8.53600  -29.36800 -21.19100 1.000 66.56061  ? 273 GLN B OE1 1 
ATOM   4437 N NE2 . GLN B 1 273 ? -6.41800  -28.80200 -21.67300 1.000 61.77583  ? 273 GLN B NE2 1 
ATOM   4438 N N   . ASN B 1 274 ? -12.50100 -25.30900 -22.22200 1.000 55.70142  ? 274 ASN B N   1 
ATOM   4439 C CA  . ASN B 1 274 ? -13.88200 -25.39200 -22.68700 1.000 60.94415  ? 274 ASN B CA  1 
ATOM   4440 C C   . ASN B 1 274 ? -14.74300 -24.16100 -22.43600 1.000 60.88888  ? 274 ASN B C   1 
ATOM   4441 O O   . ASN B 1 274 ? -15.83300 -24.07300 -23.01700 1.000 62.86280  ? 274 ASN B O   1 
ATOM   4442 C CB  . ASN B 1 274 ? -14.58300 -26.59800 -22.04700 1.000 61.94427  ? 274 ASN B CB  1 
ATOM   4443 C CG  . ASN B 1 274 ? -13.79500 -27.88000 -22.24900 1.000 68.41610  ? 274 ASN B CG  1 
ATOM   4444 O OD1 . ASN B 1 274 ? -13.66000 -28.67300 -21.32800 1.000 80.64125  ? 274 ASN B OD1 1 
ATOM   4445 N ND2 . ASN B 1 274 ? -13.20800 -28.04800 -23.43000 1.000 67.40808  ? 274 ASN B ND2 1 
ATOM   4446 N N   . GLY B 1 275 ? -14.33300 -23.24700 -21.56300 1.000 59.44923  ? 275 GLY B N   1 
ATOM   4447 C CA  . GLY B 1 275 ? -15.15000 -22.10900 -21.24400 1.000 55.21188  ? 275 GLY B CA  1 
ATOM   4448 C C   . GLY B 1 275 ? -16.22400 -22.51500 -20.24800 1.000 56.43571  ? 275 GLY B C   1 
ATOM   4449 O O   . GLY B 1 275 ? -16.19700 -23.60800 -19.69500 1.000 56.88577  ? 275 GLY B O   1 
ATOM   4450 N N   . MET B 1 276 ? -17.20600 -21.63700 -20.05500 1.000 58.08328  ? 276 MET B N   1 
ATOM   4451 C CA  . MET B 1 276 ? -18.20700 -21.88800 -19.03400 1.000 59.07550  ? 276 MET B CA  1 
ATOM   4452 C C   . MET B 1 276 ? -19.51500 -22.46900 -19.57200 1.000 63.31285  ? 276 MET B C   1 
ATOM   4453 O O   . MET B 1 276 ? -20.37300 -22.86400 -18.76600 1.000 58.88864  ? 276 MET B O   1 
ATOM   4454 C CB  . MET B 1 276 ? -18.47400 -20.60900 -18.25600 1.000 58.82021  ? 276 MET B CB  1 
ATOM   4455 C CG  . MET B 1 276 ? -17.26700 -20.14300 -17.46100 1.000 55.59088  ? 276 MET B CG  1 
ATOM   4456 S SD  . MET B 1 276 ? -17.86000 -18.96500 -16.20800 1.000 55.44349  ? 276 MET B SD  1 
ATOM   4457 C CE  . MET B 1 276 ? -16.23000 -18.18900 -15.88500 1.000 48.74532  ? 276 MET B CE  1 
ATOM   4458 N N   . ASN B 1 277 ? -19.69000 -22.54300 -20.89700 1.000 64.51037  ? 277 ASN B N   1 
ATOM   4459 C CA  . ASN B 1 277 ? -20.92200 -23.07500 -21.49300 1.000 69.04249  ? 277 ASN B CA  1 
ATOM   4460 C C   . ASN B 1 277 ? -22.14800 -22.33300 -20.96500 1.000 68.48453  ? 277 ASN B C   1 
ATOM   4461 O O   . ASN B 1 277 ? -23.14600 -22.95000 -20.55600 1.000 67.53704  ? 277 ASN B O   1 
ATOM   4462 C CB  . ASN B 1 277 ? -21.06800 -24.58000 -21.24000 1.000 77.77248  ? 277 ASN B CB  1 
ATOM   4463 C CG  . ASN B 1 277 ? -19.97000 -25.39500 -21.89000 1.000 91.15830  ? 277 ASN B CG  1 
ATOM   4464 O OD1 . ASN B 1 277 ? -20.06100 -25.72000 -23.07300 1.000 94.55344  ? 277 ASN B OD1 1 
ATOM   4465 N ND2 . ASN B 1 277 ? -18.91600 -25.72000 -21.12400 1.000 89.71076  ? 277 ASN B ND2 1 
ATOM   4466 N N   . GLY B 1 278 ? -22.05400 -20.99800 -20.93100 1.000 64.58406  ? 278 GLY B N   1 
ATOM   4467 C CA  . GLY B 1 278 ? -23.17900 -20.18500 -20.52500 1.000 62.72068  ? 278 GLY B CA  1 
ATOM   4468 C C   . GLY B 1 278 ? -23.46100 -20.13300 -19.03900 1.000 63.07862  ? 278 GLY B C   1 
ATOM   4469 O O   . GLY B 1 278 ? -24.47400 -19.54900 -18.64200 1.000 64.46562  ? 278 GLY B O   1 
ATOM   4470 N N   . ARG B 1 279 ? -22.64600 -20.76700 -18.20400 1.000 60.49673  ? 279 ARG B N   1 
ATOM   4471 C CA  . ARG B 1 279 ? -22.83700 -20.67600 -16.76500 1.000 56.35149  ? 279 ARG B CA  1 
ATOM   4472 C C   . ARG B 1 279 ? -21.95900 -19.57000 -16.21100 1.000 52.57472  ? 279 ARG B C   1 
ATOM   4473 O O   . ARG B 1 279 ? -21.11300 -19.00600 -16.90700 1.000 55.26452  ? 279 ARG B O   1 
ATOM   4474 C CB  . ARG B 1 279 ? -22.54200 -22.02100 -16.09300 1.000 55.95145  ? 279 ARG B CB  1 
ATOM   4475 C CG  . ARG B 1 279 ? -23.76100 -22.94600 -16.12300 1.000 60.32302  ? 279 ARG B CG  1 
ATOM   4476 C CD  . ARG B 1 279 ? -23.36800 -24.39200 -16.01600 1.000 59.47292  ? 279 ARG B CD  1 
ATOM   4477 N NE  . ARG B 1 279 ? -22.26800 -24.69900 -16.91200 1.000 59.63873  ? 279 ARG B NE  1 
ATOM   4478 C CZ  . ARG B 1 279 ? -21.69200 -25.89100 -17.01600 1.000 63.21284  ? 279 ARG B CZ  1 
ATOM   4479 N NH1 . ARG B 1 279 ? -22.12900 -26.93700 -16.31500 1.000 58.42806  ? 279 ARG B NH1 1 
ATOM   4480 N NH2 . ARG B 1 279 ? -20.63200 -26.03200 -17.81800 1.000 61.92848  ? 279 ARG B NH2 1 
ATOM   4481 N N   . THR B 1 280 ? -22.17200 -19.24600 -14.94800 1.000 49.30328  ? 280 THR B N   1 
ATOM   4482 C CA  . THR B 1 280 ? -21.42600 -18.18300 -14.30200 1.000 48.04260  ? 280 THR B CA  1 
ATOM   4483 C C   . THR B 1 280 ? -20.89900 -18.69900 -12.97300 1.000 46.97142  ? 280 THR B C   1 
ATOM   4484 O O   . THR B 1 280 ? -21.37800 -19.71000 -12.42800 1.000 42.86303  ? 280 THR B O   1 
ATOM   4485 C CB  . THR B 1 280 ? -22.26100 -16.92400 -14.09100 1.000 47.61360  ? 280 THR B CB  1 
ATOM   4486 O OG1 . THR B 1 280 ? -23.38900 -17.29600 -13.31800 1.000 47.99523  ? 280 THR B OG1 1 
ATOM   4487 C CG2 . THR B 1 280 ? -22.75500 -16.34400 -15.43400 1.000 49.14273  ? 280 THR B CG2 1 
ATOM   4488 N N   . ILE B 1 281 ? -19.84700 -18.03400 -12.51100 1.000 42.33929  ? 281 ILE B N   1 
ATOM   4489 C CA  . ILE B 1 281 ? -19.21600 -18.31400 -11.23000 1.000 39.26523  ? 281 ILE B CA  1 
ATOM   4490 C C   . ILE B 1 281 ? -19.23400 -17.02300 -10.43700 1.000 43.48679  ? 281 ILE B C   1 
ATOM   4491 O O   . ILE B 1 281 ? -18.66000 -16.00900 -10.85700 1.000 36.27277  ? 281 ILE B O   1 
ATOM   4492 C CB  . ILE B 1 281 ? -17.78500 -18.85600 -11.40900 1.000 38.60200  ? 281 ILE B CB  1 
ATOM   4493 C CG1 . ILE B 1 281 ? -17.80400 -20.09700 -12.25800 1.000 41.83133  ? 281 ILE B CG1 1 
ATOM   4494 C CG2 . ILE B 1 281 ? -17.17800 -19.10600 -10.07100 1.000 38.45461  ? 281 ILE B CG2 1 
ATOM   4495 C CD1 . ILE B 1 281 ? -16.38600 -20.69000 -12.58200 1.000 42.13400  ? 281 ILE B CD1 1 
ATOM   4496 N N   . LEU B 1 282 ? -19.91300 -17.04500 -9.30000  1.000 39.11522  ? 282 LEU B N   1 
ATOM   4497 C CA  . LEU B 1 282 ? -20.05100 -15.87600 -8.43500  1.000 40.93122  ? 282 LEU B CA  1 
ATOM   4498 C C   . LEU B 1 282 ? -20.50700 -14.66100 -9.22400  1.000 41.77869  ? 282 LEU B C   1 
ATOM   4499 O O   . LEU B 1 282 ? -19.99700 -13.55300 -9.04800  1.000 42.99989  ? 282 LEU B O   1 
ATOM   4500 C CB  . LEU B 1 282 ? -18.75400 -15.58300 -7.70100  1.000 40.36800  ? 282 LEU B CB  1 
ATOM   4501 C CG  . LEU B 1 282 ? -18.42100 -16.61700 -6.66100  1.000 39.06521  ? 282 LEU B CG  1 
ATOM   4502 C CD1 . LEU B 1 282 ? -17.03900 -16.33800 -6.08700  1.000 38.55199  ? 282 LEU B CD1 1 
ATOM   4503 C CD2 . LEU B 1 282 ? -19.55700 -16.57500 -5.53100  1.000 39.74424  ? 282 LEU B CD2 1 
ATOM   4504 N N   . GLY B 1 283 ? -21.39400 -14.89500 -10.19000 1.000 40.94701  ? 283 GLY B N   1 
ATOM   4505 C CA  . GLY B 1 283 ? -21.94500 -13.79000 -10.95100 1.000 42.87883  ? 283 GLY B CA  1 
ATOM   4506 C C   . GLY B 1 283 ? -21.08700 -13.32800 -12.10800 1.000 47.53728  ? 283 GLY B C   1 
ATOM   4507 O O   . GLY B 1 283 ? -21.35500 -12.27000 -12.68900 1.000 47.86363  ? 283 GLY B O   1 
ATOM   4508 N N   . SER B 1 284 ? -20.05300 -14.05700 -12.44000 1.000 43.22097  ? 284 SER B N   1 
ATOM   4509 C CA  . SER B 1 284 ? -19.15700 -13.63100 -13.51200 1.000 39.81267  ? 284 SER B CA  1 
ATOM   4510 C C   . SER B 1 284 ? -19.13900 -14.67800 -14.60600 1.000 43.21044  ? 284 SER B C   1 
ATOM   4511 O O   . SER B 1 284 ? -19.11800 -15.90000 -14.33300 1.000 41.23389  ? 284 SER B O   1 
ATOM   4512 C CB  . SER B 1 284 ? -17.75900 -13.36000 -12.92500 1.000 41.95503  ? 284 SER B CB  1 
ATOM   4513 O OG  . SER B 1 284 ? -16.81100 -13.07800 -13.95200 1.000 46.38188  ? 284 SER B OG  1 
ATOM   4514 N N   . ALA B 1 285 ? -19.10300 -14.21200 -15.86600 1.000 43.68155  ? 285 ALA B N   1 
ATOM   4515 C CA  . ALA B 1 285 ? -18.89800 -15.10400 -16.98800 1.000 43.84210  ? 285 ALA B CA  1 
ATOM   4516 C C   . ALA B 1 285 ? -17.41200 -15.16800 -17.38900 1.000 44.12371  ? 285 ALA B C   1 
ATOM   4517 O O   . ALA B 1 285 ? -17.07000 -15.83200 -18.36600 1.000 46.18448  ? 285 ALA B O   1 
ATOM   4518 C CB  . ALA B 1 285 ? -19.78100 -14.68700 -18.17500 1.000 44.47112  ? 285 ALA B CB  1 
ATOM   4519 N N   . LEU B 1 286 ? -16.53600 -14.51100 -16.64100 1.000 42.52878  ? 286 LEU B N   1 
ATOM   4520 C CA  . LEU B 1 286 ? -15.10000 -14.53300 -16.87600 1.000 41.75764  ? 286 LEU B CA  1 
ATOM   4521 C C   . LEU B 1 286 ? -14.42200 -15.10000 -15.63700 1.000 44.78432  ? 286 LEU B C   1 
ATOM   4522 O O   . LEU B 1 286 ? -14.93700 -14.97000 -14.51700 1.000 39.79161  ? 286 LEU B O   1 
ATOM   4523 C CB  . LEU B 1 286 ? -14.54800 -13.12200 -17.13400 1.000 41.18389  ? 286 LEU B CB  1 
ATOM   4524 C CG  . LEU B 1 286 ? -15.12800 -12.44100 -18.37300 1.000 45.95551  ? 286 LEU B CG  1 
ATOM   4525 C CD1 . LEU B 1 286 ? -14.64600 -10.99800 -18.63700 1.000 45.57389  ? 286 LEU B CD1 1 
ATOM   4526 C CD2 . LEU B 1 286 ? -14.90900 -13.33200 -19.56100 1.000 45.90550  ? 286 LEU B CD2 1 
ATOM   4527 N N   . LEU B 1 287 ? -13.21700 -15.65300 -15.81100 1.000 41.81291  ? 287 LEU B N   1 
ATOM   4528 C CA  . LEU B 1 287 ? -12.45800 -16.10000 -14.64300 1.000 37.61504  ? 287 LEU B CA  1 
ATOM   4529 C C   . LEU B 1 287 ? -11.83000 -14.87600 -13.96600 1.000 42.36034  ? 287 LEU B C   1 
ATOM   4530 O O   . LEU B 1 287 ? -11.04000 -14.12400 -14.56400 1.000 41.32074  ? 287 LEU B O   1 
ATOM   4531 C CB  . LEU B 1 287 ? -11.39800 -17.13900 -15.04600 1.000 41.76553  ? 287 LEU B CB  1 
ATOM   4532 C CG  . LEU B 1 287 ? -11.94600 -18.43700 -15.66900 1.000 41.66815  ? 287 LEU B CG  1 
ATOM   4533 C CD1 . LEU B 1 287 ? -10.92300 -19.40700 -16.34700 1.000 44.06318  ? 287 LEU B CD1 1 
ATOM   4534 C CD2 . LEU B 1 287 ? -12.86400 -19.17600 -14.65300 1.000 45.68442  ? 287 LEU B CD2 1 
ATOM   4535 N N   . GLU B 1 288 ? -12.10800 -14.69300 -12.71400 1.000 41.11019  ? 288 GLU B N   1 
ATOM   4536 C CA  . GLU B 1 288 ? -11.68700 -13.47500 -12.01000 1.000 39.05205  ? 288 GLU B CA  1 
ATOM   4537 C C   . GLU B 1 288 ? -10.32800 -13.65600 -11.33800 1.000 39.81004  ? 288 GLU B C   1 
ATOM   4538 O O   . GLU B 1 288 ? -10.10200 -14.64100 -10.63500 1.000 34.24884  ? 288 GLU B O   1 
ATOM   4539 C CB  . GLU B 1 288 ? -12.78800 -13.14400 -10.98400 1.000 40.75752  ? 288 GLU B CB  1 
ATOM   4540 C CG  . GLU B 1 288 ? -12.39800 -12.07200 -10.02700 1.000 38.59673  ? 288 GLU B CG  1 
ATOM   4541 C CD  . GLU B 1 288 ? -12.39300 -10.67300 -10.65900 1.000 49.76123  ? 288 GLU B CD  1 
ATOM   4542 O OE1 . GLU B 1 288 ? -13.43700 -10.26000 -11.25700 1.000 55.65404  ? 288 GLU B OE1 1 
ATOM   4543 O OE2 . GLU B 1 288 ? -11.31200 -10.01900 -10.57300 1.000 45.15541  ? 288 GLU B OE2 1 
ATOM   4544 N N   . ASP B 1 289 ? -9.36900  -12.73900 -11.58700 1.000 38.36513  ? 289 ASP B N   1 
ATOM   4545 C CA  . ASP B 1 289 ? -8.08100  -12.92100 -10.91900 1.000 37.31237  ? 289 ASP B CA  1 
ATOM   4546 C C   . ASP B 1 289 ? -7.69800  -11.77400 -9.96700  1.000 37.86507  ? 289 ASP B C   1 
ATOM   4547 O O   . ASP B 1 289 ? -6.52700  -11.65200 -9.61300  1.000 40.06796  ? 289 ASP B O   1 
ATOM   4548 C CB  . ASP B 1 289 ? -6.98800  -13.14900 -11.98500 1.000 35.18053  ? 289 ASP B CB  1 
ATOM   4549 C CG  . ASP B 1 289 ? -6.53900  -11.86900 -12.67000 1.000 38.87571  ? 289 ASP B CG  1 
ATOM   4550 O OD1 . ASP B 1 289 ? -7.26600  -10.86800 -12.64200 1.000 41.14177  ? 289 ASP B OD1 1 
ATOM   4551 O OD2 . ASP B 1 289 ? -5.47500  -11.88800 -13.36100 1.000 38.19405  ? 289 ASP B OD2 1 
ATOM   4552 N N   . GLU B 1 290 ? -8.65600  -10.99400 -9.46500  1.000 34.22516  ? 290 GLU B N   1 
ATOM   4553 C CA  . GLU B 1 290 ? -8.28500  -9.82500  -8.61300  1.000 37.49134  ? 290 GLU B CA  1 
ATOM   4554 C C   . GLU B 1 290 ? -8.61300  -10.06300 -7.13000  1.000 40.72857  ? 290 GLU B C   1 
ATOM   4555 O O   . GLU B 1 290 ? -8.75900  -9.07200  -6.41500  1.000 39.66002  ? 290 GLU B O   1 
ATOM   4556 C CB  . GLU B 1 290 ? -8.84700  -8.52200  -9.18300  1.000 37.60714  ? 290 GLU B CB  1 
ATOM   4557 C CG  . GLU B 1 290 ? -8.25500  -8.16400  -10.53500 1.000 38.80465  ? 290 GLU B CG  1 
ATOM   4558 C CD  . GLU B 1 290 ? -7.81400  -6.72200  -10.72000 1.000 44.95013  ? 290 GLU B CD  1 
ATOM   4559 O OE1 . GLU B 1 290 ? -8.22600  -5.87200  -9.91600  1.000 41.74448  ? 290 GLU B OE1 1 
ATOM   4560 O OE2 . GLU B 1 290 ? -7.05900  -6.45500  -11.67300 1.000 40.63119  ? 290 GLU B OE2 1 
ATOM   4561 N N   . PHE B 1 291 ? -8.78600  -11.31000 -6.70000  1.000 35.54900  ? 291 PHE B N   1 
ATOM   4562 C CA  . PHE B 1 291 ? -8.90000  -11.65600 -5.28900  1.000 37.75979  ? 291 PHE B CA  1 
ATOM   4563 C C   . PHE B 1 291 ? -7.72900  -12.54900 -4.89000  1.000 36.84126  ? 291 PHE B C   1 
ATOM   4564 O O   . PHE B 1 291 ? -7.51600  -13.60800 -5.48800  1.000 36.79915  ? 291 PHE B O   1 
ATOM   4565 C CB  . PHE B 1 291 ? -10.21500 -12.44400 -4.99600  1.000 37.81769  ? 291 PHE B CB  1 
ATOM   4566 C CG  . PHE B 1 291 ? -11.49100 -11.68100 -5.23200  1.000 42.07610  ? 291 PHE B CG  1 
ATOM   4567 C CD1 . PHE B 1 291 ? -12.02800 -10.87100 -4.23300  1.000 43.09727  ? 291 PHE B CD1 1 
ATOM   4568 C CD2 . PHE B 1 291 ? -12.19200 -11.83100 -6.42700  1.000 40.62592  ? 291 PHE B CD2 1 
ATOM   4569 C CE1 . PHE B 1 291 ? -13.25800 -10.19700 -4.39600  1.000 43.83157  ? 291 PHE B CE1 1 
ATOM   4570 C CE2 . PHE B 1 291 ? -13.39900 -11.14600 -6.61100  1.000 45.57125  ? 291 PHE B CE2 1 
ATOM   4571 C CZ  . PHE B 1 291 ? -13.93300 -10.32700 -5.58000  1.000 45.96867  ? 291 PHE B CZ  1 
ATOM   4572 N N   . THR B 1 292 ? -6.97700  -12.14900 -3.89200  1.000 40.06007  ? 292 THR B N   1 
ATOM   4573 C CA  . THR B 1 292 ? -5.94400  -13.02700 -3.38400  1.000 38.07825  ? 292 THR B CA  1 
ATOM   4574 C C   . THR B 1 292 ? -6.54600  -14.12000 -2.50100  1.000 42.05504  ? 292 THR B C   1 
ATOM   4575 O O   . THR B 1 292 ? -7.68400  -14.00800 -2.03000  1.000 38.93362  ? 292 THR B O   1 
ATOM   4576 C CB  . THR B 1 292 ? -4.94200  -12.24700 -2.55500  1.000 45.40808  ? 292 THR B CB  1 
ATOM   4577 O OG1 . THR B 1 292 ? -5.63000  -11.78600 -1.41900  1.000 39.27050  ? 292 THR B OG1 1 
ATOM   4578 C CG2 . THR B 1 292 ? -4.25800  -11.02100 -3.35200  1.000 35.47531  ? 292 THR B CG2 1 
ATOM   4579 N N   . PRO B 1 293 ? -5.78500  -15.17100 -2.22600  1.000 43.44468  ? 293 PRO B N   1 
ATOM   4580 C CA  . PRO B 1 293 ? -6.20700  -16.12800 -1.19200  1.000 37.90191  ? 293 PRO B CA  1 
ATOM   4581 C C   . PRO B 1 293 ? -6.55300  -15.46900 0.13000   1.000 43.55259  ? 293 PRO B C   1 
ATOM   4582 O O   . PRO B 1 293 ? -7.57400  -15.81100 0.75900   1.000 42.36297  ? 293 PRO B O   1 
ATOM   4583 C CB  . PRO B 1 293 ? -4.98900  -17.04800 -1.04900  1.000 41.67342  ? 293 PRO B CB  1 
ATOM   4584 C CG  . PRO B 1 293 ? -4.36300  -17.03800 -2.48800  1.000 42.42088  ? 293 PRO B CG  1 
ATOM   4585 C CD  . PRO B 1 293 ? -4.58700  -15.61500 -2.97600  1.000 40.96544  ? 293 PRO B CD  1 
ATOM   4586 N N   . PHE B 1 294 ? -5.77000  -14.46400 0.52200   1.000 44.46059  ? 294 PHE B N   1 
ATOM   4587 C CA  . PHE B 1 294 ? -6.06100  -13.71200 1.73400   1.000 46.11869  ? 294 PHE B CA  1 
ATOM   4588 C C   . PHE B 1 294 ? -7.38100  -12.96000 1.64100   1.000 42.79724  ? 294 PHE B C   1 
ATOM   4589 O O   . PHE B 1 294 ? -8.12700  -12.89800 2.63200   1.000 47.21356  ? 294 PHE B O   1 
ATOM   4590 C CB  . PHE B 1 294 ? -4.91900  -12.73000 2.03300   1.000 46.86615  ? 294 PHE B CB  1 
ATOM   4591 C CG  . PHE B 1 294 ? -5.18600  -11.85400 3.22400   1.000 50.93769  ? 294 PHE B CG  1 
ATOM   4592 C CD1 . PHE B 1 294 ? -5.83500  -10.62700 3.08300   1.000 58.00959  ? 294 PHE B CD1 1 
ATOM   4593 C CD2 . PHE B 1 294 ? -4.82200  -12.27200 4.50100   1.000 56.32254  ? 294 PHE B CD2 1 
ATOM   4594 C CE1 . PHE B 1 294 ? -6.09800  -9.82600  4.17900   1.000 56.05935  ? 294 PHE B CE1 1 
ATOM   4595 C CE2 . PHE B 1 294 ? -5.08100  -11.45800 5.62400   1.000 57.40951  ? 294 PHE B CE2 1 
ATOM   4596 C CZ  . PHE B 1 294 ? -5.72000  -10.24300 5.45400   1.000 55.61193  ? 294 PHE B CZ  1 
ATOM   4597 N N   . ASP B 1 295 ? -7.67700  -12.33700 0.49100   1.000 39.77582  ? 295 ASP B N   1 
ATOM   4598 C CA  . ASP B 1 295 ? -8.95600  -11.63800 0.33600   1.000 39.73898  ? 295 ASP B CA  1 
ATOM   4599 C C   . ASP B 1 295 ? -10.12800 -12.58700 0.49800   1.000 43.19728  ? 295 ASP B C   1 
ATOM   4600 O O   . ASP B 1 295 ? -11.20600 -12.17100 0.93400   1.000 39.18101  ? 295 ASP B O   1 
ATOM   4601 C CB  . ASP B 1 295 ? -9.09000  -10.98500 -1.03400  1.000 41.50234  ? 295 ASP B CB  1 
ATOM   4602 C CG  . ASP B 1 295 ? -8.02700  -9.92500  -1.25900  1.000 43.21834  ? 295 ASP B CG  1 
ATOM   4603 O OD1 . ASP B 1 295 ? -7.49000  -9.46300  -0.21700  1.000 43.47363  ? 295 ASP B OD1 1 
ATOM   4604 O OD2 . ASP B 1 295 ? -7.74400  -9.60300  -2.43900  1.000 40.83911  ? 295 ASP B OD2 1 
ATOM   4605 N N   . VAL B 1 296 ? -9.95600  -13.82300 0.06300   1.000 40.84437  ? 296 VAL B N   1 
ATOM   4606 C CA  . VAL B 1 296 ? -11.09400 -14.77500 0.12600   1.000 41.82080  ? 296 VAL B CA  1 
ATOM   4607 C C   . VAL B 1 296 ? -11.32900 -15.11700 1.59900   1.000 43.03411  ? 296 VAL B C   1 
ATOM   4608 O O   . VAL B 1 296 ? -12.46100 -14.99600 2.05900   1.000 46.99511  ? 296 VAL B O   1 
ATOM   4609 C CB  . VAL B 1 296 ? -10.84800 -16.01700 -0.74600  1.000 35.93589  ? 296 VAL B CB  1 
ATOM   4610 C CG1 . VAL B 1 296 ? -11.88300 -17.10000 -0.49300  1.000 38.90730  ? 296 VAL B CG1 1 
ATOM   4611 C CG2 . VAL B 1 296 ? -10.78400 -15.66200 -2.22100  1.000 34.75154  ? 296 VAL B CG2 1 
ATOM   4612 N N   . VAL B 1 297 ? -10.26100 -15.46500 2.30600   1.000 42.37350  ? 297 VAL B N   1 
ATOM   4613 C CA  . VAL B 1 297 ? -10.40300 -15.80000 3.75000   1.000 47.40305  ? 297 VAL B CA  1 
ATOM   4614 C C   . VAL B 1 297 ? -10.99200 -14.59700 4.49100   1.000 51.74305  ? 297 VAL B C   1 
ATOM   4615 O O   . VAL B 1 297 ? -11.91000 -14.79900 5.28700   1.000 51.04296  ? 297 VAL B O   1 
ATOM   4616 C CB  . VAL B 1 297 ? -9.06600  -16.24900 4.36200   1.000 50.49816  ? 297 VAL B CB  1 
ATOM   4617 C CG1 . VAL B 1 297 ? -9.17200  -16.46400 5.86100   1.000 54.95659  ? 297 VAL B CG1 1 
ATOM   4618 C CG2 . VAL B 1 297 ? -8.53000  -17.49500 3.67900   1.000 51.99044  ? 297 VAL B CG2 1 
ATOM   4619 N N   . ARG B 1 298 ? -10.49700 -13.39200 4.21500   1.000 45.92130  ? 298 ARG B N   1 
ATOM   4620 C CA  . ARG B 1 298 ? -10.98000 -12.22700 4.94900   1.000 48.79006  ? 298 ARG B CA  1 
ATOM   4621 C C   . ARG B 1 298 ? -12.50000 -12.08400 4.83100   1.000 54.72761  ? 298 ARG B C   1 
ATOM   4622 O O   . ARG B 1 298 ? -13.17800 -11.74000 5.79600   1.000 54.59339  ? 298 ARG B O   1 
ATOM   4623 C CB  . ARG B 1 298 ? -10.30200 -10.93800 4.44900   1.000 51.95623  ? 298 ARG B CB  1 
ATOM   4624 C CG  . ARG B 1 298 ? -11.24500 -9.69400  4.56300   1.000 56.90419  ? 298 ARG B CG  1 
ATOM   4625 C CD  . ARG B 1 298 ? -10.61400 -8.32400  4.25700   1.000 55.70668  ? 298 ARG B CD  1 
ATOM   4626 N NE  . ARG B 1 298 ? -9.63100  -8.36100  3.18700   1.000 66.87381  ? 298 ARG B NE  1 
ATOM   4627 C CZ  . ARG B 1 298 ? -9.60100  -7.54000  2.13800   1.000 68.43978  ? 298 ARG B CZ  1 
ATOM   4628 N NH1 . ARG B 1 298 ? -10.58900 -6.66100  1.90600   1.000 57.88589  ? 298 ARG B NH1 1 
ATOM   4629 N NH2 . ARG B 1 298 ? -8.53000  -7.56000  1.33000   1.000 53.67749  ? 298 ARG B NH2 1 
ATOM   4630 N N   . GLN B 1 299 ? -13.04300 -12.34200 3.65400   1.000 45.79496  ? 299 GLN B N   1 
ATOM   4631 C CA  . GLN B 1 299 ? -14.43900 -12.05800 3.36800   1.000 50.14812  ? 299 GLN B CA  1 
ATOM   4632 C C   . GLN B 1 299 ? -15.33000 -13.25200 3.67200   1.000 52.94319  ? 299 GLN B C   1 
ATOM   4633 O O   . GLN B 1 299 ? -16.44300 -13.08600 4.19400   1.000 53.75381  ? 299 GLN B O   1 
ATOM   4634 C CB  . GLN B 1 299 ? -14.56600 -11.62800 1.91200   1.000 46.03973  ? 299 GLN B CB  1 
ATOM   4635 C CG  . GLN B 1 299 ? -15.94900 -11.35100 1.57100   1.000 43.51311  ? 299 GLN B CG  1 
ATOM   4636 C CD  . GLN B 1 299 ? -16.18400 -10.70200 0.24400   1.000 46.54769  ? 299 GLN B CD  1 
ATOM   4637 O OE1 . GLN B 1 299 ? -17.32800 -10.64000 -0.17800  1.000 37.83348  ? 299 GLN B OE1 1 
ATOM   4638 N NE2 . GLN B 1 299 ? -15.10100 -10.16500 -0.44000  1.000 39.22839  ? 299 GLN B NE2 1 
ATOM   4639 N N   . CYS B 1 300 ? -14.85000 -14.45800 3.39000   1.000 48.31895  ? 300 CYS B N   1 
ATOM   4640 C CA  . CYS B 1 300 ? -15.62100 -15.66000 3.66700   1.000 54.36441  ? 300 CYS B CA  1 
ATOM   4641 C C   . CYS B 1 300 ? -15.57400 -16.05700 5.15300   1.000 58.35437  ? 300 CYS B C   1 
ATOM   4642 O O   . CYS B 1 300 ? -16.41600 -16.86600 5.57800   1.000 68.66086  ? 300 CYS B O   1 
ATOM   4643 C CB  . CYS B 1 300 ? -15.11500 -16.77700 2.74600   1.000 49.56647  ? 300 CYS B CB  1 
ATOM   4644 S SG  . CYS B 1 300 ? -15.58000 -16.48300 0.97200   1.000 54.81447  ? 300 CYS B SG  1 
ATOM   4645 N N   . SER B 1 301 ? -14.57400 -15.56900 5.93400   1.000 64.06031  ? 301 SER B N   1 
ATOM   4646 C CA  . SER B 1 301 ? -14.51700 -15.68800 7.40400   1.000 76.17492  ? 301 SER B CA  1 
ATOM   4647 C C   . SER B 1 301 ? -14.93500 -14.41200 8.14900   1.000 76.99081  ? 301 SER B C   1 
ATOM   4648 O O   . SER B 1 301 ? -15.05600 -14.45500 9.37900   1.000 79.62007  ? 301 SER B O   1 
ATOM   4649 C CB  . SER B 1 301 ? -13.11400 -16.08000 7.92800   1.000 76.37495  ? 301 SER B CB  1 
ATOM   4650 O OG  . SER B 1 301 ? -12.15700 -15.01100 7.88700   1.000 79.63323  ? 301 SER B OG  1 
ATOM   4651 N N   . GLY B 1 302 ? -15.06800 -13.26600 7.46100   1.000 72.98770  ? 302 GLY B N   1 
ATOM   4652 C CA  . GLY B 1 302 ? -15.51400 -12.02000 8.08600   1.000 75.40378  ? 302 GLY B CA  1 
ATOM   4653 C C   . GLY B 1 302 ? -14.66000 -11.47500 9.22300   1.000 90.79773  ? 302 GLY B C   1 
ATOM   4654 O O   . GLY B 1 302 ? -15.13400 -11.36000 10.36400  1.000 86.40510  ? 302 GLY B O   1 
ATOM   4655 N N   . VAL B 1 303 ? -13.40800 -11.11700 8.91300   1.000 108.94464 ? 303 VAL B N   1 
ATOM   4656 C CA  . VAL B 1 303 ? -12.42400 -10.67000 9.91200   1.000 113.77943 ? 303 VAL B CA  1 
ATOM   4657 C C   . VAL B 1 303 ? -12.70400 -9.24700  10.44200  1.000 106.96019 ? 303 VAL B C   1 
ATOM   4658 O O   . VAL B 1 303 ? -13.21200 -8.37300  9.73100   1.000 94.02706  ? 303 VAL B O   1 
ATOM   4659 C CB  . VAL B 1 303 ? -10.97900 -10.76700 9.33100   1.000 93.92442  ? 303 VAL B CB  1 
ATOM   4660 C CG1 . VAL B 1 303 ? -10.87600 -9.98200  8.05000   1.000 91.19514  ? 303 VAL B CG1 1 
ATOM   4661 C CG2 . VAL B 1 303 ? -9.93200  -10.26600 10.34400  1.000 95.60094  ? 303 VAL B CG2 1 
HETATM 4662 N N1  . THC C 2 1   ? -35.73600 -24.42100 2.74300   1.000 87.27625  ? 1   THC C N1  1 
HETATM 4663 C CN  . THC C 2 1   ? -35.37500 -25.77600 3.01800   1.000 112.47664 ? 1   THC C CN  1 
HETATM 4664 O ON  . THC C 2 1   ? -35.02800 -26.59200 2.15900   1.000 129.53395 ? 1   THC C ON  1 
HETATM 4665 C CM  . THC C 2 1   ? -36.42700 -26.04600 4.06000   1.000 96.73528  ? 1   THC C CM  1 
HETATM 4666 C CA  . THC C 2 1   ? -34.88800 -23.67100 3.66200   1.000 77.36980  ? 1   THC C CA  1 
HETATM 4667 C CB  . THC C 2 1   ? -33.56000 -23.26400 3.02700   1.000 75.32482  ? 1   THC C CB  1 
HETATM 4668 O OG1 . THC C 2 1   ? -33.58200 -23.61900 1.63900   1.000 86.09717  ? 1   THC C OG1 1 
HETATM 4669 C CG2 . THC C 2 1   ? -32.38200 -23.92700 3.73800   1.000 76.68288  ? 1   THC C CG2 1 
HETATM 4670 C C   . THC C 2 1   ? -35.59600 -22.41300 4.12000   1.000 67.62390  ? 1   THC C C   1 
HETATM 4671 O O   . THC C 2 1   ? -36.51200 -21.90700 3.45700   1.000 65.01306  ? 1   THC C O   1 
ATOM   4672 N N   A SER C 2 2   ? -35.17000 -21.89300 5.26200   0.440 64.77882  ? 2   SER C N   1 
ATOM   4673 N N   B SER C 2 2   ? -35.15600 -21.88500 5.25000   0.560 64.78408  ? 2   SER C N   1 
ATOM   4674 C CA  A SER C 2 2   ? -35.76500 -20.68900 5.80900   0.440 61.55475  ? 2   SER C CA  1 
ATOM   4675 C CA  B SER C 2 2   ? -35.77100 -20.69700 5.80400   0.560 61.75477  ? 2   SER C CA  1 
ATOM   4676 C C   A SER C 2 2   ? -34.77500 -19.53600 5.77900   0.440 57.41478  ? 2   SER C C   1 
ATOM   4677 C C   B SER C 2 2   ? -34.77700 -19.54400 5.82600   0.560 57.43320  ? 2   SER C C   1 
ATOM   4678 O O   A SER C 2 2   ? -33.55900 -19.71700 5.65600   0.440 57.47005  ? 2   SER C O   1 
ATOM   4679 O O   B SER C 2 2   ? -33.55700 -19.72800 5.73900   0.560 57.32529  ? 2   SER C O   1 
ATOM   4680 C CB  A SER C 2 2   ? -36.23000 -20.90200 7.24800   0.440 59.48608  ? 2   SER C CB  1 
ATOM   4681 C CB  B SER C 2 2   ? -36.31600 -20.98400 7.20900   0.560 59.69400  ? 2   SER C CB  1 
ATOM   4682 O OG  A SER C 2 2   ? -35.11300 -20.82600 8.11400   0.440 58.00169  ? 2   SER C OG  1 
ATOM   4683 O OG  B SER C 2 2   ? -37.01300 -22.22800 7.22500   0.560 58.35700  ? 2   SER C OG  1 
ATOM   4684 N N   . ALA C 2 3   ? -35.32800 -18.34100 5.93600   1.000 55.22241  ? 3   ALA C N   1 
ATOM   4685 C CA  . ALA C 2 3   ? -34.51200 -17.16000 6.12800   1.000 53.96700  ? 3   ALA C CA  1 
ATOM   4686 C C   . ALA C 2 3   ? -33.68100 -17.28600 7.40500   1.000 54.96712  ? 3   ALA C C   1 
ATOM   4687 O O   . ALA C 2 3   ? -34.02600 -18.01000 8.35900   1.000 53.82224  ? 3   ALA C O   1 
ATOM   4688 C CB  . ALA C 2 3   ? -35.41200 -15.93000 6.17800   1.000 52.01413  ? 3   ALA C CB  1 
ATOM   4689 N N   . VAL C 2 4   ? -32.56800 -16.57900 7.41700   1.000 46.68981  ? 4   VAL C N   1 
ATOM   4690 C CA  . VAL C 2 4   ? -31.59500 -16.62500 8.49100   1.000 48.77164  ? 4   VAL C CA  1 
ATOM   4691 C C   . VAL C 2 4   ? -31.41000 -15.18800 8.95300   1.000 49.41382  ? 4   VAL C C   1 
ATOM   4692 O O   . VAL C 2 4   ? -30.80100 -14.38800 8.22900   1.000 47.40305  ? 4   VAL C O   1 
ATOM   4693 C CB  . VAL C 2 4   ? -30.24600 -17.21800 8.01600   1.000 51.61145  ? 4   VAL C CB  1 
ATOM   4694 C CG1 . VAL C 2 4   ? -29.15700 -17.06300 9.10500   1.000 48.52424  ? 4   VAL C CG1 1 
ATOM   4695 C CG2 . VAL C 2 4   ? -30.43600 -18.68000 7.62100   1.000 56.40150  ? 4   VAL C CG2 1 
ATOM   4696 N N   . LEU C 2 5   ? -31.81800 -14.89000 10.18200  1.000 46.16606  ? 5   LEU C N   1 
ATOM   4697 C CA  . LEU C 2 5   ? -31.55600 -13.57300 10.73800  1.000 44.85538  ? 5   LEU C CA  1 
ATOM   4698 C C   . LEU C 2 5   ? -30.09300 -13.51000 11.11100  1.000 46.20554  ? 5   LEU C C   1 
ATOM   4699 O O   . LEU C 2 5   ? -29.62800 -14.29500 11.93400  1.000 47.06091  ? 5   LEU C O   1 
ATOM   4700 C CB  . LEU C 2 5   ? -32.43600 -13.30500 11.96100  1.000 48.41633  ? 5   LEU C CB  1 
ATOM   4701 C CG  . LEU C 2 5   ? -33.90200 -13.10500 11.60200  1.000 48.75321  ? 5   LEU C CG  1 
ATOM   4702 C CD1 . LEU C 2 5   ? -34.72600 -13.21700 12.88600  1.000 50.76661  ? 5   LEU C CD1 1 
ATOM   4703 C CD2 . LEU C 2 5   ? -34.11200 -11.77200 11.00400  1.000 47.44779  ? 5   LEU C CD2 1 
ATOM   4704 N N   . GLN C 2 6   ? -29.34100 -12.63400 10.45700  1.000 44.26057  ? 6   GLN C N   1 
ATOM   4705 C CA  . GLN C 2 6   ? -27.89600 -12.75000 10.59700  1.000 43.02095  ? 6   GLN C CA  1 
ATOM   4706 C C   . GLN C 2 6   ? -27.32500 -12.00600 11.79900  1.000 46.63717  ? 6   GLN C C   1 
ATOM   4707 O O   . GLN C 2 6   ? -26.27900 -11.35200 11.73000  1.000 44.07634  ? 6   GLN C O   1 
ATOM   4708 C CB  . GLN C 2 6   ? -27.24700 -12.32800 9.29800   1.000 40.44432  ? 6   GLN C CB  1 
ATOM   4709 C CG  . GLN C 2 6   ? -27.40800 -13.43600 8.26600   1.000 42.43404  ? 6   GLN C CG  1 
ATOM   4710 C CD  . GLN C 2 6   ? -26.66500 -13.10000 6.94400   1.000 44.55797  ? 6   GLN C CD  1 
ATOM   4711 O OE1 . GLN C 2 6   ? -26.90900 -12.04000 6.35000   1.000 40.09691  ? 6   GLN C OE1 1 
ATOM   4712 N NE2 . GLN C 2 6   ? -25.83000 -14.01900 6.47100   1.000 45.10804  ? 6   GLN C NE2 1 
ATOM   4713 N N   . SER C 2 7   ? -27.98100 -12.14900 12.95300  1.000 46.10553  ? 7   SER C N   1 
ATOM   4714 C CA  . SER C 2 7   ? -27.29800 -11.82300 14.19900  1.000 47.84521  ? 7   SER C CA  1 
ATOM   4715 C C   . SER C 2 7   ? -26.18300 -12.84100 14.45500  1.000 50.29814  ? 7   SER C C   1 
ATOM   4716 O O   . SER C 2 7   ? -26.08500 -13.89000 13.80500  1.000 50.55343  ? 7   SER C O   1 
ATOM   4717 C CB  . SER C 2 7   ? -28.29900 -11.80800 15.38100  1.000 47.78731  ? 7   SER C CB  1 
ATOM   4718 O OG  . SER C 2 7   ? -29.02800 -13.01400 15.42400  1.000 52.52998  ? 7   SER C OG  1 
ATOM   4719 N N   . GLY C 2 8   ? -25.32100 -12.51300 15.40800  1.000 51.94307  ? 8   GLY C N   1 
ATOM   4720 C CA  . GLY C 2 8   ? -24.21600 -13.36700 15.77500  1.000 55.39875  ? 8   GLY C CA  1 
ATOM   4721 C C   . GLY C 2 8   ? -24.38800 -13.84000 17.20600  1.000 62.87070  ? 8   GLY C C   1 
ATOM   4722 O O   . GLY C 2 8   ? -25.33600 -13.45900 17.89800  1.000 63.09178  ? 8   GLY C O   1 
ATOM   4723 N N   . PHE C 2 9   ? -23.46700 -14.69300 17.63000  1.000 67.42651  ? 9   PHE C N   1 
ATOM   4724 C CA  A PHE C 2 9   ? -23.45300 -15.25400 18.97900  0.560 71.85335  ? 9   PHE C CA  1 
ATOM   4725 C CA  B PHE C 2 9   ? -23.49100 -15.18900 18.99400  0.440 71.85335  ? 9   PHE C CA  1 
ATOM   4726 C C   . PHE C 2 9   ? -22.25200 -14.70200 19.72500  1.000 73.96150  ? 9   PHE C C   1 
ATOM   4727 O O   . PHE C 2 9   ? -21.21700 -14.41000 19.12300  1.000 74.61421  ? 9   PHE C O   1 
ATOM   4728 C CB  A PHE C 2 9   ? -23.40200 -16.79000 18.95700  0.560 73.32458  ? 9   PHE C CB  1 
ATOM   4729 C CB  B PHE C 2 9   ? -23.61700 -16.71600 19.03600  0.440 73.33248  ? 9   PHE C CB  1 
ATOM   4730 C CG  A PHE C 2 9   ? -23.06000 -17.42100 20.29500  0.560 75.67486  ? 9   PHE C CG  1 
ATOM   4731 C CG  B PHE C 2 9   ? -24.98000 -17.21600 18.61300  0.440 74.50367  ? 9   PHE C CG  1 
ATOM   4732 C CD1 A PHE C 2 9   ? -24.06000 -17.75200 21.20800  0.560 74.79055  ? 9   PHE C CD1 1 
ATOM   4733 C CD1 B PHE C 2 9   ? -26.08900 -16.38200 18.67600  0.440 73.31932  ? 9   PHE C CD1 1 
ATOM   4734 C CD2 A PHE C 2 9   ? -21.73100 -17.70400 20.62700  0.560 77.06713  ? 9   PHE C CD2 1 
ATOM   4735 C CD2 B PHE C 2 9   ? -25.15100 -18.50800 18.13900  0.440 76.54076  ? 9   PHE C CD2 1 
ATOM   4736 C CE1 A PHE C 2 9   ? -23.73600 -18.33700 22.42800  0.560 73.10350  ? 9   PHE C CE1 1 
ATOM   4737 C CE1 B PHE C 2 9   ? -27.33800 -16.82700 18.28100  0.440 76.60919  ? 9   PHE C CE1 1 
ATOM   4738 C CE2 A PHE C 2 9   ? -21.40500 -18.28400 21.84100  0.560 77.74880  ? 9   PHE C CE2 1 
ATOM   4739 C CE2 B PHE C 2 9   ? -26.39600 -18.95800 17.73900  0.440 78.18832  ? 9   PHE C CE2 1 
ATOM   4740 C CZ  A PHE C 2 9   ? -22.40900 -18.60200 22.74100  0.560 77.53035  ? 9   PHE C CZ  1 
ATOM   4741 C CZ  B PHE C 2 9   ? -27.49000 -18.11900 17.81400  0.440 80.76495  ? 9   PHE C CZ  1 
ATOM   4742 N N   . ARG C 2 10  ? -22.39400 -14.54500 21.03600  1.000 75.54327  ? 10  ARG C N   1 
ATOM   4743 C CA  . ARG C 2 10  ? -21.32000 -13.95900 21.82200  1.000 81.02550  ? 10  ARG C CA  1 
ATOM   4744 C C   . ARG C 2 10  ? -21.30900 -14.59600 23.19700  1.000 83.47317  ? 10  ARG C C   1 
ATOM   4745 O O   . ARG C 2 10  ? -22.31400 -14.52700 23.91300  1.000 80.19909  ? 10  ARG C O   1 
ATOM   4746 C CB  . ARG C 2 10  ? -21.47900 -12.44300 21.92900  1.000 80.74916  ? 10  ARG C CB  1 
ATOM   4747 C CG  . ARG C 2 10  ? -20.30600 -11.76800 22.57700  1.000 87.41048  ? 10  ARG C CG  1 
ATOM   4748 C CD  . ARG C 2 10  ? -20.56700 -10.30100 22.71600  1.000 85.51552  ? 10  ARG C CD  1 
ATOM   4749 N NE  . ARG C 2 10  ? -19.83100 -9.75000  23.84200  1.000 94.68504  ? 10  ARG C NE  1 
ATOM   4750 C CZ  . ARG C 2 10  ? -19.80800 -8.46500  24.16400  1.000 100.30676 ? 10  ARG C CZ  1 
ATOM   4751 N NH1 . ARG C 2 10  ? -20.45500 -7.56100  23.44400  1.000 104.19144 ? 10  ARG C NH1 1 
ATOM   4752 N NH2 . ARG C 2 10  ? -19.11900 -8.07800  25.23600  1.000 106.56014 ? 10  ARG C NH2 1 
ATOM   4753 N N   . LYS C 2 11  ? -20.18000 -15.23300 23.53100  1.000 89.33966  ? 11  LYS C N   1 
ATOM   4754 C CA  . LYS C 2 11  ? -19.85500 -15.73900 24.87100  1.000 89.64496  ? 11  LYS C CA  1 
ATOM   4755 C C   . LYS C 2 11  ? -20.98600 -16.51400 25.52500  1.000 89.52916  ? 11  LYS C C   1 
ATOM   4756 O O   . LYS C 2 11  ? -21.46900 -16.13100 26.59200  1.000 89.94763  ? 11  LYS C O   1 
ATOM   4757 C CB  . LYS C 2 11  ? -19.43400 -14.57700 25.78200  1.000 91.70573  ? 11  LYS C CB  1 
ATOM   4758 C CG  . LYS C 2 11  ? -18.31300 -13.68800 25.21000  1.000 97.66961  ? 11  LYS C CG  1 
ATOM   4759 C CD  . LYS C 2 11  ? -17.00000 -14.45500 24.94100  1.000 106.99178 ? 11  LYS C CD  1 
ATOM   4760 C CE  . LYS C 2 11  ? -16.44900 -15.20900 26.18000  1.000 111.43441 ? 11  LYS C CE  1 
ATOM   4761 N NZ  . LYS C 2 11  ? -16.03300 -14.36800 27.35300  1.000 101.66219 ? 11  LYS C NZ  1 
HETATM 4762 N N1  . THC D 2 1   ? 1.07400   6.86500   -28.26400 1.000 64.74724  ? 1   THC D N1  1 
HETATM 4763 C CN  . THC D 2 1   ? 2.25500   7.09200   -28.85900 1.000 67.91867  ? 1   THC D CN  1 
HETATM 4764 O ON  . THC D 2 1   ? 2.83500   8.19200   -28.72700 1.000 64.90515  ? 1   THC D ON  1 
HETATM 4765 C CM  . THC D 2 1   ? 2.82700   5.96100   -29.68200 1.000 69.04249  ? 1   THC D CM  1 
HETATM 4766 C CA  . THC D 2 1   ? 0.49100   7.93500   -27.45100 1.000 58.38858  ? 1   THC D CA  1 
HETATM 4767 C CB  . THC D 2 1   ? -0.99700  7.65200   -27.12400 1.000 58.64914  ? 1   THC D CB  1 
HETATM 4768 O OG1 . THC D 2 1   ? -1.42200  6.49500   -27.85400 1.000 64.48931  ? 1   THC D OG1 1 
HETATM 4769 C CG2 . THC D 2 1   ? -1.88400  8.84600   -27.52700 1.000 59.05182  ? 1   THC D CG2 1 
HETATM 4770 C C   . THC D 2 1   ? 1.30000   8.16100   -26.12900 1.000 52.73527  ? 1   THC D C   1 
HETATM 4771 O O   . THC D 2 1   ? 2.07100   7.30900   -25.66700 1.000 52.46155  ? 1   THC D O   1 
ATOM   4772 N N   . SER D 2 2   ? 1.10700   9.32000   -25.52200 1.000 54.28546  ? 2   SER D N   1 
ATOM   4773 C CA  A SER D 2 2   ? 1.81600   9.72500   -24.32000 0.540 53.81172  ? 2   SER D CA  1 
ATOM   4774 C CA  B SER D 2 2   ? 1.84200   9.65300   -24.31500 0.460 51.76673  ? 2   SER D CA  1 
ATOM   4775 C C   . SER D 2 2   ? 1.04500   9.33000   -23.05700 1.000 50.60870  ? 2   SER D C   1 
ATOM   4776 O O   . SER D 2 2   ? -0.19000  9.31700   -23.04500 1.000 47.32673  ? 2   SER D O   1 
ATOM   4777 C CB  A SER D 2 2   ? 2.03700   11.23900  -24.35900 0.540 50.07706  ? 2   SER D CB  1 
ATOM   4778 C CB  B SER D 2 2   ? 2.22100   11.12700  -24.30100 0.460 50.34814  ? 2   SER D CB  1 
ATOM   4779 O OG  A SER D 2 2   ? 2.81000   11.59900  -25.51400 0.540 49.52173  ? 2   SER D OG  1 
ATOM   4780 O OG  B SER D 2 2   ? 1.10000   11.92100  -24.57200 0.460 48.77953  ? 2   SER D OG  1 
ATOM   4781 N N   . ALA D 2 3   ? 1.78800   9.03800   -21.98700 1.000 46.91089  ? 3   ALA D N   1 
ATOM   4782 C CA  . ALA D 2 3   ? 1.20400   9.06000   -20.65500 1.000 45.20279  ? 3   ALA D CA  1 
ATOM   4783 C C   . ALA D 2 3   ? 0.54500   10.41500  -20.36600 1.000 44.31847  ? 3   ALA D C   1 
ATOM   4784 O O   . ALA D 2 3   ? 0.90200   11.45900  -20.93100 1.000 42.06820  ? 3   ALA D O   1 
ATOM   4785 C CB  . ALA D 2 3   ? 2.30000   8.74500   -19.62700 1.000 43.19992  ? 3   ALA D CB  1 
ATOM   4786 N N   . VAL D 2 4   ? -0.45400  10.39000  -19.49400 1.000 40.88385  ? 4   VAL D N   1 
ATOM   4787 C CA  . VAL D 2 4   ? -1.11000  11.58900  -18.98200 1.000 40.59960  ? 4   VAL D CA  1 
ATOM   4788 C C   . VAL D 2 4   ? -0.81600  11.67100  -17.48000 1.000 41.46813  ? 4   VAL D C   1 
ATOM   4789 O O   . VAL D 2 4   ? -1.25800  10.79900  -16.71900 1.000 42.43140  ? 4   VAL D O   1 
ATOM   4790 C CB  . VAL D 2 4   ? -2.62200  11.53600  -19.25000 1.000 44.02370  ? 4   VAL D CB  1 
ATOM   4791 C CG1 . VAL D 2 4   ? -3.38900  12.75900  -18.56800 1.000 41.36285  ? 4   VAL D CG1 1 
ATOM   4792 C CG2 . VAL D 2 4   ? -2.82400  11.43900  -20.79000 1.000 43.14991  ? 4   VAL D CG2 1 
ATOM   4793 N N   . LEU D 2 5   ? -0.12600  12.73300  -17.04400 1.000 37.24920  ? 5   LEU D N   1 
ATOM   4794 C CA  . LEU D 2 5   ? 0.02400   12.98200  -15.61100 1.000 37.91507  ? 5   LEU D CA  1 
ATOM   4795 C C   . LEU D 2 5   ? -1.28900  13.51500  -15.08800 1.000 40.71541  ? 5   LEU D C   1 
ATOM   4796 O O   . LEU D 2 5   ? -1.79300  14.53200  -15.58600 1.000 41.58920  ? 5   LEU D O   1 
ATOM   4797 C CB  . LEU D 2 5   ? 1.13800   13.98600  -15.33700 1.000 40.48380  ? 5   LEU D CB  1 
ATOM   4798 C CG  . LEU D 2 5   ? 2.53300   13.42100  -15.48800 1.000 44.55797  ? 5   LEU D CG  1 
ATOM   4799 C CD1 . LEU D 2 5   ? 3.49500   14.57900  -15.36700 1.000 45.93445  ? 5   LEU D CD1 1 
ATOM   4800 C CD2 . LEU D 2 5   ? 2.81200   12.37300  -14.47300 1.000 42.76829  ? 5   LEU D CD2 1 
ATOM   4801 N N   . GLN D 2 6   ? -1.89200  12.79400  -14.13300 1.000 37.01233  ? 6   GLN D N   1 
ATOM   4802 C CA  . GLN D 2 6   ? -3.25800  13.13000  -13.73700 1.000 37.85717  ? 6   GLN D CA  1 
ATOM   4803 C C   . GLN D 2 6   ? -3.35700  14.10100  -12.53700 1.000 41.09440  ? 6   GLN D C   1 
ATOM   4804 O O   . GLN D 2 6   ? -4.23400  13.99000  -11.64500 1.000 39.27050  ? 6   GLN D O   1 
ATOM   4805 C CB  . GLN D 2 6   ? -4.00400  11.81900  -13.50000 1.000 35.97537  ? 6   GLN D CB  1 
ATOM   4806 C CG  . GLN D 2 6   ? -4.37900  11.18600  -14.85100 1.000 38.43092  ? 6   GLN D CG  1 
ATOM   4807 C CD  . GLN D 2 6   ? -5.34300  10.00400  -14.66800 1.000 38.46514  ? 6   GLN D CD  1 
ATOM   4808 O OE1 . GLN D 2 6   ? -4.99500  9.07000   -13.97300 1.000 36.08064  ? 6   GLN D OE1 1 
ATOM   4809 N NE2 . GLN D 2 6   ? -6.50700  10.02600  -15.34500 1.000 38.13878  ? 6   GLN D NE2 1 
ATOM   4810 N N   . SER D 2 7   ? -2.48500  15.10800  -12.52500 1.000 42.31823  ? 7   SER D N   1 
ATOM   4811 C CA  . SER D 2 7   ? -2.73400  16.29800  -11.74400 1.000 41.72869  ? 7   SER D CA  1 
ATOM   4812 C C   . SER D 2 7   ? -3.94100  17.02700  -12.33500 1.000 45.26859  ? 7   SER D C   1 
ATOM   4813 O O   . SER D 2 7   ? -4.39600  16.73400  -13.44000 1.000 44.98697  ? 7   SER D O   1 
ATOM   4814 C CB  . SER D 2 7   ? -1.49300  17.19500  -11.75400 1.000 44.32637  ? 7   SER D CB  1 
ATOM   4815 O OG  . SER D 2 7   ? -1.06700  17.44200  -13.07000 1.000 45.03172  ? 7   SER D OG  1 
ATOM   4816 N N   . GLY D 2 8   ? -4.43600  18.02200  -11.61500 1.000 48.32422  ? 8   GLY D N   1 
ATOM   4817 C CA  . GLY D 2 8   ? -5.53700  18.82200  -12.08800 1.000 54.41179  ? 8   GLY D CA  1 
ATOM   4818 C C   . GLY D 2 8   ? -5.18100  20.29400  -12.16300 1.000 60.09142  ? 8   GLY D C   1 
ATOM   4819 O O   . GLY D 2 8   ? -4.10100  20.72900  -11.75000 1.000 56.13305  ? 8   GLY D O   1 
ATOM   4820 N N   A PHE D 2 9   ? -6.14200  21.06200  -12.68000 0.610 65.91317  ? 9   PHE D N   1 
ATOM   4821 N N   B PHE D 2 9   ? -6.13900  21.05700  -12.66900 0.390 65.87369  ? 9   PHE D N   1 
ATOM   4822 C CA  A PHE D 2 9   ? -6.03800  22.50300  -12.89200 0.610 68.62928  ? 9   PHE D CA  1 
ATOM   4823 C CA  B PHE D 2 9   ? -6.01000  22.49300  -12.84200 0.390 68.62928  ? 9   PHE D CA  1 
ATOM   4824 C C   A PHE D 2 9   ? -6.82800  23.21900  -11.80400 0.610 70.31369  ? 9   PHE D C   1 
ATOM   4825 C C   B PHE D 2 9   ? -6.82300  23.21300  -11.77800 0.390 70.32685  ? 9   PHE D C   1 
ATOM   4826 O O   A PHE D 2 9   ? -7.84300  22.69800  -11.32300 0.610 72.01916  ? 9   PHE D O   1 
ATOM   4827 O O   B PHE D 2 9   ? -7.83700  22.69800  -11.29400 0.390 72.01127  ? 9   PHE D O   1 
ATOM   4828 C CB  A PHE D 2 9   ? -6.58100  22.88400  -14.27800 0.610 70.06630  ? 9   PHE D CB  1 
ATOM   4829 C CB  B PHE D 2 9   ? -6.47000  22.90700  -14.23800 0.390 70.09788  ? 9   PHE D CB  1 
ATOM   4830 C CG  A PHE D 2 9   ? -6.10500  24.23600  -14.79500 0.610 72.97980  ? 9   PHE D CG  1 
ATOM   4831 C CG  B PHE D 2 9   ? -5.40000  22.78400  -15.28000 0.390 70.82428  ? 9   PHE D CG  1 
ATOM   4832 C CD1 A PHE D 2 9   ? -4.83600  24.37700  -15.34600 0.610 73.10877  ? 9   PHE D CD1 1 
ATOM   4833 C CD1 B PHE D 2 9   ? -5.15900  21.58000  -15.90800 0.390 70.12683  ? 9   PHE D CD1 1 
ATOM   4834 C CD2 A PHE D 2 9   ? -6.94000  25.35300  -14.76800 0.610 74.04046  ? 9   PHE D CD2 1 
ATOM   4835 C CD2 B PHE D 2 9   ? -4.62500  23.88000  -15.62300 0.390 72.64555  ? 9   PHE D CD2 1 
ATOM   4836 C CE1 A PHE D 2 9   ? -4.41300  25.61000  -15.83800 0.610 72.50343  ? 9   PHE D CE1 1 
ATOM   4837 C CE1 B PHE D 2 9   ? -4.17300  21.47100  -16.86100 0.390 71.44014  ? 9   PHE D CE1 1 
ATOM   4838 C CE2 A PHE D 2 9   ? -6.50900  26.58300  -15.25400 0.610 73.21931  ? 9   PHE D CE2 1 
ATOM   4839 C CE2 B PHE D 2 9   ? -3.64100  23.77700  -16.57700 0.390 74.04572  ? 9   PHE D CE2 1 
ATOM   4840 C CZ  A PHE D 2 9   ? -5.25800  26.70400  -15.78600 0.610 70.93745  ? 9   PHE D CZ  1 
ATOM   4841 C CZ  B PHE D 2 9   ? -3.41300  22.57000  -17.19600 0.390 74.76949  ? 9   PHE D CZ  1 
ATOM   4842 N N   . ARG D 2 10  ? -6.35300  24.39600  -11.39900 1.000 73.00612  ? 10  ARG D N   1 
ATOM   4843 C CA  . ARG D 2 10  ? -7.08100  25.23600  -10.43200 1.000 80.25173  ? 10  ARG D CA  1 
ATOM   4844 C C   . ARG D 2 10  ? -7.45500  26.59300  -11.05000 1.000 84.36011  ? 10  ARG D C   1 
ATOM   4845 O O   . ARG D 2 10  ? -6.85400  27.02300  -12.04500 1.000 88.23953  ? 10  ARG D O   1 
ATOM   4846 C CB  . ARG D 2 10  ? -6.25800  25.44800  -9.15400  1.000 76.74604  ? 10  ARG D CB  1 
ATOM   4847 C CG  . ARG D 2 10  ? -6.95700  24.93200  -7.90100  1.000 75.36693  ? 10  ARG D CG  1 
ATOM   4848 C CD  . ARG D 2 10  ? -6.24000  25.35600  -6.62900  1.000 74.39839  ? 10  ARG D CD  1 
ATOM   4849 N NE  . ARG D 2 10  ? -7.05700  25.08600  -5.45900  1.000 77.01450  ? 10  ARG D NE  1 
ATOM   4850 C CZ  . ARG D 2 10  ? -6.99800  25.75800  -4.32100  1.000 85.87345  ? 10  ARG D CZ  1 
ATOM   4851 N NH1 . ARG D 2 10  ? -6.05800  26.67200  -4.10800  1.000 85.03914  ? 10  ARG D NH1 1 
ATOM   4852 N NH2 . ARG D 2 10  ? -7.92700  25.53300  -3.38700  1.000 83.66529  ? 10  ARG D NH2 1 
HETATM 4853 O O   . HOH E 3 .   ? -35.14600 -5.74400  34.08600  1.000 80.09118  ? 401 HOH A O   1 
HETATM 4854 O O   . HOH E 3 .   ? -27.56100 -7.97100  -12.82000 1.000 43.78946  ? 402 HOH A O   1 
HETATM 4855 O O   . HOH E 3 .   ? -9.27400  -3.44500  -11.00900 1.000 45.24490  ? 403 HOH A O   1 
HETATM 4856 O O   . HOH E 3 .   ? -27.99900 -15.83200 21.33800  1.000 70.69005  ? 404 HOH A O   1 
HETATM 4857 O O   . HOH E 3 .   ? -25.93800 -16.68700 7.94700   1.000 49.96915  ? 405 HOH A O   1 
HETATM 4858 O O   . HOH E 3 .   ? -35.65900 12.68700  -23.21100 1.000 50.54027  ? 406 HOH A O   1 
HETATM 4859 O O   . HOH E 3 .   ? -22.48000 -0.64700  8.74300   1.000 42.86303  ? 407 HOH A O   1 
HETATM 4860 O O   . HOH E 3 .   ? -23.19100 -3.50900  -7.23500  1.000 45.83444  ? 408 HOH A O   1 
HETATM 4861 O O   . HOH E 3 .   ? -28.56100 -9.39700  -19.76700 1.000 40.38379  ? 409 HOH A O   1 
HETATM 4862 O O   . HOH E 3 .   ? -36.31200 5.22300   12.94100  1.000 52.21679  ? 410 HOH A O   1 
HETATM 4863 O O   . HOH E 3 .   ? -38.47700 0.02400   -33.92700 1.000 53.80382  ? 411 HOH A O   1 
HETATM 4864 O O   . HOH E 3 .   ? -19.32800 -5.49900  -14.43400 1.000 46.73718  ? 412 HOH A O   1 
HETATM 4865 O O   . HOH E 3 .   ? -22.50200 -5.27900  22.77500  1.000 65.88158  ? 413 HOH A O   1 
HETATM 4866 O O   . HOH E 3 .   ? -41.68200 -10.57800 12.17800  1.000 53.93541  ? 414 HOH A O   1 
HETATM 4867 O O   . HOH E 3 .   ? -39.75400 -3.92700  -8.63000  1.000 48.11630  ? 415 HOH A O   1 
HETATM 4868 O O   . HOH E 3 .   ? -30.08000 12.50100  -15.43000 1.000 45.64231  ? 416 HOH A O   1 
HETATM 4869 O O   . HOH E 3 .   ? -43.34100 1.61000   -24.63600 1.000 55.58824  ? 417 HOH A O   1 
HETATM 4870 O O   . HOH E 3 .   ? -25.30100 -0.78900  -14.92200 1.000 33.31978  ? 418 HOH A O   1 
HETATM 4871 O O   . HOH E 3 .   ? -26.22700 2.07100   -31.53000 1.000 48.79796  ? 419 HOH A O   1 
HETATM 4872 O O   . HOH E 3 .   ? -19.25100 -9.40000  5.12500   1.000 42.76829  ? 420 HOH A O   1 
HETATM 4873 O O   . HOH E 3 .   ? -17.84100 -12.34500 -24.34600 1.000 62.13903  ? 421 HOH A O   1 
HETATM 4874 O O   . HOH E 3 .   ? -31.71000 3.25200   -11.77200 1.000 37.24920  ? 422 HOH A O   1 
HETATM 4875 O O   . HOH E 3 .   ? -22.79100 6.34300   -6.35300  1.000 49.26643  ? 423 HOH A O   1 
HETATM 4876 O O   . HOH E 3 .   ? -37.28300 5.69000   -32.84300 1.000 54.86184  ? 424 HOH A O   1 
HETATM 4877 O O   . HOH E 3 .   ? -40.84500 -5.73100  -14.66300 1.000 56.32517  ? 425 HOH A O   1 
HETATM 4878 O O   . HOH E 3 .   ? -19.92000 -13.89500 -26.40100 1.000 64.83409  ? 426 HOH A O   1 
HETATM 4879 O O   . HOH E 3 .   ? -41.67000 -16.02300 0.50200   1.000 57.84378  ? 427 HOH A O   1 
HETATM 4880 O O   . HOH E 3 .   ? -13.18700 8.07500   -12.80300 1.000 42.79460  ? 428 HOH A O   1 
HETATM 4881 O O   . HOH E 3 .   ? -42.32200 -9.51500  -26.01200 1.000 52.80633  ? 429 HOH A O   1 
HETATM 4882 O O   . HOH E 3 .   ? -39.52400 -10.04200 -3.81000  1.000 43.10780  ? 430 HOH A O   1 
HETATM 4883 O O   . HOH E 3 .   ? -29.26400 -9.65200  -17.10400 1.000 44.21056  ? 431 HOH A O   1 
HETATM 4884 O O   . HOH E 3 .   ? -46.71200 4.30000   -28.21300 1.000 53.06689  ? 432 HOH A O   1 
HETATM 4885 O O   . HOH E 3 .   ? -27.63400 8.48500   -32.19900 1.000 45.44229  ? 433 HOH A O   1 
HETATM 4886 O O   . HOH E 3 .   ? -22.70600 -14.40500 -28.79400 1.000 60.47830  ? 434 HOH A O   1 
HETATM 4887 O O   . HOH E 3 .   ? -24.29900 15.98900  -20.74900 1.000 51.78779  ? 435 HOH A O   1 
HETATM 4888 O O   . HOH E 3 .   ? -21.84400 -8.69100  15.22300  1.000 51.42722  ? 436 HOH A O   1 
HETATM 4889 O O   . HOH E 3 .   ? -35.14200 -6.41800  1.53000   1.000 38.96257  ? 437 HOH A O   1 
HETATM 4890 O O   . HOH E 3 .   ? -18.59300 9.43900   11.88800  1.000 51.39564  ? 438 HOH A O   1 
HETATM 4891 O O   . HOH E 3 .   ? -27.54000 -6.06500  -5.34800  1.000 39.58896  ? 439 HOH A O   1 
HETATM 4892 O O   . HOH E 3 .   ? -33.18700 -10.62000 -16.23000 1.000 46.00815  ? 440 HOH A O   1 
HETATM 4893 O O   . HOH E 3 .   ? -22.85800 1.86000   -8.20800  1.000 40.20219  ? 441 HOH A O   1 
HETATM 4894 O O   . HOH E 3 .   ? -38.92000 13.31000  -16.97700 1.000 47.42411  ? 442 HOH A O   1 
HETATM 4895 O O   . HOH E 3 .   ? -16.04600 6.60600   -27.60700 1.000 47.70835  ? 443 HOH A O   1 
HETATM 4896 O O   . HOH E 3 .   ? -32.17300 -12.27100 -20.07800 1.000 48.79532  ? 444 HOH A O   1 
HETATM 4897 O O   . HOH E 3 .   ? -42.73000 -5.84500  3.99100   1.000 54.83289  ? 445 HOH A O   1 
HETATM 4898 O O   . HOH E 3 .   ? -28.46900 -18.70700 1.98800   1.000 53.65643  ? 446 HOH A O   1 
HETATM 4899 O O   . HOH E 3 .   ? -43.99300 -2.32900  -26.21100 1.000 47.36094  ? 447 HOH A O   1 
HETATM 4900 O O   . HOH E 3 .   ? -13.63500 -4.65200  -22.11500 1.000 48.18736  ? 448 HOH A O   1 
HETATM 4901 O O   . HOH E 3 .   ? -19.19700 13.48100  -15.49400 1.000 63.76291  ? 449 HOH A O   1 
HETATM 4902 O O   . HOH E 3 .   ? -40.25400 -0.03800  -15.61900 1.000 41.00755  ? 450 HOH A O   1 
HETATM 4903 O O   . HOH E 3 .   ? -32.12500 10.45500  -26.75300 1.000 44.92118  ? 451 HOH A O   1 
HETATM 4904 O O   . HOH E 3 .   ? -24.64400 4.76100   -4.96100  1.000 39.45210  ? 452 HOH A O   1 
HETATM 4905 O O   . HOH E 3 .   ? -36.73100 11.47500  -15.63700 1.000 45.24753  ? 453 HOH A O   1 
HETATM 4906 O O   . HOH E 3 .   ? -41.67200 -4.21000  7.37900   1.000 40.86806  ? 454 HOH A O   1 
HETATM 4907 O O   . HOH E 3 .   ? -42.75500 8.64000   -24.73800 1.000 40.92859  ? 455 HOH A O   1 
HETATM 4908 O O   . HOH E 3 .   ? -25.91400 -12.34500 -2.41600  1.000 44.31584  ? 456 HOH A O   1 
HETATM 4909 O O   . HOH E 3 .   ? -26.95100 6.38700   -7.74900  1.000 43.57101  ? 457 HOH A O   1 
HETATM 4910 O O   . HOH E 3 .   ? -28.79100 5.65100   -5.94000  1.000 43.84736  ? 458 HOH A O   1 
HETATM 4911 O O   . HOH E 3 .   ? -39.00700 14.41700  -22.38000 1.000 52.27469  ? 459 HOH A O   1 
HETATM 4912 O O   . HOH E 3 .   ? -19.78900 5.64800   -9.67800  1.000 42.12610  ? 460 HOH A O   1 
HETATM 4913 O O   . HOH E 3 .   ? -43.32900 0.99500   -32.69500 1.000 56.05672  ? 461 HOH A O   1 
HETATM 4914 O O   . HOH E 3 .   ? -37.26100 8.56700   1.32100   1.000 50.55343  ? 462 HOH A O   1 
HETATM 4915 O O   . HOH E 3 .   ? -40.36800 5.08900   -14.63100 1.000 41.08124  ? 463 HOH A O   1 
HETATM 4916 O O   . HOH E 3 .   ? -45.06200 -8.06600  18.25900  1.000 60.51252  ? 464 HOH A O   1 
HETATM 4917 O O   . HOH E 3 .   ? -30.54900 -15.04400 18.57400  1.000 74.39313  ? 465 HOH A O   1 
HETATM 4918 O O   . HOH E 3 .   ? -31.49300 -10.42800 -11.66600 1.000 46.31082  ? 466 HOH A O   1 
HETATM 4919 O O   . HOH E 3 .   ? -32.60200 -11.83600 -5.75200  1.000 44.48954  ? 467 HOH A O   1 
HETATM 4920 O O   . HOH E 3 .   ? -14.88900 -2.55600  -6.94500  1.000 46.19764  ? 468 HOH A O   1 
HETATM 4921 O O   . HOH E 3 .   ? -33.96600 4.88600   5.84300   1.000 46.34503  ? 469 HOH A O   1 
HETATM 4922 O O   . HOH E 3 .   ? -30.28800 -9.50200  -13.64300 1.000 48.44002  ? 470 HOH A O   1 
HETATM 4923 O O   . HOH E 3 .   ? -38.59900 7.82700   -26.02200 1.000 45.33438  ? 471 HOH A O   1 
HETATM 4924 O O   . HOH E 3 .   ? -18.00900 -2.13300  -4.57900  1.000 43.79736  ? 472 HOH A O   1 
HETATM 4925 O O   . HOH E 3 .   ? -25.05400 -6.66300  -12.92800 1.000 43.74209  ? 473 HOH A O   1 
HETATM 4926 O O   . HOH E 3 .   ? -42.62200 3.07900   -21.94300 1.000 41.40496  ? 474 HOH A O   1 
HETATM 4927 O O   . HOH E 3 .   ? -18.10500 -3.08000  -15.97200 1.000 43.27098  ? 475 HOH A O   1 
HETATM 4928 O O   . HOH E 3 .   ? -31.10300 -3.38500  -33.01100 1.000 53.39061  ? 476 HOH A O   1 
HETATM 4929 O O   . HOH E 3 .   ? -12.91900 7.24600   -15.51400 1.000 45.26595  ? 477 HOH A O   1 
HETATM 4930 O O   . HOH E 3 .   ? -19.15800 -12.23000 3.65100   1.000 43.04463  ? 478 HOH A O   1 
HETATM 4931 O O   . HOH E 3 .   ? -31.60600 -11.44100 -8.11800  1.000 46.81351  ? 479 HOH A O   1 
HETATM 4932 O O   . HOH E 3 .   ? -42.00600 0.25400   21.70500  1.000 57.54111  ? 480 HOH A O   1 
HETATM 4933 O O   . HOH E 3 .   ? -22.79500 -11.10500 -3.69300  1.000 55.44612  ? 481 HOH A O   1 
HETATM 4934 O O   . HOH E 3 .   ? -27.64000 10.78600  -17.95800 1.000 40.82332  ? 482 HOH A O   1 
HETATM 4935 O O   . HOH E 3 .   ? -34.94000 3.62800   -9.46600  1.000 49.51120  ? 483 HOH A O   1 
HETATM 4936 O O   . HOH E 3 .   ? -10.03700 3.85500   -21.94700 1.000 51.39564  ? 484 HOH A O   1 
HETATM 4937 O O   . HOH E 3 .   ? -12.24700 5.52600   10.77100  1.000 57.46742  ? 485 HOH A O   1 
HETATM 4938 O O   . HOH E 3 .   ? -40.55100 -6.07200  -19.69700 1.000 47.76625  ? 486 HOH A O   1 
HETATM 4939 O O   . HOH E 3 .   ? -44.31100 -9.87300  16.30900  1.000 54.96712  ? 487 HOH A O   1 
HETATM 4940 O O   . HOH E 3 .   ? -43.16100 5.72000   -21.01500 1.000 38.79413  ? 488 HOH A O   1 
HETATM 4941 O O   . HOH E 3 .   ? -33.25300 11.85000  -23.19700 1.000 45.67127  ? 489 HOH A O   1 
HETATM 4942 O O   . HOH E 3 .   ? -39.11900 1.36700   -1.99000  1.000 50.89294  ? 490 HOH A O   1 
HETATM 4943 O O   . HOH E 3 .   ? -15.57300 -5.83800  -32.52200 1.000 60.10984  ? 491 HOH A O   1 
HETATM 4944 O O   . HOH E 3 .   ? -10.74400 2.95500   8.45500   1.000 50.21655  ? 492 HOH A O   1 
HETATM 4945 O O   . HOH E 3 .   ? -35.07700 -7.49200  13.16500  1.000 41.29442  ? 493 HOH A O   1 
HETATM 4946 O O   . HOH E 3 .   ? -33.77100 8.73200   -28.19600 1.000 45.00540  ? 494 HOH A O   1 
HETATM 4947 O O   . HOH E 3 .   ? -15.26300 -3.16100  -10.29500 1.000 44.15793  ? 495 HOH A O   1 
HETATM 4948 O O   . HOH E 3 .   ? -29.36300 6.52700   0.21300   1.000 45.32912  ? 496 HOH A O   1 
HETATM 4949 O O   . HOH E 3 .   ? -10.15700 10.33100  -18.45200 1.000 50.59554  ? 497 HOH A O   1 
HETATM 4950 O O   . HOH E 3 .   ? -29.79200 -17.05000 13.18900  1.000 66.60799  ? 498 HOH A O   1 
HETATM 4951 O O   . HOH E 3 .   ? -40.59400 5.58800   -29.65400 1.000 45.29754  ? 499 HOH A O   1 
HETATM 4952 O O   . HOH E 3 .   ? -17.25500 14.09300  -23.03900 1.000 68.32661  ? 500 HOH A O   1 
HETATM 4953 O O   . HOH E 3 .   ? -13.77400 -6.96100  -26.49100 1.000 52.47998  ? 501 HOH A O   1 
HETATM 4954 O O   . HOH E 3 .   ? -44.16900 -0.00100  15.20000  1.000 61.02311  ? 502 HOH A O   1 
HETATM 4955 O O   . HOH E 3 .   ? -25.85300 -10.33900 -19.66200 1.000 44.52376  ? 503 HOH A O   1 
HETATM 4956 O O   . HOH E 3 .   ? -35.36700 0.31500   -16.41500 1.000 34.09883  ? 504 HOH A O   1 
HETATM 4957 O O   . HOH E 3 .   ? -42.75900 3.76200   -29.35100 1.000 44.20004  ? 505 HOH A O   1 
HETATM 4958 O O   . HOH E 3 .   ? -28.42100 15.78800  10.39800  1.000 54.98554  ? 506 HOH A O   1 
HETATM 4959 O O   . HOH E 3 .   ? -41.09000 -4.08100  -21.41800 1.000 43.09990  ? 507 HOH A O   1 
HETATM 4960 O O   . HOH E 3 .   ? -27.06100 -8.32900  27.20900  1.000 66.94487  ? 508 HOH A O   1 
HETATM 4961 O O   . HOH E 3 .   ? -29.36500 -12.47400 -23.88900 1.000 53.61169  ? 509 HOH A O   1 
HETATM 4962 O O   . HOH E 3 .   ? -36.06800 -10.80700 -29.71700 1.000 63.34970  ? 510 HOH A O   1 
HETATM 4963 O O   . HOH E 3 .   ? -14.99400 -6.75100  12.01400  1.000 55.71721  ? 511 HOH A O   1 
HETATM 4964 O O   . HOH E 3 .   ? -21.06800 -11.34200 15.81800  1.000 59.03603  ? 512 HOH A O   1 
HETATM 4965 O O   . HOH E 3 .   ? -20.27800 2.92400   -8.28700  1.000 41.04176  ? 513 HOH A O   1 
HETATM 4966 O O   . HOH E 3 .   ? -32.65800 -14.39500 -5.51300  1.000 50.23760  ? 514 HOH A O   1 
HETATM 4967 O O   . HOH E 3 .   ? -42.26000 -6.62600  7.47600   1.000 49.60332  ? 515 HOH A O   1 
HETATM 4968 O O   . HOH E 3 .   ? -37.12600 11.55800  -25.63900 1.000 46.78192  ? 516 HOH A O   1 
HETATM 4969 O O   . HOH E 3 .   ? -26.88200 -11.51300 -24.21000 1.000 55.58561  ? 517 HOH A O   1 
HETATM 4970 O O   . HOH E 3 .   ? -22.70500 -16.97900 7.96400   1.000 52.00624  ? 518 HOH A O   1 
HETATM 4971 O O   . HOH E 3 .   ? -31.91000 6.16000   -11.91000 1.000 46.31871  ? 519 HOH A O   1 
HETATM 4972 O O   . HOH E 3 .   ? -43.42500 4.61200   11.63300  1.000 73.65620  ? 520 HOH A O   1 
HETATM 4973 O O   . HOH E 3 .   ? -37.87200 3.18100   27.89400  1.000 64.01557  ? 521 HOH A O   1 
HETATM 4974 O O   . HOH E 3 .   ? -34.53300 11.86800  8.13100   1.000 51.11139  ? 522 HOH A O   1 
HETATM 4975 O O   . HOH E 3 .   ? -34.86200 -16.85100 -1.70700  1.000 50.17970  ? 523 HOH A O   1 
HETATM 4976 O O   . HOH E 3 .   ? -39.66600 -5.88600  -31.09700 1.000 52.88792  ? 524 HOH A O   1 
HETATM 4977 O O   . HOH E 3 .   ? -11.79100 -5.07400  11.02800  1.000 58.48070  ? 525 HOH A O   1 
HETATM 4978 O O   . HOH E 3 .   ? -41.53800 -2.78100  -0.63000  1.000 48.39791  ? 526 HOH A O   1 
HETATM 4979 O O   . HOH E 3 .   ? -18.36500 -11.17700 -16.62500 1.000 34.62520  ? 527 HOH A O   1 
HETATM 4980 O O   . HOH E 3 .   ? -29.71200 7.92700   -11.61800 1.000 39.17575  ? 528 HOH A O   1 
HETATM 4981 O O   . HOH E 3 .   ? -40.23400 -10.55500 -18.28500 1.000 56.57257  ? 529 HOH A O   1 
HETATM 4982 O O   . HOH E 3 .   ? -12.39000 0.26800   -17.33400 1.000 50.57185  ? 530 HOH A O   1 
HETATM 4983 O O   . HOH E 3 .   ? -14.29400 8.47800   -17.75500 1.000 54.18281  ? 531 HOH A O   1 
HETATM 4984 O O   . HOH E 3 .   ? -46.97700 0.67300   -24.77000 1.000 54.09333  ? 532 HOH A O   1 
HETATM 4985 O O   . HOH E 3 .   ? -43.72700 3.73700   9.44800   1.000 61.73635  ? 533 HOH A O   1 
HETATM 4986 O O   . HOH E 3 .   ? -45.44300 0.55400   -31.79200 1.000 60.84414  ? 534 HOH A O   1 
HETATM 4987 O O   . HOH E 3 .   ? -37.16000 3.26000   30.05400  1.000 69.83732  ? 535 HOH A O   1 
HETATM 4988 O O   . HOH E 3 .   ? -44.17900 -0.48800  -24.17700 1.000 49.56384  ? 536 HOH A O   1 
HETATM 4989 O O   . HOH E 3 .   ? -41.98500 -11.71100 -24.08900 1.000 56.90682  ? 537 HOH A O   1 
HETATM 4990 O O   . HOH E 3 .   ? -41.82600 -1.34100  -14.38200 1.000 44.59745  ? 538 HOH A O   1 
HETATM 4991 O O   . HOH E 3 .   ? -19.49800 -9.54800  -14.37700 1.000 54.32230  ? 539 HOH A O   1 
HETATM 4992 O O   . HOH E 3 .   ? -43.65900 -9.11700  11.12600  1.000 54.19860  ? 540 HOH A O   1 
HETATM 4993 O O   . HOH E 3 .   ? -38.48500 6.13100   -13.23300 1.000 46.28976  ? 541 HOH A O   1 
HETATM 4994 O O   . HOH E 3 .   ? -43.86400 3.54200   -31.56400 1.000 57.45426  ? 542 HOH A O   1 
HETATM 4995 O O   . HOH E 3 .   ? -29.91000 7.56000   -4.55200  1.000 59.40975  ? 543 HOH A O   1 
HETATM 4996 O O   . HOH E 3 .   ? -31.77200 -12.46500 -17.79600 1.000 60.76255  ? 544 HOH A O   1 
HETATM 4997 O O   . HOH E 3 .   ? -36.98500 6.34600   5.57400   1.000 51.89306  ? 545 HOH A O   1 
HETATM 4998 O O   . HOH E 3 .   ? -40.63700 2.37200   -14.13800 1.000 39.89163  ? 546 HOH A O   1 
HETATM 4999 O O   . HOH E 3 .   ? -22.97800 -10.29500 -6.07000  1.000 50.23234  ? 547 HOH A O   1 
HETATM 5000 O O   . HOH E 3 .   ? -43.08200 11.16200  -25.51800 1.000 48.97429  ? 548 HOH A O   1 
HETATM 5001 O O   . HOH E 3 .   ? -42.98500 -4.92900  -1.60200  1.000 49.95862  ? 549 HOH A O   1 
HETATM 5002 O O   . HOH E 3 .   ? -34.34100 2.69500   -11.93700 1.000 46.67139  ? 550 HOH A O   1 
HETATM 5003 O O   . HOH E 3 .   ? -44.25900 -4.24400  -23.80900 1.000 49.98231  ? 551 HOH A O   1 
HETATM 5004 O O   . HOH E 3 .   ? -34.85500 13.54200  -15.43700 1.000 50.67976  ? 552 HOH A O   1 
HETATM 5005 O O   . HOH E 3 .   ? -44.37900 -0.89100  -21.52800 1.000 50.17444  ? 553 HOH A O   1 
HETATM 5006 O O   . HOH E 3 .   ? -38.14300 16.69500  -20.98000 1.000 58.38068  ? 554 HOH A O   1 
HETATM 5007 O O   . HOH E 3 .   ? -24.91000 -11.16700 -22.31300 1.000 69.41885  ? 555 HOH A O   1 
HETATM 5008 O O   . HOH E 3 .   ? -43.54800 -3.50200  -21.85500 1.000 44.60008  ? 556 HOH A O   1 
HETATM 5009 O O   . HOH E 3 .   ? -40.52800 7.20700   -27.90200 1.000 45.23437  ? 557 HOH A O   1 
HETATM 5010 O O   . HOH E 3 .   ? -43.11300 7.42800   -26.73400 1.000 47.12144  ? 558 HOH A O   1 
HETATM 5011 O O   . HOH E 3 .   ? -46.25400 -2.54500  -27.75300 1.000 55.46454  ? 559 HOH A O   1 
HETATM 5012 O O   . HOH E 3 .   ? -34.15800 9.15800   -30.70400 1.000 48.45581  ? 560 HOH A O   1 
HETATM 5013 O O   . HOH E 3 .   ? -44.35100 1.55500   -20.60100 1.000 48.45055  ? 561 HOH A O   1 
HETATM 5014 O O   . HOH E 3 .   ? -42.42700 -6.82100  -18.91400 1.000 55.20136  ? 562 HOH A O   1 
HETATM 5015 O O   . HOH E 3 .   ? -39.63700 6.92600   -31.88700 1.000 56.46203  ? 563 HOH A O   1 
HETATM 5016 O O   . HOH E 3 .   ? -41.80800 -2.54400  -7.66500  1.000 47.87942  ? 564 HOH A O   1 
HETATM 5017 O O   . HOH E 3 .   ? -16.79400 -4.83500  -8.37000  1.000 47.41884  ? 565 HOH A O   1 
HETATM 5018 O O   . HOH E 3 .   ? -44.70800 -6.75400  7.72100   1.000 60.87572  ? 566 HOH A O   1 
HETATM 5019 O O   . HOH E 3 .   ? -26.37300 -11.68100 -17.25400 1.000 52.75633  ? 567 HOH A O   1 
HETATM 5020 O O   . HOH E 3 .   ? -36.59000 9.25400   -27.28500 1.000 45.99762  ? 568 HOH A O   1 
HETATM 5021 O O   . HOH E 3 .   ? -38.92400 17.56900  -18.69900 1.000 58.70178  ? 569 HOH A O   1 
HETATM 5022 O O   . HOH E 3 .   ? -30.52000 -15.00300 -23.37000 1.000 60.54673  ? 570 HOH A O   1 
HETATM 5023 O O   . HOH E 3 .   ? -29.88000 -11.71500 -21.24900 1.000 50.56396  ? 571 HOH A O   1 
HETATM 5024 O O   . HOH E 3 .   ? -43.43000 -6.05900  -3.75200  1.000 56.35413  ? 572 HOH A O   1 
HETATM 5025 O O   . HOH E 3 .   ? -43.81000 -3.27300  -14.52900 1.000 52.67737  ? 573 HOH A O   1 
HETATM 5026 O O   . HOH E 3 .   ? -44.33700 -4.81300  -16.83000 1.000 51.25351  ? 574 HOH A O   1 
HETATM 5027 O O   . HOH E 3 .   ? -42.84000 2.28300   -12.95700 1.000 46.12132  ? 575 HOH A O   1 
HETATM 5028 O O   . HOH E 3 .   ? -37.67200 10.05200  -29.87600 1.000 58.72809  ? 576 HOH A O   1 
HETATM 5029 O O   . HOH F 3 .   ? -8.87900  16.38600  2.68400   1.000 50.14549  ? 401 HOH B O   1 
HETATM 5030 O O   . HOH F 3 .   ? -15.93400 -19.19700 5.45300   1.000 61.89163  ? 402 HOH B O   1 
HETATM 5031 O O   . HOH F 3 .   ? 14.11700  24.17300  -3.20400  1.000 55.84880  ? 403 HOH B O   1 
HETATM 5032 O O   . HOH F 3 .   ? 9.17500   30.39900  1.65600   1.000 66.98172  ? 404 HOH B O   1 
HETATM 5033 O O   . HOH F 3 .   ? -9.91500  14.26800  3.76400   1.000 53.09847  ? 405 HOH B O   1 
HETATM 5034 O O   . HOH F 3 .   ? -12.10300 -30.32600 -9.52500  1.000 50.24550  ? 406 HOH B O   1 
HETATM 5035 O O   . HOH F 3 .   ? -10.05100 -5.54700  -8.23000  1.000 43.13675  ? 407 HOH B O   1 
HETATM 5036 O O   . HOH F 3 .   ? 0.19100   26.05700  2.41400   1.000 66.11845  ? 408 HOH B O   1 
HETATM 5037 O O   . HOH F 3 .   ? -9.17300  -16.65000 -18.18400 1.000 41.99188  ? 409 HOH B O   1 
HETATM 5038 O O   . HOH F 3 .   ? 7.77100   21.57300  -16.40100 1.000 71.60332  ? 410 HOH B O   1 
HETATM 5039 O O   . HOH F 3 .   ? -11.98600 -5.67100  3.77400   1.000 48.37422  ? 411 HOH B O   1 
HETATM 5040 O O   . HOH F 3 .   ? 10.79700  1.72000   -10.14500 1.000 47.58728  ? 412 HOH B O   1 
HETATM 5041 O O   . HOH F 3 .   ? -1.54200  24.09200  -14.33700 1.000 69.12145  ? 413 HOH B O   1 
HETATM 5042 O O   . HOH F 3 .   ? -15.86200 -10.90900 -10.81800 1.000 50.14285  ? 414 HOH B O   1 
HETATM 5043 O O   . HOH F 3 .   ? -8.31500  1.11700   -16.11200 1.000 42.49457  ? 415 HOH B O   1 
HETATM 5044 O O   . HOH F 3 .   ? -19.78700 -26.10200 -1.78500  1.000 50.55080  ? 416 HOH B O   1 
HETATM 5045 O O   . HOH F 3 .   ? 5.79700   -18.46300 -5.64400  1.000 57.62270  ? 417 HOH B O   1 
HETATM 5046 O O   . HOH F 3 .   ? 2.53300   1.48600   -11.99600 1.000 34.06724  ? 418 HOH B O   1 
HETATM 5047 O O   . HOH F 3 .   ? 5.96400   -7.47700  -15.85200 1.000 45.79233  ? 419 HOH B O   1 
HETATM 5048 O O   . HOH F 3 .   ? 1.57900   20.84600  -14.58500 1.000 65.58155  ? 420 HOH B O   1 
HETATM 5049 O O   . HOH F 3 .   ? -11.96800 8.55800   -9.60100  1.000 41.25495  ? 421 HOH B O   1 
HETATM 5050 O O   . HOH F 3 .   ? 8.76700   4.52100   -19.21900 1.000 42.93146  ? 422 HOH B O   1 
HETATM 5051 O O   . HOH F 3 .   ? -3.98800  23.32200  -2.21700  1.000 57.43583  ? 423 HOH B O   1 
HETATM 5052 O O   . HOH F 3 .   ? -17.87200 -4.28200  -5.12500  1.000 50.51922  ? 424 HOH B O   1 
HETATM 5053 O O   . HOH F 3 .   ? -6.54500  -5.99000  -0.37100  1.000 40.29167  ? 425 HOH B O   1 
HETATM 5054 O O   . HOH F 3 .   ? -9.19700  22.93700  -6.31500  1.000 78.05936  ? 426 HOH B O   1 
HETATM 5055 O O   . HOH F 3 .   ? 2.75900   -32.23100 -9.59800  1.000 59.55977  ? 427 HOH B O   1 
HETATM 5056 O O   . HOH F 3 .   ? 5.18400   -9.46600  -12.87000 1.000 46.34503  ? 428 HOH B O   1 
HETATM 5057 O O   . HOH F 3 .   ? 11.01400  1.60400   -3.38300  1.000 49.87966  ? 429 HOH B O   1 
HETATM 5058 O O   . HOH F 3 .   ? -16.70800 9.18900   4.80000   1.000 47.62413  ? 430 HOH B O   1 
HETATM 5059 O O   . HOH F 3 .   ? 4.86300   2.31600   -0.09300  1.000 44.29742  ? 431 HOH B O   1 
HETATM 5060 O O   . HOH F 3 .   ? 6.48300   20.38600  12.11000  1.000 62.24167  ? 432 HOH B O   1 
HETATM 5061 O O   . HOH F 3 .   ? -8.17500  -10.15400 -15.05000 1.000 46.31871  ? 433 HOH B O   1 
HETATM 5062 O O   . HOH F 3 .   ? -13.75800 14.85100  -4.19900  1.000 51.44564  ? 434 HOH B O   1 
HETATM 5063 O O   . HOH F 3 .   ? 10.64800  5.74700   -12.95800 1.000 46.70560  ? 435 HOH B O   1 
HETATM 5064 O O   . HOH F 3 .   ? -4.00500  -5.63200  -17.96300 1.000 48.75848  ? 436 HOH B O   1 
HETATM 5065 O O   . HOH F 3 .   ? -20.14100 -14.50700 2.11000   1.000 48.45318  ? 437 HOH B O   1 
HETATM 5066 O O   . HOH F 3 .   ? -12.26200 -9.72700  0.58900   1.000 46.38714  ? 438 HOH B O   1 
HETATM 5067 O O   . HOH F 3 .   ? 4.54900   -3.11600  -18.07700 1.000 37.95718  ? 439 HOH B O   1 
HETATM 5068 O O   . HOH F 3 .   ? 8.93300   8.09300   1.69400   1.000 54.38810  ? 440 HOH B O   1 
HETATM 5069 O O   . HOH F 3 .   ? -6.26200  8.68900   -1.41400  1.000 41.63131  ? 441 HOH B O   1 
HETATM 5070 O O   . HOH F 3 .   ? 10.93800  17.58400  3.35400   1.000 53.51431  ? 442 HOH B O   1 
HETATM 5071 O O   . HOH F 3 .   ? -1.71200  -13.25400 -5.28300  1.000 41.02597  ? 443 HOH B O   1 
HETATM 5072 O O   . HOH F 3 .   ? -20.72700 -17.95300 -19.38500 1.000 58.97812  ? 444 HOH B O   1 
HETATM 5073 O O   . HOH F 3 .   ? -23.07900 -17.58400 4.93300   1.000 57.37004  ? 445 HOH B O   1 
HETATM 5074 O O   . HOH F 3 .   ? 6.84100   -4.96900  -6.81400  1.000 45.46335  ? 446 HOH B O   1 
HETATM 5075 O O   . HOH F 3 .   ? -6.05100  -3.84700  -11.22800 1.000 41.37865  ? 447 HOH B O   1 
HETATM 5076 O O   . HOH F 3 .   ? -14.03800 -2.49400  -4.84500  1.000 40.28641  ? 448 HOH B O   1 
HETATM 5077 O O   . HOH F 3 .   ? -5.57700  -20.50400 1.60300   1.000 51.65883  ? 449 HOH B O   1 
HETATM 5078 O O   . HOH F 3 .   ? 9.17100   7.56500   -22.68100 1.000 39.12311  ? 450 HOH B O   1 
HETATM 5079 O O   . HOH F 3 .   ? 2.89400   -19.63600 -17.76800 1.000 53.45115  ? 451 HOH B O   1 
HETATM 5080 O O   . HOH F 3 .   ? -9.41500  -13.84700 -8.07400  1.000 36.85968  ? 452 HOH B O   1 
HETATM 5081 O O   . HOH F 3 .   ? -4.81400  -9.02300  -17.80900 1.000 48.15841  ? 453 HOH B O   1 
HETATM 5082 O O   . HOH F 3 .   ? -4.65200  -9.54700  -0.16500  1.000 45.35807  ? 454 HOH B O   1 
HETATM 5083 O O   . HOH F 3 .   ? -5.81300  6.77600   -21.61900 1.000 54.30651  ? 455 HOH B O   1 
HETATM 5084 O O   . HOH F 3 .   ? 12.04700  13.67000  -16.25800 1.000 47.26093  ? 456 HOH B O   1 
HETATM 5085 O O   . HOH F 3 .   ? 5.52000   11.46600  8.12200   1.000 52.39576  ? 457 HOH B O   1 
HETATM 5086 O O   . HOH F 3 .   ? -2.51600  -3.28800  -18.10500 1.000 39.91531  ? 458 HOH B O   1 
HETATM 5087 O O   . HOH F 3 .   ? -10.43000 0.23300   -15.25500 1.000 47.78204  ? 459 HOH B O   1 
HETATM 5088 O O   . HOH F 3 .   ? -6.97800  17.38900  -7.32000  1.000 44.06581  ? 460 HOH B O   1 
HETATM 5089 O O   . HOH F 3 .   ? -9.62800  -7.86000  -3.48600  1.000 40.03112  ? 461 HOH B O   1 
HETATM 5090 O O   . HOH F 3 .   ? -7.87600  -14.06300 -17.95200 1.000 48.49792  ? 462 HOH B O   1 
HETATM 5091 O O   . HOH F 3 .   ? -9.93200  -12.70600 -16.69000 1.000 48.66899  ? 463 HOH B O   1 
HETATM 5092 O O   . HOH F 3 .   ? -17.08900 -19.14300 -21.30600 1.000 57.01210  ? 464 HOH B O   1 
HETATM 5093 O O   . HOH F 3 .   ? -23.05900 -17.27400 -10.53900 1.000 48.23210  ? 465 HOH B O   1 
HETATM 5094 O O   . HOH F 3 .   ? -17.03500 -12.95200 -8.93800  1.000 43.36573  ? 466 HOH B O   1 
HETATM 5095 O O   . HOH F 3 .   ? -6.39300  -16.77600 -21.99400 1.000 49.88493  ? 467 HOH B O   1 
HETATM 5096 O O   . HOH F 3 .   ? 4.49900   -17.26900 -11.15900 1.000 54.01437  ? 468 HOH B O   1 
HETATM 5097 O O   . HOH F 3 .   ? 5.09500   12.79700  -10.07900 1.000 35.97010  ? 469 HOH B O   1 
HETATM 5098 O O   . HOH F 3 .   ? 12.76000  21.36600  -16.12100 1.000 57.97800  ? 470 HOH B O   1 
HETATM 5099 O O   . HOH F 3 .   ? 10.44000  11.82900  -15.16900 1.000 40.64961  ? 471 HOH B O   1 
HETATM 5100 O O   . HOH F 3 .   ? 8.64600   19.60500  -21.48500 1.000 65.83421  ? 472 HOH B O   1 
HETATM 5101 O O   . HOH F 3 .   ? 14.18000  12.32900  -7.31100  1.000 46.20817  ? 473 HOH B O   1 
HETATM 5102 O O   . HOH F 3 .   ? 10.28900  8.82500   -13.26100 1.000 41.00755  ? 474 HOH B O   1 
HETATM 5103 O O   . HOH F 3 .   ? 10.74900  5.10800   -10.25900 1.000 41.85502  ? 475 HOH B O   1 
HETATM 5104 O O   . HOH F 3 .   ? 15.54300  15.83400  -12.01500 1.000 53.13005  ? 476 HOH B O   1 
HETATM 5105 O O   . HOH F 3 .   ? 15.35400  17.18700  -2.56700  1.000 47.86363  ? 477 HOH B O   1 
HETATM 5106 O O   . HOH F 3 .   ? -0.07600  -17.43200 -9.89600  1.000 43.59733  ? 478 HOH B O   1 
HETATM 5107 O O   . HOH F 3 .   ? 8.71700   -2.64800  -11.19500 1.000 45.27911  ? 479 HOH B O   1 
HETATM 5108 O O   . HOH F 3 .   ? -11.91100 -15.53600 -18.37700 1.000 44.81327  ? 480 HOH B O   1 
HETATM 5109 O O   . HOH F 3 .   ? 1.37700   25.31800  -12.74900 1.000 71.73228  ? 481 HOH B O   1 
HETATM 5110 O O   . HOH F 3 .   ? 11.28900  26.34800  -14.14000 1.000 59.89929  ? 482 HOH B O   1 
HETATM 5111 O O   . HOH F 3 .   ? 3.17100   17.20000  -22.08300 1.000 58.24909  ? 483 HOH B O   1 
HETATM 5112 O O   . HOH F 3 .   ? 3.80000   19.98200  -21.87800 1.000 71.25065  ? 484 HOH B O   1 
HETATM 5113 O O   . HOH F 3 .   ? -10.36000 -10.23200 -13.32400 1.000 49.35592  ? 485 HOH B O   1 
HETATM 5114 O O   . HOH F 3 .   ? 3.32000   23.83200  -11.02700 1.000 58.12802  ? 486 HOH B O   1 
HETATM 5115 O O   . HOH F 3 .   ? -9.63400  -33.17500 -3.68000  1.000 51.59829  ? 487 HOH B O   1 
HETATM 5116 O O   . HOH F 3 .   ? -4.73700  -28.11000 2.53000   1.000 62.01007  ? 488 HOH B O   1 
HETATM 5117 O O   . HOH F 3 .   ? -0.60200  1.47800   -22.38800 1.000 34.94103  ? 489 HOH B O   1 
HETATM 5118 O O   . HOH F 3 .   ? -9.11200  -31.30400 -16.43000 1.000 56.64627  ? 490 HOH B O   1 
HETATM 5119 O O   . HOH F 3 .   ? 7.27800   2.60100   6.73200   1.000 50.64028  ? 491 HOH B O   1 
HETATM 5120 O O   . HOH F 3 .   ? -2.69500  -7.96500  -0.95400  1.000 42.97884  ? 492 HOH B O   1 
HETATM 5121 O O   . HOH F 3 .   ? 7.54800   10.69500  -26.43300 1.000 50.59817  ? 493 HOH B O   1 
HETATM 5122 O O   . HOH F 3 .   ? 1.27800   29.28800  -3.16100  1.000 65.48680  ? 494 HOH B O   1 
HETATM 5123 O O   . HOH F 3 .   ? 6.89400   2.34900   -22.47000 1.000 44.53429  ? 495 HOH B O   1 
HETATM 5124 O O   . HOH F 3 .   ? -0.43900  -2.54800  1.40000   1.000 43.38941  ? 496 HOH B O   1 
HETATM 5125 O O   . HOH F 3 .   ? -13.63000 18.04800  -5.23500  1.000 53.90120  ? 497 HOH B O   1 
HETATM 5126 O O   . HOH F 3 .   ? -2.64300  -30.52100 -4.33000  1.000 50.84557  ? 498 HOH B O   1 
HETATM 5127 O O   . HOH F 3 .   ? -2.08900  16.45800  -17.87800 1.000 58.69651  ? 499 HOH B O   1 
HETATM 5128 O O   . HOH F 3 .   ? -0.84500  -30.81000 -19.78600 1.000 68.67402  ? 500 HOH B O   1 
HETATM 5129 O O   . HOH F 3 .   ? 7.75600   -21.97900 -4.90900  1.000 53.15901  ? 501 HOH B O   1 
HETATM 5130 O O   . HOH F 3 .   ? -6.87000  11.86500  -17.78400 1.000 44.32374  ? 502 HOH B O   1 
HETATM 5131 O O   . HOH F 3 .   ? 3.86400   -34.57400 -14.95400 1.000 66.04213  ? 503 HOH B O   1 
HETATM 5132 O O   . HOH F 3 .   ? 0.49300   27.59700  -5.29000  1.000 60.61779  ? 504 HOH B O   1 
HETATM 5133 O O   . HOH F 3 .   ? 1.43000   -29.53800 -1.73700  1.000 58.96496  ? 505 HOH B O   1 
HETATM 5134 O O   . HOH F 3 .   ? 7.96000   -3.26600  1.70900   1.000 45.09751  ? 506 HOH B O   1 
HETATM 5135 O O   . HOH F 3 .   ? -9.74100  -19.74000 -21.91900 1.000 53.72486  ? 507 HOH B O   1 
HETATM 5136 O O   . HOH F 3 .   ? -2.19200  18.39700  16.05400  1.000 64.94200  ? 508 HOH B O   1 
HETATM 5137 O O   . HOH F 3 .   ? 2.86200   -7.93500  -1.55900  1.000 48.04787  ? 509 HOH B O   1 
HETATM 5138 O O   . HOH F 3 .   ? -3.14100  -2.43500  -20.41800 1.000 44.78695  ? 510 HOH B O   1 
HETATM 5139 O O   . HOH F 3 .   ? -2.85900  -13.96300 -0.22600  1.000 44.67641  ? 511 HOH B O   1 
HETATM 5140 O O   . HOH F 3 .   ? 13.78000  14.81900  -13.55800 1.000 50.70608  ? 512 HOH B O   1 
HETATM 5141 O O   . HOH F 3 .   ? -24.31200 -20.94900 -13.57900 1.000 52.15362  ? 513 HOH B O   1 
HETATM 5142 O O   . HOH F 3 .   ? -4.39400  -27.05300 -23.19300 1.000 66.77906  ? 514 HOH B O   1 
HETATM 5143 O O   . HOH F 3 .   ? 13.53700  22.98000  2.45600   1.000 58.99918  ? 515 HOH B O   1 
HETATM 5144 O O   . HOH F 3 .   ? -0.88300  21.19200  -15.63700 1.000 68.44242  ? 516 HOH B O   1 
HETATM 5145 O O   . HOH F 3 .   ? 4.08800   -11.38800 -11.26700 1.000 56.40413  ? 517 HOH B O   1 
HETATM 5146 O O   . HOH F 3 .   ? -9.83500  12.98700  -16.97400 1.000 47.93996  ? 518 HOH B O   1 
HETATM 5147 O O   . HOH F 3 .   ? -12.01900 -7.90700  -1.85200  1.000 40.49696  ? 519 HOH B O   1 
HETATM 5148 O O   . HOH F 3 .   ? 8.30500   -5.61100  0.41800   1.000 55.75669  ? 520 HOH B O   1 
HETATM 5149 O O   . HOH F 3 .   ? -18.60400 -19.26900 5.52600   1.000 66.57377  ? 521 HOH B O   1 
HETATM 5150 O O   . HOH F 3 .   ? -16.09400 -21.46500 7.68600   1.000 73.98782  ? 522 HOH B O   1 
HETATM 5151 O O   . HOH F 3 .   ? -16.24800 -9.93200  -14.94000 1.000 56.45414  ? 523 HOH B O   1 
HETATM 5152 O O   . HOH F 3 .   ? 12.27400  19.40600  4.69000   1.000 66.13688  ? 524 HOH B O   1 
HETATM 5153 O O   . HOH F 3 .   ? -18.61300 -6.07100  -6.50600  1.000 42.89462  ? 525 HOH B O   1 
HETATM 5154 O O   . HOH F 3 .   ? -18.30400 -7.71900  -7.31600  1.000 52.05624  ? 526 HOH B O   1 
HETATM 5155 O O   . HOH F 3 .   ? 11.00800  -1.42500  -10.27700 1.000 54.72498  ? 527 HOH B O   1 
HETATM 5156 O O   . HOH F 3 .   ? -8.10900  5.17600   -22.89800 1.000 55.90670  ? 528 HOH B O   1 
HETATM 5157 O O   . HOH F 3 .   ? 15.68700  21.85500  -4.18000  1.000 58.76494  ? 529 HOH B O   1 
HETATM 5158 O O   . HOH F 3 .   ? -0.85200  -7.40300  1.06000   1.000 60.86519  ? 530 HOH B O   1 
HETATM 5159 O O   . HOH F 3 .   ? -19.10500 -17.07400 2.65000   1.000 56.07514  ? 531 HOH B O   1 
HETATM 5160 O O   . HOH F 3 .   ? -25.41300 -15.66200 -10.52700 1.000 63.86292  ? 532 HOH B O   1 
HETATM 5161 O O   . HOH F 3 .   ? 9.34700   7.96100   4.38700   1.000 56.07251  ? 533 HOH B O   1 
HETATM 5162 O O   . HOH F 3 .   ? 3.27100   -31.02300 -7.23100  1.000 60.74413  ? 534 HOH B O   1 
HETATM 5163 O O   . HOH F 3 .   ? -1.23100  16.07000  17.23200  1.000 69.10039  ? 535 HOH B O   1 
HETATM 5164 O O   . HOH F 3 .   ? -11.42500 -2.36300  -14.72000 1.000 47.05564  ? 536 HOH B O   1 
HETATM 5165 O O   . HOH F 3 .   ? -13.66500 20.03200  2.68200   1.000 70.30317  ? 537 HOH B O   1 
HETATM 5166 O O   . HOH F 3 .   ? 6.90700   -18.01800 -11.54900 1.000 56.39624  ? 538 HOH B O   1 
HETATM 5167 O O   . HOH F 3 .   ? -10.72800 -12.93500 -19.04100 1.000 50.69029  ? 539 HOH B O   1 
HETATM 5168 O O   . HOH F 3 .   ? 16.01200  17.63800  -5.14800  1.000 56.25938  ? 540 HOH B O   1 
HETATM 5169 O O   . HOH F 3 .   ? -8.62200  -17.62100 -20.94100 1.000 51.90096  ? 541 HOH B O   1 
HETATM 5170 O O   . HOH G 3 .   ? -38.01400 -20.75000 2.22000   1.000 74.16416  ? 201 HOH C O   1 
HETATM 5171 O O   . HOH G 3 .   ? -32.99100 -20.47400 9.19500   1.000 56.55152  ? 202 HOH C O   1 
HETATM 5172 O O   . HOH G 3 .   ? -31.40200 -13.25200 16.52000  1.000 69.50833  ? 203 HOH C O   1 
HETATM 5173 O O   . HOH G 3 .   ? -31.73700 -18.58800 4.08300   1.000 57.40688  ? 204 HOH C O   1 
HETATM 5174 O O   . HOH G 3 .   ? -38.49600 -24.31700 2.30400   1.000 77.59615  ? 205 HOH C O   1 
HETATM 5175 O O   . HOH H 3 .   ? -2.06900  8.05900   -21.78000 1.000 45.24227  ? 201 HOH D O   1 
HETATM 5176 O O   . HOH H 3 .   ? -3.62400  16.12400  -16.58800 1.000 58.72283  ? 202 HOH D O   1 
HETATM 5177 O O   . HOH H 3 .   ? -0.32100  13.11900  -22.63700 1.000 50.40868  ? 203 HOH D O   1 
HETATM 5178 O O   . HOH H 3 .   ? 1.48900   18.09900  -13.57900 1.000 52.21152  ? 204 HOH D O   1 
HETATM 5179 O O   . HOH H 3 .   ? 5.22800   12.56400  -26.37500 1.000 68.63718  ? 205 HOH D O   1 
HETATM 5180 O O   . HOH H 3 .   ? -9.21800  23.07100  -8.84900  1.000 78.89893  ? 206 HOH D O   1 
HETATM 5181 O O   . HOH H 3 .   ? 2.77500   4.61100   -26.23400 1.000 57.88589  ? 207 HOH D O   1 
HETATM 5182 O O   . HOH H 3 .   ? -2.63400  19.50300  -14.45000 1.000 58.45438  ? 208 HOH D O   1 
HETATM 5183 O O   . HOH H 3 .   ? -1.96900  11.30500  -24.37400 1.000 58.21487  ? 209 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 1   ? 0.50780 0.47710 0.53140 0.01170  0.02910  0.03760  1   SER A N   
2    C CA  . SER A 1   ? 0.57030 0.54590 0.58040 0.01200  0.02940  0.03530  1   SER A CA  
3    C C   . SER A 1   ? 0.50820 0.47820 0.51140 0.01080  0.02640  0.02670  1   SER A C   
4    O O   . SER A 1   ? 0.44880 0.41160 0.45650 0.00960  0.02420  0.02280  1   SER A O   
5    C CB  . SER A 1   ? 0.54010 0.52460 0.54790 0.01230  0.03280  0.03790  1   SER A CB  
6    O OG  . SER A 1   ? 0.64640 0.63890 0.65900 0.01340  0.03580  0.04720  1   SER A OG  
7    N N   . GLY A 2   ? 0.49960 0.47390 0.49260 0.01080  0.02630  0.02400  2   GLY A N   
8    C CA  . GLY A 2   ? 0.49680 0.46660 0.48380 0.00960  0.02360  0.01710  2   GLY A CA  
9    C C   . GLY A 2   ? 0.50720 0.47570 0.48940 0.00960  0.02170  0.01570  2   GLY A C   
10   O O   . GLY A 2   ? 0.55180 0.52070 0.53730 0.01060  0.02200  0.01920  2   GLY A O   
11   N N   . PHE A 3   ? 0.48870 0.45610 0.46450 0.00860  0.01990  0.01100  3   PHE A N   
12   C CA  . PHE A 3   ? 0.51100 0.47810 0.48280 0.00850  0.01840  0.01000  3   PHE A CA  
13   C C   . PHE A 3   ? 0.51200 0.47520 0.48030 0.00680  0.01610  0.00530  3   PHE A C   
14   O O   . PHE A 3   ? 0.52950 0.49420 0.49530 0.00600  0.01610  0.00300  3   PHE A O   
15   C CB  . PHE A 3   ? 0.53090 0.50600 0.49810 0.00910  0.01940  0.01210  3   PHE A CB  
16   C CG  . PHE A 3   ? 0.53210 0.50780 0.49790 0.00950  0.01830  0.01270  3   PHE A CG  
17   C CD1 . PHE A 3   ? 0.57320 0.54760 0.54500 0.01110  0.01890  0.01630  3   PHE A CD1 
18   C CD2 . PHE A 3   ? 0.56150 0.53870 0.52170 0.00820  0.01680  0.00940  3   PHE A CD2 
19   C CE1 . PHE A 3   ? 0.61250 0.58770 0.58420 0.01180  0.01830  0.01650  3   PHE A CE1 
20   C CE2 . PHE A 3   ? 0.55130 0.52990 0.51100 0.00860  0.01600  0.01010  3   PHE A CE2 
21   C CZ  . PHE A 3   ? 0.55200 0.52970 0.51720 0.01060  0.01690  0.01350  3   PHE A CZ  
22   N N   . ARG A 4   ? 0.51120 0.47010 0.48020 0.00630  0.01430  0.00380  4   ARG A N   
23   C CA  . ARG A 4   ? 0.49410 0.45030 0.46050 0.00470  0.01200  0.00100  4   ARG A CA  
24   C C   . ARG A 4   ? 0.46320 0.42010 0.42600 0.00440  0.01110  0.00020  4   ARG A C   
25   O O   . ARG A 4   ? 0.46960 0.42680 0.43410 0.00560  0.01180  0.00070  4   ARG A O   
26   C CB  . ARG A 4   ? 0.50620 0.45830 0.47620 0.00410  0.01040  0.00000  4   ARG A CB  
27   C CG  . ARG A 4   ? 0.50420 0.45590 0.47960 0.00450  0.01150  0.00100  4   ARG A CG  
28   C CD  . ARG A 4   ? 0.56390 0.51650 0.53790 0.00390  0.01170  -0.00010 4   ARG A CD  
29   N NE  . ARG A 4   ? 0.56930 0.51990 0.54150 0.00250  0.00910  -0.00120 4   ARG A NE  
30   C CZ  . ARG A 4   ? 0.64290 0.59110 0.61850 0.00180  0.00690  -0.00110 4   ARG A CZ  
31   N NH1 . ARG A 4   ? 0.57290 0.52010 0.55450 0.00220  0.00710  -0.00060 4   ARG A NH1 
32   N NH2 . ARG A 4   ? 0.58450 0.53220 0.55790 0.00050  0.00430  -0.00060 4   ARG A NH2 
33   N N   . LYS A 5   ? 0.45750 0.41440 0.41720 0.00280  0.00960  -0.00080 5   LYS A N   
34   C CA  . LYS A 5   ? 0.48670 0.44500 0.44320 0.00240  0.00890  -0.00130 5   LYS A CA  
35   C C   . LYS A 5   ? 0.52640 0.48280 0.48370 0.00240  0.00770  -0.00280 5   LYS A C   
36   O O   . LYS A 5   ? 0.58310 0.53820 0.54070 0.00120  0.00570  -0.00300 5   LYS A O   
37   C CB  . LYS A 5   ? 0.53880 0.49820 0.49300 0.00040  0.00780  -0.00090 5   LYS A CB  
38   C CG  . LYS A 5   ? 0.62980 0.59340 0.58130 -0.00000 0.00820  -0.00040 5   LYS A CG  
39   C CD  . LYS A 5   ? 0.71540 0.67980 0.66750 -0.00200 0.00750  0.00010  5   LYS A CD  
40   C CE  . LYS A 5   ? 0.66250 0.63090 0.61430 -0.00170 0.00850  -0.00040 5   LYS A CE  
41   N NZ  . LYS A 5   ? 0.75970 0.72830 0.71360 -0.00400 0.00750  -0.00130 5   LYS A NZ  
42   N N   . MET A 6   ? 0.43910 0.39580 0.39800 0.00380  0.00880  -0.00410 6   MET A N   
43   C CA  . MET A 6   ? 0.51760 0.47260 0.47890 0.00390  0.00790  -0.00720 6   MET A CA  
44   C C   . MET A 6   ? 0.54880 0.50710 0.50640 0.00400  0.00800  -0.01020 6   MET A C   
45   O O   . MET A 6   ? 0.58370 0.54390 0.54190 0.00540  0.01000  -0.01040 6   MET A O   
46   C CB  . MET A 6   ? 0.51680 0.46920 0.48550 0.00560  0.00950  -0.00700 6   MET A CB  
47   C CG  . MET A 6   ? 0.58180 0.53180 0.55530 0.00540  0.00830  -0.01080 6   MET A CG  
48   S SD  . MET A 6   ? 0.71670 0.66300 0.70170 0.00670  0.01000  -0.00840 6   MET A SD  
49   C CE  . MET A 6   ? 0.63070 0.57780 0.62060 0.00940  0.01300  -0.00650 6   MET A CE  
50   N N   . ALA A 7   ? 0.49450 0.45480 0.44870 0.00250  0.00590  -0.01240 7   ALA A N   
51   C CA  . ALA A 7   ? 0.52320 0.48840 0.47310 0.00260  0.00630  -0.01600 7   ALA A CA  
52   C C   . ALA A 7   ? 0.61230 0.57620 0.56700 0.00370  0.00660  -0.02230 7   ALA A C   
53   O O   . ALA A 7   ? 0.50890 0.46820 0.47000 0.00370  0.00560  -0.02320 7   ALA A O   
54   C CB  . ALA A 7   ? 0.54130 0.51130 0.48480 0.00040  0.00380  -0.01480 7   ALA A CB  
55   N N   . PHE A 8   ? 0.53080 0.49880 0.48370 0.00470  0.00820  -0.02680 8   PHE A N   
56   C CA  . PHE A 8   ? 0.52390 0.49130 0.48160 0.00540  0.00830  -0.03470 8   PHE A CA  
57   C C   . PHE A 8   ? 0.54030 0.51120 0.49360 0.00310  0.00470  -0.03830 8   PHE A C   
58   O O   . PHE A 8   ? 0.52920 0.50520 0.47430 0.00130  0.00280  -0.03480 8   PHE A O   
59   C CB  . PHE A 8   ? 0.54920 0.52090 0.50690 0.00730  0.01140  -0.03990 8   PHE A CB  
60   C CG  . PHE A 8   ? 0.58080 0.54910 0.54590 0.00990  0.01450  -0.03700 8   PHE A CG  
61   C CD1 . PHE A 8   ? 0.60030 0.56270 0.57750 0.01180  0.01560  -0.03910 8   PHE A CD1 
62   C CD2 . PHE A 8   ? 0.58010 0.55200 0.54110 0.01040  0.01620  -0.03150 8   PHE A CD2 
63   C CE1 . PHE A 8   ? 0.65270 0.61320 0.63750 0.01430  0.01830  -0.03490 8   PHE A CE1 
64   C CE2 . PHE A 8   ? 0.56020 0.53050 0.52820 0.01280  0.01860  -0.02830 8   PHE A CE2 
65   C CZ  . PHE A 8   ? 0.63900 0.60390 0.61870 0.01490  0.01960  -0.02950 8   PHE A CZ  
66   N N   . PRO A 9   ? 0.56220 0.53060 0.52200 0.00290  0.00330  -0.04480 9   PRO A N   
67   C CA  . PRO A 9   ? 0.56100 0.53460 0.51630 0.00060  -0.00060 -0.04900 9   PRO A CA  
68   C C   . PRO A 9   ? 0.56160 0.54580 0.50650 0.00020  -0.00020 -0.05330 9   PRO A C   
69   O O   . PRO A 9   ? 0.57030 0.55640 0.51590 0.00200  0.00310  -0.05880 9   PRO A O   
70   C CB  . PRO A 9   ? 0.58720 0.55600 0.55380 0.00060  -0.00150 -0.05660 9   PRO A CB  
71   C CG  . PRO A 9   ? 0.58600 0.54540 0.56380 0.00270  0.00150  -0.05210 9   PRO A CG  
72   C CD  . PRO A 9   ? 0.53530 0.49700 0.50760 0.00470  0.00520  -0.04850 9   PRO A CD  
73   N N   . SER A 10  ? 0.58260 0.57450 0.51840 -0.00200 -0.00340 -0.05030 10  SER A N   
74   C CA  . SER A 10  ? 0.53490 0.53840 0.45950 -0.00250 -0.00270 -0.05070 10  SER A CA  
75   C C   . SER A 10  ? 0.58530 0.59830 0.50530 -0.00350 -0.00450 -0.06080 10  SER A C   
76   O O   . SER A 10  ? 0.55770 0.58250 0.46780 -0.00390 -0.00370 -0.06180 10  SER A O   
77   C CB  . SER A 10  ? 0.54340 0.55130 0.46130 -0.00440 -0.00500 -0.03990 10  SER A CB  
78   O OG  . SER A 10  ? 0.58930 0.59730 0.50860 -0.00630 -0.00990 -0.03820 10  SER A OG  
79   N N   . GLY A 11  ? 0.53620 0.54510 0.46360 -0.00400 -0.00690 -0.06860 11  GLY A N   
80   C CA  . GLY A 11  ? 0.56870 0.58770 0.49190 -0.00550 -0.00960 -0.07950 11  GLY A CA  
81   C C   . GLY A 11  ? 0.58720 0.61560 0.50420 -0.00410 -0.00590 -0.08860 11  GLY A C   
82   O O   . GLY A 11  ? 0.60740 0.65040 0.51300 -0.00560 -0.00740 -0.09210 11  GLY A O   
83   N N   . LYS A 12  ? 0.58250 0.60380 0.50770 -0.00120 -0.00090 -0.09280 12  LYS A N   
84   C CA  . LYS A 12  ? 0.65090 0.68040 0.57270 0.00060  0.00340  -0.10250 12  LYS A CA  
85   C C   . LYS A 12  ? 0.58150 0.62350 0.48940 0.00040  0.00550  -0.09560 12  LYS A C   
86   O O   . LYS A 12  ? 0.64080 0.69500 0.54170 0.00100  0.00800  -0.10370 12  LYS A O   
87   C CB  . LYS A 12  ? 0.65240 0.67090 0.58820 0.00400  0.00830  -0.10590 12  LYS A CB  
88   C CG  . LYS A 12  ? 0.70190 0.70920 0.65360 0.00430  0.00680  -0.11340 12  LYS A CG  
89   C CD  . LYS A 12  ? 0.75080 0.74820 0.71720 0.00780  0.01170  -0.11460 12  LYS A CD  
90   C CE  . LYS A 12  ? 0.85580 0.84360 0.83970 0.00800  0.01070  -0.12330 12  LYS A CE  
91   N NZ  . LYS A 12  ? 0.86650 0.84830 0.85350 0.00510  0.00570  -0.11780 12  LYS A NZ  
92   N N   . VAL A 13  ? 0.56570 0.60530 0.47020 -0.00040 0.00480  -0.08140 13  VAL A N   
93   C CA  . VAL A 13  ? 0.59230 0.64330 0.48570 -0.00090 0.00660  -0.07330 13  VAL A CA  
94   C C   . VAL A 13  ? 0.58840 0.65210 0.47030 -0.00400 0.00200  -0.06850 13  VAL A C   
95   O O   . VAL A 13  ? 0.58680 0.66560 0.45780 -0.00470 0.00350  -0.06660 13  VAL A O   
96   C CB  . VAL A 13  ? 0.56210 0.60380 0.45990 -0.00030 0.00820  -0.06090 13  VAL A CB  
97   C CG1 . VAL A 13  ? 0.57120 0.62400 0.46000 -0.00120 0.01010  -0.05200 13  VAL A CG1 
98   C CG2 . VAL A 13  ? 0.56960 0.60110 0.47850 0.00280  0.01230  -0.06480 13  VAL A CG2 
99   N N   . GLU A 14  ? 0.57800 0.63680 0.46250 -0.00590 -0.00340 -0.06580 14  GLU A N   
100  C CA  . GLU A 14  ? 0.55660 0.62780 0.43180 -0.00880 -0.00840 -0.06040 14  GLU A CA  
101  C C   . GLU A 14  ? 0.58320 0.67200 0.44790 -0.00950 -0.00870 -0.07070 14  GLU A C   
102  O O   . GLU A 14  ? 0.63310 0.73780 0.48640 -0.01120 -0.01020 -0.06470 14  GLU A O   
103  C CB  . GLU A 14  ? 0.57090 0.63440 0.45290 -0.01030 -0.01420 -0.05860 14  GLU A CB  
104  C CG  . GLU A 14  ? 0.50570 0.55310 0.39760 -0.00960 -0.01380 -0.04850 14  GLU A CG  
105  C CD  . GLU A 14  ? 0.60770 0.64730 0.50830 -0.01070 -0.01850 -0.04970 14  GLU A CD  
106  O OE1 . GLU A 14  ? 0.61570 0.66420 0.51260 -0.01280 -0.02360 -0.05070 14  GLU A OE1 
107  O OE2 . GLU A 14  ? 0.59190 0.61770 0.50270 -0.00940 -0.01700 -0.04930 14  GLU A OE2 
108  N N   . GLY A 15  ? 0.57360 0.66040 0.44260 -0.00830 -0.00710 -0.08630 15  GLY A N   
109  C CA  . GLY A 15  ? 0.64060 0.74360 0.50070 -0.00890 -0.00750 -0.09890 15  GLY A CA  
110  C C   . GLY A 15  ? 0.61930 0.73600 0.46970 -0.00750 -0.00170 -0.10040 15  GLY A C   
111  O O   . GLY A 15  ? 0.64820 0.78020 0.49020 -0.00780 -0.00110 -0.11190 15  GLY A O   
112  N N   . CYS A 16  ? 0.59270 0.70430 0.44480 -0.00610 0.00260  -0.08980 16  CYS A N   
113  C CA  . CYS A 16  ? 0.58730 0.71060 0.43240 -0.00460 0.00860  -0.08920 16  CYS A CA  
114  C C   . CYS A 16  ? 0.63190 0.76620 0.46760 -0.00660 0.00800  -0.07230 16  CYS A C   
115  O O   . CYS A 16  ? 0.59830 0.74510 0.42750 -0.00590 0.01300  -0.07010 16  CYS A O   
116  C CB  . CYS A 16  ? 0.55920 0.66880 0.41590 -0.00130 0.01430  -0.09010 16  CYS A CB  
117  S SG  . CYS A 16  ? 0.64310 0.74050 0.51350 0.00150  0.01610  -0.10820 16  CYS A SG  
118  N N   . MET A 17  ? 0.59600 0.72620 0.43240 -0.00890 0.00260  -0.06000 17  MET A N   
119  C CA  . MET A 17  ? 0.62370 0.76170 0.45520 -0.01060 0.00230  -0.04280 17  MET A CA  
120  C C   . MET A 17  ? 0.64980 0.81110 0.46710 -0.01290 -0.00030 -0.04040 17  MET A C   
121  O O   . MET A 17  ? 0.66010 0.82670 0.47370 -0.01430 -0.00560 -0.04600 17  MET A O   
122  C CB  . MET A 17  ? 0.58000 0.70320 0.42050 -0.01180 -0.00180 -0.03020 17  MET A CB  
123  C CG  . MET A 17  ? 0.57950 0.68190 0.43280 -0.00980 0.00050  -0.03150 17  MET A CG  
124  S SD  . MET A 17  ? 0.59260 0.69330 0.44880 -0.00730 0.00830  -0.03220 17  MET A SD  
125  C CE  . MET A 17  ? 0.56570 0.67850 0.41650 -0.00980 0.00870  -0.01450 17  MET A CE  
126  N N   . VAL A 18  ? 0.63700 0.81370 0.44650 -0.01330 0.00360  -0.03220 18  VAL A N   
127  C CA  . VAL A 18  ? 0.63030 0.83160 0.42590 -0.01550 0.00180  -0.02640 18  VAL A CA  
128  C C   . VAL A 18  ? 0.61620 0.82140 0.41310 -0.01710 0.00220  -0.00510 18  VAL A C   
129  O O   . VAL A 18  ? 0.60040 0.79020 0.40820 -0.01650 0.00440  0.00250  18  VAL A O   
130  C CB  . VAL A 18  ? 0.65670 0.87730 0.44060 -0.01440 0.00710  -0.03880 18  VAL A CB  
131  C CG1 . VAL A 18  ? 0.68110 0.89680 0.46620 -0.01290 0.00630  -0.06030 18  VAL A CG1 
132  C CG2 . VAL A 18  ? 0.63380 0.85300 0.42130 -0.01230 0.01530  -0.03660 18  VAL A CG2 
133  N N   . GLN A 19  ? 0.65580 0.88180 0.44240 -0.01940 -0.00060 0.00460  19  GLN A N   
134  C CA  . GLN A 19  ? 0.62310 0.85650 0.41110 -0.02130 -0.00030 0.02560  19  GLN A CA  
135  C C   . GLN A 19  ? 0.65340 0.90950 0.43010 -0.02130 0.00590  0.02650  19  GLN A C   
136  O O   . GLN A 19  ? 0.70180 0.97640 0.46490 -0.02110 0.00650  0.01540  19  GLN A O   
137  C CB  . GLN A 19  ? 0.66490 0.90730 0.45070 -0.02390 -0.00800 0.03810  19  GLN A CB  
138  C CG  . GLN A 19  ? 0.75850 1.00640 0.54960 -0.02590 -0.00860 0.06190  19  GLN A CG  
139  C CD  . GLN A 19  ? 0.80510 1.06000 0.59720 -0.02800 -0.01680 0.07490  19  GLN A CD  
140  O OE1 . GLN A 19  ? 0.82300 1.08410 0.60820 -0.02830 -0.02200 0.06640  19  GLN A OE1 
141  N NE2 . GLN A 19  ? 0.81240 1.06640 0.61460 -0.02950 -0.01790 0.09560  19  GLN A NE2 
142  N N   . VAL A 20  ? 0.63390 0.88870 0.41670 -0.02140 0.01080  0.03840  20  VAL A N   
143  C CA  . VAL A 20  ? 0.63700 0.91450 0.41040 -0.02160 0.01710  0.04220  20  VAL A CA  
144  C C   . VAL A 20  ? 0.65670 0.94360 0.43350 -0.02450 0.01610  0.06650  20  VAL A C   
145  O O   . VAL A 20  ? 0.63860 0.90820 0.43050 -0.02510 0.01550  0.07740  20  VAL A O   
146  C CB  . VAL A 20  ? 0.63000 0.89950 0.40920 -0.01900 0.02500  0.03370  20  VAL A CB  
147  C CG1 . VAL A 20  ? 0.59780 0.89400 0.36710 -0.01930 0.03230  0.03850  20  VAL A CG1 
148  C CG2 . VAL A 20  ? 0.65340 0.91040 0.43350 -0.01590 0.02610  0.01120  20  VAL A CG2 
149  N N   . THR A 21  ? 0.70740 1.02270 0.47110 -0.02610 0.01650  0.07470  21  THR A N   
150  C CA  . THR A 21  ? 0.73440 1.06170 0.50160 -0.02900 0.01560  0.09940  21  THR A CA  
151  C C   . THR A 21  ? 0.73630 1.09070 0.49340 -0.02950 0.02280  0.10570  21  THR A C   
152  O O   . THR A 21  ? 0.77140 1.14650 0.51170 -0.02860 0.02520  0.09400  21  THR A O   
153  C CB  . THR A 21  ? 0.76340 1.10080 0.52580 -0.03100 0.00720  0.10910  21  THR A CB  
154  O OG1 . THR A 21  ? 0.78000 1.09360 0.55120 -0.03020 0.00130  0.10110  21  THR A OG1 
155  C CG2 . THR A 21  ? 0.80650 1.15060 0.57830 -0.03370 0.00540  0.13630  21  THR A CG2 
156  N N   . CYS A 22  ? 0.71540 1.07020 0.48360 -0.03120 0.02600  0.12430  22  CYS A N   
157  C CA  . CYS A 22  ? 0.79540 1.17600 0.55750 -0.03230 0.03280  0.13540  22  CYS A CA  
158  C C   . CYS A 22  ? 0.81520 1.20260 0.58680 -0.03580 0.02990  0.16300  22  CYS A C   
159  O O   . CYS A 22  ? 0.77850 1.14560 0.56970 -0.03680 0.02910  0.17350  22  CYS A O   
160  C CB  . CYS A 22  ? 0.85570 1.22750 0.62650 -0.03090 0.04090  0.13020  22  CYS A CB  
161  S SG  . CYS A 22  ? 0.91750 1.28800 0.67800 -0.02660 0.04630  0.10070  22  CYS A SG  
162  N N   . GLY A 23  ? 0.79780 1.21320 0.55660 -0.03750 0.02780  0.17460  23  GLY A N   
163  C CA  . GLY A 23  ? 0.76380 1.18630 0.53300 -0.04060 0.02440  0.20220  23  GLY A CA  
164  C C   . GLY A 23  ? 0.79360 1.19140 0.57720 -0.04090 0.01590  0.20590  23  GLY A C   
165  O O   . GLY A 23  ? 0.80700 1.20180 0.58240 -0.03990 0.00990  0.19430  23  GLY A O   
166  N N   . THR A 24  ? 0.79990 1.17910 0.60610 -0.04240 0.01530  0.22040  24  THR A N   
167  C CA  . THR A 24  ? 0.75930 1.11360 0.58070 -0.04230 0.00800  0.22210  24  THR A CA  
168  C C   . THR A 24  ? 0.81910 1.14080 0.65150 -0.04030 0.00900  0.20460  24  THR A C   
169  O O   . THR A 24  ? 0.81670 1.11660 0.66220 -0.04000 0.00370  0.20460  24  THR A O   
170  C CB  . THR A 24  ? 0.80060 1.15400 0.64210 -0.04500 0.00530  0.24920  24  THR A CB  
171  O OG1 . THR A 24  ? 0.80810 1.15720 0.66370 -0.04650 0.01150  0.25810  24  THR A OG1 
172  C CG2 . THR A 24  ? 0.71990 1.10470 0.55180 -0.04690 0.00240  0.26830  24  THR A CG2 
173  N N   . THR A 25  ? 0.74450 1.06340 0.57180 -0.03880 0.01570  0.18990  25  THR A N   
174  C CA  . THR A 25  ? 0.73080 1.02150 0.56760 -0.03680 0.01680  0.17400  25  THR A CA  
175  C C   . THR A 25  ? 0.72240 1.00690 0.54630 -0.03390 0.01480  0.15120  25  THR A C   
176  O O   . THR A 25  ? 0.71800 1.01940 0.52480 -0.03270 0.01780  0.13980  25  THR A O   
177  C CB  . THR A 25  ? 0.73370 1.02500 0.57410 -0.03660 0.02480  0.17120  25  THR A CB  
178  O OG1 . THR A 25  ? 0.75320 1.05180 0.60640 -0.03970 0.02680  0.19300  25  THR A OG1 
179  C CG2 . THR A 25  ? 0.64330 0.90560 0.49480 -0.03470 0.02550  0.15620  25  THR A CG2 
180  N N   . THR A 26  ? 0.65320 0.91370 0.48610 -0.03290 0.01000  0.14390  26  THR A N   
181  C CA  . THR A 26  ? 0.64850 0.90150 0.47210 -0.03050 0.00790  0.12330  26  THR A CA  
182  C C   . THR A 26  ? 0.66680 0.89170 0.50250 -0.02860 0.00900  0.11180  26  THR A C   
183  O O   . THR A 26  ? 0.65970 0.86910 0.51130 -0.02960 0.00860  0.12040  26  THR A O   
184  C CB  . THR A 26  ? 0.72330 0.97950 0.54330 -0.03110 -0.00010 0.12620  26  THR A CB  
185  O OG1 . THR A 26  ? 0.75400 1.00880 0.56300 -0.02920 -0.00170 0.10610  26  THR A OG1 
186  C CG2 . THR A 26  ? 0.72130 0.95450 0.56000 -0.03150 -0.00490 0.13360  26  THR A CG2 
187  N N   . LEU A 27  ? 0.58220 0.80160 0.41070 -0.02610 0.01060  0.09230  27  LEU A N   
188  C CA  . LEU A 27  ? 0.60910 0.80380 0.44750 -0.02420 0.01090  0.08120  27  LEU A CA  
189  C C   . LEU A 27  ? 0.58060 0.77370 0.40960 -0.02180 0.01030  0.06170  27  LEU A C   
190  O O   . LEU A 27  ? 0.61600 0.82640 0.43190 -0.02190 0.00900  0.05730  27  LEU A O   
191  C CB  . LEU A 27  ? 0.57160 0.76100 0.41790 -0.02380 0.01700  0.08220  27  LEU A CB  
192  C CG  . LEU A 27  ? 0.56450 0.77250 0.40260 -0.02330 0.02390  0.08070  27  LEU A CG  
193  C CD1 . LEU A 27  ? 0.58210 0.79570 0.40790 -0.02040 0.02610  0.06130  27  LEU A CD1 
194  C CD2 . LEU A 27  ? 0.54440 0.74120 0.39560 -0.02320 0.02820  0.08300  27  LEU A CD2 
195  N N   . ASN A 28  ? 0.55660 0.73050 0.39250 -0.01960 0.01160  0.04980  28  ASN A N   
196  C CA  . ASN A 28  ? 0.54480 0.71430 0.37560 -0.01730 0.01100  0.03180  28  ASN A CA  
197  C C   . ASN A 28  ? 0.58550 0.76010 0.41220 -0.01490 0.01750  0.01940  28  ASN A C   
198  O O   . ASN A 28  ? 0.56410 0.73660 0.39640 -0.01430 0.02240  0.02300  28  ASN A O   
199  C CB  . ASN A 28  ? 0.59350 0.73910 0.43550 -0.01630 0.00800  0.02690  28  ASN A CB  
200  C CG  . ASN A 28  ? 0.58020 0.71930 0.42860 -0.01830 0.00200  0.03870  28  ASN A CG  
201  O OD1 . ASN A 28  ? 0.59390 0.73830 0.43750 -0.01900 -0.00290 0.03780  28  ASN A OD1 
202  N ND2 . ASN A 28  ? 0.51980 0.64750 0.37990 -0.01910 0.00230  0.04890  28  ASN A ND2 
203  N N   . GLY A 29  ? 0.55810 0.73870 0.37680 -0.01340 0.01750  0.00410  29  GLY A N   
204  C CA  . GLY A 29  ? 0.58370 0.76700 0.40090 -0.01050 0.02360  -0.01010 29  GLY A CA  
205  C C   . GLY A 29  ? 0.60370 0.77250 0.42560 -0.00830 0.02210  -0.02650 29  GLY A C   
206  O O   . GLY A 29  ? 0.59680 0.75720 0.42050 -0.00920 0.01630  -0.02830 29  GLY A O   
207  N N   . LEU A 30  ? 0.61190 0.77770 0.43780 -0.00530 0.02760  -0.03800 30  LEU A N   
208  C CA  . LEU A 30  ? 0.59010 0.74160 0.42370 -0.00270 0.02730  -0.05320 30  LEU A CA  
209  C C   . LEU A 30  ? 0.63300 0.79830 0.45990 -0.00090 0.03090  -0.06990 30  LEU A C   
210  O O   . LEU A 30  ? 0.57770 0.75420 0.40220 0.00080  0.03730  -0.07250 30  LEU A O   
211  C CB  . LEU A 30  ? 0.54070 0.67520 0.38800 -0.00040 0.03050  -0.05190 30  LEU A CB  
212  C CG  . LEU A 30  ? 0.54790 0.66670 0.40570 0.00230  0.03040  -0.06440 30  LEU A CG  
213  C CD1 . LEU A 30  ? 0.55200 0.65720 0.41360 0.00040  0.02380  -0.05980 30  LEU A CD1 
214  C CD2 . LEU A 30  ? 0.54890 0.65720 0.41860 0.00530  0.03500  -0.06450 30  LEU A CD2 
215  N N   . TRP A 31  ? 0.59360 0.75960 0.41770 -0.00150 0.02670  -0.08150 31  TRP A N   
216  C CA  . TRP A 31  ? 0.57950 0.76080 0.39580 -0.00060 0.02870  -0.09860 31  TRP A CA  
217  C C   . TRP A 31  ? 0.64510 0.81170 0.47460 0.00250  0.03060  -0.11560 31  TRP A C   
218  O O   . TRP A 31  ? 0.64780 0.79980 0.48540 0.00190  0.02580  -0.11950 31  TRP A O   
219  C CB  . TRP A 31  ? 0.59740 0.79130 0.40210 -0.00400 0.02210  -0.09950 31  TRP A CB  
220  C CG  . TRP A 31  ? 0.66220 0.87520 0.45660 -0.00390 0.02290  -0.11790 31  TRP A CG  
221  C CD1 . TRP A 31  ? 0.70530 0.93160 0.49570 -0.00130 0.03000  -0.13090 31  TRP A CD1 
222  C CD2 . TRP A 31  ? 0.70080 0.92240 0.48810 -0.00640 0.01620  -0.12600 31  TRP A CD2 
223  N NE1 . TRP A 31  ? 0.73710 0.97940 0.51810 -0.00230 0.02810  -0.14710 31  TRP A NE1 
224  C CE2 . TRP A 31  ? 0.73500 0.97470 0.51380 -0.00560 0.01940  -0.14430 31  TRP A CE2 
225  C CE3 . TRP A 31  ? 0.74260 0.95860 0.53050 -0.00940 0.00780  -0.11970 31  TRP A CE3 
226  C CZ2 . TRP A 31  ? 0.78800 1.04110 0.55820 -0.00790 0.01400  -0.15680 31  TRP A CZ2 
227  C CZ3 . TRP A 31  ? 0.73890 0.96800 0.51900 -0.01160 0.00230  -0.13130 31  TRP A CZ3 
228  C CH2 . TRP A 31  ? 0.78570 1.03300 0.55700 -0.01100 0.00530  -0.14990 31  TRP A CH2 
229  N N   . LEU A 32  ? 0.61200 0.78150 0.44590 0.00590  0.03790  -0.12400 32  LEU A N   
230  C CA  . LEU A 32  ? 0.65750 0.81410 0.50630 0.00940  0.04080  -0.13940 32  LEU A CA  
231  C C   . LEU A 32  ? 0.71480 0.88810 0.55900 0.01160  0.04620  -0.15720 32  LEU A C   
232  O O   . LEU A 32  ? 0.65870 0.84730 0.49610 0.01280  0.05220  -0.15530 32  LEU A O   
233  C CB  . LEU A 32  ? 0.61300 0.75390 0.47600 0.01220  0.04450  -0.13130 32  LEU A CB  
234  C CG  . LEU A 32  ? 0.57900 0.70380 0.44670 0.01030  0.03970  -0.11490 32  LEU A CG  
235  C CD1 . LEU A 32  ? 0.58920 0.70460 0.46780 0.01280  0.04380  -0.10660 32  LEU A CD1 
236  C CD2 . LEU A 32  ? 0.59930 0.70710 0.47600 0.00940  0.03370  -0.11850 32  LEU A CD2 
237  N N   . ASP A 33  ? 0.73730 0.90830 0.58620 0.01190  0.04440  -0.17510 33  ASP A N   
238  C CA  . ASP A 33  ? 0.72880 0.91660 0.57290 0.01350  0.04870  -0.19500 33  ASP A CA  
239  C C   . ASP A 33  ? 0.74120 0.95540 0.56260 0.01070  0.04840  -0.18890 33  ASP A C   
240  O O   . ASP A 33  ? 0.70780 0.92430 0.51980 0.00680  0.04160  -0.17750 33  ASP A O   
241  C CB  . ASP A 33  ? 0.77800 0.96120 0.63600 0.01860  0.05710  -0.20300 33  ASP A CB  
242  C CG  . ASP A 33  ? 0.81550 0.97240 0.69700 0.02110  0.05630  -0.20600 33  ASP A CG  
243  O OD1 . ASP A 33  ? 0.82140 0.96910 0.70910 0.01960  0.05120  -0.21510 33  ASP A OD1 
244  O OD2 . ASP A 33  ? 0.83600 0.98200 0.72990 0.02420  0.06040  -0.19840 33  ASP A OD2 
245  N N   . ASP A 34  ? 0.70450 0.93810 0.51780 0.01260  0.05570  -0.19310 34  ASP A N   
246  C CA  . ASP A 34  ? 0.75000 1.01090 0.54160 0.00990  0.05570  -0.18690 34  ASP A CA  
247  C C   . ASP A 34  ? 0.76380 1.03050 0.55070 0.00950  0.05910  -0.16510 34  ASP A C   
248  O O   . ASP A 34  ? 0.74580 1.03680 0.51810 0.00870  0.06280  -0.16130 34  ASP A O   
249  C CB  . ASP A 34  ? 0.80170 1.08600 0.58400 0.01150  0.06110  -0.20760 34  ASP A CB  
250  C CG  . ASP A 34  ? 0.85510 1.13980 0.64750 0.01650  0.07130  -0.21580 34  ASP A CG  
251  O OD1 . ASP A 34  ? 0.82620 1.09080 0.63490 0.01900  0.07350  -0.20730 34  ASP A OD1 
252  O OD2 . ASP A 34  ? 0.85790 1.16490 0.64140 0.01800  0.07710  -0.23010 34  ASP A OD2 
253  N N   . VAL A 35  ? 0.71310 0.95890 0.51210 0.00960  0.05770  -0.15040 35  VAL A N   
254  C CA  . VAL A 35  ? 0.66570 0.91420 0.46310 0.00880  0.06000  -0.12970 35  VAL A CA  
255  C C   . VAL A 35  ? 0.66120 0.89610 0.46000 0.00530  0.05240  -0.11150 35  VAL A C   
256  O O   . VAL A 35  ? 0.63300 0.84630 0.44270 0.00540  0.04770  -0.11300 35  VAL A O   
257  C CB  . VAL A 35  ? 0.67910 0.91610 0.49200 0.01280  0.06670  -0.12990 35  VAL A CB  
258  C CG1 . VAL A 35  ? 0.66400 0.90220 0.47700 0.01130  0.06810  -0.10860 35  VAL A CG1 
259  C CG2 . VAL A 35  ? 0.69330 0.94520 0.50600 0.01660  0.07510  -0.14700 35  VAL A CG2 
260  N N   . VAL A 36  ? 0.62690 0.87460 0.41610 0.00240  0.05160  -0.09380 36  VAL A N   
261  C CA  . VAL A 36  ? 0.61520 0.85070 0.40800 -0.00050 0.04570  -0.07500 36  VAL A CA  
262  C C   . VAL A 36  ? 0.63520 0.86540 0.43640 -0.00000 0.05010  -0.06110 36  VAL A C   
263  O O   . VAL A 36  ? 0.61040 0.85840 0.40580 -0.00010 0.05550  -0.05520 36  VAL A O   
264  C CB  . VAL A 36  ? 0.65900 0.91170 0.43750 -0.00450 0.04060  -0.06400 36  VAL A CB  
265  C CG1 . VAL A 36  ? 0.60200 0.84320 0.38650 -0.00710 0.03590  -0.04330 36  VAL A CG1 
266  C CG2 . VAL A 36  ? 0.66490 0.92110 0.43660 -0.00550 0.03460  -0.07740 36  VAL A CG2 
267  N N   . TYR A 37  ? 0.57230 0.77920 0.38710 0.00040  0.04780  -0.05580 37  TYR A N   
268  C CA  . TYR A 37  ? 0.51570 0.71550 0.34010 0.00060  0.05070  -0.04330 37  TYR A CA  
269  C C   . TYR A 37  ? 0.57970 0.77510 0.40470 -0.00330 0.04550  -0.02480 37  TYR A C   
270  O O   . TYR A 37  ? 0.58090 0.76400 0.40770 -0.00450 0.03920  -0.02350 37  TYR A O   
271  C CB  . TYR A 37  ? 0.56350 0.74170 0.40320 0.00360  0.05160  -0.04970 37  TYR A CB  
272  C CG  . TYR A 37  ? 0.59890 0.77790 0.44230 0.00770  0.05630  -0.06790 37  TYR A CG  
273  C CD1 . TYR A 37  ? 0.63170 0.80840 0.47290 0.00860  0.05380  -0.08290 37  TYR A CD1 
274  C CD2 . TYR A 37  ? 0.63460 0.81640 0.48550 0.01080  0.06320  -0.07050 37  TYR A CD2 
275  C CE1 . TYR A 37  ? 0.63020 0.80720 0.47710 0.01240  0.05830  -0.10050 37  TYR A CE1 
276  C CE2 . TYR A 37  ? 0.60820 0.79050 0.46490 0.01500  0.06790  -0.08740 37  TYR A CE2 
277  C CZ  . TYR A 37  ? 0.63970 0.81930 0.49450 0.01580  0.06550  -0.10250 37  TYR A CZ  
278  O OH  . TYR A 37  ? 0.62990 0.80940 0.49250 0.01990  0.07020  -0.11960 37  TYR A OH  
279  N N   . CYS A 38  ? 0.55190 0.75580 0.37760 -0.00500 0.04820  -0.01040 38  CYS A N   
280  C CA  . CYS A 38  ? 0.52690 0.72540 0.35590 -0.00860 0.04320  0.00680  38  CYS A CA  
281  C C   . CYS A 38  ? 0.54990 0.75020 0.38710 -0.00970 0.04700  0.01970  38  CYS A C   
282  O O   . CYS A 38  ? 0.54750 0.76030 0.38360 -0.00840 0.05360  0.01760  38  CYS A O   
283  C CB  . CYS A 38  ? 0.54980 0.76500 0.36660 -0.01140 0.03960  0.01400  38  CYS A CB  
284  S SG  . CYS A 38  ? 0.61030 0.85630 0.41580 -0.01280 0.04500  0.02320  38  CYS A SG  
285  N N   . PRO A 39  ? 0.52140 0.71100 0.36720 -0.01250 0.04310  0.03330  39  PRO A N   
286  C CA  . PRO A 39  ? 0.55700 0.74950 0.41170 -0.01430 0.04640  0.04580  39  PRO A CA  
287  C C   . PRO A 39  ? 0.57230 0.78950 0.41940 -0.01600 0.05040  0.05560  39  PRO A C   
288  O O   . PRO A 39  ? 0.55320 0.78340 0.39040 -0.01770 0.04810  0.06120  39  PRO A O   
289  C CB  . PRO A 39  ? 0.50390 0.68110 0.36870 -0.01710 0.04060  0.05730  39  PRO A CB  
290  C CG  . PRO A 39  ? 0.47660 0.63600 0.34110 -0.01540 0.03540  0.04640  39  PRO A CG  
291  C CD  . PRO A 39  ? 0.55560 0.72930 0.40560 -0.01390 0.03600  0.03670  39  PRO A CD  
292  N N   . ARG A 40  ? 0.56000 0.78540 0.41170 -0.01560 0.05670  0.05790  40  ARG A N   
293  C CA  . ARG A 40  ? 0.57590 0.82590 0.42110 -0.01730 0.06120  0.06800  40  ARG A CA  
294  C C   . ARG A 40  ? 0.58320 0.83630 0.43370 -0.02180 0.05790  0.08860  40  ARG A C   
295  O O   . ARG A 40  ? 0.63350 0.90870 0.47690 -0.02370 0.06040  0.09930  40  ARG A O   
296  C CB  . ARG A 40  ? 0.57350 0.83160 0.42440 -0.01580 0.06900  0.06630  40  ARG A CB  
297  C CG  . ARG A 40  ? 0.57240 0.81670 0.44130 -0.01760 0.06870  0.07500  40  ARG A CG  
298  C CD  . ARG A 40  ? 0.52010 0.77590 0.39430 -0.01610 0.07660  0.07340  40  ARG A CD  
299  N NE  . ARG A 40  ? 0.53950 0.78220 0.43120 -0.01790 0.07560  0.08020  40  ARG A NE  
300  C CZ  . ARG A 40  ? 0.56320 0.81420 0.46390 -0.01790 0.08120  0.08330  40  ARG A CZ  
301  N NH1 . ARG A 40  ? 0.54000 0.81160 0.43410 -0.01580 0.08860  0.08030  40  ARG A NH1 
302  N NH2 . ARG A 40  ? 0.54990 0.78890 0.46680 -0.02010 0.07920  0.08930  40  ARG A NH2 
303  N N   . ALA A 41  ? 0.58150 0.81390 0.44410 -0.02350 0.05230  0.09400  41  ALA A N   
304  C CA  . ALA A 41  ? 0.59240 0.82500 0.46290 -0.02760 0.04860  0.11260  41  ALA A CA  
305  C C   . ALA A 41  ? 0.59910 0.84640 0.45750 -0.02870 0.04540  0.11940  41  ALA A C   
306  O O   . ALA A 41  ? 0.62330 0.87710 0.48730 -0.03200 0.04350  0.13730  41  ALA A O   
307  C CB  . ALA A 41  ? 0.62700 0.83390 0.51120 -0.02840 0.04300  0.11280  41  ALA A CB  
308  N N   . VAL A 42  ? 0.48630 0.73940 0.32930 -0.02620 0.04460  0.10590  42  VAL A N   
309  C CA  . VAL A 42  ? 0.55540 0.82470 0.38570 -0.02730 0.04110  0.11140  42  VAL A CA  
310  C C   . VAL A 42  ? 0.68340 0.98190 0.50520 -0.02900 0.04570  0.12350  42  VAL A C   
311  O O   . VAL A 42  ? 0.64030 0.95400 0.45550 -0.03100 0.04250  0.13520  42  VAL A O   
312  C CB  . VAL A 42  ? 0.60660 0.87560 0.42340 -0.02440 0.03910  0.09200  42  VAL A CB  
313  C CG1 . VAL A 42  ? 0.60510 0.88910 0.41100 -0.02180 0.04610  0.07820  42  VAL A CG1 
314  C CG2 . VAL A 42  ? 0.66630 0.94620 0.47320 -0.02600 0.03300  0.09730  42  VAL A CG2 
315  N N   . ILE A 43  ? 0.65930 0.96810 0.48120 -0.02810 0.05340  0.12130  43  ILE A N   
316  C CA  . ILE A 43  ? 0.70380 1.04200 0.51810 -0.02980 0.05850  0.13400  43  ILE A CA  
317  C C   . ILE A 43  ? 0.71840 1.05810 0.54830 -0.03380 0.05890  0.15750  43  ILE A C   
318  O O   . ILE A 43  ? 0.70410 1.06830 0.52990 -0.03560 0.06320  0.17110  43  ILE A O   
319  C CB  . ILE A 43  ? 0.63420 0.98750 0.44110 -0.02720 0.06750  0.12250  43  ILE A CB  
320  C CG1 . ILE A 43  ? 0.63580 0.97440 0.45970 -0.02670 0.07160  0.12150  43  ILE A CG1 
321  C CG2 . ILE A 43  ? 0.67830 1.03460 0.47000 -0.02350 0.06790  0.09980  43  ILE A CG2 
322  C CD1 . ILE A 43  ? 0.69840 1.05400 0.51690 -0.02390 0.08120  0.11150  43  ILE A CD1 
323  N N   . CYS A 44  ? 0.70140 1.01650 0.54940 -0.03520 0.05470  0.16260  44  CYS A N   
324  C CA  . CYS A 44  ? 0.75630 1.06980 0.62220 -0.03910 0.05410  0.18400  44  CYS A CA  
325  C C   . CYS A 44  ? 0.81610 1.13540 0.68250 -0.04160 0.04810  0.20060  44  CYS A C   
326  O O   . CYS A 44  ? 0.90320 1.21740 0.76130 -0.04040 0.04230  0.19440  44  CYS A O   
327  C CB  . CYS A 44  ? 0.84020 1.12480 0.72570 -0.03960 0.05160  0.18070  44  CYS A CB  
328  S SG  . CYS A 44  ? 0.94960 1.23140 0.84160 -0.03830 0.05890  0.17070  44  CYS A SG  
329  N N   . THR A 45  ? 0.95170 1.28190 0.82940 -0.04510 0.04950  0.22250  45  THR A N   
330  C CA  . THR A 45  ? 1.03000 1.36380 0.91540 -0.04790 0.04420  0.24280  45  THR A CA  
331  C C   . THR A 45  ? 1.10430 1.41230 1.01630 -0.05020 0.04070  0.25030  45  THR A C   
332  O O   . THR A 45  ? 1.11580 1.40840 1.03920 -0.05020 0.04330  0.24260  45  THR A O   
333  C CB  . THR A 45  ? 1.04290 1.40760 0.92520 -0.05060 0.04840  0.26370  45  THR A CB  
334  O OG1 . THR A 45  ? 1.08840 1.46300 0.97000 -0.05050 0.05690  0.26030  45  THR A OG1 
335  C CG2 . THR A 45  ? 0.93510 1.32500 0.79330 -0.04940 0.04700  0.26340  45  THR A CG2 
336  N N   . SER A 46  ? 1.13640 1.44030 1.05890 -0.05200 0.03480  0.26520  46  SER A N   
337  C CA  . SER A 46  ? 1.21290 1.49320 1.16220 -0.05410 0.03160  0.27230  46  SER A CA  
338  C C   . SER A 46  ? 1.30870 1.59100 1.27620 -0.05740 0.03680  0.28360  46  SER A C   
339  O O   . SER A 46  ? 1.33400 1.59450 1.32230 -0.05880 0.03550  0.28180  46  SER A O   
340  C CB  . SER A 46  ? 1.29350 1.57330 1.25270 -0.05550 0.02520  0.28930  46  SER A CB  
341  O OG  . SER A 46  ? 1.20370 1.48390 1.14610 -0.05270 0.02020  0.27930  46  SER A OG  
342  N N   . GLU A 47  ? 1.30800 1.61660 1.26810 -0.05870 0.04280  0.29420  47  GLU A N   
343  C CA  . GLU A 47  ? 1.33140 1.64550 1.30830 -0.06200 0.04830  0.30590  47  GLU A CA  
344  C C   . GLU A 47  ? 1.35360 1.66550 1.32490 -0.06040 0.05420  0.28840  47  GLU A C   
345  O O   . GLU A 47  ? 1.37220 1.67780 1.36220 -0.06290 0.05700  0.29230  47  GLU A O   
346  C CB  . GLU A 47  ? 1.36910 1.71490 1.34230 -0.06430 0.05230  0.32850  47  GLU A CB  
347  C CG  . GLU A 47  ? 1.43210 1.78890 1.40220 -0.06490 0.04710  0.34510  47  GLU A CG  
348  C CD  . GLU A 47  ? 1.46720 1.84060 1.40630 -0.06150 0.04600  0.33390  47  GLU A CD  
349  O OE1 . GLU A 47  ? 1.42390 1.82340 1.34440 -0.06080 0.05200  0.33290  47  GLU A OE1 
350  O OE2 . GLU A 47  ? 1.37620 1.73660 1.31040 -0.05950 0.03930  0.32540  47  GLU A OE2 
351  N N   . ASP A 48  ? 1.39640 1.71320 1.34430 -0.05620 0.05590  0.26920  48  ASP A N   
352  C CA  . ASP A 48  ? 1.34350 1.65880 1.28710 -0.05420 0.06150  0.25290  48  ASP A CA  
353  C C   . ASP A 48  ? 1.29550 1.58270 1.24220 -0.05170 0.05770  0.23280  48  ASP A C   
354  O O   . ASP A 48  ? 1.40360 1.69010 1.33600 -0.04800 0.05990  0.21430  48  ASP A O   
355  C CB  . ASP A 48  ? 1.27940 1.61800 1.19730 -0.05080 0.06670  0.24310  48  ASP A CB  
356  C CG  . ASP A 48  ? 1.40260 1.77300 1.31480 -0.05290 0.07210  0.26100  48  ASP A CG  
357  O OD1 . ASP A 48  ? 1.45420 1.83320 1.37820 -0.05510 0.07790  0.27040  48  ASP A OD1 
358  O OD2 . ASP A 48  ? 1.41270 1.80080 1.30790 -0.05220 0.07070  0.26500  48  ASP A OD2 
359  N N   . MET A 49  ? 1.14250 1.40680 1.10810 -0.05370 0.05230  0.23540  49  MET A N   
360  C CA  . MET A 49  ? 0.98120 1.22090 0.94870 -0.05130 0.04920  0.21640  49  MET A CA  
361  C C   . MET A 49  ? 0.88950 1.11610 0.87720 -0.05360 0.05040  0.21500  49  MET A C   
362  O O   . MET A 49  ? 0.79140 1.00330 0.77820 -0.05130 0.04960  0.19840  49  MET A O   
363  C CB  . MET A 49  ? 0.93340 1.15600 0.90260 -0.05070 0.04170  0.21450  49  MET A CB  
364  C CG  . MET A 49  ? 0.94610 1.17890 0.89270 -0.04770 0.03970  0.20950  49  MET A CG  
365  S SD  . MET A 49  ? 1.18370 1.39550 1.12720 -0.04540 0.03160  0.19890  49  MET A SD  
366  C CE  . MET A 49  ? 1.02130 1.23480 0.97930 -0.04860 0.02640  0.22180  49  MET A CE  
367  N N   . LEU A 50  ? 0.91700 1.15090 0.92250 -0.05790 0.05250  0.23190  50  LEU A N   
368  C CA  . LEU A 50  ? 0.88240 1.10440 0.90860 -0.06060 0.05300  0.23040  50  LEU A CA  
369  C C   . LEU A 50  ? 0.94330 1.17580 0.96400 -0.05910 0.05930  0.22200  50  LEU A C   
370  O O   . LEU A 50  ? 0.91670 1.13610 0.94410 -0.05860 0.05860  0.20980  50  LEU A O   
371  C CB  . LEU A 50  ? 0.91660 1.14110 0.96690 -0.06610 0.05260  0.25150  50  LEU A CB  
372  C CG  . LEU A 50  ? 0.89340 1.10570 0.96740 -0.06960 0.05250  0.24980  50  LEU A CG  
373  C CD1 . LEU A 50  ? 0.82630 1.01140 0.90770 -0.06880 0.04600  0.23500  50  LEU A CD1 
374  C CD2 . LEU A 50  ? 0.89450 1.11440 0.99270 -0.07530 0.05360  0.27220  50  LEU A CD2 
375  N N   . ASN A 51  ? 1.05040 1.30750 1.06070 -0.05870 0.06550  0.22930  51  ASN A N   
376  C CA  . ASN A 51  ? 1.22670 1.49570 1.23120 -0.05660 0.07220  0.22090  51  ASN A CA  
377  C C   . ASN A 51  ? 1.14940 1.44200 1.13080 -0.05340 0.07750  0.21980  51  ASN A C   
378  O O   . ASN A 51  ? 1.06230 1.37790 1.04310 -0.05470 0.08390  0.23070  51  ASN A O   
379  C CB  . ASN A 51  ? 1.36140 1.63700 1.38720 -0.06100 0.07600  0.23260  51  ASN A CB  
380  C CG  . ASN A 51  ? 1.52170 1.77450 1.56760 -0.06310 0.07150  0.22590  51  ASN A CG  
381  O OD1 . ASN A 51  ? 1.36460 1.60530 1.40540 -0.05990 0.07000  0.20830  51  ASN A OD1 
382  N ND2 . ASN A 51  ? 1.49860 1.74640 1.56800 -0.06860 0.06930  0.23990  51  ASN A ND2 
383  N N   . PRO A 52  ? 0.94920 1.23740 0.91170 -0.04920 0.07520  0.20550  52  PRO A N   
384  C CA  . PRO A 52  ? 0.86130 1.17140 0.80130 -0.04610 0.07970  0.20150  52  PRO A CA  
385  C C   . PRO A 52  ? 0.76280 1.08290 0.69730 -0.04280 0.08700  0.18910  52  PRO A C   
386  O O   . PRO A 52  ? 0.76480 1.06970 0.70580 -0.04090 0.08650  0.17620  52  PRO A O   
387  C CB  . PRO A 52  ? 0.83870 1.13570 0.76480 -0.04300 0.07380  0.18810  52  PRO A CB  
388  C CG  . PRO A 52  ? 0.87460 1.14360 0.81310 -0.04240 0.06940  0.17720  52  PRO A CG  
389  C CD  . PRO A 52  ? 0.86670 1.12950 0.82840 -0.04700 0.06880  0.19060  52  PRO A CD  
390  N N   . ASN A 53  ? 0.65750 1.00460 0.58000 -0.04190 0.09380  0.19280  53  ASN A N   
391  C CA  . ASN A 53  ? 0.64610 1.00430 0.56050 -0.03770 0.10110  0.17850  53  ASN A CA  
392  C C   . ASN A 53  ? 0.62120 0.98490 0.51280 -0.03350 0.10070  0.16340  53  ASN A C   
393  O O   . ASN A 53  ? 0.65460 1.04020 0.53160 -0.03380 0.10280  0.16910  53  ASN A O   
394  C CB  . ASN A 53  ? 0.66310 1.04890 0.57990 -0.03910 0.11010  0.19000  53  ASN A CB  
395  C CG  . ASN A 53  ? 0.70960 1.10370 0.62160 -0.03440 0.11740  0.17360  53  ASN A CG  
396  O OD1 . ASN A 53  ? 0.69450 1.10090 0.58780 -0.03040 0.12070  0.16120  53  ASN A OD1 
397  N ND2 . ASN A 53  ? 0.76990 1.15580 0.69920 -0.03450 0.11950  0.17180  53  ASN A ND2 
398  N N   . TYR A 54  ? 0.66180 1.00550 0.55090 -0.02990 0.09730  0.14480  54  TYR A N   
399  C CA  . TYR A 54  ? 0.64900 0.99430 0.51900 -0.02650 0.09540  0.13050  54  TYR A CA  
400  C C   . TYR A 54  ? 0.67190 1.04170 0.52710 -0.02300 0.10360  0.12030  54  TYR A C   
401  O O   . TYR A 54  ? 0.66540 1.04650 0.50290 -0.02160 0.10290  0.11360  54  TYR A O   
402  C CB  . TYR A 54  ? 0.60360 0.92190 0.47670 -0.02360 0.09030  0.11400  54  TYR A CB  
403  C CG  . TYR A 54  ? 0.62210 0.91740 0.50460 -0.02640 0.08170  0.12050  54  TYR A CG  
404  C CD1 . TYR A 54  ? 0.61090 0.90300 0.48430 -0.02720 0.07560  0.12210  54  TYR A CD1 
405  C CD2 . TYR A 54  ? 0.62900 0.90590 0.53000 -0.02800 0.07940  0.12360  54  TYR A CD2 
406  C CE1 . TYR A 54  ? 0.59690 0.86810 0.47950 -0.02920 0.06820  0.12700  54  TYR A CE1 
407  C CE2 . TYR A 54  ? 0.58830 0.84360 0.49790 -0.03020 0.07160  0.12720  54  TYR A CE2 
408  C CZ  . TYR A 54  ? 0.59250 0.84570 0.49290 -0.03070 0.06640  0.12940  54  TYR A CZ  
409  O OH  . TYR A 54  ? 0.62440 0.85810 0.53310 -0.03250 0.05940  0.13280  54  TYR A OH  
410  N N   . GLU A 55  ? 0.66000 1.03830 0.52240 -0.02140 0.11110  0.11760  55  GLU A N   
411  C CA  . GLU A 55  ? 0.69850 1.10210 0.54780 -0.01800 0.11980  0.10810  55  GLU A CA  
412  C C   . GLU A 55  ? 0.68060 1.11320 0.51640 -0.02070 0.12250  0.12210  55  GLU A C   
413  O O   . GLU A 55  ? 0.62750 1.07670 0.44430 -0.01870 0.12420  0.11260  55  GLU A O   
414  C CB  . GLU A 55  ? 0.66770 1.07580 0.53020 -0.01610 0.12750  0.10580  55  GLU A CB  
415  C CG  . GLU A 55  ? 0.84710 1.27860 0.69800 -0.01150 0.13700  0.09190  55  GLU A CG  
416  C CD  . GLU A 55  ? 0.93740 1.37360 0.80230 -0.00890 0.14500  0.08800  55  GLU A CD  
417  O OE1 . GLU A 55  ? 1.19820 1.62420 1.08160 -0.01140 0.14380  0.09890  55  GLU A OE1 
418  O OE2 . GLU A 55  ? 0.86920 1.32030 0.72700 -0.00420 0.15250  0.07330  55  GLU A OE2 
419  N N   . ASP A 56  ? 0.65450 1.09280 0.50060 -0.02570 0.12200  0.14510  56  ASP A N   
420  C CA  . ASP A 56  ? 0.71630 1.18120 0.55230 -0.02890 0.12350  0.16270  56  ASP A CA  
421  C C   . ASP A 56  ? 0.72320 1.18710 0.54370 -0.02940 0.11600  0.16150  56  ASP A C   
422  O O   . ASP A 56  ? 0.66580 1.15510 0.46710 -0.02890 0.11830  0.16110  56  ASP A O   
423  C CB  . ASP A 56  ? 0.74620 1.20890 0.60150 -0.03450 0.12220  0.18790  56  ASP A CB  
424  C CG  . ASP A 56  ? 0.77030 1.25420 0.63410 -0.03570 0.13160  0.19860  56  ASP A CG  
425  O OD1 . ASP A 56  ? 0.75640 1.26240 0.60870 -0.03250 0.14000  0.18910  56  ASP A OD1 
426  O OD2 . ASP A 56  ? 0.94820 1.42580 0.83210 -0.04010 0.13040  0.21630  56  ASP A OD2 
427  N N   . LEU A 57  ? 0.66130 1.09740 0.49060 -0.03080 0.10690  0.16270  57  LEU A N   
428  C CA  . LEU A 57  ? 0.67130 1.10500 0.48920 -0.03150 0.09910  0.16370  57  LEU A CA  
429  C C   . LEU A 57  ? 0.68900 1.13110 0.48580 -0.02740 0.09990  0.14160  57  LEU A C   
430  O O   . LEU A 57  ? 0.71870 1.17870 0.49890 -0.02800 0.09760  0.14370  57  LEU A O   
431  C CB  . LEU A 57  ? 0.62210 1.02220 0.45470 -0.03280 0.09030  0.16430  57  LEU A CB  
432  C CG  . LEU A 57  ? 0.65650 1.04960 0.51030 -0.03750 0.08870  0.18670  57  LEU A CG  
433  C CD1 . LEU A 57  ? 0.72680 1.08660 0.59690 -0.03850 0.08080  0.18570  57  LEU A CD1 
434  C CD2 . LEU A 57  ? 0.73170 1.14840 0.58130 -0.04110 0.08830  0.20970  57  LEU A CD2 
435  N N   . LEU A 58  ? 0.63400 1.06550 0.43220 -0.02320 0.10330  0.12070  58  LEU A N   
436  C CA  . LEU A 58  ? 0.68720 1.12330 0.46920 -0.01910 0.10420  0.09760  58  LEU A CA  
437  C C   . LEU A 58  ? 0.67780 1.14930 0.44290 -0.01780 0.11230  0.09410  58  LEU A C   
438  O O   . LEU A 58  ? 0.67930 1.16470 0.42600 -0.01690 0.11070  0.08390  58  LEU A O   
439  C CB  . LEU A 58  ? 0.62230 1.03560 0.41440 -0.01490 0.10560  0.07830  58  LEU A CB  
440  C CG  . LEU A 58  ? 0.68130 1.09110 0.46200 -0.01090 0.10460  0.05410  58  LEU A CG  
441  C CD1 . LEU A 58  ? 0.70950 1.11270 0.48110 -0.01300 0.09510  0.05520  58  LEU A CD1 
442  C CD2 . LEU A 58  ? 0.67600 1.05740 0.47210 -0.00770 0.10380  0.04110  58  LEU A CD2 
443  N N   . ILE A 59  ? 0.69840 1.18650 0.46900 -0.01800 0.12100  0.10240  59  ILE A N   
444  C CA  . ILE A 59  ? 0.66650 1.18880 0.42140 -0.01680 0.12880  0.09930  59  ILE A CA  
445  C C   . ILE A 59  ? 0.67340 1.20950 0.41940 -0.02010 0.12260  0.11360  59  ILE A C   
446  O O   . ILE A 59  ? 0.74630 1.30180 0.47930 -0.01880 0.12360  0.10590  59  ILE A O   
447  C CB  . ILE A 59  ? 0.69990 1.23460 0.46610 -0.01630 0.13810  0.10610  59  ILE A CB  
448  C CG1 . ILE A 59  ? 0.80960 1.33180 0.58710 -0.01240 0.14420  0.09120  59  ILE A CG1 
449  C CG2 . ILE A 59  ? 0.62470 1.18480 0.37910 -0.01420 0.14290  0.09830  59  ILE A CG2 
450  C CD1 . ILE A 59  ? 0.81860 1.35470 0.60860 -0.01270 0.15330  0.10150  59  ILE A CD1 
451  N N   . ARG A 60  ? 0.65410 1.18210 0.40870 -0.02450 0.11660  0.13560  60  ARG A N   
452  C CA  . ARG A 60  ? 0.70910 1.25090 0.45710 -0.02730 0.11050  0.14960  60  ARG A CA  
453  C C   . ARG A 60  ? 0.68300 1.22100 0.41680 -0.02680 0.10250  0.13910  60  ARG A C   
454  O O   . ARG A 60  ? 0.74140 1.29300 0.46920 -0.02880 0.09730  0.14970  60  ARG A O   
455  C CB  . ARG A 60  ? 0.72770 1.26290 0.49250 -0.03200 0.10690  0.17750  60  ARG A CB  
456  C CG  . ARG A 60  ? 0.61430 1.15670 0.39320 -0.03300 0.11420  0.18900  60  ARG A CG  
457  C CD  . ARG A 60  ? 0.69810 1.22810 0.49760 -0.03750 0.11110  0.21250  60  ARG A CD  
458  N NE  . ARG A 60  ? 0.61570 1.15560 0.42840 -0.03850 0.11840  0.22250  60  ARG A NE  
459  C CZ  . ARG A 60  ? 0.66370 1.19040 0.49710 -0.04090 0.12040  0.23300  60  ARG A CZ  
460  N NH1 . ARG A 60  ? 0.80210 1.30510 0.64640 -0.04310 0.11540  0.23700  60  ARG A NH1 
461  N NH2 . ARG A 60  ? 0.75030 1.28910 0.59440 -0.04150 0.12750  0.23970  60  ARG A NH2 
462  N N   . LYS A 61  ? 0.71340 1.23560 0.44200 -0.02410 0.10140  0.11840  61  LYS A N   
463  C CA  . LYS A 61  ? 0.78780 1.30710 0.50340 -0.02370 0.09360  0.10700  61  LYS A CA  
464  C C   . LYS A 61  ? 0.79150 1.32170 0.49340 -0.01970 0.09710  0.08030  61  LYS A C   
465  O O   . LYS A 61  ? 0.78310 1.31560 0.48730 -0.01660 0.10530  0.06750  61  LYS A O   
466  C CB  . LYS A 61  ? 0.75290 1.24150 0.47630 -0.02360 0.08730  0.10230  61  LYS A CB  
467  C CG  . LYS A 61  ? 0.78950 1.25790 0.53270 -0.02700 0.08270  0.12470  61  LYS A CG  
468  C CD  . LYS A 61  ? 0.82380 1.27470 0.56940 -0.02860 0.07190  0.12860  61  LYS A CD  
469  C CE  . LYS A 61  ? 0.82280 1.27170 0.58160 -0.03280 0.06810  0.15670  61  LYS A CE  
470  N NZ  . LYS A 61  ? 0.81230 1.23630 0.59430 -0.03350 0.06930  0.16280  61  LYS A NZ  
471  N N   . SER A 62  ? 0.82040 1.35620 0.50970 -0.02000 0.09030  0.07140  62  SER A N   
472  C CA  . SER A 62  ? 0.81160 1.35290 0.48920 -0.01670 0.09130  0.04390  62  SER A CA  
473  C C   . SER A 62  ? 0.81240 1.33530 0.48670 -0.01660 0.08340  0.03150  62  SER A C   
474  O O   . SER A 62  ? 0.81490 1.32380 0.49410 -0.01910 0.07710  0.04530  62  SER A O   
475  C CB  . SER A 62  ? 0.83410 1.40310 0.49920 -0.01740 0.09050  0.04310  62  SER A CB  
476  O OG  . SER A 62  ? 0.89830 1.47290 0.56230 -0.02130 0.08260  0.06430  62  SER A OG  
477  N N   . ASN A 63  ? 0.79700 1.32030 0.46400 -0.01370 0.08390  0.00510  63  ASN A N   
478  C CA  . ASN A 63  ? 0.80050 1.30720 0.46520 -0.01340 0.07680  -0.00970 63  ASN A CA  
479  C C   . ASN A 63  ? 0.82200 1.33060 0.48180 -0.01740 0.06640  0.00520  63  ASN A C   
480  O O   . ASN A 63  ? 0.87600 1.36570 0.53990 -0.01840 0.06030  0.00790  63  ASN A O   
481  C CB  . ASN A 63  ? 0.82770 1.33990 0.48570 -0.01050 0.07840  -0.03870 63  ASN A CB  
482  C CG  . ASN A 63  ? 0.84530 1.34950 0.51150 -0.00590 0.08790  -0.05680 63  ASN A CG  
483  O OD1 . ASN A 63  ? 0.85060 1.33830 0.52780 -0.00460 0.09160  -0.05240 63  ASN A OD1 
484  N ND2 . ASN A 63  ? 0.73520 1.25080 0.39710 -0.00330 0.09170  -0.07770 63  ASN A ND2 
485  N N   . HIS A 64  ? 0.84170 1.37350 0.49420 -0.01960 0.06420  0.01680  64  HIS A N   
486  C CA  . HIS A 64  ? 0.80180 1.33690 0.45070 -0.02290 0.05410  0.03020  64  HIS A CA  
487  C C   . HIS A 64  ? 0.84970 1.37290 0.50960 -0.02550 0.05080  0.05710  64  HIS A C   
488  O O   . HIS A 64  ? 0.90840 1.42720 0.56850 -0.02780 0.04200  0.06660  64  HIS A O   
489  C CB  . HIS A 64  ? 0.81680 1.38130 0.45550 -0.02450 0.05240  0.03520  64  HIS A CB  
490  C CG  . HIS A 64  ? 0.87540 1.45710 0.51760 -0.02570 0.05730  0.05780  64  HIS A CG  
491  N ND1 . HIS A 64  ? 0.89960 1.48290 0.54920 -0.02890 0.05290  0.08590  64  HIS A ND1 
492  C CD2 . HIS A 64  ? 0.86260 1.46140 0.50300 -0.02430 0.06590  0.05630  64  HIS A CD2 
493  C CE1 . HIS A 64  ? 0.84540 1.44570 0.49810 -0.02950 0.05860  0.10080  64  HIS A CE1 
494  N NE2 . HIS A 64  ? 0.87770 1.48800 0.52420 -0.02680 0.06660  0.08340  64  HIS A NE2 
495  N N   . ASN A 65  ? 0.84850 1.36370 0.51900 -0.02520 0.05730  0.06800  65  ASN A N   
496  C CA  . ASN A 65  ? 0.86440 1.36540 0.54760 -0.02780 0.05400  0.09170  65  ASN A CA  
497  C C   . ASN A 65  ? 0.82200 1.28880 0.51670 -0.02700 0.04870  0.08360  65  ASN A C   
498  O O   . ASN A 65  ? 0.81220 1.26120 0.52210 -0.02880 0.04450  0.10070  65  ASN A O   
499  C CB  . ASN A 65  ? 0.82960 1.33090 0.52450 -0.02820 0.06190  0.10670  65  ASN A CB  
500  C CG  . ASN A 65  ? 0.84930 1.37670 0.54180 -0.02910 0.06550  0.11770  65  ASN A CG  
501  O OD1 . ASN A 65  ? 0.89100 1.42600 0.58710 -0.02800 0.07390  0.11770  65  ASN A OD1 
502  N ND2 . ASN A 65  ? 0.89990 1.44250 0.58700 -0.03110 0.05920  0.12790  65  ASN A ND2 
503  N N   . PHE A 66  ? 0.83130 1.28560 0.52350 -0.02400 0.04840  0.05770  66  PHE A N   
504  C CA  . PHE A 66  ? 0.80250 1.22190 0.50880 -0.02280 0.04330  0.04800  66  PHE A CA  
505  C C   . PHE A 66  ? 0.85140 1.27060 0.54930 -0.02340 0.03480  0.03730  66  PHE A C   
506  O O   . PHE A 66  ? 0.88450 1.31510 0.57040 -0.02200 0.03560  0.01680  66  PHE A O   
507  C CB  . PHE A 66  ? 0.76720 1.17030 0.48070 -0.01900 0.04960  0.02790  66  PHE A CB  
508  C CG  . PHE A 66  ? 0.75570 1.15610 0.47980 -0.01820 0.05740  0.03700  66  PHE A CG  
509  C CD1 . PHE A 66  ? 0.73420 1.10850 0.47680 -0.01860 0.05610  0.04650  66  PHE A CD1 
510  C CD2 . PHE A 66  ? 0.72850 1.15320 0.44410 -0.01720 0.06610  0.03480  66  PHE A CD2 
511  C CE1 . PHE A 66  ? 0.75170 1.12400 0.50480 -0.01830 0.06270  0.05430  66  PHE A CE1 
512  C CE2 . PHE A 66  ? 0.76650 1.18960 0.49290 -0.01670 0.07310  0.04340  66  PHE A CE2 
513  C CZ  . PHE A 66  ? 0.73310 1.12970 0.47850 -0.01730 0.07120  0.05320  66  PHE A CZ  
514  N N   . LEU A 67  ? 0.78250 1.18870 0.48810 -0.02550 0.02660  0.05010  67  LEU A N   
515  C CA  . LEU A 67  ? 0.82080 1.22580 0.52110 -0.02630 0.01800  0.04210  67  LEU A CA  
516  C C   . LEU A 67  ? 0.79900 1.16930 0.51420 -0.02450 0.01520  0.02950  67  LEU A C   
517  O O   . LEU A 67  ? 0.77790 1.12570 0.50900 -0.02470 0.01390  0.04090  67  LEU A O   
518  C CB  . LEU A 67  ? 0.90710 1.32330 0.60650 -0.02960 0.01090  0.06550  67  LEU A CB  
519  C CG  . LEU A 67  ? 0.96830 1.37710 0.66900 -0.03080 0.00070  0.06400  67  LEU A CG  
520  C CD1 . LEU A 67  ? 0.99270 1.42210 0.67530 -0.03090 -0.00200 0.04530  67  LEU A CD1 
521  C CD2 . LEU A 67  ? 0.97400 1.39000 0.67970 -0.03360 -0.00510 0.09120  67  LEU A CD2 
522  N N   . VAL A 68  ? 0.81340 1.17980 0.52440 -0.02260 0.01510  0.00550  68  VAL A N   
523  C CA  . VAL A 68  ? 0.80100 1.13680 0.52590 -0.02080 0.01330  -0.00760 68  VAL A CA  
524  C C   . VAL A 68  ? 0.84640 1.18040 0.56860 -0.02210 0.00440  -0.01550 68  VAL A C   
525  O O   . VAL A 68  ? 0.91600 1.27110 0.62400 -0.02300 0.00250  -0.02650 68  VAL A O   
526  C CB  . VAL A 68  ? 0.79150 1.12150 0.51820 -0.01730 0.02080  -0.02820 68  VAL A CB  
527  C CG1 . VAL A 68  ? 0.76820 1.06810 0.50970 -0.01530 0.01910  -0.04110 68  VAL A CG1 
528  C CG2 . VAL A 68  ? 0.76370 1.09680 0.49410 -0.01610 0.02930  -0.01870 68  VAL A CG2 
529  N N   . GLN A 69  ? 0.79580 1.10560 0.53180 -0.02250 -0.00090 -0.01030 69  GLN A N   
530  C CA  . GLN A 69  ? 0.86030 1.16700 0.59630 -0.02400 -0.00950 -0.01520 69  GLN A CA  
531  C C   . GLN A 69  ? 0.81110 1.08810 0.56220 -0.02220 -0.01060 -0.02710 69  GLN A C   
532  O O   . GLN A 69  ? 0.69630 0.95160 0.46100 -0.02130 -0.00920 -0.01870 69  GLN A O   
533  C CB  . GLN A 69  ? 0.87150 1.18290 0.60950 -0.02660 -0.01620 0.00690  69  GLN A CB  
534  C CG  . GLN A 69  ? 0.97000 1.31150 0.69440 -0.02860 -0.01610 0.02120  69  GLN A CG  
535  C CD  . GLN A 69  ? 1.15340 1.49520 0.88480 -0.03060 -0.02170 0.04570  69  GLN A CD  
536  O OE1 . GLN A 69  ? 1.25120 1.59530 0.98710 -0.03110 -0.01830 0.06370  69  GLN A OE1 
537  N NE2 . GLN A 69  ? 1.16710 1.50580 0.90150 -0.03190 -0.03020 0.04660  69  GLN A NE2 
538  N N   . ALA A 70  ? 0.78610 1.06340 0.53470 -0.02190 -0.01280 -0.04710 70  ALA A N   
539  C CA  . ALA A 70  ? 0.87540 1.12810 0.63770 -0.02090 -0.01520 -0.05890 70  ALA A CA  
540  C C   . ALA A 70  ? 0.91450 1.17040 0.67660 -0.02360 -0.02470 -0.05520 70  ALA A C   
541  O O   . ALA A 70  ? 0.91760 1.18890 0.67090 -0.02510 -0.02880 -0.06710 70  ALA A O   
542  C CB  . ALA A 70  ? 0.87880 1.13030 0.64120 -0.01890 -0.01120 -0.08300 70  ALA A CB  
543  N N   . GLY A 71  ? 0.93260 1.17600 0.70430 -0.02430 -0.02810 -0.03800 71  GLY A N   
544  C CA  . GLY A 71  ? 0.96440 1.21300 0.73650 -0.02680 -0.03680 -0.02950 71  GLY A CA  
545  C C   . GLY A 71  ? 1.05940 1.33720 0.81660 -0.02890 -0.03910 -0.01760 71  GLY A C   
546  O O   . GLY A 71  ? 1.03300 1.31730 0.78780 -0.02870 -0.03520 -0.00240 71  GLY A O   
547  N N   . ASN A 72  ? 1.16740 1.46430 0.91450 -0.03100 -0.04530 -0.02480 72  ASN A N   
548  C CA  . ASN A 72  ? 1.20810 1.53730 0.93820 -0.03290 -0.04710 -0.01660 72  ASN A CA  
549  C C   . ASN A 72  ? 1.13940 1.48810 0.85380 -0.03250 -0.04210 -0.03410 72  ASN A C   
550  O O   . ASN A 72  ? 1.17690 1.55320 0.87600 -0.03370 -0.04130 -0.02670 72  ASN A O   
551  C CB  . ASN A 72  ? 1.25600 1.59900 0.98300 -0.03580 -0.05750 -0.01250 72  ASN A CB  
552  C CG  . ASN A 72  ? 1.33410 1.65740 1.07370 -0.03590 -0.06240 -0.02560 72  ASN A CG  
553  O OD1 . ASN A 72  ? 1.42600 1.74990 1.16280 -0.03600 -0.06250 -0.04760 72  ASN A OD1 
554  N ND2 . ASN A 72  ? 1.36980 1.67540 1.12440 -0.03580 -0.06620 -0.01230 72  ASN A ND2 
555  N N   . VAL A 73  ? 1.06810 1.40410 0.78650 -0.03080 -0.03880 -0.05700 73  VAL A N   
556  C CA  . VAL A 73  ? 1.02250 1.37610 0.72780 -0.03000 -0.03350 -0.07540 73  VAL A CA  
557  C C   . VAL A 73  ? 1.00640 1.36480 0.70790 -0.02810 -0.02430 -0.06590 73  VAL A C   
558  O O   . VAL A 73  ? 0.95750 1.29300 0.67180 -0.02580 -0.01900 -0.06150 73  VAL A O   
559  C CB  . VAL A 73  ? 0.98490 1.32120 0.69960 -0.02840 -0.03170 -0.10110 73  VAL A CB  
560  C CG1 . VAL A 73  ? 0.97260 1.32640 0.67570 -0.02700 -0.02500 -0.12060 73  VAL A CG1 
561  C CG2 . VAL A 73  ? 0.94070 1.27450 0.65960 -0.03080 -0.04090 -0.11050 73  VAL A CG2 
562  N N   . GLN A 74  ? 1.02820 1.41740 0.71210 -0.02910 -0.02240 -0.06210 74  GLN A N   
563  C CA  . GLN A 74  ? 1.05380 1.45150 0.73320 -0.02760 -0.01360 -0.05250 74  GLN A CA  
564  C C   . GLN A 74  ? 1.05120 1.44920 0.72850 -0.02470 -0.00520 -0.07560 74  GLN A C   
565  O O   . GLN A 74  ? 1.05650 1.46900 0.72430 -0.02490 -0.00610 -0.09630 74  GLN A O   
566  C CB  . GLN A 74  ? 1.11970 1.55210 0.78180 -0.03010 -0.01510 -0.03670 74  GLN A CB  
567  C CG  . GLN A 74  ? 1.13000 1.56790 0.79280 -0.02980 -0.00890 -0.01470 74  GLN A CG  
568  C CD  . GLN A 74  ? 1.28990 1.75090 0.93910 -0.02840 0.00030  -0.02260 74  GLN A CD  
569  O OE1 . GLN A 74  ? 1.45120 1.90850 1.09950 -0.02610 0.00520  -0.04600 74  GLN A OE1 
570  N NE2 . GLN A 74  ? 1.22570 1.71050 0.86630 -0.02980 0.00280  -0.00300 74  GLN A NE2 
571  N N   . LEU A 75  ? 0.98910 1.37150 0.67620 -0.02200 0.00260  -0.07230 75  LEU A N   
572  C CA  . LEU A 75  ? 0.97940 1.35980 0.66790 -0.01870 0.01120  -0.09210 75  LEU A CA  
573  C C   . LEU A 75  ? 0.98810 1.39390 0.66430 -0.01810 0.01910  -0.08580 75  LEU A C   
574  O O   . LEU A 75  ? 0.97410 1.38280 0.65120 -0.01890 0.02100  -0.06330 75  LEU A O   
575  C CB  . LEU A 75  ? 0.95180 1.29830 0.66070 -0.01590 0.01460  -0.09410 75  LEU A CB  
576  C CG  . LEU A 75  ? 0.94810 1.27220 0.66960 -0.01470 0.01150  -0.11330 75  LEU A CG  
577  C CD1 . LEU A 75  ? 1.02310 1.35430 0.73900 -0.01770 0.00220  -0.12040 75  LEU A CD1 
578  C CD2 . LEU A 75  ? 0.83780 1.12950 0.57840 -0.01340 0.01100  -0.10490 75  LEU A CD2 
579  N N   . ARG A 76  ? 0.95770 1.38310 0.62280 -0.01680 0.02370  -0.10570 76  ARG A N   
580  C CA  . ARG A 76  ? 0.91810 1.37110 0.57010 -0.01610 0.03180  -0.10190 76  ARG A CA  
581  C C   . ARG A 76  ? 0.86640 1.30400 0.53130 -0.01220 0.04160  -0.10480 76  ARG A C   
582  O O   . ARG A 76  ? 0.86420 1.28540 0.53960 -0.00920 0.04450  -0.12500 76  ARG A O   
583  C CB  . ARG A 76  ? 0.94600 1.42020 0.58840 -0.01610 0.03170  -0.12030 76  ARG A CB  
584  C CG  . ARG A 76  ? 0.95790 1.44170 0.60070 -0.01270 0.04200  -0.13400 76  ARG A CG  
585  C CD  . ARG A 76  ? 0.96080 1.46630 0.59500 -0.01330 0.04090  -0.14930 76  ARG A CD  
586  N NE  . ARG A 76  ? 1.02980 1.56200 0.65350 -0.01460 0.04330  -0.13250 76  ARG A NE  
587  C CZ  . ARG A 76  ? 1.10050 1.64670 0.72240 -0.01240 0.05240  -0.13540 76  ARG A CZ  
588  N NH1 . ARG A 76  ? 1.11480 1.65110 0.74500 -0.00840 0.06010  -0.15450 76  ARG A NH1 
589  N NH2 . ARG A 76  ? 1.14950 1.72080 0.76230 -0.01400 0.05380  -0.11860 76  ARG A NH2 
590  N N   . VAL A 77  ? 0.83420 1.27680 0.50010 -0.01250 0.04620  -0.08370 77  VAL A N   
591  C CA  . VAL A 77  ? 0.88470 1.31740 0.56180 -0.00920 0.05560  -0.08410 77  VAL A CA  
592  C C   . VAL A 77  ? 0.85510 1.31570 0.52010 -0.00700 0.06480  -0.09780 77  VAL A C   
593  O O   . VAL A 77  ? 0.83820 1.32290 0.49270 -0.00880 0.06490  -0.08910 77  VAL A O   
594  C CB  . VAL A 77  ? 0.82340 1.24980 0.50820 -0.01080 0.05630  -0.05620 77  VAL A CB  
595  C CG1 . VAL A 77  ? 0.80460 1.22390 0.50060 -0.00780 0.06580  -0.05630 77  VAL A CG1 
596  C CG2 . VAL A 77  ? 0.77260 1.16970 0.47100 -0.01250 0.04780  -0.04560 77  VAL A CG2 
597  N N   . ILE A 78  ? 0.83350 1.28320 0.50840 -0.00280 0.07130  -0.11750 78  ILE A N   
598  C CA  . ILE A 78  ? 0.85270 1.32080 0.52370 -0.00010 0.07940  -0.13220 78  ILE A CA  
599  C C   . ILE A 78  ? 0.83970 1.30470 0.52070 0.00350  0.09000  -0.13030 78  ILE A C   
600  O O   . ILE A 78  ? 0.78240 1.25720 0.46510 0.00650  0.09710  -0.14350 78  ILE A O   
601  C CB  . ILE A 78  ? 0.91450 1.37750 0.58820 0.00190  0.07790  -0.16140 78  ILE A CB  
602  C CG1 . ILE A 78  ? 0.87400 1.30860 0.56310 0.00480  0.07850  -0.17430 78  ILE A CG1 
603  C CG2 . ILE A 78  ? 0.91170 1.38240 0.57510 -0.00200 0.06760  -0.16300 78  ILE A CG2 
604  C CD1 . ILE A 78  ? 0.90790 1.33430 0.60510 0.00740  0.07860  -0.20350 78  ILE A CD1 
605  N N   . GLY A 79  ? 0.83040 1.27770 0.52270 0.00290  0.08960  -0.11160 79  GLY A N   
606  C CA  . GLY A 79  ? 0.75080 1.19170 0.45640 0.00580  0.09800  -0.10640 79  GLY A CA  
607  C C   . GLY A 79  ? 0.74190 1.15760 0.46210 0.00400  0.09370  -0.08530 79  GLY A C   
608  O O   . GLY A 79  ? 0.79980 1.19410 0.52540 0.00230  0.08510  -0.08220 79  GLY A O   
609  N N   . HIS A 80  ? 0.74800 1.16600 0.47570 0.00430  0.09960  -0.07100 80  HIS A N   
610  C CA  . HIS A 80  ? 0.71620 1.11190 0.45840 0.00240  0.09570  -0.05170 80  HIS A CA  
611  C C   . HIS A 80  ? 0.71990 1.11160 0.47600 0.00500  0.10370  -0.04900 80  HIS A C   
612  O O   . HIS A 80  ? 0.68200 1.09670 0.43330 0.00630  0.11220  -0.05030 80  HIS A O   
613  C CB  . HIS A 80  ? 0.70140 1.10770 0.43640 -0.00270 0.09110  -0.02710 80  HIS A CB  
614  C CG  . HIS A 80  ? 0.74000 1.17900 0.46390 -0.00400 0.09790  -0.01620 80  HIS A CG  
615  N ND1 . HIS A 80  ? 0.74620 1.21420 0.45000 -0.00540 0.09780  -0.01790 80  HIS A ND1 
616  C CD2 . HIS A 80  ? 0.72490 1.17350 0.45520 -0.00430 0.10500  -0.00280 80  HIS A CD2 
617  C CE1 . HIS A 80  ? 0.80240 1.29680 0.50010 -0.00640 0.10480  -0.00570 80  HIS A CE1 
618  N NE2 . HIS A 80  ? 0.80690 1.28960 0.52110 -0.00580 0.10930  0.00400  80  HIS A NE2 
619  N N   . SER A 81  ? 0.63050 0.99480 0.40380 0.00530  0.10070  -0.04390 81  SER A N   
620  C CA  . SER A 81  ? 0.65470 1.01320 0.44320 0.00720  0.10670  -0.03900 81  SER A CA  
621  C C   . SER A 81  ? 0.66900 1.00240 0.47160 0.00490  0.10060  -0.02430 81  SER A C   
622  O O   . SER A 81  ? 0.65640 0.97330 0.45900 0.00300  0.09240  -0.02210 81  SER A O   
623  C CB  . SER A 81  ? 0.66680 1.01890 0.46440 0.01290  0.11240  -0.06010 81  SER A CB  
624  O OG  . SER A 81  ? 0.70640 1.03290 0.51220 0.01460  0.10650  -0.07150 81  SER A OG  
625  N N   . MET A 82  ? 0.63500 0.96650 0.45020 0.00510  0.10480  -0.01480 82  MET A N   
626  C CA  . MET A 82  ? 0.64610 0.95590 0.47550 0.00290  0.09980  -0.00190 82  MET A CA  
627  C C   . MET A 82  ? 0.66330 0.95780 0.50880 0.00670  0.10250  -0.01040 82  MET A C   
628  O O   . MET A 82  ? 0.64070 0.94690 0.49070 0.00950  0.11020  -0.01470 82  MET A O   
629  C CB  . MET A 82  ? 0.62920 0.94990 0.46120 -0.00140 0.10090  0.01960  82  MET A CB  
630  C CG  . MET A 82  ? 0.64350 0.94290 0.49020 -0.00380 0.09580  0.03090  82  MET A CG  
631  S SD  . MET A 82  ? 0.64190 0.95280 0.49340 -0.00950 0.09610  0.05600  82  MET A SD  
632  C CE  . MET A 82  ? 0.57430 0.91240 0.42640 -0.00770 0.10780  0.05650  82  MET A CE  
633  N N   . GLN A 83  ? 0.57020 0.84000 0.42420 0.00710  0.09640  -0.01310 83  GLN A N   
634  C CA  . GLN A 83  ? 0.61610 0.86930 0.48630 0.01020  0.09710  -0.01790 83  GLN A CA  
635  C C   . GLN A 83  ? 0.60410 0.84110 0.48400 0.00670  0.09130  -0.00350 83  GLN A C   
636  O O   . GLN A 83  ? 0.59380 0.81500 0.47270 0.00500  0.08420  -0.00220 83  GLN A O   
637  C CB  . GLN A 83  ? 0.64860 0.88720 0.52060 0.01400  0.09500  -0.03530 83  GLN A CB  
638  C CG  . GLN A 83  ? 0.69480 0.91790 0.58410 0.01750  0.09580  -0.03950 83  GLN A CG  
639  C CD  . GLN A 83  ? 0.73060 0.93850 0.62530 0.02150  0.09410  -0.05510 83  GLN A CD  
640  O OE1 . GLN A 83  ? 0.68360 0.88680 0.57050 0.02090  0.09020  -0.06210 83  GLN A OE1 
641  N NE2 . GLN A 83  ? 0.76820 0.96950 0.67780 0.02560  0.09720  -0.06000 83  GLN A NE2 
642  N N   . ASN A 84  ? 0.56360 0.80470 0.45380 0.00550  0.09420  0.00680  84  ASN A N   
643  C CA  . ASN A 84  ? 0.55830 0.78560 0.45910 0.00190  0.08900  0.01960  84  ASN A CA  
644  C C   . ASN A 84  ? 0.57840 0.80470 0.47100 -0.00280 0.08350  0.02990  84  ASN A C   
645  O O   . ASN A 84  ? 0.51030 0.75480 0.39380 -0.00460 0.08620  0.03620  84  ASN A O   
646  C CB  . ASN A 84  ? 0.55050 0.75620 0.46190 0.00420  0.08500  0.01290  84  ASN A CB  
647  C CG  . ASN A 84  ? 0.62020 0.82860 0.54120 0.00890  0.09050  0.00450  84  ASN A CG  
648  O OD1 . ASN A 84  ? 0.59210 0.81340 0.51950 0.00870  0.09570  0.00970  84  ASN A OD1 
649  N ND2 . ASN A 84  ? 0.59130 0.78940 0.51430 0.01310  0.09000  -0.00840 84  ASN A ND2 
650  N N   . CYS A 85  ? 0.53930 0.74620 0.43430 -0.00430 0.07610  0.03120  85  CYS A N   
651  C CA  . CYS A 85  ? 0.53450 0.74030 0.42440 -0.00850 0.07090  0.04210  85  CYS A CA  
652  C C   . CYS A 85  ? 0.56380 0.76920 0.44030 -0.00760 0.06770  0.03460  85  CYS A C   
653  O O   . CYS A 85  ? 0.54890 0.75070 0.42240 -0.01060 0.06240  0.04250  85  CYS A O   
654  C CB  . CYS A 85  ? 0.55990 0.74690 0.46120 -0.01120 0.06500  0.04930  85  CYS A CB  
655  S SG  . CYS A 85  ? 0.53890 0.72860 0.45610 -0.01330 0.06800  0.05890  85  CYS A SG  
656  N N   . VAL A 86  ? 0.53510 0.74480 0.40490 -0.00370 0.07060  0.01940  86  VAL A N   
657  C CA  . VAL A 86  ? 0.53040 0.74170 0.38790 -0.00340 0.06730  0.01200  86  VAL A CA  
658  C C   . VAL A 86  ? 0.57620 0.81130 0.42070 -0.00230 0.07260  0.00640  86  VAL A C   
659  O O   . VAL A 86  ? 0.59780 0.84630 0.44330 -0.00030 0.07970  0.00340  86  VAL A O   
660  C CB  . VAL A 86  ? 0.51030 0.70370 0.37060 -0.00030 0.06420  -0.00250 86  VAL A CB  
661  C CG1 . VAL A 86  ? 0.53600 0.70660 0.40770 -0.00150 0.05870  0.00310  86  VAL A CG1 
662  C CG2 . VAL A 86  ? 0.60640 0.80260 0.47010 0.00430  0.07010  -0.01690 86  VAL A CG2 
663  N N   . LEU A 87  ? 0.59040 0.83330 0.42250 -0.00400 0.06890  0.00660  87  LEU A N   
664  C CA  . LEU A 87  ? 0.57390 0.83990 0.39140 -0.00300 0.07280  -0.00120 87  LEU A CA  
665  C C   . LEU A 87  ? 0.61250 0.87160 0.42630 -0.00000 0.07110  -0.02110 87  LEU A C   
666  O O   . LEU A 87  ? 0.59900 0.83990 0.41640 -0.00040 0.06470  -0.02360 87  LEU A O   
667  C CB  . LEU A 87  ? 0.59710 0.87910 0.40260 -0.00690 0.06950  0.01120  87  LEU A CB  
668  C CG  . LEU A 87  ? 0.65490 0.94730 0.46280 -0.01060 0.07030  0.03270  87  LEU A CG  
669  C CD1 . LEU A 87  ? 0.68580 0.99540 0.47950 -0.01330 0.06650  0.04030  87  LEU A CD1 
670  C CD2 . LEU A 87  ? 0.63790 0.94860 0.44660 -0.00940 0.07970  0.03410  87  LEU A CD2 
671  N N   . LYS A 88  ? 0.61610 0.89070 0.42310 0.00270  0.07690  -0.03500 88  LYS A N   
672  C CA  . LYS A 88  ? 0.64340 0.91660 0.44620 0.00530  0.07620  -0.05540 88  LYS A CA  
673  C C   . LYS A 88  ? 0.69010 0.98940 0.47410 0.00380  0.07670  -0.05890 88  LYS A C   
674  O O   . LYS A 88  ? 0.64210 0.96490 0.41840 0.00420  0.08340  -0.05760 88  LYS A O   
675  C CB  . LYS A 88  ? 0.66680 0.93590 0.47970 0.01030  0.08300  -0.07060 88  LYS A CB  
676  C CG  . LYS A 88  ? 0.66370 0.90960 0.49450 0.01160  0.08220  -0.06530 88  LYS A CG  
677  C CD  . LYS A 88  ? 0.68360 0.92030 0.52680 0.01680  0.08650  -0.08160 88  LYS A CD  
678  C CE  . LYS A 88  ? 0.76780 1.01720 0.61630 0.01950  0.09520  -0.08170 88  LYS A CE  
679  N NZ  . LYS A 88  ? 0.84710 1.08560 0.71040 0.02470  0.09870  -0.09640 88  LYS A NZ  
680  N N   . LEU A 89  ? 0.64040 0.93760 0.41700 0.00160  0.06940  -0.06080 89  LEU A N   
681  C CA  . LEU A 89  ? 0.70960 1.03220 0.46770 -0.00020 0.06840  -0.06420 89  LEU A CA  
682  C C   . LEU A 89  ? 0.72620 1.04820 0.48160 0.00220  0.06790  -0.08900 89  LEU A C   
683  O O   . LEU A 89  ? 0.67830 0.98150 0.43960 0.00190  0.06150  -0.09540 89  LEU A O   
684  C CB  . LEU A 89  ? 0.70960 1.03320 0.46160 -0.00460 0.06000  -0.04770 89  LEU A CB  
685  C CG  . LEU A 89  ? 0.69280 1.01440 0.45100 -0.00700 0.06020  -0.02360 89  LEU A CG  
686  C CD1 . LEU A 89  ? 0.69220 1.01160 0.44790 -0.01090 0.05190  -0.00780 89  LEU A CD1 
687  C CD2 . LEU A 89  ? 0.71030 1.05820 0.46040 -0.00730 0.06760  -0.01680 89  LEU A CD2 
688  N N   . LYS A 90  ? 0.72140 1.06300 0.46970 0.00460  0.07500  -0.10320 90  LYS A N   
689  C CA  . LYS A 90  ? 0.78990 1.13450 0.53530 0.00660  0.07500  -0.12810 90  LYS A CA  
690  C C   . LYS A 90  ? 0.80960 1.16990 0.53810 0.00290  0.06790  -0.12920 90  LYS A C   
691  O O   . LYS A 90  ? 0.80120 1.18480 0.51490 0.00020  0.06770  -0.11620 90  LYS A O   
692  C CB  . LYS A 90  ? 0.82080 1.18390 0.56360 0.01030  0.08510  -0.14310 90  LYS A CB  
693  C CG  . LYS A 90  ? 0.88880 1.25520 0.63040 0.01250  0.08570  -0.17080 90  LYS A CG  
694  C CD  . LYS A 90  ? 0.95520 1.29050 0.71810 0.01540  0.08410  -0.18240 90  LYS A CD  
695  C CE  . LYS A 90  ? 1.15070 1.48200 0.92830 0.02090  0.09370  -0.19300 90  LYS A CE  
696  N NZ  . LYS A 90  ? 1.10900 1.41210 0.90790 0.02390  0.09210  -0.20510 90  LYS A NZ  
697  N N   . VAL A 91  ? 0.84760 1.19490 0.57960 0.00260  0.06150  -0.14290 91  VAL A N   
698  C CA  . VAL A 91  ? 0.83690 1.19760 0.55510 -0.00100 0.05370  -0.14520 91  VAL A CA  
699  C C   . VAL A 91  ? 0.86310 1.23110 0.57830 0.00040  0.05420  -0.17360 91  VAL A C   
700  O O   . VAL A 91  ? 0.83670 1.19240 0.56480 0.00410  0.05920  -0.19070 91  VAL A O   
701  C CB  . VAL A 91  ? 0.84950 1.18850 0.57500 -0.00380 0.04400  -0.13260 91  VAL A CB  
702  C CG1 . VAL A 91  ? 0.80920 1.14540 0.53590 -0.00570 0.04330  -0.10520 91  VAL A CG1 
703  C CG2 . VAL A 91  ? 0.73260 1.04000 0.47780 -0.00160 0.04250  -0.14310 91  VAL A CG2 
704  N N   . ASP A 92  ? 0.94600 1.33530 0.64470 -0.00280 0.04880  -0.17830 92  ASP A N   
705  C CA  . ASP A 92  ? 0.95280 1.35470 0.64590 -0.00220 0.04870  -0.20580 92  ASP A CA  
706  C C   . ASP A 92  ? 0.97910 1.35640 0.68690 -0.00250 0.04210  -0.22000 92  ASP A C   
707  O O   . ASP A 92  ? 1.01500 1.39750 0.72340 -0.00180 0.04230  -0.24500 92  ASP A O   
708  C CB  . ASP A 92  ? 1.00060 1.43160 0.67480 -0.00580 0.04420  -0.20180 92  ASP A CB  
709  C CG  . ASP A 92  ? 1.00560 1.43640 0.67320 -0.01030 0.03310  -0.18830 92  ASP A CG  
710  O OD1 . ASP A 92  ? 1.00280 1.40990 0.68160 -0.01080 0.02940  -0.17490 92  ASP A OD1 
711  O OD2 . ASP A 92  ? 1.12040 1.57030 0.77760 -0.01320 0.02770  -0.18720 92  ASP A OD2 
712  N N   . THR A 93  ? 0.89170 1.24450 0.61080 -0.00390 0.03600  -0.20460 93  THR A N   
713  C CA  . THR A 93  ? 0.89330 1.22240 0.62710 -0.00460 0.02940  -0.21400 93  THR A CA  
714  C C   . THR A 93  ? 0.83150 1.12900 0.58730 -0.00150 0.03260  -0.20910 93  THR A C   
715  O O   . THR A 93  ? 0.79220 1.08010 0.55080 -0.00150 0.03310  -0.18790 93  THR A O   
716  C CB  . THR A 93  ? 0.85730 1.18670 0.58520 -0.00920 0.01890  -0.19940 93  THR A CB  
717  O OG1 . THR A 93  ? 0.95950 1.32140 0.66550 -0.01210 0.01620  -0.19850 93  THR A OG1 
718  C CG2 . THR A 93  ? 0.88850 1.19860 0.62990 -0.01040 0.01190  -0.21130 93  THR A CG2 
719  N N   . ALA A 94  ? 0.79400 1.07560 0.56610 0.00110  0.03450  -0.22810 94  ALA A N   
720  C CA  . ALA A 94  ? 0.77070 1.02220 0.56410 0.00360  0.03600  -0.22240 94  ALA A CA  
721  C C   . ALA A 94  ? 0.76800 1.00210 0.56780 0.00050  0.02690  -0.21280 94  ALA A C   
722  O O   . ALA A 94  ? 0.78250 1.02230 0.57810 -0.00240 0.02030  -0.22170 94  ALA A O   
723  C CB  . ALA A 94  ? 0.75270 0.99380 0.56320 0.00760  0.04120  -0.24470 94  ALA A CB  
724  N N   . ASN A 95  ? 0.71590 0.93080 0.52470 0.00100  0.02630  -0.19390 95  ASN A N   
725  C CA  . ASN A 95  ? 0.73320 0.93060 0.54950 -0.00150 0.01870  -0.18410 95  ASN A CA  
726  C C   . ASN A 95  ? 0.73340 0.91410 0.56670 -0.00080 0.01650  -0.20060 95  ASN A C   
727  O O   . ASN A 95  ? 0.75500 0.91890 0.60490 0.00260  0.02110  -0.20490 95  ASN A O   
728  C CB  . ASN A 95  ? 0.71020 0.89100 0.53390 -0.00050 0.02000  -0.16350 95  ASN A CB  
729  C CG  . ASN A 95  ? 0.71720 0.88220 0.54720 -0.00300 0.01260  -0.15170 95  ASN A CG  
730  O OD1 . ASN A 95  ? 0.71800 0.88170 0.54960 -0.00520 0.00660  -0.15910 95  ASN A OD1 
731  N ND2 . ASN A 95  ? 0.63640 0.78870 0.47140 -0.00250 0.01340  -0.13390 95  ASN A ND2 
732  N N   . PRO A 96  ? 0.71900 0.90380 0.55030 -0.00400 0.00950  -0.20930 96  PRO A N   
733  C CA  . PRO A 96  ? 0.73210 0.90000 0.58230 -0.00370 0.00740  -0.22430 96  PRO A CA  
734  C C   . PRO A 96  ? 0.73500 0.87640 0.60270 -0.00300 0.00600  -0.21200 96  PRO A C   
735  O O   . PRO A 96  ? 0.77750 0.90280 0.66410 -0.00170 0.00660  -0.22220 96  PRO A O   
736  C CB  . PRO A 96  ? 0.74760 0.92850 0.58950 -0.00810 -0.00080 -0.23290 96  PRO A CB  
737  C CG  . PRO A 96  ? 0.77360 0.96910 0.59670 -0.01080 -0.00480 -0.21320 96  PRO A CG  
738  C CD  . PRO A 96  ? 0.75750 0.96230 0.57080 -0.00810 0.00290  -0.20450 96  PRO A CD  
739  N N   . LYS A 97  ? 0.71190 0.84850 0.57510 -0.00360 0.00470  -0.19070 97  LYS A N   
740  C CA  . LYS A 97  ? 0.73990 0.85340 0.61790 -0.00290 0.00370  -0.17880 97  LYS A CA  
741  C C   . LYS A 97  ? 0.70380 0.80710 0.58880 0.00090  0.01060  -0.17080 97  LYS A C   
742  O O   . LYS A 97  ? 0.69520 0.78340 0.58780 0.00130  0.01000  -0.15740 97  LYS A O   
743  C CB  . LYS A 97  ? 0.72500 0.83840 0.59590 -0.00600 -0.00250 -0.16130 97  LYS A CB  
744  C CG  . LYS A 97  ? 0.83600 0.95420 0.70580 -0.00980 -0.01050 -0.16680 97  LYS A CG  
745  C CD  . LYS A 97  ? 0.97050 1.11180 0.82020 -0.01260 -0.01430 -0.16170 97  LYS A CD  
746  C CE  . LYS A 97  ? 0.90860 1.04830 0.75450 -0.01460 -0.01910 -0.14130 97  LYS A CE  
747  N NZ  . LYS A 97  ? 0.96630 1.09240 0.82450 -0.01630 -0.02490 -0.14010 97  LYS A NZ  
748  N N   . THR A 98  ? 0.71220 0.82410 0.59510 0.00360  0.01710  -0.17900 98  THR A N   
749  C CA  . THR A 98  ? 0.70160 0.80480 0.59220 0.00730  0.02350  -0.17190 98  THR A CA  
750  C C   . THR A 98  ? 0.70780 0.78890 0.62040 0.00950  0.02410  -0.17380 98  THR A C   
751  O O   . THR A 98  ? 0.65050 0.72710 0.57530 0.01060  0.02470  -0.18980 98  THR A O   
752  C CB  . THR A 98  ? 0.69640 0.81370 0.58300 0.01020  0.03060  -0.18280 98  THR A CB  
753  O OG1 . THR A 98  ? 0.70290 0.84280 0.56880 0.00790  0.03010  -0.18090 98  THR A OG1 
754  C CG2 . THR A 98  ? 0.68740 0.79760 0.58140 0.01360  0.03660  -0.17340 98  THR A CG2 
755  N N   . PRO A 99  ? 0.67480 0.74240 0.59370 0.01020  0.02400  -0.15820 99  PRO A N   
756  C CA  . PRO A 99  ? 0.66700 0.71540 0.60620 0.01250  0.02510  -0.15790 99  PRO A CA  
757  C C   . PRO A 99  ? 0.68090 0.72760 0.63040 0.01710  0.03210  -0.16240 99  PRO A C   
758  O O   . PRO A 99  ? 0.65150 0.71110 0.59200 0.01840  0.03630  -0.16400 99  PRO A O   
759  C CB  . PRO A 99  ? 0.69960 0.73890 0.63750 0.01130  0.02250  -0.13900 99  PRO A CB  
760  C CG  . PRO A 99  ? 0.64150 0.69420 0.56230 0.01030  0.02370  -0.12940 99  PRO A CG  
761  C CD  . PRO A 99  ? 0.66400 0.73410 0.57150 0.00850  0.02250  -0.13990 99  PRO A CD  
762  N N   . LYS A 100 ? 0.68190 0.71330 0.65180 0.01960  0.03340  -0.16410 100 LYS A N   
763  C CA  . LYS A 100 ? 0.71100 0.73920 0.69210 0.02410  0.03960  -0.16280 100 LYS A CA  
764  C C   . LYS A 100 ? 0.68960 0.71930 0.66110 0.02380  0.04000  -0.14490 100 LYS A C   
765  O O   . LYS A 100 ? 0.60480 0.62860 0.57200 0.02120  0.03570  -0.13290 100 LYS A O   
766  C CB  . LYS A 100 ? 0.75100 0.76240 0.75620 0.02670  0.04030  -0.16390 100 LYS A CB  
767  C CG  . LYS A 100 ? 1.01500 1.02100 1.03150 0.02550  0.03780  -0.17820 100 LYS A CG  
768  C CD  . LYS A 100 ? 1.18580 1.17410 1.22670 0.02720  0.03760  -0.17420 100 LYS A CD  
769  C CE  . LYS A 100 ? 1.07970 1.06090 1.13240 0.02470  0.03350  -0.18490 100 LYS A CE  
770  N NZ  . LYS A 100 ? 1.05530 1.04100 1.11590 0.02540  0.03530  -0.20670 100 LYS A NZ  
771  N N   . TYR A 101 ? 0.62620 0.66580 0.59280 0.02590  0.04500  -0.14380 101 TYR A N   
772  C CA  . TYR A 101 ? 0.60330 0.64460 0.56160 0.02490  0.04480  -0.12740 101 TYR A CA  
773  C C   . TYR A 101 ? 0.60420 0.64910 0.56910 0.02870  0.05070  -0.12510 101 TYR A C   
774  O O   . TYR A 101 ? 0.62430 0.67430 0.59610 0.03190  0.05560  -0.13680 101 TYR A O   
775  C CB  . TYR A 101 ? 0.60140 0.65590 0.53920 0.02110  0.04230  -0.12290 101 TYR A CB  
776  C CG  . TYR A 101 ? 0.59820 0.67050 0.52680 0.02210  0.04720  -0.13000 101 TYR A CG  
777  C CD1 . TYR A 101 ? 0.61340 0.69300 0.53930 0.02340  0.05160  -0.12200 101 TYR A CD1 
778  C CD2 . TYR A 101 ? 0.60600 0.68850 0.52890 0.02170  0.04750  -0.14520 101 TYR A CD2 
779  C CE1 . TYR A 101 ? 0.59420 0.69150 0.51220 0.02440  0.05670  -0.12860 101 TYR A CE1 
780  C CE2 . TYR A 101 ? 0.66780 0.76860 0.58140 0.02270  0.05240  -0.15240 101 TYR A CE2 
781  C CZ  . TYR A 101 ? 0.60860 0.71650 0.51990 0.02410  0.05720  -0.14340 101 TYR A CZ  
782  O OH  . TYR A 101 ? 0.69910 0.82600 0.60180 0.02530  0.06280  -0.15010 101 TYR A OH  
783  N N   . LYS A 102 ? 0.60370 0.64670 0.56670 0.02820  0.05030  -0.11030 102 LYS A N   
784  C CA  . LYS A 102 ? 0.63590 0.68660 0.60070 0.03060  0.05540  -0.10670 102 LYS A CA  
785  C C   . LYS A 102 ? 0.58040 0.63610 0.53340 0.02750  0.05370  -0.09230 102 LYS A C   
786  O O   . LYS A 102 ? 0.52810 0.57850 0.47480 0.02420  0.04870  -0.08440 102 LYS A O   
787  C CB  . LYS A 102 ? 0.64190 0.68340 0.62630 0.03490  0.05800  -0.10540 102 LYS A CB  
788  C CG  . LYS A 102 ? 0.67510 0.70290 0.66610 0.03410  0.05360  -0.09410 102 LYS A CG  
789  C CD  . LYS A 102 ? 0.79700 0.81880 0.80650 0.03830  0.05620  -0.09030 102 LYS A CD  
790  C CE  . LYS A 102 ? 0.97420 0.99310 1.00030 0.04250  0.05990  -0.10310 102 LYS A CE  
791  N NZ  . LYS A 102 ? 1.00490 1.01470 1.05170 0.04630  0.06070  -0.09740 102 LYS A NZ  
792  N N   . PHE A 103 ? 0.52930 0.59630 0.48000 0.02850  0.05810  -0.08950 103 PHE A N   
793  C CA  . PHE A 103 ? 0.53080 0.60200 0.47440 0.02580  0.05700  -0.07580 103 PHE A CA  
794  C C   . PHE A 103 ? 0.55410 0.61820 0.51060 0.02800  0.05770  -0.06840 103 PHE A C   
795  O O   . PHE A 103 ? 0.54820 0.61480 0.51560 0.03190  0.06220  -0.07270 103 PHE A O   
796  C CB  . PHE A 103 ? 0.50000 0.58910 0.43450 0.02540  0.06150  -0.07590 103 PHE A CB  
797  C CG  . PHE A 103 ? 0.54530 0.64490 0.46530 0.02300  0.06070  -0.08140 103 PHE A CG  
798  C CD1 . PHE A 103 ? 0.56650 0.65880 0.48120 0.02040  0.05490  -0.08240 103 PHE A CD1 
799  C CD2 . PHE A 103 ? 0.56800 0.68570 0.47970 0.02320  0.06560  -0.08510 103 PHE A CD2 
800  C CE1 . PHE A 103 ? 0.56000 0.66370 0.46090 0.01800  0.05350  -0.08680 103 PHE A CE1 
801  C CE2 . PHE A 103 ? 0.58180 0.71170 0.47890 0.02090  0.06460  -0.08970 103 PHE A CE2 
802  C CZ  . PHE A 103 ? 0.61710 0.74010 0.50880 0.01830  0.05840  -0.09040 103 PHE A CZ  
803  N N   . VAL A 104 ? 0.48230 0.53950 0.43760 0.02540  0.05350  -0.05730 104 VAL A N   
804  C CA  . VAL A 104 ? 0.50020 0.55250 0.46640 0.02700  0.05340  -0.04990 104 VAL A CA  
805  C C   . VAL A 104 ? 0.54160 0.59800 0.50180 0.02340  0.05150  -0.03870 104 VAL A C   
806  O O   . VAL A 104 ? 0.56670 0.62380 0.51640 0.01950  0.04860  -0.03490 104 VAL A O   
807  C CB  . VAL A 104 ? 0.54580 0.58400 0.52040 0.02780  0.04980  -0.04820 104 VAL A CB  
808  C CG1 . VAL A 104 ? 0.58100 0.61400 0.56370 0.03090  0.05130  -0.05920 104 VAL A CG1 
809  C CG2 . VAL A 104 ? 0.54370 0.57590 0.50950 0.02390  0.04460  -0.04300 104 VAL A CG2 
810  N N   . ARG A 105 ? 0.47590 0.53480 0.44410 0.02460  0.05290  -0.03310 105 ARG A N   
811  C CA  . ARG A 105 ? 0.52090 0.58220 0.48630 0.02100  0.05050  -0.02300 105 ARG A CA  
812  C C   . ARG A 105 ? 0.57900 0.63040 0.55030 0.02080  0.04640  -0.01780 105 ARG A C   
813  O O   . ARG A 105 ? 0.59450 0.64450 0.57630 0.02400  0.04720  -0.01740 105 ARG A O   
814  C CB  . ARG A 105 ? 0.56100 0.63430 0.53080 0.02180  0.05480  -0.02050 105 ARG A CB  
815  C CG  . ARG A 105 ? 0.57050 0.64710 0.53900 0.01780  0.05250  -0.01070 105 ARG A CG  
816  C CD  . ARG A 105 ? 0.51980 0.61060 0.49160 0.01820  0.05750  -0.00900 105 ARG A CD  
817  N NE  . ARG A 105 ? 0.57050 0.66380 0.54320 0.01380  0.05490  0.00050  105 ARG A NE  
818  C CZ  . ARG A 105 ? 0.59470 0.69150 0.56020 0.00950  0.05400  0.00540  105 ARG A CZ  
819  N NH1 . ARG A 105 ? 0.52750 0.62790 0.48310 0.00900  0.05550  0.00270  105 ARG A NH1 
820  N NH2 . ARG A 105 ? 0.55840 0.65550 0.52740 0.00560  0.05120  0.01330  105 ARG A NH2 
821  N N   . ILE A 106 ? 0.52510 0.57090 0.49010 0.01730  0.04210  -0.01340 106 ILE A N   
822  C CA  . ILE A 106 ? 0.57740 0.61530 0.54680 0.01710  0.03840  -0.00930 106 ILE A CA  
823  C C   . ILE A 106 ? 0.59670 0.63940 0.56880 0.01500  0.03710  -0.00230 106 ILE A C   
824  O O   . ILE A 106 ? 0.58910 0.63940 0.55900 0.01270  0.03830  0.00020  106 ILE A O   
825  C CB  . ILE A 106 ? 0.55840 0.58750 0.52100 0.01460  0.03460  -0.00910 106 ILE A CB  
826  C CG1 . ILE A 106 ? 0.51320 0.54520 0.46720 0.01040  0.03310  -0.00610 106 ILE A CG1 
827  C CG2 . ILE A 106 ? 0.64350 0.66710 0.60660 0.01690  0.03520  -0.01600 106 ILE A CG2 
828  C CD1 . ILE A 106 ? 0.63980 0.66280 0.59030 0.00810  0.02880  -0.00410 106 ILE A CD1 
829  N N   . GLN A 107 ? 0.54590 0.58480 0.52310 0.01550  0.03440  0.00100  107 GLN A N   
830  C CA  . GLN A 107 ? 0.57810 0.62080 0.55830 0.01340  0.03190  0.00670  107 GLN A CA  
831  C C   . GLN A 107 ? 0.52020 0.55740 0.49440 0.00940  0.02780  0.00860  107 GLN A C   
832  O O   . GLN A 107 ? 0.53510 0.56430 0.50480 0.00940  0.02640  0.00660  107 GLN A O   
833  C CB  . GLN A 107 ? 0.65460 0.69830 0.64350 0.01630  0.03100  0.00910  107 GLN A CB  
834  C CG  . GLN A 107 ? 0.80310 0.85070 0.80190 0.02130  0.03470  0.00780  107 GLN A CG  
835  C CD  . GLN A 107 ? 1.03330 1.08040 1.04080 0.02420  0.03290  0.01180  107 GLN A CD  
836  O OE1 . GLN A 107 ? 0.93220 0.98230 0.93960 0.02230  0.02930  0.01680  107 GLN A OE1 
837  N NE2 . GLN A 107 ? 1.15670 1.20030 1.17220 0.02860  0.03530  0.00970  107 GLN A NE2 
838  N N   . PRO A 108 ? 0.51870 0.56030 0.49430 0.00620  0.02580  0.01210  108 PRO A N   
839  C CA  . PRO A 108 ? 0.48050 0.51720 0.45290 0.00270  0.02180  0.01310  108 PRO A CA  
840  C C   . PRO A 108 ? 0.48810 0.51980 0.46020 0.00460  0.01980  0.01250  108 PRO A C   
841  O O   . PRO A 108 ? 0.47670 0.51160 0.45380 0.00770  0.02030  0.01370  108 PRO A O   
842  C CB  . PRO A 108 ? 0.52880 0.57270 0.50620 -0.00030 0.02020  0.01610  108 PRO A CB  
843  C CG  . PRO A 108 ? 0.50570 0.55710 0.48650 0.00020  0.02360  0.01740  108 PRO A CG  
844  C CD  . PRO A 108 ? 0.53210 0.58370 0.51340 0.00530  0.02730  0.01490  108 PRO A CD  
845  N N   . GLY A 109 ? 0.47820 0.50280 0.44540 0.00300  0.01780  0.01120  109 GLY A N   
846  C CA  . GLY A 109 ? 0.42800 0.44840 0.39430 0.00440  0.01630  0.01090  109 GLY A CA  
847  C C   . GLY A 109 ? 0.53790 0.55170 0.50280 0.00710  0.01800  0.00890  109 GLY A C   
848  O O   . GLY A 109 ? 0.53410 0.54320 0.49780 0.00780  0.01690  0.00880  109 GLY A O   
849  N N   . GLN A 110 ? 0.48610 0.50010 0.45140 0.00860  0.02070  0.00690  110 GLN A N   
850  C CA  . GLN A 110 ? 0.50720 0.51510 0.47200 0.01080  0.02190  0.00360  110 GLN A CA  
851  C C   . GLN A 110 ? 0.50460 0.50750 0.46260 0.00820  0.02060  0.00160  110 GLN A C   
852  O O   . GLN A 110 ? 0.46790 0.47280 0.42240 0.00530  0.01980  0.00290  110 GLN A O   
853  C CB  . GLN A 110 ? 0.50760 0.51850 0.47650 0.01380  0.02540  0.00050  110 GLN A CB  
854  C CG  . GLN A 110 ? 0.56700 0.58140 0.54530 0.01730  0.02680  0.00250  110 GLN A CG  
855  C CD  . GLN A 110 ? 0.75400 0.76370 0.73680 0.01910  0.02530  0.00520  110 GLN A CD  
856  O OE1 . GLN A 110 ? 0.70490 0.70780 0.68950 0.02030  0.02580  0.00260  110 GLN A OE1 
857  N NE2 . GLN A 110 ? 0.58010 0.59420 0.56500 0.01890  0.02340  0.01060  110 GLN A NE2 
858  N N   . THR A 111 ? 0.47880 0.47530 0.43640 0.00930  0.02020  -0.00070 111 THR A N   
859  C CA  . THR A 111 ? 0.46600 0.45810 0.41830 0.00710  0.01860  -0.00200 111 THR A CA  
860  C C   . THR A 111 ? 0.47090 0.46320 0.42140 0.00800  0.01990  -0.00660 111 THR A C   
861  O O   . THR A 111 ? 0.50470 0.49800 0.45930 0.01070  0.02210  -0.00990 111 THR A O   
862  C CB  . THR A 111 ? 0.46620 0.45190 0.41960 0.00720  0.01680  -0.00150 111 THR A CB  
863  O OG1 . THR A 111 ? 0.48280 0.46690 0.44200 0.01030  0.01830  -0.00240 111 THR A OG1 
864  C CG2 . THR A 111 ? 0.49150 0.47880 0.44490 0.00580  0.01550  0.00180  111 THR A CG2 
865  N N   . PHE A 112 ? 0.44850 0.43980 0.39350 0.00580  0.01820  -0.00710 112 PHE A N   
866  C CA  . PHE A 112 ? 0.47760 0.47000 0.41980 0.00620  0.01860  -0.01200 112 PHE A CA  
867  C C   . PHE A 112 ? 0.48930 0.47960 0.42690 0.00370  0.01560  -0.01080 112 PHE A C   
868  O O   . PHE A 112 ? 0.51600 0.50450 0.45310 0.00170  0.01370  -0.00610 112 PHE A O   
869  C CB  . PHE A 112 ? 0.47770 0.47920 0.41690 0.00650  0.02120  -0.01370 112 PHE A CB  
870  C CG  . PHE A 112 ? 0.49790 0.50460 0.43340 0.00380  0.02080  -0.00790 112 PHE A CG  
871  C CD1 . PHE A 112 ? 0.52410 0.53260 0.46350 0.00360  0.02170  -0.00400 112 PHE A CD1 
872  C CD2 . PHE A 112 ? 0.49890 0.50940 0.42840 0.00130  0.01940  -0.00590 112 PHE A CD2 
873  C CE1 . PHE A 112 ? 0.58130 0.59480 0.51930 0.00070  0.02140  0.00130  112 PHE A CE1 
874  C CE2 . PHE A 112 ? 0.56110 0.57680 0.48940 -0.00130 0.01930  0.00070  112 PHE A CE2 
875  C CZ  . PHE A 112 ? 0.55090 0.56750 0.48380 -0.00170 0.02030  0.00380  112 PHE A CZ  
876  N N   . SER A 113 ? 0.50940 0.50010 0.44500 0.00390  0.01490  -0.01550 113 SER A N   
877  C CA  . SER A 113 ? 0.51920 0.50960 0.45080 0.00180  0.01180  -0.01460 113 SER A CA  
878  C C   . SER A 113 ? 0.48760 0.48750 0.41200 0.00010  0.01170  -0.01300 113 SER A C   
879  O O   . SER A 113 ? 0.51130 0.51800 0.43300 0.00110  0.01410  -0.01690 113 SER A O   
880  C CB  . SER A 113 ? 0.52980 0.51700 0.46360 0.00260  0.01060  -0.02100 113 SER A CB  
881  O OG  . SER A 113 ? 0.49520 0.47410 0.43660 0.00410  0.01090  -0.02090 113 SER A OG  
882  N N   . VAL A 114 ? 0.49220 0.49290 0.41440 -0.00240 0.00900  -0.00710 114 VAL A N   
883  C CA  . VAL A 114 ? 0.50930 0.51960 0.42550 -0.00440 0.00840  -0.00280 114 VAL A CA  
884  C C   . VAL A 114 ? 0.52210 0.53420 0.43510 -0.00540 0.00490  -0.00360 114 VAL A C   
885  O O   . VAL A 114 ? 0.52360 0.52850 0.44080 -0.00590 0.00210  -0.00200 114 VAL A O   
886  C CB  . VAL A 114 ? 0.49060 0.50010 0.40980 -0.00650 0.00770  0.00620  114 VAL A CB  
887  C CG1 . VAL A 114 ? 0.47580 0.49480 0.39030 -0.00870 0.00640  0.01220  114 VAL A CG1 
888  C CG2 . VAL A 114 ? 0.51450 0.52450 0.43690 -0.00600 0.01090  0.00720  114 VAL A CG2 
889  N N   . LEU A 115 ? 0.45450 0.47690 0.36040 -0.00570 0.00490  -0.00680 115 LEU A N   
890  C CA  . LEU A 115 ? 0.48100 0.50870 0.38270 -0.00730 0.00080  -0.00590 115 LEU A CA  
891  C C   . LEU A 115 ? 0.54340 0.58090 0.44080 -0.00950 -0.00010 0.00420  115 LEU A C   
892  O O   . LEU A 115 ? 0.52230 0.57230 0.41250 -0.00990 0.00180  0.00450  115 LEU A O   
893  C CB  . LEU A 115 ? 0.47310 0.50710 0.36980 -0.00650 0.00080  -0.01650 115 LEU A CB  
894  C CG  . LEU A 115 ? 0.52650 0.56830 0.41800 -0.00830 -0.00380 -0.01690 115 LEU A CG  
895  C CD1 . LEU A 115 ? 0.56140 0.59190 0.46090 -0.00860 -0.00770 -0.01590 115 LEU A CD1 
896  C CD2 . LEU A 115 ? 0.53770 0.58870 0.42310 -0.00780 -0.00340 -0.02860 115 LEU A CD2 
897  N N   . ALA A 116 ? 0.53000 0.56240 0.43310 -0.01090 -0.00270 0.01290  116 ALA A N   
898  C CA  . ALA A 116 ? 0.51900 0.55960 0.42130 -0.01310 -0.00390 0.02430  116 ALA A CA  
899  C C   . ALA A 116 ? 0.55770 0.61080 0.45240 -0.01430 -0.00720 0.02590  116 ALA A C   
900  O O   . ALA A 116 ? 0.55750 0.60840 0.45270 -0.01420 -0.01080 0.02250  116 ALA A O   
901  C CB  . ALA A 116 ? 0.53610 0.56720 0.44870 -0.01410 -0.00590 0.03240  116 ALA A CB  
902  N N   . CYS A 117 ? 0.53240 0.60010 0.42000 -0.01540 -0.00600 0.03100  117 CYS A N   
903  C CA  . CYS A 117 ? 0.52610 0.60940 0.40440 -0.01660 -0.00890 0.03240  117 CYS A CA  
904  C C   . CYS A 117 ? 0.56160 0.65650 0.43960 -0.01880 -0.00970 0.04740  117 CYS A C   
905  O O   . CYS A 117 ? 0.57400 0.66880 0.45570 -0.01930 -0.00630 0.05410  117 CYS A O   
906  C CB  . CYS A 117 ? 0.59470 0.68970 0.46190 -0.01570 -0.00620 0.02190  117 CYS A CB  
907  S SG  . CYS A 117 ? 0.62620 0.71060 0.49470 -0.01320 -0.00520 0.00410  117 CYS A SG  
908  N N   . TYR A 118 ? 0.57240 0.67840 0.44610 -0.02010 -0.01430 0.05300  118 TYR A N   
909  C CA  . TYR A 118 ? 0.62560 0.74650 0.49750 -0.02220 -0.01560 0.06820  118 TYR A CA  
910  C C   . TYR A 118 ? 0.61330 0.75450 0.47130 -0.02300 -0.01830 0.06600  118 TYR A C   
911  O O   . TYR A 118 ? 0.59620 0.73640 0.45150 -0.02260 -0.02230 0.05760  118 TYR A O   
912  C CB  . TYR A 118 ? 0.61260 0.72560 0.49820 -0.02330 -0.01970 0.08130  118 TYR A CB  
913  C CG  . TYR A 118 ? 0.59060 0.68500 0.48920 -0.02270 -0.01680 0.08130  118 TYR A CG  
914  C CD1 . TYR A 118 ? 0.61070 0.70630 0.51450 -0.02380 -0.01310 0.08990  118 TYR A CD1 
915  C CD2 . TYR A 118 ? 0.57430 0.65130 0.47940 -0.02100 -0.01740 0.07210  118 TYR A CD2 
916  C CE1 . TYR A 118 ? 0.57100 0.65050 0.48620 -0.02350 -0.01070 0.08810  118 TYR A CE1 
917  C CE2 . TYR A 118 ? 0.56750 0.62970 0.48250 -0.02050 -0.01460 0.07060  118 TYR A CE2 
918  C CZ  . TYR A 118 ? 0.58050 0.64390 0.50080 -0.02180 -0.01160 0.07840  118 TYR A CZ  
919  O OH  . TYR A 118 ? 0.54090 0.59060 0.47090 -0.02150 -0.00940 0.07600  118 TYR A OH  
920  N N   . ASN A 119 ? 0.61440 0.77450 0.46330 -0.02410 -0.01580 0.07240  119 ASN A N   
921  C CA  . ASN A 119 ? 0.64000 0.82340 0.47390 -0.02510 -0.01790 0.07130  119 ASN A CA  
922  C C   . ASN A 119 ? 0.61560 0.79930 0.44050 -0.02360 -0.01780 0.05080  119 ASN A C   
923  O O   . ASN A 119 ? 0.60340 0.79840 0.42030 -0.02440 -0.02240 0.04610  119 ASN A O   
924  C CB  . ASN A 119 ? 0.66910 0.86010 0.50530 -0.02680 -0.02510 0.08410  119 ASN A CB  
925  C CG  . ASN A 119 ? 0.70380 0.89170 0.55300 -0.02800 -0.02550 0.10410  119 ASN A CG  
926  O OD1 . ASN A 119 ? 0.74690 0.91940 0.61030 -0.02790 -0.02860 0.10960  119 ASN A OD1 
927  N ND2 . ASN A 119 ? 0.68780 0.88920 0.53370 -0.02920 -0.02170 0.11440  119 ASN A ND2 
928  N N   . GLY A 120 ? 0.59920 0.77050 0.42660 -0.02160 -0.01270 0.03870  120 GLY A N   
929  C CA  . GLY A 120 ? 0.58360 0.75320 0.40570 -0.02000 -0.01220 0.01940  120 GLY A CA  
930  C C   . GLY A 120 ? 0.62820 0.78140 0.45850 -0.01960 -0.01680 0.01240  120 GLY A C   
931  O O   . GLY A 120 ? 0.62300 0.77370 0.45140 -0.01850 -0.01680 -0.00340 120 GLY A O   
932  N N   . SER A 121 ? 0.59200 0.73450 0.43260 -0.02030 -0.02060 0.02350  121 SER A N   
933  C CA  . SER A 121 ? 0.62440 0.75330 0.47310 -0.02000 -0.02500 0.01770  121 SER A CA  
934  C C   . SER A 121 ? 0.61340 0.71990 0.47500 -0.01840 -0.02240 0.01770  121 SER A C   
935  O O   . SER A 121 ? 0.59360 0.69450 0.46210 -0.01870 -0.02140 0.02960  121 SER A O   
936  C CB  . SER A 121 ? 0.60540 0.74020 0.45660 -0.02180 -0.03180 0.02900  121 SER A CB  
937  O OG  . SER A 121 ? 0.70100 0.85650 0.53990 -0.02330 -0.03520 0.02630  121 SER A OG  
938  N N   . PRO A 122 ? 0.64700 0.74120 0.51270 -0.01680 -0.02120 0.00490  122 PRO A N   
939  C CA  . PRO A 122 ? 0.63650 0.71090 0.51420 -0.01530 -0.01930 0.00530  122 PRO A CA  
940  C C   . PRO A 122 ? 0.61220 0.67910 0.49910 -0.01610 -0.02320 0.01540  122 PRO A C   
941  O O   . PRO A 122 ? 0.61900 0.68980 0.50650 -0.01710 -0.02830 0.01620  122 PRO A O   
942  C CB  . PRO A 122 ? 0.61370 0.68000 0.49390 -0.01400 -0.01880 -0.00920 122 PRO A CB  
943  C CG  . PRO A 122 ? 0.66120 0.74160 0.53080 -0.01390 -0.01730 -0.01910 122 PRO A CG  
944  C CD  . PRO A 122 ? 0.65110 0.75020 0.51090 -0.01610 -0.02070 -0.01090 122 PRO A CD  
945  N N   . SER A 123 ? 0.59580 0.65210 0.49080 -0.01560 -0.02080 0.02250  123 SER A N   
946  C CA  . SER A 123 ? 0.61330 0.66090 0.51900 -0.01590 -0.02380 0.03010  123 SER A CA  
947  C C   . SER A 123 ? 0.64030 0.67070 0.55540 -0.01430 -0.02170 0.02520  123 SER A C   
948  O O   . SER A 123 ? 0.58480 0.60850 0.50840 -0.01410 -0.02430 0.02770  123 SER A O   
949  C CB  . SER A 123 ? 0.67700 0.72800 0.58690 -0.01720 -0.02400 0.04410  123 SER A CB  
950  O OG  . SER A 123 ? 0.70650 0.75130 0.61900 -0.01670 -0.01930 0.04470  123 SER A OG  
951  N N   . GLY A 124 ? 0.58290 0.60720 0.49730 -0.01300 -0.01710 0.01910  124 GLY A N   
952  C CA  . GLY A 124 ? 0.57380 0.58400 0.49620 -0.01150 -0.01530 0.01520  124 GLY A CA  
953  C C   . GLY A 124 ? 0.58320 0.58980 0.50350 -0.01000 -0.01070 0.00850  124 GLY A C   
954  O O   . GLY A 124 ? 0.51940 0.53350 0.43340 -0.01000 -0.00830 0.00750  124 GLY A O   
955  N N   . VAL A 125 ? 0.50030 0.49650 0.42660 -0.00850 -0.00940 0.00430  125 VAL A N   
956  C CA  . VAL A 125 ? 0.51240 0.50530 0.43840 -0.00680 -0.00540 -0.00130 125 VAL A CA  
957  C C   . VAL A 125 ? 0.55020 0.53400 0.48270 -0.00600 -0.00360 0.00090  125 VAL A C   
958  O O   . VAL A 125 ? 0.53680 0.51430 0.47500 -0.00590 -0.00490 0.00190  125 VAL A O   
959  C CB  . VAL A 125 ? 0.51560 0.50770 0.44150 -0.00570 -0.00540 -0.01040 125 VAL A CB  
960  C CG1 . VAL A 125 ? 0.60080 0.58540 0.53400 -0.00540 -0.00740 -0.01160 125 VAL A CG1 
961  C CG2 . VAL A 125 ? 0.55040 0.53930 0.47790 -0.00360 -0.00150 -0.01520 125 VAL A CG2 
962  N N   . TYR A 126 ? 0.47440 0.45840 0.40600 -0.00540 -0.00050 0.00110  126 TYR A N   
963  C CA  . TYR A 126 ? 0.49870 0.47610 0.43570 -0.00490 0.00090  0.00240  126 TYR A CA  
964  C C   . TYR A 126 ? 0.54640 0.52490 0.48250 -0.00350 0.00420  0.00010  126 TYR A C   
965  O O   . TYR A 126 ? 0.50520 0.48990 0.43730 -0.00330 0.00570  -0.00120 126 TYR A O   
966  C CB  . TYR A 126 ? 0.49630 0.47290 0.43650 -0.00670 -0.00020 0.00870  126 TYR A CB  
967  C CG  . TYR A 126 ? 0.50880 0.49250 0.44630 -0.00840 0.00020  0.01340  126 TYR A CG  
968  C CD1 . TYR A 126 ? 0.57680 0.56230 0.51430 -0.00850 0.00260  0.01390  126 TYR A CD1 
969  C CD2 . TYR A 126 ? 0.54780 0.53730 0.48330 -0.00980 -0.00210 0.01830  126 TYR A CD2 
970  C CE1 . TYR A 126 ? 0.54050 0.53330 0.47650 -0.01020 0.00320  0.01900  126 TYR A CE1 
971  C CE2 . TYR A 126 ? 0.56950 0.56710 0.50270 -0.01150 -0.00150 0.02410  126 TYR A CE2 
972  C CZ  . TYR A 126 ? 0.51890 0.51760 0.45290 -0.01170 0.00130  0.02440  126 TYR A CZ  
973  O OH  . TYR A 126 ? 0.59900 0.60600 0.53210 -0.01350 0.00230  0.03070  126 TYR A OH  
974  N N   . GLN A 127 ? 0.49310 0.46660 0.43330 -0.00260 0.00530  -0.00020 127 GLN A N   
975  C CA  . GLN A 127 ? 0.54840 0.52360 0.48910 -0.00130 0.00800  -0.00120 127 GLN A CA  
976  C C   . GLN A 127 ? 0.54180 0.51980 0.48270 -0.00290 0.00830  0.00230  127 GLN A C   
977  O O   . GLN A 127 ? 0.53790 0.51350 0.48130 -0.00460 0.00690  0.00490  127 GLN A O   
978  C CB  . GLN A 127 ? 0.59730 0.56810 0.54210 0.00040  0.00890  -0.00230 127 GLN A CB  
979  C CG  . GLN A 127 ? 0.59780 0.56630 0.54480 0.00230  0.00940  -0.00540 127 GLN A CG  
980  C CD  . GLN A 127 ? 0.57580 0.54760 0.52290 0.00390  0.01140  -0.00840 127 GLN A CD  
981  O OE1 . GLN A 127 ? 0.58260 0.55660 0.52730 0.00370  0.01110  -0.01170 127 GLN A OE1 
982  N NE2 . GLN A 127 ? 0.57430 0.54650 0.52520 0.00590  0.01340  -0.00790 127 GLN A NE2 
983  N N   . CYS A 128 ? 0.56360 0.54660 0.50370 -0.00220 0.01040  0.00200  128 CYS A N   
984  C CA  . CYS A 128 ? 0.57780 0.56490 0.51910 -0.00380 0.01100  0.00520  128 CYS A CA  
985  C C   . CYS A 128 ? 0.52950 0.51890 0.47300 -0.00190 0.01290  0.00380  128 CYS A C   
986  O O   . CYS A 128 ? 0.52530 0.51540 0.46880 0.00060  0.01450  0.00100  128 CYS A O   
987  C CB  . CYS A 128 ? 0.50510 0.49970 0.44320 -0.00500 0.01190  0.00770  128 CYS A CB  
988  S SG  . CYS A 128 ? 0.69140 0.68450 0.63070 -0.00810 0.00920  0.01310  128 CYS A SG  
989  N N   . ALA A 129 ? 0.53020 0.52150 0.47660 -0.00330 0.01260  0.00580  129 ALA A N   
990  C CA  . ALA A 129 ? 0.45440 0.45070 0.40320 -0.00190 0.01420  0.00570  129 ALA A CA  
991  C C   . ALA A 129 ? 0.47000 0.47300 0.41980 -0.00380 0.01520  0.00840  129 ALA A C   
992  O O   . ALA A 129 ? 0.51150 0.51450 0.46210 -0.00680 0.01400  0.01110  129 ALA A O   
993  C CB  . ALA A 129 ? 0.46150 0.45730 0.41300 -0.00220 0.01280  0.00580  129 ALA A CB  
994  N N   . MET A 130 ? 0.46990 0.47880 0.42110 -0.00200 0.01750  0.00810  130 MET A N   
995  C CA  . MET A 130 ? 0.45950 0.47630 0.41340 -0.00360 0.01870  0.01110  130 MET A CA  
996  C C   . MET A 130 ? 0.43630 0.45400 0.39530 -0.00550 0.01670  0.01240  130 MET A C   
997  O O   . MET A 130 ? 0.49440 0.51290 0.45530 -0.00360 0.01630  0.01120  130 MET A O   
998  C CB  . MET A 130 ? 0.40080 0.42380 0.35560 -0.00050 0.02220  0.00950  130 MET A CB  
999  C CG  . MET A 130 ? 0.50810 0.54110 0.46710 -0.00170 0.02430  0.01270  130 MET A CG  
1000 S SD  . MET A 130 ? 0.63360 0.67210 0.58800 -0.00380 0.02620  0.01510  130 MET A SD  
1001 C CE  . MET A 130 ? 0.52120 0.55540 0.47710 -0.00830 0.02280  0.01970  130 MET A CE  
1002 N N   . ARG A 131 ? 0.44310 0.46060 0.40480 -0.00930 0.01490  0.01470  131 ARG A N   
1003 C CA  . ARG A 131 ? 0.44200 0.46070 0.40900 -0.01150 0.01260  0.01440  131 ARG A CA  
1004 C C   . ARG A 131 ? 0.49030 0.51800 0.46180 -0.01120 0.01360  0.01570  131 ARG A C   
1005 O O   . ARG A 131 ? 0.50790 0.54100 0.47970 -0.01000 0.01650  0.01770  131 ARG A O   
1006 C CB  . ARG A 131 ? 0.48940 0.50580 0.46110 -0.01590 0.01090  0.01620  131 ARG A CB  
1007 C CG  . ARG A 131 ? 0.49970 0.50820 0.46920 -0.01640 0.00990  0.01610  131 ARG A CG  
1008 C CD  . ARG A 131 ? 0.49130 0.49350 0.45730 -0.01440 0.00850  0.01120  131 ARG A CD  
1009 N NE  . ARG A 131 ? 0.45190 0.45660 0.42150 -0.01550 0.00680  0.00830  131 ARG A NE  
1010 C CZ  . ARG A 131 ? 0.49920 0.50280 0.46600 -0.01400 0.00590  0.00470  131 ARG A CZ  
1011 N NH1 . ARG A 131 ? 0.44900 0.44760 0.41100 -0.01140 0.00660  0.00370  131 ARG A NH1 
1012 N NH2 . ARG A 131 ? 0.48520 0.49380 0.45450 -0.01520 0.00420  0.00210  131 ARG A NH2 
1013 N N   . PRO A 132 ? 0.46090 0.49160 0.43620 -0.01220 0.01120  0.01440  132 PRO A N   
1014 C CA  . PRO A 132 ? 0.51650 0.55690 0.49770 -0.01240 0.01160  0.01640  132 PRO A CA  
1015 C C   . PRO A 132 ? 0.49460 0.53970 0.48130 -0.01550 0.01310  0.02000  132 PRO A C   
1016 O O   . PRO A 132 ? 0.53010 0.58360 0.52060 -0.01450 0.01520  0.02230  132 PRO A O   
1017 C CB  . PRO A 132 ? 0.41840 0.46150 0.40250 -0.01420 0.00780  0.01400  132 PRO A CB  
1018 C CG  . PRO A 132 ? 0.47660 0.51270 0.45400 -0.01230 0.00680  0.01100  132 PRO A CG  
1019 C CD  . PRO A 132 ? 0.47890 0.50600 0.45260 -0.01240 0.00840  0.01100  132 PRO A CD  
1020 N N   . ASN A 133 ? 0.49050 0.53130 0.47880 -0.01910 0.01220  0.02120  133 ASN A N   
1021 C CA  . ASN A 133 ? 0.49510 0.54110 0.48950 -0.02210 0.01380  0.02630  133 ASN A CA  
1022 C C   . ASN A 133 ? 0.51190 0.55900 0.50050 -0.02040 0.01760  0.02960  133 ASN A C   
1023 O O   . ASN A 133 ? 0.49920 0.55010 0.49140 -0.02310 0.01900  0.03490  133 ASN A O   
1024 C CB  . ASN A 133 ? 0.51800 0.55970 0.52000 -0.02710 0.01100  0.02710  133 ASN A CB  
1025 C CG  . ASN A 133 ? 0.50460 0.53640 0.50250 -0.02710 0.01030  0.02670  133 ASN A CG  
1026 O OD1 . ASN A 133 ? 0.48160 0.51020 0.47030 -0.02370 0.01160  0.02590  133 ASN A OD1 
1027 N ND2 . ASN A 133 ? 0.51350 0.54050 0.51940 -0.03090 0.00800  0.02710  133 ASN A ND2 
1028 N N   . PHE A 134 ? 0.44410 0.48860 0.42420 -0.01610 0.01910  0.02660  134 PHE A N   
1029 C CA  . PHE A 134 ? 0.44280 0.49030 0.41670 -0.01400 0.02270  0.02760  134 PHE A CA  
1030 C C   . PHE A 134 ? 0.50820 0.55210 0.47850 -0.01600 0.02210  0.03060  134 PHE A C   
1031 O O   . PHE A 134 ? 0.59210 0.64130 0.55730 -0.01520 0.02480  0.03250  134 PHE A O   
1032 C CB  . PHE A 134 ? 0.48100 0.54070 0.45850 -0.01380 0.02670  0.03090  134 PHE A CB  
1033 C CG  . PHE A 134 ? 0.45600 0.52040 0.43720 -0.01070 0.02800  0.02820  134 PHE A CG  
1034 C CD1 . PHE A 134 ? 0.51950 0.58420 0.49670 -0.00600 0.03060  0.02400  134 PHE A CD1 
1035 C CD2 . PHE A 134 ? 0.52970 0.59830 0.51970 -0.01260 0.02620  0.02980  134 PHE A CD2 
1036 C CE1 . PHE A 134 ? 0.57690 0.64610 0.55970 -0.00280 0.03180  0.02240  134 PHE A CE1 
1037 C CE2 . PHE A 134 ? 0.52990 0.60400 0.52430 -0.00970 0.02710  0.02840  134 PHE A CE2 
1038 C CZ  . PHE A 134 ? 0.57020 0.64450 0.56130 -0.00460 0.03010  0.02520  134 PHE A CZ  
1039 N N   . THR A 135 ? 0.53100 0.56680 0.50360 -0.01840 0.01860  0.03080  135 THR A N   
1040 C CA  . THR A 135 ? 0.43720 0.46820 0.40680 -0.01950 0.01750  0.03340  135 THR A CA  
1041 C C   . THR A 135 ? 0.48140 0.50420 0.44440 -0.01660 0.01610  0.02790  135 THR A C   
1042 O O   . THR A 135 ? 0.43890 0.45910 0.40080 -0.01440 0.01580  0.02290  135 THR A O   
1043 C CB  . THR A 135 ? 0.43960 0.46640 0.41880 -0.02370 0.01480  0.03710  135 THR A CB  
1044 O OG1 . THR A 135 ? 0.46830 0.48820 0.45100 -0.02400 0.01210  0.03150  135 THR A OG1 
1045 C CG2 . THR A 135 ? 0.46110 0.49640 0.44940 -0.02710 0.01620  0.04300  135 THR A CG2 
1046 N N   . ILE A 136 ? 0.43860 0.45840 0.39770 -0.01680 0.01520  0.02950  136 ILE A N   
1047 C CA  . ILE A 136 ? 0.47550 0.48680 0.43090 -0.01490 0.01330  0.02510  136 ILE A CA  
1048 C C   . ILE A 136 ? 0.49920 0.50450 0.45940 -0.01740 0.01060  0.02820  136 ILE A C   
1049 O O   . ILE A 136 ? 0.48240 0.49060 0.44640 -0.01990 0.01030  0.03480  136 ILE A O   
1050 C CB  . ILE A 136 ? 0.53470 0.54780 0.48150 -0.01210 0.01460  0.02250  136 ILE A CB  
1051 C CG1 . ILE A 136 ? 0.54540 0.56350 0.48900 -0.01370 0.01450  0.02760  136 ILE A CG1 
1052 C CG2 . ILE A 136 ? 0.53180 0.55140 0.47620 -0.00940 0.01800  0.01900  136 ILE A CG2 
1053 C CD1 . ILE A 136 ? 0.54650 0.56720 0.48120 -0.01130 0.01510  0.02380  136 ILE A CD1 
1054 N N   . LYS A 137 ? 0.50150 0.49870 0.46260 -0.01660 0.00880  0.02400  137 LYS A N   
1055 C CA  . LYS A 137 ? 0.50870 0.49940 0.47510 -0.01820 0.00640  0.02580  137 LYS A CA  
1056 C C   . LYS A 137 ? 0.56860 0.55790 0.52910 -0.01650 0.00580  0.02620  137 LYS A C   
1057 O O   . LYS A 137 ? 0.50310 0.48720 0.46110 -0.01450 0.00510  0.02170  137 LYS A O   
1058 C CB  . LYS A 137 ? 0.52960 0.51380 0.50060 -0.01820 0.00520  0.02030  137 LYS A CB  
1059 C CG  . LYS A 137 ? 0.56000 0.54740 0.53640 -0.02020 0.00530  0.01900  137 LYS A CG  
1060 C CD  . LYS A 137 ? 0.61580 0.59910 0.59680 -0.02080 0.00380  0.01300  137 LYS A CD  
1061 C CE  . LYS A 137 ? 0.73080 0.71440 0.72320 -0.02470 0.00260  0.01380  137 LYS A CE  
1062 N NZ  . LYS A 137 ? 0.80740 0.79020 0.80320 -0.02560 0.00130  0.00630  137 LYS A NZ  
1063 N N   . GLY A 138 ? 0.51710 0.51220 0.47560 -0.01740 0.00590  0.03220  138 GLY A N   
1064 C CA  . GLY A 138 ? 0.51980 0.51600 0.47210 -0.01620 0.00480  0.03280  138 GLY A CA  
1065 C C   . GLY A 138 ? 0.50570 0.49860 0.46400 -0.01760 0.00210  0.03830  138 GLY A C   
1066 O O   . GLY A 138 ? 0.57370 0.56100 0.54200 -0.01920 0.00110  0.04020  138 GLY A O   
1067 N N   . SER A 139 ? 0.48450 0.48160 0.43740 -0.01720 0.00080  0.04080  139 SER A N   
1068 C CA  . SER A 139 ? 0.48800 0.48440 0.44650 -0.01840 -0.00220 0.04780  139 SER A CA  
1069 C C   . SER A 139 ? 0.50360 0.51220 0.45460 -0.01900 -0.00260 0.05380  139 SER A C   
1070 O O   . SER A 139 ? 0.49260 0.50560 0.43430 -0.01760 -0.00330 0.05000  139 SER A O   
1071 C CB  . SER A 139 ? 0.50450 0.49290 0.46470 -0.01660 -0.00420 0.04320  139 SER A CB  
1072 O OG  . SER A 139 ? 0.49450 0.48310 0.46140 -0.01760 -0.00720 0.05060  139 SER A OG  
1073 N N   . PHE A 140 ? 0.53100 0.54590 0.48620 -0.02130 -0.00200 0.06290  140 PHE A N   
1074 C CA  . PHE A 140 ? 0.53390 0.56320 0.48140 -0.02220 -0.00140 0.06940  140 PHE A CA  
1075 C C   . PHE A 140 ? 0.52240 0.55600 0.47920 -0.02480 -0.00310 0.08330  140 PHE A C   
1076 O O   . PHE A 140 ? 0.55780 0.58570 0.52740 -0.02650 -0.00260 0.08760  140 PHE A O   
1077 C CB  . PHE A 140 ? 0.55230 0.58790 0.49460 -0.02210 0.00280  0.06650  140 PHE A CB  
1078 C CG  . PHE A 140 ? 0.50510 0.53950 0.43820 -0.01930 0.00470  0.05430  140 PHE A CG  
1079 C CD1 . PHE A 140 ? 0.49990 0.53970 0.42270 -0.01780 0.00400  0.04950  140 PHE A CD1 
1080 C CD2 . PHE A 140 ? 0.52450 0.55390 0.46000 -0.01840 0.00720  0.04840  140 PHE A CD2 
1081 C CE1 . PHE A 140 ? 0.52700 0.56620 0.44350 -0.01530 0.00610  0.03880  140 PHE A CE1 
1082 C CE2 . PHE A 140 ? 0.55650 0.58480 0.48560 -0.01570 0.00900  0.03860  140 PHE A CE2 
1083 C CZ  . PHE A 140 ? 0.50270 0.53590 0.42300 -0.01410 0.00880  0.03380  140 PHE A CZ  
1084 N N   . LEU A 141 ? 0.49980 0.54450 0.45090 -0.02520 -0.00510 0.09040  141 LEU A N   
1085 C CA  . LEU A 141 ? 0.56500 0.61660 0.52440 -0.02750 -0.00680 0.10560  141 LEU A CA  
1086 C C   . LEU A 141 ? 0.57800 0.64820 0.52660 -0.02850 -0.00450 0.11180  141 LEU A C   
1087 O O   . LEU A 141 ? 0.56630 0.64300 0.50120 -0.02710 -0.00200 0.10290  141 LEU A O   
1088 C CB  . LEU A 141 ? 0.55910 0.61020 0.52210 -0.02700 -0.01160 0.11090  141 LEU A CB  
1089 C CG  . LEU A 141 ? 0.64330 0.67710 0.61580 -0.02550 -0.01340 0.10340  141 LEU A CG  
1090 C CD1 . LEU A 141 ? 0.68540 0.72040 0.66030 -0.02470 -0.01810 0.10770  141 LEU A CD1 
1091 C CD2 . LEU A 141 ? 0.62350 0.64620 0.61350 -0.02680 -0.01240 0.10630  141 LEU A CD2 
1092 N N   . ASN A 142 ? 0.58770 0.66710 0.54300 -0.03080 -0.00530 0.12720  142 ASN A N   
1093 C CA  . ASN A 142 ? 0.60590 0.70580 0.54980 -0.03180 -0.00320 0.13420  142 ASN A CA  
1094 C C   . ASN A 142 ? 0.55750 0.66760 0.48430 -0.03010 -0.00530 0.12780  142 ASN A C   
1095 O O   . ASN A 142 ? 0.58900 0.69500 0.51690 -0.02930 -0.00980 0.12740  142 ASN A O   
1096 C CB  . ASN A 142 ? 0.60260 0.71230 0.55680 -0.03460 -0.00430 0.15380  142 ASN A CB  
1097 C CG  . ASN A 142 ? 0.60730 0.71010 0.57860 -0.03690 -0.00180 0.16050  142 ASN A CG  
1098 O OD1 . ASN A 142 ? 0.59100 0.68850 0.56260 -0.03680 0.00180  0.15220  142 ASN A OD1 
1099 N ND2 . ASN A 142 ? 0.66500 0.76780 0.65250 -0.03900 -0.00400 0.17620  142 ASN A ND2 
1100 N N   . GLY A 143 ? 0.58940 0.71190 0.50130 -0.02940 -0.00180 0.12120  143 GLY A N   
1101 C CA  . GLY A 143 ? 0.56620 0.69890 0.46160 -0.02780 -0.00300 0.11200  143 GLY A CA  
1102 C C   . GLY A 143 ? 0.53150 0.65400 0.42120 -0.02520 -0.00110 0.09340  143 GLY A C   
1103 O O   . GLY A 143 ? 0.55970 0.69000 0.43670 -0.02390 -0.00150 0.08360  143 GLY A O   
1104 N N   . SER A 144 ? 0.54940 0.65520 0.44870 -0.02440 0.00060  0.08840  144 SER A N   
1105 C CA  . SER A 144 ? 0.55090 0.64570 0.44720 -0.02190 0.00200  0.07250  144 SER A CA  
1106 C C   . SER A 144 ? 0.50450 0.60570 0.39460 -0.02060 0.00770  0.06520  144 SER A C   
1107 O O   . SER A 144 ? 0.48760 0.58310 0.37420 -0.01820 0.00920  0.05200  144 SER A O   
1108 C CB  . SER A 144 ? 0.57340 0.64840 0.48270 -0.02150 0.00100  0.07050  144 SER A CB  
1109 O OG  . SER A 144 ? 0.56240 0.63410 0.48160 -0.02300 0.00340  0.07680  144 SER A OG  
1110 N N   . ALA A 145 ? 0.55680 0.66960 0.44700 -0.02220 0.01100  0.07380  145 ALA A N   
1111 C CA  . ALA A 145 ? 0.51950 0.63940 0.40460 -0.02080 0.01660  0.06690  145 ALA A CA  
1112 C C   . ALA A 145 ? 0.46340 0.59190 0.33510 -0.01850 0.01750  0.05440  145 ALA A C   
1113 O O   . ALA A 145 ? 0.52680 0.66570 0.38990 -0.01910 0.01470  0.05550  145 ALA A O   
1114 C CB  . ALA A 145 ? 0.45860 0.59440 0.34440 -0.02300 0.02020  0.07940  145 ALA A CB  
1115 N N   . GLY A 146 ? 0.48190 0.60600 0.35320 -0.01580 0.02100  0.04230  146 GLY A N   
1116 C CA  . GLY A 146 ? 0.48710 0.61650 0.34880 -0.01340 0.02220  0.02850  146 GLY A CA  
1117 C C   . GLY A 146 ? 0.49950 0.61270 0.36470 -0.01180 0.01880  0.01840  146 GLY A C   
1118 O O   . GLY A 146 ? 0.51060 0.62450 0.37180 -0.00950 0.02010  0.00540  146 GLY A O   
1119 N N   . SER A 147 ? 0.47970 0.57880 0.35300 -0.01280 0.01470  0.02390  147 SER A N   
1120 C CA  . SER A 147 ? 0.51060 0.59390 0.38870 -0.01110 0.01240  0.01510  147 SER A CA  
1121 C C   . SER A 147 ? 0.54610 0.62190 0.42910 -0.00850 0.01650  0.00720  147 SER A C   
1122 O O   . SER A 147 ? 0.52450 0.60270 0.41090 -0.00860 0.01990  0.01130  147 SER A O   
1123 C CB  . SER A 147 ? 0.45870 0.52890 0.34560 -0.01250 0.00830  0.02260  147 SER A CB  
1124 O OG  . SER A 147 ? 0.48620 0.56360 0.37110 -0.01480 0.00460  0.03220  147 SER A OG  
1125 N N   . VAL A 148 ? 0.50830 0.57610 0.39300 -0.00630 0.01610  -0.00370 148 VAL A N   
1126 C CA  . VAL A 148 ? 0.49300 0.55560 0.38280 -0.00350 0.02010  -0.01090 148 VAL A CA  
1127 C C   . VAL A 148 ? 0.51720 0.56340 0.41600 -0.00240 0.01830  -0.01220 148 VAL A C   
1128 O O   . VAL A 148 ? 0.52040 0.55890 0.42080 -0.00330 0.01430  -0.01140 148 VAL A O   
1129 C CB  . VAL A 148 ? 0.50000 0.56990 0.38570 -0.00110 0.02290  -0.02340 148 VAL A CB  
1130 C CG1 . VAL A 148 ? 0.49290 0.58150 0.36910 -0.00170 0.02600  -0.02310 148 VAL A CG1 
1131 C CG2 . VAL A 148 ? 0.49120 0.55630 0.37610 -0.00090 0.01920  -0.03160 148 VAL A CG2 
1132 N N   . GLY A 149 ? 0.48690 0.52890 0.39210 -0.00050 0.02140  -0.01350 149 GLY A N   
1133 C CA  . GLY A 149 ? 0.53910 0.56800 0.45240 0.00090  0.02050  -0.01500 149 GLY A CA  
1134 C C   . GLY A 149 ? 0.53270 0.56020 0.44990 0.00430  0.02320  -0.02460 149 GLY A C   
1135 O O   . GLY A 149 ? 0.49770 0.53350 0.41350 0.00580  0.02690  -0.02900 149 GLY A O   
1136 N N   . PHE A 150 ? 0.48430 0.50150 0.40750 0.00550  0.02170  -0.02780 150 PHE A N   
1137 C CA  . PHE A 150 ? 0.50540 0.52000 0.43450 0.00850  0.02370  -0.03690 150 PHE A CA  
1138 C C   . PHE A 150 ? 0.52170 0.52450 0.46030 0.00980  0.02260  -0.03590 150 PHE A C   
1139 O O   . PHE A 150 ? 0.48580 0.48280 0.42440 0.00830  0.01980  -0.03030 150 PHE A O   
1140 C CB  . PHE A 150 ? 0.49410 0.51250 0.41880 0.00800  0.02240  -0.04540 150 PHE A CB  
1141 C CG  . PHE A 150 ? 0.52430 0.53730 0.44730 0.00570  0.01750  -0.04350 150 PHE A CG  
1142 C CD1 . PHE A 150 ? 0.53530 0.55340 0.45020 0.00280  0.01470  -0.03660 150 PHE A CD1 
1143 C CD2 . PHE A 150 ? 0.54150 0.54540 0.47230 0.00650  0.01600  -0.04780 150 PHE A CD2 
1144 C CE1 . PHE A 150 ? 0.57320 0.58690 0.48800 0.00090  0.01040  -0.03420 150 PHE A CE1 
1145 C CE2 . PHE A 150 ? 0.52870 0.52830 0.45890 0.00440  0.01170  -0.04560 150 PHE A CE2 
1146 C CZ  . PHE A 150 ? 0.53590 0.54030 0.45800 0.00170  0.00880  -0.03900 150 PHE A CZ  
1147 N N   . ASN A 151 ? 0.52800 0.52810 0.47540 0.01290  0.02510  -0.04140 151 ASN A N   
1148 C CA  . ASN A 151 ? 0.58220 0.57270 0.54000 0.01450  0.02460  -0.04140 151 ASN A CA  
1149 C C   . ASN A 151 ? 0.62780 0.61610 0.59150 0.01590  0.02510  -0.05160 151 ASN A C   
1150 O O   . ASN A 151 ? 0.58820 0.58330 0.54940 0.01660  0.02710  -0.05930 151 ASN A O   
1151 C CB  . ASN A 151 ? 0.51120 0.50060 0.47710 0.01710  0.02700  -0.03690 151 ASN A CB  
1152 C CG  . ASN A 151 ? 0.55900 0.54820 0.52090 0.01530  0.02530  -0.02740 151 ASN A CG  
1153 O OD1 . ASN A 151 ? 0.55190 0.53540 0.51430 0.01420  0.02280  -0.02370 151 ASN A OD1 
1154 N ND2 . ASN A 151 ? 0.50530 0.50120 0.46400 0.01490  0.02660  -0.02410 151 ASN A ND2 
1155 N N   . ILE A 152 ? 0.57090 0.55060 0.54290 0.01600  0.02330  -0.05200 152 ILE A N   
1156 C CA  . ILE A 152 ? 0.63430 0.61100 0.61490 0.01710  0.02380  -0.06210 152 ILE A CA  
1157 C C   . ILE A 152 ? 0.70570 0.67420 0.70270 0.01990  0.02540  -0.06010 152 ILE A C   
1158 O O   . ILE A 152 ? 0.73950 0.70270 0.73970 0.01950  0.02410  -0.05150 152 ILE A O   
1159 C CB  . ILE A 152 ? 0.64410 0.61900 0.62130 0.01420  0.01970  -0.06560 152 ILE A CB  
1160 C CG1 . ILE A 152 ? 0.64970 0.63400 0.61120 0.01140  0.01770  -0.06560 152 ILE A CG1 
1161 C CG2 . ILE A 152 ? 0.70930 0.68240 0.69640 0.01510  0.02020  -0.07800 152 ILE A CG2 
1162 C CD1 . ILE A 152 ? 0.66270 0.64790 0.62020 0.00850  0.01320  -0.06970 152 ILE A CD1 
1163 N N   . ASP A 153 ? 0.79300 0.76110 0.80090 0.02270  0.02850  -0.06790 153 ASP A N   
1164 C CA  . ASP A 153 ? 0.91320 0.87350 0.93990 0.02560  0.03010  -0.06670 153 ASP A CA  
1165 C C   . ASP A 153 ? 0.98140 0.93790 1.01940 0.02600  0.03040  -0.07920 153 ASP A C   
1166 O O   . ASP A 153 ? 0.92610 0.88750 0.96410 0.02720  0.03260  -0.09020 153 ASP A O   
1167 C CB  . ASP A 153 ? 0.92900 0.89220 0.96230 0.02920  0.03390  -0.06320 153 ASP A CB  
1168 C CG  . ASP A 153 ? 1.07540 1.03210 1.12440 0.03160  0.03450  -0.05440 153 ASP A CG  
1169 O OD1 . ASP A 153 ? 1.15290 1.10250 1.21750 0.03260  0.03480  -0.05780 153 ASP A OD1 
1170 O OD2 . ASP A 153 ? 1.12760 1.08700 1.17360 0.03210  0.03440  -0.04370 153 ASP A OD2 
1171 N N   . TYR A 154 ? 1.21150 1.15960 1.26020 0.02500  0.02830  -0.07780 154 TYR A N   
1172 C CA  . TYR A 154 ? 1.14220 1.08590 1.20190 0.02410  0.02730  -0.08940 154 TYR A CA  
1173 C C   . TYR A 154 ? 1.16040 1.11140 1.20430 0.02100  0.02460  -0.09900 154 TYR A C   
1174 O O   . TYR A 154 ? 1.24530 1.19760 1.27810 0.01770  0.02080  -0.09430 154 TYR A O   
1175 C CB  . TYR A 154 ? 1.19180 1.13270 1.27000 0.02780  0.03110  -0.09830 154 TYR A CB  
1176 C CG  . TYR A 154 ? 1.37580 1.31210 1.46880 0.03150  0.03400  -0.08740 154 TYR A CG  
1177 C CD1 . TYR A 154 ? 1.37540 1.30340 1.48300 0.03150  0.03300  -0.07790 154 TYR A CD1 
1178 C CD2 . TYR A 154 ? 1.32740 1.26900 1.42000 0.03490  0.03760  -0.08570 154 TYR A CD2 
1179 C CE1 . TYR A 154 ? 1.45400 1.37970 1.57490 0.03490  0.03540  -0.06650 154 TYR A CE1 
1180 C CE2 . TYR A 154 ? 1.39610 1.33480 1.50260 0.03830  0.03970  -0.07490 154 TYR A CE2 
1181 C CZ  . TYR A 154 ? 1.51990 1.45100 1.64010 0.03830  0.03850  -0.06510 154 TYR A CZ  
1182 O OH  . TYR A 154 ? 1.62590 1.55610 1.75950 0.04160  0.04030  -0.05330 154 TYR A OH  
1183 N N   . ASP A 155 ? 0.97250 0.92950 1.01530 0.02200  0.02660  -0.11200 155 ASP A N   
1184 C CA  . ASP A 155 ? 0.98950 0.95670 1.01550 0.01910  0.02420  -0.12050 155 ASP A CA  
1185 C C   . ASP A 155 ? 0.87170 0.85030 0.88450 0.02060  0.02760  -0.12220 155 ASP A C   
1186 O O   . ASP A 155 ? 0.85040 0.83980 0.85050 0.01890  0.02670  -0.13070 155 ASP A O   
1187 C CB  . ASP A 155 ? 1.03880 1.00540 1.07350 0.01800  0.02280  -0.13680 155 ASP A CB  
1188 C CG  . ASP A 155 ? 1.12930 1.08730 1.17320 0.01510  0.01820  -0.13500 155 ASP A CG  
1189 O OD1 . ASP A 155 ? 1.07750 1.03490 1.11230 0.01260  0.01480  -0.12400 155 ASP A OD1 
1190 O OD2 . ASP A 155 ? 1.16800 1.12000 1.22930 0.01510  0.01800  -0.14530 155 ASP A OD2 
1191 N N   . CYS A 156 ? 0.81620 0.79410 0.83210 0.02350  0.03120  -0.11390 156 CYS A N   
1192 C CA  . CYS A 156 ? 0.73690 0.72550 0.74250 0.02500  0.03470  -0.11380 156 CYS A CA  
1193 C C   . CYS A 156 ? 0.68300 0.67590 0.67280 0.02260  0.03280  -0.10040 156 CYS A C   
1194 O O   . CYS A 156 ? 0.64740 0.63360 0.64040 0.02270  0.03170  -0.08860 156 CYS A O   
1195 C CB  . CYS A 156 ? 0.69700 0.68290 0.71750 0.02960  0.03970  -0.11320 156 CYS A CB  
1196 S SG  . CYS A 156 ? 0.80370 0.80390 0.81490 0.03180  0.04500  -0.11440 156 CYS A SG  
1197 N N   . VAL A 157 ? 0.63430 0.63880 0.60780 0.02050  0.03220  -0.10240 157 VAL A N   
1198 C CA  . VAL A 157 ? 0.57990 0.58960 0.53950 0.01820  0.03060  -0.09060 157 VAL A CA  
1199 C C   . VAL A 157 ? 0.59370 0.61000 0.55200 0.02030  0.03510  -0.08650 157 VAL A C   
1200 O O   . VAL A 157 ? 0.58360 0.60990 0.53880 0.02160  0.03870  -0.09430 157 VAL A O   
1201 C CB  . VAL A 157 ? 0.57790 0.59810 0.52200 0.01480  0.02780  -0.09330 157 VAL A CB  
1202 C CG1 . VAL A 157 ? 0.53920 0.56370 0.47210 0.01260  0.02640  -0.07990 157 VAL A CG1 
1203 C CG2 . VAL A 157 ? 0.63330 0.64840 0.57940 0.01260  0.02300  -0.09820 157 VAL A CG2 
1204 N N   . SER A 158 ? 0.54820 0.56030 0.50830 0.02040  0.03490  -0.07480 158 SER A N   
1205 C CA  . SER A 158 ? 0.55470 0.57410 0.51360 0.02180  0.03860  -0.06980 158 SER A CA  
1206 C C   . SER A 158 ? 0.52090 0.54690 0.46600 0.01820  0.03660  -0.06130 158 SER A C   
1207 O O   . SER A 158 ? 0.51330 0.53380 0.45720 0.01620  0.03350  -0.05200 158 SER A O   
1208 C CB  . SER A 158 ? 0.58930 0.60140 0.56030 0.02410  0.03950  -0.06280 158 SER A CB  
1209 O OG  . SER A 158 ? 0.63650 0.64420 0.62230 0.02800  0.04220  -0.07010 158 SER A OG  
1210 N N   . PHE A 159 ? 0.51430 0.55290 0.44960 0.01720  0.03840  -0.06430 159 PHE A N   
1211 C CA  . PHE A 159 ? 0.50900 0.55480 0.43350 0.01390  0.03700  -0.05480 159 PHE A CA  
1212 C C   . PHE A 159 ? 0.56000 0.60810 0.48850 0.01460  0.03960  -0.04680 159 PHE A C   
1213 O O   . PHE A 159 ? 0.55460 0.60910 0.48720 0.01720  0.04430  -0.05050 159 PHE A O   
1214 C CB  . PHE A 159 ? 0.54670 0.60730 0.45970 0.01270  0.03840  -0.05910 159 PHE A CB  
1215 C CG  . PHE A 159 ? 0.52060 0.58170 0.42840 0.01150  0.03520  -0.06680 159 PHE A CG  
1216 C CD1 . PHE A 159 ? 0.53440 0.59260 0.43660 0.00820  0.02980  -0.06020 159 PHE A CD1 
1217 C CD2 . PHE A 159 ? 0.54210 0.60660 0.45200 0.01360  0.03740  -0.08080 159 PHE A CD2 
1218 C CE1 . PHE A 159 ? 0.48550 0.54500 0.38340 0.00680  0.02620  -0.06710 159 PHE A CE1 
1219 C CE2 . PHE A 159 ? 0.58290 0.64830 0.48850 0.01200  0.03360  -0.08890 159 PHE A CE2 
1220 C CZ  . PHE A 159 ? 0.54950 0.61310 0.44870 0.00860  0.02800  -0.08160 159 PHE A CZ  
1221 N N   . CYS A 160 ? 0.50510 0.54920 0.43220 0.01200  0.03670  -0.03640 160 CYS A N   
1222 C CA  . CYS A 160 ? 0.55490 0.60060 0.48650 0.01190  0.03810  -0.02890 160 CYS A CA  
1223 C C   . CYS A 160 ? 0.52690 0.57910 0.45230 0.00820  0.03710  -0.01960 160 CYS A C   
1224 O O   . CYS A 160 ? 0.55300 0.60850 0.48270 0.00770  0.03860  -0.01400 160 CYS A O   
1225 C CB  . CYS A 160 ? 0.53640 0.57040 0.47620 0.01260  0.03570  -0.02520 160 CYS A CB  
1226 S SG  . CYS A 160 ? 0.49590 0.51960 0.43260 0.00950  0.03000  -0.02040 160 CYS A SG  
1227 N N   . TYR A 161 ? 0.51420 0.56840 0.43150 0.00530  0.03440  -0.01720 161 TYR A N   
1228 C CA  . TYR A 161 ? 0.51420 0.57250 0.42880 0.00170  0.03290  -0.00690 161 TYR A CA  
1229 C C   . TYR A 161 ? 0.49100 0.55860 0.39580 -0.00020 0.03210  -0.00570 161 TYR A C   
1230 O O   . TYR A 161 ? 0.49900 0.56430 0.39960 0.00010  0.02980  -0.01110 161 TYR A O   
1231 C CB  . TYR A 161 ? 0.48640 0.53250 0.40560 -0.00010 0.02850  -0.00150 161 TYR A CB  
1232 C CG  . TYR A 161 ? 0.50270 0.55100 0.42170 -0.00390 0.02660  0.00840  161 TYR A CG  
1233 C CD1 . TYR A 161 ? 0.47950 0.53040 0.40430 -0.00530 0.02790  0.01400  161 TYR A CD1 
1234 C CD2 . TYR A 161 ? 0.47420 0.52280 0.38860 -0.00620 0.02350  0.01230  161 TYR A CD2 
1235 C CE1 . TYR A 161 ? 0.50020 0.55260 0.42730 -0.00890 0.02630  0.02290  161 TYR A CE1 
1236 C CE2 . TYR A 161 ? 0.48210 0.53200 0.39900 -0.00950 0.02180  0.02180  161 TYR A CE2 
1237 C CZ  . TYR A 161 ? 0.48100 0.53290 0.40450 -0.01090 0.02350  0.02700  161 TYR A CZ  
1238 O OH  . TYR A 161 ? 0.48370 0.53640 0.41260 -0.01440 0.02200  0.03660  161 TYR A OH  
1239 N N   . MET A 162 ? 0.46950 0.54860 0.37130 -0.00240 0.03380  0.00170  162 MET A N   
1240 C CA  . MET A 162 ? 0.47720 0.56580 0.37040 -0.00490 0.03220  0.00660  162 MET A CA  
1241 C C   . MET A 162 ? 0.50900 0.59660 0.40680 -0.00840 0.03020  0.01970  162 MET A C   
1242 O O   . MET A 162 ? 0.50920 0.59890 0.41320 -0.00910 0.03270  0.02450  162 MET A O   
1243 C CB  . MET A 162 ? 0.51540 0.62200 0.40010 -0.00410 0.03660  0.00350  162 MET A CB  
1244 C CG  . MET A 162 ? 0.48440 0.60410 0.35900 -0.00690 0.03460  0.00990  162 MET A CG  
1245 S SD  . MET A 162 ? 0.60510 0.74710 0.46710 -0.00530 0.03960  0.00160  162 MET A SD  
1246 C CE  . MET A 162 ? 0.58890 0.72360 0.44600 -0.00410 0.03500  -0.01180 162 MET A CE  
1247 N N   . HIS A 163 ? 0.44460 0.52930 0.34090 -0.01060 0.02580  0.02540  163 HIS A N   
1248 C CA  . HIS A 163 ? 0.50300 0.58490 0.40630 -0.01380 0.02370  0.03740  163 HIS A CA  
1249 C C   . HIS A 163 ? 0.43250 0.53020 0.33380 -0.01620 0.02600  0.04770  163 HIS A C   
1250 O O   . HIS A 163 ? 0.45430 0.56550 0.34590 -0.01630 0.02680  0.04830  163 HIS A O   
1251 C CB  . HIS A 163 ? 0.47280 0.54670 0.37720 -0.01510 0.01840  0.04070  163 HIS A CB  
1252 C CG  . HIS A 163 ? 0.44150 0.51030 0.35600 -0.01810 0.01630  0.05150  163 HIS A CG  
1253 N ND1 . HIS A 163 ? 0.44520 0.50580 0.36940 -0.01870 0.01710  0.05190  163 HIS A ND1 
1254 C CD2 . HIS A 163 ? 0.45420 0.52570 0.37180 -0.02060 0.01360  0.06220  163 HIS A CD2 
1255 C CE1 . HIS A 163 ? 0.44030 0.49770 0.37370 -0.02150 0.01500  0.06110  163 HIS A CE1 
1256 N NE2 . HIS A 163 ? 0.46810 0.53140 0.39840 -0.02260 0.01290  0.06800  163 HIS A NE2 
1257 N N   . HIS A 164 ? 0.47920 0.57600 0.39030 -0.01840 0.02700  0.05610  164 HIS A N   
1258 C CA  . HIS A 164 ? 0.50020 0.61110 0.41220 -0.02130 0.02890  0.06830  164 HIS A CA  
1259 C C   . HIS A 164 ? 0.45240 0.55700 0.37600 -0.02480 0.02550  0.08040  164 HIS A C   
1260 O O   . HIS A 164 ? 0.50390 0.61680 0.42650 -0.02690 0.02420  0.09100  164 HIS A O   
1261 C CB  . HIS A 164 ? 0.46380 0.58400 0.37860 -0.02100 0.03450  0.06850  164 HIS A CB  
1262 C CG  . HIS A 164 ? 0.52330 0.65340 0.42750 -0.01750 0.03880  0.05810  164 HIS A CG  
1263 N ND1 . HIS A 164 ? 0.49470 0.64400 0.39240 -0.01750 0.04370  0.06080  164 HIS A ND1 
1264 C CD2 . HIS A 164 ? 0.51530 0.63880 0.41590 -0.01390 0.03920  0.04460  164 HIS A CD2 
1265 C CE1 . HIS A 164 ? 0.48220 0.63610 0.37260 -0.01390 0.04700  0.04830  164 HIS A CE1 
1266 N NE2 . HIS A 164 ? 0.52030 0.65810 0.41320 -0.01160 0.04430  0.03850  164 HIS A NE2 
1267 N N   . MET A 165 ? 0.46300 0.55410 0.39830 -0.02570 0.02410  0.07940  165 MET A N   
1268 C CA  . MET A 165 ? 0.51750 0.60540 0.46610 -0.02940 0.02210  0.09110  165 MET A CA  
1269 C C   . MET A 165 ? 0.50850 0.57860 0.46780 -0.02980 0.01850  0.08700  165 MET A C   
1270 O O   . MET A 165 ? 0.49550 0.55630 0.45230 -0.02750 0.01790  0.07590  165 MET A O   
1271 C CB  . MET A 165 ? 0.48930 0.58720 0.44530 -0.03170 0.02600  0.09850  165 MET A CB  
1272 C CG  . MET A 165 ? 0.43690 0.53090 0.39630 -0.03060 0.02810  0.09010  165 MET A CG  
1273 S SD  . MET A 165 ? 0.57490 0.68630 0.54000 -0.03310 0.03360  0.09980  165 MET A SD  
1274 C CE  . MET A 165 ? 0.54320 0.64550 0.51950 -0.03320 0.03360  0.09250  165 MET A CE  
1275 N N   . GLU A 166 ? 0.52560 0.59150 0.49760 -0.03290 0.01620  0.09640  166 GLU A N   
1276 C CA  . GLU A 166 ? 0.57000 0.62050 0.55410 -0.03380 0.01320  0.09270  166 GLU A CA  
1277 C C   . GLU A 166 ? 0.55380 0.60400 0.55330 -0.03740 0.01410  0.09790  166 GLU A C   
1278 O O   . GLU A 166 ? 0.54410 0.60280 0.55090 -0.04020 0.01520  0.11000  166 GLU A O   
1279 C CB  . GLU A 166 ? 0.53700 0.58040 0.52630 -0.03420 0.00930  0.09730  166 GLU A CB  
1280 C CG  . GLU A 166 ? 0.54660 0.57500 0.54880 -0.03500 0.00680  0.09270  166 GLU A CG  
1281 C CD  . GLU A 166 ? 0.58830 0.60950 0.59390 -0.03420 0.00330  0.09470  166 GLU A CD  
1282 O OE1 . GLU A 166 ? 0.58360 0.60520 0.57710 -0.03140 0.00240  0.09010  166 GLU A OE1 
1283 O OE2 . GLU A 166 ? 0.63690 0.65210 0.65870 -0.03640 0.00150  0.10090  166 GLU A OE2 
1284 N N   . LEU A 167 ? 0.54860 0.59020 0.55330 -0.03740 0.01360  0.08910  167 LEU A N   
1285 C CA  . LEU A 167 ? 0.51970 0.56040 0.53990 -0.04090 0.01380  0.09150  167 LEU A CA  
1286 C C   . LEU A 167 ? 0.61130 0.64100 0.64780 -0.04360 0.01040  0.09420  167 LEU A C   
1287 O O   . LEU A 167 ? 0.59720 0.61940 0.63220 -0.04210 0.00810  0.09280  167 LEU A O   
1288 C CB  . LEU A 167 ? 0.50030 0.53860 0.51830 -0.03970 0.01430  0.08050  167 LEU A CB  
1289 C CG  . LEU A 167 ? 0.51840 0.56840 0.52470 -0.03730 0.01820  0.07910  167 LEU A CG  
1290 C CD1 . LEU A 167 ? 0.50530 0.55290 0.50960 -0.03550 0.01830  0.06880  167 LEU A CD1 
1291 C CD2 . LEU A 167 ? 0.57120 0.63460 0.58340 -0.04010 0.02150  0.08980  167 LEU A CD2 
1292 N N   . PRO A 168 ? 0.62610 0.65500 0.68000 -0.04770 0.01020  0.09850  168 PRO A N   
1293 C CA  . PRO A 168 ? 0.57950 0.59820 0.65190 -0.05030 0.00730  0.10150  168 PRO A CA  
1294 C C   . PRO A 168 ? 0.60480 0.61020 0.67790 -0.04870 0.00450  0.08860  168 PRO A C   
1295 O O   . PRO A 168 ? 0.64710 0.64380 0.73120 -0.04930 0.00230  0.09020  168 PRO A O   
1296 C CB  . PRO A 168 ? 0.66120 0.68260 0.75180 -0.05510 0.00790  0.10630  168 PRO A CB  
1297 C CG  . PRO A 168 ? 0.65500 0.69140 0.73700 -0.05510 0.01160  0.11310  168 PRO A CG  
1298 C CD  . PRO A 168 ? 0.61790 0.65690 0.67750 -0.05030 0.01290  0.10310  168 PRO A CD  
1299 N N   . THR A 169 ? 0.59200 0.59620 0.65460 -0.04660 0.00470  0.07640  169 THR A N   
1300 C CA  . THR A 169 ? 0.59640 0.58970 0.65840 -0.04490 0.00240  0.06470  169 THR A CA  
1301 C C   . THR A 169 ? 0.62510 0.61500 0.67460 -0.04090 0.00200  0.06310  169 THR A C   
1302 O O   . THR A 169 ? 0.61390 0.59560 0.66230 -0.03920 0.00050  0.05430  169 THR A O   
1303 C CB  . THR A 169 ? 0.60480 0.59950 0.66060 -0.04420 0.00250  0.05360  169 THR A CB  
1304 O OG1 . THR A 169 ? 0.61850 0.62210 0.65890 -0.04160 0.00490  0.05440  169 THR A OG1 
1305 C CG2 . THR A 169 ? 0.60620 0.60250 0.67750 -0.04870 0.00170  0.05260  169 THR A CG2 
1306 N N   . GLY A 170 ? 0.55440 0.55090 0.59470 -0.03950 0.00310  0.07120  170 GLY A N   
1307 C CA  . GLY A 170 ? 0.61060 0.60450 0.64010 -0.03620 0.00220  0.06950  170 GLY A CA  
1308 C C   . GLY A 170 ? 0.58780 0.58520 0.59960 -0.03270 0.00370  0.06190  170 GLY A C   
1309 O O   . GLY A 170 ? 0.59900 0.59420 0.60220 -0.03000 0.00290  0.05930  170 GLY A O   
1310 N N   . VAL A 171 ? 0.53390 0.53690 0.54160 -0.03280 0.00570  0.05850  171 VAL A N   
1311 C CA  . VAL A 171 ? 0.52290 0.52940 0.51620 -0.02940 0.00740  0.05200  171 VAL A CA  
1312 C C   . VAL A 171 ? 0.52320 0.54130 0.50820 -0.02880 0.01010  0.05760  171 VAL A C   
1313 O O   . VAL A 171 ? 0.51080 0.53520 0.50070 -0.03120 0.01070  0.06720  171 VAL A O   
1314 C CB  . VAL A 171 ? 0.50690 0.51280 0.50100 -0.02910 0.00780  0.04440  171 VAL A CB  
1315 C CG1 . VAL A 171 ? 0.57380 0.56980 0.57400 -0.02940 0.00530  0.03720  171 VAL A CG1 
1316 C CG2 . VAL A 171 ? 0.45610 0.46950 0.45790 -0.03200 0.00920  0.04870  171 VAL A CG2 
1317 N N   . HIS A 172 ? 0.49240 0.51420 0.46590 -0.02560 0.01190  0.05190  172 HIS A N   
1318 C CA  . HIS A 172 ? 0.52790 0.55980 0.49150 -0.02430 0.01410  0.05480  172 HIS A CA  
1319 C C   . HIS A 172 ? 0.47720 0.51670 0.43670 -0.02260 0.01770  0.05090  172 HIS A C   
1320 O O   . HIS A 172 ? 0.47940 0.51490 0.44120 -0.02150 0.01780  0.04500  172 HIS A O   
1321 C CB  . HIS A 172 ? 0.50540 0.53400 0.45990 -0.02180 0.01260  0.05080  172 HIS A CB  
1322 C CG  . HIS A 172 ? 0.53800 0.56040 0.49790 -0.02320 0.00920  0.05550  172 HIS A CG  
1323 N ND1 . HIS A 172 ? 0.52570 0.53670 0.48880 -0.02230 0.00680  0.05030  172 HIS A ND1 
1324 C CD2 . HIS A 172 ? 0.51690 0.54320 0.48140 -0.02550 0.00790  0.06560  172 HIS A CD2 
1325 C CE1 . HIS A 172 ? 0.52340 0.53120 0.49250 -0.02360 0.00420  0.05610  172 HIS A CE1 
1326 N NE2 . HIS A 172 ? 0.54050 0.55720 0.51070 -0.02550 0.00470  0.06580  172 HIS A NE2 
1327 N N   . ALA A 173 ? 0.51160 0.56320 0.46650 -0.02280 0.02070  0.05540  173 ALA A N   
1328 C CA  . ALA A 173 ? 0.45210 0.51290 0.40490 -0.02130 0.02480  0.05300  173 ALA A CA  
1329 C C   . ALA A 173 ? 0.45120 0.52210 0.39240 -0.01910 0.02750  0.05120  173 ALA A C   
1330 O O   . ALA A 173 ? 0.49250 0.56900 0.42910 -0.02030 0.02690  0.05680  173 ALA A O   
1331 C CB  . ALA A 173 ? 0.46150 0.52980 0.42410 -0.02470 0.02650  0.06110  173 ALA A CB  
1332 N N   . GLY A 174 ? 0.46030 0.53440 0.39740 -0.01580 0.03050  0.04350  174 GLY A N   
1333 C CA  . GLY A 174 ? 0.49740 0.58150 0.42430 -0.01360 0.03340  0.03970  174 GLY A CA  
1334 C C   . GLY A 174 ? 0.48230 0.57160 0.40930 -0.01030 0.03790  0.03270  174 GLY A C   
1335 O O   . GLY A 174 ? 0.47280 0.56000 0.40830 -0.01020 0.03870  0.03300  174 GLY A O   
1336 N N   . THR A 175 ? 0.44250 0.53830 0.36110 -0.00750 0.04040  0.02550  175 THR A N   
1337 C CA  . THR A 175 ? 0.47980 0.58300 0.39900 -0.00410 0.04550  0.01850  175 THR A CA  
1338 C C   . THR A 175 ? 0.51820 0.61300 0.43640 -0.00010 0.04510  0.00700  175 THR A C   
1339 O O   . THR A 175 ? 0.48690 0.57280 0.40150 -0.00030 0.04130  0.00410  175 THR A O   
1340 C CB  . THR A 175 ? 0.50720 0.62830 0.41860 -0.00400 0.05020  0.01910  175 THR A CB  
1341 O OG1 . THR A 175 ? 0.46590 0.59040 0.36590 -0.00380 0.04880  0.01480  175 THR A OG1 
1342 C CG2 . THR A 175 ? 0.52010 0.65050 0.43420 -0.00790 0.05110  0.03200  175 THR A CG2 
1343 N N   . ASP A 176 ? 0.49580 0.59360 0.41880 0.00340  0.04920  0.00070  176 ASP A N   
1344 C CA  . ASP A 176 ? 0.48180 0.57610 0.40380 0.00730  0.05030  -0.01090 176 ASP A CA  
1345 C C   . ASP A 176 ? 0.47730 0.58390 0.38880 0.00750  0.05290  -0.01630 176 ASP A C   
1346 O O   . ASP A 176 ? 0.47390 0.59210 0.37830 0.00470  0.05370  -0.00970 176 ASP A O   
1347 C CB  . ASP A 176 ? 0.48150 0.57440 0.41400 0.01120  0.05370  -0.01560 176 ASP A CB  
1348 C CG  . ASP A 176 ? 0.53050 0.63850 0.46500 0.01240  0.05970  -0.01510 176 ASP A CG  
1349 O OD1 . ASP A 176 ? 0.50020 0.62070 0.42630 0.01140  0.06250  -0.01550 176 ASP A OD1 
1350 O OD2 . ASP A 176 ? 0.56370 0.67200 0.50840 0.01440  0.06170  -0.01420 176 ASP A OD2 
1351 N N   . LEU A 177 ? 0.45830 0.56290 0.36870 0.01060  0.05400  -0.02820 177 LEU A N   
1352 C CA  . LEU A 177 ? 0.51160 0.62810 0.41150 0.01080  0.05570  -0.03540 177 LEU A CA  
1353 C C   . LEU A 177 ? 0.55890 0.69200 0.45770 0.01300  0.06280  -0.03980 177 LEU A C   
1354 O O   . LEU A 177 ? 0.53660 0.68230 0.42570 0.01310  0.06490  -0.04630 177 LEU A O   
1355 C CB  . LEU A 177 ? 0.52110 0.62920 0.42100 0.01280  0.05360  -0.04780 177 LEU A CB  
1356 C CG  . LEU A 177 ? 0.51070 0.61110 0.40480 0.00960  0.04700  -0.04460 177 LEU A CG  
1357 C CD1 . LEU A 177 ? 0.53530 0.65130 0.41540 0.00670  0.04620  -0.04140 177 LEU A CD1 
1358 C CD2 . LEU A 177 ? 0.48710 0.57430 0.38680 0.00760  0.04270  -0.03350 177 LEU A CD2 
1359 N N   . GLU A 178 ? 0.53110 0.66530 0.43960 0.01470  0.06650  -0.03670 178 GLU A N   
1360 C CA  . GLU A 178 ? 0.61520 0.76670 0.52360 0.01590  0.07330  -0.03680 178 GLU A CA  
1361 C C   . GLU A 178 ? 0.55990 0.72150 0.46450 0.01170  0.07350  -0.02240 178 GLU A C   
1362 O O   . GLU A 178 ? 0.57510 0.75180 0.48020 0.01230  0.07930  -0.02050 178 GLU A O   
1363 C CB  . GLU A 178 ? 0.59460 0.74290 0.51750 0.02010  0.07730  -0.04050 178 GLU A CB  
1364 C CG  . GLU A 178 ? 0.71520 0.86020 0.64260 0.02480  0.07980  -0.05610 178 GLU A CG  
1365 C CD  . GLU A 178 ? 0.86750 1.00760 0.81150 0.02930  0.08300  -0.05910 178 GLU A CD  
1366 O OE1 . GLU A 178 ? 0.87350 1.01420 0.82490 0.02880  0.08330  -0.04920 178 GLU A OE1 
1367 O OE2 . GLU A 178 ? 1.05990 1.19730 1.01050 0.03350  0.08560  -0.07170 178 GLU A OE2 
1368 N N   . GLY A 179 ? 0.51430 0.66810 0.41660 0.00770  0.06770  -0.01250 179 GLY A N   
1369 C CA  . GLY A 179 ? 0.50470 0.66640 0.40510 0.00330  0.06710  0.00160  179 GLY A CA  
1370 C C   . GLY A 179 ? 0.54850 0.70590 0.46130 0.00190  0.06700  0.01080  179 GLY A C   
1371 O O   . GLY A 179 ? 0.50640 0.67130 0.42020 -0.00190 0.06720  0.02250  179 GLY A O   
1372 N N   . ASN A 180 ? 0.50080 0.64730 0.42390 0.00440  0.06660  0.00630  180 ASN A N   
1373 C CA  . ASN A 180 ? 0.53480 0.67830 0.46960 0.00270  0.06570  0.01450  180 ASN A CA  
1374 C C   . ASN A 180 ? 0.52100 0.64970 0.45810 -0.00060 0.05880  0.02030  180 ASN A C   
1375 O O   . ASN A 180 ? 0.47830 0.59410 0.41400 0.00080  0.05510  0.01470  180 ASN A O   
1376 C CB  . ASN A 180 ? 0.52220 0.66290 0.46740 0.00690  0.06810  0.00820  180 ASN A CB  
1377 C CG  . ASN A 180 ? 0.57530 0.73110 0.52120 0.01030  0.07550  0.00280  180 ASN A CG  
1378 O OD1 . ASN A 180 ? 0.56620 0.73730 0.51160 0.00860  0.07980  0.00880  180 ASN A OD1 
1379 N ND2 . ASN A 180 ? 0.66210 0.81450 0.60990 0.01510  0.07760  -0.00860 180 ASN A ND2 
1380 N N   . PHE A 181 ? 0.49830 0.62900 0.44010 -0.00500 0.05720  0.03120  181 PHE A N   
1381 C CA  . PHE A 181 ? 0.52500 0.64190 0.47040 -0.00810 0.05100  0.03540  181 PHE A CA  
1382 C C   . PHE A 181 ? 0.51890 0.62470 0.47170 -0.00610 0.04870  0.03050  181 PHE A C   
1383 O O   . PHE A 181 ? 0.46460 0.57490 0.42470 -0.00420 0.05130  0.02890  181 PHE A O   
1384 C CB  . PHE A 181 ? 0.49760 0.61810 0.45000 -0.01310 0.04990  0.04720  181 PHE A CB  
1385 C CG  . PHE A 181 ? 0.50350 0.62640 0.44990 -0.01610 0.04830  0.05430  181 PHE A CG  
1386 C CD1 . PHE A 181 ? 0.49400 0.60390 0.44040 -0.01790 0.04280  0.05560  181 PHE A CD1 
1387 C CD2 . PHE A 181 ? 0.47530 0.61460 0.41520 -0.01660 0.05260  0.05900  181 PHE A CD2 
1388 C CE1 . PHE A 181 ? 0.47630 0.58890 0.41820 -0.02030 0.04110  0.06280  181 PHE A CE1 
1389 C CE2 . PHE A 181 ? 0.48830 0.63160 0.42240 -0.01910 0.05090  0.06650  181 PHE A CE2 
1390 C CZ  . PHE A 181 ? 0.52390 0.65340 0.45940 -0.02090 0.04490  0.06860  181 PHE A CZ  
1391 N N   . TYR A 182 ? 0.45960 0.55180 0.41070 -0.00650 0.04370  0.02840  182 TYR A N   
1392 C CA  . TYR A 182 ? 0.40520 0.48790 0.36380 -0.00650 0.04030  0.02740  182 TYR A CA  
1393 C C   . TYR A 182 ? 0.42480 0.50860 0.39130 -0.01110 0.03830  0.03520  182 TYR A C   
1394 O O   . TYR A 182 ? 0.46140 0.54440 0.42680 -0.01460 0.03670  0.04080  182 TYR A O   
1395 C CB  . TYR A 182 ? 0.42690 0.49600 0.38120 -0.00570 0.03610  0.02330  182 TYR A CB  
1396 C CG  . TYR A 182 ? 0.42520 0.49240 0.37470 -0.00130 0.03790  0.01520  182 TYR A CG  
1397 C CD1 . TYR A 182 ? 0.47580 0.54110 0.43090 0.00240  0.03900  0.01070  182 TYR A CD1 
1398 C CD2 . TYR A 182 ? 0.48840 0.55580 0.42900 -0.00080 0.03810  0.01220  182 TYR A CD2 
1399 C CE1 . TYR A 182 ? 0.54460 0.60720 0.49800 0.00640  0.04060  0.00320  182 TYR A CE1 
1400 C CE2 . TYR A 182 ? 0.46180 0.52730 0.39970 0.00290  0.03960  0.00370  182 TYR A CE2 
1401 C CZ  . TYR A 182 ? 0.50680 0.56880 0.45160 0.00640  0.04080  -0.00070 182 TYR A CZ  
1402 O OH  . TYR A 182 ? 0.52840 0.58790 0.47280 0.00990  0.04230  -0.00890 182 TYR A OH  
1403 N N   . GLY A 183 ? 0.44300 0.52900 0.41850 -0.01140 0.03810  0.03570  183 GLY A N   
1404 C CA  . GLY A 183 ? 0.46270 0.54890 0.44730 -0.01610 0.03560  0.04170  183 GLY A CA  
1405 C C   . GLY A 183 ? 0.46770 0.56660 0.45720 -0.01870 0.03920  0.04900  183 GLY A C   
1406 O O   . GLY A 183 ? 0.46410 0.57200 0.44800 -0.01690 0.04380  0.04970  183 GLY A O   
1407 N N   . PRO A 184 ? 0.48380 0.58370 0.48400 -0.02320 0.03720  0.05450  184 PRO A N   
1408 C CA  . PRO A 184 ? 0.49730 0.60970 0.50530 -0.02630 0.04060  0.06290  184 PRO A CA  
1409 C C   . PRO A 184 ? 0.53880 0.65230 0.54530 -0.02960 0.04090  0.07100  184 PRO A C   
1410 O O   . PRO A 184 ? 0.58850 0.70180 0.60580 -0.03440 0.03920  0.07800  184 PRO A O   
1411 C CB  . PRO A 184 ? 0.48900 0.59990 0.51120 -0.03010 0.03710  0.06410  184 PRO A CB  
1412 C CG  . PRO A 184 ? 0.55000 0.64560 0.57050 -0.03120 0.03120  0.05960  184 PRO A CG  
1413 C CD  . PRO A 184 ? 0.50840 0.59840 0.51530 -0.02600 0.03160  0.05270  184 PRO A CD  
1414 N N   . PHE A 185 ? 0.53310 0.64650 0.52690 -0.02720 0.04220  0.06970  185 PHE A N   
1415 C CA  . PHE A 185 ? 0.49790 0.61190 0.48900 -0.02990 0.04160  0.07750  185 PHE A CA  
1416 C C   . PHE A 185 ? 0.49840 0.62820 0.48110 -0.02850 0.04720  0.08140  185 PHE A C   
1417 O O   . PHE A 185 ? 0.51630 0.65300 0.49230 -0.02450 0.05110  0.07470  185 PHE A O   
1418 C CB  . PHE A 185 ? 0.48760 0.58830 0.47070 -0.02850 0.03730  0.07270  185 PHE A CB  
1419 C CG  . PHE A 185 ? 0.49260 0.57920 0.48210 -0.02920 0.03250  0.06730  185 PHE A CG  
1420 C CD1 . PHE A 185 ? 0.53910 0.62080 0.54190 -0.03380 0.02950  0.07210  185 PHE A CD1 
1421 C CD2 . PHE A 185 ? 0.52150 0.60050 0.50460 -0.02540 0.03120  0.05740  185 PHE A CD2 
1422 C CE1 . PHE A 185 ? 0.55490 0.62490 0.56320 -0.03440 0.02510  0.06550  185 PHE A CE1 
1423 C CE2 . PHE A 185 ? 0.52830 0.59630 0.51660 -0.02600 0.02690  0.05260  185 PHE A CE2 
1424 C CZ  . PHE A 185 ? 0.56360 0.62770 0.56350 -0.03050 0.02400  0.05610  185 PHE A CZ  
1425 N N   . VAL A 186 ? 0.53180 0.66800 0.51500 -0.03160 0.04760  0.09210  186 VAL A N   
1426 C CA  . VAL A 186 ? 0.52270 0.67600 0.49660 -0.03080 0.05270  0.09690  186 VAL A CA  
1427 C C   . VAL A 186 ? 0.52750 0.68070 0.49460 -0.03220 0.05020  0.10350  186 VAL A C   
1428 O O   . VAL A 186 ? 0.54590 0.68800 0.52070 -0.03500 0.04540  0.10850  186 VAL A O   
1429 C CB  . VAL A 186 ? 0.52820 0.69650 0.51220 -0.03380 0.05720  0.10740  186 VAL A CB  
1430 C CG1 . VAL A 186 ? 0.55820 0.73050 0.54690 -0.03140 0.06060  0.10040  186 VAL A CG1 
1431 C CG2 . VAL A 186 ? 0.49490 0.65640 0.49530 -0.03940 0.05340  0.11840  186 VAL A CG2 
1432 N N   . ASP A 187 ? 0.52210 0.68880 0.47520 -0.03020 0.05340  0.10330  187 ASP A N   
1433 C CA  . ASP A 187 ? 0.56210 0.73020 0.50650 -0.03100 0.05050  0.10840  187 ASP A CA  
1434 C C   . ASP A 187 ? 0.56910 0.75080 0.51970 -0.03520 0.05200  0.12600  187 ASP A C   
1435 O O   . ASP A 187 ? 0.55350 0.75400 0.49430 -0.03510 0.05560  0.13190  187 ASP A O   
1436 C CB  . ASP A 187 ? 0.47010 0.64610 0.39640 -0.02700 0.05230  0.09850  187 ASP A CB  
1437 C CG  . ASP A 187 ? 0.57210 0.76800 0.49180 -0.02510 0.05970  0.09630  187 ASP A CG  
1438 O OD1 . ASP A 187 ? 0.55530 0.75730 0.48490 -0.02630 0.06340  0.10120  187 ASP A OD1 
1439 O OD2 . ASP A 187 ? 0.56510 0.77100 0.47050 -0.02240 0.06170  0.08900  187 ASP A OD2 
1440 N N   . ARG A 188 ? 0.55130 0.72330 0.51910 -0.03900 0.04920  0.13440  188 ARG A N   
1441 C CA  . ARG A 188 ? 0.62670 0.80720 0.60520 -0.04360 0.04950  0.15240  188 ARG A CA  
1442 C C   . ARG A 188 ? 0.58420 0.74630 0.57860 -0.04650 0.04350  0.15650  188 ARG A C   
1443 O O   . ARG A 188 ? 0.58570 0.73210 0.58700 -0.04620 0.04080  0.14680  188 ARG A O   
1451 N N   . GLN A 189 ? 0.63400 0.79940 0.63540 -0.04950 0.04160  0.17140  189 GLN A N   
1452 C CA  . GLN A 189 ? 0.66140 0.81000 0.68020 -0.05230 0.03620  0.17620  189 GLN A CA  
1453 C C   . GLN A 189 ? 0.68110 0.82700 0.72270 -0.05680 0.03700  0.18350  189 GLN A C   
1454 O O   . GLN A 189 ? 0.69670 0.84340 0.75490 -0.06070 0.03590  0.19820  189 GLN A O   
1455 C CB  . GLN A 189 ? 0.64740 0.80030 0.66590 -0.05330 0.03360  0.18940  189 GLN A CB  
1456 C CG  . GLN A 189 ? 0.66370 0.81970 0.66060 -0.04920 0.03250  0.18080  189 GLN A CG  
1457 C CD  . GLN A 189 ? 0.70810 0.86320 0.70510 -0.04950 0.02800  0.19000  189 GLN A CD  
1458 O OE1 . GLN A 189 ? 0.70770 0.85470 0.69510 -0.04670 0.02460  0.18060  189 GLN A OE1 
1459 N NE2 . GLN A 189 ? 0.63590 0.80070 0.64430 -0.05280 0.02810  0.20920  189 GLN A NE2 
1460 N N   . THR A 190 ? 0.67730 0.82110 0.72070 -0.05630 0.03890  0.17340  190 THR A N   
1461 C CA  . THR A 190 ? 0.66430 0.80310 0.72900 -0.06040 0.03850  0.17580  190 THR A CA  
1462 C C   . THR A 190 ? 0.68800 0.80570 0.76120 -0.06060 0.03320  0.16370  190 THR A C   
1463 O O   . THR A 190 ? 0.64440 0.75200 0.70560 -0.05710 0.03050  0.15250  190 THR A O   
1464 C CB  . THR A 190 ? 0.70550 0.85600 0.76740 -0.05980 0.04350  0.17170  190 THR A CB  
1465 O OG1 . THR A 190 ? 0.63770 0.78490 0.68170 -0.05460 0.04380  0.15560  190 THR A OG1 
1466 C CG2 . THR A 190 ? 0.73850 0.91110 0.79600 -0.06040 0.04930  0.18490  190 THR A CG2 
1467 N N   . ALA A 191 ? 0.67710 0.78950 0.77140 -0.06490 0.03200  0.16560  191 ALA A N   
1468 C CA  . ALA A 191 ? 0.67850 0.77360 0.78170 -0.06560 0.02730  0.15310  191 ALA A CA  
1469 C C   . ALA A 191 ? 0.66590 0.76120 0.75570 -0.06200 0.02810  0.13820  191 ALA A C   
1470 O O   . ALA A 191 ? 0.67040 0.77590 0.76200 -0.06260 0.03120  0.13820  191 ALA A O   
1471 C CB  . ALA A 191 ? 0.72600 0.81720 0.85600 -0.07150 0.02580  0.15850  191 ALA A CB  
1472 N N   . GLN A 192 ? 0.64000 0.72490 0.71690 -0.05820 0.02550  0.12640  192 GLN A N   
1473 C CA  . GLN A 192 ? 0.61400 0.69790 0.67860 -0.05440 0.02570  0.11290  192 GLN A CA  
1474 C C   . GLN A 192 ? 0.66090 0.72880 0.72610 -0.05350 0.02090  0.10190  192 GLN A C   
1475 O O   . GLN A 192 ? 0.63370 0.69270 0.70080 -0.05380 0.01840  0.10370  192 GLN A O   
1476 C CB  . GLN A 192 ? 0.59040 0.68200 0.63360 -0.04920 0.02900  0.11020  192 GLN A CB  
1477 C CG  . GLN A 192 ? 0.59160 0.70090 0.63140 -0.04950 0.03440  0.12040  192 GLN A CG  
1478 C CD  . GLN A 192 ? 0.48750 0.60400 0.50710 -0.04450 0.03740  0.11530  192 GLN A CD  
1479 O OE1 . GLN A 192 ? 0.50310 0.61760 0.51480 -0.04090 0.03800  0.10400  192 GLN A OE1 
1480 N NE2 . GLN A 192 ? 0.51380 0.63970 0.52570 -0.04440 0.03920  0.12350  192 GLN A NE2 
1481 N N   . ALA A 193 ? 0.59110 0.65630 0.65460 -0.05230 0.01970  0.09100  193 ALA A N   
1482 C CA  . ALA A 193 ? 0.64150 0.69360 0.70570 -0.05180 0.01540  0.08040  193 ALA A CA  
1483 C C   . ALA A 193 ? 0.61110 0.66390 0.66160 -0.04750 0.01560  0.07000  193 ALA A C   
1484 O O   . ALA A 193 ? 0.64200 0.70420 0.69090 -0.04650 0.01780  0.06930  193 ALA A O   
1485 C CB  . ALA A 193 ? 0.63220 0.67960 0.71610 -0.05680 0.01210  0.07810  193 ALA A CB  
1486 N N   . ALA A 194 ? 0.65370 0.69690 0.69570 -0.04470 0.01340  0.06260  194 ALA A N   
1487 C CA  . ALA A 194 ? 0.56790 0.61010 0.59930 -0.04090 0.01290  0.05310  194 ALA A CA  
1488 C C   . ALA A 194 ? 0.64940 0.69300 0.68990 -0.04320 0.01050  0.04770  194 ALA A C   
1489 O O   . ALA A 194 ? 0.66000 0.69870 0.71270 -0.04710 0.00760  0.04620  194 ALA A O   
1490 C CB  . ALA A 194 ? 0.64820 0.67970 0.67240 -0.03860 0.01070  0.04730  194 ALA A CB  
1491 N N   . GLY A 195 ? 0.64750 0.69830 0.68310 -0.04070 0.01160  0.04460  195 GLY A N   
1492 C CA  . GLY A 195 ? 0.61750 0.67070 0.66010 -0.04250 0.00860  0.03900  195 GLY A CA  
1493 C C   . GLY A 195 ? 0.66670 0.71100 0.70570 -0.04190 0.00490  0.03030  195 GLY A C   
1494 O O   . GLY A 195 ? 0.62820 0.66470 0.65890 -0.03940 0.00510  0.02860  195 GLY A O   
1495 N N   . THR A 196 ? 0.68430 0.73090 0.72950 -0.04410 0.00150  0.02440  196 THR A N   
1496 C CA  . THR A 196 ? 0.65810 0.69830 0.69900 -0.04340 -0.00170 0.01560  196 THR A CA  
1497 C C   . THR A 196 ? 0.59430 0.63410 0.62010 -0.03780 -0.00040 0.01370  196 THR A C   
1498 O O   . THR A 196 ? 0.54920 0.59590 0.57000 -0.03480 0.00150  0.01630  196 THR A O   
1499 C CB  . THR A 196 ? 0.68320 0.72900 0.73200 -0.04680 -0.00570 0.00910  196 THR A CB  
1500 O OG1 . THR A 196 ? 0.71640 0.77330 0.76270 -0.04500 -0.00530 0.01100  196 THR A OG1 
1501 C CG2 . THR A 196 ? 0.60050 0.64550 0.66710 -0.05290 -0.00720 0.01020  196 THR A CG2 
1502 N N   . ASP A 197 ? 0.60720 0.63860 0.62700 -0.03630 -0.00110 0.00970  197 ASP A N   
1503 C CA  . ASP A 197 ? 0.57000 0.60010 0.57700 -0.03120 0.00020  0.00840  197 ASP A CA  
1504 C C   . ASP A 197 ? 0.59460 0.62790 0.59830 -0.03050 -0.00250 0.00180  197 ASP A C   
1505 O O   . ASP A 197 ? 0.57130 0.60700 0.58140 -0.03400 -0.00560 -0.00320 197 ASP A O   
1506 C CB  . ASP A 197 ? 0.52610 0.54660 0.52800 -0.02960 0.00140  0.00900  197 ASP A CB  
1507 C CG  . ASP A 197 ? 0.56780 0.58770 0.55830 -0.02460 0.00380  0.01020  197 ASP A CG  
1508 O OD1 . ASP A 197 ? 0.52430 0.55080 0.51220 -0.02220 0.00560  0.01250  197 ASP A OD1 
1509 O OD2 . ASP A 197 ? 0.53460 0.54740 0.52020 -0.02290 0.00390  0.00850  197 ASP A OD2 
1510 N N   . THR A 198 ? 0.54090 0.57540 0.53510 -0.02610 -0.00140 0.00210  198 THR A N   
1511 C CA  . THR A 198 ? 0.49100 0.53010 0.48080 -0.02480 -0.00360 -0.00230 198 THR A CA  
1512 C C   . THR A 198 ? 0.48750 0.52070 0.46820 -0.02080 -0.00180 -0.00230 198 THR A C   
1513 O O   . THR A 198 ? 0.46990 0.49670 0.44790 -0.01880 0.00080  0.00100  198 THR A O   
1514 C CB  . THR A 198 ? 0.53660 0.58720 0.52770 -0.02370 -0.00430 0.00030  198 THR A CB  
1515 O OG1 . THR A 198 ? 0.60440 0.65470 0.59300 -0.01990 -0.00090 0.00590  198 THR A OG1 
1516 C CG2 . THR A 198 ? 0.58750 0.64430 0.58910 -0.02810 -0.00600 0.00070  198 THR A CG2 
1517 N N   . THR A 199 ? 0.46980 0.50620 0.44600 -0.01970 -0.00330 -0.00580 199 THR A N   
1518 C CA  . THR A 199 ? 0.45630 0.48780 0.42500 -0.01600 -0.00160 -0.00540 199 THR A CA  
1519 C C   . THR A 199 ? 0.46250 0.49930 0.42820 -0.01200 -0.00030 -0.00020 199 THR A C   
1520 O O   . THR A 199 ? 0.47380 0.52080 0.44110 -0.01180 -0.00190 0.00130  199 THR A O   
1521 C CB  . THR A 199 ? 0.46320 0.49570 0.42890 -0.01690 -0.00320 -0.01150 199 THR A CB  
1522 O OG1 . THR A 199 ? 0.49750 0.52330 0.46830 -0.02030 -0.00390 -0.01650 199 THR A OG1 
1523 C CG2 . THR A 199 ? 0.45540 0.48420 0.41430 -0.01340 -0.00130 -0.01040 199 THR A CG2 
1524 N N   . ILE A 200 ? 0.44120 0.47160 0.40400 -0.00880 0.00230  0.00250  200 ILE A N   
1525 C CA  . ILE A 200 ? 0.41010 0.44370 0.37250 -0.00470 0.00390  0.00720  200 ILE A CA  
1526 C C   . ILE A 200 ? 0.46670 0.50470 0.42570 -0.00280 0.00310  0.00800  200 ILE A C   
1527 O O   . ILE A 200 ? 0.43630 0.46870 0.39210 -0.00110 0.00440  0.00810  200 ILE A O   
1528 C CB  . ILE A 200 ? 0.42840 0.45380 0.39000 -0.00230 0.00700  0.00860  200 ILE A CB  
1529 C CG1 . ILE A 200 ? 0.45090 0.47370 0.41460 -0.00460 0.00780  0.00810  200 ILE A CG1 
1530 C CG2 . ILE A 200 ? 0.47880 0.50750 0.44320 0.00190  0.00880  0.01260  200 ILE A CG2 
1531 C CD1 . ILE A 200 ? 0.42230 0.43620 0.38280 -0.00410 0.00950  0.00750  200 ILE A CD1 
1532 N N   . THR A 201 ? 0.43820 0.48760 0.39850 -0.00300 0.00090  0.00960  201 THR A N   
1533 C CA  . THR A 201 ? 0.44810 0.50520 0.40470 -0.00160 -0.00040 0.01130  201 THR A CA  
1534 C C   . THR A 201 ? 0.42320 0.47750 0.38000 0.00260  0.00210  0.01700  201 THR A C   
1535 O O   . THR A 201 ? 0.44470 0.49910 0.39720 0.00340  0.00260  0.01730  201 THR A O   
1536 C CB  . THR A 201 ? 0.44760 0.51880 0.40680 -0.00220 -0.00330 0.01360  201 THR A CB  
1537 O OG1 . THR A 201 ? 0.44030 0.51300 0.40170 -0.00660 -0.00550 0.00810  201 THR A OG1 
1538 C CG2 . THR A 201 ? 0.48520 0.56770 0.43950 -0.00160 -0.00530 0.01520  201 THR A CG2 
1539 N N   . VAL A 202 ? 0.41580 0.46830 0.37840 0.00550  0.00390  0.02150  202 VAL A N   
1540 C CA  . VAL A 202 ? 0.45180 0.50180 0.41720 0.00950  0.00610  0.02700  202 VAL A CA  
1541 C C   . VAL A 202 ? 0.43600 0.47460 0.39810 0.00950  0.00810  0.02400  202 VAL A C   
1542 O O   . VAL A 202 ? 0.45460 0.49230 0.41710 0.01160  0.00920  0.02750  202 VAL A O   
1543 C CB  . VAL A 202 ? 0.43850 0.48800 0.41270 0.01270  0.00800  0.03080  202 VAL A CB  
1544 C CG1 . VAL A 202 ? 0.39300 0.43370 0.36810 0.01210  0.01020  0.02610  202 VAL A CG1 
1545 C CG2 . VAL A 202 ? 0.42620 0.47440 0.40650 0.01700  0.00990  0.03730  202 VAL A CG2 
1546 N N   . ASN A 203 ? 0.42280 0.45340 0.38250 0.00720  0.00840  0.01830  203 ASN A N   
1547 C CA  . ASN A 203 ? 0.47800 0.49870 0.43510 0.00690  0.00970  0.01550  203 ASN A CA  
1548 C C   . ASN A 203 ? 0.46290 0.48520 0.41490 0.00540  0.00880  0.01340  203 ASN A C   
1549 O O   . ASN A 203 ? 0.44880 0.46690 0.40020 0.00660  0.01010  0.01420  203 ASN A O   
1550 C CB  . ASN A 203 ? 0.42130 0.43480 0.37760 0.00490  0.01000  0.01130  203 ASN A CB  
1551 C CG  . ASN A 203 ? 0.40840 0.41990 0.36870 0.00680  0.01190  0.01250  203 ASN A CG  
1552 O OD1 . ASN A 203 ? 0.39180 0.40630 0.35680 0.00980  0.01310  0.01590  203 ASN A OD1 
1553 N ND2 . ASN A 203 ? 0.41140 0.41840 0.37030 0.00520  0.01250  0.00970  203 ASN A ND2 
1554 N N   . VAL A 204 ? 0.46130 0.49000 0.41050 0.00270  0.00650  0.01000  204 VAL A N   
1555 C CA  . VAL A 204 ? 0.45410 0.48620 0.39870 0.00160  0.00600  0.00690  204 VAL A CA  
1556 C C   . VAL A 204 ? 0.48630 0.52600 0.42970 0.00430  0.00680  0.01270  204 VAL A C   
1557 O O   . VAL A 204 ? 0.43890 0.47720 0.38000 0.00500  0.00840  0.01270  204 VAL A O   
1558 C CB  . VAL A 204 ? 0.49730 0.53640 0.44020 -0.00180 0.00340  0.00120  204 VAL A CB  
1559 C CG1 . VAL A 204 ? 0.45160 0.49590 0.38940 -0.00270 0.00320  -0.00360 204 VAL A CG1 
1560 C CG2 . VAL A 204 ? 0.41660 0.44790 0.36300 -0.00460 0.00270  -0.00310 204 VAL A CG2 
1561 N N   . LEU A 205 ? 0.41620 0.46480 0.36200 0.00580  0.00590  0.01860  205 LEU A N   
1562 C CA  . LEU A 205 ? 0.47050 0.52670 0.41700 0.00860  0.00680  0.02640  205 LEU A CA  
1563 C C   . LEU A 205 ? 0.44260 0.48890 0.39360 0.01120  0.00980  0.03030  205 LEU A C   
1564 O O   . LEU A 205 ? 0.47590 0.52480 0.42560 0.01220  0.01130  0.03360  205 LEU A O   
1565 C CB  . LEU A 205 ? 0.43030 0.49690 0.38090 0.01020  0.00510  0.03310  205 LEU A CB  
1566 C CG  . LEU A 205 ? 0.44740 0.52770 0.39370 0.00760  0.00150  0.03030  205 LEU A CG  
1567 C CD1 . LEU A 205 ? 0.41870 0.50670 0.37150 0.00940  0.00000  0.03710  205 LEU A CD1 
1568 C CD2 . LEU A 205 ? 0.42040 0.51420 0.35900 0.00690  0.00030  0.03070  205 LEU A CD2 
1569 N N   . ALA A 206 ? 0.42700 0.46290 0.38350 0.01210  0.01090  0.02950  206 ALA A N   
1570 C CA  . ALA A 206 ? 0.44890 0.47550 0.41050 0.01410  0.01340  0.03170  206 ALA A CA  
1571 C C   . ALA A 206 ? 0.42220 0.44430 0.37950 0.01270  0.01420  0.02810  206 ALA A C   
1572 O O   . ALA A 206 ? 0.42220 0.44310 0.38240 0.01420  0.01600  0.03220  206 ALA A O   
1573 C CB  . ALA A 206 ? 0.43330 0.45020 0.39930 0.01460  0.01420  0.02840  206 ALA A CB  
1574 N N   . TRP A 207 ? 0.41740 0.43670 0.36900 0.01000  0.01310  0.02090  207 TRP A N   
1575 C CA  . TRP A 207 ? 0.47730 0.49160 0.42610 0.00870  0.01390  0.01670  207 TRP A CA  
1576 C C   . TRP A 207 ? 0.48140 0.50500 0.42610 0.00880  0.01460  0.01780  207 TRP A C   
1577 O O   . TRP A 207 ? 0.46330 0.48450 0.40870 0.00940  0.01650  0.01840  207 TRP A O   
1578 C CB  . TRP A 207 ? 0.45220 0.46130 0.39850 0.00590  0.01250  0.00930  207 TRP A CB  
1579 C CG  . TRP A 207 ? 0.48170 0.48670 0.42620 0.00440  0.01290  0.00400  207 TRP A CG  
1580 C CD1 . TRP A 207 ? 0.49110 0.48680 0.43800 0.00440  0.01370  0.00270  207 TRP A CD1 
1581 C CD2 . TRP A 207 ? 0.48900 0.49930 0.43020 0.00260  0.01230  -0.00130 207 TRP A CD2 
1582 N NE1 . TRP A 207 ? 0.47160 0.46640 0.41750 0.00300  0.01380  -0.00230 207 TRP A NE1 
1583 C CE2 . TRP A 207 ? 0.49970 0.50300 0.44230 0.00200  0.01320  -0.00530 207 TRP A CE2 
1584 C CE3 . TRP A 207 ? 0.47760 0.49860 0.41530 0.00140  0.01090  -0.00350 207 TRP A CE3 
1585 C CZ2 . TRP A 207 ? 0.48880 0.49440 0.43050 0.00050  0.01320  -0.01210 207 TRP A CZ2 
1586 C CZ3 . TRP A 207 ? 0.54410 0.56800 0.47980 -0.00040 0.01070  -0.01100 207 TRP A CZ3 
1587 C CH2 . TRP A 207 ? 0.47570 0.49150 0.41370 -0.00070 0.01210  -0.01530 207 TRP A CH2 
1588 N N   . LEU A 208 ? 0.45900 0.49480 0.39980 0.00820  0.01310  0.01840  208 LEU A N   
1589 C CA  . LEU A 208 ? 0.44330 0.49080 0.37980 0.00880  0.01410  0.02090  208 LEU A CA  
1590 C C   . LEU A 208 ? 0.48310 0.53250 0.42450 0.01160  0.01630  0.03090  208 LEU A C   
1591 O O   . LEU A 208 ? 0.45710 0.51100 0.39690 0.01220  0.01850  0.03310  208 LEU A O   
1592 C CB  . LEU A 208 ? 0.42260 0.48490 0.35400 0.00780  0.01150  0.02060  208 LEU A CB  
1593 C CG  . LEU A 208 ? 0.47440 0.53620 0.40240 0.00440  0.00920  0.00990  208 LEU A CG  
1594 C CD1 . LEU A 208 ? 0.47090 0.54850 0.39490 0.00310  0.00620  0.00950  208 LEU A CD1 
1595 C CD2 . LEU A 208 ? 0.50520 0.56500 0.42970 0.00330  0.01110  0.00240  208 LEU A CD2 
1596 N N   . TYR A 209 ? 0.44190 0.48850 0.39040 0.01350  0.01610  0.03730  209 TYR A N   
1597 C CA  . TYR A 209 ? 0.49410 0.54050 0.45050 0.01620  0.01820  0.04690  209 TYR A CA  
1598 C C   . TYR A 209 ? 0.48940 0.52380 0.44980 0.01610  0.02050  0.04470  209 TYR A C   
1599 O O   . TYR A 209 ? 0.47750 0.51480 0.44070 0.01700  0.02270  0.05020  209 TYR A O   
1600 C CB  . TYR A 209 ? 0.43890 0.48280 0.40450 0.01830  0.01770  0.05250  209 TYR A CB  
1601 C CG  . TYR A 209 ? 0.46610 0.52440 0.43170 0.01950  0.01610  0.05980  209 TYR A CG  
1602 C CD1 . TYR A 209 ? 0.46160 0.53120 0.42950 0.02110  0.01700  0.07030  209 TYR A CD1 
1603 C CD2 . TYR A 209 ? 0.41160 0.47240 0.37660 0.01900  0.01360  0.05730  209 TYR A CD2 
1604 C CE1 . TYR A 209 ? 0.46110 0.54600 0.42880 0.02220  0.01510  0.07820  209 TYR A CE1 
1605 C CE2 . TYR A 209 ? 0.44650 0.52210 0.41160 0.01990  0.01160  0.06410  209 TYR A CE2 
1606 C CZ  . TYR A 209 ? 0.47030 0.55750 0.43700 0.02160  0.01210  0.07460  209 TYR A CZ  
1607 O OH  . TYR A 209 ? 0.44440 0.54750 0.41190 0.02260  0.00970  0.08250  209 TYR A OH  
1608 N N   . ALA A 210 ? 0.45730 0.47950 0.41820 0.01490  0.01980  0.03720  210 ALA A N   
1609 C CA  . ALA A 210 ? 0.47330 0.48570 0.43710 0.01450  0.02120  0.03430  210 ALA A CA  
1610 C C   . ALA A 210 ? 0.51830 0.53570 0.47710 0.01360  0.02270  0.03270  210 ALA A C   
1611 O O   . ALA A 210 ? 0.49620 0.51140 0.45960 0.01420  0.02480  0.03560  210 ALA A O   
1612 C CB  . ALA A 210 ? 0.44870 0.45050 0.41090 0.01280  0.01970  0.02620  210 ALA A CB  
1613 N N   . ALA A 211 ? 0.48860 0.51310 0.43900 0.01210  0.02170  0.02770  211 ALA A N   
1614 C CA  . ALA A 211 ? 0.51500 0.54520 0.46080 0.01150  0.02340  0.02450  211 ALA A CA  
1615 C C   . ALA A 211 ? 0.55560 0.59740 0.50180 0.01310  0.02590  0.03310  211 ALA A C   
1616 O O   . ALA A 211 ? 0.49550 0.53800 0.44330 0.01340  0.02870  0.03390  211 ALA A O   
1617 C CB  . ALA A 211 ? 0.52330 0.55970 0.46120 0.00960  0.02180  0.01640  211 ALA A CB  
1618 N N   . VAL A 212 ? 0.49810 0.54980 0.44380 0.01420  0.02510  0.04040  212 VAL A N   
1619 C CA  . VAL A 212 ? 0.53540 0.59940 0.48270 0.01590  0.02740  0.05100  212 VAL A CA  
1620 C C   . VAL A 212 ? 0.54910 0.60450 0.50800 0.01720  0.02970  0.05820  212 VAL A C   
1621 O O   . VAL A 212 ? 0.52390 0.58520 0.48480 0.01780  0.03280  0.06350  212 VAL A O   
1622 C CB  . VAL A 212 ? 0.49930 0.57570 0.44560 0.01690  0.02550  0.05890  212 VAL A CB  
1623 C CG1 . VAL A 212 ? 0.51600 0.60440 0.46650 0.01890  0.02800  0.07270  212 VAL A CG1 
1624 C CG2 . VAL A 212 ? 0.48150 0.57030 0.41570 0.01520  0.02320  0.05180  212 VAL A CG2 
1625 N N   . ILE A 213 ? 0.51690 0.55940 0.48430 0.01770  0.02850  0.05820  213 ILE A N   
1626 C CA  . ILE A 213 ? 0.53020 0.56390 0.51030 0.01870  0.03020  0.06350  213 ILE A CA  
1627 C C   . ILE A 213 ? 0.55760 0.58580 0.53780 0.01750  0.03200  0.05860  213 ILE A C   
1628 O O   . ILE A 213 ? 0.48760 0.51510 0.47660 0.01800  0.03440  0.06470  213 ILE A O   
1629 C CB  . ILE A 213 ? 0.55400 0.57520 0.54190 0.01920  0.02840  0.06120  213 ILE A CB  
1630 C CG1 . ILE A 213 ? 0.53220 0.55980 0.52380 0.02110  0.02740  0.06850  213 ILE A CG1 
1631 C CG2 . ILE A 213 ? 0.56740 0.57750 0.56750 0.01940  0.02960  0.06220  213 ILE A CG2 
1632 C CD1 . ILE A 213 ? 0.49630 0.51380 0.49350 0.02180  0.02560  0.06420  213 ILE A CD1 
1633 N N   . ASN A 214 ? 0.49870 0.52370 0.47040 0.01590  0.03080  0.04820  214 ASN A N   
1634 C CA  . ASN A 214 ? 0.60190 0.62250 0.57440 0.01500  0.03240  0.04340  214 ASN A CA  
1635 C C   . ASN A 214 ? 0.57130 0.60400 0.53760 0.01490  0.03530  0.04330  214 ASN A C   
1636 O O   . ASN A 214 ? 0.56620 0.59550 0.53330 0.01430  0.03660  0.03820  214 ASN A O   
1637 C CB  . ASN A 214 ? 0.48570 0.49590 0.45480 0.01340  0.02990  0.03300  214 ASN A CB  
1638 C CG  . ASN A 214 ? 0.60650 0.60390 0.58370 0.01320  0.02820  0.03230  214 ASN A CG  
1639 O OD1 . ASN A 214 ? 0.64110 0.63250 0.62380 0.01270  0.02870  0.03100  214 ASN A OD1 
1640 N ND2 . ASN A 214 ? 0.63850 0.63260 0.61690 0.01370  0.02630  0.03300  214 ASN A ND2 
1641 N N   . GLY A 215 ? 0.55480 0.60230 0.51490 0.01560  0.03620  0.04800  215 GLY A N   
1642 C CA  . GLY A 215 ? 0.61740 0.67900 0.57080 0.01570  0.03930  0.04720  215 GLY A CA  
1643 C C   . GLY A 215 ? 0.64520 0.71430 0.58660 0.01460  0.03830  0.03670  215 GLY A C   
1644 O O   . GLY A 215 ? 0.63280 0.71460 0.56830 0.01470  0.04120  0.03470  215 GLY A O   
1645 N N   . ASP A 216 ? 0.55860 0.62040 0.49710 0.01330  0.03460  0.02910  216 ASP A N   
1646 C CA  . ASP A 216 ? 0.58180 0.65120 0.51090 0.01190  0.03340  0.01920  216 ASP A CA  
1647 C C   . ASP A 216 ? 0.63930 0.72460 0.56190 0.01210  0.03190  0.02460  216 ASP A C   
1648 O O   . ASP A 216 ? 0.60730 0.68940 0.53170 0.01220  0.02890  0.02840  216 ASP A O   
1649 C CB  . ASP A 216 ? 0.63140 0.68810 0.56140 0.01020  0.02990  0.01020  216 ASP A CB  
1650 C CG  . ASP A 216 ? 0.72100 0.76500 0.65580 0.00960  0.03070  0.00280  216 ASP A CG  
1651 O OD1 . ASP A 216 ? 0.91890 0.96770 0.85330 0.01000  0.03380  -0.00100 216 ASP A OD1 
1652 O OD2 . ASP A 216 ? 0.58140 0.61180 0.52100 0.00880  0.02830  0.00130  216 ASP A OD2 
1653 N N   . ARG A 217 ? 0.59420 0.69740 0.50880 0.01230  0.03390  0.02430  217 ARG A N   
1654 C CA  . ARG A 217 ? 0.58640 0.70690 0.49450 0.01250  0.03210  0.03050  217 ARG A CA  
1655 C C   . ARG A 217 ? 0.54890 0.68350 0.44590 0.01080  0.03090  0.01970  217 ARG A C   
1656 O O   . ARG A 217 ? 0.51910 0.67080 0.40940 0.01070  0.02900  0.02380  217 ARG A O   
1657 C CB  . ARG A 217 ? 0.64690 0.78040 0.55610 0.01450  0.03550  0.04440  217 ARG A CB  
1658 C CG  . ARG A 217 ? 0.65570 0.77750 0.57740 0.01610  0.03610  0.05600  217 ARG A CG  
1659 C CD  . ARG A 217 ? 0.74300 0.87990 0.66700 0.01780  0.03960  0.07090  217 ARG A CD  
1660 N NE  . ARG A 217 ? 0.65650 0.81100 0.57550 0.01840  0.03740  0.07970  217 ARG A NE  
1661 C CZ  . ARG A 217 ? 0.65310 0.80500 0.58040 0.01970  0.03510  0.09040  217 ARG A CZ  
1662 N NH1 . ARG A 217 ? 0.61600 0.74880 0.55650 0.02050  0.03490  0.09290  217 ARG A NH1 
1663 N NH2 . ARG A 217 ? 0.59370 0.76320 0.51660 0.02030  0.03280  0.09840  217 ARG A NH2 
1664 N N   . TRP A 218 ? 0.51900 0.64700 0.41500 0.00940  0.03160  0.00570  218 TRP A N   
1665 C CA  . TRP A 218 ? 0.57340 0.71530 0.46030 0.00780  0.03130  -0.00630 218 TRP A CA  
1666 C C   . TRP A 218 ? 0.59910 0.74630 0.48200 0.00570  0.02600  -0.01020 218 TRP A C   
1667 O O   . TRP A 218 ? 0.55540 0.71930 0.42960 0.00440  0.02500  -0.01770 218 TRP A O   
1668 C CB  . TRP A 218 ? 0.62760 0.75830 0.51790 0.00690  0.03310  -0.02060 218 TRP A CB  
1669 C CG  . TRP A 218 ? 0.57850 0.68790 0.47730 0.00540  0.03000  -0.02620 218 TRP A CG  
1670 C CD1 . TRP A 218 ? 0.60450 0.69590 0.51250 0.00620  0.03080  -0.02280 218 TRP A CD1 
1671 C CD2 . TRP A 218 ? 0.62830 0.73380 0.52750 0.00280  0.02560  -0.03560 218 TRP A CD2 
1672 N NE1 . TRP A 218 ? 0.62170 0.69910 0.53470 0.00440  0.02750  -0.02910 218 TRP A NE1 
1673 C CE2 . TRP A 218 ? 0.61170 0.69710 0.52030 0.00230  0.02450  -0.03660 218 TRP A CE2 
1674 C CE3 . TRP A 218 ? 0.57530 0.69340 0.46850 0.00050  0.02260  -0.04320 218 TRP A CE3 
1675 C CZ2 . TRP A 218 ? 0.61420 0.69140 0.52670 -0.00030 0.02090  -0.04390 218 TRP A CZ2 
1676 C CZ3 . TRP A 218 ? 0.63680 0.74620 0.53460 -0.00210 0.01890  -0.05130 218 TRP A CZ3 
1677 C CH2 . TRP A 218 ? 0.63490 0.72380 0.54250 -0.00250 0.01810  -0.05080 218 TRP A CH2 
1678 N N   . PHE A 219 ? 0.51830 0.65130 0.40780 0.00530  0.02260  -0.00670 219 PHE A N   
1679 C CA  . PHE A 219 ? 0.54230 0.67900 0.43000 0.00320  0.01760  -0.01020 219 PHE A CA  
1680 C C   . PHE A 219 ? 0.56790 0.71960 0.45250 0.00430  0.01530  0.00220  219 PHE A C   
1681 O O   . PHE A 219 ? 0.52920 0.68580 0.41290 0.00270  0.01090  0.00050  219 PHE A O   
1682 C CB  . PHE A 219 ? 0.54100 0.65680 0.43780 0.00230  0.01550  -0.01230 219 PHE A CB  
1683 C CG  . PHE A 219 ? 0.50600 0.60890 0.41000 0.00460  0.01710  -0.00110 219 PHE A CG  
1684 C CD1 . PHE A 219 ? 0.51100 0.61680 0.41750 0.00610  0.01560  0.01050  219 PHE A CD1 
1685 C CD2 . PHE A 219 ? 0.47900 0.56720 0.38850 0.00530  0.01980  -0.00270 219 PHE A CD2 
1686 C CE1 . PHE A 219 ? 0.51080 0.60420 0.42540 0.00820  0.01710  0.01920  219 PHE A CE1 
1687 C CE2 . PHE A 219 ? 0.48750 0.56450 0.40390 0.00710  0.02090  0.00610  219 PHE A CE2 
1688 C CZ  . PHE A 219 ? 0.53030 0.60970 0.44940 0.00860  0.01980  0.01660  219 PHE A CZ  
1689 N N   . LEU A 220 ? 0.49770 0.65640 0.38250 0.00690  0.01800  0.01540  220 LEU A N   
1690 C CA  . LEU A 220 ? 0.55510 0.72880 0.43850 0.00810  0.01580  0.02840  220 LEU A CA  
1691 C C   . LEU A 220 ? 0.57290 0.77190 0.44430 0.00680  0.01410  0.02480  220 LEU A C   
1692 O O   . LEU A 220 ? 0.57030 0.77620 0.43430 0.00560  0.01620  0.01370  220 LEU A O   
1693 C CB  . LEU A 220 ? 0.52970 0.70290 0.41950 0.01130  0.01910  0.04450  220 LEU A CB  
1694 C CG  . LEU A 220 ? 0.52680 0.67630 0.42900 0.01250  0.02020  0.04760  220 LEU A CG  
1695 C CD1 . LEU A 220 ? 0.50260 0.65100 0.41260 0.01510  0.02380  0.06170  220 LEU A CD1 
1696 C CD2 . LEU A 220 ? 0.45230 0.59450 0.36050 0.01250  0.01610  0.04970  220 LEU A CD2 
1697 N N   . ASN A 221 ? 0.54420 0.75750 0.41390 0.00700  0.01020  0.03310  221 ASN A N   
1698 C CA  . ASN A 221 ? 0.55730 0.79730 0.41500 0.00560  0.00780  0.03100  221 ASN A CA  
1699 C C   . ASN A 221 ? 0.59630 0.85210 0.45540 0.00770  0.00560  0.04940  221 ASN A C   
1700 O O   . ASN A 221 ? 0.55800 0.80240 0.42840 0.01010  0.00590  0.06200  221 ASN A O   
1701 C CB  . ASN A 221 ? 0.57540 0.81810 0.42860 0.00180  0.00320  0.01410  221 ASN A CB  
1702 C CG  . ASN A 221 ? 0.64760 0.87960 0.50980 0.00100  -0.00160 0.01600  221 ASN A CG  
1703 O OD1 . ASN A 221 ? 0.64990 0.88490 0.51720 0.00300  -0.00320 0.03030  221 ASN A OD1 
1704 N ND2 . ASN A 221 ? 0.62360 0.84250 0.48890 -0.00190 -0.00340 0.00190  221 ASN A ND2 
1705 N N   . ARG A 222 ? 0.59260 0.87600 0.44060 0.00700  0.00370  0.05140  222 ARG A N   
1706 C CA  . ARG A 222 ? 0.64980 0.95050 0.49940 0.00920  0.00150  0.07040  222 ARG A CA  
1707 C C   . ARG A 222 ? 0.62720 0.93200 0.48010 0.00810  -0.00520 0.07140  222 ARG A C   
1708 O O   . ARG A 222 ? 0.65350 0.97260 0.50970 0.01000  -0.00760 0.08760  222 ARG A O   
1716 N N   . PHE A 223 ? 0.61130 0.90460 0.46490 0.00520  -0.00810 0.05550  223 PHE A N   
1717 C CA  . PHE A 223 ? 0.65160 0.94960 0.50870 0.00360  -0.01440 0.05500  223 PHE A CA  
1718 C C   . PHE A 223 ? 0.60950 0.88840 0.48220 0.00600  -0.01450 0.06490  223 PHE A C   
1719 O O   . PHE A 223 ? 0.53690 0.79280 0.41770 0.00760  -0.01030 0.06520  223 PHE A O   
1720 C CB  . PHE A 223 ? 0.62210 0.91530 0.47540 -0.00080 -0.01730 0.03390  223 PHE A CB  
1721 C CG  . PHE A 223 ? 0.75860 1.07140 0.59720 -0.00350 -0.01770 0.02100  223 PHE A CG  
1722 C CD1 . PHE A 223 ? 0.73720 1.08050 0.56610 -0.00440 -0.02190 0.02480  223 PHE A CD1 
1723 C CD2 . PHE A 223 ? 0.77190 1.07390 0.60720 -0.00500 -0.01380 0.00500  223 PHE A CD2 
1724 C CE1 . PHE A 223 ? 0.83770 1.20090 0.65240 -0.00690 -0.02220 0.01170  223 PHE A CE1 
1725 C CE2 . PHE A 223 ? 0.79680 1.11740 0.61960 -0.00730 -0.01380 -0.00820 223 PHE A CE2 
1726 C CZ  . PHE A 223 ? 0.83340 1.18460 0.64540 -0.00830 -0.01790 -0.00530 223 PHE A CZ  
1727 N N   . THR A 224 ? 0.55540 0.84410 0.43260 0.00600  -0.01970 0.07110  224 THR A N   
1728 C CA  . THR A 224 ? 0.61580 0.88730 0.50770 0.00780  -0.02020 0.07660  224 THR A CA  
1729 C C   . THR A 224 ? 0.59260 0.86840 0.48520 0.00440  -0.02590 0.06710  224 THR A C   
1730 O O   . THR A 224 ? 0.66310 0.95730 0.54590 0.00120  -0.03000 0.05920  224 THR A O   
1731 C CB  . THR A 224 ? 0.61150 0.88910 0.51400 0.01230  -0.01990 0.09800  224 THR A CB  
1732 O OG1 . THR A 224 ? 0.66340 0.92040 0.58100 0.01440  -0.01880 0.10080  224 THR A OG1 
1733 C CG2 . THR A 224 ? 0.64310 0.94790 0.54330 0.01200  -0.02600 0.10610  224 THR A CG2 
1734 N N   . THR A 225 ? 0.60770 0.86690 0.51210 0.00500  -0.02600 0.06730  225 THR A N   
1735 C CA  . THR A 225 ? 0.54290 0.80420 0.45010 0.00180  -0.03090 0.05890  225 THR A CA  
1736 C C   . THR A 225 ? 0.55770 0.81770 0.47890 0.00480  -0.03220 0.07140  225 THR A C   
1737 O O   . THR A 225 ? 0.54310 0.79470 0.47270 0.00920  -0.02860 0.08340  225 THR A O   
1738 C CB  . THR A 225 ? 0.53460 0.77520 0.44220 -0.00140 -0.02900 0.04240  225 THR A CB  
1739 O OG1 . THR A 225 ? 0.54380 0.78570 0.45580 -0.00510 -0.03350 0.03420  225 THR A OG1 
1740 C CG2 . THR A 225 ? 0.52220 0.73840 0.43870 0.00150  -0.02380 0.04610  225 THR A CG2 
1741 N N   . THR A 226 ? 0.55410 0.82310 0.47900 0.00250  -0.03730 0.06840  226 THR A N   
1742 C CA  . THR A 226 ? 0.52850 0.79170 0.46850 0.00520  -0.03760 0.07720  226 THR A CA  
1743 C C   . THR A 226 ? 0.49710 0.73570 0.44360 0.00430  -0.03410 0.06800  226 THR A C   
1744 O O   . THR A 226 ? 0.49490 0.72390 0.43540 0.00050  -0.03340 0.05420  226 THR A O   
1745 C CB  . THR A 226 ? 0.52750 0.81100 0.47110 0.00360  -0.04430 0.07970  226 THR A CB  
1746 O OG1 . THR A 226 ? 0.55410 0.83820 0.49300 -0.00210 -0.04750 0.06370  226 THR A OG1 
1747 C CG2 . THR A 226 ? 0.55220 0.86360 0.49010 0.00450  -0.04870 0.09060  226 THR A CG2 
1748 N N   . LEU A 227 ? 0.49820 0.72670 0.45790 0.00800  -0.03170 0.07590  227 LEU A N   
1749 C CA  . LEU A 227 ? 0.50350 0.71200 0.46920 0.00720  -0.02870 0.06820  227 LEU A CA  
1750 C C   . LEU A 227 ? 0.49370 0.70670 0.45890 0.00200  -0.03270 0.05760  227 LEU A C   
1751 O O   . LEU A 227 ? 0.43710 0.63650 0.40000 -0.00120 -0.03110 0.04630  227 LEU A O   
1752 C CB  . LEU A 227 ? 0.45650 0.65820 0.43670 0.01210  -0.02590 0.07850  227 LEU A CB  
1753 C CG  . LEU A 227 ? 0.53200 0.71430 0.51890 0.01240  -0.02180 0.07260  227 LEU A CG  
1754 C CD1 . LEU A 227 ? 0.47100 0.63610 0.45010 0.01140  -0.01790 0.06500  227 LEU A CD1 
1755 C CD2 . LEU A 227 ? 0.51060 0.68950 0.51270 0.01770  -0.01910 0.08240  227 LEU A CD2 
1756 N N   . ASN A 228 ? 0.51590 0.74860 0.48390 0.00090  -0.03820 0.06120  228 ASN A N   
1757 C CA  . ASN A 228 ? 0.50060 0.73910 0.46970 -0.00430 -0.04250 0.05130  228 ASN A CA  
1758 C C   . ASN A 228 ? 0.50120 0.73980 0.45870 -0.00950 -0.04410 0.03710  228 ASN A C   
1759 O O   . ASN A 228 ? 0.49070 0.71840 0.45020 -0.01340 -0.04370 0.02610  228 ASN A O   
1760 C CB  . ASN A 228 ? 0.53450 0.79630 0.50840 -0.00470 -0.04880 0.05790  228 ASN A CB  
1761 C CG  . ASN A 228 ? 0.54690 0.80780 0.53620 -0.00070 -0.04760 0.06860  228 ASN A CG  
1762 O OD1 . ASN A 228 ? 0.54770 0.79100 0.54390 0.00070  -0.04280 0.06730  228 ASN A OD1 
1763 N ND2 . ASN A 228 ? 0.61710 0.89830 0.61220 0.00090  -0.05230 0.07880  228 ASN A ND2 
1764 N N   . ASP A 229 ? 0.53170 0.78190 0.47760 -0.00940 -0.04530 0.03710  229 ASP A N   
1765 C CA  . ASP A 229 ? 0.48600 0.73670 0.42160 -0.01390 -0.04620 0.02240  229 ASP A CA  
1766 C C   . ASP A 229 ? 0.48570 0.71210 0.42050 -0.01390 -0.04040 0.01550  229 ASP A C   
1767 O O   . ASP A 229 ? 0.49800 0.71700 0.43200 -0.01810 -0.04080 0.00220  229 ASP A O   
1768 C CB  . ASP A 229 ? 0.57400 0.84410 0.49700 -0.01350 -0.04820 0.02420  229 ASP A CB  
1769 C CG  . ASP A 229 ? 0.60880 0.90620 0.53100 -0.01500 -0.05540 0.02800  229 ASP A CG  
1770 O OD1 . ASP A 229 ? 0.64000 0.94050 0.57050 -0.01810 -0.05950 0.02420  229 ASP A OD1 
1771 O OD2 . ASP A 229 ? 0.61530 0.93150 0.52920 -0.01330 -0.05690 0.03560  229 ASP A OD2 
1772 N N   . PHE A 230 ? 0.47660 0.69000 0.41370 -0.00920 -0.03530 0.02440  230 PHE A N   
1773 C CA  . PHE A 230 ? 0.49220 0.68340 0.42900 -0.00920 -0.03020 0.01830  230 PHE A CA  
1774 C C   . PHE A 230 ? 0.50680 0.68520 0.45240 -0.01190 -0.03000 0.01230  230 PHE A C   
1775 O O   . PHE A 230 ? 0.50290 0.66970 0.44760 -0.01490 -0.02890 0.00210  230 PHE A O   
1776 C CB  . PHE A 230 ? 0.44370 0.62400 0.38220 -0.00400 -0.02510 0.02840  230 PHE A CB  
1777 C CG  . PHE A 230 ? 0.47120 0.62960 0.41050 -0.00410 -0.02060 0.02260  230 PHE A CG  
1778 C CD1 . PHE A 230 ? 0.48540 0.63870 0.41670 -0.00540 -0.01870 0.01490  230 PHE A CD1 
1779 C CD2 . PHE A 230 ? 0.48030 0.62480 0.42820 -0.00330 -0.01840 0.02380  230 PHE A CD2 
1780 C CE1 . PHE A 230 ? 0.48420 0.61840 0.41710 -0.00570 -0.01510 0.00990  230 PHE A CE1 
1781 C CE2 . PHE A 230 ? 0.55000 0.67610 0.49800 -0.00380 -0.01480 0.01830  230 PHE A CE2 
1782 C CZ  . PHE A 230 ? 0.49950 0.62060 0.44020 -0.00490 -0.01340 0.01190  230 PHE A CZ  
1783 N N   . ASN A 231 ? 0.44230 0.62330 0.39730 -0.01070 -0.03110 0.01910  231 ASN A N   
1784 C CA  . ASN A 231 ? 0.48650 0.65650 0.45010 -0.01300 -0.03020 0.01490  231 ASN A CA  
1785 C C   . ASN A 231 ? 0.47270 0.64760 0.43750 -0.01920 -0.03440 0.00350  231 ASN A C   
1786 O O   . ASN A 231 ? 0.50860 0.67100 0.47870 -0.02200 -0.03290 -0.00230 231 ASN A O   
1787 C CB  . ASN A 231 ? 0.42040 0.59360 0.39420 -0.00980 -0.02970 0.02500  231 ASN A CB  
1788 C CG  . ASN A 231 ? 0.47400 0.63330 0.44980 -0.00470 -0.02400 0.03190  231 ASN A CG  
1789 O OD1 . ASN A 231 ? 0.52000 0.66440 0.49180 -0.00480 -0.02050 0.02740  231 ASN A OD1 
1790 N ND2 . ASN A 231 ? 0.47660 0.64080 0.45950 -0.00020 -0.02320 0.04220  231 ASN A ND2 
1791 N N   . LEU A 232 ? 0.47570 0.66900 0.43630 -0.02170 -0.03970 0.00000  232 LEU A N   
1792 C CA  . LEU A 232 ? 0.49700 0.69450 0.45910 -0.02790 -0.04370 -0.01310 232 LEU A CA  
1793 C C   . LEU A 232 ? 0.53960 0.72250 0.49760 -0.02990 -0.04090 -0.02380 232 LEU A C   
1794 O O   . LEU A 232 ? 0.54850 0.72390 0.51350 -0.03430 -0.04160 -0.03290 232 LEU A O   
1795 C CB  . LEU A 232 ? 0.49350 0.71420 0.44980 -0.03020 -0.04980 -0.01650 232 LEU A CB  
1796 C CG  . LEU A 232 ? 0.58930 0.82880 0.55210 -0.03140 -0.05550 -0.01150 232 LEU A CG  
1797 C CD1 . LEU A 232 ? 0.57700 0.80820 0.55440 -0.03210 -0.05470 -0.00770 232 LEU A CD1 
1798 C CD2 . LEU A 232 ? 0.59130 0.84890 0.54850 -0.02730 -0.05750 0.00030  232 LEU A CD2 
1799 N N   . VAL A 233 ? 0.48620 0.66650 0.43420 -0.02680 -0.03780 -0.02280 233 VAL A N   
1800 C CA  . VAL A 233 ? 0.52600 0.69250 0.47090 -0.02790 -0.03470 -0.03220 233 VAL A CA  
1801 C C   . VAL A 233 ? 0.50830 0.65320 0.45990 -0.02670 -0.03010 -0.02930 233 VAL A C   
1802 O O   . VAL A 233 ? 0.51510 0.64860 0.47170 -0.02980 -0.02940 -0.03750 233 VAL A O   
1803 C CB  . VAL A 233 ? 0.54010 0.71200 0.47300 -0.02480 -0.03260 -0.03100 233 VAL A CB  
1804 C CG1 . VAL A 233 ? 0.63000 0.78760 0.56070 -0.02540 -0.02900 -0.04010 233 VAL A CG1 
1805 C CG2 . VAL A 233 ? 0.54700 0.74340 0.47220 -0.02630 -0.03750 -0.03390 233 VAL A CG2 
1806 N N   . ALA A 234 ? 0.53960 0.67930 0.49260 -0.02240 -0.02720 -0.01770 234 ALA A N   
1807 C CA  . ALA A 234 ? 0.53020 0.65230 0.48930 -0.02150 -0.02330 -0.01520 234 ALA A CA  
1808 C C   . ALA A 234 ? 0.49500 0.61390 0.46420 -0.02600 -0.02500 -0.01960 234 ALA A C   
1809 O O   . ALA A 234 ? 0.49270 0.59800 0.46590 -0.02770 -0.02290 -0.02300 234 ALA A O   
1810 C CB  . ALA A 234 ? 0.53780 0.65820 0.49890 -0.01680 -0.02070 -0.00350 234 ALA A CB  
1811 N N   . MET A 235 ? 0.51260 0.64430 0.48710 -0.02790 -0.02880 -0.01840 235 MET A N   
1812 C CA  . MET A 235 ? 0.56430 0.69380 0.55000 -0.03240 -0.03030 -0.02180 235 MET A CA  
1813 C C   . MET A 235 ? 0.59240 0.71670 0.58060 -0.03730 -0.03190 -0.03380 235 MET A C   
1814 O O   . MET A 235 ? 0.52260 0.63480 0.51870 -0.03970 -0.03010 -0.03560 235 MET A O   
1815 C CB  . MET A 235 ? 0.57350 0.71960 0.56490 -0.03390 -0.03460 -0.01890 235 MET A CB  
1816 C CG  . MET A 235 ? 0.69410 0.83940 0.69880 -0.03840 -0.03590 -0.02070 235 MET A CG  
1817 S SD  . MET A 235 ? 0.92970 1.09280 0.94210 -0.03780 -0.03910 -0.01250 235 MET A SD  
1818 C CE  . MET A 235 ? 0.60410 0.78770 0.60680 -0.03690 -0.04480 -0.01370 235 MET A CE  
1819 N N   . LYS A 236 ? 0.58860 0.72130 0.56990 -0.03850 -0.03450 -0.04200 236 LYS A N   
1820 C CA  . LYS A 236 ? 0.55140 0.67950 0.53660 -0.04300 -0.03590 -0.05500 236 LYS A CA  
1821 C C   . LYS A 236 ? 0.53960 0.64890 0.52530 -0.04170 -0.03120 -0.05630 236 LYS A C   
1822 O O   . LYS A 236 ? 0.53000 0.63050 0.52510 -0.04540 -0.03140 -0.06370 236 LYS A O   
1823 C CB  . LYS A 236 ? 0.57730 0.72080 0.55400 -0.04410 -0.03940 -0.06390 236 LYS A CB  
1824 C CG  . LYS A 236 ? 0.70120 0.84010 0.67900 -0.04720 -0.03960 -0.07870 236 LYS A CG  
1825 C CD  . LYS A 236 ? 0.81950 0.97790 0.78860 -0.04870 -0.04360 -0.08820 236 LYS A CD  
1826 C CE  . LYS A 236 ? 0.86480 1.01880 0.83320 -0.05050 -0.04250 -0.10350 236 LYS A CE  
1827 N NZ  . LYS A 236 ? 0.87400 1.01550 0.85910 -0.05530 -0.04330 -0.11310 236 LYS A NZ  
1828 N N   . TYR A 237 ? 0.54860 0.65140 0.52590 -0.03660 -0.02710 -0.04900 237 TYR A N   
1829 C CA  . TYR A 237 ? 0.50360 0.59000 0.48100 -0.03530 -0.02300 -0.04980 237 TYR A CA  
1830 C C   . TYR A 237 ? 0.50840 0.58320 0.49050 -0.03370 -0.02000 -0.04040 237 TYR A C   
1831 O O   . TYR A 237 ? 0.45430 0.51720 0.43470 -0.03160 -0.01660 -0.03830 237 TYR A O   
1832 C CB  . TYR A 237 ? 0.47270 0.55960 0.43810 -0.03120 -0.02060 -0.04950 237 TYR A CB  
1833 C CG  . TYR A 237 ? 0.53740 0.63440 0.49870 -0.03320 -0.02290 -0.06090 237 TYR A CG  
1834 C CD1 . TYR A 237 ? 0.57710 0.66610 0.54240 -0.03520 -0.02190 -0.07160 237 TYR A CD1 
1835 C CD2 . TYR A 237 ? 0.56210 0.67770 0.51650 -0.03340 -0.02610 -0.06140 237 TYR A CD2 
1836 C CE1 . TYR A 237 ? 0.61780 0.71690 0.57980 -0.03710 -0.02370 -0.08380 237 TYR A CE1 
1837 C CE2 . TYR A 237 ? 0.62930 0.75610 0.57920 -0.03550 -0.02830 -0.07280 237 TYR A CE2 
1838 C CZ  . TYR A 237 ? 0.61150 0.72980 0.56510 -0.03730 -0.02690 -0.08470 237 TYR A CZ  
1839 O OH  . TYR A 237 ? 0.66710 0.79730 0.61630 -0.03940 -0.02870 -0.09740 237 TYR A OH  
1840 N N   . ASN A 238 ? 0.49970 0.57890 0.48820 -0.03490 -0.02100 -0.03490 238 ASN A N   
1841 C CA  . ASN A 238 ? 0.51180 0.58190 0.50460 -0.03360 -0.01780 -0.02680 238 ASN A CA  
1842 C C   . ASN A 238 ? 0.49980 0.56520 0.48390 -0.02810 -0.01400 -0.01950 238 ASN A C   
1843 O O   . ASN A 238 ? 0.49380 0.54820 0.47820 -0.02680 -0.01090 -0.01620 238 ASN A O   
1844 C CB  . ASN A 238 ? 0.52580 0.58340 0.52670 -0.03660 -0.01670 -0.02980 238 ASN A CB  
1845 C CG  . ASN A 238 ? 0.63970 0.69220 0.64570 -0.03630 -0.01410 -0.02140 238 ASN A CG  
1846 O OD1 . ASN A 238 ? 0.65290 0.71310 0.65960 -0.03530 -0.01390 -0.01590 238 ASN A OD1 
1847 N ND2 . ASN A 238 ? 0.68400 0.72470 0.69280 -0.03650 -0.01170 -0.01960 238 ASN A ND2 
1848 N N   . TYR A 239 ? 0.49540 0.56940 0.47220 -0.02490 -0.01450 -0.01710 239 TYR A N   
1849 C CA  . TYR A 239 ? 0.49100 0.56230 0.46200 -0.01980 -0.01140 -0.00990 239 TYR A CA  
1850 C C   . TYR A 239 ? 0.49110 0.56960 0.46630 -0.01790 -0.01120 -0.00260 239 TYR A C   
1851 O O   . TYR A 239 ? 0.47690 0.56710 0.45580 -0.01960 -0.01430 -0.00270 239 TYR A O   
1852 C CB  . TYR A 239 ? 0.43410 0.51160 0.39680 -0.01740 -0.01200 -0.01040 239 TYR A CB  
1853 C CG  . TYR A 239 ? 0.45820 0.52680 0.41570 -0.01670 -0.01000 -0.01450 239 TYR A CG  
1854 C CD1 . TYR A 239 ? 0.47190 0.53370 0.43210 -0.02010 -0.01040 -0.02260 239 TYR A CD1 
1855 C CD2 . TYR A 239 ? 0.44670 0.51280 0.39850 -0.01260 -0.00740 -0.00970 239 TYR A CD2 
1856 C CE1 . TYR A 239 ? 0.49490 0.54850 0.45180 -0.01920 -0.00840 -0.02620 239 TYR A CE1 
1857 C CE2 . TYR A 239 ? 0.47630 0.53530 0.42410 -0.01200 -0.00550 -0.01330 239 TYR A CE2 
1858 C CZ  . TYR A 239 ? 0.48830 0.54130 0.43850 -0.01520 -0.00600 -0.02150 239 TYR A CZ  
1859 O OH  . TYR A 239 ? 0.52050 0.56640 0.46820 -0.01430 -0.00390 -0.02470 239 TYR A OH  
1860 N N   . GLU A 240 ? 0.43320 0.50530 0.40810 -0.01420 -0.00750 0.00300  240 GLU A N   
1861 C CA  . GLU A 240 ? 0.49640 0.57510 0.47600 -0.01160 -0.00660 0.00950  240 GLU A CA  
1862 C C   . GLU A 240 ? 0.49210 0.58300 0.47050 -0.00930 -0.00890 0.01310  240 GLU A C   
1863 O O   . GLU A 240 ? 0.46050 0.55190 0.43260 -0.00770 -0.00920 0.01310  240 GLU A O   
1864 C CB  . GLU A 240 ? 0.52800 0.59810 0.50720 -0.00750 -0.00210 0.01350  240 GLU A CB  
1865 C CG  . GLU A 240 ? 0.57370 0.63450 0.55390 -0.00910 0.00040  0.01200  240 GLU A CG  
1866 C CD  . GLU A 240 ? 0.73530 0.80160 0.72290 -0.00970 0.00170  0.01490  240 GLU A CD  
1867 O OE1 . GLU A 240 ? 0.80270 0.87270 0.79310 -0.00600 0.00390  0.01880  240 GLU A OE1 
1868 O OE2 . GLU A 240 ? 0.81840 0.88580 0.81030 -0.01400 0.00060  0.01340  240 GLU A OE2 
1869 N N   . PRO A 241 ? 0.48140 0.58310 0.46650 -0.00880 -0.01030 0.01720  241 PRO A N   
1870 C CA  . PRO A 241 ? 0.41770 0.53190 0.40290 -0.00600 -0.01250 0.02280  241 PRO A CA  
1871 C C   . PRO A 241 ? 0.40680 0.51550 0.39100 -0.00050 -0.00900 0.02880  241 PRO A C   
1872 O O   . PRO A 241 ? 0.43750 0.53500 0.42370 0.00160  -0.00490 0.02920  241 PRO A O   
1873 C CB  . PRO A 241 ? 0.48910 0.61370 0.48440 -0.00620 -0.01390 0.02660  241 PRO A CB  
1874 C CG  . PRO A 241 ? 0.46690 0.58760 0.46530 -0.01100 -0.01410 0.02090  241 PRO A CG  
1875 C CD  . PRO A 241 ? 0.46410 0.56860 0.45760 -0.01110 -0.01030 0.01750  241 PRO A CD  
1876 N N   . LEU A 242 ? 0.44450 0.56100 0.42510 0.00130  -0.01080 0.03260  242 LEU A N   
1877 C CA  . LEU A 242 ? 0.42430 0.53700 0.40580 0.00620  -0.00800 0.03930  242 LEU A CA  
1878 C C   . LEU A 242 ? 0.35920 0.48190 0.35070 0.00990  -0.00840 0.04830  242 LEU A C   
1879 O O   . LEU A 242 ? 0.37220 0.51030 0.36500 0.00910  -0.01250 0.05180  242 LEU A O   
1880 C CB  . LEU A 242 ? 0.40900 0.52560 0.38180 0.00620  -0.00920 0.03990  242 LEU A CB  
1881 C CG  . LEU A 242 ? 0.42080 0.53020 0.39520 0.01050  -0.00570 0.04600  242 LEU A CG  
1882 C CD1 . LEU A 242 ? 0.44620 0.53760 0.41840 0.01010  -0.00190 0.03980  242 LEU A CD1 
1883 C CD2 . LEU A 242 ? 0.46170 0.58010 0.42940 0.01080  -0.00700 0.04930  242 LEU A CD2 
1884 N N   . THR A 243 ? 0.38900 0.50380 0.38810 0.01390  -0.00450 0.05180  243 THR A N   
1885 C CA  . THR A 243 ? 0.42110 0.54410 0.43240 0.01810  -0.00430 0.06020  243 THR A CA  
1886 C C   . THR A 243 ? 0.43330 0.55590 0.44890 0.02270  -0.00290 0.06870  243 THR A C   
1887 O O   . THR A 243 ? 0.43060 0.54490 0.44050 0.02290  -0.00130 0.06760  243 THR A O   
1888 C CB  . THR A 243 ? 0.45500 0.57130 0.47500 0.01980  -0.00040 0.05830  243 THR A CB  
1889 O OG1 . THR A 243 ? 0.41680 0.51870 0.43740 0.02250  0.00430  0.05610  243 THR A OG1 
1890 C CG2 . THR A 243 ? 0.45710 0.57320 0.47370 0.01510  -0.00110 0.05100  243 THR A CG2 
1891 N N   . GLN A 244 ? 0.42230 0.55450 0.44990 0.02640  -0.00360 0.07790  244 GLN A N   
1892 C CA  . GLN A 244 ? 0.46860 0.59980 0.50420 0.03120  -0.00190 0.08730  244 GLN A CA  
1893 C C   . GLN A 244 ? 0.46740 0.58060 0.50810 0.03380  0.00360  0.08360  244 GLN A C   
1894 O O   . GLN A 244 ? 0.43650 0.54380 0.47870 0.03580  0.00520  0.08740  244 GLN A O   
1895 C CB  . GLN A 244 ? 0.39710 0.54130 0.44740 0.03500  -0.00350 0.09810  244 GLN A CB  
1896 C CG  . GLN A 244 ? 0.40940 0.55540 0.46990 0.03970  -0.00260 0.11020  244 GLN A CG  
1897 C CD  . GLN A 244 ? 0.50740 0.66040 0.55610 0.03770  -0.00530 0.11450  244 GLN A CD  
1898 O OE1 . GLN A 244 ? 0.44790 0.61530 0.48570 0.03420  -0.01000 0.11420  244 GLN A OE1 
1899 N NE2 . GLN A 244 ? 0.45080 0.59460 0.50220 0.03990  -0.00220 0.11840  244 GLN A NE2 
1900 N N   . ASP A 245 ? 0.39760 0.50260 0.44000 0.03350  0.00640  0.07570  245 ASP A N   
1901 C CA  . ASP A 245 ? 0.44760 0.53700 0.49280 0.03530  0.01120  0.07020  245 ASP A CA  
1902 C C   . ASP A 245 ? 0.47160 0.55160 0.50400 0.03240  0.01120  0.06540  245 ASP A C   
1903 O O   . ASP A 245 ? 0.45450 0.52490 0.49040 0.03440  0.01370  0.06570  245 ASP A O   
1904 C CB  . ASP A 245 ? 0.47450 0.55940 0.52130 0.03490  0.01410  0.06230  245 ASP A CB  
1905 C CG  . ASP A 245 ? 0.45120 0.54050 0.51500 0.03970  0.01650  0.06600  245 ASP A CG  
1906 O OD1 . ASP A 245 ? 0.42630 0.52560 0.49960 0.04220  0.01440  0.07550  245 ASP A OD1 
1907 O OD2 . ASP A 245 ? 0.49640 0.58080 0.56430 0.04090  0.02050  0.05980  245 ASP A OD2 
1908 N N   . HIS A 246 ? 0.45390 0.53630 0.47300 0.02760  0.00860  0.06040  246 HIS A N   
1909 C CA  . HIS A 246 ? 0.44480 0.52000 0.45240 0.02490  0.00840  0.05620  246 HIS A CA  
1910 C C   . HIS A 246 ? 0.47090 0.55080 0.47850 0.02640  0.00740  0.06390  246 HIS A C   
1911 O O   . HIS A 246 ? 0.43990 0.51100 0.44590 0.02690  0.00930  0.06330  246 HIS A O   
1912 C CB  . HIS A 246 ? 0.41990 0.49830 0.41610 0.01980  0.00560  0.04970  246 HIS A CB  
1913 C CG  . HIS A 246 ? 0.47360 0.54790 0.46950 0.01770  0.00660  0.04320  246 HIS A CG  
1914 N ND1 . HIS A 246 ? 0.46060 0.54290 0.45440 0.01420  0.00370  0.04080  246 HIS A ND1 
1915 C CD2 . HIS A 246 ? 0.46250 0.52670 0.45990 0.01820  0.01000  0.03860  246 HIS A CD2 
1916 C CE1 . HIS A 246 ? 0.42480 0.50200 0.41950 0.01270  0.00560  0.03620  246 HIS A CE1 
1917 N NE2 . HIS A 246 ? 0.45490 0.52160 0.45070 0.01510  0.00940  0.03480  246 HIS A NE2 
1918 N N   . VAL A 247 ? 0.44950 0.54440 0.45860 0.02690  0.00420  0.07150  247 VAL A N   
1919 C CA  . VAL A 247 ? 0.44400 0.54560 0.45330 0.02850  0.00350  0.08050  247 VAL A CA  
1920 C C   . VAL A 247 ? 0.49470 0.58730 0.51730 0.03290  0.00710  0.08660  247 VAL A C   
1921 O O   . VAL A 247 ? 0.45090 0.53820 0.47200 0.03310  0.00870  0.08860  247 VAL A O   
1922 C CB  . VAL A 247 ? 0.45260 0.57380 0.46340 0.02880  -0.00060 0.08900  247 VAL A CB  
1923 C CG1 . VAL A 247 ? 0.43710 0.56780 0.45010 0.03100  -0.00120 0.10090  247 VAL A CG1 
1924 C CG2 . VAL A 247 ? 0.42660 0.55670 0.42470 0.02390  -0.00450 0.08150  247 VAL A CG2 
1925 N N   . ASP A 248 ? 0.43880 0.52810 0.47520 0.03620  0.00890  0.08810  248 ASP A N   
1926 C CA  . ASP A 248 ? 0.49270 0.57320 0.54460 0.04050  0.01240  0.09280  248 ASP A CA  
1927 C C   . ASP A 248 ? 0.50130 0.56520 0.55020 0.03950  0.01550  0.08400  248 ASP A C   
1928 O O   . ASP A 248 ? 0.51420 0.57210 0.56960 0.04100  0.01720  0.08810  248 ASP A O   
1929 C CB  . ASP A 248 ? 0.46010 0.54070 0.52820 0.04430  0.01400  0.09430  248 ASP A CB  
1930 C CG  . ASP A 248 ? 0.48540 0.58230 0.56130 0.04640  0.01100  0.10560  248 ASP A CG  
1931 O OD1 . ASP A 248 ? 0.52180 0.63010 0.59360 0.04580  0.00800  0.11460  248 ASP A OD1 
1932 O OD2 . ASP A 248 ? 0.58990 0.68930 0.67710 0.04890  0.01180  0.10580  248 ASP A OD2 
1933 N N   . ILE A 249 ? 0.46900 0.52630 0.50790 0.03660  0.01590  0.07250  249 ILE A N   
1934 C CA  . ILE A 249 ? 0.50130 0.54410 0.53780 0.03570  0.01850  0.06480  249 ILE A CA  
1935 C C   . ILE A 249 ? 0.46580 0.50720 0.49280 0.03330  0.01760  0.06570  249 ILE A C   
1936 O O   . ILE A 249 ? 0.48400 0.51480 0.51280 0.03330  0.01950  0.06270  249 ILE A O   
1937 C CB  . ILE A 249 ? 0.51470 0.55030 0.54380 0.03350  0.01960  0.05320  249 ILE A CB  
1938 C CG1 . ILE A 249 ? 0.56660 0.60490 0.58000 0.02890  0.01710  0.04870  249 ILE A CG1 
1939 C CG2 . ILE A 249 ? 0.52280 0.56150 0.55890 0.03530  0.02090  0.05100  249 ILE A CG2 
1940 C CD1 . ILE A 249 ? 0.78120 0.81500 0.78960 0.02690  0.01800  0.03980  249 ILE A CD1 
1941 N N   . LEU A 250 ? 0.42590 0.47800 0.44300 0.03110  0.01480  0.06890  250 LEU A N   
1942 C CA  . LEU A 250 ? 0.43290 0.48630 0.44210 0.02940  0.01440  0.07070  250 LEU A CA  
1943 C C   . LEU A 250 ? 0.48810 0.54570 0.50740 0.03230  0.01530  0.08260  250 LEU A C   
1944 O O   . LEU A 250 ? 0.48320 0.54240 0.49770 0.03130  0.01580  0.08540  250 LEU A O   
1945 C CB  . LEU A 250 ? 0.42100 0.48580 0.41670 0.02610  0.01130  0.06880  250 LEU A CB  
1946 C CG  . LEU A 250 ? 0.44930 0.50800 0.43570 0.02260  0.01060  0.05710  250 LEU A CG  
1947 C CD1 . LEU A 250 ? 0.43480 0.50540 0.41170 0.01950  0.00720  0.05460  250 LEU A CD1 
1948 C CD2 . LEU A 250 ? 0.46330 0.50960 0.44510 0.02110  0.01230  0.05030  250 LEU A CD2 
1949 N N   . GLY A 251 ? 0.45010 0.50870 0.48480 0.03600  0.01620  0.08970  251 GLY A N   
1950 C CA  . GLY A 251 ? 0.47950 0.54310 0.52670 0.03900  0.01690  0.10290  251 GLY A CA  
1951 C C   . GLY A 251 ? 0.47230 0.52710 0.52230 0.03870  0.01930  0.10400  251 GLY A C   
1952 O O   . GLY A 251 ? 0.46910 0.53180 0.51800 0.03860  0.01930  0.11310  251 GLY A O   
1953 N N   . PRO A 252 ? 0.48970 0.52890 0.54470 0.03870  0.02160  0.09550  252 PRO A N   
1954 C CA  . PRO A 252 ? 0.48740 0.51830 0.54790 0.03830  0.02370  0.09680  252 PRO A CA  
1955 C C   . PRO A 252 ? 0.48720 0.52160 0.53210 0.03500  0.02310  0.09500  252 PRO A C   
1956 O O   . PRO A 252 ? 0.49340 0.53000 0.54230 0.03510  0.02440  0.10270  252 PRO A O   
1957 C CB  . PRO A 252 ? 0.51740 0.53260 0.58410 0.03850  0.02530  0.08540  252 PRO A CB  
1958 C CG  . PRO A 252 ? 0.55700 0.57390 0.63190 0.04120  0.02530  0.08450  252 PRO A CG  
1959 C CD  . PRO A 252 ? 0.52210 0.55300 0.58500 0.04030  0.02260  0.08800  252 PRO A CD  
1960 N N   . LEU A 253 ? 0.43930 0.47520 0.46760 0.03210  0.02140  0.08550  253 LEU A N   
1961 C CA  . LEU A 253 ? 0.50560 0.54480 0.52000 0.02920  0.02110  0.08260  253 LEU A CA  
1962 C C   . LEU A 253 ? 0.52220 0.57840 0.53150 0.02940  0.02020  0.09220  253 LEU A C   
1963 O O   . LEU A 253 ? 0.48400 0.54430 0.48950 0.02850  0.02160  0.09550  253 LEU A O   
1964 C CB  . LEU A 253 ? 0.45740 0.49310 0.45830 0.02620  0.01960  0.07010  253 LEU A CB  
1965 C CG  . LEU A 253 ? 0.47120 0.49140 0.47400 0.02540  0.02060  0.06050  253 LEU A CG  
1966 C CD1 . LEU A 253 ? 0.46410 0.48340 0.45520 0.02270  0.01890  0.05110  253 LEU A CD1 
1967 C CD2 . LEU A 253 ? 0.50510 0.51870 0.50860 0.02450  0.02220  0.05970  253 LEU A CD2 
1968 N N   . SER A 254 ? 0.44200 0.50930 0.45150 0.03050  0.01810  0.09710  254 SER A N   
1969 C CA  . SER A 254 ? 0.45310 0.53910 0.45910 0.03090  0.01670  0.10770  254 SER A CA  
1970 C C   . SER A 254 ? 0.49670 0.58610 0.51540 0.03350  0.01900  0.12210  254 SER A C   
1971 O O   . SER A 254 ? 0.50220 0.60370 0.51500 0.03290  0.01950  0.12890  254 SER A O   
1972 C CB  . SER A 254 ? 0.49240 0.58850 0.50010 0.03200  0.01360  0.11090  254 SER A CB  
1973 O OG  . SER A 254 ? 0.51130 0.62700 0.51490 0.03230  0.01190  0.12140  254 SER A OG  
1974 N N   . ALA A 255 ? 0.48270 0.56200 0.51980 0.03630  0.02050  0.12690  255 ALA A N   
1975 C CA  . ALA A 255 ? 0.53940 0.62060 0.59200 0.03860  0.02280  0.14120  255 ALA A CA  
1976 C C   . ALA A 255 ? 0.52320 0.59800 0.57420 0.03680  0.02550  0.13950  255 ALA A C   
1977 O O   . ALA A 255 ? 0.54420 0.62820 0.59840 0.03720  0.02710  0.15140  255 ALA A O   
1978 C CB  . ALA A 255 ? 0.53700 0.60690 0.61150 0.04190  0.02390  0.14420  255 ALA A CB  
1979 N N   . GLN A 256 ? 0.55080 0.61040 0.59750 0.03490  0.02620  0.12560  256 GLN A N   
1980 C CA  . GLN A 256 ? 0.56010 0.61300 0.60680 0.03330  0.02860  0.12350  256 GLN A CA  
1981 C C   . GLN A 256 ? 0.57720 0.64320 0.60750 0.03120  0.02890  0.12420  256 GLN A C   
1982 O O   . GLN A 256 ? 0.54200 0.61150 0.57530 0.03090  0.03140  0.13080  256 GLN A O   
1983 C CB  . GLN A 256 ? 0.56670 0.60230 0.61190 0.03170  0.02860  0.10840  256 GLN A CB  
1984 C CG  . GLN A 256 ? 0.58890 0.61800 0.63390 0.02980  0.03050  0.10540  256 GLN A CG  
1985 C CD  . GLN A 256 ? 0.68520 0.70030 0.72610 0.02800  0.02970  0.09100  256 GLN A CD  
1986 O OE1 . GLN A 256 ? 0.73220 0.74230 0.77110 0.02830  0.02810  0.08360  256 GLN A OE1 
1987 N NE2 . GLN A 256 ? 0.71420 0.72430 0.75320 0.02610  0.03070  0.08700  256 GLN A NE2 
1988 N N   . THR A 257 ? 0.51590 0.59010 0.53000 0.02980  0.02650  0.11740  257 THR A N   
1989 C CA  . THR A 257 ? 0.52320 0.60990 0.52170 0.02780  0.02690  0.11540  257 THR A CA  
1990 C C   . THR A 257 ? 0.54610 0.65420 0.54100 0.02880  0.02620  0.12760  257 THR A C   
1991 O O   . THR A 257 ? 0.53660 0.65760 0.51990 0.02750  0.02710  0.12760  257 THR A O   
1992 C CB  . THR A 257 ? 0.51640 0.60060 0.49960 0.02520  0.02460  0.09990  257 THR A CB  
1993 O OG1 . THR A 257 ? 0.48670 0.57600 0.46780 0.02560  0.02130  0.09910  257 THR A OG1 
1994 C CG2 . THR A 257 ? 0.51070 0.57550 0.49620 0.02400  0.02530  0.08870  257 THR A CG2 
1995 N N   . GLY A 258 ? 0.51240 0.62550 0.51680 0.03120  0.02440  0.13740  258 GLY A N   
1996 C CA  . GLY A 258 ? 0.50810 0.64350 0.50880 0.03210  0.02290  0.14950  258 GLY A CA  
1997 C C   . GLY A 258 ? 0.55660 0.70540 0.53900 0.03000  0.01950  0.14120  258 GLY A C   
1998 O O   . GLY A 258 ? 0.56650 0.73640 0.54190 0.03010  0.01810  0.14920  258 GLY A O   
1999 N N   . ILE A 259 ? 0.54060 0.67850 0.51570 0.02790  0.01780  0.12540  259 ILE A N   
2000 C CA  . ILE A 259 ? 0.48370 0.63240 0.44380 0.02550  0.01440  0.11600  259 ILE A CA  
2001 C C   . ILE A 259 ? 0.48930 0.63480 0.45570 0.02630  0.01110  0.11520  259 ILE A C   
2002 O O   . ILE A 259 ? 0.45310 0.58080 0.42750 0.02680  0.01180  0.10980  259 ILE A O   
2003 C CB  . ILE A 259 ? 0.50670 0.64580 0.45590 0.02240  0.01530  0.09940  259 ILE A CB  
2004 C CG1 . ILE A 259 ? 0.53870 0.68010 0.48360 0.02200  0.01920  0.10010  259 ILE A CG1 
2005 C CG2 . ILE A 259 ? 0.49920 0.64690 0.43550 0.01950  0.01160  0.08790  259 ILE A CG2 
2006 C CD1 . ILE A 259 ? 0.49560 0.62260 0.43540 0.01980  0.02020  0.08490  259 ILE A CD1 
2007 N N   . ALA A 260 ? 0.49940 0.66320 0.46400 0.02680  0.00770  0.12250  260 ALA A N   
2008 C CA  . ALA A 260 ? 0.42880 0.59220 0.40000 0.02760  0.00450  0.12260  260 ALA A CA  
2009 C C   . ALA A 260 ? 0.45310 0.60690 0.41670 0.02450  0.00290  0.10590  260 ALA A C   
2010 O O   . ALA A 260 ? 0.45790 0.61360 0.40850 0.02130  0.00250  0.09520  260 ALA A O   
2011 C CB  . ALA A 260 ? 0.47130 0.65960 0.43970 0.02820  0.00060  0.13310  260 ALA A CB  
2012 N N   . VAL A 261 ? 0.48130 0.62500 0.45410 0.02550  0.00220  0.10360  261 VAL A N   
2013 C CA  . VAL A 261 ? 0.44920 0.58340 0.41670 0.02250  0.00110  0.08930  261 VAL A CA  
2014 C C   . VAL A 261 ? 0.42680 0.57610 0.38200 0.01900  -0.00290 0.08290  261 VAL A C   
2015 O O   . VAL A 261 ? 0.41560 0.56040 0.36140 0.01570  -0.00300 0.07070  261 VAL A O   
2016 C CB  . VAL A 261 ? 0.49710 0.62260 0.47670 0.02440  0.00120  0.08970  261 VAL A CB  
2017 C CG1 . VAL A 261 ? 0.44990 0.56960 0.42410 0.02120  -0.00030 0.07700  261 VAL A CG1 
2018 C CG2 . VAL A 261 ? 0.49880 0.60670 0.48980 0.02730  0.00550  0.09170  261 VAL A CG2 
2019 N N   . LEU A 262 ? 0.40420 0.57270 0.35980 0.01970  -0.00640 0.09130  262 LEU A N   
2020 C CA  . LEU A 262 ? 0.48290 0.66690 0.42710 0.01600  -0.01070 0.08400  262 LEU A CA  
2021 C C   . LEU A 262 ? 0.50350 0.69630 0.43420 0.01400  -0.01000 0.07950  262 LEU A C   
2022 O O   . LEU A 262 ? 0.49520 0.69540 0.41600 0.01030  -0.01260 0.06820  262 LEU A O   
2023 C CB  . LEU A 262 ? 0.44230 0.64630 0.39050 0.01710  -0.01530 0.09390  262 LEU A CB  
2024 C CG  . LEU A 262 ? 0.47530 0.67100 0.43690 0.01850  -0.01600 0.09510  262 LEU A CG  
2025 C CD1 . LEU A 262 ? 0.52330 0.73820 0.49110 0.02020  -0.02010 0.10640  262 LEU A CD1 
2026 C CD2 . LEU A 262 ? 0.50970 0.69720 0.46770 0.01450  -0.01720 0.08040  262 LEU A CD2 
2027 N N   . ASP A 263 ? 0.46270 0.65490 0.39370 0.01630  -0.00640 0.08740  263 ASP A N   
2028 C CA  . ASP A 263 ? 0.49330 0.69130 0.41200 0.01440  -0.00460 0.08120  263 ASP A CA  
2029 C C   . ASP A 263 ? 0.48530 0.66420 0.40130 0.01210  -0.00240 0.06610  263 ASP A C   
2030 O O   . ASP A 263 ? 0.46140 0.64460 0.36730 0.00910  -0.00300 0.05410  263 ASP A O   
2031 C CB  . ASP A 263 ? 0.48230 0.68530 0.40430 0.01760  -0.00110 0.09540  263 ASP A CB  
2032 C CG  . ASP A 263 ? 0.67980 0.89090 0.59010 0.01630  0.00170  0.09140  263 ASP A CG  
2033 O OD1 . ASP A 263 ? 0.61810 0.83160 0.51720 0.01320  0.00110  0.07660  263 ASP A OD1 
2034 O OD2 . ASP A 263 ? 0.66440 0.88080 0.57830 0.01880  0.00460  0.10450  263 ASP A OD2 
2035 N N   . MET A 264 ? 0.42360 0.58170 0.34910 0.01350  0.00010  0.06610  264 MET A N   
2036 C CA  . MET A 264 ? 0.46370 0.60450 0.38750 0.01140  0.00180  0.05330  264 MET A CA  
2037 C C   . MET A 264 ? 0.47320 0.61350 0.39410 0.00800  -0.00170 0.04190  264 MET A C   
2038 O O   . MET A 264 ? 0.44970 0.58320 0.36620 0.00520  -0.00140 0.02980  264 MET A O   
2039 C CB  . MET A 264 ? 0.41490 0.53580 0.34920 0.01350  0.00460  0.05620  264 MET A CB  
2040 C CG  . MET A 264 ? 0.39940 0.50310 0.33190 0.01160  0.00660  0.04450  264 MET A CG  
2041 S SD  . MET A 264 ? 0.45170 0.55800 0.37710 0.01130  0.00990  0.04210  264 MET A SD  
2042 C CE  . MET A 264 ? 0.51450 0.61050 0.45060 0.01470  0.01360  0.05330  264 MET A CE  
2043 N N   . CYS A 265 ? 0.44980 0.59710 0.37510 0.00810  -0.00510 0.04580  265 CYS A N   
2044 C CA  . CYS A 265 ? 0.50130 0.65060 0.42490 0.00440  -0.00870 0.03570  265 CYS A CA  
2045 C C   . CYS A 265 ? 0.49570 0.65960 0.40880 0.00110  -0.01110 0.02690  265 CYS A C   
2046 O O   . CYS A 265 ? 0.48220 0.64180 0.39370 -0.00250 -0.01260 0.01440  265 CYS A O   
2047 C CB  . CYS A 265 ? 0.48320 0.63990 0.41410 0.00520  -0.01190 0.04230  265 CYS A CB  
2048 S SG  . CYS A 265 ? 0.48670 0.62520 0.43070 0.00820  -0.00900 0.04750  265 CYS A SG  
2049 N N   . ALA A 266 ? 0.45900 0.64090 0.36540 0.00220  -0.01160 0.03280  266 ALA A N   
2050 C CA  . ALA A 266 ? 0.51810 0.71490 0.41340 -0.00080 -0.01330 0.02280  266 ALA A CA  
2051 C C   . ALA A 266 ? 0.51220 0.69670 0.40380 -0.00200 -0.00950 0.01140  266 ALA A C   
2052 O O   . ALA A 266 ? 0.52880 0.71570 0.41610 -0.00540 -0.01100 -0.00250 266 ALA A O   
2053 C CB  . ALA A 266 ? 0.55990 0.78060 0.44770 0.00080  -0.01420 0.03250  266 ALA A CB  
2054 N N   . SER A 267 ? 0.51110 0.68160 0.40610 0.00070  -0.00480 0.01660  267 SER A N   
2055 C CA  . SER A 267 ? 0.49450 0.65170 0.38840 -0.00010 -0.00130 0.00680  267 SER A CA  
2056 C C   . SER A 267 ? 0.52240 0.66410 0.42160 -0.00290 -0.00260 -0.00410 267 SER A C   
2057 O O   . SER A 267 ? 0.50100 0.64020 0.39820 -0.00540 -0.00240 -0.01680 267 SER A O   
2058 C CB  . SER A 267 ? 0.52100 0.66570 0.41960 0.00320  0.00330  0.01560  267 SER A CB  
2059 O OG  . SER A 267 ? 0.55720 0.71580 0.45110 0.00520  0.00540  0.02360  267 SER A OG  
2060 N N   . LEU A 268 ? 0.49450 0.62590 0.40170 -0.00230 -0.00370 0.00110  268 LEU A N   
2061 C CA  . LEU A 268 ? 0.49400 0.61160 0.40690 -0.00490 -0.00480 -0.00700 268 LEU A CA  
2062 C C   . LEU A 268 ? 0.51950 0.64680 0.43080 -0.00900 -0.00880 -0.01740 268 LEU A C   
2063 O O   . LEU A 268 ? 0.53070 0.65000 0.44430 -0.01180 -0.00890 -0.02850 268 LEU A O   
2064 C CB  . LEU A 268 ? 0.46640 0.57540 0.38730 -0.00340 -0.00510 0.00100  268 LEU A CB  
2065 C CG  . LEU A 268 ? 0.49940 0.59570 0.42660 -0.00600 -0.00590 -0.00500 268 LEU A CG  
2066 C CD1 . LEU A 268 ? 0.48930 0.57160 0.41690 -0.00720 -0.00350 -0.01310 268 LEU A CD1 
2067 C CD2 . LEU A 268 ? 0.45160 0.53980 0.38540 -0.00350 -0.00460 0.00350  268 LEU A CD2 
2068 N N   . LYS A 269 ? 0.49420 0.63920 0.40250 -0.00940 -0.01230 -0.01410 269 LYS A N   
2069 C CA  . LYS A 269 ? 0.53080 0.68720 0.43770 -0.01360 -0.01670 -0.02480 269 LYS A CA  
2070 C C   . LYS A 269 ? 0.58400 0.74310 0.48510 -0.01560 -0.01560 -0.03810 269 LYS A C   
2071 O O   . LYS A 269 ? 0.57080 0.72590 0.47580 -0.01930 -0.01730 -0.05070 269 LYS A O   
2072 C CB  . LYS A 269 ? 0.56740 0.74540 0.47040 -0.01330 -0.02070 -0.01800 269 LYS A CB  
2073 C CG  . LYS A 269 ? 0.62650 0.82050 0.52610 -0.01770 -0.02560 -0.02920 269 LYS A CG  
2074 C CD  . LYS A 269 ? 0.68220 0.89990 0.57810 -0.01730 -0.03040 -0.02100 269 LYS A CD  
2075 C CE  . LYS A 269 ? 0.60590 0.82170 0.51030 -0.01440 -0.03110 -0.00590 269 LYS A CE  
2076 N NZ  . LYS A 269 ? 0.64620 0.88750 0.54660 -0.01420 -0.03600 0.00130  269 LYS A NZ  
2077 N N   . GLU A 270 ? 0.52470 0.69120 0.41760 -0.01310 -0.01260 -0.03540 270 GLU A N   
2078 C CA  . GLU A 270 ? 0.59750 0.76790 0.48500 -0.01450 -0.01090 -0.04830 270 GLU A CA  
2079 C C   . GLU A 270 ? 0.59720 0.74570 0.49290 -0.01530 -0.00800 -0.05620 270 GLU A C   
2080 O O   . GLU A 270 ? 0.63050 0.77690 0.52900 -0.01830 -0.00880 -0.07040 270 GLU A O   
2081 C CB  . GLU A 270 ? 0.58160 0.76470 0.45950 -0.01130 -0.00740 -0.04170 270 GLU A CB  
2082 C CG  . GLU A 270 ? 0.75990 0.95150 0.63080 -0.01240 -0.00510 -0.05520 270 GLU A CG  
2083 C CD  . GLU A 270 ? 1.03130 1.23800 0.89210 -0.00930 -0.00110 -0.04790 270 GLU A CD  
2084 O OE1 . GLU A 270 ? 0.89860 1.10000 0.76110 -0.00590 0.00200  -0.03350 270 GLU A OE1 
2085 O OE2 . GLU A 270 ? 1.25240 1.47780 1.10400 -0.01050 -0.00110 -0.05690 270 GLU A OE2 
2086 N N   . LEU A 271 ? 0.55650 0.68830 0.45740 -0.01270 -0.00510 -0.04720 271 LEU A N   
2087 C CA  . LEU A 271 ? 0.56810 0.67990 0.47680 -0.01320 -0.00280 -0.05260 271 LEU A CA  
2088 C C   . LEU A 271 ? 0.61090 0.71500 0.52850 -0.01700 -0.00590 -0.06010 271 LEU A C   
2089 O O   . LEU A 271 ? 0.59310 0.68740 0.51680 -0.01880 -0.00510 -0.06980 271 LEU A O   
2090 C CB  . LEU A 271 ? 0.55440 0.65240 0.46640 -0.01000 0.00010  -0.04090 271 LEU A CB  
2091 C CG  . LEU A 271 ? 0.56590 0.66740 0.47260 -0.00650 0.00410  -0.03460 271 LEU A CG  
2092 C CD1 . LEU A 271 ? 0.55220 0.64150 0.46340 -0.00370 0.00600  -0.02300 271 LEU A CD1 
2093 C CD2 . LEU A 271 ? 0.58660 0.68320 0.49370 -0.00680 0.00710  -0.04460 271 LEU A CD2 
2094 N N   . LEU A 272 ? 0.55460 0.66260 0.47440 -0.01810 -0.00940 -0.05490 272 LEU A N   
2095 C CA  . LEU A 272 ? 0.58770 0.69050 0.51680 -0.02210 -0.01250 -0.06130 272 LEU A CA  
2096 C C   . LEU A 272 ? 0.61460 0.72750 0.54380 -0.02590 -0.01520 -0.07600 272 LEU A C   
2097 O O   . LEU A 272 ? 0.62290 0.72680 0.56180 -0.02910 -0.01600 -0.08530 272 LEU A O   
2098 C CB  . LEU A 272 ? 0.55500 0.66250 0.48650 -0.02230 -0.01530 -0.05230 272 LEU A CB  
2099 C CG  . LEU A 272 ? 0.54830 0.64380 0.48230 -0.01900 -0.01260 -0.04020 272 LEU A CG  
2100 C CD1 . LEU A 272 ? 0.52590 0.62710 0.46320 -0.01870 -0.01490 -0.03190 272 LEU A CD1 
2101 C CD2 . LEU A 272 ? 0.53680 0.61440 0.47860 -0.02010 -0.01070 -0.04300 272 LEU A CD2 
2102 N N   . GLN A 273 ? 0.59340 0.72590 0.51280 -0.02580 -0.01680 -0.07830 273 GLN A N   
2103 C CA  . GLN A 273 ? 0.60560 0.74980 0.52510 -0.02990 -0.02010 -0.09330 273 GLN A CA  
2104 C C   . GLN A 273 ? 0.69280 0.83330 0.61210 -0.03010 -0.01690 -0.10640 273 GLN A C   
2105 O O   . GLN A 273 ? 0.69940 0.83990 0.62540 -0.03380 -0.01880 -0.12120 273 GLN A O   
2106 C CB  . GLN A 273 ? 0.59530 0.76400 0.50380 -0.03000 -0.02350 -0.09120 273 GLN A CB  
2107 C CG  . GLN A 273 ? 0.61310 0.78680 0.52540 -0.03090 -0.02790 -0.08160 273 GLN A CG  
2108 C CD  . GLN A 273 ? 0.67820 0.87590 0.58000 -0.02980 -0.03090 -0.07520 273 GLN A CD  
2109 O OE1 . GLN A 273 ? 0.72490 0.93450 0.61560 -0.02770 -0.02900 -0.07470 273 GLN A OE1 
2110 N NE2 . GLN A 273 ? 0.64990 0.85560 0.55560 -0.03100 -0.03540 -0.06880 273 GLN A NE2 
2111 N N   . ASN A 274 ? 0.66440 0.80150 0.57770 -0.02610 -0.01200 -0.10140 274 ASN A N   
2112 C CA  . ASN A 274 ? 0.68930 0.82580 0.60170 -0.02550 -0.00840 -0.11320 274 ASN A CA  
2113 C C   . ASN A 274 ? 0.71770 0.83310 0.63860 -0.02360 -0.00410 -0.11170 274 ASN A C   
2114 O O   . ASN A 274 ? 0.73380 0.84600 0.65830 -0.02360 -0.00140 -0.12310 274 ASN A O   
2115 C CB  . ASN A 274 ? 0.67800 0.83260 0.57570 -0.02270 -0.00590 -0.11030 274 ASN A CB  
2116 C CG  . ASN A 274 ? 0.73550 0.91380 0.62360 -0.02440 -0.01030 -0.11090 274 ASN A CG  
2117 O OD1 . ASN A 274 ? 0.83760 1.02950 0.71560 -0.02190 -0.01010 -0.09900 274 ASN A OD1 
2118 N ND2 . ASN A 274 ? 0.77080 0.95440 0.66320 -0.02870 -0.01470 -0.12380 274 ASN A ND2 
2119 N N   . GLY A 275 ? 0.72450 0.82650 0.64890 -0.02180 -0.00340 -0.09830 275 GLY A N   
2120 C CA  . GLY A 275 ? 0.66100 0.74500 0.59240 -0.01980 0.00030  -0.09560 275 GLY A CA  
2121 C C   . GLY A 275 ? 0.69130 0.77850 0.61480 -0.01580 0.00480  -0.09030 275 GLY A C   
2122 O O   . GLY A 275 ? 0.69690 0.79940 0.60960 -0.01420 0.00520  -0.08550 275 GLY A O   
2123 N N   . MET A 276 ? 0.70780 0.78130 0.63790 -0.01420 0.00810  -0.09070 276 MET A N   
2124 C CA  . MET A 276 ? 0.73770 0.81290 0.66240 -0.01050 0.01250  -0.08490 276 MET A CA  
2125 C C   . MET A 276 ? 0.81390 0.89650 0.73700 -0.00970 0.01610  -0.09630 276 MET A C   
2126 O O   . MET A 276 ? 0.75680 0.84440 0.67460 -0.00680 0.02000  -0.09150 276 MET A O   
2127 C CB  . MET A 276 ? 0.73420 0.79150 0.66610 -0.00880 0.01400  -0.07630 276 MET A CB  
2128 C CG  . MET A 276 ? 0.69470 0.74710 0.62600 -0.00850 0.01170  -0.06390 276 MET A CG  
2129 S SD  . MET A 276 ? 0.71930 0.75550 0.65580 -0.00600 0.01390  -0.05400 276 MET A SD  
2130 C CE  . MET A 276 ? 0.59910 0.63010 0.53730 -0.00720 0.01030  -0.04580 276 MET A CE  
2131 N N   . ASN A 277 ? 0.84140 0.92540 0.76980 -0.01220 0.01520  -0.11150 277 ASN A N   
2132 C CA  . ASN A 277 ? 0.96120 1.05280 0.88910 -0.01140 0.01900  -0.12440 277 ASN A CA  
2133 C C   . ASN A 277 ? 0.89990 0.98040 0.83380 -0.00810 0.02390  -0.12110 277 ASN A C   
2134 O O   . ASN A 277 ? 0.87720 0.96740 0.80490 -0.00560 0.02830  -0.12150 277 ASN A O   
2135 C CB  . ASN A 277 ? 0.98510 1.10070 0.89750 -0.01070 0.02010  -0.12600 277 ASN A CB  
2136 C CG  . ASN A 277 ? 1.09140 1.22070 0.99820 -0.01410 0.01500  -0.13180 277 ASN A CG  
2137 O OD1 . ASN A 277 ? 1.15470 1.28890 1.06490 -0.01670 0.01380  -0.14810 277 ASN A OD1 
2138 N ND2 . ASN A 277 ? 1.04060 1.17690 0.93970 -0.01410 0.01200  -0.11880 277 ASN A ND2 
2139 N N   . GLY A 278 ? 0.87810 0.93930 0.82410 -0.00820 0.02300  -0.11670 278 GLY A N   
2140 C CA  . GLY A 278 ? 0.81120 0.86170 0.76460 -0.00550 0.02680  -0.11370 278 GLY A CA  
2141 C C   . GLY A 278 ? 0.78870 0.83920 0.73570 -0.00270 0.02870  -0.09900 278 GLY A C   
2142 O O   . GLY A 278 ? 0.75600 0.79860 0.70910 -0.00050 0.03160  -0.09610 278 GLY A O   
2143 N N   . ARG A 279 ? 0.77510 0.83390 0.71140 -0.00270 0.02700  -0.08950 279 ARG A N   
2144 C CA  . ARG A 279 ? 0.70640 0.76350 0.63940 -0.00020 0.02870  -0.07560 279 ARG A CA  
2145 C C   . ARG A 279 ? 0.66780 0.70980 0.60620 -0.00070 0.02550  -0.06640 279 ARG A C   
2146 O O   . ARG A 279 ? 0.65770 0.69280 0.60080 -0.00300 0.02210  -0.06920 279 ARG A O   
2147 C CB  . ARG A 279 ? 0.65840 0.73330 0.57880 0.00060  0.02930  -0.06940 279 ARG A CB  
2148 C CG  . ARG A 279 ? 0.75580 0.84560 0.67070 0.00240  0.03430  -0.07410 279 ARG A CG  
2149 C CD  . ARG A 279 ? 0.72490 0.83580 0.62720 0.00220  0.03400  -0.07240 279 ARG A CD  
2150 N NE  . ARG A 279 ? 0.81010 0.92480 0.71010 -0.00080 0.02910  -0.07970 279 ARG A NE  
2151 C CZ  . ARG A 279 ? 0.79140 0.92470 0.68090 -0.00180 0.02710  -0.07970 279 ARG A CZ  
2152 N NH1 . ARG A 279 ? 0.78770 0.93870 0.66740 -0.00000 0.02970  -0.07220 279 ARG A NH1 
2153 N NH2 . ARG A 279 ? 0.79990 0.93520 0.68940 -0.00490 0.02230  -0.08690 279 ARG A NH2 
2154 N N   . THR A 280 ? 0.66480 0.70250 0.60320 0.00130  0.02680  -0.05550 280 THR A N   
2155 C CA  . THR A 280 ? 0.59270 0.61780 0.53510 0.00090  0.02410  -0.04760 280 THR A CA  
2156 C C   . THR A 280 ? 0.58510 0.61490 0.52180 0.00230  0.02410  -0.03620 280 THR A C   
2157 O O   . THR A 280 ? 0.53630 0.57700 0.46790 0.00390  0.02670  -0.03260 280 THR A O   
2158 C CB  . THR A 280 ? 0.61890 0.63050 0.57080 0.00170  0.02490  -0.04650 280 THR A CB  
2159 O OG1 . THR A 280 ? 0.59740 0.61200 0.54910 0.00410  0.02850  -0.04280 280 THR A OG1 
2160 C CG2 . THR A 280 ? 0.64590 0.65220 0.60630 0.00050  0.02490  -0.05720 280 THR A CG2 
2161 N N   . ILE A 281 ? 0.53670 0.55940 0.47480 0.00170  0.02130  -0.03070 281 ILE A N   
2162 C CA  . ILE A 281 ? 0.49710 0.52160 0.43290 0.00320  0.02120  -0.02030 281 ILE A CA  
2163 C C   . ILE A 281 ? 0.52730 0.53840 0.46910 0.00370  0.02070  -0.01590 281 ILE A C   
2164 O O   . ILE A 281 ? 0.52470 0.52750 0.46950 0.00230  0.01830  -0.01750 281 ILE A O   
2165 C CB  . ILE A 281 ? 0.55240 0.58380 0.48390 0.00230  0.01840  -0.01800 281 ILE A CB  
2166 C CG1 . ILE A 281 ? 0.56510 0.61200 0.49000 0.00160  0.01850  -0.02280 281 ILE A CG1 
2167 C CG2 . ILE A 281 ? 0.52630 0.55790 0.45830 0.00420  0.01840  -0.00740 281 ILE A CG2 
2168 C CD1 . ILE A 281 ? 0.57760 0.63320 0.49890 0.00050  0.01510  -0.02040 281 ILE A CD1 
2169 N N   . LEU A 282 ? 0.51830 0.52830 0.46220 0.00550  0.02280  -0.00980 282 LEU A N   
2170 C CA  . LEU A 282 ? 0.54650 0.54490 0.49620 0.00590  0.02200  -0.00630 282 LEU A CA  
2171 C C   . LEU A 282 ? 0.54710 0.53630 0.50110 0.00460  0.02070  -0.01170 282 LEU A C   
2172 O O   . LEU A 282 ? 0.56190 0.54330 0.51820 0.00380  0.01850  -0.01050 282 LEU A O   
2173 C CB  . LEU A 282 ? 0.53530 0.53100 0.48480 0.00600  0.02000  -0.00130 282 LEU A CB  
2174 C CG  . LEU A 282 ? 0.51600 0.51780 0.46550 0.00780  0.02130  0.00630  282 LEU A CG  
2175 C CD1 . LEU A 282 ? 0.47960 0.47890 0.43040 0.00820  0.01960  0.00990  282 LEU A CD1 
2176 C CD2 . LEU A 282 ? 0.48170 0.48020 0.43690 0.00900  0.02350  0.01000  282 LEU A CD2 
2177 N N   . GLY A 283 ? 0.53230 0.52330 0.48770 0.00440  0.02220  -0.01780 283 GLY A N   
2178 C CA  . GLY A 283 ? 0.57630 0.55910 0.53820 0.00350  0.02130  -0.02230 283 GLY A CA  
2179 C C   . GLY A 283 ? 0.63960 0.61960 0.60270 0.00130  0.01870  -0.02680 283 GLY A C   
2180 O O   . GLY A 283 ? 0.65850 0.63140 0.62870 0.00050  0.01770  -0.02920 283 GLY A O   
2181 N N   . SER A 284 ? 0.57780 0.56380 0.53540 0.00020  0.01760  -0.02770 284 SER A N   
2182 C CA  . SER A 284 ? 0.57140 0.55540 0.53110 -0.00220 0.01500  -0.03120 284 SER A CA  
2183 C C   . SER A 284 ? 0.58200 0.57440 0.53990 -0.00330 0.01540  -0.03930 284 SER A C   
2184 O O   . SER A 284 ? 0.56520 0.56800 0.51640 -0.00230 0.01680  -0.03990 284 SER A O   
2185 C CB  . SER A 284 ? 0.56030 0.54440 0.51640 -0.00270 0.01300  -0.02530 284 SER A CB  
2186 O OG  . SER A 284 ? 0.58470 0.56870 0.54310 -0.00530 0.01080  -0.02820 284 SER A OG  
2187 N N   . ALA A 285 ? 0.52380 0.51220 0.48860 -0.00550 0.01400  -0.04580 285 ALA A N   
2188 C CA  . ALA A 285 ? 0.55960 0.55560 0.52390 -0.00730 0.01350  -0.05490 285 ALA A CA  
2189 C C   . ALA A 285 ? 0.55000 0.54890 0.51270 -0.00970 0.01030  -0.05360 285 ALA A C   
2190 O O   . ALA A 285 ? 0.60830 0.61420 0.57090 -0.01180 0.00900  -0.06100 285 ALA A O   
2191 C CB  . ALA A 285 ? 0.57650 0.56670 0.55190 -0.00830 0.01400  -0.06380 285 ALA A CB  
2192 N N   . LEU A 286 ? 0.55060 0.54530 0.51240 -0.00960 0.00910  -0.04500 286 LEU A N   
2193 C CA  . LEU A 286 ? 0.56930 0.56730 0.53010 -0.01150 0.00650  -0.04260 286 LEU A CA  
2194 C C   . LEU A 286 ? 0.52860 0.53230 0.48110 -0.00940 0.00690  -0.03490 286 LEU A C   
2195 O O   . LEU A 286 ? 0.54440 0.54530 0.49450 -0.00680 0.00870  -0.02970 286 LEU A O   
2196 C CB  . LEU A 286 ? 0.58200 0.57060 0.55050 -0.01320 0.00510  -0.03900 286 LEU A CB  
2197 C CG  . LEU A 286 ? 0.64190 0.62360 0.62170 -0.01550 0.00440  -0.04470 286 LEU A CG  
2198 C CD1 . LEU A 286 ? 0.67590 0.65030 0.66250 -0.01700 0.00310  -0.03820 286 LEU A CD1 
2199 C CD2 . LEU A 286 ? 0.65040 0.63900 0.63260 -0.01820 0.00290  -0.05380 286 LEU A CD2 
2200 N N   . LEU A 287 ? 0.49830 0.50980 0.44840 -0.01050 0.00500  -0.03380 287 LEU A N   
2201 C CA  . LEU A 287 ? 0.50770 0.52420 0.45270 -0.00830 0.00510  -0.02590 287 LEU A CA  
2202 C C   . LEU A 287 ? 0.51200 0.51970 0.46010 -0.00780 0.00530  -0.01990 287 LEU A C   
2203 O O   . LEU A 287 ? 0.51150 0.51660 0.46390 -0.01000 0.00390  -0.02010 287 LEU A O   
2204 C CB  . LEU A 287 ? 0.50920 0.53780 0.45160 -0.00960 0.00280  -0.02660 287 LEU A CB  
2205 C CG  . LEU A 287 ? 0.50030 0.54030 0.43820 -0.01030 0.00240  -0.03320 287 LEU A CG  
2206 C CD1 . LEU A 287 ? 0.57770 0.63060 0.51410 -0.01250 -0.00100 -0.03550 287 LEU A CD1 
2207 C CD2 . LEU A 287 ? 0.56850 0.61410 0.50000 -0.00710 0.00510  -0.02950 287 LEU A CD2 
2208 N N   . GLU A 288 ? 0.47350 0.47810 0.41970 -0.00510 0.00700  -0.01440 288 GLU A N   
2209 C CA  . GLU A 288 ? 0.47420 0.47100 0.42270 -0.00450 0.00740  -0.01020 288 GLU A CA  
2210 C C   . GLU A 288 ? 0.47170 0.47270 0.41960 -0.00340 0.00720  -0.00550 288 GLU A C   
2211 O O   . GLU A 288 ? 0.48740 0.49400 0.43350 -0.00120 0.00780  -0.00210 288 GLU A O   
2212 C CB  . GLU A 288 ? 0.53100 0.52220 0.47910 -0.00220 0.00920  -0.00820 288 GLU A CB  
2213 C CG  . GLU A 288 ? 0.55520 0.54000 0.50460 -0.00130 0.00950  -0.00460 288 GLU A CG  
2214 C CD  . GLU A 288 ? 0.62530 0.60430 0.57760 -0.00350 0.00840  -0.00580 288 GLU A CD  
2215 O OE1 . GLU A 288 ? 0.62700 0.60220 0.58200 -0.00450 0.00800  -0.00860 288 GLU A OE1 
2216 O OE2 . GLU A 288 ? 0.54560 0.52490 0.49800 -0.00400 0.00800  -0.00350 288 GLU A OE2 
2217 N N   . ASP A 289 ? 0.46090 0.45990 0.41140 -0.00470 0.00650  -0.00460 289 ASP A N   
2218 C CA  . ASP A 289 ? 0.48050 0.48410 0.43140 -0.00330 0.00690  -0.00050 289 ASP A CA  
2219 C C   . ASP A 289 ? 0.45700 0.45530 0.40880 -0.00190 0.00840  0.00200  289 ASP A C   
2220 O O   . ASP A 289 ? 0.46370 0.46550 0.41710 -0.00130 0.00890  0.00410  289 ASP A O   
2221 C CB  . ASP A 289 ? 0.45940 0.46960 0.41270 -0.00580 0.00510  -0.00150 289 ASP A CB  
2222 C CG  . ASP A 289 ? 0.49680 0.50280 0.45370 -0.00840 0.00480  -0.00200 289 ASP A CG  
2223 O OD1 . ASP A 289 ? 0.46700 0.46530 0.42430 -0.00900 0.00530  -0.00260 289 ASP A OD1 
2224 O OD2 . ASP A 289 ? 0.47190 0.48320 0.43200 -0.01010 0.00400  -0.00130 289 ASP A OD2 
2225 N N   . GLU A 290 ? 0.42590 0.41680 0.37690 -0.00150 0.00910  0.00140  290 GLU A N   
2226 C CA  . GLU A 290 ? 0.47030 0.45790 0.42140 -0.00040 0.01020  0.00270  290 GLU A CA  
2227 C C   . GLU A 290 ? 0.54210 0.52720 0.49370 0.00260  0.01160  0.00340  290 GLU A C   
2228 O O   . GLU A 290 ? 0.52860 0.50970 0.48000 0.00320  0.01220  0.00270  290 GLU A O   
2229 C CB  . GLU A 290 ? 0.48730 0.47000 0.43810 -0.00260 0.00940  0.00190  290 GLU A CB  
2230 C CG  . GLU A 290 ? 0.51810 0.50400 0.47130 -0.00570 0.00840  0.00240  290 GLU A CG  
2231 C CD  . GLU A 290 ? 0.56700 0.55190 0.52070 -0.00730 0.00840  0.00470  290 GLU A CD  
2232 O OE1 . GLU A 290 ? 0.57590 0.55780 0.52720 -0.00630 0.00860  0.00510  290 GLU A OE1 
2233 O OE2 . GLU A 290 ? 0.53380 0.52180 0.49090 -0.00980 0.00790  0.00630  290 GLU A OE2 
2234 N N   . PHE A 291 ? 0.43250 0.42050 0.38520 0.00440  0.01210  0.00520  291 PHE A N   
2235 C CA  . PHE A 291 ? 0.44690 0.43330 0.40290 0.00720  0.01360  0.00710  291 PHE A CA  
2236 C C   . PHE A 291 ? 0.44070 0.43320 0.40030 0.00930  0.01430  0.01040  291 PHE A C   
2237 O O   . PHE A 291 ? 0.44590 0.44520 0.40490 0.00920  0.01350  0.01280  291 PHE A O   
2238 C CB  . PHE A 291 ? 0.46010 0.44530 0.41640 0.00780  0.01380  0.00840  291 PHE A CB  
2239 C CG  . PHE A 291 ? 0.51960 0.49900 0.47410 0.00620  0.01330  0.00550  291 PHE A CG  
2240 C CD1 . PHE A 291 ? 0.57560 0.54890 0.53240 0.00680  0.01360  0.00460  291 PHE A CD1 
2241 C CD2 . PHE A 291 ? 0.52330 0.50380 0.47520 0.00440  0.01240  0.00350  291 PHE A CD2 
2242 C CE1 . PHE A 291 ? 0.53250 0.50120 0.48870 0.00540  0.01270  0.00260  291 PHE A CE1 
2243 C CE2 . PHE A 291 ? 0.59610 0.57120 0.54820 0.00330  0.01200  0.00130  291 PHE A CE2 
2244 C CZ  . PHE A 291 ? 0.57160 0.54110 0.52590 0.00390  0.01210  0.00140  291 PHE A CZ  
2245 N N   . THR A 292 ? 0.51670 0.50780 0.48060 0.01130  0.01580  0.01040  292 THR A N   
2246 C CA  . THR A 292 ? 0.48560 0.48190 0.45560 0.01400  0.01680  0.01410  292 THR A CA  
2247 C C   . THR A 292 ? 0.49240 0.48860 0.46760 0.01620  0.01730  0.01880  292 THR A C   
2248 O O   . THR A 292 ? 0.48330 0.47390 0.45850 0.01600  0.01760  0.01810  292 THR A O   
2249 C CB  . THR A 292 ? 0.50110 0.49570 0.47580 0.01580  0.01870  0.01170  292 THR A CB  
2250 O OG1 . THR A 292 ? 0.48110 0.46830 0.45860 0.01680  0.01960  0.00930  292 THR A OG1 
2251 C CG2 . THR A 292 ? 0.47420 0.47050 0.44380 0.01360  0.01860  0.00830  292 THR A CG2 
2252 N N   . PRO A 293 ? 0.49180 0.49440 0.47270 0.01840  0.01760  0.02420  293 PRO A N   
2253 C CA  . PRO A 293 ? 0.48570 0.48860 0.47450 0.02100  0.01860  0.03030  293 PRO A CA  
2254 C C   . PRO A 293 ? 0.50720 0.50060 0.50380 0.02260  0.02050  0.02800  293 PRO A C   
2255 O O   . PRO A 293 ? 0.49810 0.48800 0.49710 0.02260  0.02090  0.03010  293 PRO A O   
2256 C CB  . PRO A 293 ? 0.47100 0.48250 0.46640 0.02340  0.01860  0.03620  293 PRO A CB  
2257 C CG  . PRO A 293 ? 0.48270 0.50140 0.46970 0.02090  0.01640  0.03390  293 PRO A CG  
2258 C CD  . PRO A 293 ? 0.46110 0.47240 0.44160 0.01830  0.01660  0.02590  293 PRO A CD  
2259 N N   . PHE A 294 ? 0.52910 0.51870 0.52840 0.02320  0.02160  0.02260  294 PHE A N   
2260 C CA  . PHE A 294 ? 0.49000 0.47110 0.49550 0.02410  0.02300  0.01780  294 PHE A CA  
2261 C C   . PHE A 294 ? 0.53340 0.50890 0.53210 0.02140  0.02180  0.01400  294 PHE A C   
2262 O O   . PHE A 294 ? 0.53500 0.50480 0.54020 0.02180  0.02230  0.01340  294 PHE A O   
2263 C CB  . PHE A 294 ? 0.57630 0.55670 0.58280 0.02490  0.02430  0.01100  294 PHE A CB  
2264 C CG  . PHE A 294 ? 0.60410 0.57690 0.61520 0.02520  0.02530  0.00380  294 PHE A CG  
2265 C CD1 . PHE A 294 ? 0.66070 0.63040 0.66260 0.02240  0.02410  -0.00210 294 PHE A CD1 
2266 C CD2 . PHE A 294 ? 0.68220 0.65150 0.70770 0.02820  0.02730  0.00290  294 PHE A CD2 
2267 C CE1 . PHE A 294 ? 0.70540 0.66980 0.71110 0.02240  0.02440  -0.00920 294 PHE A CE1 
2268 C CE2 . PHE A 294 ? 0.68080 0.64380 0.71110 0.02810  0.02790  -0.00520 294 PHE A CE2 
2269 C CZ  . PHE A 294 ? 0.71900 0.68010 0.73870 0.02510  0.02630  -0.01140 294 PHE A CZ  
2270 N N   . ASP A 295 ? 0.48660 0.46360 0.47390 0.01860  0.02030  0.01140  295 ASP A N   
2271 C CA  . ASP A 295 ? 0.53800 0.51010 0.52030 0.01630  0.01910  0.00850  295 ASP A CA  
2272 C C   . ASP A 295 ? 0.55160 0.52340 0.53640 0.01640  0.01910  0.01330  295 ASP A C   
2273 O O   . ASP A 295 ? 0.50630 0.47310 0.49330 0.01570  0.01900  0.01200  295 ASP A O   
2274 C CB  . ASP A 295 ? 0.48530 0.45920 0.45730 0.01340  0.01750  0.00630  295 ASP A CB  
2275 C CG  . ASP A 295 ? 0.55540 0.53060 0.52450 0.01300  0.01770  0.00240  295 ASP A CG  
2276 O OD1 . ASP A 295 ? 0.53230 0.50590 0.50610 0.01460  0.01900  -0.00060 295 ASP A OD1 
2277 O OD2 . ASP A 295 ? 0.53440 0.51270 0.49750 0.01080  0.01660  0.00230  295 ASP A OD2 
2278 N N   . VAL A 296 ? 0.49490 0.47350 0.47930 0.01710  0.01930  0.01910  296 VAL A N   
2279 C CA  . VAL A 296 ? 0.49420 0.47470 0.48010 0.01720  0.01980  0.02420  296 VAL A CA  
2280 C C   . VAL A 296 ? 0.53020 0.50670 0.52850 0.01930  0.02130  0.02790  296 VAL A C   
2281 O O   . VAL A 296 ? 0.54920 0.52240 0.55060 0.01870  0.02180  0.02870  296 VAL A O   
2282 C CB  . VAL A 296 ? 0.49210 0.48300 0.47410 0.01750  0.01940  0.02950  296 VAL A CB  
2283 C CG1 . VAL A 296 ? 0.49410 0.48930 0.47790 0.01800  0.02060  0.03580  296 VAL A CG1 
2284 C CG2 . VAL A 296 ? 0.44270 0.43670 0.41420 0.01500  0.01770  0.02470  296 VAL A CG2 
2285 N N   . VAL A 297 ? 0.49420 0.47150 0.50140 0.02170  0.02230  0.03070  297 VAL A N   
2286 C CA  . VAL A 297 ? 0.57100 0.54410 0.59310 0.02380  0.02390  0.03440  297 VAL A CA  
2287 C C   . VAL A 297 ? 0.59610 0.55960 0.62220 0.02270  0.02380  0.02690  297 VAL A C   
2288 O O   . VAL A 297 ? 0.61260 0.57230 0.64750 0.02260  0.02440  0.02920  297 VAL A O   
2289 C CB  . VAL A 297 ? 0.59200 0.56710 0.62440 0.02680  0.02490  0.03740  297 VAL A CB  
2290 C CG1 . VAL A 297 ? 0.61960 0.58810 0.67010 0.02880  0.02660  0.03930  297 VAL A CG1 
2291 C CG2 . VAL A 297 ? 0.56230 0.54900 0.59300 0.02810  0.02450  0.04710  297 VAL A CG2 
2292 N N   . ARG A 298 ? 0.53520 0.49580 0.55510 0.02170  0.02290  0.01810  298 ARG A N   
2293 C CA  . ARG A 298 ? 0.59110 0.54450 0.61370 0.02040  0.02230  0.01040  298 ARG A CA  
2294 C C   . ARG A 298 ? 0.64480 0.59600 0.66450 0.01820  0.02120  0.01100  298 ARG A C   
2295 O O   . ARG A 298 ? 0.62870 0.57470 0.65690 0.01760  0.02100  0.00870  298 ARG A O   
2296 C CB  . ARG A 298 ? 0.62200 0.57570 0.63520 0.01930  0.02130  0.00190  298 ARG A CB  
2297 C CG  . ARG A 298 ? 0.69600 0.64580 0.70380 0.01660  0.01930  -0.00430 298 ARG A CG  
2298 C CD  . ARG A 298 ? 0.75070 0.70150 0.75180 0.01570  0.01840  -0.01280 298 ARG A CD  
2299 N NE  . ARG A 298 ? 0.80250 0.75760 0.79040 0.01390  0.01720  -0.01280 298 ARG A NE  
2300 C CZ  . ARG A 298 ? 0.88570 0.84110 0.86610 0.01150  0.01510  -0.01640 298 ARG A CZ  
2301 N NH1 . ARG A 298 ? 0.64930 0.60140 0.63250 0.01050  0.01340  -0.02050 298 ARG A NH1 
2302 N NH2 . ARG A 298 ? 0.77370 0.73330 0.74430 0.01020  0.01440  -0.01560 298 ARG A NH2 
2303 N N   . GLN A 299 ? 0.62100 0.57660 0.63020 0.01690  0.02050  0.01360  299 GLN A N   
2304 C CA  . GLN A 299 ? 0.60920 0.56330 0.61500 0.01490  0.01960  0.01320  299 GLN A CA  
2305 C C   . GLN A 299 ? 0.63180 0.58850 0.64310 0.01550  0.02120  0.02090  299 GLN A C   
2306 O O   . GLN A 299 ? 0.68140 0.63510 0.69760 0.01450  0.02130  0.02100  299 GLN A O   
2307 C CB  . GLN A 299 ? 0.61140 0.56810 0.60420 0.01310  0.01810  0.01050  299 GLN A CB  
2308 C CG  . GLN A 299 ? 0.56590 0.52150 0.55640 0.01150  0.01750  0.01020  299 GLN A CG  
2309 C CD  . GLN A 299 ? 0.56530 0.52170 0.54600 0.00970  0.01580  0.00690  299 GLN A CD  
2310 O OE1 . GLN A 299 ? 0.49040 0.44650 0.47020 0.00870  0.01550  0.00690  299 GLN A OE1 
2311 N NE2 . GLN A 299 ? 0.50470 0.46270 0.47950 0.00930  0.01500  0.00460  299 GLN A NE2 
2312 N N   . CYS A 300 ? 0.58060 0.54410 0.59180 0.01700  0.02260  0.02780  300 CYS A N   
2313 C CA  . CYS A 300 ? 0.69150 0.66040 0.70620 0.01760  0.02430  0.03610  300 CYS A CA  
2314 C C   . CYS A 300 ? 0.76880 0.73520 0.80000 0.01910  0.02600  0.04240  300 CYS A C   
2315 O O   . CYS A 300 ? 0.75950 0.72050 0.80060 0.02030  0.02600  0.04070  300 CYS A O   
2316 C CB  . CYS A 300 ? 0.60220 0.58150 0.60910 0.01840  0.02470  0.04100  300 CYS A CB  
2317 S SG  . CYS A 300 ? 0.62600 0.60920 0.61650 0.01610  0.02320  0.03460  300 CYS A SG  
2318 N N   . SER A 301 ? 0.85220 0.82310 0.88750 0.01910  0.02780  0.05000  301 SER A N   
2319 C CA  . SER A 301 ? 0.94530 0.91550 0.99740 0.02050  0.02970  0.05850  301 SER A CA  
2320 C C   . SER A 301 ? 1.05830 1.03600 1.11340 0.02310  0.03040  0.06730  301 SER A C   
2321 O O   . SER A 301 ? 1.04240 1.02790 1.08500 0.02340  0.02960  0.06750  301 SER A O   
2322 C CB  . SER A 301 ? 0.95570 0.92960 1.01180 0.01960  0.03170  0.06480  301 SER A CB  
2323 O OG  . SER A 301 ? 0.84800 0.83390 0.89250 0.01980  0.03290  0.07010  301 SER A OG  
2324 N N   . GLY A 302 ? 0.98270 0.95780 1.05590 0.02480  0.03170  0.07430  302 GLY A N   
2325 C CA  . GLY A 302 ? 0.91760 0.89950 0.99800 0.02760  0.03240  0.08430  302 GLY A CA  
2326 C C   . GLY A 302 ? 0.89880 0.88820 0.99040 0.02850  0.03470  0.09930  302 GLY A C   
2327 O O   . GLY A 302 ? 0.89500 0.88990 0.98070 0.02690  0.03590  0.10260  302 GLY A O   
2328 N N   . SER B 1   ? 0.57360 0.58180 0.57570 -0.02950 -0.00410 0.09220  1   SER B N   
2329 C CA  . SER B 1   ? 0.62830 0.62280 0.63940 -0.02900 -0.00440 0.08310  1   SER B CA  
2330 C C   . SER B 1   ? 0.57700 0.56760 0.57630 -0.02620 -0.00360 0.07020  1   SER B C   
2331 O O   . SER B 1   ? 0.52980 0.52740 0.51530 -0.02490 -0.00220 0.06720  1   SER B O   
2332 C CB  . SER B 1   ? 0.59020 0.58220 0.61250 -0.03170 -0.00280 0.08300  1   SER B CB  
2333 O OG  . SER B 1   ? 0.69990 0.69340 0.73750 -0.03440 -0.00370 0.09520  1   SER B OG  
2334 N N   . GLY B 2   ? 0.57240 0.55240 0.57840 -0.02550 -0.00410 0.06240  2   GLY B N   
2335 C CA  . GLY B 2   ? 0.53610 0.51190 0.53320 -0.02290 -0.00330 0.05130  2   GLY B CA  
2336 C C   . GLY B 2   ? 0.54040 0.51120 0.53740 -0.02080 -0.00510 0.04920  2   GLY B C   
2337 O O   . GLY B 2   ? 0.56560 0.53860 0.56500 -0.02090 -0.00720 0.05610  2   GLY B O   
2338 N N   . PHE B 3   ? 0.51580 0.48100 0.51040 -0.01900 -0.00440 0.04010  3   PHE B N   
2339 C CA  . PHE B 3   ? 0.54010 0.50130 0.53510 -0.01700 -0.00580 0.03800  3   PHE B CA  
2340 C C   . PHE B 3   ? 0.51000 0.46980 0.49580 -0.01480 -0.00430 0.02930  3   PHE B C   
2341 O O   . PHE B 3   ? 0.56070 0.51750 0.54770 -0.01460 -0.00270 0.02340  3   PHE B O   
2342 C CB  . PHE B 3   ? 0.57960 0.53320 0.58940 -0.01720 -0.00660 0.03790  3   PHE B CB  
2343 C CG  . PHE B 3   ? 0.54120 0.49270 0.55360 -0.01540 -0.00850 0.03930  3   PHE B CG  
2344 C CD1 . PHE B 3   ? 0.54380 0.50040 0.55710 -0.01590 -0.01110 0.04860  3   PHE B CD1 
2345 C CD2 . PHE B 3   ? 0.57090 0.51720 0.58430 -0.01340 -0.00760 0.03170  3   PHE B CD2 
2346 C CE1 . PHE B 3   ? 0.60170 0.55750 0.61800 -0.01440 -0.01320 0.05030  3   PHE B CE1 
2347 C CE2 . PHE B 3   ? 0.54590 0.49090 0.56290 -0.01180 -0.00910 0.03320  3   PHE B CE2 
2348 C CZ  . PHE B 3   ? 0.53600 0.48560 0.55460 -0.01230 -0.01220 0.04230  3   PHE B CZ  
2349 N N   . ARG B 4   ? 0.52340 0.48610 0.50060 -0.01330 -0.00480 0.02860  4   ARG B N   
2350 C CA  . ARG B 4   ? 0.53060 0.49230 0.50070 -0.01130 -0.00320 0.02150  4   ARG B CA  
2351 C C   . ARG B 4   ? 0.52230 0.48150 0.49270 -0.00980 -0.00450 0.01980  4   ARG B C   
2352 O O   . ARG B 4   ? 0.51260 0.47330 0.48510 -0.01010 -0.00690 0.02420  4   ARG B O   
2353 C CB  . ARG B 4   ? 0.51740 0.48510 0.47770 -0.01090 -0.00200 0.02040  4   ARG B CB  
2354 C CG  . ARG B 4   ? 0.59460 0.56560 0.55340 -0.01190 -0.00000 0.02050  4   ARG B CG  
2355 C CD  . ARG B 4   ? 0.62340 0.59200 0.58050 -0.01020 0.00190  0.01410  4   ARG B CD  
2356 N NE  . ARG B 4   ? 0.62090 0.59440 0.57520 -0.01040 0.00380  0.01370  4   ARG B NE  
2357 C CZ  . ARG B 4   ? 0.66600 0.63910 0.62040 -0.00950 0.00500  0.01010  4   ARG B CZ  
2358 N NH1 . ARG B 4   ? 0.72050 0.68960 0.67590 -0.00830 0.00500  0.00660  4   ARG B NH1 
2359 N NH2 . ARG B 4   ? 0.55700 0.53510 0.51090 -0.01010 0.00630  0.01060  4   ARG B NH2 
2360 N N   . LYS B 5   ? 0.51400 0.47030 0.48240 -0.00810 -0.00290 0.01410  5   LYS B N   
2361 C CA  . LYS B 5   ? 0.56290 0.51780 0.53130 -0.00670 -0.00380 0.01240  5   LYS B CA  
2362 C C   . LYS B 5   ? 0.54350 0.50340 0.50430 -0.00670 -0.00480 0.01230  5   LYS B C   
2363 O O   . LYS B 5   ? 0.57990 0.54180 0.53510 -0.00610 -0.00310 0.00940  5   LYS B O   
2364 C CB  . LYS B 5   ? 0.57800 0.52960 0.54710 -0.00510 -0.00140 0.00740  5   LYS B CB  
2365 C CG  . LYS B 5   ? 0.63950 0.58800 0.61490 -0.00410 -0.00190 0.00660  5   LYS B CG  
2366 C CD  . LYS B 5   ? 0.68300 0.62940 0.66060 -0.00290 0.00100  0.00280  5   LYS B CD  
2367 C CE  . LYS B 5   ? 0.63900 0.58250 0.62540 -0.00290 0.00110  0.00240  5   LYS B CE  
2368 N NZ  . LYS B 5   ? 0.74210 0.68600 0.72830 -0.00190 0.00420  -0.00230 5   LYS B NZ  
2369 N N   . MET B 6   ? 0.49220 0.45530 0.45330 -0.00750 -0.00770 0.01580  6   MET B N   
2370 C CA  . MET B 6   ? 0.53880 0.50890 0.49250 -0.00800 -0.00910 0.01560  6   MET B CA  
2371 C C   . MET B 6   ? 0.52120 0.49180 0.47530 -0.00760 -0.01150 0.01300  6   MET B C   
2372 O O   . MET B 6   ? 0.56330 0.53440 0.52240 -0.00810 -0.01440 0.01670  6   MET B O   
2373 C CB  . MET B 6   ? 0.51960 0.49630 0.47220 -0.00980 -0.01100 0.02290  6   MET B CB  
2374 C CG  . MET B 6   ? 0.58810 0.57400 0.53190 -0.01040 -0.01190 0.02250  6   MET B CG  
2375 S SD  . MET B 6   ? 0.67550 0.67030 0.61780 -0.01250 -0.01230 0.03240  6   MET B SD  
2376 C CE  . MET B 6   ? 0.62590 0.62100 0.57720 -0.01350 -0.01670 0.04160  6   MET B CE  
2377 N N   . ALA B 7   ? 0.50100 0.47280 0.45060 -0.00690 -0.01070 0.00710  7   ALA B N   
2378 C CA  . ALA B 7   ? 0.50680 0.47950 0.45780 -0.00690 -0.01320 0.00360  7   ALA B CA  
2379 C C   . ALA B 7   ? 0.57830 0.56070 0.52320 -0.00840 -0.01650 0.00440  7   ALA B C   
2380 O O   . ALA B 7   ? 0.53900 0.52770 0.47720 -0.00900 -0.01590 0.00650  7   ALA B O   
2381 C CB  . ALA B 7   ? 0.53230 0.50160 0.48360 -0.00560 -0.01080 -0.00330 7   ALA B CB  
2382 N N   . PHE B 8   ? 0.49930 0.48410 0.44630 -0.00900 -0.02010 0.00290  8   PHE B N   
2383 C CA  . PHE B 8   ? 0.53440 0.53010 0.47430 -0.01050 -0.02340 0.00150  8   PHE B CA  
2384 C C   . PHE B 8   ? 0.55630 0.55420 0.49030 -0.01000 -0.02120 -0.00770 8   PHE B C   
2385 O O   . PHE B 8   ? 0.56640 0.55650 0.50480 -0.00860 -0.01850 -0.01320 8   PHE B O   
2386 C CB  . PHE B 8   ? 0.56560 0.56450 0.50980 -0.01160 -0.02840 0.00130  8   PHE B CB  
2387 C CG  . PHE B 8   ? 0.59940 0.59930 0.54940 -0.01200 -0.03130 0.01100  8   PHE B CG  
2388 C CD1 . PHE B 8   ? 0.59340 0.60350 0.53880 -0.01330 -0.03420 0.01840  8   PHE B CD1 
2389 C CD2 . PHE B 8   ? 0.54660 0.53770 0.50760 -0.01100 -0.03070 0.01300  8   PHE B CD2 
2390 C CE1 . PHE B 8   ? 0.61250 0.62330 0.56550 -0.01350 -0.03670 0.02830  8   PHE B CE1 
2391 C CE2 . PHE B 8   ? 0.61050 0.60190 0.57880 -0.01100 -0.03300 0.02150  8   PHE B CE2 
2392 C CZ  . PHE B 8   ? 0.64990 0.65060 0.61500 -0.01230 -0.03620 0.02940  8   PHE B CZ  
2393 N N   . PRO B 9   ? 0.57760 0.58670 0.50230 -0.01100 -0.02210 -0.00930 9   PRO B N   
2394 C CA  . PRO B 9   ? 0.58060 0.59260 0.50090 -0.01030 -0.02000 -0.01970 9   PRO B CA  
2395 C C   . PRO B 9   ? 0.57290 0.58150 0.49940 -0.01060 -0.02240 -0.02780 9   PRO B C   
2396 O O   . PRO B 9   ? 0.59810 0.60940 0.52730 -0.01210 -0.02700 -0.02590 9   PRO B O   
2397 C CB  . PRO B 9   ? 0.59120 0.61860 0.50020 -0.01170 -0.02150 -0.01930 9   PRO B CB  
2398 C CG  . PRO B 9   ? 0.61330 0.64440 0.52110 -0.01270 -0.02280 -0.00620 9   PRO B CG  
2399 C CD  . PRO B 9   ? 0.54360 0.56440 0.46220 -0.01270 -0.02530 -0.00200 9   PRO B CD  
2400 N N   . SER B 10  ? 0.56380 0.56570 0.49490 -0.00910 -0.01920 -0.03580 10  SER B N   
2401 C CA  . SER B 10  ? 0.57320 0.56840 0.51460 -0.00920 -0.02040 -0.04180 10  SER B CA  
2402 C C   . SER B 10  ? 0.56860 0.56970 0.50930 -0.01020 -0.02230 -0.05370 10  SER B C   
2403 O O   . SER B 10  ? 0.59000 0.58590 0.54060 -0.01060 -0.02370 -0.05930 10  SER B O   
2404 C CB  . SER B 10  ? 0.52590 0.50940 0.47570 -0.00700 -0.01580 -0.04190 10  SER B CB  
2405 O OG  . SER B 10  ? 0.59760 0.58230 0.54420 -0.00540 -0.01200 -0.04680 10  SER B OG  
2406 N N   . GLY B 11  ? 0.56750 0.58000 0.49720 -0.01060 -0.02230 -0.05780 11  GLY B N   
2407 C CA  . GLY B 11  ? 0.57280 0.59200 0.50140 -0.01130 -0.02340 -0.07110 11  GLY B CA  
2408 C C   . GLY B 11  ? 0.60270 0.62380 0.53690 -0.01370 -0.02910 -0.07640 11  GLY B C   
2409 O O   . GLY B 11  ? 0.56970 0.58730 0.51260 -0.01390 -0.02920 -0.08750 11  GLY B O   
2410 N N   . LYS B 12  ? 0.57010 0.59750 0.50080 -0.01560 -0.03400 -0.06860 12  LYS B N   
2411 C CA  . LYS B 12  ? 0.60590 0.63760 0.54150 -0.01820 -0.04020 -0.07300 12  LYS B CA  
2412 C C   . LYS B 12  ? 0.57360 0.59150 0.52590 -0.01800 -0.03990 -0.07460 12  LYS B C   
2413 O O   . LYS B 12  ? 0.60040 0.61980 0.56010 -0.02010 -0.04380 -0.08260 12  LYS B O   
2414 C CB  . LYS B 12  ? 0.62570 0.66640 0.55610 -0.01980 -0.04530 -0.06180 12  LYS B CB  
2415 C CG  . LYS B 12  ? 0.69240 0.75000 0.60740 -0.02070 -0.04700 -0.05960 12  LYS B CG  
2416 C CD  . LYS B 12  ? 0.76460 0.82980 0.67780 -0.02210 -0.05210 -0.04650 12  LYS B CD  
2417 C CE  . LYS B 12  ? 0.88420 0.96970 0.78260 -0.02370 -0.05530 -0.04470 12  LYS B CE  
2418 N NZ  . LYS B 12  ? 0.96210 1.05050 0.85050 -0.02220 -0.04940 -0.04620 12  LYS B NZ  
2419 N N   . VAL B 13  ? 0.57260 0.57820 0.53120 -0.01580 -0.03540 -0.06700 13  VAL B N   
2420 C CA  . VAL B 13  ? 0.57170 0.56520 0.54590 -0.01550 -0.03440 -0.06690 13  VAL B CA  
2421 C C   . VAL B 13  ? 0.58680 0.57270 0.56940 -0.01410 -0.03020 -0.07590 13  VAL B C   
2422 O O   . VAL B 13  ? 0.51520 0.49570 0.51150 -0.01500 -0.03120 -0.08120 13  VAL B O   
2423 C CB  . VAL B 13  ? 0.50080 0.48660 0.47740 -0.01380 -0.03160 -0.05430 13  VAL B CB  
2424 C CG1 . VAL B 13  ? 0.51220 0.48680 0.50480 -0.01320 -0.02960 -0.05280 13  VAL B CG1 
2425 C CG2 . VAL B 13  ? 0.51230 0.50540 0.48420 -0.01510 -0.03610 -0.04620 13  VAL B CG2 
2426 N N   . GLU B 14  ? 0.56820 0.55450 0.54390 -0.01210 -0.02590 -0.07800 14  GLU B N   
2427 C CA  . GLU B 14  ? 0.50890 0.48840 0.49380 -0.01040 -0.02190 -0.08600 14  GLU B CA  
2428 C C   . GLU B 14  ? 0.54460 0.52700 0.53670 -0.01230 -0.02490 -0.09970 14  GLU B C   
2429 O O   . GLU B 14  ? 0.58930 0.56310 0.59670 -0.01180 -0.02310 -0.10530 14  GLU B O   
2430 C CB  . GLU B 14  ? 0.52220 0.50460 0.49760 -0.00790 -0.01730 -0.08710 14  GLU B CB  
2431 C CG  . GLU B 14  ? 0.49150 0.47070 0.46120 -0.00620 -0.01420 -0.07440 14  GLU B CG  
2432 C CD  . GLU B 14  ? 0.58670 0.57210 0.54560 -0.00450 -0.01060 -0.07530 14  GLU B CD  
2433 O OE1 . GLU B 14  ? 0.56150 0.54760 0.52350 -0.00310 -0.00800 -0.08470 14  GLU B OE1 
2434 O OE2 . GLU B 14  ? 0.55740 0.54760 0.50610 -0.00470 -0.01070 -0.06700 14  GLU B OE2 
2435 N N   . GLY B 15  ? 0.52890 0.52380 0.51100 -0.01470 -0.02970 -0.10530 15  GLY B N   
2436 C CA  . GLY B 15  ? 0.55510 0.55420 0.54320 -0.01680 -0.03280 -0.12010 15  GLY B CA  
2437 C C   . GLY B 15  ? 0.60180 0.59580 0.60520 -0.01930 -0.03700 -0.12120 15  GLY B C   
2438 O O   . GLY B 15  ? 0.63670 0.63250 0.64880 -0.02130 -0.03960 -0.13440 15  GLY B O   
2439 N N   . CYS B 16  ? 0.56810 0.55580 0.57650 -0.01920 -0.03720 -0.10840 16  CYS B N   
2440 C CA  . CYS B 16  ? 0.56400 0.54760 0.58730 -0.02150 -0.04080 -0.10750 16  CYS B CA  
2441 C C   . CYS B 16  ? 0.56060 0.52990 0.60130 -0.02000 -0.03620 -0.10290 16  CYS B C   
2442 O O   . CYS B 16  ? 0.60040 0.56570 0.65570 -0.02180 -0.03830 -0.10170 16  CYS B O   
2443 C CB  . CYS B 16  ? 0.55890 0.54730 0.57630 -0.02250 -0.04440 -0.09570 16  CYS B CB  
2444 S SG  . CYS B 16  ? 0.62460 0.63100 0.62290 -0.02440 -0.05010 -0.09740 16  CYS B SG  
2445 N N   . MET B 17  ? 0.56410 0.52660 0.60390 -0.01660 -0.03010 -0.09920 17  MET B N   
2446 C CA  . MET B 17  ? 0.53790 0.48860 0.59270 -0.01490 -0.02560 -0.09240 17  MET B CA  
2447 C C   . MET B 17  ? 0.56680 0.51150 0.63930 -0.01530 -0.02460 -0.10280 17  MET B C   
2448 O O   . MET B 17  ? 0.55140 0.49820 0.62180 -0.01460 -0.02380 -0.11380 17  MET B O   
2449 C CB  . MET B 17  ? 0.54100 0.48810 0.58780 -0.01130 -0.02000 -0.08300 17  MET B CB  
2450 C CG  . MET B 17  ? 0.55460 0.50630 0.58620 -0.01090 -0.02060 -0.07310 17  MET B CG  
2451 S SD  . MET B 17  ? 0.55240 0.50510 0.58870 -0.01310 -0.02430 -0.06510 17  MET B SD  
2452 C CE  . MET B 17  ? 0.50920 0.45100 0.56520 -0.01190 -0.01990 -0.05960 17  MET B CE  
2453 N N   . VAL B 18  ? 0.55670 0.49460 0.64810 -0.01660 -0.02480 -0.09980 18  VAL B N   
2454 C CA  . VAL B 18  ? 0.53980 0.47020 0.65280 -0.01700 -0.02360 -0.10730 18  VAL B CA  
2455 C C   . VAL B 18  ? 0.49670 0.41770 0.62460 -0.01530 -0.01890 -0.09450 18  VAL B C   
2456 O O   . VAL B 18  ? 0.52930 0.45060 0.65040 -0.01420 -0.01720 -0.08170 18  VAL B O   
2457 C CB  . VAL B 18  ? 0.58360 0.51680 0.70830 -0.02140 -0.02950 -0.11840 18  VAL B CB  
2458 C CG1 . VAL B 18  ? 0.57670 0.52120 0.68600 -0.02300 -0.03390 -0.13200 18  VAL B CG1 
2459 C CG2 . VAL B 18  ? 0.52020 0.45480 0.64920 -0.02380 -0.03260 -0.10910 18  VAL B CG2 
2460 N N   . GLN B 19  ? 0.55680 0.47000 0.70530 -0.01490 -0.01660 -0.09830 19  GLN B N   
2461 C CA  . GLN B 19  ? 0.56680 0.47200 0.73270 -0.01350 -0.01230 -0.08650 19  GLN B CA  
2462 C C   . GLN B 19  ? 0.55730 0.45940 0.74520 -0.01720 -0.01500 -0.08810 19  GLN B C   
2463 O O   . GLN B 19  ? 0.58790 0.49020 0.78520 -0.01990 -0.01880 -0.10210 19  GLN B O   
2464 C CB  . GLN B 19  ? 0.57770 0.47630 0.75450 -0.01030 -0.00760 -0.08800 19  GLN B CB  
2465 C CG  . GLN B 19  ? 0.62690 0.51930 0.81980 -0.00850 -0.00300 -0.07300 19  GLN B CG  
2466 C CD  . GLN B 19  ? 0.69830 0.58470 0.90310 -0.00490 0.00160  -0.07250 19  GLN B CD  
2467 O OE1 . GLN B 19  ? 0.70640 0.59170 0.91320 -0.00410 0.00140  -0.08550 19  GLN B OE1 
2468 N NE2 . GLN B 19  ? 0.72310 0.60680 0.93640 -0.00260 0.00580  -0.05710 19  GLN B NE2 
2469 N N   . VAL B 20  ? 0.54350 0.44410 0.73900 -0.01750 -0.01330 -0.07450 20  VAL B N   
2470 C CA  . VAL B 20  ? 0.55220 0.45050 0.76990 -0.02100 -0.01530 -0.07370 20  VAL B CA  
2471 C C   . VAL B 20  ? 0.56780 0.45950 0.80450 -0.01930 -0.00970 -0.06060 20  VAL B C   
2472 O O   . VAL B 20  ? 0.53130 0.42470 0.75870 -0.01660 -0.00550 -0.04700 20  VAL B O   
2473 C CB  . VAL B 20  ? 0.52510 0.43020 0.73500 -0.02330 -0.01860 -0.06870 20  VAL B CB  
2474 C CG1 . VAL B 20  ? 0.53040 0.43340 0.76590 -0.02720 -0.02050 -0.06780 20  VAL B CG1 
2475 C CG2 . VAL B 20  ? 0.55710 0.47030 0.74740 -0.02470 -0.02420 -0.07890 20  VAL B CG2 
2476 N N   . THR B 21  ? 0.61120 0.49610 0.87500 -0.02110 -0.00960 -0.06440 21  THR B N   
2477 C CA  . THR B 21  ? 0.62770 0.50670 0.91300 -0.01970 -0.00440 -0.05120 21  THR B CA  
2478 C C   . THR B 21  ? 0.62150 0.49790 0.93360 -0.02380 -0.00590 -0.04910 21  THR B C   
2479 O O   . THR B 21  ? 0.65450 0.52910 0.97900 -0.02740 -0.01060 -0.06310 21  THR B O   
2480 C CB  . THR B 21  ? 0.66820 0.53980 0.96580 -0.01700 -0.00160 -0.05540 21  THR B CB  
2481 O OG1 . THR B 21  ? 0.67370 0.54850 0.94670 -0.01350 -0.00050 -0.05880 21  THR B OG1 
2482 C CG2 . THR B 21  ? 0.67580 0.54300 0.99340 -0.01500 0.00400  -0.03860 21  THR B CG2 
2483 N N   . CYS B 22  ? 0.57220 0.44950 0.89350 -0.02320 -0.00180 -0.03180 22  CYS B N   
2484 C CA  . CYS B 22  ? 0.61730 0.49270 0.96650 -0.02680 -0.00170 -0.02580 22  CYS B CA  
2485 C C   . CYS B 22  ? 0.66090 0.53260 1.02820 -0.02430 0.00480  -0.00930 22  CYS B C   
2486 O O   . CYS B 22  ? 0.61620 0.49350 0.97130 -0.02160 0.00920  0.00580  22  CYS B O   
2487 C CB  . CYS B 22  ? 0.68010 0.56370 1.02110 -0.02870 -0.00270 -0.01880 22  CYS B CB  
2488 S SG  . CYS B 22  ? 0.74860 0.63680 1.07990 -0.03270 -0.01090 -0.03540 22  CYS B SG  
2489 N N   . GLY B 23  ? 0.68490 0.54790 1.08110 -0.02530 0.00530  -0.01210 23  GLY B N   
2490 C CA  . GLY B 23  ? 0.64940 0.50910 1.06430 -0.02270 0.01120  0.00440  23  GLY B CA  
2491 C C   . GLY B 23  ? 0.65290 0.51390 1.04800 -0.01740 0.01440  0.00820  23  GLY B C   
2492 O O   . GLY B 23  ? 0.67520 0.53270 1.06090 -0.01590 0.01240  -0.00590 23  GLY B O   
2493 N N   . THR B 24  ? 0.67950 0.54700 1.06540 -0.01450 0.01910  0.02660  24  THR B N   
2494 C CA  . THR B 24  ? 0.68480 0.55560 1.04980 -0.00970 0.02180  0.03140  24  THR B CA  
2495 C C   . THR B 24  ? 0.68240 0.56190 1.01170 -0.00870 0.02070  0.02930  24  THR B C   
2496 O O   . THR B 24  ? 0.75900 0.64210 1.06940 -0.00510 0.02260  0.03290  24  THR B O   
2497 C CB  . THR B 24  ? 0.69440 0.56870 1.07080 -0.00700 0.02750  0.05300  24  THR B CB  
2498 O OG1 . THR B 24  ? 0.74670 0.62880 1.12480 -0.00900 0.02940  0.06570  24  THR B OG1 
2499 C CG2 . THR B 24  ? 0.68510 0.54990 1.09740 -0.00680 0.02890  0.05590  24  THR B CG2 
2500 N N   . THR B 25  ? 0.60700 0.48990 0.92810 -0.01190 0.01750  0.02360  25  THR B N   
2501 C CA  . THR B 25  ? 0.60960 0.50020 0.89960 -0.01100 0.01650  0.02180  25  THR B CA  
2502 C C   . THR B 25  ? 0.58000 0.46850 0.85410 -0.01150 0.01150  0.00380  25  THR B C   
2503 O O   . THR B 25  ? 0.62360 0.50830 0.90800 -0.01480 0.00720  -0.00860 25  THR B O   
2504 C CB  . THR B 25  ? 0.61920 0.51590 0.90880 -0.01370 0.01610  0.02670  25  THR B CB  
2505 O OG1 . THR B 25  ? 0.65050 0.55040 0.95600 -0.01330 0.02110  0.04370  25  THR B OG1 
2506 C CG2 . THR B 25  ? 0.57770 0.48200 0.83680 -0.01210 0.01570  0.02630  25  THR B CG2 
2507 N N   . THR B 26  ? 0.54750 0.43930 0.79700 -0.00860 0.01210  0.00250  26  THR B N   
2508 C CA  . THR B 26  ? 0.58100 0.47250 0.81430 -0.00900 0.00790  -0.01290 26  THR B CA  
2509 C C   . THR B 26  ? 0.56040 0.45920 0.76520 -0.00800 0.00720  -0.01150 26  THR B C   
2510 O O   . THR B 26  ? 0.53690 0.44000 0.73230 -0.00580 0.01070  0.00000  26  THR B O   
2511 C CB  . THR B 26  ? 0.63200 0.51860 0.86770 -0.00630 0.00920  -0.01860 26  THR B CB  
2512 O OG1 . THR B 26  ? 0.64040 0.52710 0.86510 -0.00730 0.00510  -0.03520 26  THR B OG1 
2513 C CG2 . THR B 26  ? 0.65230 0.54280 0.87230 -0.00220 0.01310  -0.00840 26  THR B CG2 
2514 N N   . LEU B 27  ? 0.50320 0.40400 0.69520 -0.00970 0.00250  -0.02330 27  LEU B N   
2515 C CA  . LEU B 27  ? 0.51950 0.42640 0.68650 -0.00870 0.00150  -0.02290 27  LEU B CA  
2516 C C   . LEU B 27  ? 0.51260 0.42110 0.66850 -0.01020 -0.00360 -0.03720 27  LEU B C   
2517 O O   . LEU B 27  ? 0.49520 0.40040 0.66130 -0.01150 -0.00560 -0.04790 27  LEU B O   
2518 C CB  . LEU B 27  ? 0.48150 0.39330 0.64600 -0.00970 0.00180  -0.01450 27  LEU B CB  
2519 C CG  . LEU B 27  ? 0.49820 0.41000 0.67950 -0.01320 -0.00070 -0.01510 27  LEU B CG  
2520 C CD1 . LEU B 27  ? 0.48640 0.39870 0.66700 -0.01630 -0.00720 -0.02910 27  LEU B CD1 
2521 C CD2 . LEU B 27  ? 0.47640 0.39430 0.65130 -0.01300 0.00080  -0.00580 27  LEU B CD2 
2522 N N   . ASN B 28  ? 0.47860 0.39300 0.61440 -0.01020 -0.00560 -0.03740 28  ASN B N   
2523 C CA  . ASN B 28  ? 0.49120 0.40950 0.61410 -0.01150 -0.01020 -0.04860 28  ASN B CA  
2524 C C   . ASN B 28  ? 0.48860 0.41110 0.61350 -0.01490 -0.01550 -0.05230 28  ASN B C   
2525 O O   . ASN B 28  ? 0.46460 0.38850 0.59380 -0.01560 -0.01540 -0.04440 28  ASN B O   
2526 C CB  . ASN B 28  ? 0.46920 0.39170 0.56950 -0.00920 -0.00920 -0.04560 28  ASN B CB  
2527 C CG  . ASN B 28  ? 0.52640 0.44580 0.62490 -0.00590 -0.00410 -0.04080 28  ASN B CG  
2528 O OD1 . ASN B 28  ? 0.51330 0.43080 0.61310 -0.00490 -0.00340 -0.04770 28  ASN B OD1 
2529 N ND2 . ASN B 28  ? 0.46430 0.38390 0.56040 -0.00410 -0.00050 -0.02940 28  ASN B ND2 
2530 N N   . GLY B 29  ? 0.48110 0.40700 0.60290 -0.01700 -0.02030 -0.06460 29  GLY B N   
2531 C CA  . GLY B 29  ? 0.52170 0.45380 0.64280 -0.02030 -0.02640 -0.06880 29  GLY B CA  
2532 C C   . GLY B 29  ? 0.52240 0.46300 0.62340 -0.02060 -0.03020 -0.07480 29  GLY B C   
2533 O O   . GLY B 29  ? 0.50780 0.44890 0.59740 -0.01870 -0.02830 -0.07870 29  GLY B O   
2534 N N   . LEU B 30  ? 0.54570 0.49360 0.64280 -0.02290 -0.03550 -0.07470 30  LEU B N   
2535 C CA  . LEU B 30  ? 0.55540 0.51320 0.63420 -0.02360 -0.03980 -0.07830 30  LEU B CA  
2536 C C   . LEU B 30  ? 0.56090 0.52600 0.64450 -0.02740 -0.04670 -0.09040 30  LEU B C   
2537 O O   . LEU B 30  ? 0.49960 0.46650 0.59490 -0.03010 -0.05060 -0.08970 30  LEU B O   
2538 C CB  . LEU B 30  ? 0.51770 0.47950 0.58800 -0.02280 -0.04060 -0.06680 30  LEU B CB  
2539 C CG  . LEU B 30  ? 0.54780 0.52020 0.60040 -0.02330 -0.04490 -0.06740 30  LEU B CG  
2540 C CD1 . LEU B 30  ? 0.50400 0.47590 0.54130 -0.02060 -0.04070 -0.06720 30  LEU B CD1 
2541 C CD2 . LEU B 30  ? 0.49920 0.47640 0.54950 -0.02330 -0.04750 -0.05740 30  LEU B CD2 
2542 N N   . TRP B 31  ? 0.54090 0.51140 0.61520 -0.02790 -0.04820 -0.10180 31  TRP B N   
2543 C CA  . TRP B 31  ? 0.56630 0.54400 0.64520 -0.03150 -0.05410 -0.11650 31  TRP B CA  
2544 C C   . TRP B 31  ? 0.60080 0.59390 0.66160 -0.03310 -0.06010 -0.11750 31  TRP B C   
2545 O O   . TRP B 31  ? 0.58050 0.58010 0.62400 -0.03170 -0.05910 -0.11950 31  TRP B O   
2546 C CB  . TRP B 31  ? 0.55680 0.53100 0.63860 -0.03070 -0.05120 -0.12950 31  TRP B CB  
2547 C CG  . TRP B 31  ? 0.57700 0.55750 0.66490 -0.03420 -0.05630 -0.14750 31  TRP B CG  
2548 C CD1 . TRP B 31  ? 0.58060 0.56660 0.67900 -0.03850 -0.06310 -0.15380 31  TRP B CD1 
2549 C CD2 . TRP B 31  ? 0.63400 0.61670 0.71890 -0.03360 -0.05480 -0.16260 31  TRP B CD2 
2550 N NE1 . TRP B 31  ? 0.60050 0.59190 0.70170 -0.04080 -0.06620 -0.17250 31  TRP B NE1 
2551 C CE2 . TRP B 31  ? 0.64470 0.63430 0.73760 -0.03770 -0.06090 -0.17840 31  TRP B CE2 
2552 C CE3 . TRP B 31  ? 0.63750 0.61770 0.71360 -0.02980 -0.04870 -0.16460 31  TRP B CE3 
2553 C CZ2 . TRP B 31  ? 0.66780 0.66170 0.76070 -0.03820 -0.06100 -0.19720 31  TRP B CZ2 
2554 C CZ3 . TRP B 31  ? 0.67060 0.65490 0.74730 -0.03010 -0.04850 -0.18240 31  TRP B CZ3 
2555 C CH2 . TRP B 31  ? 0.68120 0.67240 0.76580 -0.03420 -0.05450 -0.19880 31  TRP B CH2 
2556 N N   . LEU B 32  ? 0.58280 0.58270 0.64820 -0.03600 -0.06650 -0.11540 32  LEU B N   
2557 C CA  . LEU B 32  ? 0.58840 0.60440 0.63840 -0.03760 -0.07280 -0.11480 32  LEU B CA  
2558 C C   . LEU B 32  ? 0.63710 0.66290 0.69480 -0.04230 -0.08080 -0.12700 32  LEU B C   
2559 O O   . LEU B 32  ? 0.58160 0.60390 0.65710 -0.04450 -0.08330 -0.12630 32  LEU B O   
2560 C CB  . LEU B 32  ? 0.56970 0.58690 0.61640 -0.03640 -0.07340 -0.09830 32  LEU B CB  
2561 C CG  . LEU B 32  ? 0.54320 0.55170 0.58300 -0.03220 -0.06630 -0.08610 32  LEU B CG  
2562 C CD1 . LEU B 32  ? 0.55910 0.56780 0.60030 -0.03110 -0.06690 -0.07160 32  LEU B CD1 
2563 C CD2 . LEU B 32  ? 0.51120 0.52560 0.53080 -0.03050 -0.06430 -0.08760 32  LEU B CD2 
2564 N N   . ASP B 33  ? 0.57960 0.61900 0.62400 -0.04390 -0.08470 -0.13840 33  ASP B N   
2565 C CA  . ASP B 33  ? 0.60910 0.65900 0.66000 -0.04850 -0.09230 -0.15360 33  ASP B CA  
2566 C C   . ASP B 33  ? 0.62940 0.66490 0.70350 -0.04950 -0.08940 -0.16350 33  ASP B C   
2567 O O   . ASP B 33  ? 0.62330 0.64750 0.69960 -0.04670 -0.08230 -0.16650 33  ASP B O   
2568 C CB  . ASP B 33  ? 0.67280 0.73470 0.72490 -0.05140 -0.10060 -0.14660 33  ASP B CB  
2569 C CG  . ASP B 33  ? 0.74260 0.81850 0.77320 -0.05010 -0.10290 -0.13530 33  ASP B CG  
2570 O OD1 . ASP B 33  ? 0.72610 0.81200 0.73900 -0.04960 -0.10260 -0.14130 33  ASP B OD1 
2571 O OD2 . ASP B 33  ? 0.82570 0.90250 0.85790 -0.04940 -0.10470 -0.12020 33  ASP B OD2 
2572 N N   . ASP B 34  ? 0.61760 0.65250 0.71100 -0.05330 -0.09440 -0.16740 34  ASP B N   
2573 C CA  . ASP B 34  ? 0.62790 0.64940 0.74560 -0.05460 -0.09190 -0.17640 34  ASP B CA  
2574 C C   . ASP B 34  ? 0.63020 0.63730 0.76650 -0.05340 -0.08770 -0.16180 34  ASP B C   
2575 O O   . ASP B 34  ? 0.65140 0.65180 0.81160 -0.05620 -0.08870 -0.16610 34  ASP B O   
2576 C CB  . ASP B 34  ? 0.65670 0.68720 0.78660 -0.06020 -0.10020 -0.19350 34  ASP B CB  
2577 C CG  . ASP B 34  ? 0.69490 0.73510 0.83040 -0.06370 -0.10800 -0.18670 34  ASP B CG  
2578 O OD1 . ASP B 34  ? 0.73160 0.77380 0.85880 -0.06170 -0.10770 -0.16960 34  ASP B OD1 
2579 O OD2 . ASP B 34  ? 0.73690 0.78200 0.88770 -0.06860 -0.11450 -0.19870 34  ASP B OD2 
2580 N N   . VAL B 35  ? 0.61540 0.61870 0.74200 -0.04970 -0.08310 -0.14500 35  VAL B N   
2581 C CA  . VAL B 35  ? 0.59510 0.58700 0.73620 -0.04810 -0.07850 -0.13070 35  VAL B CA  
2582 C C   . VAL B 35  ? 0.60810 0.58970 0.74120 -0.04310 -0.06960 -0.12200 35  VAL B C   
2583 O O   . VAL B 35  ? 0.54230 0.52830 0.65440 -0.04060 -0.06820 -0.11920 35  VAL B O   
2584 C CB  . VAL B 35  ? 0.58300 0.58250 0.72140 -0.04860 -0.08220 -0.11820 35  VAL B CB  
2585 C CG1 . VAL B 35  ? 0.58270 0.57160 0.73610 -0.04690 -0.07670 -0.10490 35  VAL B CG1 
2586 C CG2 . VAL B 35  ? 0.60180 0.61360 0.74760 -0.05360 -0.09180 -0.12620 35  VAL B CG2 
2587 N N   . VAL B 36  ? 0.57370 0.54230 0.72380 -0.04190 -0.06370 -0.11720 36  VAL B N   
2588 C CA  . VAL B 36  ? 0.55100 0.51040 0.69540 -0.03720 -0.05550 -0.10700 36  VAL B CA  
2589 C C   . VAL B 36  ? 0.57600 0.53210 0.72670 -0.03610 -0.05270 -0.09140 36  VAL B C   
2590 O O   . VAL B 36  ? 0.49390 0.44750 0.66450 -0.03830 -0.05340 -0.08950 36  VAL B O   
2591 C CB  . VAL B 36  ? 0.54260 0.49110 0.70110 -0.03620 -0.05060 -0.11290 36  VAL B CB  
2592 C CG1 . VAL B 36  ? 0.52120 0.46060 0.67810 -0.03180 -0.04240 -0.10010 36  VAL B CG1 
2593 C CG2 . VAL B 36  ? 0.53420 0.48690 0.68410 -0.03670 -0.05260 -0.12930 36  VAL B CG2 
2594 N N   . TYR B 37  ? 0.48510 0.44230 0.61990 -0.03280 -0.04950 -0.08090 37  TYR B N   
2595 C CA  . TYR B 37  ? 0.51940 0.47460 0.65800 -0.03120 -0.04630 -0.06700 37  TYR B CA  
2596 C C   . TYR B 37  ? 0.52620 0.47220 0.66580 -0.02770 -0.03810 -0.05970 37  TYR B C   
2597 O O   . TYR B 37  ? 0.51830 0.46260 0.64460 -0.02530 -0.03550 -0.06110 37  TYR B O   
2598 C CB  . TYR B 37  ? 0.53240 0.49520 0.65370 -0.02990 -0.04840 -0.06060 37  TYR B CB  
2599 C CG  . TYR B 37  ? 0.53320 0.50720 0.65180 -0.03310 -0.05690 -0.06600 37  TYR B CG  
2600 C CD1 . TYR B 37  ? 0.53040 0.51140 0.63750 -0.03450 -0.06140 -0.07640 37  TYR B CD1 
2601 C CD2 . TYR B 37  ? 0.57070 0.54940 0.70010 -0.03480 -0.06050 -0.06090 37  TYR B CD2 
2602 C CE1 . TYR B 37  ? 0.51810 0.51130 0.62260 -0.03770 -0.06960 -0.08100 37  TYR B CE1 
2603 C CE2 . TYR B 37  ? 0.57190 0.56200 0.70020 -0.03780 -0.06870 -0.06510 37  TYR B CE2 
2604 C CZ  . TYR B 37  ? 0.59130 0.58880 0.70640 -0.03920 -0.07340 -0.07470 37  TYR B CZ  
2605 O OH  . TYR B 37  ? 0.59040 0.60100 0.70420 -0.04230 -0.08190 -0.07830 37  TYR B OH  
2606 N N   . CYS B 38  ? 0.48320 0.42460 0.63810 -0.02740 -0.03420 -0.05140 38  CYS B N   
2607 C CA  . CYS B 38  ? 0.48110 0.41590 0.63600 -0.02400 -0.02670 -0.04340 38  CYS B CA  
2608 C C   . CYS B 38  ? 0.46340 0.39830 0.62840 -0.02340 -0.02280 -0.03160 38  CYS B C   
2609 O O   . CYS B 38  ? 0.45600 0.39430 0.63270 -0.02590 -0.02570 -0.03080 38  CYS B O   
2610 C CB  . CYS B 38  ? 0.46600 0.39370 0.63360 -0.02430 -0.02460 -0.04890 38  CYS B CB  
2611 S SG  . CYS B 38  ? 0.48270 0.40640 0.68120 -0.02770 -0.02510 -0.04900 38  CYS B SG  
2612 N N   . PRO B 39  ? 0.45570 0.38810 0.61630 -0.02010 -0.01630 -0.02250 39  PRO B N   
2613 C CA  . PRO B 39  ? 0.45720 0.39140 0.62750 -0.01950 -0.01200 -0.01160 39  PRO B CA  
2614 C C   . PRO B 39  ? 0.46060 0.39220 0.65530 -0.02190 -0.01100 -0.00970 39  PRO B C   
2615 O O   . PRO B 39  ? 0.43520 0.36110 0.63990 -0.02240 -0.01020 -0.01250 39  PRO B O   
2616 C CB  . PRO B 39  ? 0.37710 0.31010 0.53660 -0.01570 -0.00550 -0.00390 39  PRO B CB  
2617 C CG  . PRO B 39  ? 0.42550 0.35790 0.56410 -0.01420 -0.00780 -0.01070 39  PRO B CG  
2618 C CD  . PRO B 39  ? 0.46970 0.39980 0.61480 -0.01690 -0.01280 -0.02150 39  PRO B CD  
2619 N N   . ARG B 40  ? 0.44720 0.38300 0.65350 -0.02320 -0.01070 -0.00410 40  ARG B N   
2620 C CA  . ARG B 40  ? 0.43400 0.36770 0.66500 -0.02570 -0.00930 -0.00080 40  ARG B CA  
2621 C C   . ARG B 40  ? 0.45430 0.38490 0.69140 -0.02340 -0.00190 0.00930  40  ARG B C   
2622 O O   . ARG B 40  ? 0.49930 0.42680 0.75810 -0.02520 -0.00050 0.01230  40  ARG B O   
2623 C CB  . ARG B 40  ? 0.42950 0.36940 0.67250 -0.02760 -0.01030 0.00350  40  ARG B CB  
2624 C CG  . ARG B 40  ? 0.42980 0.37510 0.66470 -0.02440 -0.00430 0.01420  40  ARG B CG  
2625 C CD  . ARG B 40  ? 0.39890 0.35090 0.64830 -0.02620 -0.00510 0.01800  40  ARG B CD  
2626 N NE  . ARG B 40  ? 0.38810 0.34610 0.63050 -0.02290 0.00100  0.02690  40  ARG B NE  
2627 C CZ  . ARG B 40  ? 0.48150 0.44620 0.73560 -0.02350 0.00250  0.03200  40  ARG B CZ  
2628 N NH1 . ARG B 40  ? 0.45410 0.42040 0.72710 -0.02730 -0.00210 0.02970  40  ARG B NH1 
2629 N NH2 . ARG B 40  ? 0.41380 0.38430 0.66140 -0.02010 0.00890  0.03900  40  ARG B NH2 
2630 N N   . ALA B 41  ? 0.47740 0.40940 0.69700 -0.01960 0.00240  0.01440  41  ALA B N   
2631 C CA  . ALA B 41  ? 0.51380 0.44460 0.73780 -0.01740 0.00880  0.02430  41  ALA B CA  
2632 C C   . ALA B 41  ? 0.51510 0.43810 0.75210 -0.01810 0.00820  0.02100  41  ALA B C   
2633 O O   . ALA B 41  ? 0.49470 0.41670 0.74370 -0.01710 0.01300  0.03060  41  ALA B O   
2634 C CB  . ALA B 41  ? 0.48480 0.41840 0.68550 -0.01340 0.01210  0.02740  41  ALA B CB  
2635 N N   . VAL B 42  ? 0.48960 0.40780 0.72560 -0.01980 0.00250  0.00780  42  VAL B N   
2636 C CA  . VAL B 42  ? 0.49290 0.40350 0.74280 -0.02040 0.00210  0.00270  42  VAL B CA  
2637 C C   . VAL B 42  ? 0.55400 0.46170 0.83400 -0.02340 0.00270  0.00660  42  VAL B C   
2638 O O   . VAL B 42  ? 0.50010 0.40150 0.79620 -0.02320 0.00450  0.00760  42  VAL B O   
2639 C CB  . VAL B 42  ? 0.46720 0.37520 0.70940 -0.02190 -0.00410 -0.01370 42  VAL B CB  
2640 C CG1 . VAL B 42  ? 0.50370 0.41370 0.75730 -0.02640 -0.01020 -0.02190 42  VAL B CG1 
2641 C CG2 . VAL B 42  ? 0.53560 0.43630 0.78470 -0.02070 -0.00320 -0.01970 42  VAL B CG2 
2642 N N   . ILE B 43  ? 0.51030 0.42220 0.80020 -0.02630 0.00120  0.00880  43  ILE B N   
2643 C CA  . ILE B 43  ? 0.56530 0.47480 0.88590 -0.02950 0.00210  0.01350  43  ILE B CA  
2644 C C   . ILE B 43  ? 0.56930 0.48300 0.89840 -0.02780 0.00950  0.03190  43  ILE B C   
2645 O O   . ILE B 43  ? 0.62710 0.54000 0.98220 -0.03030 0.01120  0.03890  43  ILE B O   
2646 C CB  . ILE B 43  ? 0.54570 0.45800 0.87800 -0.03410 -0.00350 0.00670  43  ILE B CB  
2647 C CG1 . ILE B 43  ? 0.51870 0.44040 0.84260 -0.03360 -0.00200 0.01490  43  ILE B CG1 
2648 C CG2 . ILE B 43  ? 0.57000 0.48010 0.89190 -0.03580 -0.01110 -0.01150 43  ILE B CG2 
2649 C CD1 . ILE B 43  ? 0.51510 0.44080 0.85300 -0.03820 -0.00760 0.00960  43  ILE B CD1 
2650 N N   . CYS B 44  ? 0.58550 0.50420 0.89410 -0.02380 0.01400  0.03990  44  CYS B N   
2651 C CA  . CYS B 44  ? 0.60100 0.52580 0.91450 -0.02190 0.02120  0.05700  44  CYS B CA  
2652 C C   . CYS B 44  ? 0.70010 0.61980 1.02820 -0.02070 0.02440  0.06410  44  CYS B C   
2653 O O   . CYS B 44  ? 0.70700 0.62010 1.02910 -0.01910 0.02260  0.05700  44  CYS B O   
2654 C CB  . CYS B 44  ? 0.64870 0.58100 0.93450 -0.01790 0.02440  0.06100  44  CYS B CB  
2655 S SG  . CYS B 44  ? 0.78880 0.73320 1.06850 -0.01720 0.02880  0.07030  44  CYS B SG  
2656 N N   . THR B 45  ? 0.82060 0.74440 1.16740 -0.02100 0.02960  0.07940  45  THR B N   
2657 C CA  . THR B 45  ? 0.86410 0.78460 1.22510 -0.01940 0.03310  0.08930  45  THR B CA  
2658 C C   . THR B 45  ? 0.90530 0.83530 1.24750 -0.01520 0.03870  0.10210  45  THR B C   
2659 O O   . THR B 45  ? 0.84800 0.78840 1.17460 -0.01420 0.04130  0.10670  45  THR B O   
2660 C CB  . THR B 45  ? 0.84400 0.76340 1.23980 -0.02250 0.03530  0.09980  45  THR B CB  
2661 O OG1 . THR B 45  ? 0.86180 0.78710 1.26360 -0.02570 0.03500  0.10060  45  THR B OG1 
2662 C CG2 . THR B 45  ? 0.82060 0.72670 1.23840 -0.02480 0.03100  0.08900  45  THR B CG2 
2663 N N   . SER B 46  ? 0.95450 0.88170 1.29990 -0.01260 0.04050  0.10770  46  SER B N   
2664 C CA  . SER B 46  ? 1.07380 1.01060 1.40120 -0.00860 0.04500  0.11910  46  SER B CA  
2665 C C   . SER B 46  ? 1.08240 1.03270 1.41440 -0.00840 0.05110  0.13700  46  SER B C   
2666 O O   . SER B 46  ? 1.10890 1.07060 1.41930 -0.00570 0.05440  0.14290  46  SER B O   
2667 C CB  . SER B 46  ? 1.11900 1.05050 1.45460 -0.00610 0.04550  0.12340  46  SER B CB  
2668 O OG  . SER B 46  ? 1.09500 1.01480 1.42730 -0.00620 0.04040  0.10630  46  SER B OG  
2669 N N   . GLU B 47  ? 1.08920 1.03960 1.44840 -0.01140 0.05280  0.14500  47  GLU B N   
2670 C CA  . GLU B 47  ? 1.09080 1.05580 1.45520 -0.01120 0.05930  0.16320  47  GLU B CA  
2671 C C   . GLU B 47  ? 1.08110 1.05430 1.43470 -0.01250 0.06030  0.15960  47  GLU B C   
2672 O O   . GLU B 47  ? 1.13120 1.11920 1.47560 -0.01090 0.06600  0.17090  47  GLU B O   
2673 C CB  . GLU B 47  ? 1.13130 1.09410 1.53200 -0.01360 0.06170  0.17700  47  GLU B CB  
2674 C CG  . GLU B 47  ? 1.15770 1.10520 1.58430 -0.01770 0.05650  0.16550  47  GLU B CG  
2675 C CD  . GLU B 47  ? 1.18260 1.11610 1.61580 -0.01660 0.05260  0.15670  47  GLU B CD  
2676 O OE1 . GLU B 47  ? 1.22150 1.15710 1.63650 -0.01260 0.05350  0.15850  47  GLU B OE1 
2677 O OE2 . GLU B 47  ? 1.16590 1.08710 1.62300 -0.01970 0.04880  0.14760  47  GLU B OE2 
2678 N N   . ASP B 48  ? 0.99160 0.95670 1.34640 -0.01520 0.05500  0.14420  48  ASP B N   
2679 C CA  . ASP B 48  ? 0.95260 0.92550 1.29820 -0.01600 0.05570  0.14080  48  ASP B CA  
2680 C C   . ASP B 48  ? 0.81660 0.78690 1.13410 -0.01460 0.05130  0.12460  48  ASP B C   
2681 O O   . ASP B 48  ? 0.75150 0.71780 1.07010 -0.01680 0.04680  0.11350  48  ASP B O   
2682 C CB  . ASP B 48  ? 1.02960 0.99880 1.40280 -0.02070 0.05370  0.13960  48  ASP B CB  
2683 C CG  . ASP B 48  ? 1.19970 1.17330 1.60280 -0.02240 0.05880  0.15770  48  ASP B CG  
2684 O OD1 . ASP B 48  ? 1.27720 1.26520 1.67930 -0.02130 0.06570  0.17230  48  ASP B OD1 
2685 O OD2 . ASP B 48  ? 1.23720 1.20020 1.66550 -0.02500 0.05620  0.15750  48  ASP B OD2 
2686 N N   . MET B 49  ? 0.82420 0.79800 1.11700 -0.01090 0.05260  0.12400  49  MET B N   
2687 C CA  . MET B 49  ? 0.68200 0.65390 0.94890 -0.00940 0.04910  0.11040  49  MET B CA  
2688 C C   . MET B 49  ? 0.62720 0.61130 0.87950 -0.00780 0.05300  0.11230  49  MET B C   
2689 O O   . MET B 49  ? 0.56630 0.54950 0.80000 -0.00680 0.05040  0.10180  49  MET B O   
2690 C CB  . MET B 49  ? 0.71890 0.68740 0.96870 -0.00650 0.04810  0.10790  49  MET B CB  
2691 C CG  . MET B 49  ? 0.74450 0.69990 1.00690 -0.00760 0.04370  0.10200  49  MET B CG  
2692 S SD  . MET B 49  ? 0.88240 0.83220 1.12590 -0.00460 0.04140  0.09530  49  MET B SD  
2693 C CE  . MET B 49  ? 0.64390 0.59170 0.86320 -0.00470 0.03660  0.07900  49  MET B CE  
2694 N N   . LEU B 50  ? 0.61270 0.60860 0.87390 -0.00750 0.05960  0.12600  50  LEU B N   
2695 C CA  . LEU B 50  ? 0.58280 0.59200 0.83260 -0.00590 0.06450  0.12850  50  LEU B CA  
2696 C C   . LEU B 50  ? 0.60830 0.61770 0.86930 -0.00810 0.06330  0.12370  50  LEU B C   
2697 O O   . LEU B 50  ? 0.58220 0.59440 0.82960 -0.00680 0.06280  0.11570  50  LEU B O   
2698 C CB  . LEU B 50  ? 0.67180 0.69560 0.92610 -0.00460 0.07240  0.14560  50  LEU B CB  
2699 C CG  . LEU B 50  ? 0.65510 0.69570 0.89820 -0.00250 0.07900  0.14930  50  LEU B CG  
2700 C CD1 . LEU B 50  ? 0.64830 0.69110 0.86220 0.00070  0.07840  0.14010  50  LEU B CD1 
2701 C CD2 . LEU B 50  ? 0.63120 0.68750 0.88430 -0.00220 0.08680  0.16760  50  LEU B CD2 
2702 N N   . ASN B 51  ? 0.59050 0.59660 0.87760 -0.01160 0.06230  0.12810  51  ASN B N   
2703 C CA  . ASN B 51  ? 0.55740 0.56550 0.85740 -0.01390 0.06130  0.12510  51  ASN B CA  
2704 C C   . ASN B 51  ? 0.53070 0.52630 0.85000 -0.01800 0.05410  0.11820  51  ASN B C   
2705 O O   . ASN B 51  ? 0.59140 0.58800 0.93590 -0.02130 0.05460  0.12390  51  ASN B O   
2706 C CB  . ASN B 51  ? 0.60310 0.62560 0.91750 -0.01410 0.06930  0.13980  51  ASN B CB  
2707 C CG  . ASN B 51  ? 0.62180 0.65860 0.91610 -0.01000 0.07670  0.14560  51  ASN B CG  
2708 O OD1 . ASN B 51  ? 0.61800 0.65710 0.89190 -0.00750 0.07640  0.13630  51  ASN B OD1 
2709 N ND2 . ASN B 51  ? 0.67690 0.72410 0.97730 -0.00940 0.08320  0.16100  51  ASN B ND2 
2710 N N   . PRO B 52  ? 0.57520 0.55990 0.88350 -0.01830 0.04700  0.10480  52  PRO B N   
2711 C CA  . PRO B 52  ? 0.56000 0.53420 0.88610 -0.02230 0.04000  0.09680  52  PRO B CA  
2712 C C   . PRO B 52  ? 0.52570 0.50280 0.86110 -0.02490 0.03670  0.09170  52  PRO B C   
2713 O O   . PRO B 52  ? 0.53940 0.52170 0.85990 -0.02300 0.03650  0.08760  52  PRO B O   
2714 C CB  . PRO B 52  ? 0.54480 0.50930 0.85210 -0.02120 0.03420  0.08410  52  PRO B CB  
2715 C CG  . PRO B 52  ? 0.52460 0.49530 0.80420 -0.01720 0.03640  0.08220  52  PRO B CG  
2716 C CD  . PRO B 52  ? 0.53340 0.51570 0.81350 -0.01510 0.04500  0.09600  52  PRO B CD  
2717 N N   . ASN B 53  ? 0.51390 0.48810 0.87580 -0.02930 0.03390  0.09200  53  ASN B N   
2718 C CA  . ASN B 53  ? 0.51670 0.49190 0.88710 -0.03220 0.02820  0.08400  53  ASN B CA  
2719 C C   . ASN B 53  ? 0.52590 0.49000 0.89620 -0.03490 0.01910  0.06950  53  ASN B C   
2720 O O   . ASN B 53  ? 0.48520 0.44260 0.87600 -0.03830 0.01660  0.06780  53  ASN B O   
2721 C CB  . ASN B 53  ? 0.48220 0.46310 0.88150 -0.03580 0.03030  0.09230  53  ASN B CB  
2722 C CG  . ASN B 53  ? 0.54070 0.52470 0.94500 -0.03810 0.02450  0.08430  53  ASN B CG  
2723 O OD1 . ASN B 53  ? 0.58850 0.56600 1.00120 -0.04170 0.01630  0.07370  53  ASN B OD1 
2724 N ND2 . ASN B 53  ? 0.57630 0.57030 0.97280 -0.03560 0.02810  0.08790  53  ASN B ND2 
2725 N N   . TYR B 54  ? 0.52650 0.48900 0.87360 -0.03310 0.01450  0.05910  54  TYR B N   
2726 C CA  . TYR B 54  ? 0.48710 0.44090 0.83010 -0.03500 0.00670  0.04550  54  TYR B CA  
2727 C C   . TYR B 54  ? 0.51610 0.46920 0.87960 -0.04020 -0.00050 0.03760  54  TYR B C   
2728 O O   . TYR B 54  ? 0.53560 0.48150 0.90440 -0.04280 -0.00610 0.02720  54  TYR B O   
2729 C CB  . TYR B 54  ? 0.46610 0.42020 0.78060 -0.03210 0.00360  0.03760  54  TYR B CB  
2730 C CG  . TYR B 54  ? 0.47160 0.42440 0.76660 -0.02770 0.00890  0.04170  54  TYR B CG  
2731 C CD1 . TYR B 54  ? 0.47600 0.42070 0.76630 -0.02720 0.00800  0.03750  54  TYR B CD1 
2732 C CD2 . TYR B 54  ? 0.50220 0.46190 0.78240 -0.02400 0.01440  0.04860  54  TYR B CD2 
2733 C CE1 . TYR B 54  ? 0.48610 0.43020 0.75780 -0.02320 0.01230  0.04110  54  TYR B CE1 
2734 C CE2 . TYR B 54  ? 0.45030 0.40930 0.71090 -0.02010 0.01850  0.05100  54  TYR B CE2 
2735 C CZ  . TYR B 54  ? 0.47900 0.43040 0.73630 -0.01990 0.01740  0.04810  54  TYR B CZ  
2736 O OH  . TYR B 54  ? 0.51870 0.47000 0.75750 -0.01630 0.02100  0.05060  54  TYR B OH  
2737 N N   . GLU B 55  ? 0.48850 0.44950 0.86300 -0.04190 -0.00100 0.04120  55  GLU B N   
2738 C CA  . GLU B 55  ? 0.53320 0.49450 0.92910 -0.04730 -0.00820 0.03400  55  GLU B CA  
2739 C C   . GLU B 55  ? 0.55940 0.51460 0.98320 -0.05100 -0.00710 0.03650  55  GLU B C   
2740 O O   . GLU B 55  ? 0.52080 0.47030 0.95670 -0.05500 -0.01380 0.02520  55  GLU B O   
2741 C CB  . GLU B 55  ? 0.59440 0.56620 0.99880 -0.04800 -0.00810 0.03920  55  GLU B CB  
2742 C CG  . GLU B 55  ? 0.65100 0.62490 1.07330 -0.05350 -0.01720 0.03020  55  GLU B CG  
2743 C CD  . GLU B 55  ? 0.85380 0.83910 1.28480 -0.05390 -0.01770 0.03530  55  GLU B CD  
2744 O OE1 . GLU B 55  ? 0.87140 0.86250 1.29840 -0.05020 -0.00970 0.04630  55  GLU B OE1 
2745 O OE2 . GLU B 55  ? 0.82480 0.81380 1.26740 -0.05800 -0.02600 0.02800  55  GLU B OE2 
2746 N N   . ASP B 56  ? 0.47790 0.43480 0.91260 -0.04960 0.00160  0.05120  56  ASP B N   
2747 C CA  . ASP B 56  ? 0.53190 0.48270 0.99350 -0.05230 0.00400  0.05650  56  ASP B CA  
2748 C C   . ASP B 56  ? 0.56610 0.50550 1.02200 -0.05160 0.00170  0.04800  56  ASP B C   
2749 O O   . ASP B 56  ? 0.51760 0.44930 0.99480 -0.05550 -0.00230 0.04080  56  ASP B O   
2750 C CB  . ASP B 56  ? 0.55840 0.51490 1.02460 -0.04950 0.01440  0.07550  56  ASP B CB  
2751 C CG  . ASP B 56  ? 0.59930 0.56470 1.09010 -0.05230 0.01770  0.08620  56  ASP B CG  
2752 O OD1 . ASP B 56  ? 0.61020 0.57530 1.12010 -0.05710 0.01170  0.07940  56  ASP B OD1 
2753 O OD2 . ASP B 56  ? 0.66930 0.64290 1.15960 -0.04970 0.02640  0.10140  56  ASP B OD2 
2754 N N   . LEU B 57  ? 0.48840 0.42680 0.91780 -0.04660 0.00500  0.04950  57  LEU B N   
2755 C CA  . LEU B 57  ? 0.55950 0.48810 0.98370 -0.04540 0.00390  0.04290  57  LEU B CA  
2756 C C   . LEU B 57  ? 0.57080 0.49380 0.99450 -0.04850 -0.00530 0.02360  57  LEU B C   
2757 O O   . LEU B 57  ? 0.59010 0.50420 1.02660 -0.05010 -0.00750 0.01600  57  LEU B O   
2758 C CB  . LEU B 57  ? 0.54960 0.48000 0.94260 -0.03960 0.00800  0.04630  57  LEU B CB  
2759 C CG  . LEU B 57  ? 0.58770 0.52420 0.97900 -0.03620 0.01730  0.06460  57  LEU B CG  
2760 C CD1 . LEU B 57  ? 0.55110 0.48960 0.91040 -0.03100 0.01990  0.06500  57  LEU B CD1 
2761 C CD2 . LEU B 57  ? 0.58360 0.51470 0.99940 -0.03700 0.02110  0.07400  57  LEU B CD2 
2762 N N   . LEU B 58  ? 0.53660 0.46540 0.94630 -0.04930 -0.01080 0.01550  58  LEU B N   
2763 C CA  . LEU B 58  ? 0.54670 0.47290 0.95230 -0.05210 -0.01980 -0.00260 58  LEU B CA  
2764 C C   . LEU B 58  ? 0.56110 0.48500 0.99820 -0.05820 -0.02470 -0.00930 58  LEU B C   
2765 O O   . LEU B 58  ? 0.56150 0.47910 1.00580 -0.06060 -0.02950 -0.02310 58  LEU B O   
2766 C CB  . LEU B 58  ? 0.53300 0.46760 0.91620 -0.05140 -0.02450 -0.00750 58  LEU B CB  
2767 C CG  . LEU B 58  ? 0.61500 0.54820 0.98720 -0.05320 -0.03300 -0.02550 58  LEU B CG  
2768 C CD1 . LEU B 58  ? 0.57870 0.50370 0.93980 -0.05040 -0.03050 -0.02990 58  LEU B CD1 
2769 C CD2 . LEU B 58  ? 0.64150 0.58310 0.98890 -0.05160 -0.03690 -0.02800 58  LEU B CD2 
2770 N N   . ILE B 59  ? 0.50840 0.43780 0.96600 -0.06080 -0.02330 0.00010  59  ILE B N   
2771 C CA  . ILE B 59  ? 0.52860 0.45590 1.01780 -0.06700 -0.02820 -0.00650 59  ILE B CA  
2772 C C   . ILE B 59  ? 0.57730 0.49330 1.08750 -0.06800 -0.02570 -0.00740 59  ILE B C   
2773 O O   . ILE B 59  ? 0.59370 0.50440 1.12240 -0.07250 -0.03160 -0.02100 59  ILE B O   
2774 C CB  . ILE B 59  ? 0.53080 0.46590 1.04180 -0.06970 -0.02620 0.00540  59  ILE B CB  
2775 C CG1 . ILE B 59  ? 0.64050 0.58680 1.13430 -0.06900 -0.02980 0.00430  59  ILE B CG1 
2776 C CG2 . ILE B 59  ? 0.55340 0.48600 1.09960 -0.07670 -0.03180 -0.00200 59  ILE B CG2 
2777 C CD1 . ILE B 59  ? 0.68500 0.64020 1.19590 -0.07020 -0.02600 0.01770  59  ILE B CD1 
2778 N N   . ARG B 60  ? 0.52770 0.43980 1.03500 -0.06370 -0.01730 0.00590  60  ARG B N   
2779 C CA  . ARG B 60  ? 0.56230 0.46380 1.09280 -0.06440 -0.01450 0.00720  60  ARG B CA  
2780 C C   . ARG B 60  ? 0.63030 0.52350 1.14860 -0.06280 -0.01770 -0.00810 60  ARG B C   
2781 O O   . ARG B 60  ? 0.65470 0.53830 1.19200 -0.06280 -0.01550 -0.00850 60  ARG B O   
2782 C CB  . ARG B 60  ? 0.53550 0.43780 1.06890 -0.06050 -0.00460 0.02860  60  ARG B CB  
2783 C CG  . ARG B 60  ? 0.50150 0.41270 1.04760 -0.06200 -0.00080 0.04320  60  ARG B CG  
2784 C CD  . ARG B 60  ? 0.56260 0.47870 1.10140 -0.05740 0.00880  0.06330  60  ARG B CD  
2785 N NE  . ARG B 60  ? 0.47560 0.40130 1.03140 -0.05960 0.01240  0.07680  60  ARG B NE  
2786 C CZ  . ARG B 60  ? 0.53830 0.47480 1.08390 -0.05640 0.02000  0.09300  60  ARG B CZ  
2787 N NH1 . ARG B 60  ? 0.61780 0.55660 1.13750 -0.05080 0.02500  0.09910  60  ARG B NH1 
2788 N NH2 . ARG B 60  ? 0.58100 0.52680 1.14390 -0.05890 0.02290  0.10310  60  ARG B NH2 
2789 N N   . LYS B 61  ? 0.60390 0.50070 1.09290 -0.06140 -0.02260 -0.02050 61  LYS B N   
2790 C CA  . LYS B 61  ? 0.67160 0.56200 1.14810 -0.05980 -0.02510 -0.03520 61  LYS B CA  
2791 C C   . LYS B 61  ? 0.69670 0.58730 1.18080 -0.06490 -0.03440 -0.05630 61  LYS B C   
2792 O O   . LYS B 61  ? 0.61710 0.51500 1.10660 -0.06890 -0.03970 -0.05950 61  LYS B O   
2793 C CB  . LYS B 61  ? 0.62180 0.51680 1.05940 -0.05450 -0.02370 -0.03420 61  LYS B CB  
2794 C CG  . LYS B 61  ? 0.77750 0.66620 1.20480 -0.04910 -0.01720 -0.02810 61  LYS B CG  
2795 C CD  . LYS B 61  ? 0.76300 0.65520 1.18220 -0.04480 -0.00890 -0.00700 61  LYS B CD  
2796 C CE  . LYS B 61  ? 0.86100 0.75210 1.31200 -0.04670 -0.00410 0.00820  61  LYS B CE  
2797 N NZ  . LYS B 61  ? 0.63350 0.53460 1.08070 -0.04600 0.00030  0.02440  61  LYS B NZ  
2798 N N   . SER B 62  ? 0.77300 0.65660 1.25770 -0.06460 -0.03640 -0.07110 62  SER B N   
2799 C CA  . SER B 62  ? 0.73310 0.61830 1.21870 -0.06870 -0.04500 -0.09360 62  SER B CA  
2800 C C   . SER B 62  ? 0.71090 0.59790 1.16440 -0.06500 -0.04640 -0.10510 62  SER B C   
2801 O O   . SER B 62  ? 0.70670 0.59090 1.14310 -0.05960 -0.04040 -0.09660 62  SER B O   
2802 C CB  . SER B 62  ? 0.77870 0.65400 1.30110 -0.07270 -0.04630 -0.10360 62  SER B CB  
2803 O OG  . SER B 62  ? 0.94510 0.82010 1.46140 -0.07410 -0.05220 -0.12700 62  SER B OG  
2804 N N   . ASN B 63  ? 0.68880 0.58120 1.13460 -0.06810 -0.05430 -0.12490 63  ASN B N   
2805 C CA  . ASN B 63  ? 0.67910 0.57450 1.09560 -0.06490 -0.05550 -0.13620 63  ASN B CA  
2806 C C   . ASN B 63  ? 0.68040 0.56480 1.10070 -0.06070 -0.04900 -0.13700 63  ASN B C   
2807 O O   . ASN B 63  ? 0.70920 0.59430 1.10480 -0.05570 -0.04500 -0.13160 63  ASN B O   
2808 C CB  . ASN B 63  ? 0.67420 0.57710 1.08820 -0.06950 -0.06480 -0.15890 63  ASN B CB  
2809 C CG  . ASN B 63  ? 0.67310 0.59000 1.07400 -0.07250 -0.07170 -0.15790 63  ASN B CG  
2810 O OD1 . ASN B 63  ? 0.67910 0.60130 1.06070 -0.06960 -0.06970 -0.14330 63  ASN B OD1 
2811 N ND2 . ASN B 63  ? 0.63540 0.55870 1.04750 -0.07830 -0.08020 -0.17380 63  ASN B ND2 
2812 N N   . HIS B 64  ? 0.71370 0.58760 1.16720 -0.06260 -0.04740 -0.14120 64  HIS B N   
2813 C CA  . HIS B 64  ? 0.71980 0.58340 1.17960 -0.05850 -0.04180 -0.14340 64  HIS B CA  
2814 C C   . HIS B 64  ? 0.70730 0.56660 1.16280 -0.05320 -0.03330 -0.12070 64  HIS B C   
2815 O O   . HIS B 64  ? 0.72080 0.57380 1.17450 -0.04890 -0.02870 -0.12040 64  HIS B O   
2816 C CB  . HIS B 64  ? 0.70010 0.55330 1.19950 -0.06200 -0.04270 -0.15480 64  HIS B CB  
2817 C CG  . HIS B 64  ? 0.75680 0.60370 1.28970 -0.06430 -0.03970 -0.13870 64  HIS B CG  
2818 N ND1 . HIS B 64  ? 0.78000 0.63010 1.33220 -0.07050 -0.04490 -0.14080 64  HIS B ND1 
2819 C CD2 . HIS B 64  ? 0.71680 0.55570 1.26730 -0.06140 -0.03220 -0.11940 64  HIS B CD2 
2820 C CE1 . HIS B 64  ? 0.75140 0.59550 1.33220 -0.07140 -0.04030 -0.12360 64  HIS B CE1 
2821 N NE2 . HIS B 64  ? 0.80630 0.64390 1.38600 -0.06590 -0.03260 -0.10990 64  HIS B NE2 
2822 N N   . ASN B 65  ? 0.71010 0.57400 1.16150 -0.05310 -0.03130 -0.10240 65  ASN B N   
2823 C CA  . ASN B 65  ? 0.71450 0.57750 1.15690 -0.04810 -0.02370 -0.08140 65  ASN B CA  
2824 C C   . ASN B 65  ? 0.68140 0.55040 1.08520 -0.04350 -0.02260 -0.08050 65  ASN B C   
2825 O O   . ASN B 65  ? 0.71120 0.57960 1.10520 -0.03900 -0.01650 -0.06590 65  ASN B O   
2826 C CB  . ASN B 65  ? 0.70110 0.56850 1.15230 -0.04960 -0.02150 -0.06320 65  ASN B CB  
2827 C CG  . ASN B 65  ? 0.76110 0.62280 1.25190 -0.05410 -0.02170 -0.06070 65  ASN B CG  
2828 O OD1 . ASN B 65  ? 0.84220 0.69650 1.35530 -0.05670 -0.02440 -0.07450 65  ASN B OD1 
2829 N ND2 . ASN B 65  ? 0.79300 0.65870 1.29400 -0.05510 -0.01860 -0.04350 65  ASN B ND2 
2830 N N   . PHE B 66  ? 0.67810 0.55360 1.06070 -0.04460 -0.02840 -0.09590 66  PHE B N   
2831 C CA  . PHE B 66  ? 0.65400 0.53580 1.00100 -0.04080 -0.02790 -0.09570 66  PHE B CA  
2832 C C   . PHE B 66  ? 0.70830 0.58760 1.04690 -0.03880 -0.02820 -0.11100 66  PHE B C   
2833 O O   . PHE B 66  ? 0.68080 0.56300 1.01920 -0.04170 -0.03370 -0.12940 66  PHE B O   
2834 C CB  . PHE B 66  ? 0.61430 0.50720 0.94200 -0.04320 -0.03380 -0.09910 66  PHE B CB  
2835 C CG  . PHE B 66  ? 0.63340 0.53010 0.96440 -0.04400 -0.03270 -0.08350 66  PHE B CG  
2836 C CD1 . PHE B 66  ? 0.62790 0.52770 0.94010 -0.04010 -0.02810 -0.06890 66  PHE B CD1 
2837 C CD2 . PHE B 66  ? 0.61120 0.50900 0.96540 -0.04880 -0.03610 -0.08400 66  PHE B CD2 
2838 C CE1 . PHE B 66  ? 0.59980 0.50390 0.91540 -0.04060 -0.02640 -0.05550 66  PHE B CE1 
2839 C CE2 . PHE B 66  ? 0.65560 0.55780 1.01340 -0.04930 -0.03450 -0.06970 66  PHE B CE2 
2840 C CZ  . PHE B 66  ? 0.57300 0.47840 0.91130 -0.04510 -0.02940 -0.05580 66  PHE B CZ  
2841 N N   . LEU B 67  ? 0.63690 0.51250 0.96690 -0.03380 -0.02230 -0.10370 67  LEU B N   
2842 C CA  . LEU B 67  ? 0.68110 0.55480 1.00290 -0.03110 -0.02150 -0.11640 67  LEU B CA  
2843 C C   . LEU B 67  ? 0.68300 0.56610 0.96850 -0.02890 -0.02240 -0.11670 67  LEU B C   
2844 O O   . LEU B 67  ? 0.65670 0.54070 0.92750 -0.02530 -0.01820 -0.10260 67  LEU B O   
2845 C CB  . LEU B 67  ? 0.73160 0.59610 1.06830 -0.02700 -0.01460 -0.10680 67  LEU B CB  
2846 C CG  . LEU B 67  ? 0.81700 0.67240 1.17700 -0.02600 -0.01290 -0.11780 67  LEU B CG  
2847 C CD1 . LEU B 67  ? 0.85240 0.71070 1.19140 -0.02250 -0.01190 -0.12910 67  LEU B CD1 
2848 C CD2 . LEU B 67  ? 0.88990 0.74220 1.27530 -0.03140 -0.01790 -0.13330 67  LEU B CD2 
2849 N N   . VAL B 68  ? 0.68850 0.57900 0.96010 -0.03090 -0.02780 -0.13280 68  VAL B N   
2850 C CA  . VAL B 68  ? 0.68510 0.58530 0.92400 -0.02920 -0.02910 -0.13320 68  VAL B CA  
2851 C C   . VAL B 68  ? 0.70110 0.60240 0.93110 -0.02700 -0.02790 -0.14720 68  VAL B C   
2852 O O   . VAL B 68  ? 0.77260 0.67390 1.01340 -0.02910 -0.03060 -0.16460 68  VAL B O   
2853 C CB  . VAL B 68  ? 0.65910 0.57000 0.88690 -0.03330 -0.03630 -0.13800 68  VAL B CB  
2854 C CG1 . VAL B 68  ? 0.60020 0.52130 0.79560 -0.03150 -0.03750 -0.13650 68  VAL B CG1 
2855 C CG2 . VAL B 68  ? 0.61570 0.52550 0.85470 -0.03530 -0.03690 -0.12450 68  VAL B CG2 
2856 N N   . GLN B 69  ? 0.65010 0.55310 0.86040 -0.02270 -0.02380 -0.14030 69  GLN B N   
2857 C CA  . GLN B 69  ? 0.69640 0.60060 0.89870 -0.02000 -0.02150 -0.15140 69  GLN B CA  
2858 C C   . GLN B 69  ? 0.68030 0.59510 0.85080 -0.01850 -0.02200 -0.14930 69  GLN B C   
2859 O O   . GLN B 69  ? 0.63370 0.54910 0.79160 -0.01650 -0.01980 -0.13400 69  GLN B O   
2860 C CB  . GLN B 69  ? 0.75450 0.64850 0.97150 -0.01570 -0.01480 -0.14440 69  GLN B CB  
2861 C CG  . GLN B 69  ? 0.84540 0.72840 1.09650 -0.01690 -0.01370 -0.14450 69  GLN B CG  
2862 C CD  . GLN B 69  ? 0.97780 0.85180 1.24340 -0.01250 -0.00710 -0.13370 69  GLN B CD  
2863 O OE1 . GLN B 69  ? 1.00710 0.87650 1.28370 -0.01190 -0.00460 -0.11710 69  GLN B OE1 
2864 N NE2 . GLN B 69  ? 0.96680 0.83930 1.23310 -0.00920 -0.00410 -0.14290 69  GLN B NE2 
2865 N N   . ALA B 70  ? 0.71770 0.64160 0.87600 -0.01960 -0.02500 -0.16480 70  ALA B N   
2866 C CA  . ALA B 70  ? 0.72530 0.66010 0.85530 -0.01810 -0.02510 -0.16420 70  ALA B CA  
2867 C C   . ALA B 70  ? 0.76640 0.69950 0.89610 -0.01430 -0.01970 -0.17150 70  ALA B C   
2868 O O   . ALA B 70  ? 0.74580 0.68310 0.87770 -0.01480 -0.02050 -0.18890 70  ALA B O   
2869 C CB  . ALA B 70  ? 0.74290 0.69130 0.85900 -0.02190 -0.03180 -0.17490 70  ALA B CB  
2870 N N   . GLY B 71  ? 0.75440 0.68140 0.88320 -0.01030 -0.01420 -0.15850 71  GLY B N   
2871 C CA  . GLY B 71  ? 0.89520 0.81860 1.02930 -0.00630 -0.00870 -0.16290 71  GLY B CA  
2872 C C   . GLY B 71  ? 0.94610 0.85830 1.11070 -0.00610 -0.00720 -0.16980 71  GLY B C   
2873 O O   . GLY B 71  ? 0.94350 0.84690 1.12570 -0.00690 -0.00710 -0.15990 71  GLY B O   
2874 N N   . ASN B 72  ? 0.98970 0.90290 1.16190 -0.00550 -0.00630 -0.18770 72  ASN B N   
2875 C CA  . ASN B 72  ? 1.06850 0.97120 1.27230 -0.00590 -0.00550 -0.19640 72  ASN B CA  
2876 C C   . ASN B 72  ? 1.01800 0.92330 1.22960 -0.01130 -0.01180 -0.21040 72  ASN B C   
2877 O O   . ASN B 72  ? 1.22740 1.12310 1.46740 -0.01280 -0.01220 -0.21510 72  ASN B O   
2878 C CB  . ASN B 72  ? 1.19400 1.09460 1.40780 -0.00220 -0.00080 -0.20980 72  ASN B CB  
2879 C CG  . ASN B 72  ? 1.30120 1.20100 1.50720 0.00310  0.00510  -0.19740 72  ASN B CG  
2880 O OD1 . ASN B 72  ? 1.29410 1.20390 1.47380 0.00430  0.00580  -0.19530 72  ASN B OD1 
2881 N ND2 . ASN B 72  ? 1.35420 1.24240 1.58360 0.00620  0.00930  -0.18840 72  ASN B ND2 
2882 N N   . VAL B 73  ? 0.89750 0.81620 1.08590 -0.01420 -0.01680 -0.21690 73  VAL B N   
2883 C CA  . VAL B 73  ? 0.89520 0.81830 1.09060 -0.01950 -0.02340 -0.23080 73  VAL B CA  
2884 C C   . VAL B 73  ? 0.83690 0.75260 1.04710 -0.02250 -0.02620 -0.21770 73  VAL B C   
2885 O O   . VAL B 73  ? 0.78930 0.70730 0.98610 -0.02260 -0.02700 -0.20090 73  VAL B O   
2886 C CB  . VAL B 73  ? 0.83000 0.77110 0.99660 -0.02180 -0.02830 -0.23900 73  VAL B CB  
2887 C CG1 . VAL B 73  ? 0.86060 0.80750 1.03360 -0.02760 -0.03610 -0.25060 73  VAL B CG1 
2888 C CG2 . VAL B 73  ? 0.85900 0.80800 1.01560 -0.01940 -0.02530 -0.25490 73  VAL B CG2 
2889 N N   . GLN B 74  ? 0.83600 0.74300 1.07550 -0.02490 -0.02750 -0.22550 74  GLN B N   
2890 C CA  . GLN B 74  ? 0.85330 0.75440 1.10880 -0.02810 -0.03000 -0.21390 74  GLN B CA  
2891 C C   . GLN B 74  ? 0.86230 0.77510 1.10780 -0.03340 -0.03810 -0.22180 74  GLN B C   
2892 O O   . GLN B 74  ? 0.87850 0.79900 1.12210 -0.03590 -0.04220 -0.24190 74  GLN B O   
2893 C CB  . GLN B 74  ? 0.87400 0.76120 1.16720 -0.02870 -0.02800 -0.21780 74  GLN B CB  
2894 C CG  . GLN B 74  ? 0.94510 0.82900 1.25880 -0.03370 -0.03230 -0.21410 74  GLN B CG  
2895 C CD  . GLN B 74  ? 1.03710 0.90800 1.37540 -0.03230 -0.02760 -0.19530 74  GLN B CD  
2896 O OE1 . GLN B 74  ? 1.05910 0.92690 1.38980 -0.02770 -0.02200 -0.17920 74  GLN B OE1 
2897 N NE2 . GLN B 74  ? 1.02740 0.89190 1.39560 -0.03640 -0.02990 -0.19690 74  GLN B NE2 
2898 N N   . LEU B 75  ? 0.83120 0.74680 1.06870 -0.03490 -0.04050 -0.20600 75  LEU B N   
2899 C CA  . LEU B 75  ? 0.80850 0.73500 1.03860 -0.03980 -0.04840 -0.21020 75  LEU B CA  
2900 C C   . LEU B 75  ? 0.82780 0.74690 1.08690 -0.04370 -0.05080 -0.20720 75  LEU B C   
2901 O O   . LEU B 75  ? 0.83410 0.74400 1.10520 -0.04220 -0.04670 -0.19020 75  LEU B O   
2902 C CB  . LEU B 75  ? 0.76140 0.69680 0.96440 -0.03880 -0.04950 -0.19480 75  LEU B CB  
2903 C CG  . LEU B 75  ? 0.74040 0.68520 0.91370 -0.03560 -0.04790 -0.19630 75  LEU B CG  
2904 C CD1 . LEU B 75  ? 0.68990 0.64290 0.84010 -0.03510 -0.04960 -0.18130 75  LEU B CD1 
2905 C CD2 . LEU B 75  ? 0.79450 0.75070 0.96050 -0.03790 -0.05220 -0.21840 75  LEU B CD2 
2906 N N   . ARG B 76  ? 0.81100 0.73520 1.08150 -0.04880 -0.05750 -0.22340 76  ARG B N   
2907 C CA  . ARG B 76  ? 0.80570 0.72300 1.10640 -0.05300 -0.05990 -0.22160 76  ARG B CA  
2908 C C   . ARG B 76  ? 0.74420 0.66920 1.03660 -0.05550 -0.06430 -0.20850 76  ARG B C   
2909 O O   . ARG B 76  ? 0.74520 0.68440 1.01700 -0.05740 -0.07040 -0.21340 76  ARG B O   
2910 C CB  . ARG B 76  ? 0.85350 0.77180 1.17490 -0.05780 -0.06530 -0.24520 76  ARG B CB  
2911 C CG  . ARG B 76  ? 1.00810 0.93530 1.31460 -0.05750 -0.06710 -0.26780 76  ARG B CG  
2912 C CD  . ARG B 76  ? 1.05110 0.96870 1.36130 -0.05220 -0.05920 -0.27260 76  ARG B CD  
2913 N NE  . ARG B 76  ? 1.18870 1.11500 1.46530 -0.04780 -0.05620 -0.26900 76  ARG B NE  
2914 C CZ  . ARG B 76  ? 1.16290 1.10170 1.42010 -0.04760 -0.05810 -0.28600 76  ARG B CZ  
2915 N NH1 . ARG B 76  ? 1.15450 1.09940 1.42100 -0.05150 -0.06300 -0.30970 76  ARG B NH1 
2916 N NH2 . ARG B 76  ? 1.03950 0.98590 1.26730 -0.04350 -0.05490 -0.27920 76  ARG B NH2 
2917 N N   . VAL B 77  ? 0.74060 0.65720 1.04940 -0.05520 -0.06100 -0.19120 77  VAL B N   
2918 C CA  . VAL B 77  ? 0.70210 0.62510 1.00790 -0.05740 -0.06430 -0.17860 77  VAL B CA  
2919 C C   . VAL B 77  ? 0.69580 0.62220 1.02360 -0.06380 -0.07170 -0.18940 77  VAL B C   
2920 O O   . VAL B 77  ? 0.67140 0.58840 1.02940 -0.06620 -0.07090 -0.19540 77  VAL B O   
2921 C CB  . VAL B 77  ? 0.66390 0.57820 0.97770 -0.05440 -0.05720 -0.15630 77  VAL B CB  
2922 C CG1 . VAL B 77  ? 0.61520 0.53650 0.92770 -0.05650 -0.06030 -0.14450 77  VAL B CG1 
2923 C CG2 . VAL B 77  ? 0.64810 0.56050 0.93850 -0.04830 -0.05070 -0.14680 77  VAL B CG2 
2924 N N   . ILE B 78  ? 0.68300 0.62350 0.99720 -0.06690 -0.07910 -0.19200 78  ILE B N   
2925 C CA  . ILE B 78  ? 0.68020 0.62680 1.01300 -0.07330 -0.08730 -0.20290 78  ILE B CA  
2926 C C   . ILE B 78  ? 0.67200 0.62470 1.00760 -0.07530 -0.09040 -0.18830 78  ILE B C   
2927 O O   . ILE B 78  ? 0.61970 0.58080 0.96590 -0.08060 -0.09820 -0.19590 78  ILE B O   
2928 C CB  . ILE B 78  ? 0.67850 0.63910 0.99630 -0.07630 -0.09550 -0.22410 78  ILE B CB  
2929 C CG1 . ILE B 78  ? 0.71790 0.69330 1.00100 -0.07420 -0.09830 -0.21720 78  ILE B CG1 
2930 C CG2 . ILE B 78  ? 0.67760 0.63240 0.99680 -0.07470 -0.09240 -0.24140 78  ILE B CG2 
2931 C CD1 . ILE B 78  ? 0.71990 0.71330 0.98850 -0.07800 -0.10770 -0.23510 78  ILE B CD1 
2932 N N   . GLY B 79  ? 0.69700 0.64650 1.02330 -0.07110 -0.08430 -0.16800 79  GLY B N   
2933 C CA  . GLY B 79  ? 0.61410 0.56950 0.94340 -0.07230 -0.08630 -0.15410 79  GLY B CA  
2934 C C   . GLY B 79  ? 0.62440 0.57530 0.94010 -0.06650 -0.07810 -0.13460 79  GLY B C   
2935 O O   . GLY B 79  ? 0.60010 0.54830 0.89560 -0.06210 -0.07380 -0.13360 79  GLY B O   
2936 N N   . HIS B 80  ? 0.59930 0.54930 0.92660 -0.06640 -0.07540 -0.11940 80  HIS B N   
2937 C CA  . HIS B 80  ? 0.59070 0.53730 0.90590 -0.06120 -0.06750 -0.10180 80  HIS B CA  
2938 C C   . HIS B 80  ? 0.61390 0.56760 0.93320 -0.06180 -0.06840 -0.08960 80  HIS B C   
2939 O O   . HIS B 80  ? 0.57340 0.53000 0.91480 -0.06610 -0.07220 -0.09060 80  HIS B O   
2940 C CB  . HIS B 80  ? 0.58680 0.52040 0.91750 -0.05890 -0.05880 -0.09420 80  HIS B CB  
2941 C CG  . HIS B 80  ? 0.62130 0.55070 0.98580 -0.06280 -0.05820 -0.09080 80  HIS B CG  
2942 N ND1 . HIS B 80  ? 0.62880 0.55210 1.01690 -0.06650 -0.06050 -0.10290 80  HIS B ND1 
2943 C CD2 . HIS B 80  ? 0.63120 0.56220 1.01090 -0.06350 -0.05540 -0.07690 80  HIS B CD2 
2944 C CE1 . HIS B 80  ? 0.67990 0.60060 1.09710 -0.06960 -0.05940 -0.09570 80  HIS B CE1 
2945 N NE2 . HIS B 80  ? 0.64200 0.56780 1.05420 -0.06780 -0.05600 -0.07960 80  HIS B NE2 
2946 N N   . SER B 81  ? 0.54760 0.50420 0.84670 -0.05750 -0.06500 -0.07840 81  SER B N   
2947 C CA  . SER B 81  ? 0.54170 0.50390 0.84550 -0.05700 -0.06400 -0.06580 81  SER B CA  
2948 C C   . SER B 81  ? 0.56560 0.52580 0.85110 -0.05130 -0.05650 -0.05330 81  SER B C   
2949 O O   . SER B 81  ? 0.54210 0.49870 0.80810 -0.04810 -0.05400 -0.05530 81  SER B O   
2950 C CB  . SER B 81  ? 0.59030 0.56540 0.89000 -0.05980 -0.07320 -0.07010 81  SER B CB  
2951 O OG  . SER B 81  ? 0.62460 0.60510 0.89710 -0.05740 -0.07600 -0.07310 81  SER B OG  
2952 N N   . MET B 82  ? 0.51110 0.47430 0.80340 -0.05010 -0.05300 -0.04110 82  MET B N   
2953 C CA  . MET B 82  ? 0.54100 0.50310 0.81910 -0.04490 -0.04560 -0.02950 82  MET B CA  
2954 C C   . MET B 82  ? 0.54400 0.51520 0.81250 -0.04370 -0.04870 -0.02550 82  MET B C   
2955 O O   . MET B 82  ? 0.54220 0.52010 0.82520 -0.04640 -0.05270 -0.02450 82  MET B O   
2956 C CB  . MET B 82  ? 0.53900 0.49730 0.83400 -0.04400 -0.03740 -0.01810 82  MET B CB  
2957 C CG  . MET B 82  ? 0.49920 0.45780 0.78040 -0.03900 -0.02980 -0.00730 82  MET B CG  
2958 S SD  . MET B 82  ? 0.54860 0.50430 0.84710 -0.03790 -0.01990 0.00570  82  MET B SD  
2959 C CE  . MET B 82  ? 0.52580 0.48770 0.85500 -0.04230 -0.02160 0.00980  82  MET B CE  
2960 N N   . GLN B 83  ? 0.49250 0.46430 0.73810 -0.04000 -0.04750 -0.02390 83  GLN B N   
2961 C CA  . GLN B 83  ? 0.53200 0.51100 0.76890 -0.03780 -0.04870 -0.01810 83  GLN B CA  
2962 C C   . GLN B 83  ? 0.48210 0.45740 0.70890 -0.03280 -0.03990 -0.00890 83  GLN B C   
2963 O O   . GLN B 83  ? 0.49120 0.46240 0.69980 -0.03030 -0.03770 -0.01030 83  GLN B O   
2964 C CB  . GLN B 83  ? 0.59450 0.57890 0.81380 -0.03820 -0.05630 -0.02470 83  GLN B CB  
2965 C CG  . GLN B 83  ? 0.56900 0.56090 0.78100 -0.03590 -0.05820 -0.01800 83  GLN B CG  
2966 C CD  . GLN B 83  ? 0.67480 0.67300 0.86860 -0.03600 -0.06520 -0.02220 83  GLN B CD  
2967 O OE1 . GLN B 83  ? 0.65020 0.64660 0.83140 -0.03680 -0.06700 -0.02990 83  GLN B OE1 
2968 N NE2 . GLN B 83  ? 0.65590 0.66180 0.84870 -0.03480 -0.06850 -0.01610 83  GLN B NE2 
2969 N N   . ASN B 84  ? 0.42840 0.40620 0.66650 -0.03140 -0.03470 0.00000  84  ASN B N   
2970 C CA  . ASN B 84  ? 0.49350 0.46930 0.72280 -0.02680 -0.02610 0.00780  84  ASN B CA  
2971 C C   . ASN B 84  ? 0.50600 0.47410 0.72990 -0.02590 -0.02100 0.00750  84  ASN B C   
2972 O O   . ASN B 84  ? 0.47060 0.43580 0.70940 -0.02860 -0.02060 0.00670  84  ASN B O   
2973 C CB  . ASN B 84  ? 0.43990 0.41820 0.65210 -0.02370 -0.02740 0.00830  84  ASN B CB  
2974 C CG  . ASN B 84  ? 0.56650 0.55250 0.78630 -0.02480 -0.03350 0.00870  84  ASN B CG  
2975 O OD1 . ASN B 84  ? 0.55590 0.54640 0.79270 -0.02540 -0.03210 0.01310  84  ASN B OD1 
2976 N ND2 . ASN B 84  ? 0.49060 0.47950 0.69970 -0.02570 -0.04090 0.00430  84  ASN B ND2 
2977 N N   . CYS B 85  ? 0.42610 0.39070 0.63040 -0.02280 -0.01820 0.00730  85  CYS B N   
2978 C CA  . CYS B 85  ? 0.45400 0.41250 0.65470 -0.02160 -0.01290 0.00860  85  CYS B CA  
2979 C C   . CYS B 85  ? 0.44830 0.40170 0.64180 -0.02300 -0.01720 -0.00030 85  CYS B C   
2980 O O   . CYS B 85  ? 0.44880 0.39700 0.63720 -0.02160 -0.01350 0.00020  85  CYS B O   
2981 C CB  . CYS B 85  ? 0.48840 0.44720 0.67430 -0.01730 -0.00640 0.01420  85  CYS B CB  
2982 S SG  . CYS B 85  ? 0.43210 0.39820 0.62760 -0.01520 0.00050  0.02390  85  CYS B SG  
2983 N N   . VAL B 86  ? 0.45030 0.40590 0.64380 -0.02580 -0.02500 -0.00840 86  VAL B N   
2984 C CA  . VAL B 86  ? 0.46520 0.41720 0.65300 -0.02730 -0.02880 -0.01810 86  VAL B CA  
2985 C C   . VAL B 86  ? 0.50460 0.45660 0.71100 -0.03180 -0.03370 -0.02520 86  VAL B C   
2986 O O   . VAL B 86  ? 0.48420 0.44100 0.70460 -0.03440 -0.03710 -0.02440 86  VAL B O   
2987 C CB  . VAL B 86  ? 0.50500 0.46050 0.67240 -0.02670 -0.03360 -0.02360 86  VAL B CB  
2988 C CG1 . VAL B 86  ? 0.48190 0.43600 0.63150 -0.02250 -0.02860 -0.01780 86  VAL B CG1 
2989 C CG2 . VAL B 86  ? 0.50520 0.46890 0.67550 -0.02880 -0.04040 -0.02490 86  VAL B CG2 
2990 N N   . LEU B 87  ? 0.44150 0.38780 0.65000 -0.03260 -0.03380 -0.03230 87  LEU B N   
2991 C CA  . LEU B 87  ? 0.46890 0.41440 0.69330 -0.03690 -0.03890 -0.04230 87  LEU B CA  
2992 C C   . LEU B 87  ? 0.53050 0.48060 0.74000 -0.03820 -0.04590 -0.05440 87  LEU B C   
2993 O O   . LEU B 87  ? 0.50580 0.45570 0.69540 -0.03550 -0.04460 -0.05560 87  LEU B O   
2994 C CB  . LEU B 87  ? 0.49210 0.42840 0.72920 -0.03660 -0.03430 -0.04300 87  LEU B CB  
2995 C CG  . LEU B 87  ? 0.60560 0.53760 0.87020 -0.03880 -0.03170 -0.03870 87  LEU B CG  
2996 C CD1 . LEU B 87  ? 0.56720 0.50490 0.84120 -0.03930 -0.02990 -0.02710 87  LEU B CD1 
2997 C CD2 . LEU B 87  ? 0.51880 0.44270 0.78600 -0.03590 -0.02490 -0.03390 87  LEU B CD2 
2998 N N   . LYS B 88  ? 0.50680 0.46220 0.72650 -0.04250 -0.05320 -0.06330 88  LYS B N   
2999 C CA  . LYS B 88  ? 0.53080 0.49280 0.73960 -0.04470 -0.06050 -0.07640 88  LYS B CA  
3000 C C   . LYS B 88  ? 0.59050 0.54810 0.81610 -0.04810 -0.06250 -0.08920 88  LYS B C   
3001 O O   . LYS B 88  ? 0.55480 0.51260 0.80250 -0.05190 -0.06540 -0.09150 88  LYS B O   
3002 C CB  . LYS B 88  ? 0.53920 0.51320 0.74640 -0.04730 -0.06820 -0.07650 88  LYS B CB  
3003 C CG  . LYS B 88  ? 0.58200 0.55980 0.77550 -0.04380 -0.06610 -0.06390 88  LYS B CG  
3004 C CD  . LYS B 88  ? 0.61820 0.60890 0.80450 -0.04530 -0.07410 -0.06380 88  LYS B CD  
3005 C CE  . LYS B 88  ? 0.77530 0.77120 0.97860 -0.04700 -0.07670 -0.05730 88  LYS B CE  
3006 N NZ  . LYS B 88  ? 0.80330 0.81200 0.99540 -0.04740 -0.08410 -0.05610 88  LYS B NZ  
3007 N N   . LEU B 89  ? 0.55540 0.50880 0.77230 -0.04670 -0.06070 -0.09780 89  LEU B N   
3008 C CA  . LEU B 89  ? 0.56650 0.51460 0.80020 -0.04930 -0.06190 -0.11110 89  LEU B CA  
3009 C C   . LEU B 89  ? 0.61070 0.56850 0.83220 -0.05170 -0.06910 -0.12750 89  LEU B C   
3010 O O   . LEU B 89  ? 0.61280 0.57390 0.81230 -0.04910 -0.06830 -0.13070 89  LEU B O   
3011 C CB  . LEU B 89  ? 0.55000 0.48690 0.78600 -0.04580 -0.05430 -0.10960 89  LEU B CB  
3012 C CG  . LEU B 89  ? 0.54590 0.47540 0.78940 -0.04280 -0.04670 -0.09270 89  LEU B CG  
3013 C CD1 . LEU B 89  ? 0.52670 0.44690 0.77090 -0.03930 -0.04030 -0.09220 89  LEU B CD1 
3014 C CD2 . LEU B 89  ? 0.53840 0.46580 0.80970 -0.04630 -0.04740 -0.08840 89  LEU B CD2 
3015 N N   . LYS B 90  ? 0.56710 0.53080 0.80220 -0.05680 -0.07630 -0.13730 90  LYS B N   
3016 C CA  . LYS B 90  ? 0.63590 0.61040 0.86130 -0.05970 -0.08360 -0.15450 90  LYS B CA  
3017 C C   . LYS B 90  ? 0.64530 0.61240 0.87710 -0.05940 -0.08090 -0.16920 90  LYS B C   
3018 O O   . LYS B 90  ? 0.65050 0.60570 0.90650 -0.06000 -0.07730 -0.17020 90  LYS B O   
3019 C CB  . LYS B 90  ? 0.66650 0.64970 0.90720 -0.06540 -0.09230 -0.16080 90  LYS B CB  
3020 C CG  . LYS B 90  ? 0.73100 0.72830 0.96180 -0.06900 -0.10090 -0.17820 90  LYS B CG  
3021 C CD  . LYS B 90  ? 0.78400 0.79580 0.98610 -0.06740 -0.10450 -0.17260 90  LYS B CD  
3022 C CE  . LYS B 90  ? 0.85730 0.88100 1.06420 -0.07070 -0.11230 -0.16670 90  LYS B CE  
3023 N NZ  . LYS B 90  ? 0.84830 0.88830 1.02980 -0.06980 -0.11730 -0.16220 90  LYS B NZ  
3024 N N   . VAL B 91  ? 0.68280 0.65650 0.89340 -0.05790 -0.08160 -0.17910 91  VAL B N   
3025 C CA  . VAL B 91  ? 0.67640 0.64450 0.89130 -0.05700 -0.07870 -0.19400 91  VAL B CA  
3026 C C   . VAL B 91  ? 0.73370 0.71580 0.94150 -0.06090 -0.08640 -0.21470 91  VAL B C   
3027 O O   . VAL B 91  ? 0.71760 0.71460 0.91290 -0.06350 -0.09360 -0.21500 91  VAL B O   
3028 C CB  . VAL B 91  ? 0.69520 0.65860 0.89170 -0.05120 -0.07110 -0.18750 91  VAL B CB  
3029 C CG1 . VAL B 91  ? 0.64590 0.59540 0.85270 -0.04770 -0.06340 -0.16940 91  VAL B CG1 
3030 C CG2 . VAL B 91  ? 0.65400 0.63080 0.82000 -0.04970 -0.07330 -0.18210 91  VAL B CG2 
3031 N N   . ASP B 92  ? 0.77070 0.74860 0.98920 -0.06140 -0.08520 -0.23250 92  ASP B N   
3032 C CA  . ASP B 92  ? 0.79670 0.78830 1.01080 -0.06540 -0.09240 -0.25470 92  ASP B CA  
3033 C C   . ASP B 92  ? 0.83010 0.83640 1.01160 -0.06320 -0.09280 -0.25980 92  ASP B C   
3034 O O   . ASP B 92  ? 0.84490 0.86700 1.01730 -0.06650 -0.09940 -0.27620 92  ASP B O   
3035 C CB  . ASP B 92  ? 0.88470 0.86680 1.12430 -0.06700 -0.09100 -0.27370 92  ASP B CB  
3036 C CG  . ASP B 92  ? 0.97970 0.95140 1.21740 -0.06170 -0.08210 -0.27530 92  ASP B CG  
3037 O OD1 . ASP B 92  ? 0.96080 0.92820 1.18380 -0.05680 -0.07610 -0.25810 92  ASP B OD1 
3038 O OD2 . ASP B 92  ? 1.06070 1.02860 1.31290 -0.06240 -0.08130 -0.29440 92  ASP B OD2 
3039 N N   . THR B 93  ? 0.77920 0.78120 0.94410 -0.05780 -0.08580 -0.24680 93  THR B N   
3040 C CA  . THR B 93  ? 0.78130 0.79580 0.91700 -0.05520 -0.08470 -0.24960 93  THR B CA  
3041 C C   . THR B 93  ? 0.68710 0.70780 0.80180 -0.05330 -0.08500 -0.22900 93  THR B C   
3042 O O   . THR B 93  ? 0.66250 0.67110 0.78090 -0.05030 -0.07980 -0.21170 93  THR B O   
3043 C CB  . THR B 93  ? 0.78490 0.78880 0.92130 -0.05040 -0.07580 -0.25340 93  THR B CB  
3044 O OG1 . THR B 93  ? 0.86850 0.86300 1.03070 -0.05190 -0.07480 -0.27020 93  THR B OG1 
3045 C CG2 . THR B 93  ? 0.78090 0.79910 0.88960 -0.04830 -0.07460 -0.25980 93  THR B CG2 
3046 N N   . ALA B 94  ? 0.69110 0.73090 0.78390 -0.05490 -0.09080 -0.23090 94  ALA B N   
3047 C CA  . ALA B 94  ? 0.65880 0.70470 0.73130 -0.05250 -0.09040 -0.21210 94  ALA B CA  
3048 C C   . ALA B 94  ? 0.66290 0.70650 0.71870 -0.04770 -0.08270 -0.20860 94  ALA B C   
3049 O O   . ALA B 94  ? 0.71290 0.76230 0.76180 -0.04720 -0.08110 -0.22320 94  ALA B O   
3050 C CB  . ALA B 94  ? 0.65860 0.72690 0.71500 -0.05590 -0.09940 -0.21360 94  ALA B CB  
3051 N N   . ASN B 95  ? 0.63790 0.67310 0.68870 -0.04410 -0.07780 -0.18990 95  ASN B N   
3052 C CA  . ASN B 95  ? 0.65010 0.68360 0.68550 -0.03980 -0.07090 -0.18450 95  ASN B CA  
3053 C C   . ASN B 95  ? 0.68060 0.73410 0.69130 -0.04030 -0.07380 -0.18800 95  ASN B C   
3054 O O   . ASN B 95  ? 0.67490 0.73870 0.67350 -0.04110 -0.07790 -0.17640 95  ASN B O   
3055 C CB  . ASN B 95  ? 0.62880 0.65240 0.66270 -0.03670 -0.06670 -0.16360 95  ASN B CB  
3056 C CG  . ASN B 95  ? 0.68090 0.70110 0.70170 -0.03240 -0.05940 -0.15780 95  ASN B CG  
3057 O OD1 . ASN B 95  ? 0.68110 0.70830 0.69180 -0.03150 -0.05760 -0.16800 95  ASN B OD1 
3058 N ND2 . ASN B 95  ? 0.61010 0.62110 0.63090 -0.02980 -0.05550 -0.14150 95  ASN B ND2 
3059 N N   . PRO B 96  ? 0.70640 0.76630 0.70940 -0.03940 -0.07130 -0.20240 96  PRO B N   
3060 C CA  . PRO B 96  ? 0.73580 0.81710 0.71440 -0.04000 -0.07380 -0.20500 96  PRO B CA  
3061 C C   . PRO B 96  ? 0.74380 0.82730 0.70550 -0.03690 -0.07020 -0.18620 96  PRO B C   
3062 O O   . PRO B 96  ? 0.75970 0.86140 0.70190 -0.03760 -0.07290 -0.18310 96  PRO B O   
3063 C CB  . PRO B 96  ? 0.69920 0.78360 0.67700 -0.03900 -0.06990 -0.22490 96  PRO B CB  
3064 C CG  . PRO B 96  ? 0.72460 0.78610 0.72180 -0.03580 -0.06250 -0.22430 96  PRO B CG  
3065 C CD  . PRO B 96  ? 0.71780 0.76610 0.73410 -0.03750 -0.06540 -0.21570 96  PRO B CD  
3066 N N   . LYS B 97  ? 0.70080 0.76690 0.66990 -0.03370 -0.06420 -0.17370 97  LYS B N   
3067 C CA  . LYS B 97  ? 0.73760 0.80330 0.69400 -0.03100 -0.06070 -0.15630 97  LYS B CA  
3068 C C   . LYS B 97  ? 0.67650 0.73770 0.63690 -0.03160 -0.06380 -0.13960 97  LYS B C   
3069 O O   . LYS B 97  ? 0.68480 0.73950 0.64160 -0.02900 -0.05980 -0.12540 97  LYS B O   
3070 C CB  . LYS B 97  ? 0.74200 0.79280 0.70310 -0.02690 -0.05190 -0.15360 97  LYS B CB  
3071 C CG  . LYS B 97  ? 0.79330 0.84490 0.75560 -0.02550 -0.04770 -0.17010 97  LYS B CG  
3072 C CD  . LYS B 97  ? 0.86130 0.89400 0.83710 -0.02190 -0.04030 -0.16710 97  LYS B CD  
3073 C CE  . LYS B 97  ? 0.94480 0.98070 0.90880 -0.01850 -0.03410 -0.16540 97  LYS B CE  
3074 N NZ  . LYS B 97  ? 1.04740 1.09980 1.00070 -0.01960 -0.03520 -0.18100 97  LYS B NZ  
3075 N N   . THR B 98  ? 0.65070 0.71470 0.62030 -0.03480 -0.07040 -0.14140 98  THR B N   
3076 C CA  . THR B 98  ? 0.68470 0.74560 0.65860 -0.03500 -0.07300 -0.12570 98  THR B CA  
3077 C C   . THR B 98  ? 0.64950 0.72340 0.60580 -0.03450 -0.07490 -0.11320 98  THR B C   
3078 O O   . THR B 98  ? 0.67470 0.76720 0.61900 -0.03670 -0.08020 -0.11720 98  THR B O   
3079 C CB  . THR B 98  ? 0.64030 0.70510 0.62670 -0.03880 -0.08050 -0.12980 98  THR B CB  
3080 O OG1 . THR B 98  ? 0.63410 0.68750 0.63860 -0.03970 -0.07910 -0.14160 98  THR B OG1 
3081 C CG2 . THR B 98  ? 0.64010 0.69940 0.63360 -0.03830 -0.08170 -0.11360 98  THR B CG2 
3082 N N   . PRO B 99  ? 0.65150 0.71740 0.60670 -0.03190 -0.07110 -0.09790 99  PRO B N   
3083 C CA  . PRO B 99  ? 0.64120 0.71840 0.58350 -0.03160 -0.07320 -0.08450 99  PRO B CA  
3084 C C   . PRO B 99  ? 0.66590 0.74960 0.61370 -0.03360 -0.08040 -0.07620 99  PRO B C   
3085 O O   . PRO B 99  ? 0.67480 0.75170 0.63770 -0.03480 -0.08270 -0.07860 99  PRO B O   
3086 C CB  . PRO B 99  ? 0.63110 0.69430 0.57460 -0.02820 -0.06610 -0.07320 99  PRO B CB  
3087 C CG  . PRO B 99  ? 0.64220 0.68790 0.60260 -0.02730 -0.06310 -0.07560 99  PRO B CG  
3088 C CD  . PRO B 99  ? 0.63660 0.68310 0.60270 -0.02910 -0.06440 -0.09230 99  PRO B CD  
3089 N N   . LYS B 100 ? 0.64520 0.74240 0.58230 -0.03390 -0.08370 -0.06520 100 LYS B N   
3090 C CA  . LYS B 100 ? 0.69770 0.79810 0.64250 -0.03460 -0.08910 -0.05310 100 LYS B CA  
3091 C C   . LYS B 100 ? 0.64570 0.72700 0.60360 -0.03190 -0.08400 -0.04420 100 LYS B C   
3092 O O   . LYS B 100 ? 0.66400 0.73580 0.61850 -0.02930 -0.07740 -0.03970 100 LYS B O   
3093 C CB  . LYS B 100 ? 0.79410 0.91120 0.72730 -0.03490 -0.09300 -0.04030 100 LYS B CB  
3094 C CG  . LYS B 100 ? 0.96870 1.10720 0.88550 -0.03720 -0.09700 -0.04740 100 LYS B CG  
3095 C CD  . LYS B 100 ? 1.16010 1.31500 1.06630 -0.03720 -0.10000 -0.03180 100 LYS B CD  
3096 C CE  . LYS B 100 ? 1.30070 1.47870 1.18830 -0.03930 -0.10280 -0.03860 100 LYS B CE  
3097 N NZ  . LYS B 100 ? 1.34040 1.53970 1.22030 -0.04050 -0.10920 -0.02370 100 LYS B NZ  
3098 N N   . TYR B 101 ? 0.60560 0.68160 0.57880 -0.03270 -0.08670 -0.04270 101 TYR B N   
3099 C CA  . TYR B 101 ? 0.57720 0.63610 0.56240 -0.03000 -0.08110 -0.03590 101 TYR B CA  
3100 C C   . TYR B 101 ? 0.60570 0.66500 0.60500 -0.03040 -0.08520 -0.02780 101 TYR B C   
3101 O O   . TYR B 101 ? 0.59810 0.66960 0.60040 -0.03300 -0.09270 -0.02890 101 TYR B O   
3102 C CB  . TYR B 101 ? 0.57910 0.62420 0.57180 -0.02960 -0.07590 -0.04640 101 TYR B CB  
3103 C CG  . TYR B 101 ? 0.55720 0.60240 0.56390 -0.03220 -0.08000 -0.05440 101 TYR B CG  
3104 C CD1 . TYR B 101 ? 0.58970 0.62730 0.61290 -0.03190 -0.07980 -0.04860 101 TYR B CD1 
3105 C CD2 . TYR B 101 ? 0.57610 0.62960 0.58070 -0.03520 -0.08410 -0.06820 101 TYR B CD2 
3106 C CE1 . TYR B 101 ? 0.53940 0.57770 0.57670 -0.03460 -0.08370 -0.05520 101 TYR B CE1 
3107 C CE2 . TYR B 101 ? 0.58750 0.64070 0.60680 -0.03800 -0.08820 -0.07610 101 TYR B CE2 
3108 C CZ  . TYR B 101 ? 0.59910 0.64480 0.63480 -0.03780 -0.08800 -0.06880 101 TYR B CZ  
3109 O OH  . TYR B 101 ? 0.62040 0.66640 0.67220 -0.04080 -0.09190 -0.07560 101 TYR B OH  
3110 N N   . LYS B 102 ? 0.57640 0.62290 0.58470 -0.02770 -0.08010 -0.01990 102 LYS B N   
3111 C CA  . LYS B 102 ? 0.62860 0.67250 0.65350 -0.02760 -0.08200 -0.01460 102 LYS B CA  
3112 C C   . LYS B 102 ? 0.58040 0.60790 0.61440 -0.02510 -0.07420 -0.01370 102 LYS B C   
3113 O O   . LYS B 102 ? 0.52550 0.54470 0.55230 -0.02320 -0.06800 -0.01450 102 LYS B O   
3114 C CB  . LYS B 102 ? 0.66850 0.72060 0.69510 -0.02680 -0.08600 -0.00150 102 LYS B CB  
3115 C CG  . LYS B 102 ? 0.67680 0.72280 0.69860 -0.02380 -0.08090 0.00740  102 LYS B CG  
3116 C CD  . LYS B 102 ? 0.76720 0.82040 0.79420 -0.02280 -0.08480 0.02100  102 LYS B CD  
3117 C CE  . LYS B 102 ? 0.96520 1.03730 0.98420 -0.02540 -0.09320 0.02350  102 LYS B CE  
3118 N NZ  . LYS B 102 ? 1.03620 1.11550 1.05660 -0.02410 -0.09580 0.03850  102 LYS B NZ  
3119 N N   . PHE B 103 ? 0.52720 0.55130 0.57720 -0.02540 -0.07470 -0.01270 103 PHE B N   
3120 C CA  . PHE B 103 ? 0.54300 0.55460 0.60350 -0.02300 -0.06770 -0.01010 103 PHE B CA  
3121 C C   . PHE B 103 ? 0.56670 0.57840 0.63300 -0.02060 -0.06710 0.00100  103 PHE B C   
3122 O O   . PHE B 103 ? 0.54700 0.56770 0.61970 -0.02150 -0.07300 0.00570  103 PHE B O   
3123 C CB  . PHE B 103 ? 0.49260 0.50160 0.56890 -0.02480 -0.06820 -0.01510 103 PHE B CB  
3124 C CG  . PHE B 103 ? 0.52990 0.53690 0.60410 -0.02710 -0.06820 -0.02670 103 PHE B CG  
3125 C CD1 . PHE B 103 ? 0.50830 0.51380 0.56740 -0.02650 -0.06590 -0.03140 103 PHE B CD1 
3126 C CD2 . PHE B 103 ? 0.52970 0.53620 0.61830 -0.02970 -0.07020 -0.03270 103 PHE B CD2 
3127 C CE1 . PHE B 103 ? 0.53560 0.53850 0.59440 -0.02800 -0.06530 -0.04230 103 PHE B CE1 
3128 C CE2 . PHE B 103 ? 0.52740 0.53100 0.61650 -0.03170 -0.06990 -0.04380 103 PHE B CE2 
3129 C CZ  . PHE B 103 ? 0.57340 0.57510 0.64780 -0.03060 -0.06740 -0.04880 103 PHE B CZ  
3130 N N   . VAL B 104 ? 0.50280 0.50560 0.56680 -0.01760 -0.06040 0.00500  104 VAL B N   
3131 C CA  . VAL B 104 ? 0.46380 0.46580 0.53490 -0.01510 -0.05910 0.01410  104 VAL B CA  
3132 C C   . VAL B 104 ? 0.53140 0.52270 0.60890 -0.01260 -0.05110 0.01410  104 VAL B C   
3133 O O   . VAL B 104 ? 0.53270 0.51740 0.60460 -0.01230 -0.04630 0.00910  104 VAL B O   
3134 C CB  . VAL B 104 ? 0.54440 0.54910 0.60560 -0.01410 -0.06000 0.02020  104 VAL B CB  
3135 C CG1 . VAL B 104 ? 0.56380 0.58140 0.61650 -0.01680 -0.06780 0.02030  104 VAL B CG1 
3136 C CG2 . VAL B 104 ? 0.55660 0.55300 0.60690 -0.01270 -0.05370 0.01780  104 VAL B CG2 
3137 N N   . ARG B 105 ? 0.44120 0.43200 0.53100 -0.01060 -0.04970 0.01970  105 ARG B N   
3138 C CA  . ARG B 105 ? 0.47960 0.46240 0.57490 -0.00790 -0.04190 0.02010  105 ARG B CA  
3139 C C   . ARG B 105 ? 0.53780 0.51750 0.62970 -0.00530 -0.03930 0.02450  105 ARG B C   
3140 O O   . ARG B 105 ? 0.51330 0.49700 0.61160 -0.00450 -0.04270 0.03040  105 ARG B O   
3141 C CB  . ARG B 105 ? 0.50070 0.48540 0.61370 -0.00720 -0.04120 0.02200  105 ARG B CB  
3142 C CG  . ARG B 105 ? 0.47190 0.45010 0.58900 -0.00450 -0.03250 0.02160  105 ARG B CG  
3143 C CD  . ARG B 105 ? 0.51350 0.49450 0.64710 -0.00440 -0.03110 0.02260  105 ARG B CD  
3144 N NE  . ARG B 105 ? 0.46790 0.44480 0.60420 -0.00170 -0.02250 0.02230  105 ARG B NE  
3145 C CZ  . ARG B 105 ? 0.48030 0.45440 0.61430 -0.00220 -0.01770 0.01970  105 ARG B CZ  
3146 N NH1 . ARG B 105 ? 0.43970 0.41330 0.57030 -0.00510 -0.02040 0.01680  105 ARG B NH1 
3147 N NH2 . ARG B 105 ? 0.47170 0.44460 0.60810 0.00030  -0.01000 0.02010  105 ARG B NH2 
3148 N N   . ILE B 106 ? 0.51150 0.48460 0.59450 -0.00410 -0.03370 0.02180  106 ILE B N   
3149 C CA  . ILE B 106 ? 0.54420 0.51420 0.62420 -0.00230 -0.03160 0.02500  106 ILE B CA  
3150 C C   . ILE B 106 ? 0.54540 0.51150 0.63650 0.00060  -0.02600 0.02560  106 ILE B C   
3151 O O   . ILE B 106 ? 0.52050 0.48590 0.61810 0.00130  -0.02220 0.02320  106 ILE B O   
3152 C CB  . ILE B 106 ? 0.51270 0.47880 0.57760 -0.00270 -0.02900 0.02190  106 ILE B CB  
3153 C CG1 . ILE B 106 ? 0.47930 0.44060 0.54080 -0.00220 -0.02330 0.01660  106 ILE B CG1 
3154 C CG2 . ILE B 106 ? 0.60030 0.57160 0.65450 -0.00510 -0.03440 0.02190  106 ILE B CG2 
3155 C CD1 . ILE B 106 ? 0.59870 0.55590 0.64890 -0.00160 -0.01990 0.01500  106 ILE B CD1 
3156 N N   . GLN B 107 ? 0.50460 0.46850 0.59840 0.00230  -0.02510 0.02880  107 GLN B N   
3157 C CA  . GLN B 107 ? 0.55390 0.51410 0.65780 0.00530  -0.01930 0.02760  107 GLN B CA  
3158 C C   . GLN B 107 ? 0.52040 0.47520 0.61450 0.00600  -0.01360 0.02270  107 GLN B C   
3159 O O   . GLN B 107 ? 0.50670 0.45990 0.58820 0.00450  -0.01470 0.02210  107 GLN B O   
3160 C CB  . GLN B 107 ? 0.60050 0.56080 0.71690 0.00700  -0.02120 0.03300  107 GLN B CB  
3161 C CG  . GLN B 107 ? 0.66340 0.63040 0.78920 0.00630  -0.02800 0.03960  107 GLN B CG  
3162 C CD  . GLN B 107 ? 0.65470 0.62490 0.79240 0.00710  -0.02690 0.03850  107 GLN B CD  
3163 O OE1 . GLN B 107 ? 0.66760 0.63520 0.81480 0.00970  -0.02100 0.03580  107 GLN B OE1 
3164 N NE2 . GLN B 107 ? 0.68130 0.65780 0.81840 0.00470  -0.03240 0.03980  107 GLN B NE2 
3165 N N   . PRO B 108 ? 0.49670 0.44980 0.59690 0.00820  -0.00760 0.01920  108 PRO B N   
3166 C CA  . PRO B 108 ? 0.54980 0.49930 0.64230 0.00910  -0.00220 0.01420  108 PRO B CA  
3167 C C   . PRO B 108 ? 0.51760 0.46360 0.60840 0.00890  -0.00390 0.01540  108 PRO B C   
3168 O O   . PRO B 108 ? 0.51700 0.46260 0.61870 0.00960  -0.00660 0.01960  108 PRO B O   
3169 C CB  . PRO B 108 ? 0.55550 0.50620 0.65850 0.01180  0.00380  0.01080  108 PRO B CB  
3170 C CG  . PRO B 108 ? 0.57950 0.53360 0.69760 0.01240  0.00110  0.01510  108 PRO B CG  
3171 C CD  . PRO B 108 ? 0.55480 0.51100 0.66760 0.00970  -0.00500 0.01890  108 PRO B CD  
3172 N N   . GLY B 109 ? 0.52730 0.47110 0.60540 0.00780  -0.00250 0.01270  109 GLY B N   
3173 C CA  . GLY B 109 ? 0.50210 0.44280 0.57830 0.00720  -0.00400 0.01400  109 GLY B CA  
3174 C C   . GLY B 109 ? 0.53900 0.48160 0.60640 0.00480  -0.00930 0.01900  109 GLY B C   
3175 O O   . GLY B 109 ? 0.53160 0.47240 0.59350 0.00370  -0.00980 0.01980  109 GLY B O   
3176 N N   . GLN B 110 ? 0.49100 0.43780 0.55670 0.00370  -0.01320 0.02180  110 GLN B N   
3177 C CA  . GLN B 110 ? 0.54710 0.49730 0.60310 0.00140  -0.01800 0.02520  110 GLN B CA  
3178 C C   . GLN B 110 ? 0.52140 0.47110 0.56300 0.00030  -0.01600 0.02030  110 GLN B C   
3179 O O   . GLN B 110 ? 0.51410 0.46210 0.55430 0.00110  -0.01230 0.01570  110 GLN B O   
3180 C CB  . GLN B 110 ? 0.49550 0.45160 0.55590 0.00050  -0.02340 0.02910  110 GLN B CB  
3181 C CG  . GLN B 110 ? 0.57900 0.53710 0.65370 0.00150  -0.02650 0.03620  110 GLN B CG  
3182 C CD  . GLN B 110 ? 0.68540 0.64310 0.76060 0.00120  -0.02800 0.04210  110 GLN B CD  
3183 O OE1 . GLN B 110 ? 0.77500 0.73750 0.84070 -0.00080 -0.03170 0.04600  110 GLN B OE1 
3184 N NE2 . GLN B 110 ? 0.63740 0.58960 0.72410 0.00300  -0.02490 0.04250  110 GLN B NE2 
3185 N N   . THR B 111 ? 0.46440 0.41600 0.49610 -0.00130 -0.01820 0.02190  111 THR B N   
3186 C CA  . THR B 111 ? 0.47690 0.42810 0.49640 -0.00200 -0.01630 0.01750  111 THR B CA  
3187 C C   . THR B 111 ? 0.48230 0.43850 0.49550 -0.00360 -0.02000 0.01670  111 THR B C   
3188 O O   . THR B 111 ? 0.51160 0.47300 0.52680 -0.00460 -0.02470 0.02010  111 THR B O   
3189 C CB  . THR B 111 ? 0.49620 0.44650 0.50890 -0.00260 -0.01530 0.01850  111 THR B CB  
3190 O OG1 . THR B 111 ? 0.50670 0.46120 0.52050 -0.00380 -0.01940 0.02480  111 THR B OG1 
3191 C CG2 . THR B 111 ? 0.48640 0.43180 0.50500 -0.00140 -0.01150 0.01720  111 THR B CG2 
3192 N N   . PHE B 112 ? 0.47430 0.42960 0.47950 -0.00390 -0.01790 0.01190  112 PHE B N   
3193 C CA  . PHE B 112 ? 0.53420 0.49370 0.53330 -0.00530 -0.02070 0.00910  112 PHE B CA  
3194 C C   . PHE B 112 ? 0.50010 0.45750 0.49110 -0.00500 -0.01740 0.00460  112 PHE B C   
3195 O O   . PHE B 112 ? 0.49780 0.45090 0.48870 -0.00370 -0.01320 0.00380  112 PHE B O   
3196 C CB  . PHE B 112 ? 0.49300 0.45340 0.49920 -0.00570 -0.02260 0.00670  112 PHE B CB  
3197 C CG  . PHE B 112 ? 0.49480 0.45000 0.50790 -0.00430 -0.01820 0.00490  112 PHE B CG  
3198 C CD1 . PHE B 112 ? 0.47880 0.43160 0.48960 -0.00410 -0.01540 0.00080  112 PHE B CD1 
3199 C CD2 . PHE B 112 ? 0.53000 0.48360 0.55240 -0.00300 -0.01670 0.00770  112 PHE B CD2 
3200 C CE1 . PHE B 112 ? 0.49090 0.44030 0.50790 -0.00290 -0.01120 0.00060  112 PHE B CE1 
3201 C CE2 . PHE B 112 ? 0.50600 0.45680 0.53420 -0.00180 -0.01220 0.00630  112 PHE B CE2 
3202 C CZ  . PHE B 112 ? 0.45950 0.40860 0.48460 -0.00180 -0.00950 0.00340  112 PHE B CZ  
3203 N N   . SER B 113 ? 0.50390 0.46550 0.48860 -0.00620 -0.01950 0.00150  113 SER B N   
3204 C CA  . SER B 113 ? 0.50830 0.46870 0.48700 -0.00570 -0.01660 -0.00320 113 SER B CA  
3205 C C   . SER B 113 ? 0.46130 0.41860 0.44580 -0.00540 -0.01570 -0.00780 113 SER B C   
3206 O O   . SER B 113 ? 0.49780 0.45730 0.48710 -0.00660 -0.01890 -0.00960 113 SER B O   
3207 C CB  . SER B 113 ? 0.50670 0.47400 0.47620 -0.00700 -0.01890 -0.00510 113 SER B CB  
3208 O OG  . SER B 113 ? 0.51320 0.48400 0.47840 -0.00750 -0.01980 0.00080  113 SER B OG  
3209 N N   . VAL B 114 ? 0.46090 0.41400 0.44580 -0.00410 -0.01150 -0.00930 114 VAL B N   
3210 C CA  . VAL B 114 ? 0.49920 0.44910 0.49120 -0.00360 -0.00980 -0.01240 114 VAL B CA  
3211 C C   . VAL B 114 ? 0.50010 0.45040 0.48800 -0.00340 -0.00900 -0.01730 114 VAL B C   
3212 O O   . VAL B 114 ? 0.51370 0.46430 0.49520 -0.00230 -0.00660 -0.01650 114 VAL B O   
3213 C CB  . VAL B 114 ? 0.49430 0.44010 0.49060 -0.00190 -0.00530 -0.00890 114 VAL B CB  
3214 C CG1 . VAL B 114 ? 0.47640 0.41950 0.48100 -0.00130 -0.00330 -0.01070 114 VAL B CG1 
3215 C CG2 . VAL B 114 ? 0.46630 0.41200 0.46790 -0.00170 -0.00520 -0.00510 114 VAL B CG2 
3216 N N   . LEU B 115 ? 0.47530 0.42610 0.46810 -0.00430 -0.01080 -0.02290 115 LEU B N   
3217 C CA  . LEU B 115 ? 0.46480 0.41490 0.45750 -0.00370 -0.00930 -0.02880 115 LEU B CA  
3218 C C   . LEU B 115 ? 0.53500 0.47910 0.53960 -0.00250 -0.00630 -0.02810 115 LEU B C   
3219 O O   . LEU B 115 ? 0.52680 0.46900 0.54180 -0.00360 -0.00760 -0.03070 115 LEU B O   
3220 C CB  . LEU B 115 ? 0.45310 0.40830 0.44420 -0.00550 -0.01330 -0.03650 115 LEU B CB  
3221 C CG  . LEU B 115 ? 0.50500 0.45990 0.49730 -0.00480 -0.01170 -0.04460 115 LEU B CG  
3222 C CD1 . LEU B 115 ? 0.50310 0.46190 0.48310 -0.00350 -0.00930 -0.04280 115 LEU B CD1 
3223 C CD2 . LEU B 115 ? 0.53070 0.49090 0.52350 -0.00690 -0.01570 -0.05450 115 LEU B CD2 
3224 N N   . ALA B 116 ? 0.50530 0.44700 0.50900 -0.00040 -0.00230 -0.02390 116 ALA B N   
3225 C CA  . ALA B 116 ? 0.47570 0.41320 0.49070 0.00080  0.00080  -0.02160 116 ALA B CA  
3226 C C   . ALA B 116 ? 0.53390 0.46920 0.55670 0.00110  0.00100  -0.02810 116 ALA B C   
3227 O O   . ALA B 116 ? 0.52560 0.46280 0.54260 0.00180  0.00120  -0.03300 116 ALA B O   
3228 C CB  . ALA B 116 ? 0.51870 0.45640 0.53000 0.00290  0.00460  -0.01520 116 ALA B CB  
3229 N N   . CYS B 117 ? 0.47410 0.40570 0.51120 0.00050  0.00090  -0.02880 117 CYS B N   
3230 C CA  . CYS B 117 ? 0.50150 0.43010 0.54960 0.00050  0.00090  -0.03590 117 CYS B CA  
3231 C C   . CYS B 117 ? 0.55100 0.47440 0.61580 0.00160  0.00400  -0.03060 117 CYS B C   
3232 O O   . CYS B 117 ? 0.50240 0.42540 0.57270 0.00120  0.00490  -0.02310 117 CYS B O   
3233 C CB  . CYS B 117 ? 0.53430 0.46380 0.58680 -0.00230 -0.00350 -0.04450 117 CYS B CB  
3234 S SG  . CYS B 117 ? 0.61500 0.55250 0.65040 -0.00410 -0.00800 -0.05070 117 CYS B SG  
3235 N N   . TYR B 118 ? 0.52520 0.44530 0.59990 0.00290  0.00550  -0.03490 118 TYR B N   
3236 C CA  . TYR B 118 ? 0.56620 0.48100 0.66030 0.00390  0.00820  -0.03050 118 TYR B CA  
3237 C C   . TYR B 118 ? 0.57370 0.48430 0.68210 0.00320  0.00700  -0.04150 118 TYR B C   
3238 O O   . TYR B 118 ? 0.52180 0.43380 0.62400 0.00390  0.00640  -0.05110 118 TYR B O   
3239 C CB  . TYR B 118 ? 0.54730 0.46260 0.64100 0.00730  0.01230  -0.02180 118 TYR B CB  
3240 C CG  . TYR B 118 ? 0.54080 0.46110 0.62060 0.00760  0.01310  -0.01290 118 TYR B CG  
3241 C CD1 . TYR B 118 ? 0.53470 0.45580 0.62040 0.00730  0.01460  -0.00350 118 TYR B CD1 
3242 C CD2 . TYR B 118 ? 0.53740 0.46200 0.59870 0.00790  0.01230  -0.01470 118 TYR B CD2 
3243 C CE1 . TYR B 118 ? 0.51080 0.43690 0.58430 0.00750  0.01550  0.00280  118 TYR B CE1 
3244 C CE2 . TYR B 118 ? 0.52160 0.45030 0.57190 0.00790  0.01300  -0.00780 118 TYR B CE2 
3245 C CZ  . TYR B 118 ? 0.52920 0.45850 0.58580 0.00780  0.01450  0.00020  118 TYR B CZ  
3246 O OH  . TYR B 118 ? 0.50560 0.43940 0.55260 0.00790  0.01550  0.00570  118 TYR B OH  
3247 N N   . ASN B 119 ? 0.54830 0.45420 0.67630 0.00170  0.00660  -0.04080 119 ASN B N   
3248 C CA  . ASN B 119 ? 0.58890 0.48970 0.73440 0.00070  0.00550  -0.05190 119 ASN B CA  
3249 C C   . ASN B 119 ? 0.57320 0.47800 0.70850 -0.00140 0.00130  -0.06690 119 ASN B C   
3250 O O   . ASN B 119 ? 0.57030 0.47400 0.71000 -0.00090 0.00120  -0.07880 119 ASN B O   
3251 C CB  . ASN B 119 ? 0.64620 0.54290 0.80280 0.00420  0.00940  -0.05160 119 ASN B CB  
3252 C CG  . ASN B 119 ? 0.66070 0.55570 0.82690 0.00640  0.01320  -0.03570 119 ASN B CG  
3253 O OD1 . ASN B 119 ? 0.72180 0.61320 0.90630 0.00520  0.01390  -0.02930 119 ASN B OD1 
3254 N ND2 . ASN B 119 ? 0.65240 0.55090 0.80700 0.00930  0.01580  -0.02890 119 ASN B ND2 
3255 N N   . GLY B 120 ? 0.55120 0.46160 0.67160 -0.00360 -0.00210 -0.06630 120 GLY B N   
3256 C CA  . GLY B 120 ? 0.53540 0.45190 0.64380 -0.00570 -0.00640 -0.07840 120 GLY B CA  
3257 C C   . GLY B 120 ? 0.56900 0.49090 0.65850 -0.00360 -0.00520 -0.08150 120 GLY B C   
3258 O O   . GLY B 120 ? 0.54350 0.47200 0.62270 -0.00510 -0.00830 -0.09140 120 GLY B O   
3259 N N   . SER B 121 ? 0.54320 0.46360 0.62900 -0.00030 -0.00080 -0.07370 121 SER B N   
3260 C CA  . SER B 121 ? 0.57400 0.49980 0.64360 0.00150  0.00060  -0.07690 121 SER B CA  
3261 C C   . SER B 121 ? 0.58530 0.51540 0.63770 0.00190  0.00080  -0.06650 121 SER B C   
3262 O O   . SER B 121 ? 0.56550 0.49260 0.62020 0.00340  0.00340  -0.05570 121 SER B O   
3263 C CB  . SER B 121 ? 0.62210 0.54420 0.70030 0.00510  0.00520  -0.07740 121 SER B CB  
3264 O OG  . SER B 121 ? 0.71770 0.63730 0.80920 0.00520  0.00530  -0.09000 121 SER B OG  
3265 N N   . PRO B 122 ? 0.61090 0.54850 0.64660 0.00060  -0.00180 -0.06930 122 PRO B N   
3266 C CA  . PRO B 122 ? 0.60740 0.54840 0.62850 0.00100  -0.00130 -0.05980 122 PRO B CA  
3267 C C   . PRO B 122 ? 0.57600 0.51590 0.59530 0.00400  0.00310  -0.05460 122 PRO B C   
3268 O O   . PRO B 122 ? 0.58420 0.52550 0.60360 0.00560  0.00510  -0.06030 122 PRO B O   
3269 C CB  . PRO B 122 ? 0.57870 0.52870 0.58510 -0.00070 -0.00440 -0.06500 122 PRO B CB  
3270 C CG  . PRO B 122 ? 0.63300 0.58460 0.64560 -0.00310 -0.00830 -0.07480 122 PRO B CG  
3271 C CD  . PRO B 122 ? 0.58470 0.52870 0.61520 -0.00180 -0.00570 -0.08050 122 PRO B CD  
3272 N N   . SER B 123 ? 0.55060 0.48890 0.56790 0.00470  0.00450  -0.04420 123 SER B N   
3273 C CA  . SER B 123 ? 0.62250 0.56120 0.63710 0.00720  0.00800  -0.03850 123 SER B CA  
3274 C C   . SER B 123 ? 0.60090 0.54420 0.60070 0.00670  0.00760  -0.03350 123 SER B C   
3275 O O   . SER B 123 ? 0.60300 0.54900 0.59810 0.00830  0.00980  -0.03180 123 SER B O   
3276 C CB  . SER B 123 ? 0.59440 0.52860 0.62020 0.00870  0.01030  -0.03060 123 SER B CB  
3277 O OG  . SER B 123 ? 0.64160 0.57610 0.66410 0.00730  0.00930  -0.02450 123 SER B OG  
3278 N N   . GLY B 124 ? 0.56380 0.50850 0.55770 0.00470  0.00500  -0.03100 124 GLY B N   
3279 C CA  . GLY B 124 ? 0.54500 0.49350 0.52750 0.00430  0.00480  -0.02650 124 GLY B CA  
3280 C C   . GLY B 124 ? 0.58130 0.53130 0.55940 0.00200  0.00150  -0.02500 124 GLY B C   
3281 O O   . GLY B 124 ? 0.53680 0.48490 0.52080 0.00090  -0.00060 -0.02610 124 GLY B O   
3282 N N   . VAL B 125 ? 0.49470 0.44830 0.46380 0.00140  0.00090  -0.02190 125 VAL B N   
3283 C CA  . VAL B 125 ? 0.53120 0.48660 0.49750 -0.00050 -0.00230 -0.01960 125 VAL B CA  
3284 C C   . VAL B 125 ? 0.56360 0.51840 0.52710 -0.00040 -0.00140 -0.01340 125 VAL B C   
3285 O O   . VAL B 125 ? 0.55880 0.51520 0.51780 0.00010  0.00050  -0.01190 125 VAL B O   
3286 C CB  . VAL B 125 ? 0.50960 0.47170 0.46900 -0.00200 -0.00510 -0.02300 125 VAL B CB  
3287 C CG1 . VAL B 125 ? 0.57780 0.54460 0.52910 -0.00170 -0.00350 -0.02180 125 VAL B CG1 
3288 C CG2 . VAL B 125 ? 0.52470 0.48940 0.48310 -0.00380 -0.00900 -0.01970 125 VAL B CG2 
3289 N N   . TYR B 126 ? 0.45040 0.40330 0.41770 -0.00100 -0.00260 -0.01030 126 TYR B N   
3290 C CA  . TYR B 126 ? 0.50800 0.46010 0.47430 -0.00100 -0.00180 -0.00590 126 TYR B CA  
3291 C C   . TYR B 126 ? 0.54420 0.49570 0.51470 -0.00190 -0.00420 -0.00350 126 TYR B C   
3292 O O   . TYR B 126 ? 0.50290 0.45410 0.47830 -0.00220 -0.00590 -0.00470 126 TYR B O   
3293 C CB  . TYR B 126 ? 0.46020 0.40990 0.42880 0.00050  0.00170  -0.00480 126 TYR B CB  
3294 C CG  . TYR B 126 ? 0.52080 0.46790 0.49660 0.00130  0.00280  -0.00490 126 TYR B CG  
3295 C CD1 . TYR B 126 ? 0.52460 0.47070 0.50520 0.00120  0.00280  -0.00310 126 TYR B CD1 
3296 C CD2 . TYR B 126 ? 0.53420 0.48040 0.51350 0.00230  0.00410  -0.00660 126 TYR B CD2 
3297 C CE1 . TYR B 126 ? 0.50530 0.45010 0.49350 0.00190  0.00420  -0.00250 126 TYR B CE1 
3298 C CE2 . TYR B 126 ? 0.51980 0.46400 0.50760 0.00280  0.00530  -0.00550 126 TYR B CE2 
3299 C CZ  . TYR B 126 ? 0.48820 0.43210 0.47990 0.00260  0.00540  -0.00320 126 TYR B CZ  
3300 O OH  . TYR B 126 ? 0.53350 0.47630 0.53420 0.00300  0.00690  -0.00140 126 TYR B OH  
3301 N N   . GLN B 127 ? 0.44620 0.39740 0.41660 -0.00220 -0.00410 -0.00030 127 GLN B N   
3302 C CA  . GLN B 127 ? 0.52780 0.47830 0.50420 -0.00260 -0.00590 0.00240  127 GLN B CA  
3303 C C   . GLN B 127 ? 0.51530 0.46250 0.49810 -0.00130 -0.00330 0.00200  127 GLN B C   
3304 O O   . GLN B 127 ? 0.54940 0.49570 0.53060 -0.00040 -0.00020 0.00100  127 GLN B O   
3305 C CB  . GLN B 127 ? 0.55660 0.50770 0.53300 -0.00340 -0.00680 0.00610  127 GLN B CB  
3306 C CG  . GLN B 127 ? 0.55660 0.51250 0.52840 -0.00480 -0.00970 0.00880  127 GLN B CG  
3307 C CD  . GLN B 127 ? 0.53050 0.48970 0.50490 -0.00550 -0.01380 0.01030  127 GLN B CD  
3308 O OE1 . GLN B 127 ? 0.55650 0.51880 0.52720 -0.00590 -0.01510 0.00710  127 GLN B OE1 
3309 N NE2 . GLN B 127 ? 0.52420 0.48380 0.50520 -0.00590 -0.01600 0.01530  127 GLN B NE2 
3310 N N   . CYS B 128 ? 0.49030 0.43710 0.48030 -0.00120 -0.00470 0.00300  128 CYS B N   
3311 C CA  . CYS B 128 ? 0.54220 0.48730 0.53920 0.00010  -0.00200 0.00280  128 CYS B CA  
3312 C C   . CYS B 128 ? 0.50160 0.44640 0.50640 0.00010  -0.00380 0.00510  128 CYS B C   
3313 O O   . CYS B 128 ? 0.55880 0.50540 0.56520 -0.00090 -0.00780 0.00740  128 CYS B O   
3314 C CB  . CYS B 128 ? 0.49280 0.43800 0.49420 0.00040  -0.00130 0.00180  128 CYS B CB  
3315 S SG  . CYS B 128 ? 0.61830 0.56330 0.61550 0.00140  0.00280  0.00060  128 CYS B SG  
3316 N N   . ALA B 129 ? 0.56160 0.50510 0.57220 0.00140  -0.00080 0.00430  129 ALA B N   
3317 C CA  . ALA B 129 ? 0.46790 0.41120 0.48910 0.00200  -0.00200 0.00610  129 ALA B CA  
3318 C C   . ALA B 129 ? 0.46120 0.40570 0.48910 0.00310  0.00030  0.00520  129 ALA B C   
3319 O O   . ALA B 129 ? 0.48950 0.43480 0.51460 0.00380  0.00400  0.00330  129 ALA B O   
3320 C CB  . ALA B 129 ? 0.45550 0.39680 0.48160 0.00290  -0.00000 0.00520  129 ALA B CB  
3321 N N   . MET B 130 ? 0.45390 0.39950 0.49120 0.00320  -0.00210 0.00750  130 MET B N   
3322 C CA  . MET B 130 ? 0.45170 0.39890 0.49810 0.00450  0.00060  0.00710  130 MET B CA  
3323 C C   . MET B 130 ? 0.42120 0.36790 0.47280 0.00650  0.00500  0.00490  130 MET B C   
3324 O O   . MET B 130 ? 0.45960 0.40480 0.51810 0.00710  0.00360  0.00590  130 MET B O   
3325 C CB  . MET B 130 ? 0.42520 0.37450 0.48060 0.00380  -0.00380 0.01020  130 MET B CB  
3326 C CG  . MET B 130 ? 0.45500 0.40660 0.52300 0.00510  -0.00100 0.01050  130 MET B CG  
3327 S SD  . MET B 130 ? 0.48530 0.43810 0.55020 0.00440  0.00210  0.00920  130 MET B SD  
3328 C CE  . MET B 130 ? 0.46460 0.41770 0.52750 0.00170  -0.00430 0.00970  130 MET B CE  
3329 N N   . ARG B 131 ? 0.43230 0.38070 0.48060 0.00760  0.01020  0.00180  131 ARG B N   
3330 C CA  . ARG B 131 ? 0.43390 0.38340 0.48610 0.00950  0.01480  -0.00200 131 ARG B CA  
3331 C C   . ARG B 131 ? 0.48770 0.43890 0.55420 0.01120  0.01610  -0.00150 131 ARG B C   
3332 O O   . ARG B 131 ? 0.45550 0.40840 0.52790 0.01080  0.01450  0.00190  131 ARG B O   
3333 C CB  . ARG B 131 ? 0.44080 0.39450 0.48570 0.01020  0.02000  -0.00450 131 ARG B CB  
3334 C CG  . ARG B 131 ? 0.51480 0.46810 0.54690 0.00890  0.01910  -0.00440 131 ARG B CG  
3335 C CD  . ARG B 131 ? 0.50780 0.45760 0.53580 0.00810  0.01720  -0.00680 131 ARG B CD  
3336 N NE  . ARG B 131 ? 0.50010 0.45020 0.53370 0.00940  0.01980  -0.01160 131 ARG B NE  
3337 C CZ  . ARG B 131 ? 0.52900 0.47550 0.56400 0.00870  0.01810  -0.01390 131 ARG B CZ  
3338 N NH1 . ARG B 131 ? 0.49340 0.43680 0.52270 0.00690  0.01430  -0.01110 131 ARG B NH1 
3339 N NH2 . ARG B 131 ? 0.50220 0.44850 0.54540 0.01000  0.02060  -0.01910 131 ARG B NH2 
3340 N N   . PRO B 132 ? 0.51490 0.46590 0.58850 0.01310  0.01910  -0.00550 132 PRO B N   
3341 C CA  . PRO B 132 ? 0.49980 0.45320 0.58820 0.01520  0.02130  -0.00570 132 PRO B CA  
3342 C C   . PRO B 132 ? 0.50300 0.46270 0.59270 0.01600  0.02550  -0.00520 132 PRO B C   
3343 O O   . PRO B 132 ? 0.46760 0.42980 0.56990 0.01710  0.02610  -0.00320 132 PRO B O   
3344 C CB  . PRO B 132 ? 0.45720 0.40960 0.55070 0.01710  0.02500  -0.01230 132 PRO B CB  
3345 C CG  . PRO B 132 ? 0.45800 0.40480 0.54370 0.01520  0.02130  -0.01260 132 PRO B CG  
3346 C CD  . PRO B 132 ? 0.49160 0.43960 0.56190 0.01310  0.01960  -0.00990 132 PRO B CD  
3347 N N   . ASN B 133 ? 0.45970 0.42270 0.53800 0.01540  0.02870  -0.00640 133 ASN B N   
3348 C CA  . ASN B 133 ? 0.47500 0.44470 0.55530 0.01590  0.03280  -0.00410 133 ASN B CA  
3349 C C   . ASN B 133 ? 0.47450 0.44270 0.55370 0.01370  0.02880  0.00180  133 ASN B C   
3350 O O   . ASN B 133 ? 0.45860 0.43130 0.53800 0.01340  0.03180  0.00460  133 ASN B O   
3351 C CB  . ASN B 133 ? 0.45400 0.43000 0.52420 0.01670  0.03860  -0.00720 133 ASN B CB  
3352 C CG  . ASN B 133 ? 0.45870 0.43270 0.51460 0.01490  0.03640  -0.00610 133 ASN B CG  
3353 O OD1 . ASN B 133 ? 0.46900 0.43670 0.52200 0.01320  0.03110  -0.00380 133 ASN B OD1 
3354 N ND2 . ASN B 133 ? 0.49650 0.47720 0.54360 0.01550  0.04070  -0.00780 133 ASN B ND2 
3355 N N   . PHE B 134 ? 0.40620 0.36870 0.48430 0.01190  0.02240  0.00360  134 PHE B N   
3356 C CA  . PHE B 134 ? 0.40320 0.36430 0.48220 0.00970  0.01790  0.00740  134 PHE B CA  
3357 C C   . PHE B 134 ? 0.45040 0.41130 0.51970 0.00840  0.01850  0.00820  134 PHE B C   
3358 O O   . PHE B 134 ? 0.52460 0.48530 0.59750 0.00680  0.01650  0.01070  134 PHE B O   
3359 C CB  . PHE B 134 ? 0.45930 0.42440 0.55250 0.00980  0.01850  0.01030  134 PHE B CB  
3360 C CG  . PHE B 134 ? 0.46080 0.42620 0.56550 0.01090  0.01650  0.01060  134 PHE B CG  
3361 C CD1 . PHE B 134 ? 0.50250 0.46540 0.60950 0.00940  0.00940  0.01260  134 PHE B CD1 
3362 C CD2 . PHE B 134 ? 0.52310 0.49220 0.63640 0.01360  0.02180  0.00890  134 PHE B CD2 
3363 C CE1 . PHE B 134 ? 0.52150 0.48530 0.64100 0.01080  0.00720  0.01420  134 PHE B CE1 
3364 C CE2 . PHE B 134 ? 0.54870 0.51780 0.67520 0.01510  0.02020  0.00930  134 PHE B CE2 
3365 C CZ  . PHE B 134 ? 0.53160 0.49800 0.66160 0.01370  0.01260  0.01270  134 PHE B CZ  
3366 N N   . THR B 135 ? 0.46070 0.42180 0.51930 0.00900  0.02130  0.00620  135 THR B N   
3367 C CA  . THR B 135 ? 0.39700 0.35730 0.44660 0.00800  0.02120  0.00730  135 THR B CA  
3368 C C   . THR B 135 ? 0.43840 0.39390 0.47900 0.00700  0.01700  0.00530  135 THR B C   
3369 O O   . THR B 135 ? 0.42960 0.38290 0.47040 0.00710  0.01490  0.00350  135 THR B O   
3370 C CB  . THR B 135 ? 0.41550 0.38130 0.45920 0.00940  0.02700  0.00730  135 THR B CB  
3371 O OG1 . THR B 135 ? 0.46680 0.43350 0.50450 0.01040  0.02850  0.00260  135 THR B OG1 
3372 C CG2 . THR B 135 ? 0.42760 0.40050 0.48050 0.01050  0.03210  0.01010  135 THR B CG2 
3373 N N   . ILE B 136 ? 0.38310 0.33720 0.41690 0.00600  0.01600  0.00600  136 ILE B N   
3374 C CA  . ILE B 136 ? 0.42280 0.37380 0.44710 0.00530  0.01320  0.00400  136 ILE B CA  
3375 C C   . ILE B 136 ? 0.48330 0.43640 0.49960 0.00590  0.01630  0.00400  136 ILE B C   
3376 O O   . ILE B 136 ? 0.46320 0.41910 0.48130 0.00640  0.01900  0.00660  136 ILE B O   
3377 C CB  . ILE B 136 ? 0.49000 0.43810 0.51340 0.00360  0.00820  0.00420  136 ILE B CB  
3378 C CG1 . ILE B 136 ? 0.50540 0.45320 0.53000 0.00310  0.00880  0.00510  136 ILE B CG1 
3379 C CG2 . ILE B 136 ? 0.49820 0.44620 0.52990 0.00280  0.00460  0.00480  136 ILE B CG2 
3380 C CD1 . ILE B 136 ? 0.47580 0.42140 0.49980 0.00140  0.00420  0.00320  136 ILE B CD1 
3381 N N   . LYS B 137 ? 0.52980 0.48210 0.53810 0.00580  0.01570  0.00180  137 LYS B N   
3382 C CA  . LYS B 137 ? 0.49520 0.45030 0.49590 0.00630  0.01780  0.00200  137 LYS B CA  
3383 C C   . LYS B 137 ? 0.50760 0.45980 0.50460 0.00540  0.01500  0.00270  137 LYS B C   
3384 O O   . LYS B 137 ? 0.50900 0.45930 0.50080 0.00460  0.01280  0.00110  137 LYS B O   
3385 C CB  . LYS B 137 ? 0.48240 0.43930 0.47840 0.00650  0.01890  -0.00160 137 LYS B CB  
3386 C CG  . LYS B 137 ? 0.59550 0.55540 0.59640 0.00760  0.02200  -0.00420 137 LYS B CG  
3387 C CD  . LYS B 137 ? 0.69020 0.65170 0.68660 0.00750  0.02270  -0.00920 137 LYS B CD  
3388 C CE  . LYS B 137 ? 0.73290 0.69640 0.73520 0.00860  0.02540  -0.01400 137 LYS B CE  
3389 N NZ  . LYS B 137 ? 0.77770 0.73960 0.77830 0.00780  0.02450  -0.01950 137 LYS B NZ  
3390 N N   . GLY B 138 ? 0.50350 0.45520 0.50430 0.00540  0.01520  0.00500  138 GLY B N   
3391 C CA  . GLY B 138 ? 0.51450 0.46360 0.51370 0.00480  0.01300  0.00450  138 GLY B CA  
3392 C C   . GLY B 138 ? 0.46610 0.41730 0.46210 0.00590  0.01520  0.00660  138 GLY B C   
3393 O O   . GLY B 138 ? 0.49670 0.45240 0.48920 0.00680  0.01780  0.00820  138 GLY B O   
3394 N N   . SER B 139 ? 0.45010 0.39890 0.44840 0.00580  0.01410  0.00630  139 SER B N   
3395 C CA  . SER B 139 ? 0.45390 0.40410 0.45270 0.00700  0.01600  0.00890  139 SER B CA  
3396 C C   . SER B 139 ? 0.46150 0.40810 0.47060 0.00690  0.01550  0.00900  139 SER B C   
3397 O O   . SER B 139 ? 0.48770 0.43080 0.49740 0.00600  0.01290  0.00440  139 SER B O   
3398 C CB  . SER B 139 ? 0.45810 0.40870 0.44860 0.00710  0.01480  0.00650  139 SER B CB  
3399 O OG  . SER B 139 ? 0.47770 0.42980 0.47120 0.00860  0.01660  0.00960  139 SER B OG  
3400 N N   . PHE B 140 ? 0.45610 0.40400 0.47410 0.00750  0.01780  0.01400  140 PHE B N   
3401 C CA  . PHE B 140 ? 0.46200 0.40610 0.49290 0.00690  0.01750  0.01430  140 PHE B CA  
3402 C C   . PHE B 140 ? 0.48130 0.42790 0.52070 0.00840  0.02090  0.02190  140 PHE B C   
3403 O O   . PHE B 140 ? 0.49080 0.44340 0.52850 0.00920  0.02370  0.02790  140 PHE B O   
3404 C CB  . PHE B 140 ? 0.44340 0.38710 0.48030 0.00540  0.01660  0.01400  140 PHE B CB  
3405 C CG  . PHE B 140 ? 0.44270 0.38430 0.47490 0.00380  0.01260  0.00770  140 PHE B CG  
3406 C CD1 . PHE B 140 ? 0.50290 0.44120 0.53600 0.00260  0.00920  0.00190  140 PHE B CD1 
3407 C CD2 . PHE B 140 ? 0.47400 0.41780 0.50080 0.00360  0.01220  0.00750  140 PHE B CD2 
3408 C CE1 . PHE B 140 ? 0.47700 0.41530 0.50520 0.00110  0.00520  -0.00280 140 PHE B CE1 
3409 C CE2 . PHE B 140 ? 0.48920 0.43190 0.51290 0.00220  0.00830  0.00340  140 PHE B CE2 
3410 C CZ  . PHE B 140 ? 0.49130 0.43180 0.51570 0.00090  0.00470  -0.00110 140 PHE B CZ  
3411 N N   . LEU B 141 ? 0.44970 0.39210 0.49980 0.00860  0.02070  0.02180  141 LEU B N   
3412 C CA  . LEU B 141 ? 0.50140 0.44530 0.56340 0.00990  0.02360  0.03020  141 LEU B CA  
3413 C C   . LEU B 141 ? 0.51560 0.45490 0.59490 0.00850  0.02330  0.03050  141 LEU B C   
3414 O O   . LEU B 141 ? 0.50520 0.44040 0.58600 0.00650  0.02040  0.02320  141 LEU B O   
3415 C CB  . LEU B 141 ? 0.50700 0.44970 0.57110 0.01180  0.02400  0.03090  141 LEU B CB  
3416 C CG  . LEU B 141 ? 0.57090 0.51850 0.61910 0.01290  0.02390  0.03000  141 LEU B CG  
3417 C CD1 . LEU B 141 ? 0.62840 0.57460 0.67910 0.01480  0.02390  0.02920  141 LEU B CD1 
3418 C CD2 . LEU B 141 ? 0.57030 0.52700 0.61280 0.01380  0.02640  0.03840  141 LEU B CD2 
3419 N N   . ASN B 142 ? 0.48530 0.42570 0.57850 0.00930  0.02610  0.03920  142 ASN B N   
3420 C CA  . ASN B 142 ? 0.51170 0.44680 0.62450 0.00770  0.02570  0.03940  142 ASN B CA  
3421 C C   . ASN B 142 ? 0.51530 0.44220 0.63280 0.00700  0.02230  0.02830  142 ASN B C   
3422 O O   . ASN B 142 ? 0.49720 0.42260 0.60940 0.00860  0.02200  0.02470  142 ASN B O   
3423 C CB  . ASN B 142 ? 0.48860 0.42610 0.61720 0.00900  0.02930  0.05160  142 ASN B CB  
3424 C CG  . ASN B 142 ? 0.57480 0.52220 0.70040 0.00930  0.03300  0.06260  142 ASN B CG  
3425 O OD1 . ASN B 142 ? 0.56170 0.51210 0.68050 0.00800  0.03290  0.06040  142 ASN B OD1 
3426 N ND2 . ASN B 142 ? 0.62740 0.58090 0.75850 0.01110  0.03620  0.07450  142 ASN B ND2 
3427 N N   . GLY B 143 ? 0.51060 0.43340 0.63610 0.00430  0.01960  0.02170  143 GLY B N   
3428 C CA  . GLY B 143 ? 0.46990 0.38690 0.59820 0.00300  0.01590  0.00940  143 GLY B CA  
3429 C C   . GLY B 143 ? 0.45910 0.37790 0.57070 0.00160  0.01220  0.00060  143 GLY B C   
3430 O O   . GLY B 143 ? 0.50910 0.42520 0.62230 -0.00000 0.00870  -0.00970 143 GLY B O   
3431 N N   . SER B 144 ? 0.44860 0.37240 0.54530 0.00210  0.01280  0.00440  144 SER B N   
3432 C CA  . SER B 144 ? 0.50530 0.43110 0.58660 0.00110  0.00940  -0.00230 144 SER B CA  
3433 C C   . SER B 144 ? 0.46010 0.38680 0.54520 -0.00150 0.00640  -0.00440 144 SER B C   
3434 O O   . SER B 144 ? 0.42500 0.35330 0.50070 -0.00270 0.00270  -0.01040 144 SER B O   
3435 C CB  . SER B 144 ? 0.47290 0.40320 0.53820 0.00280  0.01120  0.00230  144 SER B CB  
3436 O OG  . SER B 144 ? 0.47330 0.40710 0.54120 0.00320  0.01410  0.01040  144 SER B OG  
3437 N N   . ALA B 145 ? 0.47900 0.40550 0.57840 -0.00230 0.00790  0.00100  145 ALA B N   
3438 C CA  . ALA B 145 ? 0.44690 0.37480 0.55190 -0.00470 0.00490  -0.00100 145 ALA B CA  
3439 C C   . ALA B 145 ? 0.41480 0.34090 0.52160 -0.00710 -0.00050 -0.01180 145 ALA B C   
3440 O O   . ALA B 145 ? 0.47900 0.40140 0.59130 -0.00730 -0.00110 -0.01750 145 ALA B O   
3441 C CB  . ALA B 145 ? 0.42560 0.35350 0.54900 -0.00560 0.00760  0.00610  145 ALA B CB  
3442 N N   . GLY B 146 ? 0.40210 0.33170 0.50270 -0.00870 -0.00450 -0.01490 146 GLY B N   
3443 C CA  . GLY B 146 ? 0.43080 0.36150 0.52970 -0.01090 -0.01010 -0.02480 146 GLY B CA  
3444 C C   . GLY B 146 ? 0.47750 0.41100 0.55730 -0.01000 -0.01180 -0.02890 146 GLY B C   
3445 O O   . GLY B 146 ? 0.42520 0.36230 0.50030 -0.01190 -0.01670 -0.03610 146 GLY B O   
3446 N N   . SER B 147 ? 0.45270 0.38550 0.52190 -0.00730 -0.00790 -0.02450 147 SER B N   
3447 C CA  . SER B 147 ? 0.46290 0.39910 0.51490 -0.00670 -0.00940 -0.02670 147 SER B CA  
3448 C C   . SER B 147 ? 0.50070 0.44130 0.54750 -0.00780 -0.01250 -0.02420 147 SER B C   
3449 O O   . SER B 147 ? 0.46960 0.41020 0.52320 -0.00770 -0.01150 -0.01880 147 SER B O   
3450 C CB  . SER B 147 ? 0.44180 0.37690 0.48520 -0.00400 -0.00490 -0.02160 147 SER B CB  
3451 O OG  . SER B 147 ? 0.49120 0.42250 0.54240 -0.00260 -0.00160 -0.02150 147 SER B OG  
3452 N N   . VAL B 148 ? 0.44050 0.38580 0.47630 -0.00860 -0.01620 -0.02760 148 VAL B N   
3453 C CA  . VAL B 148 ? 0.43080 0.38090 0.46380 -0.00970 -0.02000 -0.02510 148 VAL B CA  
3454 C C   . VAL B 148 ? 0.48840 0.44070 0.50880 -0.00840 -0.01930 -0.02070 148 VAL B C   
3455 O O   . VAL B 148 ? 0.50240 0.45420 0.51360 -0.00730 -0.01720 -0.02170 148 VAL B O   
3456 C CB  . VAL B 148 ? 0.46560 0.42150 0.49930 -0.01250 -0.02620 -0.03160 148 VAL B CB  
3457 C CG1 . VAL B 148 ? 0.49300 0.44690 0.54310 -0.01440 -0.02770 -0.03590 148 VAL B CG1 
3458 C CG2 . VAL B 148 ? 0.46180 0.42160 0.48370 -0.01270 -0.02750 -0.03830 148 VAL B CG2 
3459 N N   . GLY B 149 ? 0.45740 0.41200 0.47900 -0.00860 -0.02100 -0.01580 149 GLY B N   
3460 C CA  . GLY B 149 ? 0.47470 0.43140 0.48750 -0.00780 -0.02120 -0.01140 149 GLY B CA  
3461 C C   . GLY B 149 ? 0.49330 0.45720 0.50380 -0.00960 -0.02720 -0.01120 149 GLY B C   
3462 O O   . GLY B 149 ? 0.51960 0.48640 0.53760 -0.01110 -0.03090 -0.01280 149 GLY B O   
3463 N N   . PHE B 150 ? 0.46360 0.43140 0.46420 -0.00960 -0.02840 -0.00890 150 PHE B N   
3464 C CA  . PHE B 150 ? 0.51880 0.49570 0.51520 -0.01140 -0.03420 -0.00810 150 PHE B CA  
3465 C C   . PHE B 150 ? 0.51750 0.49740 0.50670 -0.01090 -0.03420 -0.00140 150 PHE B C   
3466 O O   . PHE B 150 ? 0.46870 0.44420 0.45360 -0.00960 -0.03000 -0.00010 150 PHE B O   
3467 C CB  . PHE B 150 ? 0.48040 0.46260 0.47060 -0.01310 -0.03650 -0.01620 150 PHE B CB  
3468 C CG  . PHE B 150 ? 0.52140 0.50250 0.50180 -0.01210 -0.03270 -0.01920 150 PHE B CG  
3469 C CD1 . PHE B 150 ? 0.54230 0.51540 0.52570 -0.01070 -0.02790 -0.02300 150 PHE B CD1 
3470 C CD2 . PHE B 150 ? 0.55810 0.54700 0.52710 -0.01260 -0.03400 -0.01750 150 PHE B CD2 
3471 C CE1 . PHE B 150 ? 0.52990 0.50250 0.50570 -0.00960 -0.02450 -0.02540 150 PHE B CE1 
3472 C CE2 . PHE B 150 ? 0.53160 0.51990 0.49250 -0.01160 -0.03010 -0.01990 150 PHE B CE2 
3473 C CZ  . PHE B 150 ? 0.52950 0.50940 0.49420 -0.01000 -0.02540 -0.02410 150 PHE B CZ  
3474 N N   . ASN B 151 ? 0.51090 0.49910 0.49960 -0.01210 -0.03930 0.00310  151 ASN B N   
3475 C CA  . ASN B 151 ? 0.55670 0.55050 0.53880 -0.01230 -0.04060 0.00990  151 ASN B CA  
3476 C C   . ASN B 151 ? 0.58810 0.59440 0.56130 -0.01450 -0.04550 0.00800  151 ASN B C   
3477 O O   . ASN B 151 ? 0.56890 0.57950 0.54390 -0.01580 -0.04910 0.00230  151 ASN B O   
3478 C CB  . ASN B 151 ? 0.53090 0.52430 0.52230 -0.01160 -0.04220 0.01920  151 ASN B CB  
3479 C CG  . ASN B 151 ? 0.56480 0.54720 0.56300 -0.00950 -0.03680 0.02080  151 ASN B CG  
3480 O OD1 . ASN B 151 ? 0.58480 0.56440 0.57860 -0.00890 -0.03370 0.02240  151 ASN B OD1 
3481 N ND2 . ASN B 151 ? 0.51130 0.48860 0.52070 -0.00830 -0.03560 0.02010  151 ASN B ND2 
3482 N N   . ILE B 152 ? 0.59430 0.60740 0.55790 -0.01490 -0.04560 0.01220  152 ILE B N   
3483 C CA  . ILE B 152 ? 0.63670 0.66440 0.59040 -0.01680 -0.05000 0.01120  152 ILE B CA  
3484 C C   . ILE B 152 ? 0.72130 0.75800 0.67470 -0.01740 -0.05340 0.02370  152 ILE B C   
3485 O O   . ILE B 152 ? 0.74430 0.77630 0.70030 -0.01630 -0.05050 0.03160  152 ILE B O   
3486 C CB  . ILE B 152 ? 0.64070 0.67130 0.58220 -0.01690 -0.04670 0.00390  152 ILE B CB  
3487 C CG1 . ILE B 152 ? 0.61660 0.63800 0.56160 -0.01620 -0.04370 -0.00780 152 ILE B CG1 
3488 C CG2 . ILE B 152 ? 0.69160 0.73960 0.62210 -0.01900 -0.05110 0.00250  152 ILE B CG2 
3489 C CD1 . ILE B 152 ? 0.71390 0.73840 0.64950 -0.01610 -0.04070 -0.01700 152 ILE B CD1 
3490 N N   . ASP B 153 ? 0.78910 0.83860 0.74130 -0.01910 -0.05980 0.02600  153 ASP B N   
3491 C CA  . ASP B 153 ? 0.92080 0.98220 0.87200 -0.01990 -0.06390 0.03870  153 ASP B CA  
3492 C C   . ASP B 153 ? 0.93300 1.01290 0.87010 -0.02210 -0.06810 0.03590  153 ASP B C   
3493 O O   . ASP B 153 ? 0.93580 1.02310 0.87200 -0.02360 -0.07280 0.02900  153 ASP B O   
3494 C CB  . ASP B 153 ? 0.93840 0.99940 0.90390 -0.01950 -0.06840 0.04630  153 ASP B CB  
3495 C CG  . ASP B 153 ? 1.14780 1.21380 1.11860 -0.01910 -0.07020 0.06190  153 ASP B CG  
3496 O OD1 . ASP B 153 ? 1.15680 1.22370 1.12160 -0.01900 -0.06700 0.06680  153 ASP B OD1 
3497 O OD2 . ASP B 153 ? 1.25020 1.31970 1.23230 -0.01890 -0.07480 0.06960  153 ASP B OD2 
3498 N N   . TYR B 154 ? 0.99350 1.08220 0.92040 -0.02250 -0.06640 0.04150  154 TYR B N   
3499 C CA  . TYR B 154 ? 1.01110 1.11860 0.92230 -0.02440 -0.06880 0.03810  154 TYR B CA  
3500 C C   . TYR B 154 ? 0.96170 1.06610 0.86650 -0.02460 -0.06640 0.02020  154 TYR B C   
3501 O O   . TYR B 154 ? 1.00880 1.10280 0.91200 -0.02320 -0.06010 0.01420  154 TYR B O   
3502 C CB  . TYR B 154 ? 1.07510 1.20010 0.98560 -0.02630 -0.07710 0.04430  154 TYR B CB  
3503 C CG  . TYR B 154 ? 1.27500 1.39790 1.19920 -0.02550 -0.07990 0.06090  154 TYR B CG  
3504 C CD1 . TYR B 154 ? 1.27630 1.40260 1.20120 -0.02510 -0.07820 0.07580  154 TYR B CD1 
3505 C CD2 . TYR B 154 ? 1.23670 1.35360 1.17500 -0.02510 -0.08370 0.06170  154 TYR B CD2 
3506 C CE1 . TYR B 154 ? 1.33780 1.46100 1.27800 -0.02420 -0.08050 0.09080  154 TYR B CE1 
3507 C CE2 . TYR B 154 ? 1.29630 1.41080 1.24900 -0.02400 -0.08590 0.07630  154 TYR B CE2 
3508 C CZ  . TYR B 154 ? 1.42220 1.53960 1.37630 -0.02340 -0.08430 0.09070  154 TYR B CZ  
3509 O OH  . TYR B 154 ? 1.51370 1.62810 1.48450 -0.02220 -0.08630 0.10500  154 TYR B OH  
3510 N N   . ASP B 155 ? 0.93740 1.04990 0.84090 -0.02630 -0.07160 0.01140  155 ASP B N   
3511 C CA  . ASP B 155 ? 0.95840 1.06570 0.86020 -0.02640 -0.06960 -0.00610 155 ASP B CA  
3512 C C   . ASP B 155 ? 0.86210 0.95950 0.77770 -0.02680 -0.07240 -0.01180 155 ASP B C   
3513 O O   . ASP B 155 ? 0.81770 0.91330 0.73410 -0.02770 -0.07260 -0.02610 155 ASP B O   
3514 C CB  . ASP B 155 ? 1.04280 1.16950 0.92980 -0.02850 -0.07220 -0.01570 155 ASP B CB  
3515 C CG  . ASP B 155 ? 1.16710 1.30100 1.04070 -0.02760 -0.06680 -0.01500 155 ASP B CG  
3516 O OD1 . ASP B 155 ? 1.07520 1.19520 0.95130 -0.02550 -0.05990 -0.01550 155 ASP B OD1 
3517 O OD2 . ASP B 155 ? 1.22220 1.37680 1.08250 -0.02920 -0.06940 -0.01390 155 ASP B OD2 
3518 N N   . CYS B 156 ? 0.80080 0.89160 0.72860 -0.02610 -0.07430 -0.00100 156 CYS B N   
3519 C CA  . CYS B 156 ? 0.71810 0.79980 0.66040 -0.02630 -0.07650 -0.00420 156 CYS B CA  
3520 C C   . CYS B 156 ? 0.68980 0.75100 0.64190 -0.02370 -0.06940 -0.00500 156 CYS B C   
3521 O O   . CYS B 156 ? 0.63220 0.68620 0.58690 -0.02180 -0.06580 0.00460  156 CYS B O   
3522 C CB  . CYS B 156 ? 0.70280 0.79180 0.65330 -0.02680 -0.08270 0.00780  156 CYS B CB  
3523 S SG  . CYS B 156 ? 0.77360 0.85540 0.74300 -0.02740 -0.08620 0.00400  156 CYS B SG  
3524 N N   . VAL B 157 ? 0.63990 0.69250 0.59750 -0.02390 -0.06750 -0.01650 157 VAL B N   
3525 C CA  . VAL B 157 ? 0.59600 0.63110 0.56270 -0.02170 -0.06120 -0.01770 157 VAL B CA  
3526 C C   . VAL B 157 ? 0.58320 0.61260 0.56520 -0.02150 -0.06300 -0.01330 157 VAL B C   
3527 O O   . VAL B 157 ? 0.56810 0.60120 0.55690 -0.02350 -0.06730 -0.01850 157 VAL B O   
3528 C CB  . VAL B 157 ? 0.53550 0.56450 0.50230 -0.02180 -0.05790 -0.03080 157 VAL B CB  
3529 C CG1 . VAL B 157 ? 0.52900 0.54170 0.50470 -0.01940 -0.05140 -0.02960 157 VAL B CG1 
3530 C CG2 . VAL B 157 ? 0.57290 0.60870 0.52510 -0.02170 -0.05580 -0.03650 157 VAL B CG2 
3531 N N   . SER B 158 ? 0.54560 0.56620 0.53390 -0.01930 -0.05930 -0.00490 158 SER B N   
3532 C CA  . SER B 158 ? 0.52300 0.53760 0.52640 -0.01860 -0.05950 -0.00110 158 SER B CA  
3533 C C   . SER B 158 ? 0.51820 0.51960 0.52710 -0.01700 -0.05290 -0.00560 158 SER B C   
3534 O O   . SER B 158 ? 0.52280 0.51680 0.52910 -0.01490 -0.04750 -0.00250 158 SER B O   
3535 C CB  . SER B 158 ? 0.54080 0.55540 0.54870 -0.01700 -0.05970 0.01060  158 SER B CB  
3536 O OG  . SER B 158 ? 0.62050 0.64850 0.62600 -0.01860 -0.06650 0.01590  158 SER B OG  
3537 N N   . PHE B 159 ? 0.52900 0.52810 0.54560 -0.01820 -0.05350 -0.01260 159 PHE B N   
3538 C CA  . PHE B 159 ? 0.50090 0.48880 0.52480 -0.01680 -0.04760 -0.01530 159 PHE B CA  
3539 C C   . PHE B 159 ? 0.52730 0.51090 0.56300 -0.01530 -0.04560 -0.00830 159 PHE B C   
3540 O O   . PHE B 159 ? 0.52130 0.50950 0.56640 -0.01630 -0.04970 -0.00590 159 PHE B O   
3541 C CB  . PHE B 159 ? 0.50530 0.49270 0.53580 -0.01890 -0.04900 -0.02470 159 PHE B CB  
3542 C CG  . PHE B 159 ? 0.50410 0.49520 0.52440 -0.02000 -0.05000 -0.03340 159 PHE B CG  
3543 C CD1 . PHE B 159 ? 0.49900 0.48360 0.51350 -0.01830 -0.04440 -0.03600 159 PHE B CD1 
3544 C CD2 . PHE B 159 ? 0.52490 0.52680 0.54210 -0.02280 -0.05650 -0.03950 159 PHE B CD2 
3545 C CE1 . PHE B 159 ? 0.49460 0.48290 0.50030 -0.01890 -0.04470 -0.04460 159 PHE B CE1 
3546 C CE2 . PHE B 159 ? 0.53550 0.54180 0.54310 -0.02370 -0.05690 -0.04870 159 PHE B CE2 
3547 C CZ  . PHE B 159 ? 0.53660 0.53590 0.53860 -0.02160 -0.05080 -0.05130 159 PHE B CZ  
3548 N N   . CYS B 160 ? 0.48060 0.45630 0.51640 -0.01290 -0.03930 -0.00540 160 CYS B N   
3549 C CA  . CYS B 160 ? 0.49880 0.47130 0.54490 -0.01120 -0.03670 0.00010  160 CYS B CA  
3550 C C   . CYS B 160 ? 0.48450 0.44990 0.53670 -0.00990 -0.03050 -0.00110 160 CYS B C   
3551 O O   . CYS B 160 ? 0.50350 0.46780 0.56570 -0.00870 -0.02820 0.00250  160 CYS B O   
3552 C CB  . CYS B 160 ? 0.47990 0.45180 0.52200 -0.00920 -0.03530 0.00630  160 CYS B CB  
3553 S SG  . CYS B 160 ? 0.51610 0.48260 0.54500 -0.00790 -0.03010 0.00510  160 CYS B SG  
3554 N N   . TYR B 161 ? 0.44810 0.40960 0.49570 -0.01000 -0.02770 -0.00550 161 TYR B N   
3555 C CA  . TYR B 161 ? 0.45010 0.40620 0.50300 -0.00850 -0.02170 -0.00470 161 TYR B CA  
3556 C C   . TYR B 161 ? 0.47650 0.43010 0.53160 -0.00970 -0.02120 -0.00990 161 TYR B C   
3557 O O   . TYR B 161 ? 0.46250 0.41680 0.50980 -0.01060 -0.02330 -0.01480 161 TYR B O   
3558 C CB  . TYR B 161 ? 0.42840 0.38140 0.47250 -0.00610 -0.01690 -0.00200 161 TYR B CB  
3559 C CG  . TYR B 161 ? 0.41960 0.36890 0.46640 -0.00450 -0.01080 -0.00080 161 TYR B CG  
3560 C CD1 . TYR B 161 ? 0.43040 0.38010 0.48510 -0.00320 -0.00710 0.00290  161 TYR B CD1 
3561 C CD2 . TYR B 161 ? 0.43950 0.38600 0.48170 -0.00430 -0.00850 -0.00310 161 TYR B CD2 
3562 C CE1 . TYR B 161 ? 0.42900 0.37760 0.48540 -0.00180 -0.00140 0.00480  161 TYR B CE1 
3563 C CE2 . TYR B 161 ? 0.41650 0.36120 0.46140 -0.00280 -0.00310 -0.00050 161 TYR B CE2 
3564 C CZ  . TYR B 161 ? 0.45940 0.40570 0.51140 -0.00170 0.00030  0.00360  161 TYR B CZ  
3565 O OH  . TYR B 161 ? 0.43730 0.38420 0.49140 -0.00030 0.00570  0.00710  161 TYR B OH  
3566 N N   . MET B 162 ? 0.42670 0.37800 0.49400 -0.00990 -0.01860 -0.00890 162 MET B N   
3567 C CA  . MET B 162 ? 0.45220 0.39950 0.52410 -0.01030 -0.01650 -0.01210 162 MET B CA  
3568 C C   . MET B 162 ? 0.46310 0.40750 0.53860 -0.00810 -0.00980 -0.00630 162 MET B C   
3569 O O   . MET B 162 ? 0.44620 0.39220 0.52930 -0.00760 -0.00750 -0.00140 162 MET B O   
3570 C CB  . MET B 162 ? 0.45720 0.40530 0.54300 -0.01310 -0.02010 -0.01620 162 MET B CB  
3571 C CG  . MET B 162 ? 0.43090 0.37380 0.52580 -0.01360 -0.01770 -0.01930 162 MET B CG  
3572 S SD  . MET B 162 ? 0.55180 0.49600 0.66130 -0.01770 -0.02380 -0.02780 162 MET B SD  
3573 C CE  . MET B 162 ? 0.51620 0.46260 0.61140 -0.01840 -0.02800 -0.03870 162 MET B CE  
3574 N N   . HIS B 163 ? 0.43370 0.37490 0.50450 -0.00690 -0.00660 -0.00670 163 HIS B N   
3575 C CA  . HIS B 163 ? 0.45100 0.39130 0.52300 -0.00470 -0.00060 -0.00060 163 HIS B CA  
3576 C C   . HIS B 163 ? 0.43880 0.37820 0.52730 -0.00550 0.00170  0.00270  163 HIS B C   
3577 O O   . HIS B 163 ? 0.41990 0.35640 0.51750 -0.00710 -0.00040 -0.00110 163 HIS B O   
3578 C CB  . HIS B 163 ? 0.45140 0.38960 0.51410 -0.00310 0.00160  -0.00130 163 HIS B CB  
3579 C CG  . HIS B 163 ? 0.38160 0.32100 0.44350 -0.00100 0.00710  0.00530  163 HIS B CG  
3580 N ND1 . HIS B 163 ? 0.39790 0.34090 0.45570 0.00020  0.00960  0.00900  163 HIS B ND1 
3581 C CD2 . HIS B 163 ? 0.39950 0.33810 0.46540 0.00020  0.01060  0.00900  163 HIS B CD2 
3582 C CE1 . HIS B 163 ? 0.40020 0.34570 0.45810 0.00180  0.01430  0.01430  163 HIS B CE1 
3583 N NE2 . HIS B 163 ? 0.44920 0.39220 0.51160 0.00190  0.01490  0.01520  163 HIS B NE2 
3584 N N   . HIS B 164 ? 0.43180 0.37400 0.52460 -0.00420 0.00630  0.00970  164 HIS B N   
3585 C CA  . HIS B 164 ? 0.42710 0.36980 0.53550 -0.00460 0.00970  0.01530  164 HIS B CA  
3586 C C   . HIS B 164 ? 0.38460 0.32960 0.49050 -0.00230 0.01570  0.02270  164 HIS B C   
3587 O O   . HIS B 164 ? 0.42150 0.36470 0.53670 -0.00230 0.01750  0.02620  164 HIS B O   
3588 C CB  . HIS B 164 ? 0.40190 0.34860 0.52090 -0.00570 0.00980  0.01810  164 HIS B CB  
3589 C CG  . HIS B 164 ? 0.43510 0.38060 0.56130 -0.00850 0.00360  0.01220  164 HIS B CG  
3590 N ND1 . HIS B 164 ? 0.42640 0.37190 0.57080 -0.01100 0.00230  0.01270  164 HIS B ND1 
3591 C CD2 . HIS B 164 ? 0.44100 0.38670 0.55880 -0.00930 -0.00180 0.00620  164 HIS B CD2 
3592 C CE1 . HIS B 164 ? 0.42100 0.36690 0.56700 -0.01330 -0.00410 0.00620  164 HIS B CE1 
3593 N NE2 . HIS B 164 ? 0.43970 0.38630 0.56940 -0.01220 -0.00670 0.00270  164 HIS B NE2 
3594 N N   . MET B 165 ? 0.44730 0.39690 0.54200 -0.00030 0.01870  0.02510  165 MET B N   
3595 C CA  . MET B 165 ? 0.43950 0.39450 0.53380 0.00160  0.02450  0.03290  165 MET B CA  
3596 C C   . MET B 165 ? 0.39830 0.35720 0.47590 0.00370  0.02660  0.03230  165 MET B C   
3597 O O   . MET B 165 ? 0.43360 0.39130 0.50130 0.00390  0.02430  0.02660  165 MET B O   
3598 C CB  . MET B 165 ? 0.43240 0.39330 0.53930 0.00120  0.02820  0.03900  165 MET B CB  
3599 C CG  . MET B 165 ? 0.42930 0.39300 0.53220 0.00160  0.02770  0.03570  165 MET B CG  
3600 S SD  . MET B 165 ? 0.53270 0.50280 0.65430 0.00070  0.03150  0.04250  165 MET B SD  
3601 C CE  . MET B 165 ? 0.46760 0.44450 0.58030 0.00300  0.03470  0.04060  165 MET B CE  
3602 N N   . GLU B 166 ? 0.42410 0.38880 0.49990 0.00530  0.03110  0.03880  166 GLU B N   
3603 C CA  . GLU B 166 ? 0.47230 0.44270 0.53370 0.00710  0.03340  0.03840  166 GLU B CA  
3604 C C   . GLU B 166 ? 0.48100 0.46170 0.54360 0.00820  0.03890  0.04360  166 GLU B C   
3605 O O   . GLU B 166 ? 0.48240 0.46750 0.55500 0.00820  0.04210  0.05150  166 GLU B O   
3606 C CB  . GLU B 166 ? 0.44570 0.41630 0.50090 0.00810  0.03360  0.04080  166 GLU B CB  
3607 C CG  . GLU B 166 ? 0.47200 0.44970 0.51280 0.00960  0.03560  0.04000  166 GLU B CG  
3608 C CD  . GLU B 166 ? 0.52090 0.49810 0.55520 0.01040  0.03450  0.04110  166 GLU B CD  
3609 O OE1 . GLU B 166 ? 0.50790 0.47730 0.54090 0.00980  0.03080  0.03620  166 GLU B OE1 
3610 O OE2 . GLU B 166 ? 0.56330 0.54910 0.59470 0.01170  0.03740  0.04740  166 GLU B OE2 
3611 N N   . LEU B 167 ? 0.46030 0.44480 0.51390 0.00920  0.04000  0.03900  167 LEU B N   
3612 C CA  . LEU B 167 ? 0.46080 0.45590 0.51380 0.01050  0.04540  0.04140  167 LEU B CA  
3613 C C   . LEU B 167 ? 0.50270 0.50690 0.54460 0.01190  0.04850  0.04410  167 LEU B C   
3614 O O   . LEU B 167 ? 0.52080 0.52170 0.55500 0.01190  0.04580  0.04290  167 LEU B O   
3615 C CB  . LEU B 167 ? 0.45980 0.45400 0.51080 0.01090  0.04500  0.03380  167 LEU B CB  
3616 C CG  . LEU B 167 ? 0.45640 0.44470 0.52010 0.00960  0.04230  0.03270  167 LEU B CG  
3617 C CD1 . LEU B 167 ? 0.46940 0.45560 0.53170 0.01020  0.04080  0.02550  167 LEU B CD1 
3618 C CD2 . LEU B 167 ? 0.51280 0.50780 0.59020 0.00950  0.04650  0.03950  167 LEU B CD2 
3619 N N   . PRO B 168 ? 0.48180 0.49860 0.52270 0.01310  0.05400  0.04800  168 PRO B N   
3620 C CA  . PRO B 168 ? 0.52560 0.55380 0.55610 0.01420  0.05680  0.05190  168 PRO B CA  
3621 C C   . PRO B 168 ? 0.55510 0.58340 0.57070 0.01470  0.05470  0.04360  168 PRO B C   
3622 O O   . PRO B 168 ? 0.54810 0.58330 0.55600 0.01520  0.05500  0.04700  168 PRO B O   
3623 C CB  . PRO B 168 ? 0.58020 0.62280 0.61230 0.01530  0.06330  0.05590  168 PRO B CB  
3624 C CG  . PRO B 168 ? 0.52890 0.56720 0.57780 0.01440  0.06410  0.06040  168 PRO B CG  
3625 C CD  . PRO B 168 ? 0.45460 0.47740 0.50670 0.01320  0.05830  0.05190  168 PRO B CD  
3626 N N   . THR B 169 ? 0.50030 0.52280 0.51310 0.01450  0.05290  0.03350  169 THR B N   
3627 C CA  . THR B 169 ? 0.54220 0.56400 0.54330 0.01450  0.05070  0.02570  169 THR B CA  
3628 C C   . THR B 169 ? 0.56480 0.57550 0.56410 0.01340  0.04530  0.02510  169 THR B C   
3629 O O   . THR B 169 ? 0.53780 0.54720 0.52860 0.01310  0.04300  0.01930  169 THR B O   
3630 C CB  . THR B 169 ? 0.50720 0.52680 0.50850 0.01480  0.05120  0.01590  169 THR B CB  
3631 O OG1 . THR B 169 ? 0.55550 0.56440 0.56730 0.01420  0.04870  0.01530  169 THR B OG1 
3632 C CG2 . THR B 169 ? 0.59510 0.62800 0.59660 0.01640  0.05740  0.01480  169 THR B CG2 
3633 N N   . GLY B 170 ? 0.49560 0.49880 0.50320 0.01270  0.04310  0.03020  170 GLY B N   
3634 C CA  . GLY B 170 ? 0.51400 0.50820 0.51960 0.01190  0.03860  0.02900  170 GLY B CA  
3635 C C   . GLY B 170 ? 0.53840 0.52190 0.54590 0.01070  0.03460  0.02250  170 GLY B C   
3636 O O   . GLY B 170 ? 0.59410 0.57190 0.59720 0.01010  0.03110  0.01970  170 GLY B O   
3637 N N   . VAL B 171 ? 0.47670 0.45910 0.48950 0.01060  0.03520  0.01980  171 VAL B N   
3638 C CA  . VAL B 171 ? 0.45590 0.42950 0.47220 0.00950  0.03110  0.01540  171 VAL B CA  
3639 C C   . VAL B 171 ? 0.44480 0.41450 0.47250 0.00850  0.02970  0.01870  171 VAL B C   
3640 O O   . VAL B 171 ? 0.45530 0.42850 0.48980 0.00870  0.03230  0.02440  171 VAL B O   
3641 C CB  . VAL B 171 ? 0.43750 0.41210 0.45440 0.01000  0.03200  0.01040  171 VAL B CB  
3642 C CG1 . VAL B 171 ? 0.49200 0.47030 0.49940 0.01060  0.03320  0.00590  171 VAL B CG1 
3643 C CG2 . VAL B 171 ? 0.38440 0.36500 0.41000 0.01100  0.03620  0.01230  171 VAL B CG2 
3644 N N   . HIS B 172 ? 0.42320 0.38650 0.45390 0.00740  0.02550  0.01540  172 HIS B N   
3645 C CA  . HIS B 172 ? 0.45220 0.41120 0.49170 0.00590  0.02280  0.01680  172 HIS B CA  
3646 C C   . HIS B 172 ? 0.46320 0.42140 0.51160 0.00510  0.02090  0.01560  172 HIS B C   
3647 O O   . HIS B 172 ? 0.48000 0.43830 0.52630 0.00560  0.02010  0.01290  172 HIS B O   
3648 C CB  . HIS B 172 ? 0.43700 0.39050 0.47070 0.00490  0.01850  0.01360  172 HIS B CB  
3649 C CG  . HIS B 172 ? 0.46750 0.42230 0.49500 0.00590  0.02040  0.01550  172 HIS B CG  
3650 N ND1 . HIS B 172 ? 0.50030 0.45570 0.51680 0.00640  0.02010  0.01320  172 HIS B ND1 
3651 C CD2 . HIS B 172 ? 0.45670 0.41340 0.48880 0.00650  0.02300  0.02040  172 HIS B CD2 
3652 C CE1 . HIS B 172 ? 0.48160 0.43920 0.49560 0.00730  0.02190  0.01620  172 HIS B CE1 
3653 N NE2 . HIS B 172 ? 0.52000 0.47860 0.54350 0.00750  0.02370  0.02100  172 HIS B NE2 
3654 N N   . ALA B 173 ? 0.43690 0.39440 0.49650 0.00400  0.02020  0.01800  173 ALA B N   
3655 C CA  . ALA B 173 ? 0.40950 0.36770 0.47980 0.00310  0.01860  0.01780  173 ALA B CA  
3656 C C   . ALA B 173 ? 0.38960 0.34380 0.46720 0.00070  0.01370  0.01630  173 ALA B C   
3657 O O   . ALA B 173 ? 0.41090 0.36290 0.49150 -0.00010 0.01380  0.01720  173 ALA B O   
3658 C CB  . ALA B 173 ? 0.43340 0.39800 0.51300 0.00410  0.02410  0.02260  173 ALA B CB  
3659 N N   . GLY B 174 ? 0.39920 0.35280 0.48020 -0.00040 0.00920  0.01370  174 GLY B N   
3660 C CA  . GLY B 174 ? 0.40100 0.35250 0.48870 -0.00300 0.00410  0.01110  174 GLY B CA  
3661 C C   . GLY B 174 ? 0.39630 0.35040 0.49170 -0.00410 -0.00010 0.01040  174 GLY B C   
3662 O O   . GLY B 174 ? 0.40690 0.36410 0.50610 -0.00270 0.00210  0.01300  174 GLY B O   
3663 N N   . THR B 175 ? 0.38420 0.33750 0.48200 -0.00660 -0.00610 0.00660  175 THR B N   
3664 C CA  . THR B 175 ? 0.43930 0.39640 0.54650 -0.00820 -0.01090 0.00630  175 THR B CA  
3665 C C   . THR B 175 ? 0.45150 0.40990 0.54930 -0.00920 -0.01730 0.00290  175 THR B C   
3666 O O   . THR B 175 ? 0.47790 0.43420 0.56350 -0.00910 -0.01790 -0.00010 175 THR B O   
3667 C CB  . THR B 175 ? 0.43530 0.39300 0.55760 -0.01100 -0.01300 0.00510  175 THR B CB  
3668 O OG1 . THR B 175 ? 0.43850 0.39340 0.55780 -0.01310 -0.01660 -0.00110 175 THR B OG1 
3669 C CG2 . THR B 175 ? 0.41550 0.37330 0.54930 -0.01030 -0.00650 0.01030  175 THR B CG2 
3670 N N   . ASP B 176 ? 0.42710 0.39030 0.53120 -0.01010 -0.02190 0.00390  176 ASP B N   
3671 C CA  . ASP B 176 ? 0.46890 0.43570 0.56690 -0.01200 -0.02910 0.00070  176 ASP B CA  
3672 C C   . ASP B 176 ? 0.43880 0.40630 0.54170 -0.01520 -0.03300 -0.00540 176 ASP B C   
3673 O O   . ASP B 176 ? 0.44720 0.41140 0.55990 -0.01600 -0.03010 -0.00650 176 ASP B O   
3674 C CB  . ASP B 176 ? 0.45810 0.43070 0.56140 -0.01170 -0.03310 0.00490  176 ASP B CB  
3675 C CG  . ASP B 176 ? 0.47900 0.45540 0.60070 -0.01280 -0.03430 0.00680  176 ASP B CG  
3676 O OD1 . ASP B 176 ? 0.44580 0.42190 0.57530 -0.01510 -0.03500 0.00350  176 ASP B OD1 
3677 O OD2 . ASP B 176 ? 0.46090 0.44050 0.58980 -0.01130 -0.03460 0.01150  176 ASP B OD2 
3678 N N   . LEU B 177 ? 0.43740 0.40990 0.53430 -0.01730 -0.03960 -0.00960 177 LEU B N   
3679 C CA  . LEU B 177 ? 0.47330 0.44690 0.57380 -0.02040 -0.04340 -0.01750 177 LEU B CA  
3680 C C   . LEU B 177 ? 0.51500 0.49290 0.63250 -0.02320 -0.04760 -0.01830 177 LEU B C   
3681 O O   . LEU B 177 ? 0.50260 0.48130 0.62640 -0.02610 -0.05080 -0.02560 177 LEU B O   
3682 C CB  . LEU B 177 ? 0.52350 0.50230 0.60980 -0.02180 -0.04860 -0.02320 177 LEU B CB  
3683 C CG  . LEU B 177 ? 0.45110 0.42490 0.52450 -0.02040 -0.04470 -0.02690 177 LEU B CG  
3684 C CD1 . LEU B 177 ? 0.53120 0.49930 0.61250 -0.02150 -0.04260 -0.03420 177 LEU B CD1 
3685 C CD2 . LEU B 177 ? 0.50660 0.47490 0.57240 -0.01690 -0.03820 -0.02010 177 LEU B CD2 
3686 N N   . GLU B 178 ? 0.51250 0.49330 0.63890 -0.02220 -0.04730 -0.01150 178 GLU B N   
3687 C CA  . GLU B 178 ? 0.55210 0.53610 0.69760 -0.02450 -0.04960 -0.01110 178 GLU B CA  
3688 C C   . GLU B 178 ? 0.50310 0.48110 0.66070 -0.02350 -0.04220 -0.00780 178 GLU B C   
3689 O O   . GLU B 178 ? 0.53110 0.51150 0.70610 -0.02530 -0.04290 -0.00630 178 GLU B O   
3690 C CB  . GLU B 178 ? 0.55930 0.55080 0.71050 -0.02380 -0.05310 -0.00490 178 GLU B CB  
3691 C CG  . GLU B 178 ? 0.67780 0.67820 0.82140 -0.02570 -0.06180 -0.00720 178 GLU B CG  
3692 C CD  . GLU B 178 ? 0.96690 0.97400 1.11510 -0.02410 -0.06450 0.00090  178 GLU B CD  
3693 O OE1 . GLU B 178 ? 0.82040 0.82530 0.98010 -0.02170 -0.05970 0.00680  178 GLU B OE1 
3694 O OE2 . GLU B 178 ? 1.16240 1.17740 1.30230 -0.02480 -0.07110 0.00160  178 GLU B OE2 
3695 N N   . GLY B 179 ? 0.45690 0.42820 0.60610 -0.02080 -0.03530 -0.00580 179 GLY B N   
3696 C CA  . GLY B 179 ? 0.45200 0.41890 0.61040 -0.01980 -0.02810 -0.00200 179 GLY B CA  
3697 C C   . GLY B 179 ? 0.48680 0.45560 0.64940 -0.01690 -0.02240 0.00590  179 GLY B C   
3698 O O   . GLY B 179 ? 0.48400 0.45190 0.65650 -0.01640 -0.01670 0.01010  179 GLY B O   
3699 N N   . ASN B 180 ? 0.45300 0.42530 0.61010 -0.01510 -0.02390 0.00810  180 ASN B N   
3700 C CA  . ASN B 180 ? 0.44230 0.41630 0.60310 -0.01190 -0.01800 0.01400  180 ASN B CA  
3701 C C   . ASN B 180 ? 0.45160 0.42160 0.59780 -0.00880 -0.01220 0.01470  180 ASN B C   
3702 O O   . ASN B 180 ? 0.44710 0.41510 0.57970 -0.00810 -0.01470 0.01250  180 ASN B O   
3703 C CB  . ASN B 180 ? 0.50110 0.48060 0.66630 -0.01130 -0.02240 0.01590  180 ASN B CB  
3704 C CG  . ASN B 180 ? 0.58830 0.57360 0.77100 -0.01420 -0.02730 0.01620  180 ASN B CG  
3705 O OD1 . ASN B 180 ? 0.64080 0.63120 0.82570 -0.01560 -0.03470 0.01550  180 ASN B OD1 
3706 N ND2 . ASN B 180 ? 0.55780 0.54310 0.75340 -0.01530 -0.02340 0.01770  180 ASN B ND2 
3707 N N   . PHE B 181 ? 0.42270 0.39260 0.57180 -0.00690 -0.00460 0.01820  181 PHE B N   
3708 C CA  . PHE B 181 ? 0.45910 0.42650 0.59450 -0.00410 0.00070  0.01850  181 PHE B CA  
3709 C C   . PHE B 181 ? 0.43690 0.40510 0.56640 -0.00180 0.00040  0.01820  181 PHE B C   
3710 O O   . PHE B 181 ? 0.39720 0.36920 0.53670 -0.00100 -0.00030 0.01990  181 PHE B O   
3711 C CB  . PHE B 181 ? 0.44600 0.41600 0.58610 -0.00250 0.00890  0.02290  181 PHE B CB  
3712 C CG  . PHE B 181 ? 0.44850 0.41580 0.58670 -0.00350 0.01120  0.02400  181 PHE B CG  
3713 C CD1 . PHE B 181 ? 0.42310 0.38740 0.54610 -0.00200 0.01340  0.02300  181 PHE B CD1 
3714 C CD2 . PHE B 181 ? 0.37560 0.34290 0.52820 -0.00600 0.01040  0.02600  181 PHE B CD2 
3715 C CE1 . PHE B 181 ? 0.40750 0.36970 0.53010 -0.00260 0.01520  0.02470  181 PHE B CE1 
3716 C CE2 . PHE B 181 ? 0.45410 0.41830 0.60720 -0.00680 0.01220  0.02750  181 PHE B CE2 
3717 C CZ  . PHE B 181 ? 0.40050 0.36190 0.53790 -0.00490 0.01460  0.02690  181 PHE B CZ  
3718 N N   . TYR B 182 ? 0.41230 0.37690 0.52690 -0.00070 0.00090  0.01610  182 TYR B N   
3719 C CA  . TYR B 182 ? 0.38710 0.35180 0.49690 0.00200  0.00350  0.01600  182 TYR B CA  
3720 C C   . TYR B 182 ? 0.40220 0.36960 0.51350 0.00430  0.01160  0.01720  182 TYR B C   
3721 O O   . TYR B 182 ? 0.44550 0.41260 0.55090 0.00420  0.01510  0.01770  182 TYR B O   
3722 C CB  . TYR B 182 ? 0.40060 0.36100 0.49480 0.00200  0.00160  0.01340  182 TYR B CB  
3723 C CG  . TYR B 182 ? 0.39700 0.35670 0.48830 -0.00010 -0.00600 0.01260  182 TYR B CG  
3724 C CD1 . TYR B 182 ? 0.43880 0.40040 0.53420 0.00050  -0.00960 0.01440  182 TYR B CD1 
3725 C CD2 . TYR B 182 ? 0.39170 0.35000 0.47700 -0.00240 -0.00940 0.01010  182 TYR B CD2 
3726 C CE1 . TYR B 182 ? 0.48370 0.44690 0.57560 -0.00140 -0.01680 0.01470  182 TYR B CE1 
3727 C CE2 . TYR B 182 ? 0.43040 0.39030 0.51200 -0.00430 -0.01620 0.00880  182 TYR B CE2 
3728 C CZ  . TYR B 182 ? 0.46870 0.43150 0.55240 -0.00380 -0.01980 0.01160  182 TYR B CZ  
3729 O OH  . TYR B 182 ? 0.45650 0.42280 0.53590 -0.00570 -0.02630 0.01130  182 TYR B OH  
3730 N N   . GLY B 183 ? 0.42150 0.39250 0.54070 0.00640  0.01470  0.01770  183 GLY B N   
3731 C CA  . GLY B 183 ? 0.43340 0.40890 0.55280 0.00880  0.02270  0.01770  183 GLY B CA  
3732 C C   . GLY B 183 ? 0.43620 0.41760 0.56750 0.00830  0.02640  0.02190  183 GLY B C   
3733 O O   . GLY B 183 ? 0.44970 0.43040 0.58880 0.00580  0.02280  0.02430  183 GLY B O   
3734 N N   . PRO B 184 ? 0.45200 0.43970 0.58440 0.01050  0.03380  0.02260  184 PRO B N   
3735 C CA  . PRO B 184 ? 0.45870 0.45380 0.60380 0.01020  0.03840  0.02760  184 PRO B CA  
3736 C C   . PRO B 184 ? 0.43450 0.43080 0.57540 0.00870  0.04080  0.03210  184 PRO B C   
3737 O O   . PRO B 184 ? 0.48360 0.48770 0.62370 0.01000  0.04790  0.03540  184 PRO B O   
3738 C CB  . PRO B 184 ? 0.42810 0.43080 0.57460 0.01360  0.04580  0.02560  184 PRO B CB  
3739 C CG  . PRO B 184 ? 0.47470 0.47470 0.60450 0.01490  0.04680  0.02070  184 PRO B CG  
3740 C CD  . PRO B 184 ? 0.43690 0.42690 0.56070 0.01330  0.03880  0.01840  184 PRO B CD  
3741 N N   . PHE B 185 ? 0.39780 0.38710 0.53600 0.00620  0.03520  0.03220  185 PHE B N   
3742 C CA  . PHE B 185 ? 0.40980 0.39810 0.54470 0.00490  0.03650  0.03600  185 PHE B CA  
3743 C C   . PHE B 185 ? 0.41910 0.40540 0.56910 0.00180  0.03310  0.03920  185 PHE B C   
3744 O O   . PHE B 185 ? 0.43800 0.42150 0.59560 0.00020  0.02750  0.03650  185 PHE B O   
3745 C CB  . PHE B 185 ? 0.44240 0.42380 0.56130 0.00480  0.03300  0.03200  185 PHE B CB  
3746 C CG  . PHE B 185 ? 0.47390 0.45670 0.57990 0.00730  0.03520  0.02800  185 PHE B CG  
3747 C CD1 . PHE B 185 ? 0.45150 0.44240 0.55270 0.00940  0.04230  0.02970  185 PHE B CD1 
3748 C CD2 . PHE B 185 ? 0.43560 0.41280 0.53480 0.00740  0.03050  0.02250  185 PHE B CD2 
3749 C CE1 . PHE B 185 ? 0.45370 0.44650 0.54420 0.01150  0.04440  0.02440  185 PHE B CE1 
3750 C CE2 . PHE B 185 ? 0.44960 0.42790 0.53990 0.00950  0.03290  0.01860  185 PHE B CE2 
3751 C CZ  . PHE B 185 ? 0.46800 0.45390 0.55430 0.01150  0.03980  0.01880  185 PHE B CZ  
3752 N N   . VAL B 186 ? 0.40810 0.39550 0.56230 0.00080  0.03600  0.04480  186 VAL B N   
3753 C CA  . VAL B 186 ? 0.42610 0.41110 0.59670 -0.00230 0.03320  0.04760  186 VAL B CA  
3754 C C   . VAL B 186 ? 0.43340 0.41300 0.60100 -0.00330 0.03250  0.04920  186 VAL B C   
3755 O O   . VAL B 186 ? 0.44630 0.42760 0.60230 -0.00130 0.03620  0.05150  186 VAL B O   
3756 C CB  . VAL B 186 ? 0.43680 0.43040 0.62410 -0.00260 0.03880  0.05530  186 VAL B CB  
3757 C CG1 . VAL B 186 ? 0.37290 0.37110 0.56720 -0.00190 0.03840  0.05300  186 VAL B CG1 
3758 C CG2 . VAL B 186 ? 0.40560 0.40730 0.58550 -0.00010 0.04690  0.06150  186 VAL B CG2 
3759 N N   . ASP B 187 ? 0.42170 0.39520 0.60070 -0.00640 0.02750  0.04740  187 ASP B N   
3760 C CA  . ASP B 187 ? 0.46160 0.42870 0.63990 -0.00720 0.02620  0.04720  187 ASP B CA  
3761 C C   . ASP B 187 ? 0.45370 0.42360 0.64730 -0.00790 0.03110  0.05700  187 ASP B C   
3762 O O   . ASP B 187 ? 0.45620 0.42200 0.66720 -0.01060 0.02900  0.05790  187 ASP B O   
3763 C CB  . ASP B 187 ? 0.44830 0.40760 0.62980 -0.01000 0.01840  0.03850  187 ASP B CB  
3764 C CG  . ASP B 187 ? 0.44700 0.40740 0.64680 -0.01320 0.01480  0.03720  187 ASP B CG  
3765 O OD1 . ASP B 187 ? 0.45060 0.41750 0.66080 -0.01330 0.01770  0.04240  187 ASP B OD1 
3766 O OD2 . ASP B 187 ? 0.42660 0.38170 0.63140 -0.01580 0.00890  0.03030  187 ASP B OD2 
3767 N N   . ARG B 188 ? 0.45080 0.42860 0.63810 -0.00530 0.03790  0.06460  188 ARG B N   
3768 C CA  . ARG B 188 ? 0.43150 0.41420 0.63030 -0.00530 0.04340  0.07610  188 ARG B CA  
3769 C C   . ARG B 188 ? 0.41730 0.40740 0.59900 -0.00200 0.04860  0.08070  188 ARG B C   
3770 O O   . ARG B 188 ? 0.45750 0.45080 0.62280 -0.00000 0.04910  0.07540  188 ARG B O   
3771 C CB  . ARG B 188 ? 0.44180 0.43240 0.65810 -0.00660 0.04710  0.08300  188 ARG B CB  
3772 C CG  . ARG B 188 ? 0.47000 0.46870 0.67530 -0.00430 0.05010  0.08090  188 ARG B CG  
3773 C CD  . ARG B 188 ? 0.45680 0.46150 0.67990 -0.00580 0.05160  0.08360  188 ARG B CD  
3774 N NE  . ARG B 188 ? 0.50930 0.51960 0.75160 -0.00740 0.05620  0.09510  188 ARG B NE  
3775 C CZ  . ARG B 188 ? 0.51930 0.53670 0.77780 -0.00860 0.05890  0.09950  188 ARG B CZ  
3776 N NH1 . ARG B 188 ? 0.45890 0.47690 0.71920 -0.00870 0.05620  0.09270  188 ARG B NH1 
3777 N NH2 . ARG B 188 ? 0.55190 0.57660 0.82690 -0.00970 0.06440  0.11190  188 ARG B NH2 
3778 N N   . GLN B 189 ? 0.47950 0.47280 0.66610 -0.00150 0.05210  0.09050  189 GLN B N   
3779 C CA  . GLN B 189 ? 0.50720 0.50900 0.67800 0.00140  0.05650  0.09550  189 GLN B CA  
3780 C C   . GLN B 189 ? 0.55240 0.56960 0.72280 0.00270  0.06380  0.10380  189 GLN B C   
3781 O O   . GLN B 189 ? 0.55240 0.57940 0.72300 0.00380  0.06870  0.11480  189 GLN B O   
3782 C CB  . GLN B 189 ? 0.49900 0.49780 0.67540 0.00150  0.05650  0.10270  189 GLN B CB  
3783 C CG  . GLN B 189 ? 0.52890 0.51300 0.70610 0.00030  0.04970  0.09290  189 GLN B CG  
3784 C CD  . GLN B 189 ? 0.52900 0.50980 0.70550 0.00150  0.04920  0.09660  189 GLN B CD  
3785 O OE1 . GLN B 189 ? 0.53090 0.50420 0.69710 0.00210  0.04520  0.08780  189 GLN B OE1 
3786 N NE2 . GLN B 189 ? 0.51850 0.50540 0.70700 0.00200  0.05350  0.11020  189 GLN B NE2 
3787 N N   . THR B 190 ? 0.53010 0.55080 0.69960 0.00290  0.06480  0.09850  190 THR B N   
3788 C CA  . THR B 190 ? 0.51740 0.55340 0.68240 0.00480  0.07190  0.10320  190 THR B CA  
3789 C C   . THR B 190 ? 0.53560 0.57540 0.67790 0.00750  0.07260  0.09510  190 THR B C   
3790 O O   . THR B 190 ? 0.52630 0.55620 0.65750 0.00770  0.06730  0.08600  190 THR B O   
3791 C CB  . THR B 190 ? 0.53140 0.57010 0.70960 0.00390  0.07330  0.10180  190 THR B CB  
3792 O OG1 . THR B 190 ? 0.49620 0.52400 0.67090 0.00340  0.06690  0.08930  190 THR B OG1 
3793 C CG2 . THR B 190 ? 0.52750 0.56550 0.73040 0.00090  0.07380  0.11140  190 THR B CG2 
3794 N N   . ALA B 191 ? 0.53310 0.58800 0.66940 0.00950  0.07940  0.09800  191 ALA B N   
3795 C CA  . ALA B 191 ? 0.55340 0.61440 0.66970 0.01200  0.08110  0.09000  191 ALA B CA  
3796 C C   . ALA B 191 ? 0.52760 0.57950 0.64150 0.01220  0.07730  0.07710  191 ALA B C   
3797 O O   . ALA B 191 ? 0.46900 0.52120 0.59480 0.01190  0.07820  0.07590  191 ALA B O   
3798 C CB  . ALA B 191 ? 0.58470 0.66560 0.69790 0.01390  0.08970  0.09550  191 ALA B CB  
3799 N N   . GLN B 192 ? 0.46660 0.50950 0.56770 0.01250  0.07230  0.06840  192 GLN B N   
3800 C CA  . GLN B 192 ? 0.46340 0.49780 0.56230 0.01280  0.06850  0.05730  192 GLN B CA  
3801 C C   . GLN B 192 ? 0.51720 0.55100 0.59810 0.01420  0.06740  0.04950  192 GLN B C   
3802 O O   . GLN B 192 ? 0.46740 0.50220 0.53900 0.01420  0.06670  0.05230  192 GLN B O   
3803 C CB  . GLN B 192 ? 0.47150 0.49110 0.57880 0.01040  0.06090  0.05500  192 GLN B CB  
3804 C CG  . GLN B 192 ? 0.50260 0.52110 0.62920 0.00830  0.06050  0.06190  192 GLN B CG  
3805 C CD  . GLN B 192 ? 0.46210 0.46760 0.59570 0.00580  0.05280  0.05800  192 GLN B CD  
3806 O OE1 . GLN B 192 ? 0.41090 0.41120 0.54390 0.00560  0.04860  0.05090  192 GLN B OE1 
3807 N NE2 . GLN B 192 ? 0.44730 0.44830 0.58780 0.00390  0.05080  0.06270  192 GLN B NE2 
3808 N N   . ALA B 193 ? 0.48400 0.51600 0.56160 0.01550  0.06690  0.04010  193 ALA B N   
3809 C CA  . ALA B 193 ? 0.44720 0.47860 0.50960 0.01650  0.06590  0.03220  193 ALA B CA  
3810 C C   . ALA B 193 ? 0.51200 0.53290 0.57670 0.01650  0.06150  0.02360  193 ALA B C   
3811 O O   . ALA B 193 ? 0.49700 0.51700 0.57320 0.01690  0.06190  0.02240  193 ALA B O   
3812 C CB  . ALA B 193 ? 0.50700 0.55330 0.56120 0.01870  0.07270  0.02960  193 ALA B CB  
3813 N N   . ALA B 194 ? 0.43740 0.45110 0.49210 0.01610  0.05710  0.01850  194 ALA B N   
3814 C CA  . ALA B 194 ? 0.47700 0.48170 0.53300 0.01610  0.05300  0.01120  194 ALA B CA  
3815 C C   . ALA B 194 ? 0.50920 0.51960 0.56740 0.01830  0.05740  0.00440  194 ALA B C   
3816 O O   . ALA B 194 ? 0.49230 0.51300 0.54370 0.01970  0.06270  0.00200  194 ALA B O   
3817 C CB  . ALA B 194 ? 0.46260 0.46090 0.50650 0.01510  0.04870  0.00800  194 ALA B CB  
3818 N N   . GLY B 195 ? 0.48380 0.48850 0.55220 0.01890  0.05540  0.00100  195 GLY B N   
3819 C CA  . GLY B 195 ? 0.52890 0.53780 0.60120 0.02130  0.05950  -0.00660 195 GLY B CA  
3820 C C   . GLY B 195 ? 0.57340 0.58000 0.63580 0.02150  0.05870  -0.01480 195 GLY B C   
3821 O O   . GLY B 195 ? 0.52850 0.52970 0.58130 0.01980  0.05450  -0.01410 195 GLY B O   
3822 N N   . THR B 196 ? 0.56970 0.58060 0.63530 0.02370  0.06290  -0.02320 196 THR B N   
3823 C CA  . THR B 196 ? 0.57450 0.58130 0.63370 0.02350  0.06110  -0.03160 196 THR B CA  
3824 C C   . THR B 196 ? 0.52830 0.52120 0.59310 0.02220  0.05410  -0.03040 196 THR B C   
3825 O O   . THR B 196 ? 0.52070 0.50850 0.59810 0.02260  0.05180  -0.02700 196 THR B O   
3826 C CB  . THR B 196 ? 0.62040 0.63300 0.68450 0.02590  0.06650  -0.04240 196 THR B CB  
3827 O OG1 . THR B 196 ? 0.70160 0.71010 0.78310 0.02770  0.06690  -0.04250 196 THR B OG1 
3828 C CG2 . THR B 196 ? 0.68450 0.71360 0.74150 0.02730  0.07390  -0.04370 196 THR B CG2 
3829 N N   . ASP B 197 ? 0.51120 0.49950 0.56670 0.02050  0.05060  -0.03220 197 ASP B N   
3830 C CA  . ASP B 197 ? 0.57850 0.55550 0.63670 0.01900  0.04410  -0.03020 197 ASP B CA  
3831 C C   . ASP B 197 ? 0.61240 0.58500 0.67720 0.01960  0.04390  -0.03830 197 ASP B C   
3832 O O   . ASP B 197 ? 0.59150 0.56970 0.65760 0.02120  0.04870  -0.04680 197 ASP B O   
3833 C CB  . ASP B 197 ? 0.52910 0.50390 0.57410 0.01660  0.04040  -0.02630 197 ASP B CB  
3834 C CG  . ASP B 197 ? 0.57540 0.54060 0.62250 0.01480  0.03380  -0.02080 197 ASP B CG  
3835 O OD1 . ASP B 197 ? 0.51390 0.47610 0.57180 0.01520  0.03180  -0.01750 197 ASP B OD1 
3836 O OD2 . ASP B 197 ? 0.51840 0.48050 0.55640 0.01300  0.03050  -0.01970 197 ASP B OD2 
3837 N N   . THR B 198 ? 0.56690 0.53000 0.63790 0.01860  0.03860  -0.03540 198 THR B N   
3838 C CA  . THR B 198 ? 0.56720 0.52490 0.64670 0.01890  0.03780  -0.04140 198 THR B CA  
3839 C C   . THR B 198 ? 0.51240 0.46270 0.58740 0.01620  0.03170  -0.03650 198 THR B C   
3840 O O   . THR B 198 ? 0.47390 0.42340 0.54110 0.01470  0.02830  -0.02910 198 THR B O   
3841 C CB  . THR B 198 ? 0.58690 0.54190 0.68540 0.02120  0.03870  -0.04190 198 THR B CB  
3842 O OG1 . THR B 198 ? 0.68670 0.63830 0.78940 0.02060  0.03400  -0.03190 198 THR B OG1 
3843 C CG2 . THR B 198 ? 0.68360 0.64730 0.78660 0.02400  0.04530  -0.04640 198 THR B CG2 
3844 N N   . THR B 199 ? 0.53140 0.47670 0.61190 0.01560  0.03060  -0.04090 199 THR B N   
3845 C CA  . THR B 199 ? 0.45380 0.39330 0.53040 0.01300  0.02530  -0.03600 199 THR B CA  
3846 C C   . THR B 199 ? 0.48850 0.42210 0.57840 0.01310  0.02130  -0.02860 199 THR B C   
3847 O O   . THR B 199 ? 0.50030 0.43200 0.60590 0.01520  0.02270  -0.03050 199 THR B O   
3848 C CB  . THR B 199 ? 0.47050 0.40870 0.54670 0.01180  0.02610  -0.04400 199 THR B CB  
3849 O OG1 . THR B 199 ? 0.49760 0.44370 0.55990 0.01170  0.02940  -0.04940 199 THR B OG1 
3850 C CG2 . THR B 199 ? 0.52790 0.46060 0.60160 0.00890  0.02110  -0.03880 199 THR B CG2 
3851 N N   . ILE B 200 ? 0.47100 0.40250 0.55480 0.01110  0.01630  -0.02010 200 ILE B N   
3852 C CA  . ILE B 200 ? 0.43330 0.36150 0.52810 0.01110  0.01180  -0.01170 200 ILE B CA  
3853 C C   . ILE B 200 ? 0.49880 0.42140 0.60400 0.01020  0.01010  -0.01120 200 ILE B C   
3854 O O   . ILE B 200 ? 0.44960 0.37090 0.54780 0.00770  0.00730  -0.00750 200 ILE B O   
3855 C CB  . ILE B 200 ? 0.45370 0.38380 0.53770 0.00930  0.00740  -0.00360 200 ILE B CB  
3856 C CG1 . ILE B 200 ? 0.47750 0.41240 0.55350 0.01000  0.00960  -0.00490 200 ILE B CG1 
3857 C CG2 . ILE B 200 ? 0.47260 0.40160 0.56740 0.00910  0.00250  0.00530  200 ILE B CG2 
3858 C CD1 . ILE B 200 ? 0.45180 0.38840 0.51220 0.00780  0.00730  -0.00220 200 ILE B CD1 
3859 N N   . THR B 201 ? 0.47810 0.39780 0.60160 0.01230  0.01190  -0.01420 201 THR B N   
3860 C CA  . THR B 201 ? 0.48950 0.40320 0.62680 0.01160  0.01100  -0.01490 201 THR B CA  
3861 C C   . THR B 201 ? 0.48790 0.39950 0.62780 0.00960  0.00530  -0.00260 201 THR B C   
3862 O O   . THR B 201 ? 0.49150 0.40020 0.63080 0.00730  0.00400  -0.00170 201 THR B O   
3863 C CB  . THR B 201 ? 0.50820 0.41900 0.66730 0.01470  0.01380  -0.01920 201 THR B CB  
3864 O OG1 . THR B 201 ? 0.47350 0.38840 0.62890 0.01670  0.01950  -0.03050 201 THR B OG1 
3865 C CG2 . THR B 201 ? 0.47030 0.37410 0.64590 0.01400  0.01360  -0.02200 201 THR B CG2 
3866 N N   . VAL B 202 ? 0.46380 0.37750 0.60770 0.01030  0.00180  0.00720  202 VAL B N   
3867 C CA  . VAL B 202 ? 0.49830 0.41230 0.64440 0.00840  -0.00370 0.01950  202 VAL B CA  
3868 C C   . VAL B 202 ? 0.47920 0.39570 0.60570 0.00530  -0.00540 0.02150  202 VAL B C   
3869 O O   . VAL B 202 ? 0.47630 0.39200 0.60500 0.00320  -0.00810 0.02830  202 VAL B O   
3870 C CB  . VAL B 202 ? 0.47170 0.39030 0.62190 0.00960  -0.00750 0.02860  202 VAL B CB  
3871 C CG1 . VAL B 202 ? 0.51390 0.43820 0.64610 0.00920  -0.00750 0.02640  202 VAL B CG1 
3872 C CG2 . VAL B 202 ? 0.49090 0.41190 0.64380 0.00760  -0.01340 0.04220  202 VAL B CG2 
3873 N N   . ASN B 203 ? 0.46660 0.38640 0.57530 0.00490  -0.00360 0.01590  203 ASN B N   
3874 C CA  . ASN B 203 ? 0.49210 0.41440 0.58330 0.00240  -0.00460 0.01660  203 ASN B CA  
3875 C C   . ASN B 203 ? 0.47120 0.39020 0.56200 0.00110  -0.00240 0.01100  203 ASN B C   
3876 O O   . ASN B 203 ? 0.48160 0.40160 0.56570 -0.00130 -0.00410 0.01490  203 ASN B O   
3877 C CB  . ASN B 203 ? 0.45830 0.38450 0.53340 0.00270  -0.00310 0.01240  203 ASN B CB  
3878 C CG  . ASN B 203 ? 0.45600 0.38640 0.52900 0.00310  -0.00640 0.01830  203 ASN B CG  
3879 O OD1 . ASN B 203 ? 0.43270 0.36400 0.51560 0.00320  -0.00990 0.02560  203 ASN B OD1 
3880 N ND2 . ASN B 203 ? 0.48920 0.42250 0.55100 0.00320  -0.00540 0.01520  203 ASN B ND2 
3881 N N   . VAL B 204 ? 0.47300 0.38940 0.56980 0.00230  0.00160  0.00100  204 VAL B N   
3882 C CA  . VAL B 204 ? 0.48580 0.39970 0.58400 0.00060  0.00310  -0.00490 204 VAL B CA  
3883 C C   . VAL B 204 ? 0.51630 0.42570 0.62960 -0.00090 0.00040  0.00200  204 VAL B C   
3884 O O   . VAL B 204 ? 0.48300 0.39220 0.59330 -0.00370 -0.00070 0.00390  204 VAL B O   
3885 C CB  . VAL B 204 ? 0.47790 0.39090 0.58100 0.00220  0.00760  -0.01760 204 VAL B CB  
3886 C CG1 . VAL B 204 ? 0.46950 0.38020 0.57620 -0.00000 0.00830  -0.02430 204 VAL B CG1 
3887 C CG2 . VAL B 204 ? 0.46510 0.38410 0.55210 0.00330  0.01030  -0.02270 204 VAL B CG2 
3888 N N   . LEU B 205 ? 0.46200 0.36820 0.59350 0.00080  -0.00050 0.00630  205 LEU B N   
3889 C CA  . LEU B 205 ? 0.52580 0.42840 0.67360 -0.00060 -0.00330 0.01540  205 LEU B CA  
3890 C C   . LEU B 205 ? 0.48310 0.39070 0.62000 -0.00300 -0.00730 0.02780  205 LEU B C   
3891 O O   . LEU B 205 ? 0.47090 0.37740 0.61280 -0.00540 -0.00860 0.03330  205 LEU B O   
3892 C CB  . LEU B 205 ? 0.46580 0.36520 0.63500 0.00210  -0.00400 0.01970  205 LEU B CB  
3893 C CG  . LEU B 205 ? 0.46270 0.35680 0.64780 0.00450  0.00040  0.00730  205 LEU B CG  
3894 C CD1 . LEU B 205 ? 0.50460 0.39690 0.70980 0.00790  0.00000  0.01180  205 LEU B CD1 
3895 C CD2 . LEU B 205 ? 0.50130 0.38910 0.69990 0.00270  0.00170  0.00100  205 LEU B CD2 
3896 N N   . ALA B 206 ? 0.46410 0.37770 0.58670 -0.00240 -0.00910 0.03220  206 ALA B N   
3897 C CA  . ALA B 206 ? 0.49010 0.40990 0.60110 -0.00450 -0.01260 0.04240  206 ALA B CA  
3898 C C   . ALA B 206 ? 0.47670 0.39750 0.57550 -0.00700 -0.01120 0.03910  206 ALA B C   
3899 O O   . ALA B 206 ? 0.50030 0.42370 0.59940 -0.00940 -0.01300 0.04730  206 ALA B O   
3900 C CB  . ALA B 206 ? 0.47890 0.40510 0.57600 -0.00360 -0.01440 0.04420  206 ALA B CB  
3901 N N   . TRP B 207 ? 0.47070 0.39030 0.55990 -0.00660 -0.00800 0.02780  207 TRP B N   
3902 C CA  . TRP B 207 ? 0.51170 0.43310 0.58920 -0.00860 -0.00680 0.02400  207 TRP B CA  
3903 C C   . TRP B 207 ? 0.51040 0.42750 0.60100 -0.01070 -0.00620 0.02270  207 TRP B C   
3904 O O   . TRP B 207 ? 0.46320 0.38270 0.54920 -0.01320 -0.00670 0.02570  207 TRP B O   
3905 C CB  . TRP B 207 ? 0.47090 0.39340 0.53560 -0.00730 -0.00390 0.01360  207 TRP B CB  
3906 C CG  . TRP B 207 ? 0.49210 0.41650 0.54680 -0.00880 -0.00220 0.00760  207 TRP B CG  
3907 C CD1 . TRP B 207 ? 0.48590 0.41520 0.52580 -0.00990 -0.00260 0.00960  207 TRP B CD1 
3908 C CD2 . TRP B 207 ? 0.52040 0.44260 0.57980 -0.00930 0.00010  -0.00180 207 TRP B CD2 
3909 N NE1 . TRP B 207 ? 0.49550 0.42570 0.53120 -0.01080 -0.00070 0.00250  207 TRP B NE1 
3910 C CE2 . TRP B 207 ? 0.47460 0.40080 0.52180 -0.01080 0.00060  -0.00440 207 TRP B CE2 
3911 C CE3 . TRP B 207 ? 0.50330 0.42100 0.57670 -0.00850 0.00170  -0.00890 207 TRP B CE3 
3912 C CZ2 . TRP B 207 ? 0.48570 0.41260 0.53300 -0.01170 0.00220  -0.01360 207 TRP B CZ2 
3913 C CZ3 . TRP B 207 ? 0.54010 0.45830 0.61340 -0.00950 0.00360  -0.01930 207 TRP B CZ3 
3914 C CH2 . TRP B 207 ? 0.46840 0.39150 0.52870 -0.01120 0.00360  -0.02120 207 TRP B CH2 
3915 N N   . LEU B 208 ? 0.45410 0.36500 0.56230 -0.00970 -0.00500 0.01790  208 LEU B N   
3916 C CA  . LEU B 208 ? 0.45990 0.36600 0.58470 -0.01190 -0.00500 0.01790  208 LEU B CA  
3917 C C   . LEU B 208 ? 0.50230 0.40980 0.63500 -0.01380 -0.00820 0.03310  208 LEU B C   
3918 O O   . LEU B 208 ? 0.47550 0.38260 0.61380 -0.01680 -0.00850 0.03600  208 LEU B O   
3919 C CB  . LEU B 208 ? 0.40500 0.30400 0.55020 -0.01030 -0.00320 0.01010  208 LEU B CB  
3920 C CG  . LEU B 208 ? 0.48830 0.38760 0.62620 -0.00890 0.00040  -0.00600 208 LEU B CG  
3921 C CD1 . LEU B 208 ? 0.49670 0.38990 0.65540 -0.00680 0.00270  -0.01460 208 LEU B CD1 
3922 C CD2 . LEU B 208 ? 0.49090 0.39290 0.61850 -0.01170 0.00120  -0.01360 208 LEU B CD2 
3923 N N   . TYR B 209 ? 0.45870 0.36900 0.59310 -0.01240 -0.01050 0.04340  209 TYR B N   
3924 C CA  . TYR B 209 ? 0.49020 0.40430 0.63030 -0.01420 -0.01350 0.05880  209 TYR B CA  
3925 C C   . TYR B 209 ? 0.50200 0.42410 0.62290 -0.01650 -0.01400 0.06290  209 TYR B C   
3926 O O   . TYR B 209 ? 0.51090 0.43540 0.63720 -0.01920 -0.01480 0.07160  209 TYR B O   
3927 C CB  . TYR B 209 ? 0.46390 0.38150 0.60800 -0.01230 -0.01650 0.06900  209 TYR B CB  
3928 C CG  . TYR B 209 ? 0.51880 0.42930 0.68880 -0.01060 -0.01670 0.07100  209 TYR B CG  
3929 C CD1 . TYR B 209 ? 0.53130 0.43850 0.72240 -0.01220 -0.01770 0.07990  209 TYR B CD1 
3930 C CD2 . TYR B 209 ? 0.49090 0.39840 0.66560 -0.00720 -0.01580 0.06450  209 TYR B CD2 
3931 C CE1 . TYR B 209 ? 0.53290 0.43320 0.75040 -0.01040 -0.01790 0.08200  209 TYR B CE1 
3932 C CE2 . TYR B 209 ? 0.50980 0.41120 0.70950 -0.00530 -0.01580 0.06610  209 TYR B CE2 
3933 C CZ  . TYR B 209 ? 0.54100 0.43840 0.76220 -0.00680 -0.01680 0.07450  209 TYR B CZ  
3934 O OH  . TYR B 209 ? 0.52390 0.41450 0.77240 -0.00470 -0.01660 0.07610  209 TYR B OH  
3935 N N   . ALA B 210 ? 0.47670 0.40330 0.57680 -0.01540 -0.01340 0.05730  210 ALA B N   
3936 C CA  . ALA B 210 ? 0.51680 0.45050 0.59900 -0.01710 -0.01310 0.05830  210 ALA B CA  
3937 C C   . ALA B 210 ? 0.52030 0.45170 0.60560 -0.01950 -0.01110 0.05400  210 ALA B C   
3938 O O   . ALA B 210 ? 0.54100 0.47770 0.62320 -0.02190 -0.01140 0.06080  210 ALA B O   
3939 C CB  . ALA B 210 ? 0.47870 0.41480 0.54230 -0.01520 -0.01190 0.04970  210 ALA B CB  
3940 N N   . ALA B 211 ? 0.47550 0.40010 0.56780 -0.01910 -0.00920 0.04270  211 ALA B N   
3941 C CA  . ALA B 211 ? 0.52100 0.44380 0.61700 -0.02170 -0.00780 0.03710  211 ALA B CA  
3942 C C   . ALA B 211 ? 0.56410 0.48530 0.67840 -0.02460 -0.00900 0.04650  211 ALA B C   
3943 O O   . ALA B 211 ? 0.50670 0.43160 0.61930 -0.02740 -0.00880 0.04920  211 ALA B O   
3944 C CB  . ALA B 211 ? 0.50380 0.42090 0.60480 -0.02070 -0.00590 0.02280  211 ALA B CB  
3945 N N   . VAL B 212 ? 0.55230 0.46850 0.68550 -0.02400 -0.01020 0.05220  212 VAL B N   
3946 C CA  . VAL B 212 ? 0.53050 0.44490 0.68430 -0.02660 -0.01150 0.06320  212 VAL B CA  
3947 C C   . VAL B 212 ? 0.57470 0.49900 0.71990 -0.02820 -0.01290 0.07830  212 VAL B C   
3948 O O   . VAL B 212 ? 0.55010 0.47660 0.70370 -0.03150 -0.01280 0.08570  212 VAL B O   
3949 C CB  . VAL B 212 ? 0.50830 0.41570 0.68460 -0.02480 -0.01250 0.06700  212 VAL B CB  
3950 C CG1 . VAL B 212 ? 0.55010 0.45690 0.74920 -0.02740 -0.01420 0.08230  212 VAL B CG1 
3951 C CG2 . VAL B 212 ? 0.47700 0.37480 0.66580 -0.02380 -0.01040 0.05070  212 VAL B CG2 
3952 N N   . ILE B 213 ? 0.53800 0.46910 0.66790 -0.02610 -0.01410 0.08340  213 ILE B N   
3953 C CA  . ILE B 213 ? 0.56520 0.50790 0.68420 -0.02740 -0.01530 0.09650  213 ILE B CA  
3954 C C   . ILE B 213 ? 0.60540 0.55330 0.71060 -0.02940 -0.01320 0.09260  213 ILE B C   
3955 O O   . ILE B 213 ? 0.57950 0.53510 0.68480 -0.03180 -0.01310 0.10310  213 ILE B O   
3956 C CB  . ILE B 213 ? 0.60140 0.55060 0.70500 -0.02470 -0.01720 0.09860  213 ILE B CB  
3957 C CG1 . ILE B 213 ? 0.54020 0.48630 0.65910 -0.02280 -0.01980 0.10520  213 ILE B CG1 
3958 C CG2 . ILE B 213 ? 0.56430 0.52720 0.65150 -0.02580 -0.01800 0.10810  213 ILE B CG2 
3959 C CD1 . ILE B 213 ? 0.55300 0.50400 0.65780 -0.02000 -0.02170 0.10360  213 ILE B CD1 
3960 N N   . ASN B 214 ? 0.55980 0.50400 0.65540 -0.02850 -0.01140 0.07830  214 ASN B N   
3961 C CA  . ASN B 214 ? 0.59550 0.54440 0.67960 -0.03020 -0.00950 0.07420  214 ASN B CA  
3962 C C   . ASN B 214 ? 0.58020 0.52460 0.67880 -0.03320 -0.00850 0.07070  214 ASN B C   
3963 O O   . ASN B 214 ? 0.62170 0.56910 0.71140 -0.03420 -0.00710 0.06440  214 ASN B O   
3964 C CB  . ASN B 214 ? 0.56050 0.50960 0.62630 -0.02770 -0.00820 0.06200  214 ASN B CB  
3965 C CG  . ASN B 214 ? 0.65740 0.61460 0.70570 -0.02600 -0.00860 0.06570  214 ASN B CG  
3966 O OD1 . ASN B 214 ? 0.72050 0.68560 0.75760 -0.02680 -0.00740 0.06740  214 ASN B OD1 
3967 N ND2 . ASN B 214 ? 0.66480 0.62110 0.71200 -0.02380 -0.01030 0.06710  214 ASN B ND2 
3968 N N   . GLY B 215 ? 0.58320 0.52000 0.70460 -0.03450 -0.00940 0.07280  215 GLY B N   
3969 C CA  . GLY B 215 ? 0.59670 0.52910 0.73470 -0.03790 -0.00890 0.06930  215 GLY B CA  
3970 C C   . GLY B 215 ? 0.61210 0.53620 0.75550 -0.03750 -0.00830 0.05240  215 GLY B C   
3971 O O   . GLY B 215 ? 0.60560 0.52610 0.76370 -0.04050 -0.00830 0.04780  215 GLY B O   
3972 N N   . ASP B 216 ? 0.53480 0.45690 0.66640 -0.03410 -0.00770 0.04230  216 ASP B N   
3973 C CA  . ASP B 216 ? 0.59910 0.51500 0.73650 -0.03370 -0.00690 0.02660  216 ASP B CA  
3974 C C   . ASP B 216 ? 0.63770 0.54440 0.79920 -0.03330 -0.00740 0.02650  216 ASP B C   
3975 O O   . ASP B 216 ? 0.57620 0.48090 0.73860 -0.03030 -0.00760 0.03060  216 ASP B O   
3976 C CB  . ASP B 216 ? 0.62350 0.54140 0.74140 -0.03030 -0.00570 0.01670  216 ASP B CB  
3977 C CG  . ASP B 216 ? 0.72800 0.65340 0.82650 -0.03080 -0.00490 0.01200  216 ASP B CG  
3978 O OD1 . ASP B 216 ? 0.82670 0.75400 0.92960 -0.03390 -0.00510 0.00920  216 ASP B OD1 
3979 O OD2 . ASP B 216 ? 0.58460 0.51400 0.66480 -0.02800 -0.00420 0.01120  216 ASP B OD2 
3980 N N   . ARG B 217 ? 0.57440 0.47540 0.75710 -0.03620 -0.00750 0.02180  217 ARG B N   
3981 C CA  . ARG B 217 ? 0.55350 0.44520 0.76160 -0.03560 -0.00770 0.02150  217 ARG B CA  
3982 C C   . ARG B 217 ? 0.53860 0.42420 0.75860 -0.03600 -0.00660 0.00330  217 ARG B C   
3983 O O   . ARG B 217 ? 0.52420 0.40130 0.76820 -0.03560 -0.00640 0.00090  217 ARG B O   
3984 C CB  . ARG B 217 ? 0.59640 0.48560 0.82760 -0.03870 -0.00920 0.03600  217 ARG B CB  
3985 C CG  . ARG B 217 ? 0.63380 0.52870 0.86080 -0.03810 -0.01040 0.05570  217 ARG B CG  
3986 C CD  . ARG B 217 ? 0.62120 0.51240 0.87810 -0.04110 -0.01170 0.07000  217 ARG B CD  
3987 N NE  . ARG B 217 ? 0.65020 0.54100 0.91590 -0.03850 -0.01310 0.08410  217 ARG B NE  
3988 C CZ  . ARG B 217 ? 0.68950 0.57110 0.98110 -0.03710 -0.01350 0.08480  217 ARG B CZ  
3989 N NH1 . ARG B 217 ? 0.72200 0.59350 1.03310 -0.03770 -0.01240 0.07080  217 ARG B NH1 
3990 N NH2 . ARG B 217 ? 0.78470 0.66810 1.08350 -0.03480 -0.01520 0.09970  217 ARG B NH2 
3991 N N   . TRP B 218 ? 0.49950 0.38970 0.70410 -0.03690 -0.00590 -0.00960 218 TRP B N   
3992 C CA  . TRP B 218 ? 0.53830 0.42500 0.75410 -0.03840 -0.00530 -0.02710 218 TRP B CA  
3993 C C   . TRP B 218 ? 0.58400 0.46590 0.80560 -0.03460 -0.00330 -0.03820 218 TRP B C   
3994 O O   . TRP B 218 ? 0.57270 0.44970 0.81140 -0.03550 -0.00260 -0.05170 218 TRP B O   
3995 C CB  . TRP B 218 ? 0.58400 0.47950 0.77940 -0.03980 -0.00530 -0.03740 218 TRP B CB  
3996 C CG  . TRP B 218 ? 0.57240 0.47490 0.74000 -0.03590 -0.00380 -0.04040 218 TRP B CG  
3997 C CD1 . TRP B 218 ? 0.59000 0.49940 0.73630 -0.03500 -0.00410 -0.03110 218 TRP B CD1 
3998 C CD2 . TRP B 218 ? 0.56410 0.46740 0.72400 -0.03260 -0.00180 -0.05320 218 TRP B CD2 
3999 N NE1 . TRP B 218 ? 0.58110 0.49470 0.70880 -0.03150 -0.00250 -0.03700 218 TRP B NE1 
4000 C CE2 . TRP B 218 ? 0.60100 0.51160 0.73590 -0.03000 -0.00100 -0.04990 218 TRP B CE2 
4001 C CE3 . TRP B 218 ? 0.57720 0.47660 0.74970 -0.03150 -0.00020 -0.06760 218 TRP B CE3 
4002 C CZ2 . TRP B 218 ? 0.60920 0.52340 0.73140 -0.02660 0.00120  -0.05870 218 TRP B CZ2 
4003 C CZ3 . TRP B 218 ? 0.62580 0.52980 0.78430 -0.02800 0.00230  -0.07720 218 TRP B CZ3 
4004 C CH2 . TRP B 218 ? 0.59860 0.51000 0.73230 -0.02560 0.00290  -0.07180 218 TRP B CH2 
4005 N N   . PHE B 219 ? 0.50480 0.38870 0.71200 -0.03030 -0.00230 -0.03370 219 PHE B N   
4006 C CA  . PHE B 219 ? 0.55720 0.43800 0.76830 -0.02650 0.00010  -0.04370 219 PHE B CA  
4007 C C   . PHE B 219 ? 0.55330 0.42500 0.79070 -0.02490 0.00000  -0.03700 219 PHE B C   
4008 O O   . PHE B 219 ? 0.50290 0.37130 0.74790 -0.02160 0.00210  -0.04500 219 PHE B O   
4009 C CB  . PHE B 219 ? 0.51050 0.39790 0.69620 -0.02290 0.00120  -0.04180 219 PHE B CB  
4010 C CG  . PHE B 219 ? 0.48970 0.37930 0.66650 -0.02230 -0.00060 -0.02410 219 PHE B CG  
4011 C CD1 . PHE B 219 ? 0.48390 0.36940 0.67260 -0.02010 -0.00130 -0.01390 219 PHE B CD1 
4012 C CD2 . PHE B 219 ? 0.52090 0.41750 0.67890 -0.02410 -0.00180 -0.01780 219 PHE B CD2 
4013 C CE1 . PHE B 219 ? 0.53090 0.42010 0.71100 -0.01980 -0.00340 0.00190  219 PHE B CE1 
4014 C CE2 . PHE B 219 ? 0.52070 0.42040 0.67050 -0.02380 -0.00340 -0.00260 219 PHE B CE2 
4015 C CZ  . PHE B 219 ? 0.50130 0.39780 0.66140 -0.02170 -0.00440 0.00730  219 PHE B CZ  
4016 N N   . LEU B 220 ? 0.50910 0.37740 0.76130 -0.02710 -0.00230 -0.02180 220 LEU B N   
4017 C CA  . LEU B 220 ? 0.53800 0.39810 0.81740 -0.02550 -0.00260 -0.01430 220 LEU B CA  
4018 C C   . LEU B 220 ? 0.54240 0.39350 0.85030 -0.02660 -0.00140 -0.02800 220 LEU B C   
4019 O O   . LEU B 220 ? 0.54860 0.40000 0.85800 -0.03000 -0.00120 -0.04020 220 LEU B O   
4020 C CB  . LEU B 220 ? 0.54160 0.40260 0.82830 -0.02740 -0.00550 0.00750  220 LEU B CB  
4021 C CG  . LEU B 220 ? 0.53190 0.40210 0.79200 -0.02580 -0.00660 0.02000  220 LEU B CG  
4022 C CD1 . LEU B 220 ? 0.55800 0.43100 0.82470 -0.02840 -0.00920 0.03990  220 LEU B CD1 
4023 C CD2 . LEU B 220 ? 0.48340 0.35360 0.74040 -0.02080 -0.00630 0.02190  220 LEU B CD2 
4024 N N   . ASN B 221 ? 0.57370 0.41740 0.90510 -0.02370 -0.00040 -0.02720 221 ASN B N   
4025 C CA  . ASN B 221 ? 0.54510 0.37940 0.90720 -0.02440 0.00090  -0.03990 221 ASN B CA  
4026 C C   . ASN B 221 ? 0.56170 0.38760 0.95480 -0.02260 0.00010  -0.02640 221 ASN B C   
4027 O O   . ASN B 221 ? 0.49620 0.32500 0.88400 -0.02030 -0.00140 -0.00900 221 ASN B O   
4028 C CB  . ASN B 221 ? 0.57390 0.40860 0.93170 -0.02180 0.00460  -0.06330 221 ASN B CB  
4029 C CG  . ASN B 221 ? 0.61600 0.45250 0.96680 -0.01600 0.00670  -0.06220 221 ASN B CG  
4030 O OD1 . ASN B 221 ? 0.60930 0.44200 0.97390 -0.01360 0.00570  -0.04770 221 ASN B OD1 
4031 N ND2 . ASN B 221 ? 0.62400 0.46770 0.95200 -0.01400 0.00950  -0.07580 221 ASN B ND2 
4032 N N   . ARG B 222 ? 0.56360 0.37960 0.99010 -0.02360 0.00090  -0.03420 222 ARG B N   
4033 C CA  . ARG B 222 ? 0.57080 0.37840 1.03060 -0.02200 0.00000  -0.02020 222 ARG B CA  
4034 C C   . ARG B 222 ? 0.58500 0.38930 1.05520 -0.01590 0.00260  -0.02580 222 ARG B C   
4035 O O   . ARG B 222 ? 0.59120 0.38830 1.09150 -0.01390 0.00200  -0.01530 222 ARG B O   
4036 C CB  . ARG B 222 ? 0.63650 0.43390 1.13190 -0.02560 -0.00020 -0.02510 222 ARG B CB  
4037 C CG  . ARG B 222 ? 0.71840 0.51470 1.21160 -0.02760 0.00190  -0.05180 222 ARG B CG  
4038 C CD  . ARG B 222 ? 0.75430 0.54010 1.28080 -0.02540 0.00470  -0.06770 222 ARG B CD  
4039 N NE  . ARG B 222 ? 0.63410 0.41670 1.17130 -0.02900 0.00570  -0.09130 222 ARG B NE  
4040 C CZ  . ARG B 222 ? 0.74500 0.51790 1.31490 -0.02780 0.00810  -0.10730 222 ARG B CZ  
4041 N NH1 . ARG B 222 ? 0.76180 0.53080 1.35670 -0.02330 0.00920  -0.09790 222 ARG B NH1 
4042 N NH2 . ARG B 222 ? 0.85400 0.62840 1.42580 -0.03030 0.00940  -0.13190 222 ARG B NH2 
4043 N N   . PHE B 223 ? 0.58530 0.39460 1.03370 -0.01310 0.00560  -0.04230 223 PHE B N   
4044 C CA  . PHE B 223 ? 0.58480 0.39200 1.04270 -0.00740 0.00880  -0.05000 223 PHE B CA  
4045 C C   . PHE B 223 ? 0.58090 0.39410 1.02470 -0.00380 0.00740  -0.03300 223 PHE B C   
4046 O O   . PHE B 223 ? 0.57920 0.40040 0.99610 -0.00520 0.00470  -0.02050 223 PHE B O   
4047 C CB  . PHE B 223 ? 0.56700 0.37870 1.00810 -0.00600 0.01310  -0.07520 223 PHE B CB  
4048 C CG  . PHE B 223 ? 0.63640 0.44340 1.09220 -0.00930 0.01440  -0.09500 223 PHE B CG  
4049 C CD1 . PHE B 223 ? 0.65990 0.45570 1.15490 -0.00860 0.01590  -0.10250 223 PHE B CD1 
4050 C CD2 . PHE B 223 ? 0.68990 0.50400 1.12170 -0.01330 0.01390  -0.10590 223 PHE B CD2 
4051 C CE1 . PHE B 223 ? 0.71960 0.51120 1.22920 -0.01210 0.01680  -0.12210 223 PHE B CE1 
4052 C CE2 . PHE B 223 ? 0.65500 0.46610 1.10010 -0.01660 0.01460  -0.12450 223 PHE B CE2 
4053 C CZ  . PHE B 223 ? 0.68280 0.48250 1.16680 -0.01620 0.01600  -0.13300 223 PHE B CZ  
4054 N N   . THR B 224 ? 0.56930 0.37890 1.03140 0.00110  0.00940  -0.03420 224 THR B N   
4055 C CA  . THR B 224 ? 0.61370 0.42960 1.06370 0.00510  0.00850  -0.02220 224 THR B CA  
4056 C C   . THR B 224 ? 0.61210 0.42860 1.06390 0.01000  0.01370  -0.03980 224 THR B C   
4057 O O   . THR B 224 ? 0.64320 0.45420 1.11180 0.01070  0.01760  -0.05860 224 THR B O   
4058 C CB  . THR B 224 ? 0.65780 0.47000 1.13360 0.00620  0.00480  0.00060  224 THR B CB  
4059 O OG1 . THR B 224 ? 0.69830 0.51870 1.15860 0.00910  0.00290  0.01380  224 THR B OG1 
4060 C CG2 . THR B 224 ? 0.61970 0.42080 1.13820 0.00930  0.00730  -0.00550 224 THR B CG2 
4061 N N   . THR B 225 ? 0.65950 0.48330 1.09460 0.01320  0.01370  -0.03380 225 THR B N   
4062 C CA  . THR B 225 ? 0.63510 0.46170 1.06910 0.01790  0.01880  -0.04840 225 THR B CA  
4063 C C   . THR B 225 ? 0.62380 0.45230 1.06780 0.02210  0.01730  -0.03370 225 THR B C   
4064 O O   . THR B 225 ? 0.58810 0.41920 1.02810 0.02100  0.01210  -0.01320 225 THR B O   
4065 C CB  . THR B 225 ? 0.62210 0.45870 1.01840 0.01690  0.02090  -0.05930 225 THR B CB  
4066 O OG1 . THR B 225 ? 0.65250 0.49330 1.04790 0.02150  0.02630  -0.07220 225 THR B OG1 
4067 C CG2 . THR B 225 ? 0.59590 0.44000 0.96570 0.01550  0.01670  -0.04230 225 THR B CG2 
4068 N N   . THR B 226 ? 0.65310 0.48190 1.10870 0.02710  0.02200  -0.04420 226 THR B N   
4069 C CA  . THR B 226 ? 0.61670 0.44990 1.07650 0.03100  0.02060  -0.03130 226 THR B CA  
4070 C C   . THR B 226 ? 0.62070 0.46530 1.04460 0.03090  0.02080  -0.03110 226 THR B C   
4071 O O   . THR B 226 ? 0.63790 0.48680 1.03860 0.02950  0.02400  -0.04530 226 THR B O   
4072 C CB  . THR B 226 ? 0.68390 0.51340 1.17350 0.03670  0.02570  -0.04140 226 THR B CB  
4073 O OG1 . THR B 226 ? 0.68770 0.52130 1.16450 0.03810  0.03240  -0.06420 226 THR B OG1 
4074 C CG2 . THR B 226 ? 0.66210 0.47930 1.19210 0.03730  0.02580  -0.04170 226 THR B CG2 
4075 N N   . LEU B 227 ? 0.61050 0.46050 1.03110 0.03240  0.01710  -0.01490 227 LEU B N   
4076 C CA  . LEU B 227 ? 0.63780 0.49800 1.02770 0.03230  0.01720  -0.01470 227 LEU B CA  
4077 C C   . LEU B 227 ? 0.67480 0.53860 1.06000 0.03540  0.02440  -0.03340 227 LEU B C   
4078 O O   . LEU B 227 ? 0.58720 0.45770 0.94440 0.03390  0.02650  -0.04110 227 LEU B O   
4079 C CB  . LEU B 227 ? 0.60070 0.46610 0.99300 0.03370  0.01210  0.00410  227 LEU B CB  
4080 C CG  . LEU B 227 ? 0.64000 0.51560 1.00310 0.03300  0.01060  0.00760  227 LEU B CG  
4081 C CD1 . LEU B 227 ? 0.57730 0.45560 0.90960 0.02810  0.00840  0.00820  227 LEU B CD1 
4082 C CD2 . LEU B 227 ? 0.65710 0.53780 1.02790 0.03440  0.00510  0.02550  227 LEU B CD2 
4083 N N   . ASN B 228 ? 0.65420 0.51450 1.06760 0.03990  0.02850  -0.04060 228 ASN B N   
4084 C CA  . ASN B 228 ? 0.68460 0.54970 1.09580 0.04330  0.03610  -0.05840 228 ASN B CA  
4085 C C   . ASN B 228 ? 0.66700 0.53220 1.06540 0.04110  0.04050  -0.07790 228 ASN B C   
4086 O O   . ASN B 228 ? 0.64890 0.52280 1.02470 0.04120  0.04460  -0.08810 228 ASN B O   
4087 C CB  . ASN B 228 ? 0.75640 0.61760 1.20340 0.04870  0.03960  -0.06170 228 ASN B CB  
4088 C CG  . ASN B 228 ? 0.84970 0.71500 1.30530 0.05140  0.03600  -0.04430 228 ASN B CG  
4089 O OD1 . ASN B 228 ? 0.94510 0.81840 1.37700 0.04990  0.03300  -0.03520 228 ASN B OD1 
4090 N ND2 . ASN B 228 ? 0.88170 0.74180 1.37220 0.05550  0.03620  -0.04000 228 ASN B ND2 
4091 N N   . ASP B 229 ? 0.65010 0.50640 1.06270 0.03890  0.03960  -0.08270 229 ASP B N   
4092 C CA  . ASP B 229 ? 0.64490 0.50220 1.04470 0.03630  0.04280  -0.10120 229 ASP B CA  
4093 C C   . ASP B 229 ? 0.65070 0.51490 1.01370 0.03190  0.04000  -0.09720 229 ASP B C   
4094 O O   . ASP B 229 ? 0.63740 0.50850 0.98080 0.03080  0.04350  -0.11150 229 ASP B O   
4095 C CB  . ASP B 229 ? 0.72530 0.57150 1.14980 0.03430  0.04180  -0.10660 229 ASP B CB  
4096 C CG  . ASP B 229 ? 0.78510 0.62490 1.24620 0.03900  0.04650  -0.11770 229 ASP B CG  
4097 O OD1 . ASP B 229 ? 0.73790 0.58380 1.20100 0.04350  0.05220  -0.12690 229 ASP B OD1 
4098 O OD2 . ASP B 229 ? 0.73850 0.56740 1.22710 0.03790  0.04490  -0.11760 229 ASP B OD2 
4099 N N   . PHE B 230 ? 0.62600 0.48950 0.97950 0.02940  0.03360  -0.07800 230 PHE B N   
4100 C CA  . PHE B 230 ? 0.60600 0.47630 0.92580 0.02570  0.03130  -0.07440 230 PHE B CA  
4101 C C   . PHE B 230 ? 0.62010 0.50070 0.91880 0.02770  0.03450  -0.07720 230 PHE B C   
4102 O O   . PHE B 230 ? 0.59220 0.47960 0.86720 0.02610  0.03650  -0.08530 230 PHE B O   
4103 C CB  . PHE B 230 ? 0.58530 0.45380 0.89940 0.02290  0.02440  -0.05430 230 PHE B CB  
4104 C CG  . PHE B 230 ? 0.56830 0.44410 0.84920 0.01990  0.02240  -0.05050 230 PHE B CG  
4105 C CD1 . PHE B 230 ? 0.56290 0.43930 0.82910 0.01620  0.02240  -0.05790 230 PHE B CD1 
4106 C CD2 . PHE B 230 ? 0.51870 0.40050 0.78500 0.02060  0.02030  -0.03970 230 PHE B CD2 
4107 C CE1 . PHE B 230 ? 0.56010 0.44310 0.79760 0.01370  0.02070  -0.05410 230 PHE B CE1 
4108 C CE2 . PHE B 230 ? 0.55800 0.44590 0.79550 0.01790  0.01860  -0.03670 230 PHE B CE2 
4109 C CZ  . PHE B 230 ? 0.57740 0.46570 0.80100 0.01480  0.01900  -0.04380 230 PHE B CZ  
4110 N N   . ASN B 231 ? 0.58780 0.47040 0.89590 0.03130  0.03490  -0.06980 231 ASN B N   
4111 C CA  . ASN B 231 ? 0.59940 0.49200 0.88900 0.03290  0.03780  -0.07120 231 ASN B CA  
4112 C C   . ASN B 231 ? 0.62170 0.52020 0.90820 0.03490  0.04550  -0.09060 231 ASN B C   
4113 O O   . ASN B 231 ? 0.65090 0.55880 0.91500 0.03460  0.04810  -0.09420 231 ASN B O   
4114 C CB  . ASN B 231 ? 0.57960 0.47340 0.88270 0.03610  0.03630  -0.05940 231 ASN B CB  
4115 C CG  . ASN B 231 ? 0.62880 0.52260 0.92260 0.03350  0.02870  -0.04080 231 ASN B CG  
4116 O OD1 . ASN B 231 ? 0.61910 0.51530 0.88860 0.02980  0.02620  -0.03790 231 ASN B OD1 
4117 N ND2 . ASN B 231 ? 0.58620 0.47770 0.89920 0.03520  0.02500  -0.02810 231 ASN B ND2 
4118 N N   . LEU B 232 ? 0.63550 0.52910 0.94370 0.03660  0.04900  -0.10330 232 LEU B N   
4119 C CA  . LEU B 232 ? 0.64130 0.54170 0.94530 0.03810  0.05620  -0.12350 232 LEU B CA  
4120 C C   . LEU B 232 ? 0.64170 0.54800 0.91770 0.03400  0.05560  -0.12950 232 LEU B C   
4121 O O   . LEU B 232 ? 0.61200 0.52980 0.86790 0.03440  0.05970  -0.13600 232 LEU B O   
4122 C CB  . LEU B 232 ? 0.67230 0.56500 1.00610 0.04000  0.05910  -0.13670 232 LEU B CB  
4123 C CG  . LEU B 232 ? 0.63360 0.52490 0.99440 0.04560  0.06290  -0.13650 232 LEU B CG  
4124 C CD1 . LEU B 232 ? 0.64660 0.53170 1.03480 0.04760  0.06700  -0.15350 232 LEU B CD1 
4125 C CD2 . LEU B 232 ? 0.61900 0.52320 0.96740 0.04890  0.06840  -0.13880 232 LEU B CD2 
4126 N N   . VAL B 233 ? 0.65130 0.55070 0.92490 0.02980  0.05030  -0.12490 233 VAL B N   
4127 C CA  . VAL B 233 ? 0.61800 0.52280 0.86630 0.02580  0.04890  -0.12890 233 VAL B CA  
4128 C C   . VAL B 233 ? 0.60170 0.51380 0.82340 0.02480  0.04690  -0.11680 233 VAL B C   
4129 O O   . VAL B 233 ? 0.59050 0.51230 0.78990 0.02360  0.04890  -0.12240 233 VAL B O   
4130 C CB  . VAL B 233 ? 0.62240 0.51770 0.87820 0.02180  0.04370  -0.12600 233 VAL B CB  
4131 C CG1 . VAL B 233 ? 0.64260 0.54400 0.87270 0.01760  0.04190  -0.12900 233 VAL B CG1 
4132 C CG2 . VAL B 233 ? 0.69590 0.58380 0.97990 0.02270  0.04610  -0.13960 233 VAL B CG2 
4133 N N   . ALA B 234 ? 0.61590 0.52390 0.84000 0.02500  0.04270  -0.09980 234 ALA B N   
4134 C CA  . ALA B 234 ? 0.62670 0.54090 0.82830 0.02410  0.04070  -0.08870 234 ALA B CA  
4135 C C   . ALA B 234 ? 0.60600 0.53130 0.79640 0.02660  0.04630  -0.09480 234 ALA B C   
4136 O O   . ALA B 234 ? 0.58090 0.51380 0.74900 0.02500  0.04670  -0.09370 234 ALA B O   
4137 C CB  . ALA B 234 ? 0.61020 0.51960 0.81980 0.02450  0.03570  -0.07170 234 ALA B CB  
4138 N N   . MET B 235 ? 0.63270 0.55950 0.83940 0.03040  0.05100  -0.10040 235 MET B N   
4139 C CA  . MET B 235 ? 0.65150 0.59010 0.84870 0.03290  0.05700  -0.10560 235 MET B CA  
4140 C C   . MET B 235 ? 0.62630 0.57420 0.80570 0.03150  0.06080  -0.11850 235 MET B C   
4141 O O   . MET B 235 ? 0.63380 0.59120 0.79250 0.03070  0.06200  -0.11550 235 MET B O   
4142 C CB  . MET B 235 ? 0.67280 0.61180 0.89320 0.03740  0.06210  -0.11150 235 MET B CB  
4143 C CG  . MET B 235 ? 0.72770 0.67930 0.94210 0.04030  0.06850  -0.11440 235 MET B CG  
4144 S SD  . MET B 235 ? 0.88200 0.83040 1.12810 0.04550  0.07150  -0.11380 235 MET B SD  
4145 C CE  . MET B 235 ? 0.83590 0.77300 1.09010 0.04370  0.06170  -0.09330 235 MET B CE  
4146 N N   . LYS B 236 ? 0.64930 0.59420 0.83620 0.03070  0.06160  -0.13130 236 LYS B N   
4147 C CA  . LYS B 236 ? 0.62480 0.57990 0.79600 0.02940  0.06480  -0.14490 236 LYS B CA  
4148 C C   . LYS B 236 ? 0.65750 0.61670 0.80350 0.02560  0.06080  -0.13710 236 LYS B C   
4149 O O   . LYS B 236 ? 0.66770 0.63970 0.79560 0.02520  0.06390  -0.14250 236 LYS B O   
4150 C CB  . LYS B 236 ? 0.63470 0.58430 0.82170 0.02870  0.06540  -0.16020 236 LYS B CB  
4151 C CG  . LYS B 236 ? 0.71760 0.67690 0.88910 0.02620  0.06680  -0.17420 236 LYS B CG  
4152 C CD  . LYS B 236 ? 0.85260 0.80710 1.04310 0.02590  0.06810  -0.19210 236 LYS B CD  
4153 C CE  . LYS B 236 ? 1.02550 0.98950 1.19960 0.02230  0.06750  -0.20490 236 LYS B CE  
4154 N NZ  . LYS B 236 ? 1.12250 1.10600 1.27360 0.02340  0.07250  -0.21130 236 LYS B NZ  
4155 N N   . TYR B 237 ? 0.61290 0.56270 0.75740 0.02300  0.05430  -0.12400 237 TYR B N   
4156 C CA  . TYR B 237 ? 0.62940 0.58250 0.75190 0.01980  0.05060  -0.11690 237 TYR B CA  
4157 C C   . TYR B 237 ? 0.62670 0.58150 0.73870 0.02020  0.04900  -0.10200 237 TYR B C   
4158 O O   . TYR B 237 ? 0.59540 0.55000 0.69330 0.01770  0.04510  -0.09380 237 TYR B O   
4159 C CB  . TYR B 237 ? 0.61070 0.55410 0.73670 0.01630  0.04470  -0.11370 237 TYR B CB  
4160 C CG  . TYR B 237 ? 0.63680 0.58060 0.76910 0.01490  0.04590  -0.12920 237 TYR B CG  
4161 C CD1 . TYR B 237 ? 0.59110 0.54400 0.70600 0.01240  0.04590  -0.13630 237 TYR B CD1 
4162 C CD2 . TYR B 237 ? 0.60720 0.54300 0.76400 0.01610  0.04720  -0.13740 237 TYR B CD2 
4163 C CE1 . TYR B 237 ? 0.64350 0.59810 0.76460 0.01090  0.04680  -0.15230 237 TYR B CE1 
4164 C CE2 . TYR B 237 ? 0.63190 0.56810 0.79610 0.01460  0.04830  -0.15350 237 TYR B CE2 
4165 C CZ  . TYR B 237 ? 0.61970 0.56560 0.76550 0.01190  0.04800  -0.16120 237 TYR B CZ  
4166 O OH  . TYR B 237 ? 0.71580 0.66310 0.86910 0.01020  0.04870  -0.17770 237 TYR B OH  
4167 N N   . ASN B 238 ? 0.61180 0.56890 0.73130 0.02330  0.05220  -0.09920 238 ASN B N   
4168 C CA  . ASN B 238 ? 0.58720 0.54700 0.69820 0.02360  0.05100  -0.08650 238 ASN B CA  
4169 C C   . ASN B 238 ? 0.61430 0.56410 0.72650 0.02150  0.04400  -0.07350 238 ASN B C   
4170 O O   . ASN B 238 ? 0.58250 0.53360 0.68060 0.01970  0.04110  -0.06490 238 ASN B O   
4171 C CB  . ASN B 238 ? 0.61970 0.59060 0.70920 0.02250  0.05310  -0.08640 238 ASN B CB  
4172 C CG  . ASN B 238 ? 0.70140 0.67600 0.78540 0.02310  0.05320  -0.07530 238 ASN B CG  
4173 O OD1 . ASN B 238 ? 0.75470 0.72700 0.85120 0.02500  0.05380  -0.07110 238 ASN B OD1 
4174 N ND2 . ASN B 238 ? 0.68150 0.66140 0.74840 0.02140  0.05230  -0.06990 238 ASN B ND2 
4175 N N   . TYR B 239 ? 0.54480 0.48520 0.67410 0.02160  0.04120  -0.07240 239 TYR B N   
4176 C CA  . TYR B 239 ? 0.54090 0.47370 0.67380 0.02000  0.03490  -0.05980 239 TYR B CA  
4177 C C   . TYR B 239 ? 0.56600 0.49740 0.71390 0.02260  0.03460  -0.05320 239 TYR B C   
4178 O O   . TYR B 239 ? 0.57430 0.50650 0.73730 0.02560  0.03870  -0.05950 239 TYR B O   
4179 C CB  . TYR B 239 ? 0.50080 0.42520 0.64450 0.01830  0.03200  -0.06130 239 TYR B CB  
4180 C CG  . TYR B 239 ? 0.54910 0.47320 0.67760 0.01470  0.02920  -0.06130 239 TYR B CG  
4181 C CD1 . TYR B 239 ? 0.56200 0.49350 0.67410 0.01370  0.03190  -0.06940 239 TYR B CD1 
4182 C CD2 . TYR B 239 ? 0.54020 0.45790 0.67130 0.01220  0.02390  -0.05230 239 TYR B CD2 
4183 C CE1 . TYR B 239 ? 0.52730 0.45900 0.62660 0.01040  0.02900  -0.06860 239 TYR B CE1 
4184 C CE2 . TYR B 239 ? 0.53490 0.45280 0.65400 0.00900  0.02170  -0.05200 239 TYR B CE2 
4185 C CZ  . TYR B 239 ? 0.53620 0.46070 0.63990 0.00820  0.02420  -0.06020 239 TYR B CZ  
4186 O OH  . TYR B 239 ? 0.53720 0.46220 0.63040 0.00510  0.02160  -0.05900 239 TYR B OH  
4187 N N   . GLU B 240 ? 0.54970 0.47990 0.69380 0.02140  0.02970  -0.04110 240 GLU B N   
4188 C CA  . GLU B 240 ? 0.53950 0.46900 0.69810 0.02340  0.02800  -0.03360 240 GLU B CA  
4189 C C   . GLU B 240 ? 0.56580 0.48840 0.74700 0.02480  0.02700  -0.03370 240 GLU B C   
4190 O O   . GLU B 240 ? 0.51760 0.43460 0.70130 0.02310  0.02510  -0.03480 240 GLU B O   
4191 C CB  . GLU B 240 ? 0.53730 0.46650 0.68820 0.02120  0.02160  -0.02100 240 GLU B CB  
4192 C CG  . GLU B 240 ? 0.63790 0.57270 0.77030 0.01980  0.02180  -0.01940 240 GLU B CG  
4193 C CD  . GLU B 240 ? 0.78640 0.72630 0.92420 0.02160  0.02330  -0.01670 240 GLU B CD  
4194 O OE1 . GLU B 240 ? 0.88330 0.82250 1.03080 0.02170  0.01890  -0.00880 240 GLU B OE1 
4195 O OE2 . GLU B 240 ? 0.83050 0.77610 0.96440 0.02280  0.02880  -0.02230 240 GLU B OE2 
4196 N N   . PRO B 241 ? 0.59110 0.51420 0.79070 0.02800  0.02830  -0.03240 241 PRO B N   
4197 C CA  . PRO B 241 ? 0.53340 0.44960 0.75730 0.02950  0.02670  -0.03010 241 PRO B CA  
4198 C C   . PRO B 241 ? 0.58690 0.49930 0.81160 0.02710  0.01900  -0.01620 241 PRO B C   
4199 O O   . PRO B 241 ? 0.60510 0.52120 0.81650 0.02520  0.01480  -0.00720 241 PRO B O   
4200 C CB  . PRO B 241 ? 0.62710 0.54670 0.86850 0.03350  0.02930  -0.02970 241 PRO B CB  
4201 C CG  . PRO B 241 ? 0.57780 0.50590 0.80460 0.03430  0.03520  -0.03750 241 PRO B CG  
4202 C CD  . PRO B 241 ? 0.57680 0.50710 0.77780 0.03050  0.03210  -0.03360 241 PRO B CD  
4203 N N   . LEU B 242 ? 0.56560 0.47090 0.80560 0.02680  0.01740  -0.01480 242 LEU B N   
4204 C CA  . LEU B 242 ? 0.59570 0.49850 0.83900 0.02460  0.01050  -0.00060 242 LEU B CA  
4205 C C   . LEU B 242 ? 0.59860 0.50080 0.86640 0.02750  0.00810  0.00870  242 LEU B C   
4206 O O   . LEU B 242 ? 0.58280 0.48020 0.87410 0.03030  0.01110  0.00410  242 LEU B O   
4207 C CB  . LEU B 242 ? 0.52910 0.42520 0.77610 0.02230  0.00980  -0.00230 242 LEU B CB  
4208 C CG  . LEU B 242 ? 0.54640 0.44240 0.79080 0.01940  0.00310  0.01320  242 LEU B CG  
4209 C CD1 . LEU B 242 ? 0.55210 0.45380 0.76740 0.01640  0.00120  0.01490  242 LEU B CD1 
4210 C CD2 . LEU B 242 ? 0.51280 0.40140 0.77080 0.01770  0.00250  0.01370  242 LEU B CD2 
4211 N N   . THR B 243 ? 0.58190 0.48910 0.84500 0.02660  0.00240  0.02170  243 THR B N   
4212 C CA  . THR B 243 ? 0.61080 0.51970 0.89570 0.02910  -0.00080 0.03210  243 THR B CA  
4213 C C   . THR B 243 ? 0.65310 0.56020 0.94780 0.02750  -0.00690 0.04640  243 THR B C   
4214 O O   . THR B 243 ? 0.57040 0.47680 0.85100 0.02400  -0.00940 0.05000  243 THR B O   
4215 C CB  . THR B 243 ? 0.62580 0.54350 0.90040 0.02910  -0.00350 0.03730  243 THR B CB  
4216 O OG1 . THR B 243 ? 0.61560 0.53740 0.87090 0.02520  -0.00950 0.04620  243 THR B OG1 
4217 C CG2 . THR B 243 ? 0.63290 0.55310 0.89380 0.02980  0.00250  0.02440  243 THR B CG2 
4218 N N   . GLN B 244 ? 0.60560 0.51310 0.92510 0.03020  -0.00950 0.05590  244 GLN B N   
4219 C CA  . GLN B 244 ? 0.64880 0.55680 0.97880 0.02880  -0.01580 0.07230  244 GLN B CA  
4220 C C   . GLN B 244 ? 0.63380 0.55130 0.94010 0.02520  -0.02220 0.08290  244 GLN B C   
4221 O O   . GLN B 244 ? 0.63620 0.55470 0.93800 0.02240  -0.02600 0.09260  244 GLN B O   
4222 C CB  . GLN B 244 ? 0.62750 0.53590 0.98930 0.03280  -0.01770 0.08170  244 GLN B CB  
4223 C CG  . GLN B 244 ? 0.64170 0.55070 1.01850 0.03170  -0.02380 0.10000  244 GLN B CG  
4224 C CD  . GLN B 244 ? 0.67160 0.57120 1.05420 0.02970  -0.02180 0.09800  244 GLN B CD  
4225 O OE1 . GLN B 244 ? 0.70480 0.60700 1.08270 0.02660  -0.02640 0.11070  244 GLN B OE1 
4226 N NE2 . GLN B 244 ? 0.67230 0.56200 1.06550 0.03140  -0.01500 0.08200  244 GLN B NE2 
4227 N N   . ASP B 245 ? 0.61630 0.54080 0.90660 0.02500  -0.02280 0.07990  245 ASP B N   
4228 C CA  . ASP B 245 ? 0.62830 0.56170 0.89600 0.02150  -0.02860 0.08750  245 ASP B CA  
4229 C C   . ASP B 245 ? 0.65780 0.58850 0.90310 0.01800  -0.02720 0.08260  245 ASP B C   
4230 O O   . ASP B 245 ? 0.65250 0.58830 0.88720 0.01510  -0.03180 0.09190  245 ASP B O   
4231 C CB  . ASP B 245 ? 0.68980 0.63020 0.94670 0.02180  -0.02920 0.08360  245 ASP B CB  
4232 C CG  . ASP B 245 ? 0.77870 0.72950 1.01670 0.01840  -0.03610 0.09180  245 ASP B CG  
4233 O OD1 . ASP B 245 ? 0.80480 0.76080 1.04540 0.01700  -0.04180 0.10480  245 ASP B OD1 
4234 O OD2 . ASP B 245 ? 0.96710 0.92150 1.18800 0.01710  -0.03570 0.08520  245 ASP B OD2 
4235 N N   . HIS B 246 ? 0.62570 0.54990 0.86370 0.01830  -0.02080 0.06800  246 HIS B N   
4236 C CA  . HIS B 246 ? 0.60710 0.52840 0.82710 0.01530  -0.01900 0.06280  246 HIS B CA  
4237 C C   . HIS B 246 ? 0.61990 0.53700 0.85100 0.01390  -0.02060 0.07020  246 HIS B C   
4238 O O   . HIS B 246 ? 0.55320 0.47290 0.77010 0.01070  -0.02280 0.07490  246 HIS B O   
4239 C CB  . HIS B 246 ? 0.56210 0.47800 0.77640 0.01620  -0.01200 0.04640  246 HIS B CB  
4240 C CG  . HIS B 246 ? 0.61010 0.53050 0.81130 0.01700  -0.00980 0.03940  246 HIS B CG  
4241 N ND1 . HIS B 246 ? 0.60200 0.52040 0.80780 0.01960  -0.00370 0.02780  246 HIS B ND1 
4242 C CD2 . HIS B 246 ? 0.61740 0.54450 0.80160 0.01550  -0.01260 0.04210  246 HIS B CD2 
4243 C CE1 . HIS B 246 ? 0.59410 0.51790 0.78690 0.01950  -0.00280 0.02500  246 HIS B CE1 
4244 N NE2 . HIS B 246 ? 0.56940 0.49780 0.74960 0.01700  -0.00820 0.03320  246 HIS B NE2 
4245 N N   . VAL B 247 ? 0.61460 0.52530 0.87250 0.01630  -0.01910 0.07120  247 VAL B N   
4246 C CA  . VAL B 247 ? 0.60130 0.50790 0.87340 0.01490  -0.02080 0.07970  247 VAL B CA  
4247 C C   . VAL B 247 ? 0.63070 0.54630 0.89860 0.01290  -0.02770 0.09810  247 VAL B C   
4248 O O   . VAL B 247 ? 0.56860 0.48540 0.83060 0.00980  -0.02940 0.10500  247 VAL B O   
4249 C CB  . VAL B 247 ? 0.61370 0.51210 0.91890 0.01820  -0.01840 0.07850  247 VAL B CB  
4250 C CG1 . VAL B 247 ? 0.57660 0.47090 0.89970 0.01650  -0.02080 0.09020  247 VAL B CG1 
4251 C CG2 . VAL B 247 ? 0.56170 0.45250 0.86980 0.01990  -0.01130 0.05910  247 VAL B CG2 
4252 N N   . ASP B 248 ? 0.61390 0.53760 0.88430 0.01440  -0.03170 0.10620  248 ASP B N   
4253 C CA  . ASP B 248 ? 0.61420 0.54880 0.88050 0.01250  -0.03870 0.12360  248 ASP B CA  
4254 C C   . ASP B 248 ? 0.57990 0.52190 0.81510 0.00890  -0.04030 0.12250  248 ASP B C   
4255 O O   . ASP B 248 ? 0.64290 0.59160 0.87200 0.00630  -0.04390 0.13410  248 ASP B O   
4256 C CB  . ASP B 248 ? 0.63990 0.58250 0.91510 0.01490  -0.04290 0.13080  248 ASP B CB  
4257 C CG  . ASP B 248 ? 0.66220 0.59920 0.97140 0.01880  -0.04220 0.13530  248 ASP B CG  
4258 O OD1 . ASP B 248 ? 0.70360 0.63250 1.03090 0.01910  -0.04030 0.13810  248 ASP B OD1 
4259 O OD2 . ASP B 248 ? 0.72750 0.66800 1.04640 0.02170  -0.04320 0.13530  248 ASP B OD2 
4260 N N   . ILE B 249 ? 0.59640 0.53750 0.81250 0.00860  -0.03730 0.10880  249 ILE B N   
4261 C CA  . ILE B 249 ? 0.60230 0.54980 0.79060 0.00550  -0.03850 0.10660  249 ILE B CA  
4262 C C   . ILE B 249 ? 0.59960 0.54260 0.78150 0.00310  -0.03580 0.10500  249 ILE B C   
4263 O O   . ILE B 249 ? 0.64360 0.59350 0.80890 0.00030  -0.03790 0.10980  249 ILE B O   
4264 C CB  . ILE B 249 ? 0.58810 0.53500 0.76120 0.00610  -0.03570 0.09290  249 ILE B CB  
4265 C CG1 . ILE B 249 ? 0.61160 0.56630 0.78720 0.00730  -0.03980 0.09670  249 ILE B CG1 
4266 C CG2 . ILE B 249 ? 0.59310 0.54290 0.74100 0.00330  -0.03510 0.08780  249 ILE B CG2 
4267 C CD1 . ILE B 249 ? 0.66210 0.61340 0.83690 0.00920  -0.03580 0.08460  249 ILE B CD1 
4268 N N   . LEU B 250 ? 0.60000 0.53220 0.79610 0.00410  -0.03140 0.09850  250 LEU B N   
4269 C CA  . LEU B 250 ? 0.55810 0.48580 0.75210 0.00170  -0.02920 0.09730  250 LEU B CA  
4270 C C   . LEU B 250 ? 0.61590 0.54590 0.82460 0.00020  -0.03250 0.11350  250 LEU B C   
4271 O O   . LEU B 250 ? 0.60500 0.53170 0.81470 -0.00220 -0.03090 0.11420  250 LEU B O   
4272 C CB  . LEU B 250 ? 0.54080 0.45710 0.74560 0.00300  -0.02360 0.08340  250 LEU B CB  
4273 C CG  . LEU B 250 ? 0.58550 0.49810 0.77410 0.00270  -0.01880 0.06670  250 LEU B CG  
4274 C CD1 . LEU B 250 ? 0.52110 0.43970 0.68120 0.00050  -0.01900 0.06370  250 LEU B CD1 
4275 C CD2 . LEU B 250 ? 0.49920 0.40680 0.69570 0.00580  -0.01460 0.05440  250 LEU B CD2 
4276 N N   . GLY B 251 ? 0.59980 0.53590 0.82110 0.00140  -0.03700 0.12720  251 GLY B N   
4277 C CA  . GLY B 251 ? 0.58470 0.52380 0.82300 0.00030  -0.04010 0.14450  251 GLY B CA  
4278 C C   . GLY B 251 ? 0.59490 0.54180 0.81750 -0.00350 -0.04150 0.15260  251 GLY B C   
4279 O O   . GLY B 251 ? 0.67670 0.62000 0.91130 -0.00530 -0.04040 0.15880  251 GLY B O   
4280 N N   . PRO B 252 ? 0.60490 0.56360 0.80180 -0.00490 -0.04390 0.15330  252 PRO B N   
4281 C CA  . PRO B 252 ? 0.61530 0.58290 0.79750 -0.00840 -0.04470 0.16110  252 PRO B CA  
4282 C C   . PRO B 252 ? 0.63340 0.59200 0.81220 -0.01020 -0.03960 0.15160  252 PRO B C   
4283 O O   . PRO B 252 ? 0.62560 0.58670 0.80870 -0.01270 -0.03940 0.16100  252 PRO B O   
4284 C CB  . PRO B 252 ? 0.60530 0.58490 0.76030 -0.00900 -0.04710 0.15780  252 PRO B CB  
4285 C CG  . PRO B 252 ? 0.62250 0.60390 0.78560 -0.00620 -0.05050 0.15830  252 PRO B CG  
4286 C CD  . PRO B 252 ? 0.62030 0.58650 0.80450 -0.00360 -0.04680 0.15040  252 PRO B CD  
4287 N N   . LEU B 253 ? 0.62790 0.57670 0.80090 -0.00910 -0.03560 0.13380  253 LEU B N   
4288 C CA  . LEU B 253 ? 0.57100 0.51210 0.74080 -0.01080 -0.03110 0.12380  253 LEU B CA  
4289 C C   . LEU B 253 ? 0.59140 0.52230 0.78840 -0.01110 -0.02950 0.12600  253 LEU B C   
4290 O O   . LEU B 253 ? 0.57290 0.50210 0.77160 -0.01390 -0.02790 0.12700  253 LEU B O   
4291 C CB  . LEU B 253 ? 0.58090 0.51620 0.73740 -0.00940 -0.02760 0.10540  253 LEU B CB  
4292 C CG  . LEU B 253 ? 0.65600 0.59570 0.78580 -0.01070 -0.02600 0.09690  253 LEU B CG  
4293 C CD1 . LEU B 253 ? 0.62480 0.57640 0.73760 -0.01320 -0.02800 0.10560  253 LEU B CD1 
4294 C CD2 . LEU B 253 ? 0.50970 0.44860 0.62800 -0.00850 -0.02500 0.08560  253 LEU B CD2 
4295 N N   . SER B 254 ? 0.56170 0.48540 0.78130 -0.00840 -0.02960 0.12570  254 SER B N   
4296 C CA  . SER B 254 ? 0.60580 0.52030 0.85490 -0.00860 -0.02850 0.12920  254 SER B CA  
4297 C C   . SER B 254 ? 0.61130 0.53240 0.87050 -0.01100 -0.03170 0.14940  254 SER B C   
4298 O O   . SER B 254 ? 0.61010 0.52580 0.88550 -0.01320 -0.03040 0.15260  254 SER B O   
4299 C CB  . SER B 254 ? 0.53550 0.44260 0.80950 -0.00490 -0.02840 0.12760  254 SER B CB  
4300 O OG  . SER B 254 ? 0.70160 0.61380 0.96310 -0.00230 -0.02950 0.12430  254 SER B OG  
4301 N N   . ALA B 255 ? 0.62070 0.55440 0.87220 -0.01070 -0.03600 0.16370  255 ALA B N   
4302 C CA  . ALA B 255 ? 0.63940 0.58210 0.90060 -0.01270 -0.03920 0.18500  255 ALA B CA  
4303 C C   . ALA B 255 ? 0.60010 0.54820 0.84600 -0.01670 -0.03770 0.18730  255 ALA B C   
4304 O O   . ALA B 255 ? 0.60780 0.55500 0.87050 -0.01910 -0.03730 0.19820  255 ALA B O   
4305 C CB  . ALA B 255 ? 0.58790 0.54530 0.84020 -0.01150 -0.04440 0.19810  255 ALA B CB  
4306 N N   . GLN B 256 ? 0.62690 0.58020 0.84330 -0.01750 -0.03640 0.17650  256 GLN B N   
4307 C CA  . GLN B 256 ? 0.59230 0.55180 0.79360 -0.02090 -0.03470 0.17810  256 GLN B CA  
4308 C C   . GLN B 256 ? 0.60730 0.55470 0.82130 -0.02280 -0.03070 0.16970  256 GLN B C   
4309 O O   . GLN B 256 ? 0.58490 0.53560 0.80430 -0.02600 -0.03000 0.17870  256 GLN B O   
4310 C CB  . GLN B 256 ? 0.63020 0.59690 0.79920 -0.02070 -0.03400 0.16720  256 GLN B CB  
4311 C CG  . GLN B 256 ? 0.63080 0.60350 0.78490 -0.02380 -0.03170 0.16690  256 GLN B CG  
4312 C CD  . GLN B 256 ? 0.70090 0.67790 0.82680 -0.02320 -0.03040 0.15380  256 GLN B CD  
4313 O OE1 . GLN B 256 ? 0.74700 0.72290 0.86430 -0.02070 -0.03150 0.14580  256 GLN B OE1 
4314 N NE2 . GLN B 256 ? 0.66140 0.64270 0.77410 -0.02540 -0.02780 0.15130  256 GLN B NE2 
4315 N N   . THR B 257 ? 0.59420 0.52840 0.81430 -0.02110 -0.02820 0.15260  257 THR B N   
4316 C CA  . THR B 257 ? 0.51290 0.43660 0.74390 -0.02300 -0.02490 0.14230  257 THR B CA  
4317 C C   . THR B 257 ? 0.57190 0.48540 0.83800 -0.02320 -0.02500 0.14740  257 THR B C   
4318 O O   . THR B 257 ? 0.60010 0.50580 0.87900 -0.02550 -0.02280 0.14110  257 THR B O   
4319 C CB  . THR B 257 ? 0.57370 0.48970 0.79330 -0.02130 -0.02200 0.12050  257 THR B CB  
4320 O OG1 . THR B 257 ? 0.57270 0.48240 0.80340 -0.01760 -0.02220 0.11540  257 THR B OG1 
4321 C CG2 . THR B 257 ? 0.55430 0.47880 0.74120 -0.02130 -0.02150 0.11440  257 THR B CG2 
4322 N N   . GLY B 258 ? 0.57780 0.49100 0.86100 -0.02070 -0.02750 0.15770  258 GLY B N   
4323 C CA  . GLY B 258 ? 0.59000 0.49230 0.90920 -0.02030 -0.02720 0.16130  258 GLY B CA  
4324 C C   . GLY B 258 ? 0.59850 0.48670 0.92970 -0.01820 -0.02400 0.14070  258 GLY B C   
4325 O O   . GLY B 258 ? 0.58140 0.45910 0.94310 -0.01840 -0.02310 0.14000  258 GLY B O   
4326 N N   . ILE B 259 ? 0.56910 0.45710 0.87820 -0.01620 -0.02220 0.12420  259 ILE B N   
4327 C CA  . ILE B 259 ? 0.55750 0.43480 0.87420 -0.01420 -0.01880 0.10380  259 ILE B CA  
4328 C C   . ILE B 259 ? 0.58510 0.46240 0.90510 -0.00950 -0.01930 0.10280  259 ILE B C   
4329 O O   . ILE B 259 ? 0.58410 0.46950 0.88050 -0.00810 -0.02040 0.10310  259 ILE B O   
4330 C CB  . ILE B 259 ? 0.58770 0.46620 0.87720 -0.01530 -0.01610 0.08640  259 ILE B CB  
4331 C CG1 . ILE B 259 ? 0.62150 0.50260 0.90390 -0.02000 -0.01590 0.08840  259 ILE B CG1 
4332 C CG2 . ILE B 259 ? 0.58090 0.45030 0.87860 -0.01340 -0.01240 0.06580  259 ILE B CG2 
4333 C CD1 . ILE B 259 ? 0.62380 0.49560 0.92820 -0.02230 -0.01420 0.08030  259 ILE B CD1 
4334 N N   . ALA B 260 ? 0.56690 0.43540 0.91720 -0.00700 -0.01860 0.10180  260 ALA B N   
4335 C CA  . ALA B 260 ? 0.50960 0.37820 0.86500 -0.00230 -0.01860 0.10000  260 ALA B CA  
4336 C C   . ALA B 260 ? 0.53430 0.40360 0.86630 -0.00060 -0.01530 0.08090  260 ALA B C   
4337 O O   . ALA B 260 ? 0.52700 0.39270 0.85000 -0.00220 -0.01210 0.06540  260 ALA B O   
4338 C CB  . ALA B 260 ? 0.55590 0.41350 0.94970 0.00020  -0.01720 0.09830  260 ALA B CB  
4339 N N   . VAL B 261 ? 0.53540 0.41050 0.85750 0.00240  -0.01640 0.08260  261 VAL B N   
4340 C CA  . VAL B 261 ? 0.52400 0.40070 0.82500 0.00400  -0.01320 0.06650  261 VAL B CA  
4341 C C   . VAL B 261 ? 0.52430 0.39200 0.83940 0.00580  -0.00800 0.04780  261 VAL B C   
4342 O O   . VAL B 261 ? 0.51440 0.38210 0.81270 0.00500  -0.00470 0.03260  261 VAL B O   
4343 C CB  . VAL B 261 ? 0.56210 0.44570 0.85700 0.00710  -0.01520 0.07190  261 VAL B CB  
4344 C CG1 . VAL B 261 ? 0.49950 0.38410 0.77700 0.00890  -0.01130 0.05560  261 VAL B CG1 
4345 C CG2 . VAL B 261 ? 0.56890 0.46330 0.84520 0.00510  -0.02030 0.08700  261 VAL B CG2 
4346 N N   . LEU B 262 ? 0.52420 0.38490 0.87060 0.00840  -0.00700 0.04820  262 LEU B N   
4347 C CA  . LEU B 262 ? 0.55040 0.40340 0.90970 0.01020  -0.00170 0.02860  262 LEU B CA  
4348 C C   . LEU B 262 ? 0.56130 0.40830 0.92490 0.00650  -0.00020 0.01930  262 LEU B C   
4349 O O   . LEU B 262 ? 0.53610 0.37960 0.90170 0.00700  0.00410  0.00030  262 LEU B O   
4350 C CB  . LEU B 262 ? 0.57950 0.42650 0.97290 0.01450  -0.00060 0.02980  262 LEU B CB  
4351 C CG  . LEU B 262 ? 0.57630 0.42920 0.96760 0.01870  -0.00090 0.03400  262 LEU B CG  
4352 C CD1 . LEU B 262 ? 0.60180 0.44820 1.02930 0.02260  0.00010  0.03590  262 LEU B CD1 
4353 C CD2 . LEU B 262 ? 0.57650 0.43330 0.94650 0.02020  0.00370  0.01670  262 LEU B CD2 
4354 N N   . ASP B 263 ? 0.54900 0.39590 0.91460 0.00260  -0.00360 0.03210  263 ASP B N   
4355 C CA  . ASP B 263 ? 0.53010 0.37330 0.89490 -0.00140 -0.00250 0.02280  263 ASP B CA  
4356 C C   . ASP B 263 ? 0.53900 0.38940 0.86840 -0.00330 -0.00130 0.01300  263 ASP B C   
4357 O O   . ASP B 263 ? 0.53300 0.38160 0.85830 -0.00460 0.00150  -0.00400 263 ASP B O   
4358 C CB  . ASP B 263 ? 0.61150 0.45330 0.99020 -0.00490 -0.00620 0.04070  263 ASP B CB  
4359 C CG  . ASP B 263 ? 0.76030 0.59890 1.14060 -0.00980 -0.00560 0.03380  263 ASP B CG  
4360 O OD1 . ASP B 263 ? 0.65890 0.49630 1.02920 -0.01100 -0.00280 0.01450  263 ASP B OD1 
4361 O OD2 . ASP B 263 ? 0.87810 0.71560 1.27250 -0.01270 -0.00820 0.04930  263 ASP B OD2 
4362 N N   . MET B 264 ? 0.50040 0.35960 0.80460 -0.00330 -0.00360 0.02290  264 MET B N   
4363 C CA  . MET B 264 ? 0.50570 0.37160 0.77810 -0.00440 -0.00230 0.01400  264 MET B CA  
4364 C C   . MET B 264 ? 0.53580 0.40230 0.80140 -0.00120 0.00190  -0.00310 264 MET B C   
4365 O O   . MET B 264 ? 0.49740 0.36760 0.74360 -0.00220 0.00400  -0.01500 264 MET B O   
4366 C CB  . MET B 264 ? 0.43020 0.30500 0.68030 -0.00470 -0.00550 0.02770  264 MET B CB  
4367 C CG  . MET B 264 ? 0.45920 0.34070 0.67770 -0.00610 -0.00450 0.02080  264 MET B CG  
4368 S SD  . MET B 264 ? 0.50730 0.38830 0.72360 -0.01120 -0.00510 0.02050  264 MET B SD  
4369 C CE  . MET B 264 ? 0.52270 0.41090 0.73100 -0.01270 -0.00930 0.04200  264 MET B CE  
4370 N N   . CYS B 265 ? 0.53250 0.39690 0.81260 0.00280  0.00310  -0.00330 265 CYS B N   
4371 C CA  . CYS B 265 ? 0.52900 0.39480 0.80450 0.00580  0.00780  -0.01960 265 CYS B CA  
4372 C C   . CYS B 265 ? 0.51340 0.37470 0.79900 0.00490  0.01130  -0.03740 265 CYS B C   
4373 O O   . CYS B 265 ? 0.54400 0.40980 0.81480 0.00530  0.01480  -0.05200 265 CYS B O   
4374 C CB  . CYS B 265 ? 0.52450 0.38910 0.81740 0.01040  0.00880  -0.01650 265 CYS B CB  
4375 S SG  . CYS B 265 ? 0.54230 0.41480 0.81970 0.01170  0.00500  -0.00030 265 CYS B SG  
4376 N N   . ALA B 266 ? 0.51970 0.37290 0.83050 0.00320  0.01030  -0.03620 266 ALA B N   
4377 C CA  . ALA B 266 ? 0.55430 0.40330 0.87550 0.00150  0.01290  -0.05370 266 ALA B CA  
4378 C C   . ALA B 266 ? 0.54750 0.40210 0.84390 -0.00260 0.01230  -0.05960 266 ALA B C   
4379 O O   . ALA B 266 ? 0.56070 0.41770 0.85190 -0.00320 0.01510  -0.07730 266 ALA B O   
4380 C CB  . ALA B 266 ? 0.57470 0.41320 0.93030 0.00010  0.01140  -0.04940 266 ALA B CB  
4381 N N   . SER B 267 ? 0.54160 0.39970 0.82270 -0.00530 0.00860  -0.04500 267 SER B N   
4382 C CA  . SER B 267 ? 0.53390 0.39840 0.79090 -0.00850 0.00810  -0.04990 267 SER B CA  
4383 C C   . SER B 267 ? 0.53610 0.40910 0.76700 -0.00640 0.01060  -0.05810 267 SER B C   
4384 O O   . SER B 267 ? 0.51400 0.39200 0.73170 -0.00780 0.01220  -0.07090 267 SER B O   
4385 C CB  . SER B 267 ? 0.53940 0.40640 0.78650 -0.01150 0.00410  -0.03240 267 SER B CB  
4386 O OG  . SER B 267 ? 0.58830 0.44850 0.85890 -0.01420 0.00230  -0.02690 267 SER B OG  
4387 N N   . LEU B 268 ? 0.52190 0.39780 0.74470 -0.00320 0.01070  -0.04990 268 LEU B N   
4388 C CA  . LEU B 268 ? 0.54430 0.42830 0.74470 -0.00110 0.01340  -0.05670 268 LEU B CA  
4389 C C   . LEU B 268 ? 0.54190 0.42710 0.74800 0.00080  0.01810  -0.07520 268 LEU B C   
4390 O O   . LEU B 268 ? 0.52440 0.41710 0.71270 0.00030  0.02020  -0.08530 268 LEU B O   
4391 C CB  . LEU B 268 ? 0.51680 0.40300 0.71200 0.00180  0.01260  -0.04540 268 LEU B CB  
4392 C CG  . LEU B 268 ? 0.51510 0.40940 0.68910 0.00390  0.01510  -0.04920 268 LEU B CG  
4393 C CD1 . LEU B 268 ? 0.51270 0.41320 0.66290 0.00140  0.01490  -0.05220 268 LEU B CD1 
4394 C CD2 . LEU B 268 ? 0.45800 0.35370 0.62870 0.00560  0.01270  -0.03550 268 LEU B CD2 
4395 N N   . LYS B 269 ? 0.53540 0.41420 0.76690 0.00300  0.01990  -0.07990 269 LYS B N   
4396 C CA  . LYS B 269 ? 0.55320 0.43350 0.79190 0.00490  0.02480  -0.09910 269 LYS B CA  
4397 C C   . LYS B 269 ? 0.61480 0.49840 0.84630 0.00130  0.02510  -0.11280 269 LYS B C   
4398 O O   . LYS B 269 ? 0.63540 0.52800 0.85200 0.00190  0.02830  -0.12590 269 LYS B O   
4399 C CB  . LYS B 269 ? 0.56370 0.43460 0.83560 0.00720  0.02610  -0.10150 269 LYS B CB  
4400 C CG  . LYS B 269 ? 0.65310 0.52440 0.93720 0.00860  0.03110  -0.12310 269 LYS B CG  
4401 C CD  . LYS B 269 ? 0.73730 0.59830 1.05780 0.01130  0.03260  -0.12590 269 LYS B CD  
4402 C CE  . LYS B 269 ? 0.73040 0.58820 1.06190 0.01500  0.03160  -0.10950 269 LYS B CE  
4403 N NZ  . LYS B 269 ? 0.74250 0.59020 1.11160 0.01750  0.03300  -0.11230 269 LYS B NZ  
4404 N N   . GLU B 270 ? 0.58920 0.46670 0.83110 -0.00260 0.02150  -0.10950 270 GLU B N   
4405 C CA  . GLU B 270 ? 0.63800 0.51870 0.87540 -0.00650 0.02110  -0.12230 270 GLU B CA  
4406 C C   . GLU B 270 ? 0.62600 0.51810 0.83120 -0.00790 0.02040  -0.12110 270 GLU B C   
4407 O O   . GLU B 270 ? 0.63700 0.53720 0.83120 -0.00900 0.02190  -0.13540 270 GLU B O   
4408 C CB  . GLU B 270 ? 0.65800 0.52970 0.91510 -0.01060 0.01730  -0.11640 270 GLU B CB  
4409 C CG  . GLU B 270 ? 0.79620 0.67010 1.05450 -0.01500 0.01640  -0.13020 270 GLU B CG  
4410 C CD  . GLU B 270 ? 1.01780 0.88240 1.29880 -0.01940 0.01280  -0.12360 270 GLU B CD  
4411 O OE1 . GLU B 270 ? 0.86860 0.72910 1.15310 -0.02020 0.00990  -0.10430 270 GLU B OE1 
4412 O OE2 . GLU B 270 ? 1.20150 1.06400 1.49710 -0.02230 0.01270  -0.13820 270 GLU B OE2 
4413 N N   . LEU B 271 ? 0.54470 0.43810 0.73520 -0.00780 0.01800  -0.10440 271 LEU B N   
4414 C CA  . LEU B 271 ? 0.57190 0.47540 0.73400 -0.00860 0.01750  -0.10220 271 LEU B CA  
4415 C C   . LEU B 271 ? 0.62470 0.53720 0.77260 -0.00530 0.02160  -0.11080 271 LEU B C   
4416 O O   . LEU B 271 ? 0.58740 0.50980 0.71690 -0.00620 0.02230  -0.11690 271 LEU B O   
4417 C CB  . LEU B 271 ? 0.56340 0.46610 0.71510 -0.00870 0.01450  -0.08380 271 LEU B CB  
4418 C CG  . LEU B 271 ? 0.52680 0.42440 0.68660 -0.01240 0.01060  -0.07410 271 LEU B CG  
4419 C CD1 . LEU B 271 ? 0.52780 0.42590 0.67750 -0.01170 0.00840  -0.05710 271 LEU B CD1 
4420 C CD2 . LEU B 271 ? 0.62060 0.52330 0.77060 -0.01610 0.00930  -0.08000 271 LEU B CD2 
4421 N N   . LEU B 272 ? 0.56040 0.47060 0.71690 -0.00150 0.02440  -0.11030 272 LEU B N   
4422 C CA  . LEU B 272 ? 0.60600 0.52560 0.75100 0.00160  0.02900  -0.11850 272 LEU B CA  
4423 C C   . LEU B 272 ? 0.64690 0.57200 0.79550 0.00120  0.03220  -0.13830 272 LEU B C   
4424 O O   . LEU B 272 ? 0.68120 0.61850 0.81220 0.00170  0.03470  -0.14570 272 LEU B O   
4425 C CB  . LEU B 272 ? 0.53770 0.45380 0.69390 0.00580  0.03130  -0.11360 272 LEU B CB  
4426 C CG  . LEU B 272 ? 0.55480 0.46860 0.70460 0.00640  0.02840  -0.09560 272 LEU B CG  
4427 C CD1 . LEU B 272 ? 0.55570 0.46710 0.71860 0.01040  0.03060  -0.09240 272 LEU B CD1 
4428 C CD2 . LEU B 272 ? 0.56570 0.48880 0.68910 0.00590  0.02840  -0.09130 272 LEU B CD2 
4429 N N   . GLN B 273 ? 0.60140 0.51850 0.77340 0.00030  0.03210  -0.14720 273 GLN B N   
4430 C CA  . GLN B 273 ? 0.65620 0.57880 0.83360 0.00030  0.03550  -0.16810 273 GLN B CA  
4431 C C   . GLN B 273 ? 0.71610 0.64600 0.88090 -0.00410 0.03300  -0.17620 273 GLN B C   
4432 O O   . GLN B 273 ? 0.71000 0.65130 0.86650 -0.00410 0.03570  -0.19190 273 GLN B O   
4433 C CB  . GLN B 273 ? 0.64790 0.55890 0.85750 0.00100  0.03650  -0.17580 273 GLN B CB  
4434 C CG  . GLN B 273 ? 0.66790 0.57480 0.89130 0.00610  0.04020  -0.17280 273 GLN B CG  
4435 C CD  . GLN B 273 ? 0.72960 0.62300 0.98820 0.00710  0.04050  -0.17610 273 GLN B CD  
4436 O OE1 . GLN B 273 ? 0.79000 0.67480 1.06420 0.00370  0.03710  -0.17630 273 GLN B OE1 
4437 N NE2 . GLN B 273 ? 0.72760 0.61940 1.00020 0.01180  0.04460  -0.17820 273 GLN B NE2 
4438 N N   . ASN B 274 ? 0.67600 0.60110 0.83930 -0.00780 0.02790  -0.16560 274 ASN B N   
4439 C CA  . ASN B 274 ? 0.74290 0.67360 0.89910 -0.01230 0.02490  -0.17250 274 ASN B CA  
4440 C C   . ASN B 274 ? 0.74790 0.68610 0.87950 -0.01400 0.02190  -0.16070 274 ASN B C   
4441 O O   . ASN B 274 ? 0.77320 0.71930 0.89600 -0.01730 0.01980  -0.16720 274 ASN B O   
4442 C CB  . ASN B 274 ? 0.75150 0.67010 0.93200 -0.01600 0.02150  -0.17270 274 ASN B CB  
4443 C CG  . ASN B 274 ? 0.82700 0.73670 1.03580 -0.01430 0.02420  -0.18410 274 ASN B CG  
4444 O OD1 . ASN B 274 ? 0.97850 0.87530 1.21020 -0.01470 0.02270  -0.17620 274 ASN B OD1 
4445 N ND2 . ASN B 274 ? 0.81210 0.72950 1.01960 -0.01210 0.02860  -0.20190 274 ASN B ND2 
4446 N N   . GLY B 275 ? 0.73360 0.66960 0.85560 -0.01200 0.02150  -0.14410 275 GLY B N   
4447 C CA  . GLY B 275 ? 0.68470 0.62670 0.78640 -0.01340 0.01890  -0.13320 275 GLY B CA  
4448 C C   . GLY B 275 ? 0.70000 0.63460 0.80970 -0.01720 0.01450  -0.12470 275 GLY B C   
4449 O O   . GLY B 275 ? 0.70190 0.62640 0.83310 -0.01840 0.01350  -0.12460 275 GLY B O   
4450 N N   . MET B 276 ? 0.72430 0.66490 0.81770 -0.01890 0.01200  -0.11740 276 MET B N   
4451 C CA  . MET B 276 ? 0.73660 0.67190 0.83610 -0.02220 0.00840  -0.10760 276 MET B CA  
4452 C C   . MET B 276 ? 0.78760 0.72670 0.89130 -0.02670 0.00590  -0.11650 276 MET B C   
4453 O O   . MET B 276 ? 0.73020 0.66470 0.84260 -0.02980 0.00310  -0.10930 276 MET B O   
4454 C CB  . MET B 276 ? 0.73820 0.67640 0.82030 -0.02130 0.00730  -0.09300 276 MET B CB  
4455 C CG  . MET B 276 ? 0.69930 0.63240 0.78050 -0.01780 0.00880  -0.08300 276 MET B CG  
4456 S SD  . MET B 276 ? 0.70180 0.63610 0.76870 -0.01800 0.00650  -0.06610 276 MET B SD  
4457 C CE  . MET B 276 ? 0.61920 0.55180 0.68110 -0.01350 0.00880  -0.06040 276 MET B CE  
4458 N N   . ASN B 277 ? 0.80150 0.75000 0.89960 -0.02720 0.00670  -0.13160 277 ASN B N   
4459 C CA  . ASN B 277 ? 0.85580 0.80980 0.95770 -0.03170 0.00380  -0.14140 277 ASN B CA  
4460 C C   . ASN B 277 ? 0.85090 0.80950 0.94170 -0.03400 0.00060  -0.13020 277 ASN B C   
4461 O O   . ASN B 277 ? 0.83610 0.79170 0.93830 -0.03810 -0.00230 -0.12890 277 ASN B O   
4462 C CB  . ASN B 277 ? 0.96080 0.90400 1.09020 -0.03470 0.00270  -0.14820 277 ASN B CB  
4463 C CG  . ASN B 277 ? 1.12720 1.06650 1.26990 -0.03250 0.00610  -0.16210 277 ASN B CG  
4464 O OD1 . ASN B 277 ? 1.16780 1.11520 1.30960 -0.03340 0.00680  -0.17950 277 ASN B OD1 
4465 N ND2 . ASN B 277 ? 1.10840 1.03650 1.26370 -0.02960 0.00810  -0.15470 277 ASN B ND2 
4466 N N   . GLY B 278 ? 0.80610 0.77160 0.87620 -0.03130 0.00140  -0.12140 278 GLY B N   
4467 C CA  . GLY B 278 ? 0.78430 0.75540 0.84340 -0.03280 -0.00110 -0.11170 278 GLY B CA  
4468 C C   . GLY B 278 ? 0.78990 0.75210 0.85470 -0.03340 -0.00210 -0.09660 278 GLY B C   
4469 O O   . GLY B 278 ? 0.80830 0.77500 0.86610 -0.03480 -0.00390 -0.08910 278 GLY B O   
4470 N N   . ARG B 279 ? 0.75660 0.70720 0.83480 -0.03250 -0.00110 -0.09180 279 ARG B N   
4471 C CA  . ARG B 279 ? 0.70500 0.64920 0.78690 -0.03280 -0.00190 -0.07670 279 ARG B CA  
4472 C C   . ARG B 279 ? 0.66180 0.60580 0.73000 -0.02870 -0.00010 -0.06730 279 ARG B C   
4473 O O   . ARG B 279 ? 0.69790 0.64500 0.75690 -0.02560 0.00190  -0.07190 279 ARG B O   
4474 C CB  . ARG B 279 ? 0.69570 0.62880 0.80140 -0.03460 -0.00240 -0.07500 279 ARG B CB  
4475 C CG  . ARG B 279 ? 0.74630 0.67910 0.86660 -0.03970 -0.00490 -0.07820 279 ARG B CG  
4476 C CD  . ARG B 279 ? 0.73020 0.65270 0.87680 -0.04130 -0.00490 -0.08250 279 ARG B CD  
4477 N NE  . ARG B 279 ? 0.73190 0.65230 0.88180 -0.03860 -0.00270 -0.09520 279 ARG B NE  
4478 C CZ  . ARG B 279 ? 0.77250 0.68390 0.94540 -0.03900 -0.00200 -0.10170 279 ARG B CZ  
4479 N NH1 . ARG B 279 ? 0.70690 0.61020 0.90290 -0.04220 -0.00370 -0.09650 279 ARG B NH1 
4480 N NH2 . ARG B 279 ? 0.75610 0.66690 0.93000 -0.03580 0.00070  -0.11310 279 ARG B NH2 
4481 N N   . THR B 280 ? 0.62170 0.56290 0.68870 -0.02870 -0.00090 -0.05410 280 THR B N   
4482 C CA  . THR B 280 ? 0.60980 0.55100 0.66460 -0.02530 0.00030  -0.04540 280 THR B CA  
4483 C C   . THR B 280 ? 0.59520 0.52890 0.66060 -0.02530 -0.00030 -0.03490 280 THR B C   
4484 O O   . THR B 280 ? 0.53950 0.46930 0.61980 -0.02810 -0.00160 -0.03150 280 THR B O   
4485 C CB  . THR B 280 ? 0.60730 0.55610 0.64570 -0.02490 -0.00010 -0.03980 280 THR B CB  
4486 O OG1 . THR B 280 ? 0.61020 0.55940 0.65400 -0.02800 -0.00170 -0.03380 280 THR B OG1 
4487 C CG2 . THR B 280 ? 0.62720 0.58500 0.65500 -0.02470 0.00020  -0.04860 280 THR B CG2 
4488 N N   . ILE B 281 ? 0.53920 0.47150 0.59800 -0.02210 0.00060  -0.02970 281 ILE B N   
4489 C CA  . ILE B 281 ? 0.49960 0.42710 0.56520 -0.02150 -0.00030 -0.01890 281 ILE B CA  
4490 C C   . ILE B 281 ? 0.55690 0.48910 0.60630 -0.02000 -0.00040 -0.01100 281 ILE B C   
4491 O O   . ILE B 281 ? 0.46860 0.40320 0.50640 -0.01740 0.00080  -0.01370 281 ILE B O   
4492 C CB  . ILE B 281 ? 0.48960 0.41130 0.56580 -0.01920 0.00060  -0.02130 281 ILE B CB  
4493 C CG1 . ILE B 281 ? 0.52640 0.44360 0.61940 -0.02050 0.00120  -0.03120 281 ILE B CG1 
4494 C CG2 . ILE B 281 ? 0.48660 0.40500 0.56950 -0.01870 -0.00090 -0.00910 281 ILE B CG2 
4495 C CD1 . ILE B 281 ? 0.52790 0.43950 0.63350 -0.01770 0.00270  -0.03550 281 ILE B CD1 
4496 N N   . LEU B 282 ? 0.50100 0.43500 0.55020 -0.02170 -0.00170 -0.00150 282 LEU B N   
4497 C CA  . LEU B 282 ? 0.52720 0.46610 0.56190 -0.02050 -0.00180 0.00520  282 LEU B CA  
4498 C C   . LEU B 282 ? 0.54110 0.48500 0.56130 -0.01920 -0.00050 -0.00070 282 LEU B C   
4499 O O   . LEU B 282 ? 0.55950 0.50520 0.56910 -0.01680 0.00010  0.00040  282 LEU B O   
4500 C CB  . LEU B 282 ? 0.52100 0.45810 0.55470 -0.01830 -0.00240 0.01030  282 LEU B CB  
4501 C CG  . LEU B 282 ? 0.50100 0.43570 0.54760 -0.01950 -0.00410 0.01950  282 LEU B CG  
4502 C CD1 . LEU B 282 ? 0.49500 0.42870 0.54110 -0.01720 -0.00510 0.02360  282 LEU B CD1 
4503 C CD2 . LEU B 282 ? 0.50880 0.44960 0.55170 -0.02190 -0.00480 0.02860  282 LEU B CD2 
4504 N N   . GLY B 283 ? 0.52950 0.47560 0.55070 -0.02070 -0.00020 -0.00720 283 GLY B N   
4505 C CA  . GLY B 283 ? 0.55610 0.50830 0.56480 -0.01950 0.00080  -0.01130 283 GLY B CA  
4506 C C   . GLY B 283 ? 0.61660 0.56910 0.62050 -0.01710 0.00210  -0.01840 283 GLY B C   
4507 O O   . GLY B 283 ? 0.62240 0.58030 0.61590 -0.01560 0.00300  -0.01990 283 GLY B O   
4508 N N   . SER B 284 ? 0.56080 0.50850 0.57290 -0.01650 0.00260  -0.02210 284 SER B N   
4509 C CA  . SER B 284 ? 0.51860 0.46770 0.52640 -0.01410 0.00440  -0.02850 284 SER B CA  
4510 C C   . SER B 284 ? 0.55880 0.50790 0.57510 -0.01530 0.00490  -0.03860 284 SER B C   
4511 O O   . SER B 284 ? 0.53100 0.47450 0.56120 -0.01700 0.00410  -0.04000 284 SER B O   
4512 C CB  . SER B 284 ? 0.54670 0.49140 0.55600 -0.01170 0.00500  -0.02440 284 SER B CB  
4513 O OG  . SER B 284 ? 0.60290 0.54910 0.61030 -0.00950 0.00730  -0.03030 284 SER B OG  
4514 N N   . ALA B 285 ? 0.56510 0.52090 0.57370 -0.01420 0.00650  -0.04570 285 ALA B N   
4515 C CA  . ALA B 285 ? 0.56450 0.52190 0.57940 -0.01480 0.00740  -0.05700 285 ALA B CA  
4516 C C   . ALA B 285 ? 0.56780 0.52310 0.58560 -0.01190 0.01020  -0.06050 285 ALA B C   
4517 O O   . ALA B 285 ? 0.59160 0.54910 0.61410 -0.01180 0.01180  -0.07090 285 ALA B O   
4518 C CB  . ALA B 285 ? 0.57210 0.54050 0.57710 -0.01560 0.00730  -0.06330 285 ALA B CB  
4519 N N   . LEU B 286 ? 0.54950 0.50130 0.56510 -0.00970 0.01080  -0.05250 286 LEU B N   
4520 C CA  . LEU B 286 ? 0.53900 0.48890 0.55870 -0.00690 0.01330  -0.05420 286 LEU B CA  
4521 C C   . LEU B 286 ? 0.57650 0.51710 0.60800 -0.00670 0.01180  -0.04750 286 LEU B C   
4522 O O   . LEU B 286 ? 0.51440 0.45220 0.54530 -0.00810 0.00930  -0.03910 286 LEU B O   
4523 C CB  . LEU B 286 ? 0.53410 0.48930 0.54140 -0.00450 0.01500  -0.05000 286 LEU B CB  
4524 C CG  . LEU B 286 ? 0.59490 0.56080 0.59040 -0.00430 0.01650  -0.05440 286 LEU B CG  
4525 C CD1 . LEU B 286 ? 0.59170 0.56300 0.57690 -0.00200 0.01830  -0.04870 286 LEU B CD1 
4526 C CD2 . LEU B 286 ? 0.59140 0.56180 0.59100 -0.00440 0.01860  -0.06630 286 LEU B CD2 
4527 N N   . LEU B 287 ? 0.53660 0.47380 0.57830 -0.00480 0.01360  -0.05050 287 LEU B N   
4528 C CA  . LEU B 287 ? 0.48210 0.41200 0.53510 -0.00420 0.01200  -0.04270 287 LEU B CA  
4529 C C   . LEU B 287 ? 0.54480 0.47630 0.58840 -0.00270 0.01140  -0.03420 287 LEU B C   
4530 O O   . LEU B 287 ? 0.53220 0.46740 0.57040 -0.00050 0.01380  -0.03610 287 LEU B O   
4531 C CB  . LEU B 287 ? 0.53050 0.45630 0.60010 -0.00250 0.01400  -0.04870 287 LEU B CB  
4532 C CG  . LEU B 287 ? 0.52590 0.44910 0.60820 -0.00410 0.01450  -0.05850 287 LEU B CG  
4533 C CD1 . LEU B 287 ? 0.55170 0.47200 0.65050 -0.00190 0.01760  -0.06790 287 LEU B CD1 
4534 C CD2 . LEU B 287 ? 0.57570 0.49310 0.66700 -0.00720 0.01090  -0.05170 287 LEU B CD2 
4535 N N   . GLU B 288 ? 0.53010 0.45930 0.57260 -0.00380 0.00840  -0.02500 288 GLU B N   
4536 C CA  . GLU B 288 ? 0.50650 0.43790 0.53940 -0.00280 0.00740  -0.01810 288 GLU B CA  
4537 C C   . GLU B 288 ? 0.51400 0.44260 0.55600 -0.00120 0.00640  -0.01340 288 GLU B C   
4538 O O   . GLU B 288 ? 0.44090 0.36550 0.49490 -0.00170 0.00440  -0.00940 288 GLU B O   
4539 C CB  . GLU B 288 ? 0.53010 0.46250 0.55600 -0.00490 0.00470  -0.01160 288 GLU B CB  
4540 C CG  . GLU B 288 ? 0.50470 0.43880 0.52300 -0.00430 0.00310  -0.00510 288 GLU B CG  
4541 C CD  . GLU B 288 ? 0.64860 0.58670 0.65540 -0.00300 0.00500  -0.00770 288 GLU B CD  
4542 O OE1 . GLU B 288 ? 0.72480 0.66590 0.72390 -0.00350 0.00610  -0.01040 288 GLU B OE1 
4543 O OE2 . GLU B 288 ? 0.59020 0.52840 0.59710 -0.00140 0.00520  -0.00650 288 GLU B OE2 
4544 N N   . ASP B 289 ? 0.49620 0.42720 0.53430 0.00070  0.00770  -0.01350 289 ASP B N   
4545 C CA  . ASP B 289 ? 0.48030 0.40940 0.52800 0.00200  0.00630  -0.00880 289 ASP B CA  
4546 C C   . ASP B 289 ? 0.48900 0.42060 0.52910 0.00190  0.00370  -0.00240 289 ASP B C   
4547 O O   . ASP B 289 ? 0.51470 0.44650 0.56120 0.00310  0.00280  0.00050  289 ASP B O   
4548 C CB  . ASP B 289 ? 0.45050 0.38020 0.50600 0.00450  0.01000  -0.01500 289 ASP B CB  
4549 C CG  . ASP B 289 ? 0.49880 0.43350 0.54480 0.00570  0.01260  -0.01670 289 ASP B CG  
4550 O OD1 . ASP B 289 ? 0.53080 0.46810 0.56430 0.00470  0.01220  -0.01530 289 ASP B OD1 
4551 O OD2 . ASP B 289 ? 0.48740 0.42400 0.53980 0.00780  0.01560  -0.01980 289 ASP B OD2 
4552 N N   . GLU B 290 ? 0.44620 0.38000 0.47420 0.00050  0.00240  -0.00030 290 GLU B N   
4553 C CA  . GLU B 290 ? 0.48880 0.42500 0.51070 0.00030  0.00010  0.00400  290 GLU B CA  
4554 C C   . GLU B 290 ? 0.53000 0.46730 0.55020 -0.00140 -0.00400 0.01070  290 GLU B C   
4555 O O   . GLU B 290 ? 0.51810 0.45860 0.53020 -0.00210 -0.00580 0.01260  290 GLU B O   
4556 C CB  . GLU B 290 ? 0.49320 0.43200 0.50370 0.00050  0.00210  0.00110  290 GLU B CB  
4557 C CG  . GLU B 290 ? 0.50710 0.44700 0.52030 0.00240  0.00610  -0.00340 290 GLU B CG  
4558 C CD  . GLU B 290 ? 0.58600 0.52850 0.59340 0.00300  0.00720  -0.00310 290 GLU B CD  
4559 O OE1 . GLU B 290 ? 0.54740 0.49030 0.54840 0.00200  0.00520  -0.00090 290 GLU B OE1 
4560 O OE2 . GLU B 290 ? 0.52970 0.47430 0.53980 0.00440  0.01060  -0.00510 290 GLU B OE2 
4561 N N   . PHE B 291 ? 0.46210 0.39770 0.49090 -0.00220 -0.00550 0.01440  291 PHE B N   
4562 C CA  . PHE B 291 ? 0.48900 0.42730 0.51840 -0.00360 -0.00950 0.02250  291 PHE B CA  
4563 C C   . PHE B 291 ? 0.47290 0.41020 0.51670 -0.00270 -0.01170 0.02760  291 PHE B C   
4564 O O   . PHE B 291 ? 0.46960 0.40240 0.52620 -0.00190 -0.01030 0.02640  291 PHE B O   
4565 C CB  . PHE B 291 ? 0.48990 0.42800 0.51900 -0.00550 -0.00960 0.02520  291 PHE B CB  
4566 C CG  . PHE B 291 ? 0.54750 0.48750 0.56370 -0.00650 -0.00780 0.02150  291 PHE B CG  
4567 C CD1 . PHE B 291 ? 0.56220 0.50770 0.56760 -0.00740 -0.00930 0.02450  291 PHE B CD1 
4568 C CD2 . PHE B 291 ? 0.53010 0.46750 0.54600 -0.00640 -0.00470 0.01500  291 PHE B CD2 
4569 C CE1 . PHE B 291 ? 0.57420 0.52180 0.56940 -0.00800 -0.00750 0.02150  291 PHE B CE1 
4570 C CE2 . PHE B 291 ? 0.59540 0.53550 0.60060 -0.00720 -0.00340 0.01260  291 PHE B CE2 
4571 C CZ  . PHE B 291 ? 0.60210 0.54690 0.59760 -0.00790 -0.00470 0.01610  291 PHE B CZ  
4572 N N   . THR B 292 ? 0.51240 0.45430 0.55540 -0.00290 -0.01540 0.03300  292 THR B N   
4573 C CA  . THR B 292 ? 0.48240 0.42470 0.53970 -0.00210 -0.01820 0.03960  292 THR B CA  
4574 C C   . THR B 292 ? 0.53040 0.47410 0.59340 -0.00360 -0.02060 0.04860  292 THR B C   
4575 O O   . THR B 292 ? 0.49310 0.43950 0.54670 -0.00550 -0.02070 0.05050  292 THR B O   
4576 C CB  . THR B 292 ? 0.57410 0.52250 0.62870 -0.00210 -0.02200 0.04280  292 THR B CB  
4577 O OG1 . THR B 292 ? 0.49810 0.45320 0.54080 -0.00410 -0.02490 0.04680  292 THR B OG1 
4578 C CG2 . THR B 292 ? 0.45000 0.39760 0.50030 -0.00090 -0.01980 0.03480  292 THR B CG2 
4579 N N   . PRO B 293 ? 0.54280 0.48550 0.62240 -0.00270 -0.02250 0.05520  293 PRO B N   
4580 C CA  . PRO B 293 ? 0.46930 0.41520 0.55560 -0.00420 -0.02560 0.06670  293 PRO B CA  
4581 C C   . PRO B 293 ? 0.54220 0.49860 0.61400 -0.00610 -0.02940 0.07340  293 PRO B C   
4582 O O   . PRO B 293 ? 0.52730 0.48730 0.59500 -0.00810 -0.02980 0.07920  293 PRO B O   
4583 C CB  . PRO B 293 ? 0.51070 0.45540 0.61730 -0.00230 -0.02770 0.07310  293 PRO B CB  
4584 C CG  . PRO B 293 ? 0.52040 0.45690 0.63450 0.00020  -0.02320 0.06170  293 PRO B CG  
4585 C CD  . PRO B 293 ? 0.50780 0.44590 0.60280 -0.00010 -0.02120 0.05240  293 PRO B CD  
4586 N N   . PHE B 294 ? 0.55450 0.51660 0.61820 -0.00580 -0.03180 0.07180  294 PHE B N   
4587 C CA  . PHE B 294 ? 0.57680 0.54980 0.62570 -0.00760 -0.03520 0.07550  294 PHE B CA  
4588 C C   . PHE B 294 ? 0.54000 0.51340 0.57270 -0.00900 -0.03220 0.06930  294 PHE B C   
4589 O O   . PHE B 294 ? 0.59620 0.57790 0.61980 -0.01070 -0.03370 0.07440  294 PHE B O   
4590 C CB  . PHE B 294 ? 0.58590 0.56390 0.63090 -0.00710 -0.03830 0.07250  294 PHE B CB  
4591 C CG  . PHE B 294 ? 0.63880 0.62850 0.66810 -0.00910 -0.04170 0.07360  294 PHE B CG  
4592 C CD1 . PHE B 294 ? 0.73330 0.72310 0.74770 -0.00980 -0.03950 0.06390  294 PHE B CD1 
4593 C CD2 . PHE B 294 ? 0.70280 0.70430 0.73290 -0.01020 -0.04710 0.08420  294 PHE B CD2 
4594 C CE1 . PHE B 294 ? 0.70950 0.71020 0.71030 -0.01140 -0.04220 0.06330  294 PHE B CE1 
4595 C CE2 . PHE B 294 ? 0.71760 0.73170 0.73200 -0.01210 -0.05020 0.08400  294 PHE B CE2 
4596 C CZ  . PHE B 294 ? 0.69990 0.71320 0.69990 -0.01270 -0.04760 0.07270  294 PHE B CZ  
4597 N N   . ASP B 295 ? 0.50560 0.47140 0.53430 -0.00810 -0.02800 0.05860  295 ASP B N   
4598 C CA  . ASP B 295 ? 0.50950 0.47570 0.52470 -0.00900 -0.02510 0.05310  295 ASP B CA  
4599 C C   . ASP B 295 ? 0.55260 0.51860 0.57010 -0.01040 -0.02390 0.05830  295 ASP B C   
4600 O O   . ASP B 295 ? 0.50390 0.47450 0.51030 -0.01170 -0.02290 0.05800  295 ASP B O   
4601 C CB  . ASP B 295 ? 0.53510 0.49360 0.54820 -0.00770 -0.02090 0.04270  295 ASP B CB  
4602 C CG  . ASP B 295 ? 0.55740 0.51600 0.56870 -0.00650 -0.02150 0.03760  295 ASP B CG  
4603 O OD1 . ASP B 295 ? 0.55950 0.52510 0.56720 -0.00720 -0.02530 0.04050  295 ASP B OD1 
4604 O OD2 . ASP B 295 ? 0.52830 0.48120 0.54220 -0.00510 -0.01830 0.03130  295 ASP B OD2 
4605 N N   . VAL B 296 ? 0.51970 0.47970 0.55250 -0.01010 -0.02330 0.06170  296 VAL B N   
4606 C CA  . VAL B 296 ? 0.53070 0.48990 0.56840 -0.01180 -0.02210 0.06670  296 VAL B CA  
4607 C C   . VAL B 296 ? 0.54330 0.51280 0.57900 -0.01360 -0.02540 0.07900  296 VAL B C   
4608 O O   . VAL B 296 ? 0.59420 0.56880 0.62260 -0.01530 -0.02440 0.08170  296 VAL B O   
4609 C CB  . VAL B 296 ? 0.45280 0.40280 0.50980 -0.01120 -0.02090 0.06670  296 VAL B CB  
4610 C CG1 . VAL B 296 ? 0.48770 0.43750 0.55310 -0.01360 -0.02030 0.07380  296 VAL B CG1 
4611 C CG2 . VAL B 296 ? 0.44060 0.38250 0.49730 -0.00970 -0.01710 0.05360  296 VAL B CG2 
4612 N N   . VAL B 297 ? 0.53110 0.50500 0.57390 -0.01300 -0.02930 0.08710  297 VAL B N   
4613 C CA  . VAL B 297 ? 0.59150 0.57770 0.63190 -0.01470 -0.03280 0.09980  297 VAL B CA  
4614 C C   . VAL B 297 ? 0.65000 0.64690 0.66910 -0.01570 -0.03300 0.09670  297 VAL B C   
4615 O O   . VAL B 297 ? 0.64010 0.64630 0.65300 -0.01760 -0.03300 0.10370  297 VAL B O   
4616 C CB  . VAL B 297 ? 0.62580 0.61600 0.67690 -0.01370 -0.03750 0.10860  297 VAL B CB  
4617 C CG1 . VAL B 297 ? 0.67920 0.68480 0.72410 -0.01540 -0.04130 0.12110  297 VAL B CG1 
4618 C CG2 . VAL B 297 ? 0.63980 0.62050 0.71510 -0.01260 -0.03710 0.11380  297 VAL B CG2 
4619 N N   . ARG B 298 ? 0.58000 0.57600 0.58880 -0.01460 -0.03290 0.08600  298 ARG B N   
4620 C CA  . ARG B 298 ? 0.61920 0.62480 0.60980 -0.01550 -0.03300 0.08150  298 ARG B CA  
4621 C C   . ARG B 298 ? 0.69690 0.70280 0.67970 -0.01640 -0.02880 0.07900  298 ARG B C   
4622 O O   . ARG B 298 ? 0.69520 0.71230 0.66680 -0.01760 -0.02890 0.08140  298 ARG B O   
4623 C CB  . ARG B 298 ? 0.66260 0.66460 0.64690 -0.01410 -0.03290 0.06950  298 ARG B CB  
4624 C CG  . ARG B 298 ? 0.72940 0.73450 0.69820 -0.01440 -0.03020 0.06030  298 ARG B CG  
4625 C CD  . ARG B 298 ? 0.71680 0.71960 0.68020 -0.01340 -0.03040 0.04930  298 ARG B CD  
4626 N NE  . ARG B 298 ? 0.85810 0.85080 0.83200 -0.01190 -0.03020 0.04620  298 ARG B NE  
4627 C CZ  . ARG B 298 ? 0.88070 0.86530 0.85440 -0.01060 -0.02710 0.03730  298 ARG B CZ  
4628 N NH1 . ARG B 298 ? 0.75020 0.73400 0.71520 -0.01050 -0.02390 0.03070  298 ARG B NH1 
4629 N NH2 . ARG B 298 ? 0.69270 0.67090 0.67590 -0.00940 -0.02720 0.03550  298 ARG B NH2 
4630 N N   . GLN B 299 ? 0.58550 0.58020 0.57430 -0.01590 -0.02520 0.07390  299 GLN B N   
4631 C CA  . GLN B 299 ? 0.64310 0.63730 0.62500 -0.01660 -0.02130 0.06980  299 GLN B CA  
4632 C C   . GLN B 299 ? 0.67520 0.67160 0.66480 -0.01850 -0.02050 0.07960  299 GLN B C   
4633 O O   . GLN B 299 ? 0.68560 0.68920 0.66760 -0.01980 -0.01860 0.08140  299 GLN B O   
4634 C CB  . GLN B 299 ? 0.59430 0.57710 0.57790 -0.01510 -0.01820 0.05900  299 GLN B CB  
4635 C CG  . GLN B 299 ? 0.56420 0.54700 0.54210 -0.01570 -0.01470 0.05530  299 GLN B CG  
4636 C CD  . GLN B 299 ? 0.60570 0.58050 0.58240 -0.01430 -0.01190 0.04500  299 GLN B CD  
4637 O OE1 . GLN B 299 ? 0.49620 0.47070 0.47060 -0.01480 -0.00930 0.04260  299 GLN B OE1 
4638 N NE2 . GLN B 299 ? 0.51440 0.48370 0.49240 -0.01250 -0.01230 0.03930  299 GLN B NE2 
4639 N N   . CYS B 300 ? 0.61310 0.60370 0.61910 -0.01870 -0.02180 0.08610  300 CYS B N   
4640 C CA  . CYS B 300 ? 0.68570 0.67740 0.70250 -0.02080 -0.02120 0.09610  300 CYS B CA  
4641 C C   . CYS B 300 ? 0.73210 0.73770 0.74740 -0.02230 -0.02390 0.11040  300 CYS B C   
4642 O O   . CYS B 300 ? 0.85920 0.86890 0.88070 -0.02430 -0.02300 0.11990  300 CYS B O   
4643 C CB  . CYS B 300 ? 0.62220 0.60180 0.65930 -0.02040 -0.02130 0.09650  300 CYS B CB  
4644 S SG  . CYS B 300 ? 0.69280 0.65920 0.73070 -0.01940 -0.01730 0.08030  300 CYS B SG  
4645 N N   . SER B 301 ? 0.80400 0.81760 0.81240 -0.02140 -0.02750 0.11280  301 SER B N   
4646 C CA  . SER B 301 ? 0.95390 0.98430 0.95610 -0.02270 -0.03040 0.12490  301 SER B CA  
4647 C C   . SER B 301 ? 0.96740 1.01010 0.94780 -0.02290 -0.02980 0.11850  301 SER B C   
4648 O O   . SER B 301 ? 0.99790 1.05670 0.97060 -0.02420 -0.03160 0.12740  301 SER B O   
4649 C CB  . SER B 301 ? 0.95260 0.98690 0.96240 -0.02200 -0.03570 0.13310  301 SER B CB  
4650 O OG  . SER B 301 ? 0.99670 1.03190 0.99710 -0.02050 -0.03790 0.12340  301 SER B OG  
4651 N N   . GLY B 302 ? 0.92200 0.95830 0.89290 -0.02150 -0.02750 0.10350  302 GLY B N   
4652 C CA  . GLY B 302 ? 0.95540 1.00170 0.90790 -0.02140 -0.02640 0.09570  302 GLY B CA  
4653 C C   . GLY B 302 ? 1.14900 1.20920 1.09170 -0.02160 -0.03070 0.09690  302 GLY B C   
4654 O O   . GLY B 302 ? 1.09150 1.16790 1.02360 -0.02290 -0.03100 0.10160  302 GLY B O   
4655 N N   . VAL B 303 ? 1.37950 1.43440 1.32550 -0.02050 -0.03410 0.09220  303 VAL B N   
4656 C CA  . VAL B 303 ? 1.43880 1.50630 1.37800 -0.02090 -0.03920 0.09320  303 VAL B CA  
4657 C C   . VAL B 303 ? 1.35530 1.43120 1.27750 -0.02090 -0.03850 0.08060  303 VAL B C   
4658 O O   . VAL B 303 ? 1.19560 1.26270 1.11430 -0.01980 -0.03460 0.06860  303 VAL B O   
4659 C CB  . VAL B 303 ? 1.18650 1.24510 1.13710 -0.01970 -0.04290 0.09210  303 VAL B CB  
4660 C CG1 . VAL B 303 ? 1.15640 1.19940 1.10920 -0.01800 -0.03980 0.07850  303 VAL B CG1 
4661 C CG2 . VAL B 303 ? 1.20520 1.27760 1.14960 -0.02040 -0.04890 0.09260  303 VAL B CG2 
4662 N N1  . THC C 1   ? 1.03810 1.07180 1.20620 -0.07240 0.00990  0.15500  1   THC C N1  
4663 C CN  . THC C 1   ? 1.35090 1.37860 1.54410 -0.07580 0.00830  0.16650  1   THC C CN  
4664 O ON  . THC C 1   ? 1.56540 1.57910 1.77720 -0.07760 0.00530  0.15990  1   THC C ON  
4665 C CM  . THC C 1   ? 1.14430 1.18760 1.34360 -0.07900 0.01190  0.18290  1   THC C CM  
4666 C CA  . THC C 1   ? 0.91740 0.95770 1.06460 -0.06820 0.01100  0.15990  1   THC C CA  
4667 C CB  . THC C 1   ? 0.89880 0.92690 1.03630 -0.06420 0.00800  0.14840  1   THC C CB  
4668 O OG1 . THC C 1   ? 1.03600 1.05050 1.18480 -0.06530 0.00550  0.13460  1   THC C OG1 
4669 C CG2 . THC C 1   ? 0.91470 0.94010 1.05880 -0.06360 0.00610  0.15980  1   THC C CG2 
4670 C C   . THC C 1   ? 0.79680 0.85110 0.92150 -0.06570 0.01470  0.15730  1   THC C C   
4671 O O   . THC C 1   ? 0.76420 0.81980 0.88620 -0.06590 0.01570  0.14790  1   THC C O   
4672 N N   A SER C 2   ? 0.76230 0.82770 0.87130 -0.06330 0.01650  0.16540  2   SER C N   
4673 N N   B SER C 2   ? 0.76240 0.82770 0.87140 -0.06320 0.01650  0.16520  2   SER C N   
4674 C CA  A SER C 2   ? 0.72380 0.80310 0.81190 -0.06060 0.02040  0.16250  2   SER C CA  
4675 C CA  B SER C 2   ? 0.72630 0.80550 0.81460 -0.06060 0.02040  0.16250  2   SER C CA  
4676 C C   A SER C 2   ? 0.67970 0.75630 0.74550 -0.05550 0.01940  0.15190  2   SER C C   
4677 C C   B SER C 2   ? 0.67980 0.75690 0.74550 -0.05550 0.01950  0.15240  2   SER C C   
4678 O O   A SER C 2   ? 0.68360 0.75120 0.74880 -0.05410 0.01610  0.15080  2   SER C O   
4679 O O   B SER C 2   ? 0.68160 0.75000 0.74650 -0.05410 0.01620  0.15160  2   SER C O   
4680 C CB  A SER C 2   ? 0.69190 0.79000 0.77830 -0.06200 0.02420  0.17940  2   SER C CB  
4681 C CB  B SER C 2   ? 0.69400 0.79180 0.78230 -0.06240 0.02430  0.17980  2   SER C CB  
4682 O OG  A SER C 2   ? 0.67520 0.77730 0.75130 -0.06000 0.02300  0.18610  2   SER C OG  
4683 O OG  B SER C 2   ? 0.66870 0.76690 0.78170 -0.06760 0.02450  0.19160  2   SER C OG  
4684 N N   . ALA C 3   ? 0.65470 0.73990 0.70360 -0.05270 0.02260  0.14460  3   ALA C N   
4685 C CA  . ALA C 3   ? 0.64560 0.73120 0.67370 -0.04800 0.02240  0.13570  3   ALA C CA  
4686 C C   . ALA C 3   ? 0.65780 0.75280 0.67790 -0.04750 0.02220  0.14630  3   ALA C C   
4687 O O   . ALA C 3   ? 0.63730 0.74420 0.66350 -0.05010 0.02390  0.16120  3   ALA C O   
4688 C CB  . ALA C 3   ? 0.62230 0.71680 0.63720 -0.04540 0.02640  0.12730  3   ALA C CB  
4689 N N   . VAL C 4   ? 0.55880 0.64940 0.56580 -0.04420 0.02000  0.13900  4   VAL C N   
4690 C CA  . VAL C 4   ? 0.58530 0.68380 0.58400 -0.04340 0.01850  0.14690  4   VAL C CA  
4691 C C   . VAL C 4   ? 0.59810 0.70450 0.57490 -0.03960 0.02030  0.13660  4   VAL C C   
4692 O O   . VAL C 4   ? 0.57850 0.67400 0.54860 -0.03680 0.01850  0.12350  4   VAL C O   
4693 C CB  . VAL C 4   ? 0.62340 0.70760 0.63000 -0.04320 0.01330  0.14740  4   VAL C CB  
4694 C CG1 . VAL C 4   ? 0.58480 0.67810 0.58080 -0.04190 0.01120  0.15400  4   VAL C CG1 
4695 C CG2 . VAL C 4   ? 0.67860 0.75510 0.70930 -0.04700 0.01180  0.15730  4   VAL C CG2 
4696 N N   . LEU C 5   ? 0.55420 0.67960 0.52030 -0.03950 0.02360  0.14270  5   LEU C N   
4697 C CA  . LEU C 5   ? 0.54150 0.67520 0.48760 -0.03610 0.02500  0.13240  5   LEU C CA  
4698 C C   . LEU C 5   ? 0.56150 0.69320 0.50090 -0.03510 0.02030  0.13280  5   LEU C C   
4699 O O   . LEU C 5   ? 0.56870 0.70920 0.51020 -0.03700 0.01850  0.14630  5   LEU C O   
4700 C CB  . LEU C 5   ? 0.58220 0.73860 0.51880 -0.03630 0.03030  0.13790  5   LEU C CB  
4701 C CG  . LEU C 5   ? 0.58370 0.74320 0.52550 -0.03650 0.03550  0.13510  5   LEU C CG  
4702 C CD1 . LEU C 5   ? 0.60310 0.78650 0.53930 -0.03770 0.04070  0.14510  5   LEU C CD1 
4703 C CD2 . LEU C 5   ? 0.57200 0.72550 0.50530 -0.03270 0.03710  0.11750  5   LEU C CD2 
4704 N N   . GLN C 6   ? 0.54280 0.66290 0.47600 -0.03220 0.01810  0.11900  6   GLN C N   
4705 C CA  . GLN C 6   ? 0.52930 0.64470 0.46060 -0.03170 0.01290  0.11990  6   GLN C CA  
4706 C C   . GLN C 6   ? 0.57560 0.70660 0.48980 -0.03040 0.01240  0.11830  6   GLN C C   
4707 O O   . GLN C 6   ? 0.54710 0.67320 0.45440 -0.02860 0.00910  0.11000  6   GLN C O   
4708 C CB  . GLN C 6   ? 0.50200 0.59760 0.43710 -0.02980 0.01040  0.10770  6   GLN C CB  
4709 C CG  . GLN C 6   ? 0.52570 0.60740 0.47920 -0.03180 0.00920  0.11230  6   GLN C CG  
4710 C CD  . GLN C 6   ? 0.55750 0.62090 0.51460 -0.02990 0.00670  0.10070  6   GLN C CD  
4711 O OE1 . GLN C 6   ? 0.50480 0.56400 0.45470 -0.02760 0.00830  0.08850  6   GLN C OE1 
4712 N NE2 . GLN C 6   ? 0.56390 0.61690 0.53310 -0.03090 0.00330  0.10500  6   GLN C NE2 
4713 N N   . SER C 7   ? 0.56450 0.71550 0.47180 -0.03160 0.01550  0.12670  7   SER C N   
4714 C CA  . SER C 7   ? 0.58550 0.75390 0.47850 -0.03140 0.01380  0.12910  7   SER C CA  
4715 C C   . SER C 7   ? 0.61440 0.78170 0.51500 -0.03310 0.00800  0.14270  7   SER C C   
4716 O O   . SER C 7   ? 0.61600 0.77100 0.53380 -0.03470 0.00620  0.15170  7   SER C O   
4717 C CB  . SER C 7   ? 0.57980 0.77230 0.46360 -0.03230 0.01890  0.13590  7   SER C CB  
4718 O OG  . SER C 7   ? 0.63430 0.82990 0.53170 -0.03530 0.02070  0.15240  7   SER C OG  
4719 N N   . GLY C 8   ? 0.63490 0.81550 0.52320 -0.03270 0.00490  0.14370  8   GLY C N   
4720 C CA  . GLY C 8   ? 0.67600 0.85840 0.57050 -0.03410 -0.00090 0.15670  8   GLY C CA  
4721 C C   . GLY C 8   ? 0.76440 0.97300 0.65140 -0.03600 -0.00070 0.17230  8   GLY C C   
4722 O O   . GLY C 8   ? 0.76530 0.99070 0.64120 -0.03620 0.00430  0.17170  8   GLY C O   
4723 N N   . PHE C 9   ? 0.81850 1.03120 0.71220 -0.03730 -0.00600 0.18710  9   PHE C N   
4724 C CA  A PHE C 9   ? 0.86790 1.10640 0.75580 -0.03920 -0.00690 0.20490  9   PHE C CA  
4725 C CA  B PHE C 9   ? 0.86800 1.10710 0.75500 -0.03910 -0.00660 0.20400  9   PHE C CA  
4726 C C   . PHE C 9   ? 0.89520 1.14590 0.76910 -0.03840 -0.01260 0.20150  9   PHE C C   
4727 O O   . PHE C 9   ? 0.90730 1.14310 0.78460 -0.03700 -0.01730 0.19280  9   PHE C O   
4728 C CB  A PHE C 9   ? 0.88010 1.11610 0.78980 -0.04160 -0.00860 0.22780  9   PHE C CB  
4729 C CB  B PHE C 9   ? 0.88000 1.11840 0.78790 -0.04170 -0.00750 0.22730  9   PHE C CB  
4730 C CG  A PHE C 9   ? 0.90250 1.16430 0.80850 -0.04340 -0.01130 0.24840  9   PHE C CG  
4731 C CG  B PHE C 9   ? 0.89260 1.12640 0.81180 -0.04330 -0.00140 0.23180  9   PHE C CG  
4732 C CD1 A PHE C 9   ? 0.88540 1.16960 0.78670 -0.04540 -0.00660 0.26170  9   PHE C CD1 
4733 C CD1 B PHE C 9   ? 0.87960 1.11990 0.78630 -0.04260 0.00490  0.22030  9   PHE C CD1 
4734 C CD2 A PHE C 9   ? 0.91850 1.18310 0.82660 -0.04310 -0.01860 0.25560  9   PHE C CD2 
4735 C CD2 B PHE C 9   ? 0.91390 1.13660 0.85770 -0.04540 -0.00190 0.24670  9   PHE C CD2 
4736 C CE1 A PHE C 9   ? 0.85680 1.16640 0.75440 -0.04710 -0.00920 0.28200  9   PHE C CE1 
4737 C CE1 B PHE C 9   ? 0.91870 1.15550 0.83660 -0.04410 0.01030  0.22430  9   PHE C CE1 
4738 C CE2 A PHE C 9   ? 0.91990 1.20940 0.82480 -0.04470 -0.02150 0.27570  9   PHE C CE2 
4739 C CE2 B PHE C 9   ? 0.93240 1.15090 0.88750 -0.04720 0.00330  0.25010  9   PHE C CE2 
4740 C CZ  A PHE C 9   ? 0.91140 1.22370 0.81070 -0.04670 -0.01680 0.28910  9   PHE C CZ  
4741 C CZ  B PHE C 9   ? 0.96690 1.19300 0.90880 -0.04660 0.00930  0.23920  9   PHE C CZ  
4742 N N   . ARG C 10  ? 0.91110 1.19010 0.76910 -0.03940 -0.01220 0.20810  10  ARG C N   
4743 C CA  . ARG C 10  ? 0.98070 1.27420 0.82370 -0.03890 -0.01790 0.20370  10  ARG C CA  
4744 C C   . ARG C 10  ? 1.00390 1.32810 0.83960 -0.04100 -0.01930 0.22380  10  ARG C C   
4745 O O   . ARG C 10  ? 0.95930 1.30310 0.78480 -0.04190 -0.01380 0.22760  10  ARG C O   
4746 C CB  . ARG C 10  ? 0.98250 1.27950 0.80610 -0.03700 -0.01550 0.17920  10  ARG C CB  
4747 C CG  . ARG C 10  ? 1.06750 1.37600 0.87770 -0.03670 -0.02190 0.17150  10  ARG C CG  
4748 C CD  . ARG C 10  ? 1.04790 1.36000 0.84130 -0.03500 -0.01900 0.14720  10  ARG C CD  
4749 N NE  . ARG C 10  ? 1.16200 1.49780 0.93780 -0.03570 -0.02360 0.14270  10  ARG C NE  
4750 C CZ  . ARG C 10  ? 1.23600 1.57840 0.99680 -0.03460 -0.02270 0.12110  10  ARG C CZ  
4751 N NH1 . ARG C 10  ? 1.29020 1.61670 1.05190 -0.03250 -0.01720 0.10270  10  ARG C NH1 
4752 N NH2 . ARG C 10  ? 1.31240 1.67850 1.05790 -0.03570 -0.02750 0.11800  10  ARG C NH2 
4753 N N   . LYS C 11  ? 1.07460 1.40330 0.91660 -0.04180 -0.02670 0.23730  11  LYS C N   
4754 C CA  . LYS C 11  ? 1.07080 1.43060 0.90470 -0.04360 -0.03020 0.25630  11  LYS C CA  
4755 C C   . LYS C 11  ? 1.06270 1.44070 0.89830 -0.04570 -0.02460 0.27560  11  LYS C C   
4756 O O   . LYS C 11  ? 1.06500 1.47150 0.88110 -0.04650 -0.02180 0.27670  11  LYS C O   
4757 C CB  . LYS C 11  ? 1.09830 1.48040 0.90570 -0.04320 -0.03250 0.24150  11  LYS C CB  
4758 C CG  . LYS C 11  ? 1.18000 1.54590 0.98510 -0.04150 -0.03800 0.22140  11  LYS C CG  
4759 C CD  . LYS C 11  ? 1.29560 1.65240 1.11720 -0.04160 -0.04640 0.23400  11  LYS C CD  
4760 C CE  . LYS C 11  ? 1.34320 1.72950 1.16130 -0.04350 -0.05210 0.25700  11  LYS C CE  
4761 N NZ  . LYS C 11  ? 1.21780 1.63420 1.01070 -0.04430 -0.05590 0.24930  11  LYS C NZ  
4762 N N1  . THC D 1   ? 0.77100 0.86630 0.82280 0.01750  0.08590  0.09020  1   THC D N1  
4763 C CN  . THC D 1   ? 0.80450 0.91040 0.86570 0.01780  0.09190  0.09630  1   THC D CN  
4764 O ON  . THC D 1   ? 0.76140 0.86600 0.83870 0.01650  0.09280  0.10770  1   THC D ON  
4765 C CM  . THC D 1   ? 0.81710 0.93670 0.86950 0.01960  0.09750  0.08840  1   THC D CM  
4766 C CA  . THC D 1   ? 0.69190 0.77420 0.75240 0.01610  0.08090  0.09640  1   THC D CA  
4767 C CB  . THC D 1   ? 0.70170 0.77780 0.74890 0.01630  0.07570  0.09080  1   THC D CB  
4768 O OG1 . THC D 1   ? 0.77790 0.86440 0.80800 0.01770  0.07740  0.08250  1   THC D OG1 
4769 C CG2 . THC D 1   ? 0.70460 0.78480 0.75430 0.01650  0.07530  0.10350  1   THC D CG2 
4770 C C   . THC D 1   ? 0.62070 0.68610 0.69690 0.01430  0.07710  0.09260  1   THC D C   
4771 O O   . THC D 1   ? 0.61820 0.67940 0.69570 0.01430  0.07670  0.08380  1   THC D O   
4772 N N   . SER D 2   ? 0.63930 0.69550 0.72780 0.01280  0.07400  0.09930  2   SER D N   
4773 C CA  A SER D 2   ? 0.63290 0.67490 0.73680 0.01080  0.07010  0.09640  2   SER D CA  
4774 C CA  B SER D 2   ? 0.60720 0.64920 0.71050 0.01080  0.07010  0.09590  2   SER D CA  
4775 C C   . SER D 2   ? 0.59960 0.62620 0.69710 0.01020  0.06310  0.08540  2   SER D C   
4776 O O   . SER D 2   ? 0.56220 0.58690 0.64910 0.01090  0.06090  0.08400  2   SER D O   
4777 C CB  A SER D 2   ? 0.57980 0.62050 0.70240 0.00930  0.07080  0.10890  2   SER D CB  
4778 C CB  B SER D 2   ? 0.58310 0.62360 0.70630 0.00920  0.07090  0.10780  2   SER D CB  
4779 O OG  A SER D 2   ? 0.56530 0.62140 0.69490 0.00970  0.07770  0.12050  2   SER D OG  
4780 O OG  B SER D 2   ? 0.56370 0.60430 0.68540 0.00980  0.07010  0.11480  2   SER D OG  
4781 N N   . ALA D 3   ? 0.55370 0.57040 0.65830 0.00870  0.05950  0.07810  3   ALA D N   
4782 C CA  . ALA D 3   ? 0.53720 0.53980 0.64050 0.00750  0.05270  0.07030  3   ALA D CA  
4783 C C   . ALA D 3   ? 0.52500 0.52180 0.63710 0.00660  0.05090  0.07590  3   ALA D C   
4784 O O   . ALA D 3   ? 0.49060 0.49150 0.61630 0.00620  0.05390  0.08610  3   ALA D O   
4785 C CB  . ALA D 3   ? 0.51100 0.50680 0.62360 0.00580  0.04940  0.06410  3   ALA D CB  
4786 N N   . VAL D 4   ? 0.48680 0.47440 0.59220 0.00650  0.04610  0.06930  4   VAL D N   
4787 C CA  . VAL D 4   ? 0.48260 0.46280 0.59720 0.00580  0.04380  0.07160  4   VAL D CA  
4788 C C   . VAL D 4   ? 0.49570 0.46420 0.61570 0.00370  0.03800  0.06190  4   VAL D C   
4789 O O   . VAL D 4   ? 0.51340 0.47790 0.62090 0.00380  0.03450  0.05280  4   VAL D O   
4790 C CB  . VAL D 4   ? 0.52990 0.51100 0.63180 0.00770  0.04340  0.07200  4   VAL D CB  
4791 C CG1 . VAL D 4   ? 0.49570 0.46780 0.60810 0.00730  0.04080  0.07270  4   VAL D CG1 
4792 C CG2 . VAL D 4   ? 0.51610 0.51130 0.61210 0.00950  0.04880  0.08190  4   VAL D CG2 
4793 N N   . LEU D 5   ? 0.43750 0.40130 0.57650 0.00160  0.03690  0.06380  5   LEU D N   
4794 C CA  . LEU D 5   ? 0.44740 0.40140 0.59180 -0.00050 0.03110  0.05400  5   LEU D CA  
4795 C C   . LEU D 5   ? 0.48620 0.43380 0.62700 0.00020  0.02890  0.05030  5   LEU D C   
4796 O O   . LEU D 5   ? 0.49420 0.44130 0.64470 0.00100  0.03120  0.05720  5   LEU D O   
4797 C CB  . LEU D 5   ? 0.47330 0.42460 0.64030 -0.00320 0.03040  0.05610  5   LEU D CB  
4798 C CG  . LEU D 5   ? 0.52150 0.47800 0.69350 -0.00450 0.03110  0.05710  5   LEU D CG  
4799 C CD1 . LEU D 5   ? 0.53140 0.48590 0.72800 -0.00730 0.03090  0.06090  5   LEU D CD1 
4800 C CD2 . LEU D 5   ? 0.50300 0.45720 0.66480 -0.00510 0.02620  0.04670  5   LEU D CD2 
4801 N N   . GLN D 6   ? 0.44520 0.38890 0.57220 0.00030  0.02500  0.04050  6   GLN D N   
4802 C CA  . GLN D 6   ? 0.45930 0.39880 0.58030 0.00160  0.02380  0.03720  6   GLN D CA  
4803 C C   . GLN D 6   ? 0.49930 0.43050 0.63160 -0.00010 0.02000  0.02940  6   GLN D C   
4804 O O   . GLN D 6   ? 0.48020 0.40780 0.60410 0.00030  0.01730  0.02130  6   GLN D O   
4805 C CB  . GLN D 6   ? 0.44190 0.38330 0.54170 0.00280  0.02250  0.03200  6   GLN D CB  
4806 C CG  . GLN D 6   ? 0.47350 0.42310 0.56360 0.00490  0.02680  0.03940  6   GLN D CG  
4807 C CD  . GLN D 6   ? 0.47990 0.43060 0.55100 0.00600  0.02550  0.03430  6   GLN D CD  
4808 O OE1 . GLN D 6   ? 0.45240 0.40160 0.51690 0.00500  0.02290  0.02800  6   GLN D OE1 
4809 N NE2 . GLN D 6   ? 0.47700 0.43130 0.54080 0.00780  0.02740  0.03780  6   GLN D NE2 
4810 N N   . SER D 7   ? 0.50890 0.43760 0.66140 -0.00200 0.02010  0.03160  7   SER D N   
4811 C CA  . SER D 7   ? 0.49900 0.42020 0.66630 -0.00310 0.01790  0.02600  7   SER D CA  
4812 C C   . SER D 7   ? 0.54310 0.46290 0.71400 -0.00040 0.02110  0.03180  7   SER D C   
4813 O O   . SER D 7   ? 0.53980 0.46550 0.70400 0.00190  0.02480  0.04180  7   SER D O   
4814 C CB  . SER D 7   ? 0.52480 0.44400 0.71540 -0.00590 0.01760  0.02810  7   SER D CB  
4815 O OG  . SER D 7   ? 0.52920 0.45340 0.72840 -0.00510 0.02260  0.04200  7   SER D OG  
4816 N N   . GLY D 8   ? 0.58020 0.49290 0.76300 -0.00060 0.01960  0.02550  8   GLY D N   
4817 C CA  . GLY D 8   ? 0.65550 0.56630 0.84560 0.00210  0.02230  0.03100  8   GLY D CA  
4818 C C   . GLY D 8   ? 0.71980 0.62460 0.93880 0.00120  0.02330  0.03410  8   GLY D C   
4819 O O   . GLY D 8   ? 0.66590 0.56750 0.89940 -0.00190 0.02140  0.03050  8   GLY D O   
4820 N N   A PHE D 9   ? 0.79090 0.69420 1.01930 0.00390  0.02610  0.04100  9   PHE D N   
4821 N N   B PHE D 9   ? 0.79050 0.69370 1.01870 0.00390  0.02600  0.04080  9   PHE D N   
4822 C CA  A PHE D 9   ? 0.81740 0.71480 1.07540 0.00380  0.02770  0.04620  9   PHE D CA  
4823 C CA  B PHE D 9   ? 0.81750 0.71470 1.07540 0.00370  0.02750  0.04560  9   PHE D CA  
4824 C C   A PHE D 9   ? 0.83880 0.72730 1.10550 0.00450  0.02570  0.03290  9   PHE D C   
4825 C C   B PHE D 9   ? 0.83900 0.72750 1.10560 0.00450  0.02560  0.03260  9   PHE D C   
4826 O O   A PHE D 9   ? 0.86590 0.75520 1.11530 0.00660  0.02490  0.02570  9   PHE D O   
4827 O O   B PHE D 9   ? 0.86580 0.75510 1.11520 0.00660  0.02480  0.02530  9   PHE D O   
4828 C CB  A PHE D 9   ? 0.83160 0.73470 1.09590 0.00680  0.03230  0.06470  9   PHE D CB  
4829 C CB  B PHE D 9   ? 0.83180 0.73450 1.09710 0.00640  0.03210  0.06430  9   PHE D CB  
4830 C CG  A PHE D 9   ? 0.85890 0.75840 1.15560 0.00610  0.03460  0.07550  9   PHE D CG  
4831 C CG  B PHE D 9   ? 0.83700 0.74720 1.10680 0.00500  0.03480  0.07800  9   PHE D CG  
4832 C CD1 A PHE D 9   ? 0.85570 0.75850 1.16360 0.00340  0.03600  0.08410  9   PHE D CD1 
4833 C CD1 B PHE D 9   ? 0.83250 0.75270 1.07930 0.00530  0.03590  0.08200  9   PHE D CD1 
4834 C CD2 A PHE D 9   ? 0.86760 0.76080 1.18480 0.00830  0.03570  0.07810  9   PHE D CD2 
4835 C CD2 B PHE D 9   ? 0.85150 0.75880 1.14990 0.00330  0.03640  0.08640  9   PHE D CD2 
4836 C CE1 A PHE D 9   ? 0.83870 0.73840 1.17770 0.00260  0.03830  0.09530  9   PHE D CE1 
4837 C CE1 B PHE D 9   ? 0.84500 0.77330 1.09610 0.00420  0.03890  0.09380  9   PHE D CE1 
4838 C CE2 A PHE D 9   ? 0.84780 0.73730 1.19690 0.00770  0.03790  0.08900  9   PHE D CE2 
4839 C CE2 B PHE D 9   ? 0.86510 0.78040 1.16790 0.00190  0.03940  0.09940  9   PHE D CE2 
4840 C CZ  A PHE D 9   ? 0.81420 0.70710 1.17400 0.00470  0.03920  0.09790  9   PHE D CZ  
4841 C CZ  B PHE D 9   ? 0.87870 0.80500 1.15720 0.00250  0.04080  0.10290  9   PHE D CZ  
4842 N N   . ARG D 10  ? 0.86650 0.74690 1.16050 0.00270  0.02500  0.02900  10  ARG D N   
4843 C CA  . ARG D 10  ? 0.95690 0.82880 1.26350 0.00360  0.02380  0.01580  10  ARG D CA  
4844 C C   . ARG D 10  ? 1.00050 0.86670 1.33810 0.00550  0.02710  0.02570  10  ARG D C   
4845 O O   . ARG D 10  ? 1.04380 0.91170 1.39720 0.00490  0.02950  0.04140  10  ARG D O   
4846 C CB  . ARG D 10  ? 0.91220 0.77900 1.22480 -0.00040 0.01930  -0.00210 10  ARG D CB  
4847 C CG  . ARG D 10  ? 0.90110 0.76820 1.19430 0.00010  0.01640  -0.02000 10  ARG D CG  
4848 C CD  . ARG D 10  ? 0.88720 0.75020 1.18940 -0.00370 0.01190  -0.03830 10  ARG D CD  
4849 N NE  . ARG D 10  ? 0.92510 0.78920 1.21190 -0.00270 0.00990  -0.05480 10  ARG D NE  
4850 C CZ  . ARG D 10  ? 1.03510 0.89540 1.33230 -0.00450 0.00730  -0.07280 10  ARG D CZ  
4851 N NH1 . ARG D 10  ? 1.01790 0.87270 1.34050 -0.00790 0.00530  -0.07800 10  ARG D NH1 
4852 N NH2 . ARG D 10  ? 1.01110 0.87400 1.29380 -0.00270 0.00680  -0.08600 10  ARG D NH2 
4853 O O   . HOH E .   ? 0.92320 1.53390 0.58600 -0.02430 0.08530  0.09210  401 HOH A O   
4854 O O   . HOH E .   ? 0.56820 0.56180 0.53380 -0.01440 0.00290  -0.00790 402 HOH A O   
4855 O O   . HOH E .   ? 0.59410 0.54110 0.58390 0.00290  0.00890  -0.00180 403 HOH A O   
4856 O O   . HOH E .   ? 0.83610 1.14030 0.70950 -0.04440 0.01650  0.23310  404 HOH A O   
4857 O O   . HOH E .   ? 0.61290 0.67840 0.60730 -0.03700 0.00130  0.13900  405 HOH A O   
4858 O O   . HOH E .   ? 0.58050 0.69890 0.64090 0.04400  0.00600  0.12710  406 HOH A O   
4859 O O   . HOH E .   ? 0.56070 0.63030 0.43760 -0.00810 0.00700  -0.00940 407 HOH A O   
4860 O O   . HOH E .   ? 0.60630 0.58020 0.55500 -0.00370 0.00830  0.00290  408 HOH A O   
4861 O O   . HOH E .   ? 0.51450 0.54750 0.47240 -0.01940 -0.00450 -0.03800 409 HOH A O   
4862 O O   . HOH E .   ? 0.64150 0.81720 0.52530 0.01890  0.07790  -0.06820 410 HOH A O   
4863 O O   . HOH E .   ? 0.61170 0.91800 0.51460 -0.00670 -0.04720 0.04690  411 HOH A O   
4864 O O   . HOH E .   ? 0.61580 0.58790 0.57210 -0.00240 0.01020  -0.01150 412 HOH A O   
4865 O O   . HOH E .   ? 0.81180 1.12600 0.56540 -0.02750 -0.00190 0.06180  413 HOH A O   
4866 O O   . HOH E .   ? 0.62570 0.84710 0.57650 -0.03170 0.07050  0.12130  414 HOH A O   
4867 O O   . HOH E .   ? 0.58890 0.65420 0.58510 -0.00950 0.01480  0.02220  415 HOH A O   
4868 O O   . HOH E .   ? 0.55670 0.56900 0.60850 0.03790  0.02460  0.05670  416 HOH A O   
4869 O O   . HOH E .   ? 0.63720 0.83930 0.63560 0.00340  -0.03110 0.06080  417 HOH A O   
4870 O O   . HOH E .   ? 0.43870 0.43900 0.38830 0.00330  0.01050  0.00560  418 HOH A O   
4871 O O   . HOH E .   ? 0.59080 0.78090 0.48240 0.00930  0.00500  0.04960  419 HOH A O   
4872 O O   . HOH E .   ? 0.55460 0.57830 0.49210 -0.01830 -0.00990 0.05880  420 HOH A O   
4873 O O   . HOH E .   ? 0.79230 0.81600 0.75270 -0.00750 0.01900  -0.08800 421 HOH A O   
4874 O O   . HOH E .   ? 0.47390 0.49240 0.44900 0.01350  0.01650  0.01690  422 HOH A O   
4875 O O   . HOH E .   ? 0.64410 0.61030 0.61750 0.01340  0.01820  -0.01110 423 HOH A O   
4876 O O   . HOH E .   ? 0.62040 0.90340 0.56070 0.01580  -0.03200 0.11610  424 HOH A O   
4877 O O   . HOH E .   ? 0.68280 0.77060 0.68670 -0.01930 -0.00600 0.01250  425 HOH A O   
4878 O O   . HOH E .   ? 0.81990 0.86690 0.77660 -0.01390 0.01420  -0.11340 426 HOH A O   
4879 O O   . HOH E .   ? 0.67960 0.76710 0.75110 -0.05410 0.02520  0.09510  427 HOH A O   
4880 O O   . HOH E .   ? 0.55400 0.50430 0.56770 0.01110  0.01960  0.01680  428 HOH A O   
4881 O O   . HOH E .   ? 0.61100 0.79990 0.59550 -0.04360 -0.05010 -0.04150 429 HOH A O   
4882 O O   . HOH E .   ? 0.52060 0.58350 0.53380 -0.03050 0.01880  0.04300  430 HOH A O   
4883 O O   . HOH E .   ? 0.56450 0.58190 0.53340 -0.02060 -0.00360 -0.02760 431 HOH A O   
4884 O O   . HOH E .   ? 0.57020 0.85350 0.59260 0.01180  -0.04890 0.10460  432 HOH A O   
4885 O O   . HOH E .   ? 0.52520 0.73650 0.46490 0.02480  0.00630  0.13220  433 HOH A O   
4886 O O   . HOH E .   ? 0.75680 0.84250 0.69860 -0.02120 0.00590  -0.13290 434 HOH A O   
4887 O O   . HOH E .   ? 0.62020 0.64060 0.70690 0.03920  0.02860  0.11250  435 HOH A O   
4888 O O   . HOH E .   ? 0.64370 0.81080 0.49950 -0.02570 -0.00660 0.09170  436 HOH A O   
4889 O O   . HOH E .   ? 0.48710 0.55140 0.44190 -0.01550 0.02990  0.03900  437 HOH A O   
4890 O O   . HOH E .   ? 0.66270 0.73420 0.55590 -0.00260 0.00110  -0.12590 438 HOH A O   
4891 O O   . HOH E .   ? 0.51900 0.51170 0.47350 -0.01100 0.00960  0.01300  439 HOH A O   
4892 O O   . HOH E .   ? 0.57630 0.60840 0.56340 -0.02850 -0.00850 -0.02280 440 HOH A O   
4893 O O   . HOH E .   ? 0.53360 0.50560 0.48830 0.00640  0.01360  -0.00080 441 HOH A O   
4894 O O   . HOH E .   ? 0.54190 0.61960 0.64040 0.05170  0.01990  0.08720  442 HOH A O   
4895 O O   . HOH E .   ? 0.58800 0.68160 0.54310 0.01930  0.03820  0.07920  443 HOH A O   
4896 O O   . HOH E .   ? 0.60810 0.65450 0.59140 -0.03300 -0.01450 -0.05200 444 HOH A O   
4897 O O   . HOH E .   ? 0.65500 0.79170 0.63670 -0.01450 0.05550  0.05360  445 HOH A O   
4898 O O   . HOH E .   ? 0.65880 0.66790 0.71200 -0.04280 0.00250  0.10510  446 HOH A O   
4899 O O   . HOH E .   ? 0.53090 0.75440 0.51420 -0.01520 -0.04480 0.02870  447 HOH A O   
4900 O O   . HOH E .   ? 0.62290 0.63630 0.57170 0.00650  0.02900  -0.02270 448 HOH A O   
4901 O O   . HOH E .   ? 0.79980 0.76510 0.85780 0.02550  0.02760  0.05030  449 HOH A O   
4902 O O   . HOH E .   ? 0.48840 0.58210 0.48760 0.00260  0.00050  0.03020  450 HOH A O   
4903 O O   . HOH E .   ? 0.51880 0.66520 0.52280 0.03320  0.00260  0.12740  451 HOH A O   
4904 O O   . HOH E .   ? 0.52040 0.49780 0.48080 0.01140  0.01890  -0.01230 452 HOH A O   
4905 O O   . HOH E .   ? 0.53280 0.58970 0.59670 0.04270  0.02110  0.06530  453 HOH A O   
4906 O O   . HOH E .   ? 0.48100 0.64160 0.43020 -0.00790 0.06650  0.04430  454 HOH A O   
4907 O O   . HOH E .   ? 0.43680 0.63430 0.48400 0.03320  -0.01810 0.11980  455 HOH A O   
4908 O O   . HOH E .   ? 0.57010 0.55630 0.55740 -0.02430 0.00280  0.04080  456 HOH A O   
4909 O O   . HOH E .   ? 0.56450 0.54740 0.54360 0.01780  0.02240  -0.00170 457 HOH A O   
4910 O O   . HOH E .   ? 0.56660 0.55960 0.53980 0.01720  0.02490  -0.00650 458 HOH A O   
4911 O O   . HOH E .   ? 0.58410 0.71270 0.68940 0.05420  0.00610  0.13980  459 HOH A O   
4912 O O   . HOH E .   ? 0.55460 0.51430 0.53170 0.01160  0.01600  0.00140  460 HOH A O   
4913 O O   . HOH E .   ? 0.61950 0.94410 0.56630 -0.00560 -0.06080 0.06890  461 HOH A O   
4914 O O   . HOH E .   ? 0.62240 0.68040 0.61800 0.03400  0.05910  -0.04010 462 HOH A O   
4915 O O   . HOH E .   ? 0.48300 0.57040 0.50750 0.02270  0.01190  0.04540  463 HOH A O   
4916 O O   . HOH E .   ? 0.68330 1.03250 0.58340 -0.02200 0.11150  0.11880  464 HOH A O   
4917 O O   . HOH E .   ? 0.89070 1.14980 0.78610 -0.04240 0.02820  0.20240  465 HOH A O   
4918 O O   . HOH E .   ? 0.58860 0.59420 0.57680 -0.02500 -0.00030 -0.00340 466 HOH A O   
4919 O O   . HOH E .   ? 0.56030 0.56920 0.56090 -0.02980 0.00650  0.02740  467 HOH A O   
4920 O O   . HOH E .   ? 0.61380 0.56600 0.57550 -0.00110 0.00280  -0.00010 468 HOH A O   
4921 O O   . HOH E .   ? 0.58380 0.66410 0.51300 0.01710  0.05280  -0.04160 469 HOH A O   
4922 O O   . HOH E .   ? 0.61880 0.62560 0.59610 -0.02120 -0.00100 -0.01160 470 HOH A O   
4923 O O   . HOH E .   ? 0.51100 0.69330 0.51820 0.02750  -0.01460 0.11030  471 HOH A O   
4924 O O   . HOH E .   ? 0.58430 0.54710 0.53270 -0.00240 0.00310  0.00020  472 HOH A O   
4925 O O   . HOH E .   ? 0.57300 0.55800 0.53100 -0.00930 0.00540  -0.00770 473 HOH A O   
4926 O O   . HOH E .   ? 0.46530 0.63090 0.47700 0.01160  -0.01770 0.06420  474 HOH A O   
4927 O O   . HOH E .   ? 0.57080 0.55010 0.52320 0.00230  0.01430  -0.00630 475 HOH A O   
4928 O O   . HOH E .   ? 0.64110 0.87360 0.51390 -0.01010 -0.01990 -0.01110 476 HOH A O   
4929 O O   . HOH E .   ? 0.58280 0.54730 0.58980 0.01230  0.02400  0.02800  477 HOH A O   
4930 O O   . HOH E .   ? 0.55340 0.55930 0.52280 -0.02070 -0.01100 0.07210  478 HOH A O   
4931 O O   . HOH E .   ? 0.59370 0.59470 0.59030 -0.02770 0.00320  0.01340  479 HOH A O   
4932 O O   . HOH E .   ? 0.66510 1.04520 0.47600 0.00730  0.12350  -0.01160 480 HOH A O   
4933 O O   . HOH E .   ? 0.71870 0.69000 0.69800 -0.01830 0.00040  0.02820  481 HOH A O   
4934 O O   . HOH E .   ? 0.50180 0.52400 0.52530 0.03100  0.02060  0.06480  482 HOH A O   
4935 O O   . HOH E .   ? 0.62080 0.65270 0.60770 0.01600  0.02220  0.01540  483 HOH A O   
4936 O O   . HOH E .   ? 0.65180 0.66650 0.63450 0.01370  0.03900  0.03560  484 HOH A O   
4937 O O   . HOH E .   ? 0.74190 0.80280 0.63880 -0.01530 -0.02970 -0.07670 485 HOH A O   
4938 O O   . HOH E .   ? 0.56880 0.68660 0.55950 -0.02300 -0.02130 0.00000  486 HOH A O   
4939 O O   . HOH E .   ? 0.61770 0.92590 0.54490 -0.02940 0.09710  0.13540  487 HOH A O   
4940 O O   . HOH E .   ? 0.42600 0.58580 0.46220 0.02330  -0.01070 0.08020  488 HOH A O   
4941 O O   . HOH E .   ? 0.53060 0.63480 0.56990 0.03900  0.00860  0.11630  489 HOH A O   
4942 O O   . HOH E .   ? 0.62760 0.69750 0.60860 0.01100  0.04170  0.00840  490 HOH A O   
4943 O O   . HOH E .   ? 0.75000 0.90280 0.63110 0.00590  0.04030  -0.05450 491 HOH A O   
4944 O O   . HOH E .   ? 0.65230 0.69050 0.56520 -0.01520 -0.03290 -0.04280 492 HOH A O   
4945 O O   . HOH E .   ? 0.49680 0.68920 0.38300 -0.02090 0.05130  0.07950  493 HOH A O   
4946 O O   . HOH E .   ? 0.51570 0.69550 0.49880 0.02820  -0.00640 0.12190  494 HOH A O   
4947 O O   . HOH E .   ? 0.58680 0.54010 0.55090 0.00050  0.00790  -0.00220 495 HOH A O   
4948 O O   . HOH E .   ? 0.58440 0.59620 0.54170 0.01780  0.03360  -0.03490 496 HOH A O   
4949 O O   . HOH E .   ? 0.63380 0.61070 0.67790 0.01410  0.03390  0.05710  497 HOH A O   
4950 O O   . HOH E .   ? 0.80210 0.95820 0.77050 -0.04410 0.01700  0.18760  498 HOH A O   
4951 O O   . HOH E .   ? 0.49630 0.74930 0.47550 0.01700  -0.03410 0.10890  499 HOH A O   
4952 O O   . HOH E .   ? 0.83720 0.86440 0.89450 0.02760  0.03630  0.11490  500 HOH A O   
4953 O O   . HOH E .   ? 0.66850 0.72540 0.60010 0.00590  0.03590  -0.05120 501 HOH A O   
4954 O O   . HOH E .   ? 0.71420 0.99300 0.61140 0.01000  0.11190  0.00390  502 HOH A O   
4955 O O   . HOH E .   ? 0.57150 0.58790 0.53230 -0.01770 -0.00030 -0.04560 503 HOH A O   
4956 O O   . HOH E .   ? 0.41930 0.48310 0.39320 0.00440  0.00270  0.02350  504 HOH A O   
4957 O O   . HOH E .   ? 0.47750 0.74290 0.45900 0.00930  -0.04260 0.09250  505 HOH A O   
4958 O O   . HOH E .   ? 0.68520 0.74180 0.66220 0.03210  0.05580  -0.17770 506 HOH A O   
4959 O O   . HOH E .   ? 0.50380 0.64500 0.48880 -0.01660 -0.02460 0.01090  507 HOH A O   
4960 O O   . HOH E .   ? 0.79540 1.23420 0.51400 -0.03390 0.02380  0.13100  508 HOH A O   
4961 O O   . HOH E .   ? 0.67050 0.73550 0.63100 -0.02960 -0.01250 -0.07840 509 HOH A O   
4962 O O   . HOH E .   ? 0.76230 0.94960 0.69510 -0.04010 -0.04100 -0.08320 510 HOH A O   
4963 O O   . HOH E .   ? 0.71050 0.81160 0.59490 -0.02130 -0.03090 0.05780  511 HOH A O   
4964 O O   . HOH E .   ? 0.73130 0.90610 0.60570 -0.02990 -0.01310 0.12920  512 HOH A O   
4965 O O   . HOH E .   ? 0.54540 0.50810 0.50590 0.00710  0.01280  -0.00250 513 HOH A O   
4966 O O   . HOH E .   ? 0.62690 0.63020 0.65170 -0.03730 0.00390  0.03340  514 HOH A O   
4967 O O   . HOH E .   ? 0.58540 0.75220 0.54710 -0.01700 0.06440  0.06650  515 HOH A O   
4968 O O   . HOH E .   ? 0.52390 0.68610 0.56750 0.04060  -0.00440 0.13890  516 HOH A O   
4969 O O   . HOH E .   ? 0.70130 0.76080 0.64990 -0.02270 -0.00520 -0.07500 517 HOH A O   
4970 O O   . HOH E .   ? 0.64130 0.69470 0.64000 -0.03380 -0.00840 0.14060  518 HOH A O   
4971 O O   . HOH E .   ? 0.58320 0.60030 0.57640 0.02190  0.02040  0.02220  519 HOH A O   
4972 O O   . HOH E .   ? 0.88450 1.09440 0.81970 0.02760  0.10500  -0.04390 520 HOH A O   
4973 O O   . HOH E .   ? 0.74780 1.23050 0.45400 0.00800  0.12010  -0.08340 521 HOH A O   
4974 O O   . HOH E .   ? 0.63050 0.71280 0.59870 0.03770  0.07180  -0.11290 522 HOH A O   
4975 O O   . HOH E .   ? 0.60930 0.63360 0.66370 -0.04760 0.00920  0.07110  523 HOH A O   
4976 O O   . HOH E .   ? 0.61130 0.86340 0.53480 -0.02880 -0.05180 -0.02420 524 HOH A O   
4977 O O   . HOH E .   ? 0.74770 0.83060 0.64370 -0.02000 -0.04050 0.03800  525 HOH A O   
4978 O O   . HOH E .   ? 0.58510 0.68150 0.57230 -0.00340 0.04300  0.02860  526 HOH A O   
4979 O O   . HOH E .   ? 0.45540 0.42280 0.43740 -0.00850 0.00980  -0.03890 527 HOH A O   
4980 O O   . HOH E .   ? 0.49540 0.49660 0.49650 0.02490  0.02270  0.02050  528 HOH A O   
4981 O O   . HOH E .   ? 0.68120 0.77470 0.69360 -0.03920 -0.02300 -0.02030 529 HOH A O   
4982 O O   . HOH E .   ? 0.65750 0.63600 0.62800 0.00850  0.02380  0.00660  530 HOH A O   
4983 O O   . HOH E .   ? 0.68950 0.66950 0.69970 0.01580  0.02800  0.04420  531 HOH A O   
4984 O O   . HOH E .   ? 0.59910 0.83490 0.62130 -0.00230 -0.04160 0.06220  532 HOH A O   
4985 O O   . HOH E .   ? 0.73520 0.92310 0.68740 0.02460  0.09650  -0.02690 533 HOH A O   
4986 O O   . HOH E .   ? 0.67250 0.99940 0.63990 -0.00830 -0.06590 0.06730  534 HOH A O   
4987 O O   . HOH E .   ? 0.81810 1.33390 0.50150 0.00520  0.11570  -0.08880 535 HOH A O   
4988 O O   . HOH E .   ? 0.56080 0.76280 0.55960 -0.00570 -0.03480 0.04460  536 HOH A O   
4989 O O   . HOH E .   ? 0.66690 0.82270 0.67260 -0.05060 -0.04600 -0.05260 537 HOH A O   
4990 O O   . HOH E .   ? 0.52920 0.62800 0.53730 -0.00230 0.00120  0.02830  538 HOH A O   
4991 O O   . HOH E .   ? 0.70850 0.67310 0.68240 -0.00840 0.00730  -0.02260 539 HOH A O   
4992 O O   . HOH E .   ? 0.62550 0.84780 0.58600 -0.02660 0.07720  0.10460  540 HOH A O   
4993 O O   . HOH E .   ? 0.55740 0.62250 0.57890 0.02600  0.01810  0.03870  541 HOH A O   
4994 O O   . HOH E .   ? 0.63250 0.94440 0.60610 0.00620  -0.05450 0.09950  542 HOH A O   
4995 O O   . HOH E .   ? 0.75860 0.75500 0.74370 0.02270  0.03080  -0.01540 543 HOH A O   
4996 O O   . HOH E .   ? 0.76320 0.79040 0.75510 -0.03220 -0.01080 -0.04080 544 HOH A O   
4997 O O   . HOH E .   ? 0.64220 0.73500 0.59450 0.02560  0.06490  -0.04740 545 HOH A O   
4998 O O   . HOH E .   ? 0.47190 0.56050 0.48330 0.01250  0.00870  0.03630  546 HOH A O   
4999 O O   . HOH E .   ? 0.65500 0.62170 0.63190 -0.01620 0.00180  0.01500  547 HOH A O   
5000 O O   . HOH E .   ? 0.52580 0.73350 0.60150 0.04350  -0.01700 0.14770  548 HOH A O   
5001 O O   . HOH E .   ? 0.59700 0.70000 0.60120 -0.01210 0.03860  0.03940  549 HOH A O   
5002 O O   . HOH E .   ? 0.58550 0.62060 0.56720 0.01270  0.01570  0.02030  550 HOH A O   
5003 O O   . HOH E .   ? 0.57000 0.76270 0.56640 -0.02190 -0.03970 0.01420  551 HOH A O   
5004 O O   . HOH E .   ? 0.60190 0.63970 0.68400 0.04730  0.02540  0.06770  552 HOH A O   
5005 O O   . HOH E .   ? 0.57410 0.74820 0.58410 -0.00560 -0.02600 0.04000  553 HOH A O   
5006 O O   . HOH E .   ? 0.65930 0.75930 0.79960 0.06190  0.01520  0.14050  554 HOH A O   
5007 O O   . HOH E .   ? 0.88350 0.91590 0.83820 -0.01820 0.00050  -0.06440 555 HOH A O   
5008 O O   . HOH E .   ? 0.50940 0.67620 0.50900 -0.01660 -0.02990 0.01990  556 HOH A O   
5009 O O   . HOH E .   ? 0.49690 0.72170 0.50010 0.02460  -0.02590 0.11810  557 HOH A O   
5010 O O   . HOH E .   ? 0.51100 0.73980 0.53960 0.02680  -0.02810 0.12040  558 HOH A O   
5011 O O   . HOH E .   ? 0.61700 0.88180 0.60860 -0.01940 -0.05750 0.03200  559 HOH A O   
5012 O O   . HOH E .   ? 0.54780 0.77060 0.52270 0.02870  -0.01180 0.14180  560 HOH A O   
5013 O O   . HOH E .   ? 0.55120 0.71750 0.57220 0.00570  -0.01830 0.05490  561 HOH A O   
5014 O O   . HOH E .   ? 0.65510 0.78020 0.66210 -0.02750 -0.02300 0.00160  562 HOH A O   
5015 O O   . HOH E .   ? 0.63020 0.91390 0.60120 0.02090  -0.03570 0.13240  563 HOH A O   
5016 O O   . HOH E .   ? 0.57710 0.65840 0.58370 -0.00440 0.02110  0.02630  564 HOH A O   
5017 O O   . HOH E .   ? 0.62870 0.58260 0.59040 -0.00290 0.00450  0.00020  565 HOH A O   
5018 O O   . HOH E .   ? 0.71540 0.90440 0.69320 -0.01760 0.07290  0.07310  566 HOH A O   
5019 O O   . HOH E .   ? 0.67590 0.67440 0.65420 -0.02150 -0.00140 -0.04000 567 HOH A O   
5020 O O   . HOH E .   ? 0.51910 0.70380 0.52480 0.03140  -0.01090 0.12700  568 HOH A O   
5021 O O   . HOH E .   ? 0.66240 0.74210 0.82590 0.06700  0.02270  0.12390  569 HOH A O   
5022 O O   . HOH E .   ? 0.75240 0.80810 0.74000 -0.03870 -0.01730 -0.09350 570 HOH A O   
5023 O O   . HOH E .   ? 0.63580 0.68080 0.60460 -0.02780 -0.01060 -0.05780 571 HOH A O   
5024 O O   . HOH E .   ? 0.67540 0.77350 0.69230 -0.01750 0.02980  0.04010  572 HOH A O   
5025 O O   . HOH E .   ? 0.62220 0.73660 0.64270 -0.01110 -0.00370 0.02670  573 HOH A O   
5026 O O   . HOH E .   ? 0.59860 0.72860 0.62020 -0.01940 -0.01510 0.01980  574 HOH A O   
5027 O O   . HOH E .   ? 0.54190 0.64260 0.56790 0.01300  0.01190  0.03800  575 HOH A O   
5028 O O   . HOH E .   ? 0.66410 0.89670 0.67060 0.03350  -0.01910 0.15380  576 HOH A O   
5029 O O   . HOH F .   ? 0.63060 0.56900 0.70570 -0.00870 -0.01440 -0.11490 401 HOH B O   
5030 O O   . HOH F .   ? 0.76420 0.76510 0.82230 -0.02570 -0.02520 0.13740  402 HOH B O   
5031 O O   . HOH F .   ? 0.58070 0.50580 1.03550 -0.07080 -0.04960 -0.05700 403 HOH B O   
5032 O O   . HOH F .   ? 0.71950 0.59610 1.22940 -0.07760 -0.06260 -0.16990 404 HOH B O   
5033 O O   . HOH F .   ? 0.67560 0.63160 0.71030 -0.00810 -0.01550 -0.11080 405 HOH B O   
5034 O O   . HOH F .   ? 0.58040 0.42880 0.89990 -0.01480 -0.00110 -0.00420 406 HOH B O   
5035 O O   . HOH F .   ? 0.56860 0.51230 0.55810 -0.00040 0.00100  0.00210  407 HOH B O   
5036 O O   . HOH F .   ? 0.77060 0.65780 1.08380 -0.03920 -0.03660 -0.16710 408 HOH B O   
5037 O O   . HOH F .   ? 0.52980 0.47050 0.59520 0.00420  0.02560  -0.07170 409 HOH B O   
5038 O O   . HOH F .   ? 0.80530 0.75200 1.16330 -0.02340 0.03760  0.10080  410 HOH B O   
5039 O O   . HOH F .   ? 0.63090 0.63130 0.57580 -0.01220 -0.02430 0.02830  411 HOH B O   
5040 O O   . HOH F .   ? 0.55210 0.53370 0.72230 -0.00150 0.00180  0.02530  412 HOH B O   
5041 O O   . HOH F .   ? 0.80080 0.70100 1.12450 -0.00640 0.03100  0.07150  413 HOH B O   
5042 O O   . HOH F .   ? 0.65540 0.59870 0.65110 -0.00720 0.00430  -0.00920 414 HOH B O   
5043 O O   . HOH F .   ? 0.55090 0.51840 0.54530 0.00850  0.02480  0.00970  415 HOH B O   
5044 O O   . HOH F .   ? 0.60140 0.51970 0.79960 -0.03710 -0.01320 0.09630  416 HOH B O   
5045 O O   . HOH F .   ? 0.67360 0.61000 0.90580 0.02300  -0.01550 0.05260  417 HOH B O   
5046 O O   . HOH F .   ? 0.41830 0.37800 0.49810 0.00330  0.01350  0.01430  418 HOH B O   
5047 O O   . HOH F .   ? 0.54850 0.52270 0.66870 0.02100  0.03630  -0.00510 419 HOH B O   
5048 O O   . HOH F .   ? 0.76240 0.68460 1.04480 -0.01130 0.02930  0.06890  420 HOH B O   
5049 O O   . HOH F .   ? 0.53630 0.47500 0.55620 0.00760  0.01330  0.00060  421 HOH B O   
5050 O O   . HOH F .   ? 0.48940 0.50290 0.63890 0.00800  0.05490  0.04950  422 HOH B O   
5051 O O   . HOH F .   ? 0.68310 0.56350 0.93570 -0.01630 -0.00860 -0.09220 423 HOH B O   
5052 O O   . HOH F .   ? 0.66850 0.62930 0.62170 -0.00460 0.00180  0.00480  424 HOH B O   
5053 O O   . HOH F .   ? 0.52310 0.49100 0.51680 -0.00700 -0.02540 0.02380  425 HOH B O   
5054 O O   . HOH F .   ? 0.95170 0.82910 1.18510 0.00440  0.01440  -0.03980 426 HOH B O   
5055 O O   . HOH F .   ? 0.64700 0.49000 1.12600 0.03760  0.01200  0.01080  427 HOH B O   
5056 O O   . HOH F .   ? 0.55850 0.51600 0.68640 0.01900  0.02030  0.00020  428 HOH B O   
5057 O O   . HOH F .   ? 0.58150 0.57250 0.74120 -0.01320 -0.04060 0.01610  429 HOH B O   
5058 O O   . HOH F .   ? 0.62210 0.61380 0.57360 0.00100  0.00040  -0.08230 430 HOH B O   
5059 O O   . HOH F .   ? 0.54020 0.52410 0.61880 -0.01650 -0.04780 -0.00370 431 HOH B O   
5060 O O   . HOH F .   ? 0.71810 0.75130 0.89550 -0.07190 -0.11240 -0.23420 432 HOH B O   
5061 O O   . HOH F .   ? 0.59790 0.54500 0.61700 0.00550  0.01880  -0.02590 433 HOH B O   
5062 O O   . HOH F .   ? 0.65470 0.57620 0.72380 0.00930  0.01110  -0.04590 434 HOH B O   
5063 O O   . HOH F .   ? 0.53460 0.51870 0.72130 -0.00470 0.01820  0.03620  435 HOH B O   
5064 O O   . HOH F .   ? 0.62070 0.59330 0.63860 0.01220  0.03370  -0.01600 436 HOH B O   
5065 O O   . HOH F .   ? 0.61730 0.60800 0.61570 -0.02370 -0.00930 0.07720  437 HOH B O   
5066 O O   . HOH F .   ? 0.60260 0.57540 0.58450 -0.01110 -0.01900 0.04260  438 HOH B O   
5067 O O   . HOH F .   ? 0.45480 0.44470 0.54270 0.01690  0.04530  0.00490  439 HOH B O   
5068 O O   . HOH F .   ? 0.64290 0.63930 0.78430 -0.03380 -0.06740 -0.03500 440 HOH B O   
5069 O O   . HOH F .   ? 0.53650 0.48260 0.56270 -0.00810 -0.01580 -0.04150 441 HOH B O   
5070 O O   . HOH F .   ? 0.59890 0.57700 0.85740 -0.06060 -0.08260 -0.10570 442 HOH B O   
5071 O O   . HOH F .   ? 0.50890 0.44680 0.60310 0.00520  -0.01460 0.03260  443 HOH B O   
5072 O O   . HOH F .   ? 0.74650 0.71170 0.78270 -0.02270 0.00490  -0.08930 444 HOH B O   
5073 O O   . HOH F .   ? 0.71290 0.73120 0.73570 -0.03360 -0.00690 0.12050  445 HOH B O   
5074 O O   . HOH F .   ? 0.54580 0.51290 0.66870 0.00500  -0.01400 0.02320  446 HOH B O   
5075 O O   . HOH F .   ? 0.53880 0.48530 0.54810 0.00440  0.00950  -0.00050 447 HOH B O   
5076 O O   . HOH F .   ? 0.53860 0.49300 0.49910 -0.00260 -0.00150 0.00100  448 HOH B O   
5077 O O   . HOH F .   ? 0.62090 0.57350 0.76840 -0.00510 -0.03640 0.11520  449 HOH B O   
5078 O O   . HOH F .   ? 0.42540 0.47010 0.59100 0.00770  0.07500  0.08180  450 HOH B O   
5079 O O   . HOH F .   ? 0.63210 0.56550 0.83330 0.03290  0.04670  -0.06950 451 HOH B O   
5080 O O   . HOH F .   ? 0.47450 0.40170 0.52430 -0.00240 -0.00210 0.00850  452 HOH B O   
5081 O O   . HOH F .   ? 0.61300 0.57690 0.63990 0.01200  0.03190  -0.03150 453 HOH B O   
5082 O O   . HOH F .   ? 0.57660 0.54350 0.60330 -0.00550 -0.03040 0.04360  454 HOH B O   
5083 O O   . HOH F .   ? 0.67590 0.68430 0.70320 0.01320  0.04610  0.05530  455 HOH B O   
5084 O O   . HOH F .   ? 0.50880 0.49920 0.78770 -0.01670 0.03740  0.07850  456 HOH B O   
5085 O O   . HOH F .   ? 0.62450 0.65390 0.71240 -0.04620 -0.09060 -0.10490 457 HOH B O   
5086 O O   . HOH F .   ? 0.50470 0.48280 0.52910 0.01270  0.03640  -0.00420 458 HOH B O   
5087 O O   . HOH F .   ? 0.62300 0.58710 0.60540 0.00730  0.02080  0.00490  459 HOH B O   
5088 O O   . HOH F .   ? 0.54060 0.44560 0.68810 -0.00040 0.00870  -0.01980 460 HOH B O   
5089 O O   . HOH F .   ? 0.52510 0.47620 0.51970 -0.00510 -0.01240 0.02000  461 HOH B O   
5090 O O   . HOH F .   ? 0.61600 0.56510 0.66160 0.00730  0.02730  -0.05720 462 HOH B O   
5091 O O   . HOH F .   ? 0.62530 0.57340 0.65050 0.00330  0.02080  -0.04440 463 HOH B O   
5092 O O   . HOH F .   ? 0.71740 0.68050 0.76830 -0.01530 0.01470  -0.11470 464 HOH B O   
5093 O O   . HOH F .   ? 0.61380 0.55740 0.66140 -0.02770 -0.00220 -0.01080 465 HOH B O   
5094 O O   . HOH F .   ? 0.56590 0.50570 0.57610 -0.01190 0.00040  0.00050  466 HOH B O   
5095 O O   . HOH F .   ? 0.62060 0.58680 0.68800 0.01260  0.04320  -0.10190 467 HOH B O   
5096 O O   . HOH F .   ? 0.64090 0.57010 0.84130 0.02620  0.01360  0.00030  468 HOH B O   
5097 O O   . HOH F .   ? 0.41280 0.35540 0.59850 -0.01540 0.00400  0.01790  469 HOH B O   
5098 O O   . HOH F .   ? 0.60840 0.57310 1.02140 -0.03480 0.03580  0.10510  470 HOH B O   
5099 O O   . HOH F .   ? 0.44180 0.42390 0.67880 -0.01280 0.03060  0.06160  471 HOH B O   
5100 O O   . HOH F .   ? 0.72450 0.72750 1.04940 -0.01390 0.06610  0.15140  472 HOH B O   
5101 O O   . HOH F .   ? 0.49940 0.47520 0.78110 -0.03340 -0.02180 0.01420  473 HOH B O   
5102 O O   . HOH F .   ? 0.45800 0.43700 0.66310 -0.01000 0.01950  0.04250  474 HOH B O   
5103 O O   . HOH F .   ? 0.47620 0.45480 0.65930 -0.00810 0.00170  0.02640  475 HOH B O   
5104 O O   . HOH F .   ? 0.56200 0.54090 0.91580 -0.03510 0.00840  0.05490  476 HOH B O   
5105 O O   . HOH F .   ? 0.50140 0.47200 0.84520 -0.05770 -0.05680 -0.03580 477 HOH B O   
5106 O O   . HOH F .   ? 0.52610 0.44500 0.68540 0.01600  0.00550  0.00430  478 HOH B O   
5107 O O   . HOH F .   ? 0.53440 0.50930 0.67670 0.00850  0.00980  0.01940  479 HOH B O   
5108 O O   . HOH F .   ? 0.57180 0.52100 0.60990 -0.00090 0.02130  -0.06900 480 HOH B O   
5109 O O   . HOH F .   ? 0.82130 0.71040 1.19380 -0.01760 0.02350  0.05460  481 HOH B O   
5110 O O   . HOH F .   ? 0.61830 0.53850 1.11910 -0.04520 0.02420  0.09030  482 HOH B O   
5111 O O   . HOH F .   ? 0.66190 0.66460 0.88670 -0.00050 0.06290  0.13480  483 HOH B O   
5112 O O   . HOH F .   ? 0.81140 0.80370 1.09210 -0.00490 0.06320  0.15180  484 HOH B O   
5113 O O   . HOH F .   ? 0.64080 0.58300 0.65150 0.00150  0.01230  -0.01910 485 HOH B O   
5114 O O   . HOH F .   ? 0.65360 0.54750 1.00750 -0.02410 0.01330  0.03110  486 HOH B O   
5115 O O   . HOH F .   ? 0.56800 0.41550 0.97700 -0.01100 -0.01560 0.09630  487 HOH B O   
5116 O O   . HOH F .   ? 0.70830 0.63600 1.01180 -0.00180 -0.04070 0.17440  488 HOH B O   
5117 O O   . HOH F .   ? 0.42500 0.44510 0.45750 0.01520  0.05680  0.02590  489 HOH B O   
5118 O O   . HOH F .   ? 0.65550 0.50160 0.99520 -0.00120 0.02180  -0.11280 490 HOH B O   
5119 O O   . HOH F .   ? 0.60330 0.65080 0.67000 -0.03130 -0.09120 -0.01470 491 HOH B O   
5120 O O   . HOH F .   ? 0.54470 0.51040 0.57790 -0.00410 -0.03050 0.03500  492 HOH B O   
5121 O O   . HOH F .   ? 0.55930 0.64050 0.72270 0.00860  0.09260  0.12470  493 HOH B O   
5122 O O   . HOH F .   ? 0.73600 0.58220 1.17000 -0.03650 -0.01470 -0.09550 494 HOH B O   
5123 O O   . HOH F .   ? 0.51580 0.55250 0.62380 0.01600  0.07100  0.04140  495 HOH B O   
5124 O O   . HOH F .   ? 0.54730 0.53310 0.56820 -0.01080 -0.04350 0.01440  496 HOH B O   
5125 O O   . HOH F .   ? 0.67340 0.57990 0.79470 0.01230  0.01580  -0.04380 497 HOH B O   
5126 O O   . HOH F .   ? 0.55960 0.42340 0.94890 0.01240  -0.01500 0.08530  498 HOH B O   
5127 O O   . HOH F .   ? 0.69920 0.65630 0.87470 0.00320  0.04050  0.08500  499 HOH B O   
5128 O O   . HOH F .   ? 0.78950 0.65710 1.16270 0.03210  0.05360  -0.15580 500 HOH B O   
5129 O O   . HOH F .   ? 0.59240 0.52360 0.90380 0.03170  -0.01870 0.07210  501 HOH B O   
5130 O O   . HOH F .   ? 0.54570 0.51270 0.62570 0.01060  0.03540  0.06080  502 HOH B O   
5131 O O   . HOH F .   ? 0.71430 0.54230 1.25270 0.04990  0.04320  -0.08300 503 HOH B O   
5132 O O   . HOH F .   ? 0.68410 0.53900 1.08010 -0.02860 -0.00510 -0.05760 504 HOH B O   
5133 O O   . HOH F .   ? 0.64960 0.54180 1.04900 0.02140  -0.02870 0.12780  505 HOH B O   
5134 O O   . HOH F .   ? 0.53260 0.54330 0.63760 -0.01190 -0.06430 0.03240  506 HOH B O   
5135 O O   . HOH F .   ? 0.66750 0.62000 0.75380 0.00360  0.03460  -0.12320 507 HOH B O   
5136 O O   . HOH F .   ? 0.78690 0.86790 0.81270 -0.04950 -0.08430 -0.26450 508 HOH B O   
5137 O O   . HOH F .   ? 0.58990 0.56210 0.67360 -0.00050 -0.03660 0.04010  509 HOH B O   
5138 O O   . HOH F .   ? 0.56440 0.56040 0.57690 0.01410  0.04430  -0.00220 510 HOH B O   
5139 O O   . HOH F .   ? 0.55190 0.51210 0.63350 -0.00170 -0.03360 0.06710  511 HOH B O   
5140 O O   . HOH F .   ? 0.54330 0.52320 0.86010 -0.02670 0.01980  0.06300  512 HOH B O   
5141 O O   . HOH F .   ? 0.65000 0.58700 0.74460 -0.03720 -0.00490 -0.04420 513 HOH B O   
5142 O O   . HOH F .   ? 0.79330 0.70990 1.03410 0.01980  0.05550  -0.18590 514 HOH B O   
5143 O O   . HOH F .   ? 0.63300 0.58610 1.02260 -0.07860 -0.08500 -0.12670 515 HOH B O   
5144 O O   . HOH F .   ? 0.80260 0.72610 1.07180 -0.00460 0.03430  0.08020  516 HOH B O   
5145 O O   . HOH F .   ? 0.68780 0.63510 0.82020 0.01820  0.01190  0.00390  517 HOH B O   
5146 O O   . HOH F .   ? 0.59430 0.55380 0.67340 0.01370  0.03230  0.05870  518 HOH B O   
5147 O O   . HOH F .   ? 0.53320 0.49330 0.51220 -0.00790 -0.01320 0.02460  519 HOH B O   
5148 O O   . HOH F .   ? 0.66440 0.66700 0.78710 -0.00530 -0.05710 0.04420  520 HOH B O   
5149 O O   . HOH F .   ? 0.82360 0.83060 0.87530 -0.02990 -0.01910 0.13820  521 HOH B O   
5150 O O   . HOH F .   ? 0.90200 0.92250 0.98670 -0.02960 -0.02950 0.17900  522 HOH B O   
5151 O O   . HOH F .   ? 0.73490 0.69250 0.71760 -0.00470 0.01070  -0.02680 523 HOH B O   
5152 O O   . HOH F .   ? 0.74490 0.72930 1.03870 -0.07120 -0.09530 -0.13040 524 HOH B O   
5153 O O   . HOH F .   ? 0.57060 0.52920 0.53000 -0.00630 0.00250  0.00550  525 HOH B O   
5154 O O   . HOH F .   ? 0.68490 0.63970 0.65330 -0.00780 0.00200  0.00520  526 HOH B O   
5155 O O   . HOH F .   ? 0.64240 0.62530 0.81160 0.00510  0.00360  0.02500  527 HOH B O   
5156 O O   . HOH F .   ? 0.70120 0.72430 0.69870 0.01460  0.04540  0.04840  528 HOH B O   
5157 O O   . HOH F .   ? 0.61780 0.56270 1.05230 -0.06730 -0.04670 -0.03350 529 HOH B O   
5158 O O   . HOH F .   ? 0.76440 0.74640 0.80180 -0.00640 -0.04190 0.04120  530 HOH B O   
5159 O O   . HOH F .   ? 0.70460 0.69080 0.73520 -0.02610 -0.01350 0.09710  531 HOH B O   
5160 O O   . HOH F .   ? 0.81330 0.77210 0.84110 -0.02890 -0.00200 -0.00810 532 HOH B O   
5161 O O   . HOH F .   ? 0.66070 0.67980 0.79000 -0.03940 -0.08440 -0.04650 533 HOH B O   
5162 O O   . HOH F .   ? 0.66440 0.52290 1.12070 0.03530  -0.00060 0.04940  534 HOH B O   
5163 O O   . HOH F .   ? 0.84060 0.95680 0.82810 -0.05270 -0.09610 -0.24260 535 HOH B O   
5164 O O   . HOH F .   ? 0.61690 0.57810 0.59290 0.00540  0.01770  -0.00330 536 HOH B O   
5165 O O   . HOH F .   ? 0.87840 0.80120 0.99160 0.00510  0.00520  -0.13950 537 HOH B O   
5166 O O   . HOH F .   ? 0.65760 0.59090 0.89430 0.03260  0.01760  0.00040  538 HOH B O   
5167 O O   . HOH F .   ? 0.64950 0.61140 0.66510 0.00320  0.02550  -0.06010 539 HOH B O   
5168 O O   . HOH F .   ? 0.60020 0.56660 0.97080 -0.05490 -0.04030 -0.01030 540 HOH B O   
5169 O O   . HOH F .   ? 0.64950 0.60400 0.71850 0.00670  0.03460  -0.09990 541 HOH B O   
5170 O O   . HOH G .   ? 0.88180 0.94070 0.99540 -0.06510 0.01710  0.13000  201 HOH C O   
5171 O O   . HOH G .   ? 0.66230 0.76730 0.71910 -0.05580 0.01910  0.19130  202 HOH C O   
5172 O O   . HOH G .   ? 0.83990 1.06610 0.73500 -0.03740 0.03220  0.16410  203 HOH C O   
5173 O O   . HOH G .   ? 0.69560 0.74030 0.74530 -0.04800 0.01110  0.12600  204 HOH C O   
5174 O O   . HOH G .   ? 0.90680 0.95520 1.08630 -0.07830 0.01360  0.15280  205 HOH C O   
5175 O O   . HOH H .   ? 0.54820 0.55880 0.61200 0.01140  0.05270  0.06690  201 HOH D O   
5176 O O   . HOH H .   ? 0.70790 0.65520 0.86810 0.00440  0.03520  0.07040  202 HOH D O   
5177 O O   . HOH H .   ? 0.59000 0.60370 0.72160 0.00810  0.05980  0.10830  203 HOH D O   
5178 O O   . HOH H .   ? 0.60800 0.53610 0.83970 -0.00990 0.02390  0.05100  204 HOH D O   
5179 O O   . HOH H .   ? 0.79160 0.86290 0.95340 0.00770  0.08700  0.13790  205 HOH D O   
5180 O O   . HOH H .   ? 0.95780 0.83790 1.20210 0.00750  0.02060  -0.00680 206 HOH D O   
5181 O O   . HOH H .   ? 0.68920 0.75970 0.75050 0.01730  0.08110  0.06310  207 HOH D O   
5182 O O   . HOH H .   ? 0.69190 0.61340 0.91570 -0.00130 0.02930  0.06010  208 HOH D O   
5183 O O   . HOH H .   ? 0.69550 0.73100 0.78540 0.01250  0.06350  0.10590  209 HOH D O   
# 
