data_9CDK
# 
_entry.id   9CDK 
# 
_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   9CDK         pdb_00009cdk 10.2210/pdb9cdk/pdb 
WWPDB D_1000285268 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-05 ? 
2 'Structure model' 1 1 2025-03-12 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CDK 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              karen.anderson@yale.edu 
_pdbx_contact_author.name_first         Karen 
_pdbx_contact_author.name_last          Anderson 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3433-0780 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tang, S.'       1 0000-0002-6993-1212 
'Kenneson, J.R.' 2 0000-0001-9582-3867 
'Anderson, K.S.' 3 0000-0003-3433-0780 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Bio Med Chem Au' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2694-2437 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            5 
_citation.language                  ? 
_citation.page_first                215 
_citation.page_last                 226 
_citation.title                     
'Exploring Possible Drug-Resistant Variants of SARS-CoV-2 Main Protease (M pro ) with Noncovalent Preclinical Candidate, Mpro61.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsbiomedchemau.4c00109 
_citation.pdbx_database_id_PubMed   39990941 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kenneson, J.R.'  1 ? 
primary 'Papini, C.'      2 ? 
primary 'Tang, S.'        3 ? 
primary 'Huynh, K.'       4 ? 
primary 'Zhang, C.H.'     5 ? 
primary 'Jorgensen, W.L.' 6 ? 
primary 'Anderson, K.S.'  7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '3C-like proteinase nsp5' 33853.598 1   ? A173V ? ? 
2 non-polymer syn 
;(5P)-5-[(1P,3M,3'P)-3-{3-chloro-5-[(2-chlorophenyl)methoxy]-4-fluorophenyl}-2-oxo-2H-[1,3'-bipyridin]-5-yl]-1-methylpyrimidine-2,4(1H,3H)-dione
;
565.379   1   ? ?     ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    4   ? ?     ? ? 
4 non-polymer syn 'CHLORIDE ION' 35.453    1   ? ?     ? ? 
5 water       nat water 18.015    277 ? ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHVGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHVGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(5P)-5-[(1P,3M,3'P)-3-{3-chloro-5-[(2-chlorophenyl)methoxy]-4-fluorophenyl}-2-oxo-2H-[1,3'-bipyridin]-5-yl]-1-methylpyrimidine-2,4(1H,3H)-dione
;
XEK 
3 'DIMETHYL SULFOXIDE' DMS 
4 'CHLORIDE ION' CL  
5 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 VAL 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 
# 
_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               '2019-nCoV, SARS-CoV-2' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 rep 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CL  non-polymer         . 'CHLORIDE ION' ? 'Cl -1'               35.453  
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'           78.133  
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'         117.146 
XEK non-polymer         . 
;(5P)-5-[(1P,3M,3'P)-3-{3-chloro-5-[(2-chlorophenyl)methoxy]-4-fluorophenyl}-2-oxo-2H-[1,3'-bipyridin]-5-yl]-1-methylpyrimidine-2,4(1H,3H)-dione
;
? 'C28 H19 Cl2 F N4 O4' 565.379 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        XEK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   XEK 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 XEK 1   401 401 XEK M61 A . 
C 3 DMS 1   402 402 DMS DMS A . 
D 3 DMS 1   403 403 DMS DMS A . 
E 3 DMS 1   404 404 DMS DMS A . 
F 3 DMS 1   405 405 DMS DMS A . 
G 4 CL  1   406 1   CL  CL  A . 
H 5 HOH 1   501 91  HOH HOH A . 
H 5 HOH 2   502 215 HOH HOH A . 
H 5 HOH 3   503 167 HOH HOH A . 
H 5 HOH 4   504 132 HOH HOH A . 
H 5 HOH 5   505 108 HOH HOH A . 
H 5 HOH 6   506 34  HOH HOH A . 
H 5 HOH 7   507 116 HOH HOH A . 
H 5 HOH 8   508 72  HOH HOH A . 
H 5 HOH 9   509 166 HOH HOH A . 
H 5 HOH 10  510 246 HOH HOH A . 
H 5 HOH 11  511 75  HOH HOH A . 
H 5 HOH 12  512 265 HOH HOH A . 
H 5 HOH 13  513 145 HOH HOH A . 
H 5 HOH 14  514 148 HOH HOH A . 
H 5 HOH 15  515 15  HOH HOH A . 
H 5 HOH 16  516 61  HOH HOH A . 
H 5 HOH 17  517 40  HOH HOH A . 
H 5 HOH 18  518 45  HOH HOH A . 
H 5 HOH 19  519 11  HOH HOH A . 
H 5 HOH 20  520 165 HOH HOH A . 
H 5 HOH 21  521 264 HOH HOH A . 
H 5 HOH 22  522 27  HOH HOH A . 
H 5 HOH 23  523 39  HOH HOH A . 
H 5 HOH 24  524 33  HOH HOH A . 
H 5 HOH 25  525 248 HOH HOH A . 
H 5 HOH 26  526 196 HOH HOH A . 
H 5 HOH 27  527 104 HOH HOH A . 
H 5 HOH 28  528 83  HOH HOH A . 
H 5 HOH 29  529 30  HOH HOH A . 
H 5 HOH 30  530 105 HOH HOH A . 
H 5 HOH 31  531 220 HOH HOH A . 
H 5 HOH 32  532 36  HOH HOH A . 
H 5 HOH 33  533 118 HOH HOH A . 
H 5 HOH 34  534 143 HOH HOH A . 
H 5 HOH 35  535 194 HOH HOH A . 
H 5 HOH 36  536 106 HOH HOH A . 
H 5 HOH 37  537 13  HOH HOH A . 
H 5 HOH 38  538 159 HOH HOH A . 
H 5 HOH 39  539 170 HOH HOH A . 
H 5 HOH 40  540 238 HOH HOH A . 
H 5 HOH 41  541 126 HOH HOH A . 
H 5 HOH 42  542 120 HOH HOH A . 
H 5 HOH 43  543 50  HOH HOH A . 
H 5 HOH 44  544 237 HOH HOH A . 
H 5 HOH 45  545 160 HOH HOH A . 
H 5 HOH 46  546 157 HOH HOH A . 
H 5 HOH 47  547 119 HOH HOH A . 
H 5 HOH 48  548 18  HOH HOH A . 
H 5 HOH 49  549 184 HOH HOH A . 
H 5 HOH 50  550 268 HOH HOH A . 
H 5 HOH 51  551 171 HOH HOH A . 
H 5 HOH 52  552 17  HOH HOH A . 
H 5 HOH 53  553 208 HOH HOH A . 
H 5 HOH 54  554 181 HOH HOH A . 
H 5 HOH 55  555 48  HOH HOH A . 
H 5 HOH 56  556 103 HOH HOH A . 
H 5 HOH 57  557 31  HOH HOH A . 
H 5 HOH 58  558 109 HOH HOH A . 
H 5 HOH 59  559 230 HOH HOH A . 
H 5 HOH 60  560 125 HOH HOH A . 
H 5 HOH 61  561 231 HOH HOH A . 
H 5 HOH 62  562 3   HOH HOH A . 
H 5 HOH 63  563 66  HOH HOH A . 
H 5 HOH 64  564 69  HOH HOH A . 
H 5 HOH 65  565 12  HOH HOH A . 
H 5 HOH 66  566 56  HOH HOH A . 
H 5 HOH 67  567 26  HOH HOH A . 
H 5 HOH 68  568 180 HOH HOH A . 
H 5 HOH 69  569 153 HOH HOH A . 
H 5 HOH 70  570 130 HOH HOH A . 
H 5 HOH 71  571 20  HOH HOH A . 
H 5 HOH 72  572 146 HOH HOH A . 
H 5 HOH 73  573 47  HOH HOH A . 
H 5 HOH 74  574 38  HOH HOH A . 
H 5 HOH 75  575 113 HOH HOH A . 
H 5 HOH 76  576 16  HOH HOH A . 
H 5 HOH 77  577 190 HOH HOH A . 
H 5 HOH 78  578 29  HOH HOH A . 
H 5 HOH 79  579 2   HOH HOH A . 
H 5 HOH 80  580 62  HOH HOH A . 
H 5 HOH 81  581 51  HOH HOH A . 
H 5 HOH 82  582 139 HOH HOH A . 
H 5 HOH 83  583 101 HOH HOH A . 
H 5 HOH 84  584 70  HOH HOH A . 
H 5 HOH 85  585 210 HOH HOH A . 
H 5 HOH 86  586 59  HOH HOH A . 
H 5 HOH 87  587 21  HOH HOH A . 
H 5 HOH 88  588 68  HOH HOH A . 
H 5 HOH 89  589 221 HOH HOH A . 
H 5 HOH 90  590 260 HOH HOH A . 
H 5 HOH 91  591 254 HOH HOH A . 
H 5 HOH 92  592 172 HOH HOH A . 
H 5 HOH 93  593 7   HOH HOH A . 
H 5 HOH 94  594 209 HOH HOH A . 
H 5 HOH 95  595 99  HOH HOH A . 
H 5 HOH 96  596 52  HOH HOH A . 
H 5 HOH 97  597 41  HOH HOH A . 
H 5 HOH 98  598 8   HOH HOH A . 
H 5 HOH 99  599 117 HOH HOH A . 
H 5 HOH 100 600 129 HOH HOH A . 
H 5 HOH 101 601 22  HOH HOH A . 
H 5 HOH 102 602 214 HOH HOH A . 
H 5 HOH 103 603 174 HOH HOH A . 
H 5 HOH 104 604 156 HOH HOH A . 
H 5 HOH 105 605 14  HOH HOH A . 
H 5 HOH 106 606 58  HOH HOH A . 
H 5 HOH 107 607 98  HOH HOH A . 
H 5 HOH 108 608 114 HOH HOH A . 
H 5 HOH 109 609 49  HOH HOH A . 
H 5 HOH 110 610 4   HOH HOH A . 
H 5 HOH 111 611 42  HOH HOH A . 
H 5 HOH 112 612 97  HOH HOH A . 
H 5 HOH 113 613 207 HOH HOH A . 
H 5 HOH 114 614 43  HOH HOH A . 
H 5 HOH 115 615 6   HOH HOH A . 
H 5 HOH 116 616 65  HOH HOH A . 
H 5 HOH 117 617 57  HOH HOH A . 
H 5 HOH 118 618 5   HOH HOH A . 
H 5 HOH 119 619 19  HOH HOH A . 
H 5 HOH 120 620 127 HOH HOH A . 
H 5 HOH 121 621 81  HOH HOH A . 
H 5 HOH 122 622 161 HOH HOH A . 
H 5 HOH 123 623 74  HOH HOH A . 
H 5 HOH 124 624 24  HOH HOH A . 
H 5 HOH 125 625 168 HOH HOH A . 
H 5 HOH 126 626 37  HOH HOH A . 
H 5 HOH 127 627 137 HOH HOH A . 
H 5 HOH 128 628 201 HOH HOH A . 
H 5 HOH 129 629 110 HOH HOH A . 
H 5 HOH 130 630 32  HOH HOH A . 
H 5 HOH 131 631 107 HOH HOH A . 
H 5 HOH 132 632 257 HOH HOH A . 
H 5 HOH 133 633 86  HOH HOH A . 
H 5 HOH 134 634 44  HOH HOH A . 
H 5 HOH 135 635 84  HOH HOH A . 
H 5 HOH 136 636 85  HOH HOH A . 
H 5 HOH 137 637 178 HOH HOH A . 
H 5 HOH 138 638 55  HOH HOH A . 
H 5 HOH 139 639 64  HOH HOH A . 
H 5 HOH 140 640 183 HOH HOH A . 
H 5 HOH 141 641 241 HOH HOH A . 
H 5 HOH 142 642 191 HOH HOH A . 
H 5 HOH 143 643 95  HOH HOH A . 
H 5 HOH 144 644 195 HOH HOH A . 
H 5 HOH 145 645 76  HOH HOH A . 
H 5 HOH 146 646 90  HOH HOH A . 
H 5 HOH 147 647 197 HOH HOH A . 
H 5 HOH 148 648 115 HOH HOH A . 
H 5 HOH 149 649 223 HOH HOH A . 
H 5 HOH 150 650 96  HOH HOH A . 
H 5 HOH 151 651 217 HOH HOH A . 
H 5 HOH 152 652 228 HOH HOH A . 
H 5 HOH 153 653 199 HOH HOH A . 
H 5 HOH 154 654 88  HOH HOH A . 
H 5 HOH 155 655 149 HOH HOH A . 
H 5 HOH 156 656 67  HOH HOH A . 
H 5 HOH 157 657 54  HOH HOH A . 
H 5 HOH 158 658 155 HOH HOH A . 
H 5 HOH 159 659 252 HOH HOH A . 
H 5 HOH 160 660 147 HOH HOH A . 
H 5 HOH 161 661 232 HOH HOH A . 
H 5 HOH 162 662 212 HOH HOH A . 
H 5 HOH 163 663 276 HOH HOH A . 
H 5 HOH 164 664 80  HOH HOH A . 
H 5 HOH 165 665 270 HOH HOH A . 
H 5 HOH 166 666 133 HOH HOH A . 
H 5 HOH 167 667 273 HOH HOH A . 
H 5 HOH 168 668 77  HOH HOH A . 
H 5 HOH 169 669 9   HOH HOH A . 
H 5 HOH 170 670 225 HOH HOH A . 
H 5 HOH 171 671 242 HOH HOH A . 
H 5 HOH 172 672 46  HOH HOH A . 
H 5 HOH 173 673 23  HOH HOH A . 
H 5 HOH 174 674 10  HOH HOH A . 
H 5 HOH 175 675 35  HOH HOH A . 
H 5 HOH 176 676 244 HOH HOH A . 
H 5 HOH 177 677 134 HOH HOH A . 
H 5 HOH 178 678 198 HOH HOH A . 
H 5 HOH 179 679 1   HOH HOH A . 
H 5 HOH 180 680 79  HOH HOH A . 
H 5 HOH 181 681 158 HOH HOH A . 
H 5 HOH 182 682 226 HOH HOH A . 
H 5 HOH 183 683 175 HOH HOH A . 
H 5 HOH 184 684 138 HOH HOH A . 
H 5 HOH 185 685 25  HOH HOH A . 
H 5 HOH 186 686 263 HOH HOH A . 
H 5 HOH 187 687 131 HOH HOH A . 
H 5 HOH 188 688 274 HOH HOH A . 
H 5 HOH 189 689 251 HOH HOH A . 
H 5 HOH 190 690 93  HOH HOH A . 
H 5 HOH 191 691 192 HOH HOH A . 
H 5 HOH 192 692 266 HOH HOH A . 
H 5 HOH 193 693 142 HOH HOH A . 
H 5 HOH 194 694 28  HOH HOH A . 
H 5 HOH 195 695 89  HOH HOH A . 
H 5 HOH 196 696 271 HOH HOH A . 
H 5 HOH 197 697 63  HOH HOH A . 
H 5 HOH 198 698 111 HOH HOH A . 
H 5 HOH 199 699 227 HOH HOH A . 
H 5 HOH 200 700 60  HOH HOH A . 
H 5 HOH 201 701 100 HOH HOH A . 
H 5 HOH 202 702 256 HOH HOH A . 
H 5 HOH 203 703 206 HOH HOH A . 
H 5 HOH 204 704 229 HOH HOH A . 
H 5 HOH 205 705 154 HOH HOH A . 
H 5 HOH 206 706 186 HOH HOH A . 
H 5 HOH 207 707 151 HOH HOH A . 
H 5 HOH 208 708 193 HOH HOH A . 
H 5 HOH 209 709 261 HOH HOH A . 
H 5 HOH 210 710 258 HOH HOH A . 
H 5 HOH 211 711 200 HOH HOH A . 
H 5 HOH 212 712 236 HOH HOH A . 
H 5 HOH 213 713 112 HOH HOH A . 
H 5 HOH 214 714 136 HOH HOH A . 
H 5 HOH 215 715 188 HOH HOH A . 
H 5 HOH 216 716 122 HOH HOH A . 
H 5 HOH 217 717 234 HOH HOH A . 
H 5 HOH 218 718 152 HOH HOH A . 
H 5 HOH 219 719 233 HOH HOH A . 
H 5 HOH 220 720 245 HOH HOH A . 
H 5 HOH 221 721 222 HOH HOH A . 
H 5 HOH 222 722 259 HOH HOH A . 
H 5 HOH 223 723 218 HOH HOH A . 
H 5 HOH 224 724 162 HOH HOH A . 
H 5 HOH 225 725 239 HOH HOH A . 
H 5 HOH 226 726 82  HOH HOH A . 
H 5 HOH 227 727 185 HOH HOH A . 
H 5 HOH 228 728 187 HOH HOH A . 
H 5 HOH 229 729 205 HOH HOH A . 
H 5 HOH 230 730 250 HOH HOH A . 
H 5 HOH 231 731 243 HOH HOH A . 
H 5 HOH 232 732 203 HOH HOH A . 
H 5 HOH 233 733 202 HOH HOH A . 
H 5 HOH 234 734 123 HOH HOH A . 
H 5 HOH 235 735 78  HOH HOH A . 
H 5 HOH 236 736 163 HOH HOH A . 
H 5 HOH 237 737 189 HOH HOH A . 
H 5 HOH 238 738 224 HOH HOH A . 
H 5 HOH 239 739 128 HOH HOH A . 
H 5 HOH 240 740 53  HOH HOH A . 
H 5 HOH 241 741 87  HOH HOH A . 
H 5 HOH 242 742 169 HOH HOH A . 
H 5 HOH 243 743 140 HOH HOH A . 
H 5 HOH 244 744 141 HOH HOH A . 
H 5 HOH 245 745 173 HOH HOH A . 
H 5 HOH 246 746 216 HOH HOH A . 
H 5 HOH 247 747 73  HOH HOH A . 
H 5 HOH 248 748 182 HOH HOH A . 
H 5 HOH 249 749 262 HOH HOH A . 
H 5 HOH 250 750 179 HOH HOH A . 
H 5 HOH 251 751 235 HOH HOH A . 
H 5 HOH 252 752 150 HOH HOH A . 
H 5 HOH 253 753 240 HOH HOH A . 
H 5 HOH 254 754 253 HOH HOH A . 
H 5 HOH 255 755 121 HOH HOH A . 
H 5 HOH 256 756 164 HOH HOH A . 
H 5 HOH 257 757 267 HOH HOH A . 
H 5 HOH 258 758 124 HOH HOH A . 
H 5 HOH 259 759 94  HOH HOH A . 
H 5 HOH 260 760 177 HOH HOH A . 
H 5 HOH 261 761 144 HOH HOH A . 
H 5 HOH 262 762 277 HOH HOH A . 
H 5 HOH 263 763 71  HOH HOH A . 
H 5 HOH 264 764 92  HOH HOH A . 
H 5 HOH 265 765 272 HOH HOH A . 
H 5 HOH 266 766 249 HOH HOH A . 
H 5 HOH 267 767 213 HOH HOH A . 
H 5 HOH 268 768 176 HOH HOH A . 
H 5 HOH 269 769 275 HOH HOH A . 
H 5 HOH 270 770 204 HOH HOH A . 
H 5 HOH 271 771 211 HOH HOH A . 
H 5 HOH 272 772 247 HOH HOH A . 
H 5 HOH 273 773 102 HOH HOH A . 
H 5 HOH 274 774 269 HOH HOH A . 
H 5 HOH 275 775 219 HOH HOH A . 
H 5 HOH 276 776 255 HOH HOH A . 
H 5 HOH 277 777 135 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 100 ? CD  ? A LYS 100 CD  
2  1 Y 1 A LYS 100 ? CE  ? A LYS 100 CE  
3  1 Y 1 A LYS 100 ? NZ  ? A LYS 100 NZ  
4  1 Y 1 A TYR 154 ? CG  ? A TYR 154 CG  
5  1 Y 1 A TYR 154 ? CD1 ? A TYR 154 CD1 
6  1 Y 1 A TYR 154 ? CD2 ? A TYR 154 CD2 
7  1 Y 1 A TYR 154 ? CE1 ? A TYR 154 CE1 
8  1 Y 1 A TYR 154 ? CE2 ? A TYR 154 CE2 
9  1 Y 1 A TYR 154 ? CZ  ? A TYR 154 CZ  
10 1 Y 1 A TYR 154 ? OH  ? A TYR 154 OH  
11 1 Y 1 A ARG 217 ? NE  ? A ARG 217 NE  
12 1 Y 1 A ARG 217 ? CZ  ? A ARG 217 CZ  
13 1 Y 1 A ARG 217 ? NH1 ? A ARG 217 NH1 
14 1 Y 1 A ARG 217 ? NH2 ? A ARG 217 NH2 
15 1 Y 1 A ARG 298 ? CD  ? A ARG 298 CD  
16 1 Y 1 A ARG 298 ? NE  ? A ARG 298 NE  
17 1 Y 1 A ARG 298 ? CZ  ? A ARG 298 CZ  
18 1 Y 1 A ARG 298 ? NH1 ? A ARG 298 NH1 
19 1 Y 1 A ARG 298 ? NH2 ? A ARG 298 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.15 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CDK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     114.887 
_cell.length_a_esd                 ? 
_cell.length_b                     53.558 
_cell.length_b_esd                 ? 
_cell.length_c                     44.551 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CDK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CDK 
_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             1.98 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.84 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              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    
'1% w/v Tryptone, 0.001 M Sodium azide, 0.05 M HEPES sodium pH 7.0, 20% w/v Polyethylene glycol 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            290 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-14 
_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                    'double crystal Si(111)' 
_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   0.92010 
_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                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.92010 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CDK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.61 
_reflns.d_resolution_low                               31.03 
_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                                     34342 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.92 
_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                                0.140 
_reflns.pdbx_Rpim_I_all                                0.053 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       238600 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.129 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.61 
_reflns_shell.d_res_low                                     1.70 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           34981 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5019 
_reflns_shell.percent_possible_obs                          100.0 
_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                               7.0 
_reflns_shell.pdbx_chi_squared                              0.80 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.9 
_reflns_shell.pdbx_Rrim_I_all                               2.083 
_reflns_shell.pdbx_Rpim_I_all                               0.782 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.454 
_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                                  1.928 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CDK 
_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                            1.61 
_refine.ls_d_res_low                             31.03 
_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                     34328 
_refine.ls_number_reflns_R_free                  1660 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 4.84 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1852 
_refine.ls_R_factor_R_free                       0.2236 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1833 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.58 
_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                            0.18 
_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                       1.61 
_refine_hist.d_res_low                        31.03 
_refine_hist.number_atoms_solvent             277 
_refine_hist.number_atoms_total               2674 
_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        2341 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_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' ? 0.006  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.900  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.852 ? 353 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 378 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 445 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.61 1.66  . . 129 2750 100.00 . . . . 0.3147 . . . . . . . . . . . 0.3195 
'X-RAY DIFFRACTION' 1.66 1.71  . . 131 2690 100.00 . . . . 0.2887 . . . . . . . . . . . 0.3551 
'X-RAY DIFFRACTION' 1.71 1.77  . . 128 2704 100.00 . . . . 0.2555 . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 1.77 1.84  . . 129 2719 100.00 . . . . 0.2359 . . . . . . . . . . . 0.2745 
'X-RAY DIFFRACTION' 1.84 1.93  . . 141 2718 100.00 . . . . 0.2220 . . . . . . . . . . . 0.2657 
'X-RAY DIFFRACTION' 1.93 2.03  . . 138 2704 100.00 . . . . 0.1965 . . . . . . . . . . . 0.2361 
'X-RAY DIFFRACTION' 2.03 2.15  . . 160 2672 100.00 . . . . 0.1901 . . . . . . . . . . . 0.2303 
'X-RAY DIFFRACTION' 2.15 2.32  . . 145 2733 100.00 . . . . 0.1786 . . . . . . . . . . . 0.2115 
'X-RAY DIFFRACTION' 2.32 2.55  . . 155 2700 100.00 . . . . 0.1841 . . . . . . . . . . . 0.2321 
'X-RAY DIFFRACTION' 2.55 2.92  . . 143 2717 100.00 . . . . 0.1846 . . . . . . . . . . . 0.2193 
'X-RAY DIFFRACTION' 2.92 3.68  . . 141 2750 100.00 . . . . 0.1668 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 3.68 31.03 . . 120 2811 100.00 . . . . 0.1552 . . . . . . . . . . . 0.1821 
# 
_struct.entry_id                     9CDK 
_struct.title                        'SARS-CoV-2 Mpro A173V mutant in complex with small molecule inhibitor Mpro61' 
_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        9CDK 
_struct_keywords.text            'SARS-CoV-2, Mpro, 3CL, main protease, inhibitor, small molecule, Mpro61, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CDK 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 306 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3569 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       306 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9CDK 
_struct_ref_seq_dif.mon_id                       VAL 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      173 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P0DTD1 
_struct_ref_seq_dif.db_mon_id                    ALA 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          3436 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            173 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5110  ? 
1 MORE         -25   ? 
1 'SSA (A^2)'  24480 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_555 -x,y,-z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 47  ? ASN A 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 LYS A 61  ? HIS A 64  ? LYS A 61  HIS A 64  5 ? 4  
HELX_P HELX_P6  AA6 ILE A 200 ? GLY A 215 ? ILE A 200 GLY A 215 1 ? 16 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O VAL A 173 ? O VAL A 173 
# 
_pdbx_entry_details.entry_id                   9CDK 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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   A HOH 738 ? ? O A HOH 771 ? ? 2.00 
2 1 O   A HOH 766 ? ? O A HOH 774 ? ? 2.03 
3 1 O   A HOH 667 ? ? O A HOH 710 ? ? 2.09 
4 1 O   A HOH 544 ? ? O A HOH 712 ? ? 2.10 
5 1 OD1 A ASN 51  ? ? O A HOH 501 ? ? 2.14 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 521 ? ? 1_555 O A HOH 531 ? ? 2_554 1.92 
2 1 O A HOH 622 ? ? 1_555 O A HOH 733 ? ? 4_556 2.01 
3 1 O A HOH 572 ? ? 1_555 O A HOH 611 ? ? 4_556 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  ? ? 53.80   -131.81 
2 1 ASN A 51  ? ? -159.89 62.86   
3 1 ASN A 84  ? ? 51.76   -123.48 
4 1 MET A 130 ? ? -56.82  109.42  
5 1 TYR A 154 ? ? 58.63   -107.72 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 679 ? H HOH . 
2 1 A HOH 767 ? H HOH . 
3 1 A HOH 770 ? H HOH . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 7.6779  -10.6020 9.9200   0.1673 ? 0.0060  ? 0.0078  ? 0.1527 ? -0.0096 ? 0.1776 ? 1.4125 ? 0.0693 
? 0.0709  ? 1.0144 ? -0.6135 ? 1.0700 ? -0.0665 ? -0.0104 ? -0.0383 ? -0.0843 ? 0.0311  ? 0.0240  ? 0.1474  ? -0.0041 ? 0.0495  ? 
2 'X-RAY DIFFRACTION' ? refined 15.1317 -12.7740 27.5334  0.3142 ? -0.0044 ? 0.0174  ? 0.3384 ? 0.0066  ? 0.2537 ? 1.9934 ? 1.2937 
? 0.4815  ? 2.1689 ? -0.2912 ? 1.4813 ? 0.1627  ? -0.3642 ? 0.2450  ? 0.3407  ? -0.2347 ? -0.0157 ? -0.1765 ? -0.2612 ? 0.0965  ? 
3 'X-RAY DIFFRACTION' ? refined 12.7628 -14.1889 10.6191  0.2045 ? 0.0279  ? 0.0293  ? 0.2028 ? 0.0031  ? 0.1860 ? 0.5593 ? 
-0.0260 ? 0.4304  ? 2.0592 ? -0.7330 ? 0.6793 ? -0.0394 ? 0.0110  ? -0.0928 ? -0.2661 ? -0.0033 ? -0.1118 ? 0.1368  ? 0.0140  ? 
0.0249  ? 
4 'X-RAY DIFFRACTION' ? refined 12.4041 2.3191   7.8942   0.1836 ? -0.0065 ? -0.0045 ? 0.1831 ? -0.0051 ? 0.1874 ? 0.4604 ? 
-0.0374 ? 0.0677  ? 1.0916 ? -1.1287 ? 1.1661 ? -0.0277 ? -0.0365 ? -0.0195 ? -0.0087 ? -0.0150 ? 0.0014  ? 0.0375  ? -0.0176 ? 
0.0442  ? 
5 'X-RAY DIFFRACTION' ? refined 14.9230 22.9148  -10.9533 0.2585 ? -0.0238 ? 0.0074  ? 0.2537 ? 0.0020  ? 0.2421 ? 2.3163 ? 0.5895 
? -0.3926 ? 1.4414 ? -0.0655 ? 1.5849 ? 0.0045  ? 0.0046  ? 0.0892  ? -0.1264 ? 0.0415  ? -0.2105 ? -0.2186 ? 0.0399  ? 0.0004  ? 
6 'X-RAY DIFFRACTION' ? refined 11.9203 13.8725  -9.2856  0.1540 ? -0.0256 ? 0.0025  ? 0.1970 ? 0.0046  ? 0.1553 ? 1.9177 ? 0.0207 
? -0.0489 ? 1.1392 ? 0.3129  ? 2.6267 ? 0.0600  ? 0.0587  ? -0.0496 ? -0.0071 ? -0.0024 ? 0.0061  ? 0.0555  ? -0.0689 ? -0.0532 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 43 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 44 through 70 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 71 through 120 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 121 through 213 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 214 through 236 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 237 through 305 )
;
# 
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 776 ? 6.13 . 
2 1 O ? A HOH 777 ? 6.39 . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     GLN 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      306 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    GLN 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     306 
# 
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  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
DMS S    S  N N 89  
DMS O    O  N N 90  
DMS C1   C  N N 91  
DMS C2   C  N N 92  
DMS H11  H  N N 93  
DMS H12  H  N N 94  
DMS H13  H  N N 95  
DMS H21  H  N N 96  
DMS H22  H  N N 97  
DMS H23  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
VAL N    N  N N 383 
VAL CA   C  N S 384 
VAL C    C  N N 385 
VAL O    O  N N 386 
VAL CB   C  N N 387 
VAL CG1  C  N N 388 
VAL CG2  C  N N 389 
VAL OXT  O  N N 390 
VAL H    H  N N 391 
VAL H2   H  N N 392 
VAL HA   H  N N 393 
VAL HB   H  N N 394 
VAL HG11 H  N N 395 
VAL HG12 H  N N 396 
VAL HG13 H  N N 397 
VAL HG21 H  N N 398 
VAL HG22 H  N N 399 
VAL HG23 H  N N 400 
VAL HXT  H  N N 401 
XEK C1   C  N N 402 
XEK C2   C  N N 403 
XEK C3   C  Y N 404 
XEK C4   C  Y N 405 
XEK C5   C  Y N 406 
XEK C6   C  Y N 407 
XEK C7   C  Y N 408 
XEK C8   C  N N 409 
XEK C9   C  Y N 410 
XEK C10  C  Y N 411 
XEK C11  C  Y N 412 
XEK C12  C  Y N 413 
XEK C13  C  Y N 414 
XEK C14  C  Y N 415 
XEK C15  C  Y N 416 
XEK C17  C  N N 417 
XEK C21  C  N N 418 
XEK C22  C  N N 419 
XEK C24  C  Y N 420 
XEK C25  C  Y N 421 
XEK C27  C  Y N 422 
XEK C16  C  N N 423 
XEK C18  C  N N 424 
XEK C19  C  N N 425 
XEK C20  C  N N 426 
XEK C23  C  N N 427 
XEK C26  C  Y N 428 
XEK C28  C  Y N 429 
XEK F1   F  N N 430 
XEK N1   N  N N 431 
XEK N2   N  N N 432 
XEK N3   N  N N 433 
XEK N4   N  Y N 434 
XEK O1   O  N N 435 
XEK O2   O  N N 436 
XEK O3   O  N N 437 
XEK O4   O  N N 438 
XEK CL1  CL N N 439 
XEK CL2  CL N N 440 
XEK H1   H  N N 441 
XEK H2   H  N N 442 
XEK H3   H  N N 443 
XEK H4   H  N N 444 
XEK H5   H  N N 445 
XEK H6   H  N N 446 
XEK H7   H  N N 447 
XEK H8   H  N N 448 
XEK H13  H  N N 449 
XEK H14  H  N N 450 
XEK H12  H  N N 451 
XEK H16  H  N N 452 
XEK H18  H  N N 453 
XEK H9   H  N N 454 
XEK H11  H  N N 455 
XEK H15  H  N N 456 
XEK H17  H  N N 457 
XEK H19  H  N N 458 
XEK H10  H  N N 459 
# 
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  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
XEK O1  C1   doub N N 385 
XEK C1  C2   sing N N 386 
XEK C1  N3   sing N N 387 
XEK C2  C3   sing N N 388 
XEK C2  C16  doub N N 389 
XEK C3  C4   doub Y N 390 
XEK C3  C15  sing Y N 391 
XEK C4  C5   sing Y N 392 
XEK C5  CL1  sing N N 393 
XEK C5  C6   doub Y N 394 
XEK C6  F1   sing N N 395 
XEK C6  C7   sing Y N 396 
XEK C7  O2   sing N N 397 
XEK C7  C15  doub Y N 398 
XEK O2  C8   sing N N 399 
XEK C8  C9   sing N N 400 
XEK C9  C10  doub Y N 401 
XEK C9  C14  sing Y N 402 
XEK C10 C11  sing Y N 403 
XEK C11 C12  doub Y N 404 
XEK C12 C13  sing Y N 405 
XEK C13 C14  doub Y N 406 
XEK C14 CL2  sing N N 407 
XEK C16 C17  sing N N 408 
XEK C17 C18  sing N N 409 
XEK C17 C23  doub N N 410 
XEK C18 C19  sing N N 411 
XEK C18 C20  doub N N 412 
XEK C19 N1   sing N N 413 
XEK C19 O3   doub N N 414 
XEK N1  C22  sing N N 415 
XEK C20 N2   sing N N 416 
XEK N2  C21  sing N N 417 
XEK N2  C22  sing N N 418 
XEK C22 O4   doub N N 419 
XEK C23 N3   sing N N 420 
XEK N3  C24  sing N N 421 
XEK C24 C25  doub Y N 422 
XEK C24 C28  sing Y N 423 
XEK C25 C26  sing Y N 424 
XEK C26 C27  doub Y N 425 
XEK C27 N4   sing Y N 426 
XEK N4  C28  doub Y N 427 
XEK C4  H1   sing N N 428 
XEK C8  H2   sing N N 429 
XEK C8  H3   sing N N 430 
XEK C10 H4   sing N N 431 
XEK C11 H5   sing N N 432 
XEK C12 H6   sing N N 433 
XEK C13 H7   sing N N 434 
XEK C15 H8   sing N N 435 
XEK C21 H13  sing N N 436 
XEK C21 H14  sing N N 437 
XEK C21 H12  sing N N 438 
XEK C25 H16  sing N N 439 
XEK C27 H18  sing N N 440 
XEK C16 H9   sing N N 441 
XEK C20 H11  sing N N 442 
XEK C23 H15  sing N N 443 
XEK C26 H17  sing N N 444 
XEK C28 H19  sing N N 445 
XEK N1  H10  sing N N 446 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1U19AI171443 
_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   6y2f 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CDK 
_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]   0.008704 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002034 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018671 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.023051 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 1   ? -2.478 4.886   -16.719 1.00 29.72 ? 1   SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? -2.064 6.090   -16.016 1.00 28.52 ? 1   SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? -2.477 6.076   -14.551 1.00 31.52 ? 1   SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? -2.978 5.077   -14.033 1.00 33.47 ? 1   SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? -2.645 7.335   -16.682 1.00 37.82 ? 1   SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? -4.002 7.144   -17.015 1.00 50.12 ? 1   SER A OG  1 
ATOM   7    N  N   . GLY A 1 2   ? -2.263 7.205   -13.898 1.00 33.67 ? 2   GLY A N   1 
ATOM   8    C  CA  . GLY A 1 2   ? -2.348 7.271   -12.450 1.00 25.61 ? 2   GLY A CA  1 
ATOM   9    C  C   . GLY A 1 2   ? -1.031 6.919   -11.789 1.00 32.55 ? 2   GLY A C   1 
ATOM   10   O  O   . GLY A 1 2   ? -0.210 6.167   -12.313 1.00 30.81 ? 2   GLY A O   1 
ATOM   11   N  N   . PHE A 1 3   ? -0.823 7.471   -10.600 1.00 32.55 ? 3   PHE A N   1 
ATOM   12   C  CA  . PHE A 1 3   ? 0.402  7.201   -9.861  1.00 30.76 ? 3   PHE A CA  1 
ATOM   13   C  C   . PHE A 1 3   ? 0.075  7.135   -8.381  1.00 27.28 ? 3   PHE A C   1 
ATOM   14   O  O   . PHE A 1 3   ? -0.475 8.084   -7.813  1.00 33.97 ? 3   PHE A O   1 
ATOM   15   C  CB  . PHE A 1 3   ? 1.483  8.247   -10.137 1.00 27.41 ? 3   PHE A CB  1 
ATOM   16   C  CG  . PHE A 1 3   ? 2.885  7.731   -9.900  1.00 32.00 ? 3   PHE A CG  1 
ATOM   17   C  CD1 . PHE A 1 3   ? 3.480  6.849   -10.793 1.00 29.86 ? 3   PHE A CD1 1 
ATOM   18   C  CD2 . PHE A 1 3   ? 3.584  8.094   -8.756  1.00 34.36 ? 3   PHE A CD2 1 
ATOM   19   C  CE1 . PHE A 1 3   ? 4.757  6.360   -10.568 1.00 32.91 ? 3   PHE A CE1 1 
ATOM   20   C  CE2 . PHE A 1 3   ? 4.862  7.607   -8.513  1.00 24.93 ? 3   PHE A CE2 1 
ATOM   21   C  CZ  . PHE A 1 3   ? 5.450  6.738   -9.421  1.00 30.68 ? 3   PHE A CZ  1 
ATOM   22   N  N   . ARG A 1 4   ? 0.417  6.010   -7.772  1.00 25.82 ? 4   ARG A N   1 
ATOM   23   C  CA  . ARG A 1 4   ? -0.018 5.662   -6.434  1.00 24.59 ? 4   ARG A CA  1 
ATOM   24   C  C   . ARG A 1 4   ? 1.192  5.229   -5.633  1.00 22.84 ? 4   ARG A C   1 
ATOM   25   O  O   . ARG A 1 4   ? 2.136  4.662   -6.185  1.00 25.26 ? 4   ARG A O   1 
ATOM   26   C  CB  . ARG A 1 4   ? -1.036 4.524   -6.486  1.00 23.83 ? 4   ARG A CB  1 
ATOM   27   C  CG  . ARG A 1 4   ? -2.475 4.967   -6.782  1.00 24.82 ? 4   ARG A CG  1 
ATOM   28   C  CD  . ARG A 1 4   ? -3.115 5.525   -5.519  1.00 32.72 ? 4   ARG A CD  1 
ATOM   29   N  NE  . ARG A 1 4   ? -4.499 5.927   -5.733  1.00 40.41 ? 4   ARG A NE  1 
ATOM   30   C  CZ  . ARG A 1 4   ? -5.213 6.632   -4.867  1.00 36.93 ? 4   ARG A CZ  1 
ATOM   31   N  NH1 . ARG A 1 4   ? -4.712 6.996   -3.697  1.00 40.35 ? 4   ARG A NH1 1 
ATOM   32   N  NH2 . ARG A 1 4   ? -6.457 6.988   -5.186  1.00 31.55 ? 4   ARG A NH2 1 
ATOM   33   N  N   . LYS A 1 5   ? 1.158  5.488   -4.326  1.00 21.24 ? 5   LYS A N   1 
ATOM   34   C  CA  . LYS A 1 5   ? 2.114  4.837   -3.443  1.00 22.77 ? 5   LYS A CA  1 
ATOM   35   C  C   . LYS A 1 5   ? 1.757  3.361   -3.393  1.00 25.98 ? 5   LYS A C   1 
ATOM   36   O  O   . LYS A 1 5   ? 0.698  2.984   -2.884  1.00 40.20 ? 5   LYS A O   1 
ATOM   37   C  CB  . LYS A 1 5   ? 2.109  5.468   -2.056  1.00 31.17 ? 5   LYS A CB  1 
ATOM   38   C  CG  . LYS A 1 5   ? 3.503  5.554   -1.456  1.00 33.13 ? 5   LYS A CG  1 
ATOM   39   C  CD  . LYS A 1 5   ? 3.493  6.308   -0.148  1.00 53.30 ? 5   LYS A CD  1 
ATOM   40   C  CE  . LYS A 1 5   ? 3.905  7.745   -0.372  1.00 50.17 ? 5   LYS A CE  1 
ATOM   41   N  NZ  . LYS A 1 5   ? 5.370  7.823   -0.546  1.00 38.60 ? 5   LYS A NZ  1 
ATOM   42   N  N   . MET A 1 6   ? 2.613  2.531   -3.962  1.00 24.14 ? 6   MET A N   1 
ATOM   43   C  CA  . MET A 1 6   ? 2.293  1.139   -4.227  1.00 24.17 ? 6   MET A CA  1 
ATOM   44   C  C   . MET A 1 6   ? 3.294  0.258   -3.506  1.00 22.78 ? 6   MET A C   1 
ATOM   45   O  O   . MET A 1 6   ? 4.507  0.454   -3.627  1.00 25.27 ? 6   MET A O   1 
ATOM   46   C  CB  . MET A 1 6   ? 2.347  0.837   -5.725  1.00 24.37 ? 6   MET A CB  1 
ATOM   47   C  CG  . MET A 1 6   ? 1.312  -0.165  -6.191  1.00 41.20 ? 6   MET A CG  1 
ATOM   48   S  SD  . MET A 1 6   ? 1.175  -0.012  -7.969  1.00 47.22 ? 6   MET A SD  1 
ATOM   49   C  CE  . MET A 1 6   ? 2.873  -0.407  -8.279  1.00 23.92 ? 6   MET A CE  1 
ATOM   50   N  N   . ALA A 1 7   ? 2.778  -0.697  -2.753  1.00 22.22 ? 7   ALA A N   1 
ATOM   51   C  CA  . ALA A 1 7   ? 3.588  -1.678  -2.053  1.00 21.46 ? 7   ALA A CA  1 
ATOM   52   C  C   . ALA A 1 7   ? 3.690  -2.943  -2.890  1.00 29.69 ? 7   ALA A C   1 
ATOM   53   O  O   . ALA A 1 7   ? 2.838  -3.218  -3.737  1.00 24.65 ? 7   ALA A O   1 
ATOM   54   C  CB  . ALA A 1 7   ? 2.981  -2.003  -0.693  1.00 19.10 ? 7   ALA A CB  1 
ATOM   55   N  N   . PHE A 1 8   ? 4.752  -3.708  -2.655  1.00 23.16 ? 8   PHE A N   1 
ATOM   56   C  CA  . PHE A 1 8   ? 4.825  -5.022  -3.276  1.00 24.59 ? 8   PHE A CA  1 
ATOM   57   C  C   . PHE A 1 8   ? 3.710  -5.915  -2.736  1.00 26.06 ? 8   PHE A C   1 
ATOM   58   O  O   . PHE A 1 8   ? 3.262  -5.744  -1.599  1.00 24.98 ? 8   PHE A O   1 
ATOM   59   C  CB  . PHE A 1 8   ? 6.172  -5.683  -3.001  1.00 24.34 ? 8   PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 8   ? 7.315  -5.008  -3.670  1.00 30.16 ? 8   PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 8   ? 7.575  -5.224  -5.016  1.00 32.56 ? 8   PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 8   ? 8.117  -4.128  -2.969  1.00 32.28 ? 8   PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 8   ? 8.633  -4.590  -5.637  1.00 28.27 ? 8   PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 8   ? 9.171  -3.490  -3.588  1.00 28.49 ? 8   PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 8   ? 9.429  -3.722  -4.925  1.00 33.16 ? 8   PHE A CZ  1 
ATOM   66   N  N   . PRO A 1 9   ? 3.255  -6.884  -3.528  1.00 26.25 ? 9   PRO A N   1 
ATOM   67   C  CA  . PRO A 1 9   ? 2.298  -7.866  -3.005  1.00 27.56 ? 9   PRO A CA  1 
ATOM   68   C  C   . PRO A 1 9   ? 2.938  -8.601  -1.839  1.00 23.10 ? 9   PRO A C   1 
ATOM   69   O  O   . PRO A 1 9   ? 4.089  -9.032  -1.922  1.00 30.52 ? 9   PRO A O   1 
ATOM   70   C  CB  . PRO A 1 9   ? 2.039  -8.792  -4.201  1.00 21.51 ? 9   PRO A CB  1 
ATOM   71   C  CG  . PRO A 1 9   ? 2.478  -8.010  -5.415  1.00 29.56 ? 9   PRO A CG  1 
ATOM   72   C  CD  . PRO A 1 9   ? 3.600  -7.124  -4.940  1.00 28.47 ? 9   PRO A CD  1 
ATOM   73   N  N   . SER A 1 10  ? 2.189  -8.731  -0.743  1.00 25.83 ? 10  SER A N   1 
ATOM   74   C  CA  . SER A 1 10  ? 2.778  -9.150  0.525   1.00 24.79 ? 10  SER A CA  1 
ATOM   75   C  C   . SER A 1 10  ? 2.681  -10.644 0.790   1.00 24.27 ? 10  SER A C   1 
ATOM   76   O  O   . SER A 1 10  ? 3.287  -11.118 1.760   1.00 23.73 ? 10  SER A O   1 
ATOM   77   C  CB  . SER A 1 10  ? 2.125  -8.403  1.696   1.00 25.71 ? 10  SER A CB  1 
ATOM   78   O  OG  . SER A 1 10  ? 0.709  -8.543  1.724   1.00 27.63 ? 10  SER A OG  1 
ATOM   79   N  N   . GLY A 1 11  ? 1.965  -11.396 -0.049  1.00 29.49 ? 11  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 11  ? 1.668  -12.784 0.275   1.00 33.17 ? 11  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 11  ? 2.897  -13.611 0.610   1.00 24.43 ? 11  GLY A C   1 
ATOM   82   O  O   . GLY A 1 11  ? 2.857  -14.466 1.497   1.00 26.87 ? 11  GLY A O   1 
ATOM   83   N  N   . LYS A 1 12  ? 3.994  -13.390 -0.112  1.00 24.49 ? 12  LYS A N   1 
ATOM   84   C  CA  . LYS A 1 12  ? 5.180  -14.214 0.099   1.00 24.18 ? 12  LYS A CA  1 
ATOM   85   C  C   . LYS A 1 12  ? 5.755  -13.979 1.496   1.00 25.05 ? 12  LYS A C   1 
ATOM   86   O  O   . LYS A 1 12  ? 6.385  -14.873 2.076   1.00 21.96 ? 12  LYS A O   1 
ATOM   87   C  CB  . LYS A 1 12  ? 6.202  -13.907 -0.990  1.00 24.97 ? 12  LYS A CB  1 
ATOM   88   C  CG  . LYS A 1 12  ? 6.074  -14.826 -2.179  1.00 30.02 ? 12  LYS A CG  1 
ATOM   89   C  CD  . LYS A 1 12  ? 6.769  -14.258 -3.400  1.00 36.70 ? 12  LYS A CD  1 
ATOM   90   C  CE  . LYS A 1 12  ? 6.991  -15.346 -4.449  1.00 45.84 ? 12  LYS A CE  1 
ATOM   91   N  NZ  . LYS A 1 12  ? 8.029  -14.977 -5.438  1.00 47.15 ? 12  LYS A NZ  1 
ATOM   92   N  N   . VAL A 1 13  ? 5.519  -12.801 2.059   1.00 24.44 ? 13  VAL A N   1 
ATOM   93   C  CA  . VAL A 1 13  ? 5.976  -12.520 3.415   1.00 20.99 ? 13  VAL A CA  1 
ATOM   94   C  C   . VAL A 1 13  ? 4.932  -12.917 4.463   1.00 26.42 ? 13  VAL A C   1 
ATOM   95   O  O   . VAL A 1 13  ? 5.289  -13.329 5.572   1.00 22.76 ? 13  VAL A O   1 
ATOM   96   C  CB  . VAL A 1 13  ? 6.360  -11.035 3.518   1.00 22.72 ? 13  VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 13  ? 6.857  -10.690 4.921   1.00 28.11 ? 13  VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 13  ? 7.405  -10.718 2.473   1.00 24.28 ? 13  VAL A CG2 1 
ATOM   99   N  N   . GLU A 1 14  ? 3.642  -12.823 4.131   1.00 24.27 ? 14  GLU A N   1 
ATOM   100  C  CA  . GLU A 1 14  ? 2.608  -13.265 5.057   1.00 21.38 ? 14  GLU A CA  1 
ATOM   101  C  C   . GLU A 1 14  ? 2.851  -14.696 5.503   1.00 18.14 ? 14  GLU A C   1 
ATOM   102  O  O   . GLU A 1 14  ? 2.646  -15.033 6.676   1.00 23.27 ? 14  GLU A O   1 
ATOM   103  C  CB  . GLU A 1 14  ? 1.242  -13.140 4.387   1.00 22.20 ? 14  GLU A CB  1 
ATOM   104  C  CG  . GLU A 1 14  ? 0.799  -11.700 4.129   1.00 21.59 ? 14  GLU A CG  1 
ATOM   105  C  CD  . GLU A 1 14  ? -0.419 -11.649 3.203   1.00 25.67 ? 14  GLU A CD  1 
ATOM   106  O  OE1 . GLU A 1 14  ? -1.379 -12.408 3.417   1.00 32.47 ? 14  GLU A OE1 1 
ATOM   107  O  OE2 . GLU A 1 14  ? -0.396 -10.855 2.236   1.00 26.61 ? 14  GLU A OE2 1 
ATOM   108  N  N   . GLY A 1 15  ? 3.281  -15.560 4.581   1.00 23.32 ? 15  GLY A N   1 
ATOM   109  C  CA  . GLY A 1 15  ? 3.502  -16.963 4.898   1.00 21.26 ? 15  GLY A CA  1 
ATOM   110  C  C   . GLY A 1 15  ? 4.689  -17.234 5.792   1.00 24.07 ? 15  GLY A C   1 
ATOM   111  O  O   . GLY A 1 15  ? 4.912  -18.381 6.195   1.00 25.08 ? 15  GLY A O   1 
ATOM   112  N  N   . CYS A 1 16  ? 5.452  -16.203 6.121   1.00 21.26 ? 16  CYS A N   1 
ATOM   113  C  CA  . CYS A 1 16  ? 6.623  -16.334 6.973   1.00 17.37 ? 16  CYS A CA  1 
ATOM   114  C  C   . CYS A 1 16  ? 6.412  -15.765 8.366   1.00 21.19 ? 16  CYS A C   1 
ATOM   115  O  O   . CYS A 1 16  ? 7.314  -15.862 9.202   1.00 21.62 ? 16  CYS A O   1 
ATOM   116  C  CB  . CYS A 1 16  ? 7.813  -15.618 6.332   1.00 22.78 ? 16  CYS A CB  1 
ATOM   117  S  SG  . CYS A 1 16  ? 8.255  -16.224 4.684   1.00 24.57 ? 16  CYS A SG  1 
ATOM   118  N  N   . MET A 1 17  ? 5.275  -15.143 8.645   1.00 18.89 ? 17  MET A N   1 
ATOM   119  C  CA  . MET A 1 17  ? 5.144  -14.431 9.902   1.00 19.15 ? 17  MET A CA  1 
ATOM   120  C  C   . MET A 1 17  ? 4.672  -15.404 10.968  1.00 22.83 ? 17  MET A C   1 
ATOM   121  O  O   . MET A 1 17  ? 3.796  -16.237 10.720  1.00 22.26 ? 17  MET A O   1 
ATOM   122  C  CB  . MET A 1 17  ? 4.200  -13.241 9.766   1.00 21.81 ? 17  MET A CB  1 
ATOM   123  C  CG  . MET A 1 17  ? 4.720  -12.327 8.664   1.00 21.32 ? 17  MET A CG  1 
ATOM   124  S  SD  . MET A 1 17  ? 6.296  -11.566 9.003   1.00 21.83 ? 17  MET A SD  1 
ATOM   125  C  CE  . MET A 1 17  ? 6.157  -11.170 10.766  1.00 23.39 ? 17  MET A CE  1 
ATOM   126  N  N   . VAL A 1 18  ? 5.294  -15.327 12.146  1.00 20.69 ? 18  VAL A N   1 
ATOM   127  C  CA  . VAL A 1 18  ? 4.937  -16.160 13.291  1.00 18.10 ? 18  VAL A CA  1 
ATOM   128  C  C   . VAL A 1 18  ? 4.898  -15.273 14.526  1.00 21.20 ? 18  VAL A C   1 
ATOM   129  O  O   . VAL A 1 18  ? 5.341  -14.121 14.505  1.00 20.88 ? 18  VAL A O   1 
ATOM   130  C  CB  . VAL A 1 18  ? 5.922  -17.334 13.503  1.00 17.33 ? 18  VAL A CB  1 
ATOM   131  C  CG1 . VAL A 1 18  ? 6.005  -18.209 12.227  1.00 21.45 ? 18  VAL A CG1 1 
ATOM   132  C  CG2 . VAL A 1 18  ? 7.287  -16.812 13.903  1.00 19.86 ? 18  VAL A CG2 1 
ATOM   133  N  N   . GLN A 1 19  ? 4.353  -15.834 15.605  1.00 19.36 ? 19  GLN A N   1 
ATOM   134  C  CA  . GLN A 1 19  ? 4.315  -15.206 16.918  1.00 21.22 ? 19  GLN A CA  1 
ATOM   135  C  C   . GLN A 1 19  ? 5.439  -15.791 17.763  1.00 20.45 ? 19  GLN A C   1 
ATOM   136  O  O   . GLN A 1 19  ? 5.599  -17.012 17.827  1.00 24.93 ? 19  GLN A O   1 
ATOM   137  C  CB  . GLN A 1 19  ? 2.955  -15.441 17.585  1.00 27.72 ? 19  GLN A CB  1 
ATOM   138  C  CG  . GLN A 1 19  ? 2.732  -14.718 18.899  1.00 28.19 ? 19  GLN A CG  1 
ATOM   139  C  CD  . GLN A 1 19  ? 1.359  -15.029 19.494  1.00 38.82 ? 19  GLN A CD  1 
ATOM   140  O  OE1 . GLN A 1 19  ? 0.714  -14.165 20.086  1.00 49.06 ? 19  GLN A OE1 1 
ATOM   141  N  NE2 . GLN A 1 19  ? 0.916  -16.271 19.341  1.00 48.80 ? 19  GLN A NE2 1 
ATOM   142  N  N   . VAL A 1 20  ? 6.230  -14.933 18.398  1.00 18.52 ? 20  VAL A N   1 
ATOM   143  C  CA  . VAL A 1 20  ? 7.265  -15.398 19.313  1.00 21.38 ? 20  VAL A CA  1 
ATOM   144  C  C   . VAL A 1 20  ? 6.946  -14.874 20.704  1.00 21.22 ? 20  VAL A C   1 
ATOM   145  O  O   . VAL A 1 20  ? 6.701  -13.676 20.883  1.00 21.05 ? 20  VAL A O   1 
ATOM   146  C  CB  . VAL A 1 20  ? 8.679  -14.974 18.882  1.00 18.28 ? 20  VAL A CB  1 
ATOM   147  C  CG1 . VAL A 1 20  ? 9.691  -15.577 19.856  1.00 16.68 ? 20  VAL A CG1 1 
ATOM   148  C  CG2 . VAL A 1 20  ? 8.980  -15.445 17.466  1.00 22.68 ? 20  VAL A CG2 1 
ATOM   149  N  N   . THR A 1 21  ? 6.942  -15.781 21.676  1.00 23.77 ? 21  THR A N   1 
ATOM   150  C  CA  . THR A 1 21  ? 6.652  -15.467 23.067  1.00 22.32 ? 21  THR A CA  1 
ATOM   151  C  C   . THR A 1 21  ? 7.823  -15.897 23.934  1.00 26.68 ? 21  THR A C   1 
ATOM   152  O  O   . THR A 1 21  ? 8.285  -17.038 23.837  1.00 26.94 ? 21  THR A O   1 
ATOM   153  C  CB  . THR A 1 21  ? 5.362  -16.168 23.528  1.00 29.18 ? 21  THR A CB  1 
ATOM   154  O  OG1 . THR A 1 21  ? 4.247  -15.658 22.785  1.00 30.49 ? 21  THR A OG1 1 
ATOM   155  C  CG2 . THR A 1 21  ? 5.114  -15.959 25.010  1.00 32.94 ? 21  THR A CG2 1 
ATOM   156  N  N   . CYS A 1 22  ? 8.293  -14.983 24.782  1.00 26.23 ? 22  CYS A N   1 
ATOM   157  C  CA  . CYS A 1 22  ? 9.276  -15.279 25.824  1.00 31.91 ? 22  CYS A CA  1 
ATOM   158  C  C   . CYS A 1 22  ? 8.755  -14.754 27.153  1.00 32.63 ? 22  CYS A C   1 
ATOM   159  O  O   . CYS A 1 22  ? 8.641  -13.539 27.338  1.00 32.50 ? 22  CYS A O   1 
ATOM   160  C  CB  . CYS A 1 22  ? 10.634 -14.663 25.502  1.00 27.95 ? 22  CYS A CB  1 
ATOM   161  S  SG  . CYS A 1 22  ? 11.950 -15.405 26.470  1.00 36.77 ? 22  CYS A SG  1 
ATOM   162  N  N   . GLY A 1 23  ? 8.444  -15.660 28.070  1.00 36.98 ? 23  GLY A N   1 
ATOM   163  C  CA  . GLY A 1 23  ? 7.875  -15.232 29.335  1.00 32.60 ? 23  GLY A CA  1 
ATOM   164  C  C   . GLY A 1 23  ? 6.556  -14.531 29.081  1.00 27.67 ? 23  GLY A C   1 
ATOM   165  O  O   . GLY A 1 23  ? 5.632  -15.094 28.483  1.00 38.61 ? 23  GLY A O   1 
ATOM   166  N  N   . THR A 1 24  ? 6.467  -13.273 29.509  1.00 37.54 ? 24  THR A N   1 
ATOM   167  C  CA  . THR A 1 24  ? 5.260  -12.481 29.318  1.00 44.05 ? 24  THR A CA  1 
ATOM   168  C  C   . THR A 1 24  ? 5.239  -11.707 28.005  1.00 45.95 ? 24  THR A C   1 
ATOM   169  O  O   . THR A 1 24  ? 4.209  -11.114 27.674  1.00 38.93 ? 24  THR A O   1 
ATOM   170  C  CB  . THR A 1 24  ? 5.083  -11.503 30.490  1.00 48.37 ? 24  THR A CB  1 
ATOM   171  O  OG1 . THR A 1 24  ? 3.843  -10.796 30.349  1.00 58.83 ? 24  THR A OG1 1 
ATOM   172  C  CG2 . THR A 1 24  ? 6.227  -10.510 30.532  1.00 46.91 ? 24  THR A CG2 1 
ATOM   173  N  N   . THR A 1 25  ? 6.326  -11.705 27.239  1.00 40.19 ? 25  THR A N   1 
ATOM   174  C  CA  . THR A 1 25  ? 6.410  -10.873 26.046  1.00 38.99 ? 25  THR A CA  1 
ATOM   175  C  C   . THR A 1 25  ? 5.984  -11.658 24.807  1.00 27.55 ? 25  THR A C   1 
ATOM   176  O  O   . THR A 1 25  ? 6.284  -12.849 24.679  1.00 33.68 ? 25  THR A O   1 
ATOM   177  C  CB  . THR A 1 25  ? 7.836  -10.338 25.870  1.00 38.50 ? 25  THR A CB  1 
ATOM   178  O  OG1 . THR A 1 25  ? 8.208  -9.560  27.017  1.00 42.70 ? 25  THR A OG1 1 
ATOM   179  C  CG2 . THR A 1 25  ? 7.940  -9.475  24.619  1.00 38.64 ? 25  THR A CG2 1 
ATOM   180  N  N   . THR A 1 26  ? 5.266  -10.989 23.907  1.00 32.30 ? 26  THR A N   1 
ATOM   181  C  CA  . THR A 1 26  ? 4.887  -11.592 22.630  1.00 27.56 ? 26  THR A CA  1 
ATOM   182  C  C   . THR A 1 26  ? 5.076  -10.572 21.523  1.00 29.32 ? 26  THR A C   1 
ATOM   183  O  O   . THR A 1 26  ? 4.548  -9.460  21.598  1.00 35.53 ? 26  THR A O   1 
ATOM   184  C  CB  . THR A 1 26  ? 3.437  -12.093 22.663  1.00 39.66 ? 26  THR A CB  1 
ATOM   185  O  OG1 . THR A 1 26  ? 3.355  -13.211 23.555  1.00 35.50 ? 26  THR A OG1 1 
ATOM   186  C  CG2 . THR A 1 26  ? 2.974  -12.533 21.290  1.00 33.64 ? 26  THR A CG2 1 
ATOM   187  N  N   . LEU A 1 27  ? 5.832  -10.948 20.501  1.00 21.45 ? 27  LEU A N   1 
ATOM   188  C  CA  . LEU A 1 27  ? 5.989  -10.086 19.343  1.00 25.30 ? 27  LEU A CA  1 
ATOM   189  C  C   . LEU A 1 27  ? 6.088  -10.970 18.109  1.00 20.06 ? 27  LEU A C   1 
ATOM   190  O  O   . LEU A 1 27  ? 5.734  -12.154 18.147  1.00 20.55 ? 27  LEU A O   1 
ATOM   191  C  CB  . LEU A 1 27  ? 7.166  -9.124  19.561  1.00 24.72 ? 27  LEU A CB  1 
ATOM   192  C  CG  . LEU A 1 27  ? 8.454  -9.703  20.132  1.00 24.78 ? 27  LEU A CG  1 
ATOM   193  C  CD1 . LEU A 1 27  ? 8.994  -10.785 19.237  1.00 23.96 ? 27  LEU A CD1 1 
ATOM   194  C  CD2 . LEU A 1 27  ? 9.481  -8.606  20.327  1.00 24.28 ? 27  LEU A CD2 1 
ATOM   195  N  N   . ASN A 1 28  ? 6.517  -10.383 16.993  1.00 16.93 ? 28  ASN A N   1 
ATOM   196  C  CA  . ASN A 1 28  ? 6.505  -11.059 15.700  1.00 19.24 ? 28  ASN A CA  1 
ATOM   197  C  C   . ASN A 1 28  ? 7.872  -11.627 15.352  1.00 19.12 ? 28  ASN A C   1 
ATOM   198  O  O   . ASN A 1 28  ? 8.907  -11.043 15.669  1.00 21.20 ? 28  ASN A O   1 
ATOM   199  C  CB  . ASN A 1 28  ? 6.068  -10.116 14.572  1.00 20.70 ? 28  ASN A CB  1 
ATOM   200  C  CG  . ASN A 1 28  ? 4.740  -9.445  14.848  1.00 25.70 ? 28  ASN A CG  1 
ATOM   201  O  OD1 . ASN A 1 28  ? 3.684  -10.061 14.704  1.00 21.85 ? 28  ASN A OD1 1 
ATOM   202  N  ND2 . ASN A 1 28  ? 4.784  -8.170  15.244  1.00 20.62 ? 28  ASN A ND2 1 
ATOM   203  N  N   . GLY A 1 29  ? 7.859  -12.766 14.659  1.00 16.91 ? 29  GLY A N   1 
ATOM   204  C  CA  . GLY A 1 29  ? 9.074  -13.350 14.140  1.00 17.35 ? 29  GLY A CA  1 
ATOM   205  C  C   . GLY A 1 29  ? 8.919  -13.658 12.664  1.00 21.40 ? 29  GLY A C   1 
ATOM   206  O  O   . GLY A 1 29  ? 7.813  -13.693 12.125  1.00 19.89 ? 29  GLY A O   1 
ATOM   207  N  N   . LEU A 1 30  ? 10.063 -13.875 12.018  1.00 19.43 ? 30  LEU A N   1 
ATOM   208  C  CA  . LEU A 1 30  ? 10.178 -14.168 10.588  1.00 21.48 ? 30  LEU A CA  1 
ATOM   209  C  C   . LEU A 1 30  ? 10.769 -15.563 10.449  1.00 17.18 ? 30  LEU A C   1 
ATOM   210  O  O   . LEU A 1 30  ? 11.928 -15.789 10.817  1.00 18.81 ? 30  LEU A O   1 
ATOM   211  C  CB  . LEU A 1 30  ? 11.054 -13.135 9.886   1.00 17.80 ? 30  LEU A CB  1 
ATOM   212  C  CG  . LEU A 1 30  ? 11.074 -13.209 8.350   1.00 19.82 ? 30  LEU A CG  1 
ATOM   213  C  CD1 . LEU A 1 30  ? 9.725  -12.769 7.738   1.00 23.16 ? 30  LEU A CD1 1 
ATOM   214  C  CD2 . LEU A 1 30  ? 12.226 -12.405 7.792   1.00 20.59 ? 30  LEU A CD2 1 
ATOM   215  N  N   . TRP A 1 31  ? 9.963  -16.492 9.940   1.00 18.29 ? 31  TRP A N   1 
ATOM   216  C  CA  . TRP A 1 31  ? 10.300 -17.910 9.832   1.00 16.28 ? 31  TRP A CA  1 
ATOM   217  C  C   . TRP A 1 31  ? 10.715 -18.227 8.395   1.00 22.02 ? 31  TRP A C   1 
ATOM   218  O  O   . TRP A 1 31  ? 9.869  -18.288 7.492   1.00 21.46 ? 31  TRP A O   1 
ATOM   219  C  CB  . TRP A 1 31  ? 9.099  -18.749 10.259  1.00 17.52 ? 31  TRP A CB  1 
ATOM   220  C  CG  . TRP A 1 31  ? 9.261  -20.220 10.238  1.00 20.43 ? 31  TRP A CG  1 
ATOM   221  C  CD1 . TRP A 1 31  ? 10.419 -20.937 10.343  1.00 17.81 ? 31  TRP A CD1 1 
ATOM   222  C  CD2 . TRP A 1 31  ? 8.199  -21.178 10.149  1.00 18.90 ? 31  TRP A CD2 1 
ATOM   223  N  NE1 . TRP A 1 31  ? 10.141 -22.288 10.304  1.00 19.94 ? 31  TRP A NE1 1 
ATOM   224  C  CE2 . TRP A 1 31  ? 8.786  -22.461 10.189  1.00 22.44 ? 31  TRP A CE2 1 
ATOM   225  C  CE3 . TRP A 1 31  ? 6.806  -21.071 10.023  1.00 20.25 ? 31  TRP A CE3 1 
ATOM   226  C  CZ2 . TRP A 1 31  ? 8.029  -23.637 10.117  1.00 21.72 ? 31  TRP A CZ2 1 
ATOM   227  C  CZ3 . TRP A 1 31  ? 6.051  -22.235 9.947   1.00 22.05 ? 31  TRP A CZ3 1 
ATOM   228  C  CH2 . TRP A 1 31  ? 6.668  -23.506 9.994   1.00 23.44 ? 31  TRP A CH2 1 
ATOM   229  N  N   . LEU A 1 32  ? 12.014 -18.452 8.197   1.00 19.55 ? 32  LEU A N   1 
ATOM   230  C  CA  . LEU A 1 32  ? 12.602 -18.747 6.894   1.00 21.10 ? 32  LEU A CA  1 
ATOM   231  C  C   . LEU A 1 32  ? 13.449 -20.001 7.021   1.00 22.00 ? 32  LEU A C   1 
ATOM   232  O  O   . LEU A 1 32  ? 14.354 -20.051 7.862   1.00 23.56 ? 32  LEU A O   1 
ATOM   233  C  CB  . LEU A 1 32  ? 13.458 -17.575 6.399   1.00 22.06 ? 32  LEU A CB  1 
ATOM   234  C  CG  . LEU A 1 32  ? 12.757 -16.242 6.200   1.00 23.39 ? 32  LEU A CG  1 
ATOM   235  C  CD1 . LEU A 1 32  ? 13.820 -15.171 6.025   1.00 22.18 ? 32  LEU A CD1 1 
ATOM   236  C  CD2 . LEU A 1 32  ? 11.823 -16.266 4.988   1.00 20.99 ? 32  LEU A CD2 1 
ATOM   237  N  N   . ASP A 1 33  ? 13.169 -21.002 6.181   1.00 18.95 ? 33  ASP A N   1 
ATOM   238  C  CA  . ASP A 1 33  ? 13.789 -22.314 6.328   1.00 21.83 ? 33  ASP A CA  1 
ATOM   239  C  C   . ASP A 1 33  ? 13.522 -22.760 7.765   1.00 22.75 ? 33  ASP A C   1 
ATOM   240  O  O   . ASP A 1 33  ? 12.382 -22.646 8.233   1.00 23.24 ? 33  ASP A O   1 
ATOM   241  C  CB  . ASP A 1 33  ? 15.255 -22.239 5.945   1.00 23.96 ? 33  ASP A CB  1 
ATOM   242  C  CG  . ASP A 1 33  ? 15.465 -21.783 4.512   1.00 34.81 ? 33  ASP A CG  1 
ATOM   243  O  OD1 . ASP A 1 33  ? 14.657 -22.177 3.643   1.00 37.13 ? 33  ASP A OD1 1 
ATOM   244  O  OD2 . ASP A 1 33  ? 16.439 -21.030 4.267   1.00 37.74 ? 33  ASP A OD2 1 
ATOM   245  N  N   . ASP A 1 34  ? 14.528 -23.234 8.501   1.00 20.65 ? 34  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 34  ? 14.334 -23.715 9.863   1.00 19.43 ? 34  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 34  ? 14.818 -22.722 10.915  1.00 19.16 ? 34  ASP A C   1 
ATOM   248  O  O   . ASP A 1 34  ? 15.182 -23.130 12.024  1.00 23.40 ? 34  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 34  ? 15.040 -25.061 10.034  1.00 22.54 ? 34  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 34  ? 16.544 -24.974 9.813   1.00 26.44 ? 34  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 34  ? 17.040 -23.909 9.400   1.00 30.78 ? 34  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 34  ? 17.227 -25.996 10.027  1.00 29.66 ? 34  ASP A OD2 1 
ATOM   253  N  N   . VAL A 1 35  ? 14.809 -21.422 10.606  1.00 20.96 ? 35  VAL A N   1 
ATOM   254  C  CA  . VAL A 1 35  ? 15.201 -20.389 11.560  1.00 23.45 ? 35  VAL A CA  1 
ATOM   255  C  C   . VAL A 1 35  ? 14.094 -19.358 11.680  1.00 20.32 ? 35  VAL A C   1 
ATOM   256  O  O   . VAL A 1 35  ? 13.470 -18.983 10.680  1.00 21.47 ? 35  VAL A O   1 
ATOM   257  C  CB  . VAL A 1 35  ? 16.524 -19.706 11.162  1.00 23.04 ? 35  VAL A CB  1 
ATOM   258  C  CG1 . VAL A 1 35  ? 16.880 -18.633 12.199  1.00 23.84 ? 35  VAL A CG1 1 
ATOM   259  C  CG2 . VAL A 1 35  ? 17.624 -20.749 11.078  1.00 21.81 ? 35  VAL A CG2 1 
ATOM   260  N  N   . VAL A 1 36  ? 13.858 -18.895 12.911  1.00 18.21 ? 36  VAL A N   1 
ATOM   261  C  CA  . VAL A 1 36  ? 12.945 -17.791 13.197  1.00 16.21 ? 36  VAL A CA  1 
ATOM   262  C  C   . VAL A 1 36  ? 13.765 -16.604 13.694  1.00 19.54 ? 36  VAL A C   1 
ATOM   263  O  O   . VAL A 1 36  ? 14.558 -16.738 14.633  1.00 21.34 ? 36  VAL A O   1 
ATOM   264  C  CB  . VAL A 1 36  ? 11.875 -18.192 14.229  1.00 18.65 ? 36  VAL A CB  1 
ATOM   265  C  CG1 . VAL A 1 36  ? 11.012 -16.985 14.546  1.00 18.90 ? 36  VAL A CG1 1 
ATOM   266  C  CG2 . VAL A 1 36  ? 11.012 -19.336 13.658  1.00 23.69 ? 36  VAL A CG2 1 
ATOM   267  N  N   . TYR A 1 37  ? 13.569 -15.444 13.065  1.00 18.78 ? 37  TYR A N   1 
ATOM   268  C  CA  . TYR A 1 37  ? 14.271 -14.211 13.402  1.00 21.20 ? 37  TYR A CA  1 
ATOM   269  C  C   . TYR A 1 37  ? 13.329 -13.257 14.117  1.00 18.14 ? 37  TYR A C   1 
ATOM   270  O  O   . TYR A 1 37  ? 12.196 -13.051 13.675  1.00 20.35 ? 37  TYR A O   1 
ATOM   271  C  CB  . TYR A 1 37  ? 14.800 -13.515 12.145  1.00 18.49 ? 37  TYR A CB  1 
ATOM   272  C  CG  . TYR A 1 37  ? 15.679 -14.382 11.296  1.00 19.29 ? 37  TYR A CG  1 
ATOM   273  C  CD1 . TYR A 1 37  ? 15.126 -15.300 10.408  1.00 19.03 ? 37  TYR A CD1 1 
ATOM   274  C  CD2 . TYR A 1 37  ? 17.063 -14.296 11.379  1.00 20.87 ? 37  TYR A CD2 1 
ATOM   275  C  CE1 . TYR A 1 37  ? 15.930 -16.112 9.645   1.00 22.99 ? 37  TYR A CE1 1 
ATOM   276  C  CE2 . TYR A 1 37  ? 17.883 -15.096 10.591  1.00 23.49 ? 37  TYR A CE2 1 
ATOM   277  C  CZ  . TYR A 1 37  ? 17.311 -15.999 9.730   1.00 23.50 ? 37  TYR A CZ  1 
ATOM   278  O  OH  . TYR A 1 37  ? 18.115 -16.803 8.956   1.00 24.75 ? 37  TYR A OH  1 
ATOM   279  N  N   . CYS A 1 38  ? 13.805 -12.630 15.187  1.00 19.86 ? 38  CYS A N   1 
ATOM   280  C  CA  . CYS A 1 38  ? 12.967 -11.687 15.913  1.00 18.31 ? 38  CYS A CA  1 
ATOM   281  C  C   . CYS A 1 38  ? 13.862 -10.740 16.702  1.00 19.78 ? 38  CYS A C   1 
ATOM   282  O  O   . CYS A 1 38  ? 15.056 -11.013 16.877  1.00 17.75 ? 38  CYS A O   1 
ATOM   283  C  CB  . CYS A 1 38  ? 11.976 -12.427 16.827  1.00 16.24 ? 38  CYS A CB  1 
ATOM   284  S  SG  . CYS A 1 38  ? 12.674 -13.123 18.361  1.00 21.74 ? 38  CYS A SG  1 
ATOM   285  N  N   . PRO A 1 39  ? 13.326 -9.610  17.175  1.00 16.80 ? 39  PRO A N   1 
ATOM   286  C  CA  . PRO A 1 39  ? 14.164 -8.682  17.947  1.00 14.16 ? 39  PRO A CA  1 
ATOM   287  C  C   . PRO A 1 39  ? 14.581 -9.318  19.263  1.00 17.18 ? 39  PRO A C   1 
ATOM   288  O  O   . PRO A 1 39  ? 13.808 -10.034 19.913  1.00 17.14 ? 39  PRO A O   1 
ATOM   289  C  CB  . PRO A 1 39  ? 13.265 -7.455  18.166  1.00 16.00 ? 39  PRO A CB  1 
ATOM   290  C  CG  . PRO A 1 39  ? 12.068 -7.651  17.241  1.00 18.20 ? 39  PRO A CG  1 
ATOM   291  C  CD  . PRO A 1 39  ? 11.950 -9.112  16.987  1.00 15.69 ? 39  PRO A CD  1 
ATOM   292  N  N   . ARG A 1 40  ? 15.833 -9.072  19.641  1.00 18.72 ? 40  ARG A N   1 
ATOM   293  C  CA  . ARG A 1 40  ? 16.354 -9.686  20.850  1.00 18.47 ? 40  ARG A CA  1 
ATOM   294  C  C   . ARG A 1 40  ? 15.683 -9.154  22.103  1.00 19.04 ? 40  ARG A C   1 
ATOM   295  O  O   . ARG A 1 40  ? 15.703 -9.841  23.119  1.00 20.75 ? 40  ARG A O   1 
ATOM   296  C  CB  . ARG A 1 40  ? 17.874 -9.507  20.894  1.00 23.02 ? 40  ARG A CB  1 
ATOM   297  C  CG  . ARG A 1 40  ? 18.369 -8.102  21.162  1.00 21.03 ? 40  ARG A CG  1 
ATOM   298  C  CD  . ARG A 1 40  ? 19.859 -8.106  21.449  1.00 19.03 ? 40  ARG A CD  1 
ATOM   299  N  NE  . ARG A 1 40  ? 20.366 -6.744  21.545  1.00 18.74 ? 40  ARG A NE  1 
ATOM   300  C  CZ  . ARG A 1 40  ? 21.618 -6.433  21.854  1.00 21.08 ? 40  ARG A CZ  1 
ATOM   301  N  NH1 . ARG A 1 40  ? 22.537 -7.369  22.050  1.00 19.55 ? 40  ARG A NH1 1 
ATOM   302  N  NH2 . ARG A 1 40  ? 21.956 -5.152  21.972  1.00 19.76 ? 40  ARG A NH2 1 
ATOM   303  N  N   . HIS A 1 41  ? 15.010 -7.999  22.035  1.00 18.73 ? 41  HIS A N   1 
ATOM   304  C  CA  . HIS A 1 41  ? 14.337 -7.482  23.222  1.00 25.81 ? 41  HIS A CA  1 
ATOM   305  C  C   . HIS A 1 41  ? 13.071 -8.267  23.588  1.00 21.83 ? 41  HIS A C   1 
ATOM   306  O  O   . HIS A 1 41  ? 12.440 -7.952  24.600  1.00 21.58 ? 41  HIS A O   1 
ATOM   307  C  CB  . HIS A 1 41  ? 14.085 -5.979  23.041  1.00 24.17 ? 41  HIS A CB  1 
ATOM   308  C  CG  . HIS A 1 41  ? 12.971 -5.637  22.101  1.00 26.07 ? 41  HIS A CG  1 
ATOM   309  N  ND1 . HIS A 1 41  ? 13.155 -4.797  21.024  1.00 23.17 ? 41  HIS A ND1 1 
ATOM   310  C  CD2 . HIS A 1 41  ? 11.646 -5.918  22.133  1.00 28.93 ? 41  HIS A CD2 1 
ATOM   311  C  CE1 . HIS A 1 41  ? 12.006 -4.628  20.394  1.00 19.95 ? 41  HIS A CE1 1 
ATOM   312  N  NE2 . HIS A 1 41  ? 11.072 -5.295  21.048  1.00 29.84 ? 41  HIS A NE2 1 
ATOM   313  N  N   . VAL A 1 42  ? 12.767 -9.353  22.877  1.00 20.89 ? 42  VAL A N   1 
ATOM   314  C  CA  . VAL A 1 42  ? 11.728 -10.278 23.315  1.00 20.69 ? 42  VAL A CA  1 
ATOM   315  C  C   . VAL A 1 42  ? 12.043 -10.912 24.672  1.00 23.29 ? 42  VAL A C   1 
ATOM   316  O  O   . VAL A 1 42  ? 11.134 -11.409 25.347  1.00 24.54 ? 42  VAL A O   1 
ATOM   317  C  CB  . VAL A 1 42  ? 11.527 -11.373 22.240  1.00 20.39 ? 42  VAL A CB  1 
ATOM   318  C  CG1 . VAL A 1 42  ? 12.651 -12.371 22.280  1.00 17.73 ? 42  VAL A CG1 1 
ATOM   319  C  CG2 . VAL A 1 42  ? 10.171 -12.058 22.406  1.00 25.36 ? 42  VAL A CG2 1 
ATOM   320  N  N   . ILE A 1 43  ? 13.316 -10.928 25.088  1.00 23.48 ? 43  ILE A N   1 
ATOM   321  C  CA  . ILE A 1 43  ? 13.686 -11.522 26.372  1.00 24.61 ? 43  ILE A CA  1 
ATOM   322  C  C   . ILE A 1 43  ? 13.641 -10.530 27.529  1.00 23.50 ? 43  ILE A C   1 
ATOM   323  O  O   . ILE A 1 43  ? 13.885 -10.925 28.684  1.00 26.23 ? 43  ILE A O   1 
ATOM   324  C  CB  . ILE A 1 43  ? 15.098 -12.148 26.322  1.00 22.02 ? 43  ILE A CB  1 
ATOM   325  C  CG1 . ILE A 1 43  ? 16.164 -11.064 26.129  1.00 21.80 ? 43  ILE A CG1 1 
ATOM   326  C  CG2 . ILE A 1 43  ? 15.185 -13.207 25.229  1.00 21.57 ? 43  ILE A CG2 1 
ATOM   327  C  CD1 . ILE A 1 43  ? 17.587 -11.537 26.404  1.00 24.51 ? 43  ILE A CD1 1 
ATOM   328  N  N   . CYS A 1 44  ? 13.324 -9.264  27.272  1.00 26.02 ? 44  CYS A N   1 
ATOM   329  C  CA  . CYS A 1 44  ? 13.367 -8.233  28.308  1.00 27.39 ? 44  CYS A CA  1 
ATOM   330  C  C   . CYS A 1 44  ? 12.030 -8.083  29.020  1.00 32.67 ? 44  CYS A C   1 
ATOM   331  O  O   . CYS A 1 44  ? 10.964 -8.174  28.402  1.00 38.08 ? 44  CYS A O   1 
ATOM   332  C  CB  . CYS A 1 44  ? 13.730 -6.884  27.700  1.00 27.76 ? 44  CYS A CB  1 
ATOM   333  S  SG  . CYS A 1 44  ? 15.410 -6.780  27.143  1.00 31.66 ? 44  CYS A SG  1 
ATOM   334  N  N   . THR A 1 45  ? 12.096 -7.810  30.314  1.00 34.85 ? 45  THR A N   1 
ATOM   335  C  CA  . THR A 1 45  ? 10.944 -7.282  31.023  1.00 43.44 ? 45  THR A CA  1 
ATOM   336  C  C   . THR A 1 45  ? 10.929 -5.762  30.901  1.00 50.46 ? 45  THR A C   1 
ATOM   337  O  O   . THR A 1 45  ? 11.851 -5.145  30.364  1.00 40.30 ? 45  THR A O   1 
ATOM   338  C  CB  . THR A 1 45  ? 10.977 -7.694  32.490  1.00 43.81 ? 45  THR A CB  1 
ATOM   339  O  OG1 . THR A 1 45  ? 12.061 -7.021  33.144  1.00 43.26 ? 45  THR A OG1 1 
ATOM   340  C  CG2 . THR A 1 45  ? 11.163 -9.201  32.607  1.00 41.71 ? 45  THR A CG2 1 
ATOM   341  N  N   . SER A 1 46  ? 9.866  -5.153  31.422  1.00 59.31 ? 46  SER A N   1 
ATOM   342  C  CA  . SER A 1 46  ? 9.769  -3.701  31.360  1.00 52.05 ? 46  SER A CA  1 
ATOM   343  C  C   . SER A 1 46  ? 10.965 -3.043  32.036  1.00 53.81 ? 46  SER A C   1 
ATOM   344  O  O   . SER A 1 46  ? 11.492 -2.038  31.542  1.00 51.44 ? 46  SER A O   1 
ATOM   345  C  CB  . SER A 1 46  ? 8.462  -3.237  31.996  1.00 63.20 ? 46  SER A CB  1 
ATOM   346  O  OG  . SER A 1 46  ? 7.469  -3.090  31.000  1.00 70.82 ? 46  SER A OG  1 
ATOM   347  N  N   . GLU A 1 47  ? 11.422 -3.607  33.157  1.00 55.47 ? 47  GLU A N   1 
ATOM   348  C  CA  . GLU A 1 47  ? 12.556 -3.016  33.860  1.00 53.02 ? 47  GLU A CA  1 
ATOM   349  C  C   . GLU A 1 47  ? 13.867 -3.261  33.124  1.00 50.00 ? 47  GLU A C   1 
ATOM   350  O  O   . GLU A 1 47  ? 14.772 -2.418  33.166  1.00 48.54 ? 47  GLU A O   1 
ATOM   351  C  CB  . GLU A 1 47  ? 12.640 -3.563  35.282  1.00 64.37 ? 47  GLU A CB  1 
ATOM   352  C  CG  . GLU A 1 47  ? 13.530 -2.730  36.183  1.00 68.79 ? 47  GLU A CG  1 
ATOM   353  C  CD  . GLU A 1 47  ? 12.835 -2.328  37.461  1.00 82.60 ? 47  GLU A CD  1 
ATOM   354  O  OE1 . GLU A 1 47  ? 11.945 -3.079  37.912  1.00 90.39 ? 47  GLU A OE1 1 
ATOM   355  O  OE2 . GLU A 1 47  ? 13.172 -1.259  38.010  1.00 89.55 ? 47  GLU A OE2 1 
ATOM   356  N  N   . ASP A 1 48  ? 14.001 -4.416  32.466  1.00 49.00 ? 48  ASP A N   1 
ATOM   357  C  CA  . ASP A 1 48  ? 15.225 -4.698  31.721  1.00 49.49 ? 48  ASP A CA  1 
ATOM   358  C  C   . ASP A 1 48  ? 15.460 -3.682  30.617  1.00 40.36 ? 48  ASP A C   1 
ATOM   359  O  O   . ASP A 1 48  ? 16.613 -3.373  30.295  1.00 36.50 ? 48  ASP A O   1 
ATOM   360  C  CB  . ASP A 1 48  ? 15.179 -6.095  31.100  1.00 31.46 ? 48  ASP A CB  1 
ATOM   361  C  CG  . ASP A 1 48  ? 14.965 -7.195  32.116  1.00 48.59 ? 48  ASP A CG  1 
ATOM   362  O  OD1 . ASP A 1 48  ? 15.408 -7.046  33.279  1.00 42.99 ? 48  ASP A OD1 1 
ATOM   363  O  OD2 . ASP A 1 48  ? 14.366 -8.224  31.729  1.00 37.50 ? 48  ASP A OD2 1 
ATOM   364  N  N   . MET A 1 49  ? 14.386 -3.172  30.010  1.00 43.51 ? 49  MET A N   1 
ATOM   365  C  CA  . MET A 1 49  ? 14.522 -2.324  28.832  1.00 38.82 ? 49  MET A CA  1 
ATOM   366  C  C   . MET A 1 49  ? 15.221 -1.008  29.137  1.00 38.84 ? 49  MET A C   1 
ATOM   367  O  O   . MET A 1 49  ? 15.668 -0.328  28.208  1.00 34.55 ? 49  MET A O   1 
ATOM   368  C  CB  . MET A 1 49  ? 13.149 -2.048  28.222  1.00 43.40 ? 49  MET A CB  1 
ATOM   369  C  CG  . MET A 1 49  ? 12.414 -3.296  27.768  1.00 51.43 ? 49  MET A CG  1 
ATOM   370  S  SD  . MET A 1 49  ? 12.574 -3.590  25.998  1.00 57.90 ? 49  MET A SD  1 
ATOM   371  C  CE  . MET A 1 49  ? 11.031 -4.427  25.637  1.00 38.26 ? 49  MET A CE  1 
ATOM   372  N  N   . LEU A 1 50  ? 15.325 -0.633  30.411  1.00 38.53 ? 50  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 50  ? 15.972 0.624   30.767  1.00 38.52 ? 50  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 50  ? 17.488 0.546   30.632  1.00 35.40 ? 50  LEU A C   1 
ATOM   375  O  O   . LEU A 1 50  ? 18.126 1.549   30.294  1.00 36.41 ? 50  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 50  ? 15.591 1.028   32.191  1.00 41.08 ? 50  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 50  ? 14.171 1.574   32.364  1.00 46.88 ? 50  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 50  ? 13.768 1.574   33.841  1.00 50.51 ? 50  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 50  ? 14.029 2.965   31.752  1.00 51.74 ? 50  LEU A CD2 1 
ATOM   380  N  N   . ASN A 1 51  ? 18.083 -0.623  30.886  1.00 38.06 ? 51  ASN A N   1 
ATOM   381  C  CA  . ASN A 1 51  ? 19.527 -0.786  30.755  1.00 33.61 ? 51  ASN A CA  1 
ATOM   382  C  C   . ASN A 1 51  ? 19.865 -2.269  30.611  1.00 37.01 ? 51  ASN A C   1 
ATOM   383  O  O   . ASN A 1 51  ? 20.570 -2.834  31.460  1.00 43.98 ? 51  ASN A O   1 
ATOM   384  C  CB  . ASN A 1 51  ? 20.239 -0.174  31.964  1.00 43.87 ? 51  ASN A CB  1 
ATOM   385  C  CG  . ASN A 1 51  ? 21.742 -0.093  31.781  1.00 42.57 ? 51  ASN A CG  1 
ATOM   386  O  OD1 . ASN A 1 51  ? 22.266 -0.394  30.709  1.00 45.69 ? 51  ASN A OD1 1 
ATOM   387  N  ND2 . ASN A 1 51  ? 22.446 0.296   32.838  1.00 53.97 ? 51  ASN A ND2 1 
ATOM   388  N  N   . PRO A 1 52  ? 19.403 -2.930  29.549  1.00 31.80 ? 52  PRO A N   1 
ATOM   389  C  CA  . PRO A 1 52  ? 19.536 -4.388  29.472  1.00 32.64 ? 52  PRO A CA  1 
ATOM   390  C  C   . PRO A 1 52  ? 20.955 -4.818  29.133  1.00 28.53 ? 52  PRO A C   1 
ATOM   391  O  O   . PRO A 1 52  ? 21.634 -4.197  28.313  1.00 39.75 ? 52  PRO A O   1 
ATOM   392  C  CB  . PRO A 1 52  ? 18.578 -4.759  28.336  1.00 29.93 ? 52  PRO A CB  1 
ATOM   393  C  CG  . PRO A 1 52  ? 18.704 -3.572  27.394  1.00 28.57 ? 52  PRO A CG  1 
ATOM   394  C  CD  . PRO A 1 52  ? 18.850 -2.363  28.304  1.00 30.20 ? 52  PRO A CD  1 
ATOM   395  N  N   . ASN A 1 53  ? 21.395 -5.903  29.764  1.00 28.25 ? 53  ASN A N   1 
ATOM   396  C  CA  . ASN A 1 53  ? 22.607 -6.610  29.357  1.00 27.53 ? 53  ASN A CA  1 
ATOM   397  C  C   . ASN A 1 53  ? 22.136 -7.900  28.697  1.00 26.31 ? 53  ASN A C   1 
ATOM   398  O  O   . ASN A 1 53  ? 21.816 -8.881  29.371  1.00 26.29 ? 53  ASN A O   1 
ATOM   399  C  CB  . ASN A 1 53  ? 23.535 -6.878  30.535  1.00 29.22 ? 53  ASN A CB  1 
ATOM   400  C  CG  . ASN A 1 53  ? 24.856 -7.482  30.104  1.00 29.16 ? 53  ASN A CG  1 
ATOM   401  O  OD1 . ASN A 1 53  ? 24.893 -8.515  29.425  1.00 28.80 ? 53  ASN A OD1 1 
ATOM   402  N  ND2 . ASN A 1 53  ? 25.954 -6.845  30.504  1.00 29.20 ? 53  ASN A ND2 1 
ATOM   403  N  N   . TYR A 1 54  ? 22.082 -7.896  27.367  1.00 25.45 ? 54  TYR A N   1 
ATOM   404  C  CA  . TYR A 1 54  ? 21.371 -8.966  26.686  1.00 24.47 ? 54  TYR A CA  1 
ATOM   405  C  C   . TYR A 1 54  ? 22.068 -10.305 26.874  1.00 25.20 ? 54  TYR A C   1 
ATOM   406  O  O   . TYR A 1 54  ? 21.406 -11.338 27.029  1.00 24.84 ? 54  TYR A O   1 
ATOM   407  C  CB  . TYR A 1 54  ? 21.229 -8.615  25.213  1.00 23.88 ? 54  TYR A CB  1 
ATOM   408  C  CG  . TYR A 1 54  ? 20.158 -7.584  24.994  1.00 24.29 ? 54  TYR A CG  1 
ATOM   409  C  CD1 . TYR A 1 54  ? 18.821 -7.948  24.904  1.00 24.11 ? 54  TYR A CD1 1 
ATOM   410  C  CD2 . TYR A 1 54  ? 20.483 -6.240  24.878  1.00 25.02 ? 54  TYR A CD2 1 
ATOM   411  C  CE1 . TYR A 1 54  ? 17.833 -6.988  24.698  1.00 24.72 ? 54  TYR A CE1 1 
ATOM   412  C  CE2 . TYR A 1 54  ? 19.498 -5.276  24.676  1.00 25.64 ? 54  TYR A CE2 1 
ATOM   413  C  CZ  . TYR A 1 54  ? 18.180 -5.662  24.578  1.00 25.50 ? 54  TYR A CZ  1 
ATOM   414  O  OH  . TYR A 1 54  ? 17.212 -4.699  24.380  1.00 26.33 ? 54  TYR A OH  1 
ATOM   415  N  N   . GLU A 1 55  ? 23.401 -10.321 26.862  1.00 24.55 ? 55  GLU A N   1 
ATOM   416  C  CA  . GLU A 1 55  ? 24.090 -11.590 27.071  1.00 24.20 ? 55  GLU A CA  1 
ATOM   417  C  C   . GLU A 1 55  ? 23.760 -12.157 28.444  1.00 24.79 ? 55  GLU A C   1 
ATOM   418  O  O   . GLU A 1 55  ? 23.525 -13.361 28.587  1.00 25.60 ? 55  GLU A O   1 
ATOM   419  C  CB  . GLU A 1 55  ? 25.601 -11.414 26.901  1.00 31.30 ? 55  GLU A CB  1 
ATOM   420  C  CG  . GLU A 1 55  ? 26.355 -12.708 26.563  1.00 30.57 ? 55  GLU A CG  1 
ATOM   421  C  CD  . GLU A 1 55  ? 26.075 -13.214 25.144  1.00 34.63 ? 55  GLU A CD  1 
ATOM   422  O  OE1 . GLU A 1 55  ? 26.633 -12.638 24.189  1.00 40.35 ? 55  GLU A OE1 1 
ATOM   423  O  OE2 . GLU A 1 55  ? 25.320 -14.199 24.985  1.00 37.99 ? 55  GLU A OE2 1 
ATOM   424  N  N   . ASP A 1 56  ? 23.735 -11.304 29.469  1.00 25.71 ? 56  ASP A N   1 
ATOM   425  C  CA  . ASP A 1 56  ? 23.408 -11.784 30.810  1.00 26.52 ? 56  ASP A CA  1 
ATOM   426  C  C   . ASP A 1 56  ? 21.966 -12.266 30.885  1.00 26.19 ? 56  ASP A C   1 
ATOM   427  O  O   . ASP A 1 56  ? 21.681 -13.306 31.490  1.00 29.73 ? 56  ASP A O   1 
ATOM   428  C  CB  . ASP A 1 56  ? 23.672 -10.686 31.849  1.00 27.80 ? 56  ASP A CB  1 
ATOM   429  C  CG  . ASP A 1 56  ? 25.152 -10.393 32.037  1.00 35.05 ? 56  ASP A CG  1 
ATOM   430  O  OD1 . ASP A 1 56  ? 25.976 -11.221 31.597  1.00 34.88 ? 56  ASP A OD1 1 
ATOM   431  O  OD2 . ASP A 1 56  ? 25.494 -9.329  32.607  1.00 31.29 ? 56  ASP A OD2 1 
ATOM   432  N  N   . LEU A 1 57  ? 21.041 -11.516 30.288  1.00 25.85 ? 57  LEU A N   1 
ATOM   433  C  CA  . LEU A 1 57  ? 19.644 -11.937 30.280  1.00 29.01 ? 57  LEU A CA  1 
ATOM   434  C  C   . LEU A 1 57  ? 19.476 -13.275 29.567  1.00 26.73 ? 57  LEU A C   1 
ATOM   435  O  O   . LEU A 1 57  ? 18.638 -14.096 29.957  1.00 28.32 ? 57  LEU A O   1 
ATOM   436  C  CB  . LEU A 1 57  ? 18.790 -10.859 29.616  1.00 25.57 ? 57  LEU A CB  1 
ATOM   437  C  CG  . LEU A 1 57  ? 18.536 -9.599  30.451  1.00 26.85 ? 57  LEU A CG  1 
ATOM   438  C  CD1 . LEU A 1 57  ? 17.487 -8.725  29.788  1.00 36.44 ? 57  LEU A CD1 1 
ATOM   439  C  CD2 . LEU A 1 57  ? 18.130 -9.940  31.872  1.00 37.70 ? 57  LEU A CD2 1 
ATOM   440  N  N   . LEU A 1 58  ? 20.277 -13.516 28.526  1.00 23.93 ? 58  LEU A N   1 
ATOM   441  C  CA  . LEU A 1 58  ? 20.158 -14.746 27.746  1.00 27.47 ? 58  LEU A CA  1 
ATOM   442  C  C   . LEU A 1 58  ? 20.642 -15.969 28.525  1.00 35.54 ? 58  LEU A C   1 
ATOM   443  O  O   . LEU A 1 58  ? 20.217 -17.093 28.233  1.00 34.27 ? 58  LEU A O   1 
ATOM   444  C  CB  . LEU A 1 58  ? 20.941 -14.581 26.443  1.00 33.21 ? 58  LEU A CB  1 
ATOM   445  C  CG  . LEU A 1 58  ? 20.492 -15.249 25.144  1.00 31.88 ? 58  LEU A CG  1 
ATOM   446  C  CD1 . LEU A 1 58  ? 18.980 -15.257 24.985  1.00 22.38 ? 58  LEU A CD1 1 
ATOM   447  C  CD2 . LEU A 1 58  ? 21.137 -14.515 23.989  1.00 30.30 ? 58  LEU A CD2 1 
ATOM   448  N  N   . ILE A 1 59  ? 21.526 -15.774 29.511  1.00 28.11 ? 59  ILE A N   1 
ATOM   449  C  CA  . ILE A 1 59  ? 22.028 -16.888 30.315  1.00 30.66 ? 59  ILE A CA  1 
ATOM   450  C  C   . ILE A 1 59  ? 20.873 -17.638 30.961  1.00 37.33 ? 59  ILE A C   1 
ATOM   451  O  O   . ILE A 1 59  ? 20.951 -18.851 31.185  1.00 39.98 ? 59  ILE A O   1 
ATOM   452  C  CB  . ILE A 1 59  ? 23.022 -16.382 31.384  1.00 33.65 ? 59  ILE A CB  1 
ATOM   453  C  CG1 . ILE A 1 59  ? 24.364 -16.033 30.751  1.00 31.33 ? 59  ILE A CG1 1 
ATOM   454  C  CG2 . ILE A 1 59  ? 23.234 -17.445 32.450  1.00 31.22 ? 59  ILE A CG2 1 
ATOM   455  C  CD1 . ILE A 1 59  ? 25.326 -15.344 31.690  1.00 35.07 ? 59  ILE A CD1 1 
ATOM   456  N  N   . ARG A 1 60  ? 19.789 -16.939 31.262  1.00 33.11 ? 60  ARG A N   1 
ATOM   457  C  CA  . ARG A 1 60  ? 18.683 -17.493 32.024  1.00 37.10 ? 60  ARG A CA  1 
ATOM   458  C  C   . ARG A 1 60  ? 17.585 -18.056 31.132  1.00 30.54 ? 60  ARG A C   1 
ATOM   459  O  O   . ARG A 1 60  ? 16.500 -18.386 31.625  1.00 35.15 ? 60  ARG A O   1 
ATOM   460  C  CB  . ARG A 1 60  ? 18.133 -16.411 32.954  1.00 37.08 ? 60  ARG A CB  1 
ATOM   461  C  CG  . ARG A 1 60  ? 19.189 -15.946 33.954  1.00 50.35 ? 60  ARG A CG  1 
ATOM   462  C  CD  . ARG A 1 60  ? 18.652 -14.952 34.965  1.00 58.21 ? 60  ARG A CD  1 
ATOM   463  N  NE  . ARG A 1 60  ? 19.447 -13.728 34.944  1.00 75.71 ? 60  ARG A NE  1 
ATOM   464  C  CZ  . ARG A 1 60  ? 18.942 -12.503 34.862  1.00 68.96 ? 60  ARG A CZ  1 
ATOM   465  N  NH1 . ARG A 1 60  ? 17.636 -12.294 34.827  1.00 65.81 ? 60  ARG A NH1 1 
ATOM   466  N  NH2 . ARG A 1 60  ? 19.770 -11.462 34.807  1.00 54.37 ? 60  ARG A NH2 1 
ATOM   467  N  N   . LYS A 1 61  ? 17.848 -18.192 29.839  1.00 31.69 ? 61  LYS A N   1 
ATOM   468  C  CA  . LYS A 1 61  ? 16.839 -18.626 28.895  1.00 29.68 ? 61  LYS A CA  1 
ATOM   469  C  C   . LYS A 1 61  ? 17.330 -19.907 28.234  1.00 39.77 ? 61  LYS A C   1 
ATOM   470  O  O   . LYS A 1 61  ? 18.518 -20.035 27.913  1.00 36.87 ? 61  LYS A O   1 
ATOM   471  C  CB  . LYS A 1 61  ? 16.571 -17.545 27.842  1.00 30.05 ? 61  LYS A CB  1 
ATOM   472  C  CG  . LYS A 1 61  ? 16.021 -16.221 28.379  1.00 30.95 ? 61  LYS A CG  1 
ATOM   473  C  CD  . LYS A 1 61  ? 14.520 -16.240 28.651  1.00 28.32 ? 61  LYS A CD  1 
ATOM   474  C  CE  . LYS A 1 61  ? 14.105 -15.077 29.526  1.00 37.89 ? 61  LYS A CE  1 
ATOM   475  N  NZ  . LYS A 1 61  ? 13.997 -15.460 30.968  1.00 55.34 ? 61  LYS A NZ  1 
ATOM   476  N  N   . SER A 1 62  ? 16.421 -20.858 28.054  1.00 29.00 ? 62  SER A N   1 
ATOM   477  C  CA  . SER A 1 62  ? 16.692 -22.106 27.354  1.00 31.02 ? 62  SER A CA  1 
ATOM   478  C  C   . SER A 1 62  ? 15.775 -22.185 26.138  1.00 24.90 ? 62  SER A C   1 
ATOM   479  O  O   . SER A 1 62  ? 14.823 -21.412 26.007  1.00 26.52 ? 62  SER A O   1 
ATOM   480  C  CB  . SER A 1 62  ? 16.485 -23.316 28.284  1.00 28.98 ? 62  SER A CB  1 
ATOM   481  O  OG  . SER A 1 62  ? 17.205 -23.189 29.501  1.00 36.92 ? 62  SER A OG  1 
ATOM   482  N  N   . ASN A 1 63  ? 16.071 -23.125 25.231  1.00 26.37 ? 63  ASN A N   1 
ATOM   483  C  CA  . ASN A 1 63  ? 15.218 -23.313 24.055  1.00 21.63 ? 63  ASN A CA  1 
ATOM   484  C  C   . ASN A 1 63  ? 13.740 -23.351 24.424  1.00 21.37 ? 63  ASN A C   1 
ATOM   485  O  O   . ASN A 1 63  ? 12.914 -22.739 23.743  1.00 21.66 ? 63  ASN A O   1 
ATOM   486  C  CB  . ASN A 1 63  ? 15.590 -24.602 23.322  1.00 29.14 ? 63  ASN A CB  1 
ATOM   487  C  CG  . ASN A 1 63  ? 16.949 -24.534 22.670  1.00 25.31 ? 63  ASN A CG  1 
ATOM   488  O  OD1 . ASN A 1 63  ? 17.399 -23.471 22.266  1.00 26.18 ? 63  ASN A OD1 1 
ATOM   489  N  ND2 . ASN A 1 63  ? 17.618 -25.685 22.570  1.00 24.73 ? 63  ASN A ND2 1 
ATOM   490  N  N   . HIS A 1 64  ? 13.386 -24.080 25.495  1.00 25.28 ? 64  HIS A N   1 
ATOM   491  C  CA  . HIS A 1 64  ? 11.980 -24.271 25.836  1.00 25.05 ? 64  HIS A CA  1 
ATOM   492  C  C   . HIS A 1 64  ? 11.324 -23.015 26.404  1.00 29.80 ? 64  HIS A C   1 
ATOM   493  O  O   . HIS A 1 64  ? 10.096 -22.995 26.540  1.00 28.66 ? 64  HIS A O   1 
ATOM   494  C  CB  . HIS A 1 64  ? 11.810 -25.432 26.828  1.00 28.98 ? 64  HIS A CB  1 
ATOM   495  C  CG  . HIS A 1 64  ? 12.320 -25.143 28.206  1.00 27.63 ? 64  HIS A CG  1 
ATOM   496  N  ND1 . HIS A 1 64  ? 13.546 -25.584 28.652  1.00 32.32 ? 64  HIS A ND1 1 
ATOM   497  C  CD2 . HIS A 1 64  ? 11.752 -24.496 29.253  1.00 30.36 ? 64  HIS A CD2 1 
ATOM   498  C  CE1 . HIS A 1 64  ? 13.725 -25.203 29.907  1.00 29.04 ? 64  HIS A CE1 1 
ATOM   499  N  NE2 . HIS A 1 64  ? 12.651 -24.539 30.296  1.00 38.15 ? 64  HIS A NE2 1 
ATOM   500  N  N   . ASN A 1 65  ? 12.093 -21.967 26.718  1.00 25.84 ? 65  ASN A N   1 
ATOM   501  C  CA  . ASN A 1 65  ? 11.484 -20.704 27.118  1.00 28.27 ? 65  ASN A CA  1 
ATOM   502  C  C   . ASN A 1 65  ? 10.971 -19.892 25.939  1.00 29.07 ? 65  ASN A C   1 
ATOM   503  O  O   . ASN A 1 65  ? 10.186 -18.963 26.145  1.00 31.69 ? 65  ASN A O   1 
ATOM   504  C  CB  . ASN A 1 65  ? 12.473 -19.861 27.924  1.00 31.46 ? 65  ASN A CB  1 
ATOM   505  C  CG  . ASN A 1 65  ? 12.875 -20.527 29.230  1.00 24.09 ? 65  ASN A CG  1 
ATOM   506  O  OD1 . ASN A 1 65  ? 14.061 -20.753 29.484  1.00 28.89 ? 65  ASN A OD1 1 
ATOM   507  N  ND2 . ASN A 1 65  ? 11.885 -20.834 30.078  1.00 32.79 ? 65  ASN A ND2 1 
ATOM   508  N  N   . PHE A 1 66  ? 11.380 -20.210 24.714  1.00 23.42 ? 66  PHE A N   1 
ATOM   509  C  CA  . PHE A 1 66  ? 10.920 -19.495 23.534  1.00 21.33 ? 66  PHE A CA  1 
ATOM   510  C  C   . PHE A 1 66  ? 9.763  -20.263 22.911  1.00 29.03 ? 66  PHE A C   1 
ATOM   511  O  O   . PHE A 1 66  ? 9.914  -21.427 22.535  1.00 38.13 ? 66  PHE A O   1 
ATOM   512  C  CB  . PHE A 1 66  ? 12.050 -19.320 22.528  1.00 26.72 ? 66  PHE A CB  1 
ATOM   513  C  CG  . PHE A 1 66  ? 13.171 -18.482 23.044  1.00 25.48 ? 66  PHE A CG  1 
ATOM   514  C  CD1 . PHE A 1 66  ? 13.100 -17.101 23.017  1.00 25.25 ? 66  PHE A CD1 1 
ATOM   515  C  CD2 . PHE A 1 66  ? 14.309 -19.084 23.558  1.00 24.27 ? 66  PHE A CD2 1 
ATOM   516  C  CE1 . PHE A 1 66  ? 14.155 -16.332 23.508  1.00 26.77 ? 66  PHE A CE1 1 
ATOM   517  C  CE2 . PHE A 1 66  ? 15.363 -18.325 24.043  1.00 28.48 ? 66  PHE A CE2 1 
ATOM   518  C  CZ  . PHE A 1 66  ? 15.280 -16.947 24.016  1.00 30.10 ? 66  PHE A CZ  1 
ATOM   519  N  N   A LEU A 1 67  ? 8.613  -19.611 22.811  0.50 24.12 ? 67  LEU A N   1 
ATOM   520  N  N   B LEU A 1 67  ? 8.608  -19.615 22.817  0.50 24.13 ? 67  LEU A N   1 
ATOM   521  C  CA  A LEU A 1 67  ? 7.420  -20.198 22.223  0.50 28.50 ? 67  LEU A CA  1 
ATOM   522  C  CA  B LEU A 1 67  ? 7.418  -20.208 22.226  0.50 28.50 ? 67  LEU A CA  1 
ATOM   523  C  C   A LEU A 1 67  ? 7.194  -19.583 20.855  0.50 25.48 ? 67  LEU A C   1 
ATOM   524  C  C   B LEU A 1 67  ? 7.187  -19.587 20.860  0.50 25.48 ? 67  LEU A C   1 
ATOM   525  O  O   A LEU A 1 67  ? 7.114  -18.357 20.729  0.50 29.82 ? 67  LEU A O   1 
ATOM   526  O  O   B LEU A 1 67  ? 7.096  -18.361 20.742  0.50 29.82 ? 67  LEU A O   1 
ATOM   527  C  CB  A LEU A 1 67  ? 6.200  -19.960 23.105  0.50 29.33 ? 67  LEU A CB  1 
ATOM   528  C  CB  B LEU A 1 67  ? 6.195  -19.994 23.115  0.50 29.35 ? 67  LEU A CB  1 
ATOM   529  C  CG  A LEU A 1 67  ? 6.024  -20.857 24.323  0.50 26.65 ? 67  LEU A CG  1 
ATOM   530  C  CG  B LEU A 1 67  ? 6.274  -20.630 24.500  0.50 27.60 ? 67  LEU A CG  1 
ATOM   531  C  CD1 A LEU A 1 67  ? 7.130  -20.635 25.346  0.50 26.85 ? 67  LEU A CD1 1 
ATOM   532  C  CD1 B LEU A 1 67  ? 4.998  -20.361 25.268  0.50 34.97 ? 67  LEU A CD1 1 
ATOM   533  C  CD2 A LEU A 1 67  ? 4.671  -20.547 24.916  0.50 35.63 ? 67  LEU A CD2 1 
ATOM   534  C  CD2 B LEU A 1 67  ? 6.534  -22.125 24.382  0.50 26.59 ? 67  LEU A CD2 1 
ATOM   535  N  N   . VAL A 1 68  ? 7.095  -20.430 19.837  1.00 24.83 ? 68  VAL A N   1 
ATOM   536  C  CA  . VAL A 1 68  ? 6.899  -19.992 18.458  1.00 22.85 ? 68  VAL A CA  1 
ATOM   537  C  C   . VAL A 1 68  ? 5.631  -20.638 17.922  1.00 25.96 ? 68  VAL A C   1 
ATOM   538  O  O   . VAL A 1 68  ? 5.525  -21.868 17.886  1.00 27.06 ? 68  VAL A O   1 
ATOM   539  C  CB  . VAL A 1 68  ? 8.104  -20.344 17.581  1.00 26.82 ? 68  VAL A CB  1 
ATOM   540  C  CG1 . VAL A 1 68  ? 7.958  -19.711 16.216  1.00 25.54 ? 68  VAL A CG1 1 
ATOM   541  C  CG2 . VAL A 1 68  ? 9.396  -19.870 18.259  1.00 27.58 ? 68  VAL A CG2 1 
ATOM   542  N  N   . GLN A 1 69  ? 4.686  -19.811 17.479  1.00 24.68 ? 69  GLN A N   1 
ATOM   543  C  CA  . GLN A 1 69  ? 3.387  -20.269 17.004  1.00 29.41 ? 69  GLN A CA  1 
ATOM   544  C  C   . GLN A 1 69  ? 3.131  -19.704 15.615  1.00 26.17 ? 69  GLN A C   1 
ATOM   545  O  O   . GLN A 1 69  ? 3.368  -18.516 15.372  1.00 26.68 ? 69  GLN A O   1 
ATOM   546  C  CB  . GLN A 1 69  ? 2.294  -19.837 17.980  1.00 35.10 ? 69  GLN A CB  1 
ATOM   547  C  CG  . GLN A 1 69  ? 1.002  -20.614 17.921  1.00 43.33 ? 69  GLN A CG  1 
ATOM   548  C  CD  . GLN A 1 69  ? -0.024 -20.056 18.895  1.00 42.35 ? 69  GLN A CD  1 
ATOM   549  O  OE1 . GLN A 1 69  ? 0.287  -19.822 20.062  1.00 42.75 ? 69  GLN A OE1 1 
ATOM   550  N  NE2 . GLN A 1 69  ? -1.244 -19.836 18.422  1.00 49.81 ? 69  GLN A NE2 1 
ATOM   551  N  N   . ALA A 1 70  ? 2.656  -20.561 14.708  1.00 30.68 ? 70  ALA A N   1 
ATOM   552  C  CA  . ALA A 1 70  ? 2.411  -20.213 13.307  1.00 39.92 ? 70  ALA A CA  1 
ATOM   553  C  C   . ALA A 1 70  ? 1.030  -20.763 12.963  1.00 43.77 ? 70  ALA A C   1 
ATOM   554  O  O   . ALA A 1 70  ? 0.868  -21.973 12.785  1.00 43.83 ? 70  ALA A O   1 
ATOM   555  C  CB  . ALA A 1 70  ? 3.489  -20.793 12.402  1.00 38.50 ? 70  ALA A CB  1 
ATOM   556  N  N   . GLY A 1 71  ? 0.037  -19.885 12.866  1.00 44.65 ? 71  GLY A N   1 
ATOM   557  C  CA  . GLY A 1 71  ? -1.320 -20.368 13.030  1.00 44.88 ? 71  GLY A CA  1 
ATOM   558  C  C   . GLY A 1 71  ? -1.464 -20.857 14.458  1.00 49.89 ? 71  GLY A C   1 
ATOM   559  O  O   . GLY A 1 71  ? -1.024 -20.196 15.404  1.00 54.12 ? 71  GLY A O   1 
ATOM   560  N  N   . ASN A 1 72  ? -2.062 -22.036 14.627  1.00 55.07 ? 72  ASN A N   1 
ATOM   561  C  CA  . ASN A 1 72  ? -1.949 -22.737 15.900  1.00 60.23 ? 72  ASN A CA  1 
ATOM   562  C  C   . ASN A 1 72  ? -0.797 -23.732 15.927  1.00 64.44 ? 72  ASN A C   1 
ATOM   563  O  O   . ASN A 1 72  ? -0.425 -24.196 17.012  1.00 68.79 ? 72  ASN A O   1 
ATOM   564  C  CB  . ASN A 1 72  ? -3.254 -23.461 16.252  1.00 72.09 ? 72  ASN A CB  1 
ATOM   565  C  CG  . ASN A 1 72  ? -4.402 -22.505 16.503  1.00 74.54 ? 72  ASN A CG  1 
ATOM   566  O  OD1 . ASN A 1 72  ? -4.681 -21.626 15.689  1.00 86.23 ? 72  ASN A OD1 1 
ATOM   567  N  ND2 . ASN A 1 72  ? -5.074 -22.672 17.638  1.00 68.56 ? 72  ASN A ND2 1 
ATOM   568  N  N   . VAL A 1 73  ? -0.227 -24.071 14.767  1.00 51.90 ? 73  VAL A N   1 
ATOM   569  C  CA  . VAL A 1 73  ? 0.984  -24.885 14.714  1.00 51.99 ? 73  VAL A CA  1 
ATOM   570  C  C   . VAL A 1 73  ? 2.020  -24.343 15.681  1.00 41.03 ? 73  VAL A C   1 
ATOM   571  O  O   . VAL A 1 73  ? 2.477  -23.204 15.548  1.00 31.56 ? 73  VAL A O   1 
ATOM   572  C  CB  . VAL A 1 73  ? 1.569  -24.954 13.293  1.00 58.73 ? 73  VAL A CB  1 
ATOM   573  C  CG1 . VAL A 1 73  ? 3.077  -25.118 13.360  1.00 48.31 ? 73  VAL A CG1 1 
ATOM   574  C  CG2 . VAL A 1 73  ? 1.003  -26.141 12.578  1.00 73.65 ? 73  VAL A CG2 1 
ATOM   575  N  N   . GLN A 1 74  ? 2.407  -25.168 16.643  1.00 47.92 ? 74  GLN A N   1 
ATOM   576  C  CA  . GLN A 1 74  ? 3.417  -24.816 17.627  1.00 31.72 ? 74  GLN A CA  1 
ATOM   577  C  C   . GLN A 1 74  ? 4.725  -25.419 17.130  1.00 38.84 ? 74  GLN A C   1 
ATOM   578  O  O   . GLN A 1 74  ? 4.783  -26.616 16.831  1.00 34.25 ? 74  GLN A O   1 
ATOM   579  C  CB  . GLN A 1 74  ? 3.008  -25.344 19.004  1.00 36.87 ? 74  GLN A CB  1 
ATOM   580  C  CG  . GLN A 1 74  ? 3.781  -24.799 20.210  1.00 30.96 ? 74  GLN A CG  1 
ATOM   581  C  CD  . GLN A 1 74  ? 3.367  -23.360 20.513  1.00 41.69 ? 74  GLN A CD  1 
ATOM   582  O  OE1 . GLN A 1 74  ? 4.204  -22.471 20.642  1.00 36.64 ? 74  GLN A OE1 1 
ATOM   583  N  NE2 . GLN A 1 74  ? 2.067  -23.105 20.471  1.00 41.81 ? 74  GLN A NE2 1 
ATOM   584  N  N   . LEU A 1 75  ? 5.748  -24.586 16.977  1.00 25.81 ? 75  LEU A N   1 
ATOM   585  C  CA  . LEU A 1 75  ? 7.028  -25.053 16.470  1.00 28.93 ? 75  LEU A CA  1 
ATOM   586  C  C   . LEU A 1 75  ? 7.950  -25.395 17.623  1.00 30.69 ? 75  LEU A C   1 
ATOM   587  O  O   . LEU A 1 75  ? 7.921  -24.748 18.674  1.00 31.84 ? 75  LEU A O   1 
ATOM   588  C  CB  . LEU A 1 75  ? 7.692  -24.001 15.581  1.00 22.76 ? 75  LEU A CB  1 
ATOM   589  C  CG  . LEU A 1 75  ? 6.943  -23.527 14.346  1.00 34.02 ? 75  LEU A CG  1 
ATOM   590  C  CD1 . LEU A 1 75  ? 7.788  -22.469 13.682  1.00 27.25 ? 75  LEU A CD1 1 
ATOM   591  C  CD2 . LEU A 1 75  ? 6.730  -24.700 13.418  1.00 37.15 ? 75  LEU A CD2 1 
ATOM   592  N  N   A ARG A 1 76  ? 8.764  -26.429 17.430  0.37 24.22 ? 76  ARG A N   1 
ATOM   593  N  N   B ARG A 1 76  ? 8.777  -26.411 17.412  0.63 24.10 ? 76  ARG A N   1 
ATOM   594  C  CA  A ARG A 1 76  ? 9.686  -26.876 18.466  0.37 26.74 ? 76  ARG A CA  1 
ATOM   595  C  CA  B ARG A 1 76  ? 9.696  -26.886 18.437  0.63 26.73 ? 76  ARG A CA  1 
ATOM   596  C  C   A ARG A 1 76  ? 11.035 -26.205 18.242  0.37 26.36 ? 76  ARG A C   1 
ATOM   597  C  C   B ARG A 1 76  ? 11.056 -26.226 18.242  0.63 26.37 ? 76  ARG A C   1 
ATOM   598  O  O   A ARG A 1 76  ? 11.626 -26.327 17.163  0.37 23.95 ? 76  ARG A O   1 
ATOM   599  O  O   B ARG A 1 76  ? 11.671 -26.368 17.181  0.63 23.95 ? 76  ARG A O   1 
ATOM   600  C  CB  A ARG A 1 76  ? 9.830  -28.398 18.472  0.37 26.60 ? 76  ARG A CB  1 
ATOM   601  C  CB  B ARG A 1 76  ? 9.787  -28.412 18.394  0.63 26.54 ? 76  ARG A CB  1 
ATOM   602  C  CG  A ARG A 1 76  ? 10.712 -28.918 19.610  0.37 27.46 ? 76  ARG A CG  1 
ATOM   603  C  CG  B ARG A 1 76  ? 10.642 -29.018 19.489  0.63 27.51 ? 76  ARG A CG  1 
ATOM   604  C  CD  A ARG A 1 76  ? 10.669 -30.440 19.720  0.37 31.54 ? 76  ARG A CD  1 
ATOM   605  C  CD  B ARG A 1 76  ? 10.766 -30.525 19.302  0.63 30.58 ? 76  ARG A CD  1 
ATOM   606  N  NE  A ARG A 1 76  ? 11.952 -31.016 20.107  0.37 29.30 ? 76  ARG A NE  1 
ATOM   607  N  NE  B ARG A 1 76  ? 9.466  -31.183 19.377  0.63 24.13 ? 76  ARG A NE  1 
ATOM   608  C  CZ  A ARG A 1 76  ? 12.584 -30.769 21.248  0.37 26.35 ? 76  ARG A CZ  1 
ATOM   609  C  CZ  B ARG A 1 76  ? 8.859  -31.489 20.519  0.63 24.19 ? 76  ARG A CZ  1 
ATOM   610  N  NH1 A ARG A 1 76  ? 12.065 -29.975 22.170  0.37 19.13 ? 76  ARG A NH1 1 
ATOM   611  N  NH1 B ARG A 1 76  ? 9.435  -31.264 21.690  0.63 24.99 ? 76  ARG A NH1 1 
ATOM   612  N  NH2 A ARG A 1 76  ? 13.767 -31.335 21.469  0.37 28.80 ? 76  ARG A NH2 1 
ATOM   613  N  NH2 B ARG A 1 76  ? 7.648  -32.039 20.485  0.63 25.89 ? 76  ARG A NH2 1 
ATOM   614  N  N   . VAL A 1 77  ? 11.505 -25.495 19.260  1.00 24.50 ? 77  VAL A N   1 
ATOM   615  C  CA  . VAL A 1 77  ? 12.750 -24.742 19.209  1.00 18.94 ? 77  VAL A CA  1 
ATOM   616  C  C   . VAL A 1 77  ? 13.887 -25.655 19.647  1.00 26.45 ? 77  VAL A C   1 
ATOM   617  O  O   . VAL A 1 77  ? 13.894 -26.161 20.775  1.00 25.63 ? 77  VAL A O   1 
ATOM   618  C  CB  . VAL A 1 77  ? 12.665 -23.494 20.102  1.00 23.45 ? 77  VAL A CB  1 
ATOM   619  C  CG1 . VAL A 1 77  ? 14.014 -22.764 20.184  1.00 22.91 ? 77  VAL A CG1 1 
ATOM   620  C  CG2 . VAL A 1 77  ? 11.557 -22.567 19.586  1.00 21.09 ? 77  VAL A CG2 1 
ATOM   621  N  N   . ILE A 1 78  ? 14.858 -25.865 18.761  1.00 24.30 ? 78  ILE A N   1 
ATOM   622  C  CA  . ILE A 1 78  ? 15.954 -26.783 19.044  1.00 21.95 ? 78  ILE A CA  1 
ATOM   623  C  C   . ILE A 1 78  ? 17.285 -26.051 19.206  1.00 24.31 ? 78  ILE A C   1 
ATOM   624  O  O   . ILE A 1 78  ? 18.330 -26.693 19.370  1.00 26.25 ? 78  ILE A O   1 
ATOM   625  C  CB  . ILE A 1 78  ? 16.035 -27.894 17.983  1.00 27.76 ? 78  ILE A CB  1 
ATOM   626  C  CG1 . ILE A 1 78  ? 16.276 -27.311 16.574  1.00 21.43 ? 78  ILE A CG1 1 
ATOM   627  C  CG2 . ILE A 1 78  ? 14.748 -28.715 17.995  1.00 27.06 ? 78  ILE A CG2 1 
ATOM   628  C  CD1 . ILE A 1 78  ? 16.590 -28.376 15.498  1.00 25.28 ? 78  ILE A CD1 1 
ATOM   629  N  N   . GLY A 1 79  ? 17.276 -24.726 19.185  1.00 23.34 ? 79  GLY A N   1 
ATOM   630  C  CA  . GLY A 1 79  ? 18.498 -23.968 19.416  1.00 19.59 ? 79  GLY A CA  1 
ATOM   631  C  C   . GLY A 1 79  ? 18.205 -22.484 19.335  1.00 24.00 ? 79  GLY A C   1 
ATOM   632  O  O   . GLY A 1 79  ? 17.163 -22.059 18.826  1.00 22.94 ? 79  GLY A O   1 
ATOM   633  N  N   . HIS A 1 80  ? 19.126 -21.702 19.887  1.00 22.54 ? 80  HIS A N   1 
ATOM   634  C  CA  . HIS A 1 80  ? 18.964 -20.256 19.856  1.00 23.32 ? 80  HIS A CA  1 
ATOM   635  C  C   . HIS A 1 80  ? 20.323 -19.582 19.980  1.00 27.39 ? 80  HIS A C   1 
ATOM   636  O  O   . HIS A 1 80  ? 21.231 -20.085 20.649  1.00 26.90 ? 80  HIS A O   1 
ATOM   637  C  CB  . HIS A 1 80  ? 17.995 -19.783 20.945  1.00 26.00 ? 80  HIS A CB  1 
ATOM   638  C  CG  . HIS A 1 80  ? 18.526 -19.926 22.335  1.00 25.22 ? 80  HIS A CG  1 
ATOM   639  N  ND1 . HIS A 1 80  ? 18.366 -21.085 23.066  1.00 24.79 ? 80  HIS A ND1 1 
ATOM   640  C  CD2 . HIS A 1 80  ? 19.195 -19.063 23.136  1.00 25.51 ? 80  HIS A CD2 1 
ATOM   641  C  CE1 . HIS A 1 80  ? 18.915 -20.930 24.260  1.00 31.08 ? 80  HIS A CE1 1 
ATOM   642  N  NE2 . HIS A 1 80  ? 19.422 -19.712 24.329  1.00 28.26 ? 80  HIS A NE2 1 
ATOM   643  N  N   . SER A 1 81  ? 20.448 -18.442 19.310  1.00 25.80 ? 81  SER A N   1 
ATOM   644  C  CA  . SER A 1 81  ? 21.655 -17.637 19.388  1.00 21.53 ? 81  SER A CA  1 
ATOM   645  C  C   . SER A 1 81  ? 21.291 -16.187 19.129  1.00 24.78 ? 81  SER A C   1 
ATOM   646  O  O   . SER A 1 81  ? 20.254 -15.875 18.537  1.00 25.14 ? 81  SER A O   1 
ATOM   647  C  CB  . SER A 1 81  ? 22.713 -18.078 18.378  1.00 29.39 ? 81  SER A CB  1 
ATOM   648  O  OG  . SER A 1 81  ? 22.208 -17.948 17.064  1.00 27.45 ? 81  SER A OG  1 
ATOM   649  N  N   . MET A 1 82  ? 22.154 -15.305 19.600  1.00 23.39 ? 82  MET A N   1 
ATOM   650  C  CA  . MET A 1 82  ? 22.026 -13.878 19.367  1.00 25.90 ? 82  MET A CA  1 
ATOM   651  C  C   . MET A 1 82  ? 23.043 -13.421 18.330  1.00 20.31 ? 82  MET A C   1 
ATOM   652  O  O   . MET A 1 82  ? 24.231 -13.735 18.430  1.00 25.38 ? 82  MET A O   1 
ATOM   653  C  CB  . MET A 1 82  ? 22.169 -13.125 20.695  1.00 25.87 ? 82  MET A CB  1 
ATOM   654  C  CG  . MET A 1 82  ? 21.921 -11.655 20.608  1.00 23.61 ? 82  MET A CG  1 
ATOM   655  S  SD  . MET A 1 82  ? 21.909 -10.911 22.245  1.00 24.66 ? 82  MET A SD  1 
ATOM   656  C  CE  . MET A 1 82  ? 23.605 -11.153 22.785  1.00 21.97 ? 82  MET A CE  1 
ATOM   657  N  N   . GLN A 1 83  ? 22.554 -12.727 17.306  1.00 21.32 ? 83  GLN A N   1 
ATOM   658  C  CA  . GLN A 1 83  ? 23.385 -12.118 16.271  1.00 20.95 ? 83  GLN A CA  1 
ATOM   659  C  C   . GLN A 1 83  ? 23.100 -10.628 16.315  1.00 18.47 ? 83  GLN A C   1 
ATOM   660  O  O   . GLN A 1 83  ? 22.007 -10.192 15.927  1.00 19.86 ? 83  GLN A O   1 
ATOM   661  C  CB  . GLN A 1 83  ? 23.060 -12.690 14.892  1.00 24.12 ? 83  GLN A CB  1 
ATOM   662  C  CG  . GLN A 1 83  ? 23.444 -11.777 13.713  1.00 34.30 ? 83  GLN A CG  1 
ATOM   663  C  CD  . GLN A 1 83  ? 23.668 -12.544 12.418  1.00 29.65 ? 83  GLN A CD  1 
ATOM   664  O  OE1 . GLN A 1 83  ? 22.802 -13.317 12.007  1.00 31.10 ? 83  GLN A OE1 1 
ATOM   665  N  NE2 . GLN A 1 83  ? 24.777 -12.273 11.728  1.00 34.04 ? 83  GLN A NE2 1 
ATOM   666  N  N   . ASN A 1 84  ? 24.059 -9.847  16.817  1.00 18.15 ? 84  ASN A N   1 
ATOM   667  C  CA  . ASN A 1 84  ? 23.815 -8.415  16.975  1.00 17.93 ? 84  ASN A CA  1 
ATOM   668  C  C   . ASN A 1 84  ? 22.507 -8.202  17.745  1.00 18.12 ? 84  ASN A C   1 
ATOM   669  O  O   . ASN A 1 84  ? 22.363 -8.728  18.861  1.00 22.24 ? 84  ASN A O   1 
ATOM   670  C  CB  . ASN A 1 84  ? 23.837 -7.738  15.606  1.00 22.57 ? 84  ASN A CB  1 
ATOM   671  C  CG  . ASN A 1 84  ? 25.153 -7.977  14.884  1.00 27.15 ? 84  ASN A CG  1 
ATOM   672  O  OD1 . ASN A 1 84  ? 26.219 -7.758  15.459  1.00 26.14 ? 84  ASN A OD1 1 
ATOM   673  N  ND2 . ASN A 1 84  ? 25.090 -8.438  13.630  1.00 23.82 ? 84  ASN A ND2 1 
ATOM   674  N  N   . CYS A 1 85  ? 21.536 -7.468  17.200  1.00 19.09 ? 85  CYS A N   1 
ATOM   675  C  CA  . CYS A 1 85  ? 20.327 -7.182  17.967  1.00 18.05 ? 85  CYS A CA  1 
ATOM   676  C  C   . CYS A 1 85  ? 19.143 -8.091  17.614  1.00 19.30 ? 85  CYS A C   1 
ATOM   677  O  O   . CYS A 1 85  ? 18.001 -7.763  17.939  1.00 20.70 ? 85  CYS A O   1 
ATOM   678  C  CB  . CYS A 1 85  ? 19.925 -5.720  17.817  1.00 17.38 ? 85  CYS A CB  1 
ATOM   679  S  SG  . CYS A 1 85  ? 21.191 -4.597  18.390  1.00 20.64 ? 85  CYS A SG  1 
ATOM   680  N  N   A VAL A 1 86  ? 19.399 -9.245  17.004  0.48 19.37 ? 86  VAL A N   1 
ATOM   681  N  N   B VAL A 1 86  ? 19.382 -9.223  16.966  0.52 19.36 ? 86  VAL A N   1 
ATOM   682  C  CA  A VAL A 1 86  ? 18.346 -10.173 16.609  0.48 18.85 ? 86  VAL A CA  1 
ATOM   683  C  CA  B VAL A 1 86  ? 18.282 -10.136 16.692  0.52 18.82 ? 86  VAL A CA  1 
ATOM   684  C  C   A VAL A 1 86  ? 18.604 -11.532 17.242  0.48 21.15 ? 86  VAL A C   1 
ATOM   685  C  C   B VAL A 1 86  ? 18.592 -11.485 17.318  0.52 21.20 ? 86  VAL A C   1 
ATOM   686  O  O   A VAL A 1 86  ? 19.759 -11.954 17.383  0.48 21.49 ? 86  VAL A O   1 
ATOM   687  O  O   B VAL A 1 86  ? 19.753 -11.846 17.545  0.52 21.17 ? 86  VAL A O   1 
ATOM   688  C  CB  A VAL A 1 86  ? 18.260 -10.299 15.073  0.48 18.52 ? 86  VAL A CB  1 
ATOM   689  C  CB  B VAL A 1 86  ? 17.990 -10.292 15.183  0.52 18.11 ? 86  VAL A CB  1 
ATOM   690  C  CG1 A VAL A 1 86  ? 17.944 -11.731 14.670  0.48 23.41 ? 86  VAL A CG1 1 
ATOM   691  C  CG1 B VAL A 1 86  ? 17.362 -9.006  14.609  0.52 22.35 ? 86  VAL A CG1 1 
ATOM   692  C  CG2 A VAL A 1 86  ? 17.234 -9.314  14.500  0.48 22.96 ? 86  VAL A CG2 1 
ATOM   693  C  CG2 B VAL A 1 86  ? 19.239 -10.694 14.418  0.52 21.09 ? 86  VAL A CG2 1 
ATOM   694  N  N   . LEU A 1 87  ? 17.525 -12.213 17.627  1.00 20.75 ? 87  LEU A N   1 
ATOM   695  C  CA  . LEU A 1 87  ? 17.586 -13.593 18.084  1.00 20.90 ? 87  LEU A CA  1 
ATOM   696  C  C   . LEU A 1 87  ? 17.264 -14.509 16.909  1.00 24.78 ? 87  LEU A C   1 
ATOM   697  O  O   . LEU A 1 87  ? 16.351 -14.231 16.120  1.00 24.70 ? 87  LEU A O   1 
ATOM   698  C  CB  . LEU A 1 87  ? 16.586 -13.834 19.219  1.00 19.40 ? 87  LEU A CB  1 
ATOM   699  C  CG  . LEU A 1 87  ? 16.931 -13.278 20.591  1.00 29.50 ? 87  LEU A CG  1 
ATOM   700  C  CD1 . LEU A 1 87  ? 15.919 -13.774 21.627  1.00 32.73 ? 87  LEU A CD1 1 
ATOM   701  C  CD2 . LEU A 1 87  ? 18.342 -13.687 20.996  1.00 31.14 ? 87  LEU A CD2 1 
ATOM   702  N  N   . LYS A 1 88  ? 18.023 -15.589 16.786  1.00 20.52 ? 88  LYS A N   1 
ATOM   703  C  CA  . LYS A 1 88  ? 17.792 -16.620 15.780  1.00 18.79 ? 88  LYS A CA  1 
ATOM   704  C  C   . LYS A 1 88  ? 17.390 -17.910 16.489  1.00 23.31 ? 88  LYS A C   1 
ATOM   705  O  O   . LYS A 1 88  ? 18.216 -18.540 17.156  1.00 27.83 ? 88  LYS A O   1 
ATOM   706  C  CB  . LYS A 1 88  ? 19.036 -16.816 14.920  1.00 22.82 ? 88  LYS A CB  1 
ATOM   707  C  CG  . LYS A 1 88  ? 19.431 -15.529 14.180  1.00 21.32 ? 88  LYS A CG  1 
ATOM   708  C  CD  . LYS A 1 88  ? 20.465 -15.809 13.116  1.00 32.00 ? 88  LYS A CD  1 
ATOM   709  C  CE  . LYS A 1 88  ? 21.756 -16.282 13.750  1.00 33.27 ? 88  LYS A CE  1 
ATOM   710  N  NZ  . LYS A 1 88  ? 22.852 -16.312 12.760  1.00 38.35 ? 88  LYS A NZ  1 
ATOM   711  N  N   . LEU A 1 89  ? 16.126 -18.316 16.323  1.00 20.97 ? 89  LEU A N   1 
ATOM   712  C  CA  . LEU A 1 89  ? 15.609 -19.539 16.937  1.00 16.83 ? 89  LEU A CA  1 
ATOM   713  C  C   . LEU A 1 89  ? 15.589 -20.641 15.883  1.00 23.19 ? 89  LEU A C   1 
ATOM   714  O  O   . LEU A 1 89  ? 14.849 -20.556 14.898  1.00 25.75 ? 89  LEU A O   1 
ATOM   715  C  CB  . LEU A 1 89  ? 14.215 -19.304 17.513  1.00 17.88 ? 89  LEU A CB  1 
ATOM   716  C  CG  . LEU A 1 89  ? 14.126 -18.072 18.414  1.00 21.44 ? 89  LEU A CG  1 
ATOM   717  C  CD1 . LEU A 1 89  ? 12.686 -17.843 18.832  1.00 27.10 ? 89  LEU A CD1 1 
ATOM   718  C  CD2 . LEU A 1 89  ? 15.040 -18.209 19.640  1.00 24.30 ? 89  LEU A CD2 1 
ATOM   719  N  N   . LYS A 1 90  ? 16.414 -21.667 16.085  1.00 20.15 ? 90  LYS A N   1 
ATOM   720  C  CA  . LYS A 1 90  ? 16.402 -22.856 15.243  1.00 21.26 ? 90  LYS A CA  1 
ATOM   721  C  C   . LYS A 1 90  ? 15.211 -23.729 15.626  1.00 23.40 ? 90  LYS A C   1 
ATOM   722  O  O   . LYS A 1 90  ? 15.029 -24.068 16.800  1.00 20.65 ? 90  LYS A O   1 
ATOM   723  C  CB  . LYS A 1 90  ? 17.719 -23.622 15.418  1.00 21.88 ? 90  LYS A CB  1 
ATOM   724  C  CG  . LYS A 1 90  ? 17.965 -24.753 14.432  1.00 27.17 ? 90  LYS A CG  1 
ATOM   725  C  CD  . LYS A 1 90  ? 18.071 -24.263 12.995  1.00 32.06 ? 90  LYS A CD  1 
ATOM   726  C  CE  . LYS A 1 90  ? 19.245 -24.946 12.282  1.00 40.55 ? 90  LYS A CE  1 
ATOM   727  N  NZ  . LYS A 1 90  ? 19.746 -24.156 11.109  1.00 38.63 ? 90  LYS A NZ  1 
ATOM   728  N  N   . VAL A 1 91  ? 14.373 -24.062 14.646  1.00 23.72 ? 91  VAL A N   1 
ATOM   729  C  CA  . VAL A 1 91  ? 13.183 -24.869 14.896  1.00 19.35 ? 91  VAL A CA  1 
ATOM   730  C  C   . VAL A 1 91  ? 13.367 -26.186 14.159  1.00 26.32 ? 91  VAL A C   1 
ATOM   731  O  O   . VAL A 1 91  ? 14.255 -26.323 13.314  1.00 25.01 ? 91  VAL A O   1 
ATOM   732  C  CB  . VAL A 1 91  ? 11.881 -24.158 14.463  1.00 22.47 ? 91  VAL A CB  1 
ATOM   733  C  CG1 . VAL A 1 91  ? 11.563 -23.021 15.413  1.00 22.30 ? 91  VAL A CG1 1 
ATOM   734  C  CG2 . VAL A 1 91  ? 11.990 -23.628 13.021  1.00 20.39 ? 91  VAL A CG2 1 
ATOM   735  N  N   . ASP A 1 92  ? 12.542 -27.180 14.499  1.00 22.14 ? 92  ASP A N   1 
ATOM   736  C  CA  . ASP A 1 92  ? 12.789 -28.500 13.913  1.00 29.26 ? 92  ASP A CA  1 
ATOM   737  C  C   . ASP A 1 92  ? 12.064 -28.708 12.579  1.00 29.62 ? 92  ASP A C   1 
ATOM   738  O  O   . ASP A 1 92  ? 12.112 -29.811 12.025  1.00 30.29 ? 92  ASP A O   1 
ATOM   739  C  CB  . ASP A 1 92  ? 12.401 -29.614 14.891  1.00 25.40 ? 92  ASP A CB  1 
ATOM   740  C  CG  . ASP A 1 92  ? 10.907 -29.748 15.071  1.00 29.28 ? 92  ASP A CG  1 
ATOM   741  O  OD1 . ASP A 1 92  ? 10.155 -28.806 14.749  1.00 35.44 ? 92  ASP A OD1 1 
ATOM   742  O  OD2 . ASP A 1 92  ? 10.490 -30.815 15.574  1.00 38.13 ? 92  ASP A OD2 1 
ATOM   743  N  N   . THR A 1 93  ? 11.400 -27.684 12.052  1.00 23.36 ? 93  THR A N   1 
ATOM   744  C  CA  . THR A 1 93  ? 10.645 -27.787 10.810  1.00 27.99 ? 93  THR A CA  1 
ATOM   745  C  C   . THR A 1 93  ? 10.990 -26.605 9.923   1.00 25.37 ? 93  THR A C   1 
ATOM   746  O  O   . THR A 1 93  ? 10.968 -25.463 10.387  1.00 24.02 ? 93  THR A O   1 
ATOM   747  C  CB  . THR A 1 93  ? 9.134  -27.816 11.081  1.00 22.86 ? 93  THR A CB  1 
ATOM   748  O  OG1 . THR A 1 93  ? 8.820  -28.948 11.899  1.00 30.71 ? 93  THR A OG1 1 
ATOM   749  C  CG2 . THR A 1 93  ? 8.351  -27.901 9.786   1.00 30.22 ? 93  THR A CG2 1 
ATOM   750  N  N   . ALA A 1 94  ? 11.324 -26.890 8.664   1.00 23.68 ? 94  ALA A N   1 
ATOM   751  C  CA  . ALA A 1 94  ? 11.497 -25.850 7.665   1.00 24.57 ? 94  ALA A CA  1 
ATOM   752  C  C   . ALA A 1 94  ? 10.143 -25.277 7.276   1.00 24.24 ? 94  ALA A C   1 
ATOM   753  O  O   . ALA A 1 94  ? 9.178  -26.020 7.088   1.00 26.16 ? 94  ALA A O   1 
ATOM   754  C  CB  . ALA A 1 94  ? 12.190 -26.422 6.428   1.00 25.30 ? 94  ALA A CB  1 
ATOM   755  N  N   . ASN A 1 95  ? 10.063 -23.942 7.172   1.00 20.59 ? 95  ASN A N   1 
ATOM   756  C  CA  . ASN A 1 95  ? 8.814  -23.320 6.749   1.00 21.83 ? 95  ASN A CA  1 
ATOM   757  C  C   . ASN A 1 95  ? 8.474  -23.781 5.339   1.00 23.65 ? 95  ASN A C   1 
ATOM   758  O  O   . ASN A 1 95  ? 9.211  -23.474 4.406   1.00 22.07 ? 95  ASN A O   1 
ATOM   759  C  CB  . ASN A 1 95  ? 8.904  -21.788 6.818   1.00 19.19 ? 95  ASN A CB  1 
ATOM   760  C  CG  . ASN A 1 95  ? 7.586  -21.108 6.459   1.00 21.74 ? 95  ASN A CG  1 
ATOM   761  O  OD1 . ASN A 1 95  ? 6.603  -21.778 6.138   1.00 21.91 ? 95  ASN A OD1 1 
ATOM   762  N  ND2 . ASN A 1 95  ? 7.550  -19.780 6.556   1.00 21.08 ? 95  ASN A ND2 1 
ATOM   763  N  N   . PRO A 1 96  ? 7.380  -24.522 5.141   1.00 23.81 ? 96  PRO A N   1 
ATOM   764  C  CA  . PRO A 1 96  ? 7.029  -24.943 3.773   1.00 26.09 ? 96  PRO A CA  1 
ATOM   765  C  C   . PRO A 1 96  ? 6.701  -23.779 2.857   1.00 25.99 ? 96  PRO A C   1 
ATOM   766  O  O   . PRO A 1 96  ? 6.731  -23.935 1.627   1.00 32.16 ? 96  PRO A O   1 
ATOM   767  C  CB  . PRO A 1 96  ? 5.820  -25.864 3.987   1.00 30.34 ? 96  PRO A CB  1 
ATOM   768  C  CG  . PRO A 1 96  ? 5.241  -25.456 5.289   1.00 25.48 ? 96  PRO A CG  1 
ATOM   769  C  CD  . PRO A 1 96  ? 6.398  -24.975 6.139   1.00 24.65 ? 96  PRO A CD  1 
ATOM   770  N  N   . LYS A 1 97  ? 6.414  -22.613 3.418   1.00 24.37 ? 97  LYS A N   1 
ATOM   771  C  CA  . LYS A 1 97  ? 6.038  -21.438 2.649   1.00 28.25 ? 97  LYS A CA  1 
ATOM   772  C  C   . LYS A 1 97  ? 7.218  -20.501 2.425   1.00 26.13 ? 97  LYS A C   1 
ATOM   773  O  O   . LYS A 1 97  ? 7.014  -19.339 2.069   1.00 29.54 ? 97  LYS A O   1 
ATOM   774  C  CB  . LYS A 1 97  ? 4.902  -20.701 3.369   1.00 30.34 ? 97  LYS A CB  1 
ATOM   775  C  CG  . LYS A 1 97  ? 3.574  -21.457 3.354   1.00 35.08 ? 97  LYS A CG  1 
ATOM   776  C  CD  . LYS A 1 97  ? 2.448  -20.659 4.013   1.00 39.06 ? 97  LYS A CD  1 
ATOM   777  C  CE  . LYS A 1 97  ? 1.349  -21.587 4.519   1.00 54.79 ? 97  LYS A CE  1 
ATOM   778  N  NZ  . LYS A 1 97  ? 0.688  -21.087 5.758   1.00 52.00 ? 97  LYS A NZ  1 
ATOM   779  N  N   . THR A 1 98  ? 8.439  -20.968 2.648   1.00 23.13 ? 98  THR A N   1 
ATOM   780  C  CA  . THR A 1 98  ? 9.597  -20.099 2.483   1.00 27.67 ? 98  THR A CA  1 
ATOM   781  C  C   . THR A 1 98  ? 9.745  -19.673 1.020   1.00 23.29 ? 98  THR A C   1 
ATOM   782  O  O   . THR A 1 98  ? 9.815  -20.546 0.128   1.00 26.00 ? 98  THR A O   1 
ATOM   783  C  CB  . THR A 1 98  ? 10.871 -20.795 2.946   1.00 24.81 ? 98  THR A CB  1 
ATOM   784  O  OG1 . THR A 1 98  ? 10.731 -21.199 4.318   1.00 23.43 ? 98  THR A OG1 1 
ATOM   785  C  CG2 . THR A 1 98  ? 12.042 -19.835 2.835   1.00 28.29 ? 98  THR A CG2 1 
ATOM   786  N  N   . PRO A 1 99  ? 9.800  -18.372 0.727   1.00 26.31 ? 99  PRO A N   1 
ATOM   787  C  CA  . PRO A 1 99  ? 10.078 -17.912 -0.638  1.00 30.27 ? 99  PRO A CA  1 
ATOM   788  C  C   . PRO A 1 99  ? 11.574 -17.912 -0.897  1.00 28.66 ? 99  PRO A C   1 
ATOM   789  O  O   . PRO A 1 99  ? 12.382 -17.983 0.025   1.00 27.29 ? 99  PRO A O   1 
ATOM   790  C  CB  . PRO A 1 99  ? 9.552  -16.472 -0.632  1.00 22.62 ? 99  PRO A CB  1 
ATOM   791  C  CG  . PRO A 1 99  ? 9.839  -16.019 0.782   1.00 25.67 ? 99  PRO A CG  1 
ATOM   792  C  CD  . PRO A 1 99  ? 9.613  -17.241 1.656   1.00 24.06 ? 99  PRO A CD  1 
ATOM   793  N  N   . LYS A 1 100 ? 11.938 -17.787 -2.176  1.00 27.33 ? 100 LYS A N   1 
ATOM   794  C  CA  . LYS A 1 100 ? 13.299 -17.369 -2.484  1.00 31.34 ? 100 LYS A CA  1 
ATOM   795  C  C   . LYS A 1 100 ? 13.553 -16.052 -1.761  1.00 28.93 ? 100 LYS A C   1 
ATOM   796  O  O   . LYS A 1 100 ? 12.693 -15.167 -1.741  1.00 24.49 ? 100 LYS A O   1 
ATOM   797  C  CB  . LYS A 1 100 ? 13.500 -17.230 -4.004  1.00 27.75 ? 100 LYS A CB  1 
ATOM   798  C  CG  . LYS A 1 100 ? 13.048 -18.452 -4.764  1.00 44.84 ? 100 LYS A CG  1 
ATOM   799  N  N   . TYR A 1 101 ? 14.698 -15.939 -1.101  1.00 22.82 ? 101 TYR A N   1 
ATOM   800  C  CA  . TYR A 1 101 ? 14.920 -14.742 -0.309  1.00 24.03 ? 101 TYR A CA  1 
ATOM   801  C  C   . TYR A 1 101 ? 16.407 -14.487 -0.154  1.00 27.12 ? 101 TYR A C   1 
ATOM   802  O  O   . TYR A 1 101 ? 17.252 -15.354 -0.405  1.00 29.62 ? 101 TYR A O   1 
ATOM   803  C  CB  . TYR A 1 101 ? 14.272 -14.857 1.076   1.00 24.26 ? 101 TYR A CB  1 
ATOM   804  C  CG  . TYR A 1 101 ? 15.020 -15.761 2.033   1.00 26.09 ? 101 TYR A CG  1 
ATOM   805  C  CD1 . TYR A 1 101 ? 14.739 -17.120 2.100   1.00 25.08 ? 101 TYR A CD1 1 
ATOM   806  C  CD2 . TYR A 1 101 ? 15.984 -15.244 2.893   1.00 27.94 ? 101 TYR A CD2 1 
ATOM   807  C  CE1 . TYR A 1 101 ? 15.419 -17.952 2.975   1.00 25.57 ? 101 TYR A CE1 1 
ATOM   808  C  CE2 . TYR A 1 101 ? 16.664 -16.067 3.789   1.00 34.81 ? 101 TYR A CE2 1 
ATOM   809  C  CZ  . TYR A 1 101 ? 16.374 -17.420 3.825   1.00 30.76 ? 101 TYR A CZ  1 
ATOM   810  O  OH  . TYR A 1 101 ? 17.042 -18.245 4.708   1.00 31.01 ? 101 TYR A OH  1 
ATOM   811  N  N   . LYS A 1 102 ? 16.705 -13.262 0.259   1.00 28.55 ? 102 LYS A N   1 
ATOM   812  C  CA  . LYS A 1 102 ? 18.036 -12.859 0.673   1.00 25.71 ? 102 LYS A CA  1 
ATOM   813  C  C   . LYS A 1 102 ? 17.895 -11.698 1.649   1.00 28.97 ? 102 LYS A C   1 
ATOM   814  O  O   . LYS A 1 102 ? 16.830 -11.086 1.771   1.00 26.85 ? 102 LYS A O   1 
ATOM   815  C  CB  . LYS A 1 102 ? 18.914 -12.518 -0.539  1.00 34.05 ? 102 LYS A CB  1 
ATOM   816  C  CG  . LYS A 1 102 ? 18.818 -11.107 -1.101  1.00 31.24 ? 102 LYS A CG  1 
ATOM   817  C  CD  . LYS A 1 102 ? 19.394 -11.135 -2.534  1.00 35.08 ? 102 LYS A CD  1 
ATOM   818  C  CE  . LYS A 1 102 ? 18.847 -10.051 -3.457  1.00 44.49 ? 102 LYS A CE  1 
ATOM   819  N  NZ  . LYS A 1 102 ? 18.954 -8.670  -2.920  1.00 52.32 ? 102 LYS A NZ  1 
ATOM   820  N  N   . PHE A 1 103 ? 18.962 -11.451 2.394   1.00 25.34 ? 103 PHE A N   1 
ATOM   821  C  CA  . PHE A 1 103 ? 19.021 -10.327 3.318   1.00 24.55 ? 103 PHE A CA  1 
ATOM   822  C  C   . PHE A 1 103 ? 19.887 -9.239  2.698   1.00 27.76 ? 103 PHE A C   1 
ATOM   823  O  O   . PHE A 1 103 ? 20.989 -9.522  2.207   1.00 26.56 ? 103 PHE A O   1 
ATOM   824  C  CB  . PHE A 1 103 ? 19.592 -10.739 4.680   1.00 19.23 ? 103 PHE A CB  1 
ATOM   825  C  CG  . PHE A 1 103 ? 18.764 -11.746 5.442   1.00 25.42 ? 103 PHE A CG  1 
ATOM   826  C  CD1 . PHE A 1 103 ? 17.442 -12.002 5.117   1.00 23.45 ? 103 PHE A CD1 1 
ATOM   827  C  CD2 . PHE A 1 103 ? 19.303 -12.377 6.559   1.00 27.34 ? 103 PHE A CD2 1 
ATOM   828  C  CE1 . PHE A 1 103 ? 16.693 -12.905 5.868   1.00 24.57 ? 103 PHE A CE1 1 
ATOM   829  C  CE2 . PHE A 1 103 ? 18.569 -13.277 7.299   1.00 29.71 ? 103 PHE A CE2 1 
ATOM   830  C  CZ  . PHE A 1 103 ? 17.253 -13.536 6.964   1.00 25.93 ? 103 PHE A CZ  1 
ATOM   831  N  N   . VAL A 1 104 ? 19.385 -8.004  2.694   1.00 21.53 ? 104 VAL A N   1 
ATOM   832  C  CA  . VAL A 1 104 ? 20.139 -6.870  2.174   1.00 20.63 ? 104 VAL A CA  1 
ATOM   833  C  C   . VAL A 1 104 ? 20.064 -5.727  3.173   1.00 25.00 ? 104 VAL A C   1 
ATOM   834  O  O   . VAL A 1 104 ? 19.056 -5.551  3.867   1.00 30.07 ? 104 VAL A O   1 
ATOM   835  C  CB  . VAL A 1 104 ? 19.641 -6.413  0.790   1.00 34.11 ? 104 VAL A CB  1 
ATOM   836  C  CG1 . VAL A 1 104 ? 19.491 -7.615  -0.135  1.00 31.17 ? 104 VAL A CG1 1 
ATOM   837  C  CG2 . VAL A 1 104 ? 18.336 -5.653  0.929   1.00 33.03 ? 104 VAL A CG2 1 
ATOM   838  N  N   . ARG A 1 105 ? 21.158 -4.984  3.274   1.00 27.04 ? 105 ARG A N   1 
ATOM   839  C  CA  . ARG A 1 105 ? 21.206 -3.734  4.015   1.00 23.87 ? 105 ARG A CA  1 
ATOM   840  C  C   . ARG A 1 105 ? 21.075 -2.603  3.009   1.00 20.75 ? 105 ARG A C   1 
ATOM   841  O  O   . ARG A 1 105 ? 21.918 -2.460  2.117   1.00 30.33 ? 105 ARG A O   1 
ATOM   842  C  CB  . ARG A 1 105 ? 22.511 -3.603  4.799   1.00 26.06 ? 105 ARG A CB  1 
ATOM   843  C  CG  . ARG A 1 105 ? 22.476 -2.469  5.818   1.00 25.34 ? 105 ARG A CG  1 
ATOM   844  C  CD  . ARG A 1 105 ? 23.759 -2.429  6.645   1.00 29.00 ? 105 ARG A CD  1 
ATOM   845  N  NE  . ARG A 1 105 ? 23.792 -1.244  7.494   1.00 33.70 ? 105 ARG A NE  1 
ATOM   846  C  CZ  . ARG A 1 105 ? 23.149 -1.139  8.649   1.00 27.10 ? 105 ARG A CZ  1 
ATOM   847  N  NH1 . ARG A 1 105 ? 22.435 -2.140  9.133   1.00 24.00 ? 105 ARG A NH1 1 
ATOM   848  N  NH2 . ARG A 1 105 ? 23.219 0.002   9.329   1.00 25.54 ? 105 ARG A NH2 1 
ATOM   849  N  N   . ILE A 1 106 ? 20.021 -1.812  3.147   1.00 23.79 ? 106 ILE A N   1 
ATOM   850  C  CA  . ILE A 1 106 ? 19.718 -0.777  2.172   1.00 25.29 ? 106 ILE A CA  1 
ATOM   851  C  C   . ILE A 1 106 ? 20.379 0.533   2.577   1.00 30.73 ? 106 ILE A C   1 
ATOM   852  O  O   . ILE A 1 106 ? 20.790 0.734   3.720   1.00 25.49 ? 106 ILE A O   1 
ATOM   853  C  CB  . ILE A 1 106 ? 18.196 -0.591  1.994   1.00 22.63 ? 106 ILE A CB  1 
ATOM   854  C  CG1 . ILE A 1 106 ? 17.538 -0.207  3.330   1.00 22.92 ? 106 ILE A CG1 1 
ATOM   855  C  CG2 . ILE A 1 106 ? 17.546 -1.831  1.363   1.00 25.11 ? 106 ILE A CG2 1 
ATOM   856  C  CD1 . ILE A 1 106 ? 16.105 0.319   3.159   1.00 20.70 ? 106 ILE A CD1 1 
ATOM   857  N  N   . GLN A 1 107 ? 20.486 1.426   1.616   1.00 27.53 ? 107 GLN A N   1 
ATOM   858  C  CA  . GLN A 1 107 ? 21.042 2.758   1.787   1.00 27.44 ? 107 GLN A CA  1 
ATOM   859  C  C   . GLN A 1 107 ? 19.931 3.754   2.070   1.00 26.29 ? 107 GLN A C   1 
ATOM   860  O  O   . GLN A 1 107 ? 18.783 3.549   1.668   1.00 25.16 ? 107 GLN A O   1 
ATOM   861  C  CB  . GLN A 1 107 ? 21.789 3.180   0.519   1.00 33.81 ? 107 GLN A CB  1 
ATOM   862  C  CG  . GLN A 1 107 ? 22.942 2.268   0.131   1.00 48.35 ? 107 GLN A CG  1 
ATOM   863  C  CD  . GLN A 1 107 ? 24.135 2.423   1.054   1.00 50.54 ? 107 GLN A CD  1 
ATOM   864  O  OE1 . GLN A 1 107 ? 24.401 3.511   1.565   1.00 53.07 ? 107 GLN A OE1 1 
ATOM   865  N  NE2 . GLN A 1 107 ? 24.866 1.335   1.266   1.00 58.43 ? 107 GLN A NE2 1 
ATOM   866  N  N   . PRO A 1 108 ? 20.236 4.866   2.732   1.00 26.20 ? 108 PRO A N   1 
ATOM   867  C  CA  . PRO A 1 108 ? 19.219 5.910   2.890   1.00 27.79 ? 108 PRO A CA  1 
ATOM   868  C  C   . PRO A 1 108 ? 18.736 6.363   1.524   1.00 27.30 ? 108 PRO A C   1 
ATOM   869  O  O   . PRO A 1 108 ? 19.501 6.410   0.559   1.00 28.24 ? 108 PRO A O   1 
ATOM   870  C  CB  . PRO A 1 108 ? 19.959 7.033   3.631   1.00 34.47 ? 108 PRO A CB  1 
ATOM   871  C  CG  . PRO A 1 108 ? 21.151 6.367   4.265   1.00 39.07 ? 108 PRO A CG  1 
ATOM   872  C  CD  . PRO A 1 108 ? 21.532 5.245   3.319   1.00 29.83 ? 108 PRO A CD  1 
ATOM   873  N  N   . GLY A 1 109 ? 17.454 6.685   1.441   1.00 23.50 ? 109 GLY A N   1 
ATOM   874  C  CA  . GLY A 1 109 ? 16.831 7.009   0.182   1.00 26.22 ? 109 GLY A CA  1 
ATOM   875  C  C   . GLY A 1 109 ? 16.112 5.851   -0.476  1.00 30.97 ? 109 GLY A C   1 
ATOM   876  O  O   . GLY A 1 109 ? 15.180 6.082   -1.255  1.00 30.03 ? 109 GLY A O   1 
ATOM   877  N  N   . GLN A 1 110 ? 16.507 4.618   -0.189  1.00 24.80 ? 110 GLN A N   1 
ATOM   878  C  CA  . GLN A 1 110 ? 15.807 3.496   -0.782  1.00 23.15 ? 110 GLN A CA  1 
ATOM   879  C  C   . GLN A 1 110 ? 14.503 3.198   -0.060  1.00 18.28 ? 110 GLN A C   1 
ATOM   880  O  O   . GLN A 1 110 ? 14.349 3.428   1.140   1.00 21.82 ? 110 GLN A O   1 
ATOM   881  C  CB  . GLN A 1 110 ? 16.687 2.238   -0.864  1.00 32.25 ? 110 GLN A CB  1 
ATOM   882  C  CG  . GLN A 1 110 ? 18.179 2.503   -1.105  1.00 40.69 ? 110 GLN A CG  1 
ATOM   883  C  CD  . GLN A 1 110 ? 18.937 1.243   -1.542  1.00 44.88 ? 110 GLN A CD  1 
ATOM   884  O  OE1 . GLN A 1 110 ? 19.808 0.734   -0.831  1.00 31.78 ? 110 GLN A OE1 1 
ATOM   885  N  NE2 . GLN A 1 110 ? 18.597 0.738   -2.723  1.00 57.69 ? 110 GLN A NE2 1 
ATOM   886  N  N   . THR A 1 111 ? 13.541 2.732   -0.844  1.00 22.60 ? 111 THR A N   1 
ATOM   887  C  CA  . THR A 1 111 ? 12.186 2.444   -0.409  1.00 23.10 ? 111 THR A CA  1 
ATOM   888  C  C   . THR A 1 111 ? 12.011 0.940   -0.246  1.00 23.77 ? 111 THR A C   1 
ATOM   889  O  O   . THR A 1 111 ? 12.783 0.135   -0.783  1.00 25.11 ? 111 THR A O   1 
ATOM   890  C  CB  . THR A 1 111 ? 11.167 2.977   -1.434  1.00 22.29 ? 111 THR A CB  1 
ATOM   891  O  OG1 . THR A 1 111 ? 11.429 2.374   -2.699  1.00 24.39 ? 111 THR A OG1 1 
ATOM   892  C  CG2 . THR A 1 111 ? 11.310 4.477   -1.589  1.00 21.91 ? 111 THR A CG2 1 
ATOM   893  N  N   . PHE A 1 112 ? 10.958 0.572   0.474   1.00 21.27 ? 112 PHE A N   1 
ATOM   894  C  CA  . PHE A 1 112 ? 10.616 -0.824  0.713   1.00 23.61 ? 112 PHE A CA  1 
ATOM   895  C  C   . PHE A 1 112 ? 9.191  -0.874  1.246   1.00 22.73 ? 112 PHE A C   1 
ATOM   896  O  O   . PHE A 1 112 ? 8.643  0.135   1.693   1.00 23.04 ? 112 PHE A O   1 
ATOM   897  C  CB  . PHE A 1 112 ? 11.604 -1.497  1.688   1.00 22.72 ? 112 PHE A CB  1 
ATOM   898  C  CG  . PHE A 1 112 ? 11.727 -0.806  3.031   1.00 24.10 ? 112 PHE A CG  1 
ATOM   899  C  CD1 . PHE A 1 112 ? 10.938 -1.192  4.110   1.00 24.78 ? 112 PHE A CD1 1 
ATOM   900  C  CD2 . PHE A 1 112 ? 12.646 0.222   3.214   1.00 22.72 ? 112 PHE A CD2 1 
ATOM   901  C  CE1 . PHE A 1 112 ? 11.056 -0.563  5.335   1.00 23.15 ? 112 PHE A CE1 1 
ATOM   902  C  CE2 . PHE A 1 112 ? 12.756 0.867   4.431   1.00 23.75 ? 112 PHE A CE2 1 
ATOM   903  C  CZ  . PHE A 1 112 ? 11.971 0.474   5.499   1.00 27.24 ? 112 PHE A CZ  1 
ATOM   904  N  N   . SER A 1 113 ? 8.590  -2.060  1.170   1.00 22.47 ? 113 SER A N   1 
ATOM   905  C  CA  . SER A 1 113 ? 7.257  -2.289  1.705   1.00 20.29 ? 113 SER A CA  1 
ATOM   906  C  C   . SER A 1 113 ? 7.372  -2.860  3.106   1.00 23.63 ? 113 SER A C   1 
ATOM   907  O  O   . SER A 1 113 ? 8.272  -3.655  3.380   1.00 21.99 ? 113 SER A O   1 
ATOM   908  C  CB  . SER A 1 113 ? 6.464  -3.256  0.822   1.00 17.43 ? 113 SER A CB  1 
ATOM   909  O  OG  . SER A 1 113 ? 6.518  -2.862  -0.559  1.00 21.90 ? 113 SER A OG  1 
ATOM   910  N  N   . VAL A 1 114 ? 6.450  -2.447  3.979   1.00 20.36 ? 114 VAL A N   1 
ATOM   911  C  CA  . VAL A 1 114 ? 6.315  -2.946  5.345   1.00 18.04 ? 114 VAL A CA  1 
ATOM   912  C  C   . VAL A 1 114 ? 5.026  -3.737  5.470   1.00 19.29 ? 114 VAL A C   1 
ATOM   913  O  O   . VAL A 1 114 ? 3.952  -3.255  5.092   1.00 21.35 ? 114 VAL A O   1 
ATOM   914  C  CB  . VAL A 1 114 ? 6.326  -1.795  6.359   1.00 20.57 ? 114 VAL A CB  1 
ATOM   915  C  CG1 . VAL A 1 114 ? 5.947  -2.315  7.725   1.00 19.02 ? 114 VAL A CG1 1 
ATOM   916  C  CG2 . VAL A 1 114 ? 7.699  -1.172  6.384   1.00 22.68 ? 114 VAL A CG2 1 
ATOM   917  N  N   . LEU A 1 115 ? 5.129  -4.931  6.043   1.00 16.06 ? 115 LEU A N   1 
ATOM   918  C  CA  . LEU A 1 115 ? 3.972  -5.732  6.409   1.00 17.38 ? 115 LEU A CA  1 
ATOM   919  C  C   . LEU A 1 115 ? 3.830  -5.590  7.919   1.00 19.33 ? 115 LEU A C   1 
ATOM   920  O  O   . LEU A 1 115 ? 4.568  -6.213  8.693   1.00 19.82 ? 115 LEU A O   1 
ATOM   921  C  CB  . LEU A 1 115 ? 4.140  -7.188  6.001   1.00 17.31 ? 115 LEU A CB  1 
ATOM   922  C  CG  . LEU A 1 115 ? 2.916  -8.078  6.231   1.00 24.48 ? 115 LEU A CG  1 
ATOM   923  C  CD1 . LEU A 1 115 ? 1.700  -7.606  5.406   1.00 24.65 ? 115 LEU A CD1 1 
ATOM   924  C  CD2 . LEU A 1 115 ? 3.240  -9.555  5.971   1.00 22.37 ? 115 LEU A CD2 1 
ATOM   925  N  N   . ALA A 1 116 ? 2.931  -4.721  8.339   1.00 20.04 ? 116 ALA A N   1 
ATOM   926  C  CA  . ALA A 1 116 ? 2.721  -4.525  9.760   1.00 17.98 ? 116 ALA A CA  1 
ATOM   927  C  C   . ALA A 1 116 ? 1.949  -5.714  10.316  1.00 21.09 ? 116 ALA A C   1 
ATOM   928  O  O   . ALA A 1 116 ? 0.899  -6.082  9.778   1.00 24.43 ? 116 ALA A O   1 
ATOM   929  C  CB  . ALA A 1 116 ? 1.968  -3.220  10.015  1.00 23.17 ? 116 ALA A CB  1 
ATOM   930  N  N   . CYS A 1 117 ? 2.473  -6.318  11.388  1.00 21.38 ? 117 CYS A N   1 
ATOM   931  C  CA  . CYS A 1 117 ? 1.868  -7.490  12.014  1.00 19.47 ? 117 CYS A CA  1 
ATOM   932  C  C   . CYS A 1 117 ? 1.737  -7.310  13.513  1.00 20.87 ? 117 CYS A C   1 
ATOM   933  O  O   . CYS A 1 117 ? 2.514  -6.595  14.150  1.00 23.53 ? 117 CYS A O   1 
ATOM   934  C  CB  . CYS A 1 117 ? 2.683  -8.766  11.780  1.00 25.46 ? 117 CYS A CB  1 
ATOM   935  S  SG  . CYS A 1 117 ? 2.899  -9.114  10.067  1.00 27.53 ? 117 CYS A SG  1 
ATOM   936  N  N   . TYR A 1 118 ? 0.787  -8.061  14.073  1.00 23.25 ? 118 TYR A N   1 
ATOM   937  C  CA  . TYR A 1 118 ? 0.489  -8.083  15.500  1.00 23.67 ? 118 TYR A CA  1 
ATOM   938  C  C   . TYR A 1 118 ? 0.135  -9.512  15.868  1.00 25.87 ? 118 TYR A C   1 
ATOM   939  O  O   . TYR A 1 118 ? -0.735 -10.111 15.233  1.00 27.11 ? 118 TYR A O   1 
ATOM   940  C  CB  . TYR A 1 118 ? -0.660 -7.118  15.851  1.00 28.97 ? 118 TYR A CB  1 
ATOM   941  C  CG  . TYR A 1 118 ? -0.319 -5.694  15.488  1.00 26.35 ? 118 TYR A CG  1 
ATOM   942  C  CD1 . TYR A 1 118 ? -0.620 -5.179  14.231  1.00 26.02 ? 118 TYR A CD1 1 
ATOM   943  C  CD2 . TYR A 1 118 ? 0.395  -4.889  16.376  1.00 27.97 ? 118 TYR A CD2 1 
ATOM   944  C  CE1 . TYR A 1 118 ? -0.256 -3.880  13.891  1.00 24.97 ? 118 TYR A CE1 1 
ATOM   945  C  CE2 . TYR A 1 118 ? 0.755  -3.592  16.046  1.00 21.87 ? 118 TYR A CE2 1 
ATOM   946  C  CZ  . TYR A 1 118 ? 0.435  -3.097  14.815  1.00 27.77 ? 118 TYR A CZ  1 
ATOM   947  O  OH  . TYR A 1 118 ? 0.804  -1.811  14.494  1.00 26.64 ? 118 TYR A OH  1 
ATOM   948  N  N   . ASN A 1 119 ? 0.831  -10.073 16.858  1.00 29.05 ? 119 ASN A N   1 
ATOM   949  C  CA  . ASN A 1 119 ? 0.620  -11.471 17.249  1.00 34.35 ? 119 ASN A CA  1 
ATOM   950  C  C   . ASN A 1 119 ? 0.862  -12.426 16.081  1.00 27.59 ? 119 ASN A C   1 
ATOM   951  O  O   . ASN A 1 119 ? 0.119  -13.390 15.881  1.00 31.84 ? 119 ASN A O   1 
ATOM   952  C  CB  . ASN A 1 119 ? -0.784 -11.685 17.819  1.00 36.85 ? 119 ASN A CB  1 
ATOM   953  C  CG  . ASN A 1 119 ? -1.073 -10.806 19.004  1.00 40.80 ? 119 ASN A CG  1 
ATOM   954  O  OD1 . ASN A 1 119 ? -1.890 -9.888  18.928  1.00 48.63 ? 119 ASN A OD1 1 
ATOM   955  N  ND2 . ASN A 1 119 ? -0.414 -11.090 20.119  1.00 42.92 ? 119 ASN A ND2 1 
ATOM   956  N  N   . GLY A 1 120 ? 1.903  -12.158 15.296  1.00 25.22 ? 120 GLY A N   1 
ATOM   957  C  CA  . GLY A 1 120 ? 2.187  -12.993 14.143  1.00 30.11 ? 120 GLY A CA  1 
ATOM   958  C  C   . GLY A 1 120 ? 1.171  -12.928 13.029  1.00 28.85 ? 120 GLY A C   1 
ATOM   959  O  O   . GLY A 1 120 ? 1.235  -13.747 12.107  1.00 29.20 ? 120 GLY A O   1 
ATOM   960  N  N   . SER A 1 121 ? 0.241  -11.967 13.072  1.00 25.99 ? 121 SER A N   1 
ATOM   961  C  CA  . SER A 1 121 ? -0.837 -11.878 12.096  1.00 30.46 ? 121 SER A CA  1 
ATOM   962  C  C   . SER A 1 121 ? -0.731 -10.586 11.300  1.00 28.32 ? 121 SER A C   1 
ATOM   963  O  O   . SER A 1 121 ? -0.689 -9.500  11.896  1.00 27.46 ? 121 SER A O   1 
ATOM   964  C  CB  . SER A 1 121 ? -2.191 -11.952 12.800  1.00 34.66 ? 121 SER A CB  1 
ATOM   965  O  OG  . SER A 1 121 ? -2.592 -13.300 12.957  1.00 36.23 ? 121 SER A OG  1 
ATOM   966  N  N   . PRO A 1 122 ? -0.687 -10.656 9.970   1.00 26.99 ? 122 PRO A N   1 
ATOM   967  C  CA  . PRO A 1 122 ? -0.516 -9.431  9.177   1.00 27.16 ? 122 PRO A CA  1 
ATOM   968  C  C   . PRO A 1 122 ? -1.739 -8.535  9.255   1.00 27.71 ? 122 PRO A C   1 
ATOM   969  O  O   . PRO A 1 122 ? -2.879 -8.995  9.172   1.00 31.94 ? 122 PRO A O   1 
ATOM   970  C  CB  . PRO A 1 122 ? -0.298 -9.955  7.752   1.00 33.49 ? 122 PRO A CB  1 
ATOM   971  C  CG  . PRO A 1 122 ? 0.188  -11.373 7.932   1.00 40.20 ? 122 PRO A CG  1 
ATOM   972  C  CD  . PRO A 1 122 ? -0.575 -11.871 9.144   1.00 31.60 ? 122 PRO A CD  1 
ATOM   973  N  N   . SER A 1 123 ? -1.488 -7.239  9.408   1.00 27.99 ? 123 SER A N   1 
ATOM   974  C  CA  . SER A 1 123 ? -2.526 -6.223  9.557   1.00 31.62 ? 123 SER A CA  1 
ATOM   975  C  C   . SER A 1 123 ? -2.694 -5.338  8.335   1.00 32.32 ? 123 SER A C   1 
ATOM   976  O  O   . SER A 1 123 ? -3.820 -4.952  8.003   1.00 26.55 ? 123 SER A O   1 
ATOM   977  C  CB  . SER A 1 123 ? -2.216 -5.331  10.765  1.00 29.07 ? 123 SER A CB  1 
ATOM   978  O  OG  . SER A 1 123 ? -3.388 -4.687  11.220  1.00 52.91 ? 123 SER A OG  1 
ATOM   979  N  N   . GLY A 1 124 ? -1.600 -4.989  7.674   1.00 23.89 ? 124 GLY A N   1 
ATOM   980  C  CA  . GLY A 1 124 ? -1.666 -4.152  6.490   1.00 23.55 ? 124 GLY A CA  1 
ATOM   981  C  C   . GLY A 1 124 ? -0.280 -4.009  5.909   1.00 27.18 ? 124 GLY A C   1 
ATOM   982  O  O   . GLY A 1 124 ? 0.720  -4.415  6.511   1.00 24.14 ? 124 GLY A O   1 
ATOM   983  N  N   . VAL A 1 125 ? -0.232 -3.438  4.712   1.00 20.90 ? 125 VAL A N   1 
ATOM   984  C  CA  . VAL A 1 125 ? 1.014  -3.264  3.988   1.00 19.03 ? 125 VAL A CA  1 
ATOM   985  C  C   . VAL A 1 125 ? 1.088  -1.839  3.463   1.00 22.40 ? 125 VAL A C   1 
ATOM   986  O  O   . VAL A 1 125 ? 0.085  -1.273  3.008   1.00 23.79 ? 125 VAL A O   1 
ATOM   987  C  CB  . VAL A 1 125 ? 1.140  -4.296  2.845   1.00 27.66 ? 125 VAL A CB  1 
ATOM   988  C  CG1 . VAL A 1 125 ? 0.069  -4.069  1.805   1.00 34.09 ? 125 VAL A CG1 1 
ATOM   989  C  CG2 . VAL A 1 125 ? 2.514  -4.225  2.213   1.00 23.60 ? 125 VAL A CG2 1 
ATOM   990  N  N   . TYR A 1 126 ? 2.271  -1.247  3.559   1.00 22.76 ? 126 TYR A N   1 
ATOM   991  C  CA  . TYR A 1 126 ? 2.451  0.106   3.066   1.00 21.42 ? 126 TYR A CA  1 
ATOM   992  C  C   . TYR A 1 126 ? 3.898  0.307   2.665   1.00 24.84 ? 126 TYR A C   1 
ATOM   993  O  O   . TYR A 1 126 ? 4.784  -0.469  3.028   1.00 24.67 ? 126 TYR A O   1 
ATOM   994  C  CB  . TYR A 1 126 ? 2.026  1.150   4.109   1.00 23.18 ? 126 TYR A CB  1 
ATOM   995  C  CG  . TYR A 1 126 ? 2.752  1.062   5.423   1.00 23.94 ? 126 TYR A CG  1 
ATOM   996  C  CD1 . TYR A 1 126 ? 4.009  1.632   5.584   1.00 25.01 ? 126 TYR A CD1 1 
ATOM   997  C  CD2 . TYR A 1 126 ? 2.186  0.391   6.503   1.00 25.25 ? 126 TYR A CD2 1 
ATOM   998  C  CE1 . TYR A 1 126 ? 4.678  1.547   6.798   1.00 23.38 ? 126 TYR A CE1 1 
ATOM   999  C  CE2 . TYR A 1 126 ? 2.847  0.297   7.716   1.00 28.17 ? 126 TYR A CE2 1 
ATOM   1000 C  CZ  . TYR A 1 126 ? 4.095  0.875   7.850   1.00 23.13 ? 126 TYR A CZ  1 
ATOM   1001 O  OH  . TYR A 1 126 ? 4.742  0.792   9.059   1.00 29.17 ? 126 TYR A OH  1 
ATOM   1002 N  N   . GLN A 1 127 ? 4.128  1.374   1.919   1.00 21.16 ? 127 GLN A N   1 
ATOM   1003 C  CA  . GLN A 1 127 ? 5.445  1.703   1.406   1.00 19.16 ? 127 GLN A CA  1 
ATOM   1004 C  C   . GLN A 1 127 ? 6.098  2.767   2.276   1.00 25.09 ? 127 GLN A C   1 
ATOM   1005 O  O   . GLN A 1 127 ? 5.430  3.699   2.727   1.00 28.49 ? 127 GLN A O   1 
ATOM   1006 C  CB  . GLN A 1 127 ? 5.309  2.197   -0.033  1.00 25.75 ? 127 GLN A CB  1 
ATOM   1007 C  CG  . GLN A 1 127 ? 6.586  2.231   -0.766  1.00 34.77 ? 127 GLN A CG  1 
ATOM   1008 C  CD  . GLN A 1 127 ? 6.999  0.869   -1.239  1.00 26.18 ? 127 GLN A CD  1 
ATOM   1009 O  OE1 . GLN A 1 127 ? 6.455  -0.161  -0.810  1.00 25.11 ? 127 GLN A OE1 1 
ATOM   1010 N  NE2 . GLN A 1 127 ? 7.987  0.845   -2.105  1.00 26.49 ? 127 GLN A NE2 1 
ATOM   1011 N  N   . CYS A 1 128 ? 7.402  2.631   2.522   1.00 23.63 ? 128 CYS A N   1 
ATOM   1012 C  CA  . CYS A 1 128 ? 8.141  3.773   3.058   1.00 25.81 ? 128 CYS A CA  1 
ATOM   1013 C  C   . CYS A 1 128 ? 9.586  3.737   2.569   1.00 22.54 ? 128 CYS A C   1 
ATOM   1014 O  O   . CYS A 1 128 ? 9.949  2.989   1.653   1.00 25.65 ? 128 CYS A O   1 
ATOM   1015 C  CB  . CYS A 1 128 ? 8.062  3.842   4.587   1.00 37.28 ? 128 CYS A CB  1 
ATOM   1016 S  SG  . CYS A 1 128 ? 8.252  2.294   5.431   1.00 40.92 ? 128 CYS A SG  1 
ATOM   1017 N  N   . ALA A 1 129 ? 10.398 4.596   3.166   1.00 25.47 ? 129 ALA A N   1 
ATOM   1018 C  CA  . ALA A 1 129 ? 11.762 4.845   2.746   1.00 21.04 ? 129 ALA A CA  1 
ATOM   1019 C  C   . ALA A 1 129 ? 12.648 4.969   3.975   1.00 18.60 ? 129 ALA A C   1 
ATOM   1020 O  O   . ALA A 1 129 ? 12.233 5.521   5.000   1.00 23.81 ? 129 ALA A O   1 
ATOM   1021 C  CB  . ALA A 1 129 ? 11.854 6.128   1.913   1.00 21.72 ? 129 ALA A CB  1 
ATOM   1022 N  N   . MET A 1 130 ? 13.847 4.404   3.880   1.00 19.54 ? 130 MET A N   1 
ATOM   1023 C  CA  . MET A 1 130 ? 14.960 4.785   4.748   1.00 18.19 ? 130 MET A CA  1 
ATOM   1024 C  C   . MET A 1 130 ? 15.272 6.267   4.666   1.00 20.41 ? 130 MET A C   1 
ATOM   1025 O  O   . MET A 1 130 ? 15.775 6.734   3.644   1.00 20.40 ? 130 MET A O   1 
ATOM   1026 C  CB  . MET A 1 130 ? 16.222 4.003   4.394   1.00 24.91 ? 130 MET A CB  1 
ATOM   1027 C  CG  . MET A 1 130 ? 17.249 3.910   5.507   1.00 23.60 ? 130 MET A CG  1 
ATOM   1028 S  SD  . MET A 1 130 ? 16.768 3.677   7.232   1.00 23.85 ? 130 MET A SD  1 
ATOM   1029 C  CE  . MET A 1 130 ? 16.054 2.060   7.218   1.00 22.19 ? 130 MET A CE  1 
ATOM   1030 N  N   . ARG A 1 131 ? 14.975 7.013   5.718   1.00 18.77 ? 131 ARG A N   1 
ATOM   1031 C  CA  . ARG A 1 131 ? 15.253 8.445   5.696   1.00 22.32 ? 131 ARG A CA  1 
ATOM   1032 C  C   . ARG A 1 131 ? 16.757 8.685   5.801   1.00 20.49 ? 131 ARG A C   1 
ATOM   1033 O  O   . ARG A 1 131 ? 17.506 7.812   6.241   1.00 21.34 ? 131 ARG A O   1 
ATOM   1034 C  CB  . ARG A 1 131 ? 14.570 9.155   6.860   1.00 19.94 ? 131 ARG A CB  1 
ATOM   1035 C  CG  . ARG A 1 131 ? 13.066 8.992   6.918   1.00 22.12 ? 131 ARG A CG  1 
ATOM   1036 C  CD  . ARG A 1 131 ? 12.352 9.373   5.622   1.00 23.39 ? 131 ARG A CD  1 
ATOM   1037 N  NE  . ARG A 1 131 ? 12.747 10.696  5.142   1.00 20.94 ? 131 ARG A NE  1 
ATOM   1038 C  CZ  . ARG A 1 131 ? 12.311 11.234  4.012   1.00 22.92 ? 131 ARG A CZ  1 
ATOM   1039 N  NH1 . ARG A 1 131 ? 11.459 10.592  3.228   1.00 21.52 ? 131 ARG A NH1 1 
ATOM   1040 N  NH2 . ARG A 1 131 ? 12.753 12.440  3.651   1.00 22.72 ? 131 ARG A NH2 1 
ATOM   1041 N  N   . PRO A 1 132 ? 17.215 9.882   5.430   1.00 21.55 ? 132 PRO A N   1 
ATOM   1042 C  CA  . PRO A 1 132 ? 18.647 10.187  5.550   1.00 20.76 ? 132 PRO A CA  1 
ATOM   1043 C  C   . PRO A 1 132 ? 19.162 10.146  6.974   1.00 24.26 ? 132 PRO A C   1 
ATOM   1044 O  O   . PRO A 1 132 ? 20.375 9.995   7.172   1.00 23.84 ? 132 PRO A O   1 
ATOM   1045 C  CB  . PRO A 1 132 ? 18.741 11.595  4.959   1.00 19.88 ? 132 PRO A CB  1 
ATOM   1046 C  CG  . PRO A 1 132 ? 17.662 11.603  3.926   1.00 24.07 ? 132 PRO A CG  1 
ATOM   1047 C  CD  . PRO A 1 132 ? 16.514 10.872  4.599   1.00 21.93 ? 132 PRO A CD  1 
ATOM   1048 N  N   . ASN A 1 133 ? 18.294 10.289  7.975   1.00 19.44 ? 133 ASN A N   1 
ATOM   1049 C  CA  . ASN A 1 133 ? 18.706 10.155  9.364   1.00 17.96 ? 133 ASN A CA  1 
ATOM   1050 C  C   . ASN A 1 133 ? 18.507 8.740   9.900   1.00 21.56 ? 133 ASN A C   1 
ATOM   1051 O  O   . ASN A 1 133 ? 18.583 8.536   11.110  1.00 23.47 ? 133 ASN A O   1 
ATOM   1052 C  CB  . ASN A 1 133 ? 17.964 11.187  10.218  1.00 22.43 ? 133 ASN A CB  1 
ATOM   1053 C  CG  . ASN A 1 133 ? 16.469 10.939  10.258  1.00 24.83 ? 133 ASN A CG  1 
ATOM   1054 O  OD1 . ASN A 1 133 ? 15.973 10.008  9.633   1.00 22.73 ? 133 ASN A OD1 1 
ATOM   1055 N  ND2 . ASN A 1 133 ? 15.742 11.804  10.941  1.00 22.07 ? 133 ASN A ND2 1 
ATOM   1056 N  N   . PHE A 1 134 ? 18.237 7.768   9.019   1.00 18.31 ? 134 PHE A N   1 
ATOM   1057 C  CA  . PHE A 1 134 ? 18.166 6.340   9.353   1.00 21.03 ? 134 PHE A CA  1 
ATOM   1058 C  C   . PHE A 1 134 ? 16.970 6.005   10.235  1.00 22.00 ? 134 PHE A C   1 
ATOM   1059 O  O   . PHE A 1 134 ? 16.984 5.026   10.983  1.00 22.73 ? 134 PHE A O   1 
ATOM   1060 C  CB  . PHE A 1 134 ? 19.460 5.853   10.001  1.00 19.53 ? 134 PHE A CB  1 
ATOM   1061 C  CG  . PHE A 1 134 ? 20.629 5.918   9.086   1.00 21.70 ? 134 PHE A CG  1 
ATOM   1062 C  CD1 . PHE A 1 134 ? 20.836 4.933   8.140   1.00 24.13 ? 134 PHE A CD1 1 
ATOM   1063 C  CD2 . PHE A 1 134 ? 21.518 6.971   9.168   1.00 23.68 ? 134 PHE A CD2 1 
ATOM   1064 C  CE1 . PHE A 1 134 ? 21.922 5.001   7.282   1.00 33.05 ? 134 PHE A CE1 1 
ATOM   1065 C  CE2 . PHE A 1 134 ? 22.608 7.047   8.319   1.00 29.52 ? 134 PHE A CE2 1 
ATOM   1066 C  CZ  . PHE A 1 134 ? 22.812 6.062   7.381   1.00 22.24 ? 134 PHE A CZ  1 
ATOM   1067 N  N   . THR A 1 135 ? 15.929 6.810   10.141  1.00 21.80 ? 135 THR A N   1 
ATOM   1068 C  CA  . THR A 1 135 ? 14.614 6.486   10.652  1.00 21.21 ? 135 THR A CA  1 
ATOM   1069 C  C   . THR A 1 135 ? 13.709 6.152   9.475   1.00 25.44 ? 135 THR A C   1 
ATOM   1070 O  O   . THR A 1 135 ? 14.047 6.371   8.304   1.00 20.77 ? 135 THR A O   1 
ATOM   1071 C  CB  . THR A 1 135 ? 14.029 7.654   11.459  1.00 26.01 ? 135 THR A CB  1 
ATOM   1072 O  OG1 . THR A 1 135 ? 13.652 8.701   10.553  1.00 23.11 ? 135 THR A OG1 1 
ATOM   1073 C  CG2 . THR A 1 135 ? 15.027 8.184   12.503  1.00 23.44 ? 135 THR A CG2 1 
ATOM   1074 N  N   . ILE A 1 136 ? 12.551 5.594   9.793   1.00 22.81 ? 136 ILE A N   1 
ATOM   1075 C  CA  . ILE A 1 136 ? 11.478 5.476   8.821   1.00 21.93 ? 136 ILE A CA  1 
ATOM   1076 C  C   . ILE A 1 136 ? 10.232 6.091   9.437   1.00 21.63 ? 136 ILE A C   1 
ATOM   1077 O  O   . ILE A 1 136 ? 10.074 6.141   10.662  1.00 20.39 ? 136 ILE A O   1 
ATOM   1078 C  CB  . ILE A 1 136 ? 11.244 4.014   8.345   1.00 29.09 ? 136 ILE A CB  1 
ATOM   1079 C  CG1 . ILE A 1 136 ? 10.532 3.194   9.422   1.00 25.05 ? 136 ILE A CG1 1 
ATOM   1080 C  CG2 . ILE A 1 136 ? 12.570 3.366   7.828   1.00 24.06 ? 136 ILE A CG2 1 
ATOM   1081 C  CD1 . ILE A 1 136 ? 10.117 1.797   8.977   1.00 26.26 ? 136 ILE A CD1 1 
ATOM   1082 N  N   . LYS A 1 137 ? 9.387  6.647   8.574   1.00 23.78 ? 137 LYS A N   1 
ATOM   1083 C  CA  . LYS A 1 137 ? 8.110  7.205   9.003   1.00 22.38 ? 137 LYS A CA  1 
ATOM   1084 C  C   . LYS A 1 137 ? 7.053  6.150   8.704   1.00 27.42 ? 137 LYS A C   1 
ATOM   1085 O  O   . LYS A 1 137 ? 6.390  6.168   7.670   1.00 27.91 ? 137 LYS A O   1 
ATOM   1086 C  CB  . LYS A 1 137 ? 7.822  8.525   8.297   1.00 23.05 ? 137 LYS A CB  1 
ATOM   1087 C  CG  . LYS A 1 137 ? 8.937  9.519   8.338   1.00 26.30 ? 137 LYS A CG  1 
ATOM   1088 C  CD  . LYS A 1 137 ? 8.513  10.797  7.622   1.00 41.43 ? 137 LYS A CD  1 
ATOM   1089 C  CE  . LYS A 1 137 ? 9.611  11.842  7.654   1.00 51.46 ? 137 LYS A CE  1 
ATOM   1090 N  NZ  . LYS A 1 137 ? 9.722  12.653  6.394   1.00 45.53 ? 137 LYS A NZ  1 
ATOM   1091 N  N   . GLY A 1 138 ? 6.912  5.205   9.631   1.00 20.81 ? 138 GLY A N   1 
ATOM   1092 C  CA  . GLY A 1 138 ? 5.989  4.103   9.470   1.00 26.10 ? 138 GLY A CA  1 
ATOM   1093 C  C   . GLY A 1 138 ? 4.649  4.362   10.132  1.00 25.34 ? 138 GLY A C   1 
ATOM   1094 O  O   . GLY A 1 138 ? 4.297  5.488   10.487  1.00 28.63 ? 138 GLY A O   1 
ATOM   1095 N  N   . SER A 1 139 ? 3.887  3.281   10.284  1.00 21.89 ? 139 SER A N   1 
ATOM   1096 C  CA  . SER A 1 139 ? 2.674  3.261   11.101  1.00 22.22 ? 139 SER A CA  1 
ATOM   1097 C  C   . SER A 1 139 ? 2.731  1.982   11.920  1.00 23.00 ? 139 SER A C   1 
ATOM   1098 O  O   . SER A 1 139 ? 2.533  0.885   11.384  1.00 24.45 ? 139 SER A O   1 
ATOM   1099 C  CB  . SER A 1 139 ? 1.412  3.328   10.235  1.00 25.06 ? 139 SER A CB  1 
ATOM   1100 O  OG  . SER A 1 139 ? 0.252  3.086   11.002  1.00 26.85 ? 139 SER A OG  1 
ATOM   1101 N  N   . PHE A 1 140 ? 3.024  2.124   13.211  1.00 20.85 ? 140 PHE A N   1 
ATOM   1102 C  CA  . PHE A 1 140 ? 3.348  1.004   14.079  1.00 21.81 ? 140 PHE A CA  1 
ATOM   1103 C  C   . PHE A 1 140 ? 2.784  1.275   15.460  1.00 22.13 ? 140 PHE A C   1 
ATOM   1104 O  O   . PHE A 1 140 ? 2.987  2.360   16.008  1.00 25.22 ? 140 PHE A O   1 
ATOM   1105 C  CB  . PHE A 1 140 ? 4.868  0.812   14.205  1.00 20.53 ? 140 PHE A CB  1 
ATOM   1106 C  CG  . PHE A 1 140 ? 5.557  0.249   12.985  1.00 22.49 ? 140 PHE A CG  1 
ATOM   1107 C  CD1 . PHE A 1 140 ? 5.279  -1.032  12.526  1.00 23.51 ? 140 PHE A CD1 1 
ATOM   1108 C  CD2 . PHE A 1 140 ? 6.537  0.995   12.336  1.00 20.45 ? 140 PHE A CD2 1 
ATOM   1109 C  CE1 . PHE A 1 140 ? 5.960  -1.549  11.437  1.00 23.68 ? 140 PHE A CE1 1 
ATOM   1110 C  CE2 . PHE A 1 140 ? 7.228  0.488   11.261  1.00 22.09 ? 140 PHE A CE2 1 
ATOM   1111 C  CZ  . PHE A 1 140 ? 6.938  -0.784  10.796  1.00 22.45 ? 140 PHE A CZ  1 
ATOM   1112 N  N   . LEU A 1 141 ? 2.115  0.286   16.028  1.00 20.38 ? 141 LEU A N   1 
ATOM   1113 C  CA  . LEU A 1 141 ? 1.586  0.365   17.379  1.00 21.07 ? 141 LEU A CA  1 
ATOM   1114 C  C   . LEU A 1 141 ? 2.309  -0.654  18.238  1.00 21.77 ? 141 LEU A C   1 
ATOM   1115 O  O   . LEU A 1 141 ? 3.039  -1.510  17.737  1.00 23.75 ? 141 LEU A O   1 
ATOM   1116 C  CB  . LEU A 1 141 ? 0.082  0.093   17.389  1.00 20.00 ? 141 LEU A CB  1 
ATOM   1117 C  CG  . LEU A 1 141 ? -0.761 1.043   16.533  1.00 32.56 ? 141 LEU A CG  1 
ATOM   1118 C  CD1 . LEU A 1 141 ? -2.162 0.467   16.373  1.00 37.47 ? 141 LEU A CD1 1 
ATOM   1119 C  CD2 . LEU A 1 141 ? -0.794 2.450   17.120  1.00 37.29 ? 141 LEU A CD2 1 
ATOM   1120 N  N   . ASN A 1 142 ? 2.110  -0.570  19.550  1.00 26.81 ? 142 ASN A N   1 
ATOM   1121 C  CA  . ASN A 1 142 ? 2.695  -1.599  20.395  1.00 23.31 ? 142 ASN A CA  1 
ATOM   1122 C  C   . ASN A 1 142 ? 2.272  -2.966  19.878  1.00 23.11 ? 142 ASN A C   1 
ATOM   1123 O  O   . ASN A 1 142 ? 1.165  -3.142  19.360  1.00 26.06 ? 142 ASN A O   1 
ATOM   1124 C  CB  . ASN A 1 142 ? 2.277  -1.425  21.858  1.00 31.04 ? 142 ASN A CB  1 
ATOM   1125 C  CG  . ASN A 1 142 ? 3.024  -2.366  22.776  1.00 34.46 ? 142 ASN A CG  1 
ATOM   1126 O  OD1 . ASN A 1 142 ? 2.447  -3.301  23.330  1.00 52.30 ? 142 ASN A OD1 1 
ATOM   1127 N  ND2 . ASN A 1 142 ? 4.327  -2.146  22.916  1.00 37.66 ? 142 ASN A ND2 1 
ATOM   1128 N  N   . GLY A 1 143 ? 3.175  -3.935  20.004  1.00 20.69 ? 143 GLY A N   1 
ATOM   1129 C  CA  . GLY A 1 143 ? 2.963  -5.267  19.484  1.00 23.14 ? 143 GLY A CA  1 
ATOM   1130 C  C   . GLY A 1 143 ? 3.452  -5.470  18.063  1.00 25.05 ? 143 GLY A C   1 
ATOM   1131 O  O   . GLY A 1 143 ? 3.412  -6.604  17.569  1.00 23.02 ? 143 GLY A O   1 
ATOM   1132 N  N   . SER A 1 144 ? 3.910  -4.410  17.397  1.00 24.55 ? 144 SER A N   1 
ATOM   1133 C  CA  . SER A 1 144 ? 4.341  -4.469  16.001  1.00 19.83 ? 144 SER A CA  1 
ATOM   1134 C  C   . SER A 1 144 ? 5.808  -4.854  15.824  1.00 18.14 ? 144 SER A C   1 
ATOM   1135 O  O   . SER A 1 144 ? 6.227  -5.132  14.692  1.00 18.63 ? 144 SER A O   1 
ATOM   1136 C  CB  . SER A 1 144 ? 4.079  -3.117  15.330  1.00 21.27 ? 144 SER A CB  1 
ATOM   1137 O  OG  . SER A 1 144 ? 4.963  -2.128  15.824  1.00 19.77 ? 144 SER A OG  1 
ATOM   1138 N  N   . CYS A 1 145 ? 6.578  -4.906  16.909  1.00 21.29 ? 145 CYS A N   1 
ATOM   1139 C  CA  . CYS A 1 145 ? 7.979  -5.267  16.826  1.00 21.49 ? 145 CYS A CA  1 
ATOM   1140 C  C   . CYS A 1 145 ? 8.147  -6.615  16.139  1.00 16.28 ? 145 CYS A C   1 
ATOM   1141 O  O   . CYS A 1 145 ? 7.377  -7.553  16.370  1.00 19.64 ? 145 CYS A O   1 
ATOM   1142 C  CB  . CYS A 1 145 ? 8.581  -5.295  18.228  1.00 26.71 ? 145 CYS A CB  1 
ATOM   1143 S  SG  . CYS A 1 145 ? 8.734  -3.633  18.881  1.00 28.96 ? 145 CYS A SG  1 
ATOM   1144 N  N   . GLY A 1 146 ? 9.164  -6.702  15.288  1.00 17.23 ? 146 GLY A N   1 
ATOM   1145 C  CA  . GLY A 1 146 ? 9.398  -7.873  14.476  1.00 17.78 ? 146 GLY A CA  1 
ATOM   1146 C  C   . GLY A 1 146 ? 8.714  -7.848  13.133  1.00 22.66 ? 146 GLY A C   1 
ATOM   1147 O  O   . GLY A 1 146 ? 8.958  -8.747  12.320  1.00 22.60 ? 146 GLY A O   1 
ATOM   1148 N  N   . SER A 1 147 ? 7.855  -6.860  12.871  1.00 20.12 ? 147 SER A N   1 
ATOM   1149 C  CA  . SER A 1 147 ? 7.366  -6.642  11.514  1.00 22.79 ? 147 SER A CA  1 
ATOM   1150 C  C   . SER A 1 147 ? 8.547  -6.330  10.597  1.00 19.23 ? 147 SER A C   1 
ATOM   1151 O  O   . SER A 1 147 ? 9.517  -5.685  11.007  1.00 19.55 ? 147 SER A O   1 
ATOM   1152 C  CB  . SER A 1 147 ? 6.362  -5.488  11.494  1.00 20.39 ? 147 SER A CB  1 
ATOM   1153 O  OG  . SER A 1 147 ? 5.262  -5.762  12.343  1.00 20.52 ? 147 SER A OG  1 
ATOM   1154 N  N   . VAL A 1 148 ? 8.471  -6.771  9.339   1.00 19.29 ? 148 VAL A N   1 
ATOM   1155 C  CA  . VAL A 1 148 ? 9.621  -6.647  8.461   1.00 19.27 ? 148 VAL A CA  1 
ATOM   1156 C  C   . VAL A 1 148 ? 9.310  -5.768  7.241   1.00 24.71 ? 148 VAL A C   1 
ATOM   1157 O  O   . VAL A 1 148 ? 8.157  -5.592  6.809   1.00 19.59 ? 148 VAL A O   1 
ATOM   1158 C  CB  . VAL A 1 148 ? 10.134 -8.037  8.026   1.00 22.27 ? 148 VAL A CB  1 
ATOM   1159 C  CG1 . VAL A 1 148 ? 10.644 -8.825  9.276   1.00 17.59 ? 148 VAL A CG1 1 
ATOM   1160 C  CG2 . VAL A 1 148 ? 9.061  -8.808  7.249   1.00 23.17 ? 148 VAL A CG2 1 
ATOM   1161 N  N   . GLY A 1 149 ? 10.378 -5.198  6.691   1.00 19.36 ? 149 GLY A N   1 
ATOM   1162 C  CA  . GLY A 1 149 ? 10.333 -4.484  5.426   1.00 19.57 ? 149 GLY A CA  1 
ATOM   1163 C  C   . GLY A 1 149 ? 11.065 -5.284  4.363   1.00 21.26 ? 149 GLY A C   1 
ATOM   1164 O  O   . GLY A 1 149 ? 11.987 -6.043  4.666   1.00 19.39 ? 149 GLY A O   1 
ATOM   1165 N  N   . PHE A 1 150 ? 10.660 -5.110  3.107   1.00 20.38 ? 150 PHE A N   1 
ATOM   1166 C  CA  . PHE A 1 150 ? 11.185 -5.969  2.057   1.00 17.44 ? 150 PHE A CA  1 
ATOM   1167 C  C   . PHE A 1 150 ? 10.966 -5.337  0.691   1.00 24.08 ? 150 PHE A C   1 
ATOM   1168 O  O   . PHE A 1 150 ? 10.108 -4.473  0.510   1.00 20.91 ? 150 PHE A O   1 
ATOM   1169 C  CB  . PHE A 1 150 ? 10.509 -7.342  2.088   1.00 20.95 ? 150 PHE A CB  1 
ATOM   1170 C  CG  . PHE A 1 150 ? 9.016  -7.270  1.895   1.00 23.01 ? 150 PHE A CG  1 
ATOM   1171 C  CD1 . PHE A 1 150 ? 8.190  -6.959  2.968   1.00 24.02 ? 150 PHE A CD1 1 
ATOM   1172 C  CD2 . PHE A 1 150 ? 8.444  -7.471  0.653   1.00 28.38 ? 150 PHE A CD2 1 
ATOM   1173 C  CE1 . PHE A 1 150 ? 6.809  -6.863  2.797   1.00 24.25 ? 150 PHE A CE1 1 
ATOM   1174 C  CE2 . PHE A 1 150 ? 7.069  -7.379  0.474   1.00 28.28 ? 150 PHE A CE2 1 
ATOM   1175 C  CZ  . PHE A 1 150 ? 6.251  -7.080  1.550   1.00 26.27 ? 150 PHE A CZ  1 
ATOM   1176 N  N   . ASN A 1 151 ? 11.736 -5.829  -0.273  1.00 20.97 ? 151 ASN A N   1 
ATOM   1177 C  CA  . ASN A 1 151 ? 11.532 -5.598  -1.694  1.00 25.66 ? 151 ASN A CA  1 
ATOM   1178 C  C   . ASN A 1 151 ? 11.374 -6.959  -2.357  1.00 24.62 ? 151 ASN A C   1 
ATOM   1179 O  O   . ASN A 1 151 ? 11.812 -7.982  -1.824  1.00 27.59 ? 151 ASN A O   1 
ATOM   1180 C  CB  . ASN A 1 151 ? 12.710 -4.835  -2.303  1.00 23.28 ? 151 ASN A CB  1 
ATOM   1181 C  CG  . ASN A 1 151 ? 12.649 -3.348  -2.015  1.00 26.82 ? 151 ASN A CG  1 
ATOM   1182 O  OD1 . ASN A 1 151 ? 11.946 -2.599  -2.697  1.00 38.65 ? 151 ASN A OD1 1 
ATOM   1183 N  ND2 . ASN A 1 151 ? 13.350 -2.918  -0.967  1.00 28.78 ? 151 ASN A ND2 1 
ATOM   1184 N  N   . ILE A 1 152 ? 10.731 -6.981  -3.518  1.00 28.87 ? 152 ILE A N   1 
ATOM   1185 C  CA  . ILE A 1 152 ? 10.546 -8.225  -4.254  1.00 29.70 ? 152 ILE A CA  1 
ATOM   1186 C  C   . ILE A 1 152 ? 11.023 -7.999  -5.676  1.00 34.62 ? 152 ILE A C   1 
ATOM   1187 O  O   . ILE A 1 152 ? 10.620 -7.024  -6.316  1.00 32.83 ? 152 ILE A O   1 
ATOM   1188 C  CB  . ILE A 1 152 ? 9.080  -8.693  -4.232  1.00 35.69 ? 152 ILE A CB  1 
ATOM   1189 C  CG1 . ILE A 1 152 ? 8.699  -9.160  -2.825  1.00 37.52 ? 152 ILE A CG1 1 
ATOM   1190 C  CG2 . ILE A 1 152 ? 8.869  -9.829  -5.224  1.00 43.27 ? 152 ILE A CG2 1 
ATOM   1191 C  CD1 . ILE A 1 152 ? 7.240  -9.538  -2.692  1.00 32.43 ? 152 ILE A CD1 1 
ATOM   1192 N  N   . ASP A 1 153 ? 11.905 -8.878  -6.156  1.00 37.42 ? 153 ASP A N   1 
ATOM   1193 C  CA  . ASP A 1 153 ? 12.412 -8.816  -7.527  1.00 50.33 ? 153 ASP A CA  1 
ATOM   1194 C  C   . ASP A 1 153 ? 12.108 -10.149 -8.198  1.00 38.53 ? 153 ASP A C   1 
ATOM   1195 O  O   . ASP A 1 153 ? 12.717 -11.173 -7.864  1.00 41.97 ? 153 ASP A O   1 
ATOM   1196 C  CB  . ASP A 1 153 ? 13.910 -8.516  -7.566  1.00 50.61 ? 153 ASP A CB  1 
ATOM   1197 C  CG  . ASP A 1 153 ? 14.503 -8.711  -8.953  1.00 67.69 ? 153 ASP A CG  1 
ATOM   1198 O  OD1 . ASP A 1 153 ? 13.788 -8.441  -9.944  1.00 57.87 ? 153 ASP A OD1 1 
ATOM   1199 O  OD2 . ASP A 1 153 ? 15.674 -9.141  -9.053  1.00 76.01 ? 153 ASP A OD2 1 
ATOM   1200 N  N   . TYR A 1 154 ? 11.180 -10.130 -9.156  1.00 42.73 ? 154 TYR A N   1 
ATOM   1201 C  CA  . TYR A 1 154 ? 10.675 -11.361 -9.744  1.00 41.06 ? 154 TYR A CA  1 
ATOM   1202 C  C   . TYR A 1 154 ? 10.069 -12.235 -8.656  1.00 47.23 ? 154 TYR A C   1 
ATOM   1203 O  O   . TYR A 1 154 ? 8.996  -11.930 -8.125  1.00 52.23 ? 154 TYR A O   1 
ATOM   1204 C  CB  . TYR A 1 154 ? 11.789 -12.105 -10.486 1.00 48.92 ? 154 TYR A CB  1 
ATOM   1205 N  N   . ASP A 1 155 ? 10.752 -13.320 -8.309  1.00 45.02 ? 155 ASP A N   1 
ATOM   1206 C  CA  . ASP A 1 155 ? 10.255 -14.251 -7.308  1.00 45.44 ? 155 ASP A CA  1 
ATOM   1207 C  C   . ASP A 1 155 ? 11.116 -14.255 -6.048  1.00 39.10 ? 155 ASP A C   1 
ATOM   1208 O  O   . ASP A 1 155 ? 10.970 -15.157 -5.211  1.00 41.18 ? 155 ASP A O   1 
ATOM   1209 C  CB  . ASP A 1 155 ? 10.154 -15.649 -7.928  1.00 51.56 ? 155 ASP A CB  1 
ATOM   1210 C  CG  . ASP A 1 155 ? 11.489 -16.348 -8.010  1.00 52.29 ? 155 ASP A CG  1 
ATOM   1211 O  OD1 . ASP A 1 155 ? 11.652 -17.397 -7.344  1.00 69.98 ? 155 ASP A OD1 1 
ATOM   1212 O  OD2 . ASP A 1 155 ? 12.380 -15.830 -8.717  1.00 64.87 ? 155 ASP A OD2 1 
ATOM   1213 N  N   . CYS A 1 156 ? 11.992 -13.261 -5.879  1.00 33.89 ? 156 CYS A N   1 
ATOM   1214 C  CA  . CYS A 1 156 ? 12.951 -13.233 -4.780  1.00 33.97 ? 156 CYS A CA  1 
ATOM   1215 C  C   . CYS A 1 156 ? 12.602 -12.107 -3.819  1.00 26.30 ? 156 CYS A C   1 
ATOM   1216 O  O   . CYS A 1 156 ? 12.531 -10.938 -4.222  1.00 28.17 ? 156 CYS A O   1 
ATOM   1217 C  CB  . CYS A 1 156 ? 14.375 -13.048 -5.297  1.00 39.31 ? 156 CYS A CB  1 
ATOM   1218 S  SG  . CYS A 1 156 ? 15.620 -13.016 -3.979  1.00 40.60 ? 156 CYS A SG  1 
ATOM   1219 N  N   . VAL A 1 157 ? 12.404 -12.455 -2.546  1.00 26.25 ? 157 VAL A N   1 
ATOM   1220 C  CA  . VAL A 1 157 ? 12.139 -11.468 -1.505  1.00 25.88 ? 157 VAL A CA  1 
ATOM   1221 C  C   . VAL A 1 157 ? 13.470 -11.008 -0.921  1.00 22.29 ? 157 VAL A C   1 
ATOM   1222 O  O   . VAL A 1 157 ? 14.257 -11.827 -0.433  1.00 24.74 ? 157 VAL A O   1 
ATOM   1223 C  CB  . VAL A 1 157 ? 11.232 -12.039 -0.398  1.00 23.42 ? 157 VAL A CB  1 
ATOM   1224 C  CG1 . VAL A 1 157 ? 10.907 -10.949 0.637   1.00 22.85 ? 157 VAL A CG1 1 
ATOM   1225 C  CG2 . VAL A 1 157 ? 9.945  -12.613 -0.993  1.00 26.33 ? 157 VAL A CG2 1 
ATOM   1226 N  N   . SER A 1 158 ? 13.708 -9.697  -0.933  1.00 22.53 ? 158 SER A N   1 
ATOM   1227 C  CA  . SER A 1 158 ? 14.897 -9.107  -0.316  1.00 25.39 ? 158 SER A CA  1 
ATOM   1228 C  C   . SER A 1 158 ? 14.463 -8.415  0.975   1.00 18.54 ? 158 SER A C   1 
ATOM   1229 O  O   . SER A 1 158 ? 13.959 -7.287  0.959   1.00 21.94 ? 158 SER A O   1 
ATOM   1230 C  CB  . SER A 1 158 ? 15.593 -8.135  -1.267  1.00 26.02 ? 158 SER A CB  1 
ATOM   1231 O  OG  . SER A 1 158 ? 16.352 -8.849  -2.222  1.00 30.15 ? 158 SER A OG  1 
ATOM   1232 N  N   . PHE A 1 159 ? 14.665 -9.098  2.093   1.00 21.18 ? 159 PHE A N   1 
ATOM   1233 C  CA  . PHE A 1 159 ? 14.337 -8.537  3.396   1.00 18.16 ? 159 PHE A CA  1 
ATOM   1234 C  C   . PHE A 1 159 ? 15.389 -7.510  3.792   1.00 18.94 ? 159 PHE A C   1 
ATOM   1235 O  O   . PHE A 1 159 ? 16.584 -7.826  3.838   1.00 22.24 ? 159 PHE A O   1 
ATOM   1236 C  CB  . PHE A 1 159 ? 14.258 -9.643  4.446   1.00 23.83 ? 159 PHE A CB  1 
ATOM   1237 C  CG  . PHE A 1 159 ? 13.115 -10.608 4.243   1.00 20.56 ? 159 PHE A CG  1 
ATOM   1238 C  CD1 . PHE A 1 159 ? 11.825 -10.262 4.632   1.00 20.49 ? 159 PHE A CD1 1 
ATOM   1239 C  CD2 . PHE A 1 159 ? 13.340 -11.867 3.702   1.00 19.13 ? 159 PHE A CD2 1 
ATOM   1240 C  CE1 . PHE A 1 159 ? 10.770 -11.165 4.467   1.00 18.64 ? 159 PHE A CE1 1 
ATOM   1241 C  CE2 . PHE A 1 159 ? 12.298 -12.764 3.523   1.00 23.20 ? 159 PHE A CE2 1 
ATOM   1242 C  CZ  . PHE A 1 159 ? 11.016 -12.417 3.917   1.00 21.86 ? 159 PHE A CZ  1 
ATOM   1243 N  N   . CYS A 1 160 ? 14.949 -6.287  4.098   1.00 19.72 ? 160 CYS A N   1 
ATOM   1244 C  CA  . CYS A 1 160 ? 15.874 -5.226  4.472   1.00 19.98 ? 160 CYS A CA  1 
ATOM   1245 C  C   . CYS A 1 160 ? 15.629 -4.606  5.837   1.00 19.90 ? 160 CYS A C   1 
ATOM   1246 O  O   . CYS A 1 160 ? 16.474 -3.819  6.275   1.00 20.93 ? 160 CYS A O   1 
ATOM   1247 C  CB  . CYS A 1 160 ? 15.854 -4.088  3.437   1.00 20.78 ? 160 CYS A CB  1 
ATOM   1248 S  SG  . CYS A 1 160 ? 14.226 -3.365  3.206   1.00 23.63 ? 160 CYS A SG  1 
ATOM   1249 N  N   . TYR A 1 161 ? 14.505 -4.882  6.499   1.00 16.55 ? 161 TYR A N   1 
ATOM   1250 C  CA  . TYR A 1 161 ? 14.171 -4.147  7.716   1.00 21.46 ? 161 TYR A CA  1 
ATOM   1251 C  C   . TYR A 1 161 ? 13.416 -5.041  8.688   1.00 19.29 ? 161 TYR A C   1 
ATOM   1252 O  O   . TYR A 1 161 ? 12.539 -5.809  8.296   1.00 17.54 ? 161 TYR A O   1 
ATOM   1253 C  CB  . TYR A 1 161 ? 13.341 -2.880  7.393   1.00 17.47 ? 161 TYR A CB  1 
ATOM   1254 C  CG  . TYR A 1 161 ? 12.944 -2.046  8.615   1.00 16.75 ? 161 TYR A CG  1 
ATOM   1255 C  CD1 . TYR A 1 161 ? 13.828 -1.110  9.148   1.00 14.89 ? 161 TYR A CD1 1 
ATOM   1256 C  CD2 . TYR A 1 161 ? 11.691 -2.174  9.221   1.00 19.06 ? 161 TYR A CD2 1 
ATOM   1257 C  CE1 . TYR A 1 161 ? 13.483 -0.335  10.290  1.00 19.34 ? 161 TYR A CE1 1 
ATOM   1258 C  CE2 . TYR A 1 161 ? 11.340 -1.408  10.356  1.00 16.35 ? 161 TYR A CE2 1 
ATOM   1259 C  CZ  . TYR A 1 161 ? 12.237 -0.483  10.870  1.00 19.93 ? 161 TYR A CZ  1 
ATOM   1260 O  OH  . TYR A 1 161 ? 11.896 0.279   11.976  1.00 17.79 ? 161 TYR A OH  1 
ATOM   1261 N  N   . MET A 1 162 ? 13.776 -4.934  9.956   1.00 18.05 ? 162 MET A N   1 
ATOM   1262 C  CA  . MET A 1 162 ? 13.050 -5.516  11.081  1.00 19.55 ? 162 MET A CA  1 
ATOM   1263 C  C   . MET A 1 162 ? 12.734 -4.380  12.051  1.00 15.65 ? 162 MET A C   1 
ATOM   1264 O  O   . MET A 1 162 ? 13.647 -3.656  12.459  1.00 15.24 ? 162 MET A O   1 
ATOM   1265 C  CB  . MET A 1 162 ? 13.911 -6.540  11.821  1.00 18.46 ? 162 MET A CB  1 
ATOM   1266 C  CG  . MET A 1 162 ? 13.254 -7.114  13.063  1.00 22.45 ? 162 MET A CG  1 
ATOM   1267 S  SD  . MET A 1 162 ? 13.326 -8.898  13.452  1.00 23.60 ? 162 MET A SD  1 
ATOM   1268 C  CE  . MET A 1 162 ? 12.479 -9.813  12.165  1.00 25.03 ? 162 MET A CE  1 
ATOM   1269 N  N   . HIS A 1 163 ? 11.464 -4.218  12.412  1.00 16.83 ? 163 HIS A N   1 
ATOM   1270 C  CA  . HIS A 1 163 ? 11.059 -3.141  13.318  1.00 15.29 ? 163 HIS A CA  1 
ATOM   1271 C  C   . HIS A 1 163 ? 11.394 -3.437  14.787  1.00 15.92 ? 163 HIS A C   1 
ATOM   1272 O  O   . HIS A 1 163 ? 11.030 -4.493  15.314  1.00 17.85 ? 163 HIS A O   1 
ATOM   1273 C  CB  . HIS A 1 163 ? 9.561  -2.868  13.178  1.00 20.48 ? 163 HIS A CB  1 
ATOM   1274 C  CG  . HIS A 1 163 ? 9.132  -1.653  13.923  1.00 19.08 ? 163 HIS A CG  1 
ATOM   1275 N  ND1 . HIS A 1 163 ? 9.762  -0.437  13.772  1.00 18.32 ? 163 HIS A ND1 1 
ATOM   1276 C  CD2 . HIS A 1 163 ? 8.184  -1.478  14.872  1.00 18.09 ? 163 HIS A CD2 1 
ATOM   1277 C  CE1 . HIS A 1 163 ? 9.208  0.441   14.590  1.00 18.82 ? 163 HIS A CE1 1 
ATOM   1278 N  NE2 . HIS A 1 163 ? 8.236  -0.159  15.250  1.00 19.01 ? 163 HIS A NE2 1 
ATOM   1279 N  N   . HIS A 1 164 ? 12.055 -2.478  15.457  1.00 17.89 ? 164 HIS A N   1 
ATOM   1280 C  CA  . HIS A 1 164 ? 12.440 -2.623  16.860  1.00 17.02 ? 164 HIS A CA  1 
ATOM   1281 C  C   . HIS A 1 164 ? 11.843 -1.587  17.800  1.00 20.49 ? 164 HIS A C   1 
ATOM   1282 O  O   . HIS A 1 164 ? 11.437 -1.953  18.910  1.00 21.72 ? 164 HIS A O   1 
ATOM   1283 C  CB  . HIS A 1 164 ? 13.973 -2.581  17.033  1.00 17.96 ? 164 HIS A CB  1 
ATOM   1284 C  CG  . HIS A 1 164 ? 14.674 -3.820  16.582  1.00 18.93 ? 164 HIS A CG  1 
ATOM   1285 N  ND1 . HIS A 1 164 ? 15.386 -4.621  17.450  1.00 16.91 ? 164 HIS A ND1 1 
ATOM   1286 C  CD2 . HIS A 1 164 ? 14.813 -4.378  15.357  1.00 18.89 ? 164 HIS A CD2 1 
ATOM   1287 C  CE1 . HIS A 1 164 ? 15.913 -5.631  16.783  1.00 17.17 ? 164 HIS A CE1 1 
ATOM   1288 N  NE2 . HIS A 1 164 ? 15.586 -5.505  15.509  1.00 17.71 ? 164 HIS A NE2 1 
ATOM   1289 N  N   . MET A 1 165 ? 11.877 -0.293  17.469  1.00 19.26 ? 165 MET A N   1 
ATOM   1290 C  CA  . MET A 1 165 ? 11.402 0.690   18.444  1.00 18.58 ? 165 MET A CA  1 
ATOM   1291 C  C   . MET A 1 165 ? 10.794 1.918   17.787  1.00 20.68 ? 165 MET A C   1 
ATOM   1292 O  O   . MET A 1 165 ? 11.083 2.258   16.640  1.00 16.86 ? 165 MET A O   1 
ATOM   1293 C  CB  . MET A 1 165 ? 12.491 1.153   19.441  1.00 20.82 ? 165 MET A CB  1 
ATOM   1294 C  CG  . MET A 1 165 ? 13.681 0.241   19.631  1.00 28.38 ? 165 MET A CG  1 
ATOM   1295 S  SD  . MET A 1 165 ? 14.919 1.003   20.702  1.00 30.97 ? 165 MET A SD  1 
ATOM   1296 C  CE  . MET A 1 165 ? 15.324 2.491   19.811  1.00 27.34 ? 165 MET A CE  1 
ATOM   1297 N  N   . GLU A 1 166 ? 9.956  2.592   18.570  1.00 18.80 ? 166 GLU A N   1 
ATOM   1298 C  CA  . GLU A 1 166 ? 9.456  3.929   18.270  1.00 18.47 ? 166 GLU A CA  1 
ATOM   1299 C  C   . GLU A 1 166 ? 10.132 4.926   19.199  1.00 19.77 ? 166 GLU A C   1 
ATOM   1300 O  O   . GLU A 1 166 ? 10.129 4.732   20.420  1.00 21.60 ? 166 GLU A O   1 
ATOM   1301 C  CB  . GLU A 1 166 ? 7.932  3.988   18.435  1.00 25.41 ? 166 GLU A CB  1 
ATOM   1302 C  CG  . GLU A 1 166 ? 7.304  5.332   18.066  1.00 23.47 ? 166 GLU A CG  1 
ATOM   1303 C  CD  . GLU A 1 166 ? 5.787  5.288   18.064  1.00 33.21 ? 166 GLU A CD  1 
ATOM   1304 O  OE1 . GLU A 1 166 ? 5.186  4.851   17.060  1.00 28.27 ? 166 GLU A OE1 1 
ATOM   1305 O  OE2 . GLU A 1 166 ? 5.190  5.619   19.115  1.00 33.86 ? 166 GLU A OE2 1 
ATOM   1306 N  N   . LEU A 1 167 ? 10.698 5.983   18.625  1.00 20.18 ? 167 LEU A N   1 
ATOM   1307 C  CA  . LEU A 1 167 ? 11.347 7.029   19.398  1.00 24.94 ? 167 LEU A CA  1 
ATOM   1308 C  C   . LEU A 1 167 ? 10.299 7.953   20.008  1.00 26.16 ? 167 LEU A C   1 
ATOM   1309 O  O   . LEU A 1 167 ? 9.157  7.992   19.550  1.00 26.17 ? 167 LEU A O   1 
ATOM   1310 C  CB  . LEU A 1 167 ? 12.301 7.831   18.521  1.00 25.71 ? 167 LEU A CB  1 
ATOM   1311 C  CG  . LEU A 1 167 ? 13.414 7.041   17.830  1.00 28.35 ? 167 LEU A CG  1 
ATOM   1312 C  CD1 . LEU A 1 167 ? 14.266 7.969   16.969  1.00 29.07 ? 167 LEU A CD1 1 
ATOM   1313 C  CD2 . LEU A 1 167 ? 14.247 6.306   18.846  1.00 24.16 ? 167 LEU A CD2 1 
ATOM   1314 N  N   . PRO A 1 168 ? 10.647 8.675   21.072  1.00 26.78 ? 168 PRO A N   1 
ATOM   1315 C  CA  . PRO A 1 168 ? 9.671  9.583   21.683  1.00 29.95 ? 168 PRO A CA  1 
ATOM   1316 C  C   . PRO A 1 168 ? 9.051  10.550  20.687  1.00 29.29 ? 168 PRO A C   1 
ATOM   1317 O  O   . PRO A 1 168 ? 7.940  11.041  20.916  1.00 31.30 ? 168 PRO A O   1 
ATOM   1318 C  CB  . PRO A 1 168 ? 10.501 10.319  22.739  1.00 24.85 ? 168 PRO A CB  1 
ATOM   1319 C  CG  . PRO A 1 168 ? 11.520 9.311   23.189  1.00 24.65 ? 168 PRO A CG  1 
ATOM   1320 C  CD  . PRO A 1 168 ? 11.709 8.312   22.030  1.00 26.55 ? 168 PRO A CD  1 
ATOM   1321 N  N   . THR A 1 169 ? 9.742  10.838  19.577  1.00 25.22 ? 169 THR A N   1 
ATOM   1322 C  CA  . THR A 1 169 ? 9.172  11.737  18.581  1.00 25.20 ? 169 THR A CA  1 
ATOM   1323 C  C   . THR A 1 169 ? 8.157  11.057  17.670  1.00 31.04 ? 169 THR A C   1 
ATOM   1324 O  O   . THR A 1 169 ? 7.484  11.751  16.901  1.00 39.43 ? 169 THR A O   1 
ATOM   1325 C  CB  . THR A 1 169 ? 10.263 12.372  17.705  1.00 35.99 ? 169 THR A CB  1 
ATOM   1326 O  OG1 . THR A 1 169 ? 11.182 11.366  17.251  1.00 30.34 ? 169 THR A OG1 1 
ATOM   1327 C  CG2 . THR A 1 169 ? 11.023 13.441  18.493  1.00 30.03 ? 169 THR A CG2 1 
ATOM   1328 N  N   . GLY A 1 170 ? 8.034  9.734   17.723  1.00 23.49 ? 170 GLY A N   1 
ATOM   1329 C  CA  . GLY A 1 170 ? 7.053  9.045   16.912  1.00 24.46 ? 170 GLY A CA  1 
ATOM   1330 C  C   . GLY A 1 170 ? 7.565  8.509   15.587  1.00 25.70 ? 170 GLY A C   1 
ATOM   1331 O  O   . GLY A 1 170 ? 6.755  8.062   14.769  1.00 30.63 ? 170 GLY A O   1 
ATOM   1332 N  N   . VAL A 1 171 ? 8.870  8.546   15.345  1.00 27.47 ? 171 VAL A N   1 
ATOM   1333 C  CA  . VAL A 1 171 ? 9.453  7.936   14.161  1.00 27.06 ? 171 VAL A CA  1 
ATOM   1334 C  C   . VAL A 1 171 ? 10.016 6.584   14.573  1.00 21.43 ? 171 VAL A C   1 
ATOM   1335 O  O   . VAL A 1 171 ? 10.097 6.256   15.753  1.00 23.29 ? 171 VAL A O   1 
ATOM   1336 C  CB  . VAL A 1 171 ? 10.534 8.824   13.503  1.00 27.29 ? 171 VAL A CB  1 
ATOM   1337 C  CG1 . VAL A 1 171 ? 9.922  10.131  13.001  1.00 32.73 ? 171 VAL A CG1 1 
ATOM   1338 C  CG2 . VAL A 1 171 ? 11.679 9.072   14.467  1.00 28.88 ? 171 VAL A CG2 1 
ATOM   1339 N  N   . HIS A 1 172 ? 10.400 5.785   13.591  1.00 16.15 ? 172 HIS A N   1 
ATOM   1340 C  CA  . HIS A 1 172 ? 10.591 4.358   13.803  1.00 20.71 ? 172 HIS A CA  1 
ATOM   1341 C  C   . HIS A 1 172 ? 12.004 3.952   13.417  1.00 18.88 ? 172 HIS A C   1 
ATOM   1342 O  O   . HIS A 1 172 ? 12.563 4.469   12.447  1.00 18.83 ? 172 HIS A O   1 
ATOM   1343 C  CB  . HIS A 1 172 ? 9.542  3.603   13.000  1.00 18.33 ? 172 HIS A CB  1 
ATOM   1344 C  CG  . HIS A 1 172 ? 8.151  3.948   13.420  1.00 19.49 ? 172 HIS A CG  1 
ATOM   1345 N  ND1 . HIS A 1 172 ? 7.215  4.465   12.551  1.00 22.06 ? 172 HIS A ND1 1 
ATOM   1346 C  CD2 . HIS A 1 172 ? 7.551  3.898   14.635  1.00 19.90 ? 172 HIS A CD2 1 
ATOM   1347 C  CE1 . HIS A 1 172 ? 6.091  4.696   13.207  1.00 23.43 ? 172 HIS A CE1 1 
ATOM   1348 N  NE2 . HIS A 1 172 ? 6.267  4.361   14.472  1.00 25.09 ? 172 HIS A NE2 1 
ATOM   1349 N  N   . VAL A 1 173 ? 12.594 3.047   14.205  1.00 18.45 ? 173 VAL A N   1 
ATOM   1350 C  CA  . VAL A 1 173 ? 13.974 2.620   14.012  1.00 17.43 ? 173 VAL A CA  1 
ATOM   1351 C  C   . VAL A 1 173 ? 14.046 1.105   14.135  1.00 22.55 ? 173 VAL A C   1 
ATOM   1352 O  O   . VAL A 1 173 ? 13.250 0.472   14.843  1.00 18.41 ? 173 VAL A O   1 
ATOM   1353 C  CB  . VAL A 1 173 ? 14.942 3.305   15.019  1.00 17.10 ? 173 VAL A CB  1 
ATOM   1354 C  CG1 . VAL A 1 173 ? 14.943 4.831   14.789  1.00 18.98 ? 173 VAL A CG1 1 
ATOM   1355 C  CG2 . VAL A 1 173 ? 14.568 2.968   16.455  1.00 18.70 ? 173 VAL A CG2 1 
ATOM   1356 N  N   . GLY A 1 174 ? 15.016 0.520   13.442  1.00 15.12 ? 174 GLY A N   1 
ATOM   1357 C  CA  . GLY A 1 174 ? 15.094 -0.928  13.385  1.00 21.31 ? 174 GLY A CA  1 
ATOM   1358 C  C   . GLY A 1 174 ? 16.418 -1.377  12.801  1.00 17.87 ? 174 GLY A C   1 
ATOM   1359 O  O   . GLY A 1 174 ? 17.338 -0.578  12.614  1.00 17.02 ? 174 GLY A O   1 
ATOM   1360 N  N   . THR A 1 175 ? 16.489 -2.673  12.481  1.00 17.65 ? 175 THR A N   1 
ATOM   1361 C  CA  . THR A 1 175 ? 17.713 -3.316  12.036  1.00 17.96 ? 175 THR A CA  1 
ATOM   1362 C  C   . THR A 1 175 ? 17.536 -3.917  10.646  1.00 15.84 ? 175 THR A C   1 
ATOM   1363 O  O   . THR A 1 175 ? 16.414 -4.069  10.136  1.00 17.60 ? 175 THR A O   1 
ATOM   1364 C  CB  . THR A 1 175 ? 18.147 -4.430  12.999  1.00 19.74 ? 175 THR A CB  1 
ATOM   1365 O  OG1 . THR A 1 175 ? 17.205 -5.510  12.921  1.00 20.01 ? 175 THR A OG1 1 
ATOM   1366 C  CG2 . THR A 1 175 ? 18.298 -3.931  14.465  1.00 15.84 ? 175 THR A CG2 1 
ATOM   1367 N  N   . ASP A 1 176 ? 18.669 -4.277  10.043  1.00 20.75 ? 176 ASP A N   1 
ATOM   1368 C  CA  . ASP A 1 176 ? 18.610 -5.230  8.948   1.00 19.63 ? 176 ASP A CA  1 
ATOM   1369 C  C   . ASP A 1 176 ? 18.395 -6.626  9.535   1.00 19.27 ? 176 ASP A C   1 
ATOM   1370 O  O   . ASP A 1 176 ? 18.237 -6.800  10.752  1.00 21.13 ? 176 ASP A O   1 
ATOM   1371 C  CB  . ASP A 1 176 ? 19.853 -5.105  8.060   1.00 24.68 ? 176 ASP A CB  1 
ATOM   1372 C  CG  . ASP A 1 176 ? 21.141 -5.427  8.788   1.00 23.23 ? 176 ASP A CG  1 
ATOM   1373 O  OD1 . ASP A 1 176 ? 21.095 -6.147  9.800   1.00 19.01 ? 176 ASP A OD1 1 
ATOM   1374 O  OD2 . ASP A 1 176 ? 22.210 -4.955  8.329   1.00 23.70 ? 176 ASP A OD2 1 
ATOM   1375 N  N   . LEU A 1 177 ? 18.365 -7.647  8.681   1.00 22.00 ? 177 LEU A N   1 
ATOM   1376 C  CA  . LEU A 1 177 ? 18.074 -8.980  9.197   1.00 20.35 ? 177 LEU A CA  1 
ATOM   1377 C  C   . LEU A 1 177 ? 19.310 -9.666  9.751   1.00 21.08 ? 177 LEU A C   1 
ATOM   1378 O  O   . LEU A 1 177 ? 19.212 -10.792 10.244  1.00 26.70 ? 177 LEU A O   1 
ATOM   1379 C  CB  . LEU A 1 177 ? 17.428 -9.849  8.123   1.00 19.58 ? 177 LEU A CB  1 
ATOM   1380 C  CG  . LEU A 1 177 ? 15.900 -9.811  8.103   1.00 20.19 ? 177 LEU A CG  1 
ATOM   1381 C  CD1 . LEU A 1 177 ? 15.341 -10.421 9.403   1.00 20.72 ? 177 LEU A CD1 1 
ATOM   1382 C  CD2 . LEU A 1 177 ? 15.387 -8.396  7.924   1.00 22.78 ? 177 LEU A CD2 1 
ATOM   1383 N  N   . GLU A 1 178 ? 20.467 -9.024  9.665   1.00 21.04 ? 178 GLU A N   1 
ATOM   1384 C  CA  . GLU A 1 178 ? 21.625 -9.429  10.444  1.00 20.11 ? 178 GLU A CA  1 
ATOM   1385 C  C   . GLU A 1 178 ? 21.611 -8.806  11.832  1.00 23.13 ? 178 GLU A C   1 
ATOM   1386 O  O   . GLU A 1 178 ? 22.547 -9.018  12.606  1.00 21.91 ? 178 GLU A O   1 
ATOM   1387 C  CB  . GLU A 1 178 ? 22.907 -9.036  9.701   1.00 27.85 ? 178 GLU A CB  1 
ATOM   1388 C  CG  . GLU A 1 178 ? 22.985 -9.591  8.280   1.00 37.60 ? 178 GLU A CG  1 
ATOM   1389 C  CD  . GLU A 1 178 ? 24.392 -9.591  7.715   1.00 46.65 ? 178 GLU A CD  1 
ATOM   1390 O  OE1 . GLU A 1 178 ? 25.107 -8.579  7.902   1.00 45.07 ? 178 GLU A OE1 1 
ATOM   1391 O  OE2 . GLU A 1 178 ? 24.772 -10.577 7.051   1.00 48.82 ? 178 GLU A OE2 1 
ATOM   1392 N  N   . GLY A 1 179 ? 20.595 -8.017  12.156  1.00 22.36 ? 179 GLY A N   1 
ATOM   1393 C  CA  . GLY A 1 179 ? 20.475 -7.499  13.506  1.00 17.82 ? 179 GLY A CA  1 
ATOM   1394 C  C   . GLY A 1 179 ? 21.242 -6.219  13.777  1.00 19.16 ? 179 GLY A C   1 
ATOM   1395 O  O   . GLY A 1 179 ? 21.280 -5.780  14.941  1.00 22.15 ? 179 GLY A O   1 
ATOM   1396 N  N   . ASN A 1 180 ? 21.826 -5.590  12.747  1.00 18.34 ? 180 ASN A N   1 
ATOM   1397 C  CA  . ASN A 1 180 ? 22.520 -4.316  12.913  1.00 22.03 ? 180 ASN A CA  1 
ATOM   1398 C  C   . ASN A 1 180 ? 21.554 -3.161  12.686  1.00 19.60 ? 180 ASN A C   1 
ATOM   1399 O  O   . ASN A 1 180 ? 20.929 -3.064  11.625  1.00 22.95 ? 180 ASN A O   1 
ATOM   1400 C  CB  . ASN A 1 180 ? 23.704 -4.185  11.957  1.00 21.09 ? 180 ASN A CB  1 
ATOM   1401 C  CG  . ASN A 1 180 ? 24.838 -5.109  12.315  1.00 24.57 ? 180 ASN A CG  1 
ATOM   1402 O  OD1 . ASN A 1 180 ? 25.342 -5.083  13.441  1.00 29.70 ? 180 ASN A OD1 1 
ATOM   1403 N  ND2 . ASN A 1 180 ? 25.234 -5.942  11.374  1.00 22.03 ? 180 ASN A ND2 1 
ATOM   1404 N  N   . PHE A 1 181 ? 21.445 -2.280  13.677  1.00 18.02 ? 181 PHE A N   1 
ATOM   1405 C  CA  . PHE A 1 181 ? 20.574 -1.124  13.530  1.00 17.43 ? 181 PHE A CA  1 
ATOM   1406 C  C   . PHE A 1 181 ? 20.990 -0.306  12.321  1.00 18.45 ? 181 PHE A C   1 
ATOM   1407 O  O   . PHE A 1 181 ? 22.178 -0.140  12.040  1.00 21.02 ? 181 PHE A O   1 
ATOM   1408 C  CB  . PHE A 1 181 ? 20.604 -0.241  14.783  1.00 20.54 ? 181 PHE A CB  1 
ATOM   1409 C  CG  . PHE A 1 181 ? 19.508 -0.568  15.761  1.00 19.26 ? 181 PHE A CG  1 
ATOM   1410 C  CD1 . PHE A 1 181 ? 18.243 0.005   15.621  1.00 21.80 ? 181 PHE A CD1 1 
ATOM   1411 C  CD2 . PHE A 1 181 ? 19.709 -1.521  16.745  1.00 18.66 ? 181 PHE A CD2 1 
ATOM   1412 C  CE1 . PHE A 1 181 ? 17.216 -0.322  16.505  1.00 17.62 ? 181 PHE A CE1 1 
ATOM   1413 C  CE2 . PHE A 1 181 ? 18.698 -1.854  17.641  1.00 19.46 ? 181 PHE A CE2 1 
ATOM   1414 C  CZ  . PHE A 1 181 ? 17.430 -1.262  17.502  1.00 18.44 ? 181 PHE A CZ  1 
ATOM   1415 N  N   . TYR A 1 182 ? 19.990 0.210   11.618  1.00 17.94 ? 182 TYR A N   1 
ATOM   1416 C  CA  . TYR A 1 182 ? 20.189 1.366   10.763  1.00 20.60 ? 182 TYR A CA  1 
ATOM   1417 C  C   . TYR A 1 182 ? 20.414 2.614   11.615  1.00 23.36 ? 182 TYR A C   1 
ATOM   1418 O  O   . TYR A 1 182 ? 19.637 2.911   12.535  1.00 23.47 ? 182 TYR A O   1 
ATOM   1419 C  CB  . TYR A 1 182 ? 18.988 1.544   9.840   1.00 21.29 ? 182 TYR A CB  1 
ATOM   1420 C  CG  . TYR A 1 182 ? 18.897 0.473   8.767   1.00 17.21 ? 182 TYR A CG  1 
ATOM   1421 C  CD1 . TYR A 1 182 ? 19.680 0.557   7.612   1.00 18.77 ? 182 TYR A CD1 1 
ATOM   1422 C  CD2 . TYR A 1 182 ? 18.029 -0.616  8.905   1.00 17.70 ? 182 TYR A CD2 1 
ATOM   1423 C  CE1 . TYR A 1 182 ? 19.602 -0.415  6.611   1.00 18.62 ? 182 TYR A CE1 1 
ATOM   1424 C  CE2 . TYR A 1 182 ? 17.942 -1.593  7.927   1.00 21.90 ? 182 TYR A CE2 1 
ATOM   1425 C  CZ  . TYR A 1 182 ? 18.725 -1.487  6.771   1.00 17.90 ? 182 TYR A CZ  1 
ATOM   1426 O  OH  . TYR A 1 182 ? 18.640 -2.461  5.794   1.00 20.92 ? 182 TYR A OH  1 
ATOM   1427 N  N   . GLY A 1 183 ? 21.481 3.345   11.302  1.00 21.50 ? 183 GLY A N   1 
ATOM   1428 C  CA  . GLY A 1 183 ? 21.843 4.519   12.059  1.00 22.93 ? 183 GLY A CA  1 
ATOM   1429 C  C   . GLY A 1 183 ? 22.408 4.182   13.435  1.00 25.22 ? 183 GLY A C   1 
ATOM   1430 O  O   . GLY A 1 183 ? 22.751 3.030   13.750  1.00 21.79 ? 183 GLY A O   1 
ATOM   1431 N  N   . PRO A 1 184 ? 22.509 5.199   14.286  1.00 21.83 ? 184 PRO A N   1 
ATOM   1432 C  CA  . PRO A 1 184 ? 23.222 5.060   15.565  1.00 26.91 ? 184 PRO A CA  1 
ATOM   1433 C  C   . PRO A 1 184 ? 22.394 4.519   16.723  1.00 22.87 ? 184 PRO A C   1 
ATOM   1434 O  O   . PRO A 1 184 ? 22.871 4.553   17.859  1.00 26.23 ? 184 PRO A O   1 
ATOM   1435 C  CB  . PRO A 1 184 ? 23.659 6.507   15.846  1.00 28.69 ? 184 PRO A CB  1 
ATOM   1436 C  CG  . PRO A 1 184 ? 22.556 7.337   15.248  1.00 27.89 ? 184 PRO A CG  1 
ATOM   1437 C  CD  . PRO A 1 184 ? 22.077 6.584   14.026  1.00 21.34 ? 184 PRO A CD  1 
ATOM   1438 N  N   . PHE A 1 185 ? 21.201 3.999   16.473  1.00 23.95 ? 185 PHE A N   1 
ATOM   1439 C  CA  . PHE A 1 185 ? 20.276 3.662   17.544  1.00 19.82 ? 185 PHE A CA  1 
ATOM   1440 C  C   . PHE A 1 185 ? 20.663 2.351   18.216  1.00 22.85 ? 185 PHE A C   1 
ATOM   1441 O  O   . PHE A 1 185 ? 21.315 1.489   17.624  1.00 23.10 ? 185 PHE A O   1 
ATOM   1442 C  CB  . PHE A 1 185 ? 18.855 3.613   16.973  1.00 21.74 ? 185 PHE A CB  1 
ATOM   1443 C  CG  . PHE A 1 185 ? 18.477 4.884   16.257  1.00 21.16 ? 185 PHE A CG  1 
ATOM   1444 C  CD1 . PHE A 1 185 ? 18.231 6.052   16.987  1.00 21.21 ? 185 PHE A CD1 1 
ATOM   1445 C  CD2 . PHE A 1 185 ? 18.444 4.941   14.876  1.00 20.13 ? 185 PHE A CD2 1 
ATOM   1446 C  CE1 . PHE A 1 185 ? 17.911 7.235   16.346  1.00 26.64 ? 185 PHE A CE1 1 
ATOM   1447 C  CE2 . PHE A 1 185 ? 18.133 6.129   14.224  1.00 24.26 ? 185 PHE A CE2 1 
ATOM   1448 C  CZ  . PHE A 1 185 ? 17.870 7.275   14.951  1.00 21.27 ? 185 PHE A CZ  1 
ATOM   1449 N  N   . VAL A 1 186 ? 20.292 2.235   19.489  1.00 18.28 ? 186 VAL A N   1 
ATOM   1450 C  CA  . VAL A 1 186 ? 20.545 1.040   20.288  1.00 23.62 ? 186 VAL A CA  1 
ATOM   1451 C  C   . VAL A 1 186 ? 19.250 0.635   20.979  1.00 24.01 ? 186 VAL A C   1 
ATOM   1452 O  O   . VAL A 1 186 ? 18.398 1.481   21.271  1.00 24.51 ? 186 VAL A O   1 
ATOM   1453 C  CB  . VAL A 1 186 ? 21.665 1.289   21.315  1.00 30.00 ? 186 VAL A CB  1 
ATOM   1454 C  CG1 . VAL A 1 186 ? 22.989 1.511   20.581  1.00 26.89 ? 186 VAL A CG1 1 
ATOM   1455 C  CG2 . VAL A 1 186 ? 21.308 2.457   22.235  1.00 24.65 ? 186 VAL A CG2 1 
ATOM   1456 N  N   . ASP A 1 187 ? 19.095 -0.668  21.252  1.00 18.97 ? 187 ASP A N   1 
ATOM   1457 C  CA  . ASP A 1 187 ? 17.831 -1.167  21.800  1.00 20.04 ? 187 ASP A CA  1 
ATOM   1458 C  C   . ASP A 1 187 ? 17.865 -1.066  23.331  1.00 24.67 ? 187 ASP A C   1 
ATOM   1459 O  O   . ASP A 1 187 ? 17.984 -2.049  24.068  1.00 22.15 ? 187 ASP A O   1 
ATOM   1460 C  CB  . ASP A 1 187 ? 17.512 -2.586  21.323  1.00 16.84 ? 187 ASP A CB  1 
ATOM   1461 C  CG  . ASP A 1 187 ? 18.682 -3.538  21.400  1.00 23.61 ? 187 ASP A CG  1 
ATOM   1462 O  OD1 . ASP A 1 187 ? 19.773 -3.136  21.845  1.00 20.82 ? 187 ASP A OD1 1 
ATOM   1463 O  OD2 . ASP A 1 187 ? 18.489 -4.726  21.034  1.00 21.12 ? 187 ASP A OD2 1 
ATOM   1464 N  N   A ARG A 1 188 ? 17.786 0.182   23.790  0.43 21.50 ? 188 ARG A N   1 
ATOM   1465 N  N   B ARG A 1 188 ? 17.739 0.176   23.793  0.57 21.49 ? 188 ARG A N   1 
ATOM   1466 C  CA  A ARG A 1 188 ? 17.692 0.545   25.198  0.43 24.58 ? 188 ARG A CA  1 
ATOM   1467 C  CA  B ARG A 1 188 ? 17.670 0.505   25.209  0.57 24.54 ? 188 ARG A CA  1 
ATOM   1468 C  C   A ARG A 1 188 ? 16.702 1.692   25.326  0.43 26.97 ? 188 ARG A C   1 
ATOM   1469 C  C   B ARG A 1 188 ? 16.739 1.698   25.354  0.57 27.00 ? 188 ARG A C   1 
ATOM   1470 O  O   A ARG A 1 188 ? 16.644 2.562   24.454  0.43 24.67 ? 188 ARG A O   1 
ATOM   1471 O  O   B ARG A 1 188 ? 16.766 2.610   24.523  0.57 24.58 ? 188 ARG A O   1 
ATOM   1472 C  CB  A ARG A 1 188 ? 19.055 0.973   25.765  0.43 25.78 ? 188 ARG A CB  1 
ATOM   1473 C  CB  B ARG A 1 188 ? 19.055 0.853   25.768  0.57 25.75 ? 188 ARG A CB  1 
ATOM   1474 C  CG  A ARG A 1 188 ? 19.931 -0.148  26.304  0.43 29.60 ? 188 ARG A CG  1 
ATOM   1475 C  CG  B ARG A 1 188 ? 19.116 1.060   27.260  0.57 29.89 ? 188 ARG A CG  1 
ATOM   1476 C  CD  A ARG A 1 188 ? 21.408 0.260   26.273  0.43 21.77 ? 188 ARG A CD  1 
ATOM   1477 C  CD  B ARG A 1 188 ? 20.441 1.715   27.643  0.57 32.89 ? 188 ARG A CD  1 
ATOM   1478 N  NE  A ARG A 1 188 ? 21.575 1.687   26.511  0.43 31.27 ? 188 ARG A NE  1 
ATOM   1479 N  NE  B ARG A 1 188 ? 20.320 2.541   28.839  0.57 25.72 ? 188 ARG A NE  1 
ATOM   1480 C  CZ  A ARG A 1 188 ? 22.722 2.342   26.383  0.43 32.61 ? 188 ARG A CZ  1 
ATOM   1481 C  CZ  B ARG A 1 188 ? 21.336 2.867   29.626  0.57 38.44 ? 188 ARG A CZ  1 
ATOM   1482 N  NH1 A ARG A 1 188 ? 23.854 1.710   26.118  0.43 40.43 ? 188 ARG A NH1 1 
ATOM   1483 N  NH1 B ARG A 1 188 ? 22.580 2.538   29.318  0.57 35.55 ? 188 ARG A NH1 1 
ATOM   1484 N  NH2 A ARG A 1 188 ? 22.735 3.665   26.524  0.43 41.44 ? 188 ARG A NH2 1 
ATOM   1485 N  NH2 B ARG A 1 188 ? 21.099 3.542   30.748  0.57 38.11 ? 188 ARG A NH2 1 
ATOM   1486 N  N   . GLN A 1 189 ? 15.909 1.683   26.401  1.00 25.50 ? 189 GLN A N   1 
ATOM   1487 C  CA  . GLN A 1 189 ? 14.996 2.795   26.682  1.00 28.62 ? 189 GLN A CA  1 
ATOM   1488 C  C   . GLN A 1 189 ? 15.803 3.909   27.339  1.00 24.91 ? 189 GLN A C   1 
ATOM   1489 O  O   . GLN A 1 189 ? 15.799 4.095   28.556  1.00 33.47 ? 189 GLN A O   1 
ATOM   1490 C  CB  . GLN A 1 189 ? 13.836 2.371   27.577  1.00 26.62 ? 189 GLN A CB  1 
ATOM   1491 C  CG  . GLN A 1 189 ? 12.710 3.397   27.553  1.00 31.45 ? 189 GLN A CG  1 
ATOM   1492 C  CD  . GLN A 1 189 ? 11.437 2.926   28.232  1.00 34.73 ? 189 GLN A CD  1 
ATOM   1493 O  OE1 . GLN A 1 189 ? 11.174 1.731   28.339  1.00 38.69 ? 189 GLN A OE1 1 
ATOM   1494 N  NE2 . GLN A 1 189 ? 10.643 3.882   28.712  1.00 35.42 ? 189 GLN A NE2 1 
ATOM   1495 N  N   . THR A 1 190 ? 16.519 4.652   26.500  1.00 27.83 ? 190 THR A N   1 
ATOM   1496 C  CA  . THR A 1 190 ? 17.385 5.736   26.935  1.00 27.52 ? 190 THR A CA  1 
ATOM   1497 C  C   . THR A 1 190 ? 17.365 6.808   25.854  1.00 31.12 ? 190 THR A C   1 
ATOM   1498 O  O   . THR A 1 190 ? 17.062 6.533   24.691  1.00 30.33 ? 190 THR A O   1 
ATOM   1499 C  CB  . THR A 1 190 ? 18.812 5.237   27.204  1.00 27.35 ? 190 THR A CB  1 
ATOM   1500 O  OG1 . THR A 1 190 ? 19.563 6.255   27.874  1.00 38.60 ? 190 THR A OG1 1 
ATOM   1501 C  CG2 . THR A 1 190 ? 19.515 4.871   25.901  1.00 32.27 ? 190 THR A CG2 1 
ATOM   1502 N  N   . ALA A 1 191 ? 17.686 8.037   26.255  1.00 30.65 ? 191 ALA A N   1 
ATOM   1503 C  CA  . ALA A 1 191 ? 17.526 9.193   25.379  1.00 31.39 ? 191 ALA A CA  1 
ATOM   1504 C  C   . ALA A 1 191 ? 18.238 8.989   24.048  1.00 35.75 ? 191 ALA A C   1 
ATOM   1505 O  O   . ALA A 1 191 ? 19.439 8.705   24.002  1.00 29.50 ? 191 ALA A O   1 
ATOM   1506 C  CB  . ALA A 1 191 ? 18.052 10.455  26.068  1.00 32.96 ? 191 ALA A CB  1 
ATOM   1507 N  N   . GLN A 1 192 ? 17.488 9.167   22.968  1.00 30.02 ? 192 GLN A N   1 
ATOM   1508 C  CA  . GLN A 1 192 ? 17.969 8.945   21.610  1.00 30.07 ? 192 GLN A CA  1 
ATOM   1509 C  C   . GLN A 1 192 ? 17.154 9.838   20.692  1.00 33.42 ? 192 GLN A C   1 
ATOM   1510 O  O   . GLN A 1 192 ? 15.943 9.632   20.551  1.00 37.64 ? 192 GLN A O   1 
ATOM   1511 C  CB  . GLN A 1 192 ? 17.803 7.489   21.192  1.00 28.35 ? 192 GLN A CB  1 
ATOM   1512 C  CG  . GLN A 1 192 ? 18.575 6.525   22.028  1.00 35.83 ? 192 GLN A CG  1 
ATOM   1513 C  CD  . GLN A 1 192 ? 18.503 5.138   21.472  1.00 33.54 ? 192 GLN A CD  1 
ATOM   1514 O  OE1 . GLN A 1 192 ? 18.985 4.876   20.375  1.00 24.12 ? 192 GLN A OE1 1 
ATOM   1515 N  NE2 . GLN A 1 192 ? 17.903 4.226   22.235  1.00 28.42 ? 192 GLN A NE2 1 
ATOM   1516 N  N   . ALA A 1 193 ? 17.803 10.814  20.073  1.00 32.35 ? 193 ALA A N   1 
ATOM   1517 C  CA  . ALA A 1 193 ? 17.122 11.733  19.176  1.00 31.20 ? 193 ALA A CA  1 
ATOM   1518 C  C   . ALA A 1 193 ? 17.648 11.545  17.763  1.00 32.88 ? 193 ALA A C   1 
ATOM   1519 O  O   . ALA A 1 193 ? 18.839 11.287  17.561  1.00 29.25 ? 193 ALA A O   1 
ATOM   1520 C  CB  . ALA A 1 193 ? 17.302 13.187  19.614  1.00 26.92 ? 193 ALA A CB  1 
ATOM   1521 N  N   . ALA A 1 194 ? 16.751 11.671  16.793  1.00 28.00 ? 194 ALA A N   1 
ATOM   1522 C  CA  . ALA A 1 194 ? 17.125 11.536  15.392  1.00 26.03 ? 194 ALA A CA  1 
ATOM   1523 C  C   . ALA A 1 194 ? 17.752 12.822  14.875  1.00 26.96 ? 194 ALA A C   1 
ATOM   1524 O  O   . ALA A 1 194 ? 17.487 13.919  15.379  1.00 30.27 ? 194 ALA A O   1 
ATOM   1525 C  CB  . ALA A 1 194 ? 15.904 11.175  14.550  1.00 29.58 ? 194 ALA A CB  1 
ATOM   1526 N  N   . GLY A 1 195 ? 18.594 12.680  13.856  1.00 28.05 ? 195 GLY A N   1 
ATOM   1527 C  CA  . GLY A 1 195 ? 19.177 13.826  13.191  1.00 26.75 ? 195 GLY A CA  1 
ATOM   1528 C  C   . GLY A 1 195 ? 18.188 14.493  12.252  1.00 29.61 ? 195 GLY A C   1 
ATOM   1529 O  O   . GLY A 1 195 ? 17.001 14.172  12.206  1.00 23.19 ? 195 GLY A O   1 
ATOM   1530 N  N   . THR A 1 196 ? 18.716 15.426  11.462  1.00 24.91 ? 196 THR A N   1 
ATOM   1531 C  CA  . THR A 1 196 ? 17.901 16.207  10.543  1.00 27.53 ? 196 THR A CA  1 
ATOM   1532 C  C   . THR A 1 196 ? 17.242 15.283  9.530   1.00 23.07 ? 196 THR A C   1 
ATOM   1533 O  O   . THR A 1 196 ? 17.909 14.436  8.931   1.00 27.01 ? 196 THR A O   1 
ATOM   1534 C  CB  . THR A 1 196 ? 18.784 17.216  9.811   1.00 25.45 ? 196 THR A CB  1 
ATOM   1535 O  OG1 . THR A 1 196 ? 19.296 18.167  10.749  1.00 26.36 ? 196 THR A OG1 1 
ATOM   1536 C  CG2 . THR A 1 196 ? 17.952 17.970  8.772   1.00 29.02 ? 196 THR A CG2 1 
ATOM   1537 N  N   . ASP A 1 197 ? 15.938 15.446  9.314   1.00 24.73 ? 197 ASP A N   1 
ATOM   1538 C  CA  . ASP A 1 197 ? 15.257 14.671  8.269   1.00 31.73 ? 197 ASP A CA  1 
ATOM   1539 C  C   . ASP A 1 197 ? 15.270 15.445  6.957   1.00 30.68 ? 197 ASP A C   1 
ATOM   1540 O  O   . ASP A 1 197 ? 14.348 16.189  6.631   1.00 36.83 ? 197 ASP A O   1 
ATOM   1541 C  CB  . ASP A 1 197 ? 13.841 14.309  8.684   1.00 32.67 ? 197 ASP A CB  1 
ATOM   1542 C  CG  . ASP A 1 197 ? 13.246 13.223  7.810   1.00 40.23 ? 197 ASP A CG  1 
ATOM   1543 O  OD1 . ASP A 1 197 ? 13.989 12.585  7.021   1.00 26.73 ? 197 ASP A OD1 1 
ATOM   1544 O  OD2 . ASP A 1 197 ? 12.032 12.985  7.946   1.00 36.52 ? 197 ASP A OD2 1 
ATOM   1545 N  N   . THR A 1 198 ? 16.319 15.236  6.179   1.00 23.62 ? 198 THR A N   1 
ATOM   1546 C  CA  . THR A 1 198 ? 16.440 15.968  4.932   1.00 22.01 ? 198 THR A CA  1 
ATOM   1547 C  C   . THR A 1 198 ? 15.584 15.302  3.862   1.00 24.47 ? 198 THR A C   1 
ATOM   1548 O  O   . THR A 1 198 ? 15.068 14.200  4.048   1.00 20.00 ? 198 THR A O   1 
ATOM   1549 C  CB  . THR A 1 198 ? 17.896 16.027  4.496   1.00 23.91 ? 198 THR A CB  1 
ATOM   1550 O  OG1 . THR A 1 198 ? 18.451 14.714  4.560   1.00 36.12 ? 198 THR A OG1 1 
ATOM   1551 C  CG2 . THR A 1 198 ? 18.682 16.927  5.462   1.00 28.39 ? 198 THR A CG2 1 
ATOM   1552 N  N   . THR A 1 199 ? 15.418 15.988  2.733   1.00 19.64 ? 199 THR A N   1 
ATOM   1553 C  CA  . THR A 1 199 ? 14.624 15.460  1.625   1.00 18.81 ? 199 THR A CA  1 
ATOM   1554 C  C   . THR A 1 199 ? 15.518 14.757  0.609   1.00 19.99 ? 199 THR A C   1 
ATOM   1555 O  O   . THR A 1 199 ? 16.616 15.231  0.297   1.00 20.36 ? 199 THR A O   1 
ATOM   1556 C  CB  . THR A 1 199 ? 13.826 16.582  0.951   1.00 19.95 ? 199 THR A CB  1 
ATOM   1557 O  OG1 . THR A 1 199 ? 13.006 17.214  1.941   1.00 21.47 ? 199 THR A OG1 1 
ATOM   1558 C  CG2 . THR A 1 199 ? 12.938 16.053  -0.177  1.00 20.12 ? 199 THR A CG2 1 
ATOM   1559 N  N   . ILE A 1 200 ? 15.041 13.622  0.097   1.00 18.79 ? 200 ILE A N   1 
ATOM   1560 C  CA  . ILE A 1 200 ? 15.808 12.773  -0.815  1.00 20.44 ? 200 ILE A CA  1 
ATOM   1561 C  C   . ILE A 1 200 ? 15.647 13.332  -2.227  1.00 17.81 ? 200 ILE A C   1 
ATOM   1562 O  O   . ILE A 1 200 ? 14.682 13.023  -2.928  1.00 16.68 ? 200 ILE A O   1 
ATOM   1563 C  CB  . ILE A 1 200 ? 15.366 11.311  -0.734  1.00 17.57 ? 200 ILE A CB  1 
ATOM   1564 C  CG1 . ILE A 1 200 ? 15.256 10.880  0.741   1.00 18.32 ? 200 ILE A CG1 1 
ATOM   1565 C  CG2 . ILE A 1 200 ? 16.282 10.409  -1.564  1.00 17.36 ? 200 ILE A CG2 1 
ATOM   1566 C  CD1 . ILE A 1 200 ? 14.324 9.683   0.972   1.00 18.92 ? 200 ILE A CD1 1 
ATOM   1567 N  N   . THR A 1 201 ? 16.645 14.096  -2.671  1.00 16.79 ? 201 THR A N   1 
ATOM   1568 C  CA  . THR A 1 201 ? 16.538 14.866  -3.903  1.00 21.56 ? 201 THR A CA  1 
ATOM   1569 C  C   . THR A 1 201 ? 16.325 13.976  -5.123  1.00 17.25 ? 201 THR A C   1 
ATOM   1570 O  O   . THR A 1 201 ? 15.468 14.270  -5.958  1.00 17.63 ? 201 THR A O   1 
ATOM   1571 C  CB  . THR A 1 201 ? 17.790 15.712  -4.066  1.00 19.80 ? 201 THR A CB  1 
ATOM   1572 O  OG1 . THR A 1 201 ? 18.014 16.405  -2.835  1.00 21.33 ? 201 THR A OG1 1 
ATOM   1573 C  CG2 . THR A 1 201 ? 17.605 16.726  -5.179  1.00 16.98 ? 201 THR A CG2 1 
ATOM   1574 N  N   . VAL A 1 202 ? 17.099 12.893  -5.251  1.00 17.78 ? 202 VAL A N   1 
ATOM   1575 C  CA  . VAL A 1 202 ? 16.965 12.059  -6.445  1.00 18.18 ? 202 VAL A CA  1 
ATOM   1576 C  C   . VAL A 1 202 ? 15.550 11.507  -6.533  1.00 21.44 ? 202 VAL A C   1 
ATOM   1577 O  O   . VAL A 1 202 ? 15.004 11.342  -7.631  1.00 17.72 ? 202 VAL A O   1 
ATOM   1578 C  CB  . VAL A 1 202 ? 18.018 10.934  -6.466  1.00 18.58 ? 202 VAL A CB  1 
ATOM   1579 C  CG1 . VAL A 1 202 ? 17.868 9.991   -5.274  1.00 21.94 ? 202 VAL A CG1 1 
ATOM   1580 C  CG2 . VAL A 1 202 ? 17.962 10.151  -7.800  1.00 19.71 ? 202 VAL A CG2 1 
ATOM   1581 N  N   . ASN A 1 203 ? 14.931 11.218  -5.379  1.00 17.82 ? 203 ASN A N   1 
ATOM   1582 C  CA  . ASN A 1 203 ? 13.566 10.691  -5.416  1.00 14.93 ? 203 ASN A CA  1 
ATOM   1583 C  C   . ASN A 1 203 ? 12.555 11.752  -5.834  1.00 14.90 ? 203 ASN A C   1 
ATOM   1584 O  O   . ASN A 1 203 ? 11.602 11.447  -6.565  1.00 16.56 ? 203 ASN A O   1 
ATOM   1585 C  CB  . ASN A 1 203 ? 13.182 10.096  -4.061  1.00 16.76 ? 203 ASN A CB  1 
ATOM   1586 C  CG  . ASN A 1 203 ? 13.919 8.804   -3.753  1.00 19.01 ? 203 ASN A CG  1 
ATOM   1587 O  OD1 . ASN A 1 203 ? 14.725 8.300   -4.554  1.00 19.18 ? 203 ASN A OD1 1 
ATOM   1588 N  ND2 . ASN A 1 203 ? 13.635 8.251   -2.570  1.00 19.53 ? 203 ASN A ND2 1 
ATOM   1589 N  N   . VAL A 1 204 ? 12.710 12.992  -5.364  1.00 17.18 ? 204 VAL A N   1 
ATOM   1590 C  CA  . VAL A 1 204 ? 11.821 14.063  -5.817  1.00 15.37 ? 204 VAL A CA  1 
ATOM   1591 C  C   . VAL A 1 204 ? 11.901 14.193  -7.342  1.00 15.75 ? 204 VAL A C   1 
ATOM   1592 O  O   . VAL A 1 204 ? 10.876 14.249  -8.035  1.00 17.56 ? 204 VAL A O   1 
ATOM   1593 C  CB  . VAL A 1 204 ? 12.156 15.391  -5.109  1.00 15.09 ? 204 VAL A CB  1 
ATOM   1594 C  CG1 . VAL A 1 204 ? 11.322 16.543  -5.700  1.00 17.25 ? 204 VAL A CG1 1 
ATOM   1595 C  CG2 . VAL A 1 204 ? 11.869 15.261  -3.616  1.00 14.75 ? 204 VAL A CG2 1 
ATOM   1596 N  N   . LEU A 1 205 ? 13.124 14.186  -7.885  1.00 16.03 ? 205 LEU A N   1 
ATOM   1597 C  CA  . LEU A 1 205 ? 13.295 14.289  -9.334  1.00 15.79 ? 205 LEU A CA  1 
ATOM   1598 C  C   . LEU A 1 205 ? 12.609 13.127  -10.035 1.00 15.57 ? 205 LEU A C   1 
ATOM   1599 O  O   . LEU A 1 205 ? 11.920 13.323  -11.040 1.00 17.18 ? 205 LEU A O   1 
ATOM   1600 C  CB  . LEU A 1 205 ? 14.779 14.338  -9.707  1.00 17.57 ? 205 LEU A CB  1 
ATOM   1601 C  CG  . LEU A 1 205 ? 15.503 15.623  -9.274  1.00 19.59 ? 205 LEU A CG  1 
ATOM   1602 C  CD1 . LEU A 1 205 ? 17.028 15.487  -9.390  1.00 18.24 ? 205 LEU A CD1 1 
ATOM   1603 C  CD2 . LEU A 1 205 ? 14.995 16.843  -10.017 1.00 19.38 ? 205 LEU A CD2 1 
ATOM   1604 N  N   . ALA A 1 206 ? 12.773 11.908  -9.514  1.00 15.59 ? 206 ALA A N   1 
ATOM   1605 C  CA  . ALA A 1 206 ? 12.087 10.765  -10.113 1.00 16.47 ? 206 ALA A CA  1 
ATOM   1606 C  C   . ALA A 1 206 ? 10.581 10.984  -10.124 1.00 21.12 ? 206 ALA A C   1 
ATOM   1607 O  O   . ALA A 1 206 ? 9.913  10.709  -11.122 1.00 17.71 ? 206 ALA A O   1 
ATOM   1608 C  CB  . ALA A 1 206 ? 12.436 9.470   -9.381  1.00 15.91 ? 206 ALA A CB  1 
ATOM   1609 N  N   . TRP A 1 207 ? 10.029 11.491  -9.021  1.00 15.60 ? 207 TRP A N   1 
ATOM   1610 C  CA  . TRP A 1 207 ? 8.587  11.729  -8.973  1.00 19.43 ? 207 TRP A CA  1 
ATOM   1611 C  C   . TRP A 1 207 ? 8.149  12.848  -9.920  1.00 22.03 ? 207 TRP A C   1 
ATOM   1612 O  O   . TRP A 1 207 ? 7.042  12.790  -10.484 1.00 18.09 ? 207 TRP A O   1 
ATOM   1613 C  CB  . TRP A 1 207 ? 8.214  12.023  -7.517  1.00 21.03 ? 207 TRP A CB  1 
ATOM   1614 C  CG  . TRP A 1 207 ? 6.807  12.455  -7.217  1.00 24.99 ? 207 TRP A CG  1 
ATOM   1615 C  CD1 . TRP A 1 207 ? 5.697  11.661  -7.091  1.00 21.96 ? 207 TRP A CD1 1 
ATOM   1616 C  CD2 . TRP A 1 207 ? 6.382  13.786  -6.930  1.00 18.51 ? 207 TRP A CD2 1 
ATOM   1617 N  NE1 . TRP A 1 207 ? 4.607  12.428  -6.765  1.00 20.99 ? 207 TRP A NE1 1 
ATOM   1618 C  CE2 . TRP A 1 207 ? 5.004  13.737  -6.658  1.00 17.76 ? 207 TRP A CE2 1 
ATOM   1619 C  CE3 . TRP A 1 207 ? 7.041  15.018  -6.863  1.00 22.26 ? 207 TRP A CE3 1 
ATOM   1620 C  CZ2 . TRP A 1 207 ? 4.269  14.874  -6.328  1.00 23.66 ? 207 TRP A CZ2 1 
ATOM   1621 C  CZ3 . TRP A 1 207 ? 6.303  16.150  -6.541  1.00 24.26 ? 207 TRP A CZ3 1 
ATOM   1622 C  CH2 . TRP A 1 207 ? 4.939  16.070  -6.282  1.00 21.92 ? 207 TRP A CH2 1 
ATOM   1623 N  N   . LEU A 1 208 ? 8.991  13.861  -10.141 1.00 15.71 ? 208 LEU A N   1 
ATOM   1624 C  CA  . LEU A 1 208 ? 8.652  14.864  -11.145 1.00 16.07 ? 208 LEU A CA  1 
ATOM   1625 C  C   . LEU A 1 208 ? 8.614  14.242  -12.548 1.00 17.72 ? 208 LEU A C   1 
ATOM   1626 O  O   . LEU A 1 208 ? 7.759  14.593  -13.368 1.00 18.09 ? 208 LEU A O   1 
ATOM   1627 C  CB  . LEU A 1 208 ? 9.664  16.011  -11.073 1.00 19.27 ? 208 LEU A CB  1 
ATOM   1628 C  CG  . LEU A 1 208 ? 9.497  16.910  -9.834  1.00 21.74 ? 208 LEU A CG  1 
ATOM   1629 C  CD1 . LEU A 1 208 ? 10.545 18.011  -9.813  1.00 24.72 ? 208 LEU A CD1 1 
ATOM   1630 C  CD2 . LEU A 1 208 ? 8.063  17.488  -9.741  1.00 21.15 ? 208 LEU A CD2 1 
ATOM   1631 N  N   . TYR A 1 209 ? 9.528  13.306  -12.838 1.00 18.70 ? 209 TYR A N   1 
ATOM   1632 C  CA  . TYR A 1 209 ? 9.453  12.573  -14.104 1.00 18.44 ? 209 TYR A CA  1 
ATOM   1633 C  C   . TYR A 1 209 ? 8.173  11.750  -14.182 1.00 19.04 ? 209 TYR A C   1 
ATOM   1634 O  O   . TYR A 1 209 ? 7.504  11.729  -15.214 1.00 19.51 ? 209 TYR A O   1 
ATOM   1635 C  CB  . TYR A 1 209 ? 10.667 11.671  -14.279 1.00 17.68 ? 209 TYR A CB  1 
ATOM   1636 C  CG  . TYR A 1 209 ? 11.904 12.391  -14.784 1.00 19.58 ? 209 TYR A CG  1 
ATOM   1637 C  CD1 . TYR A 1 209 ? 11.965 12.881  -16.086 1.00 21.52 ? 209 TYR A CD1 1 
ATOM   1638 C  CD2 . TYR A 1 209 ? 13.010 12.559  -13.969 1.00 19.24 ? 209 TYR A CD2 1 
ATOM   1639 C  CE1 . TYR A 1 209 ? 13.090 13.539  -16.552 1.00 19.21 ? 209 TYR A CE1 1 
ATOM   1640 C  CE2 . TYR A 1 209 ? 14.129 13.218  -14.421 1.00 19.11 ? 209 TYR A CE2 1 
ATOM   1641 C  CZ  . TYR A 1 209 ? 14.175 13.696  -15.710 1.00 22.07 ? 209 TYR A CZ  1 
ATOM   1642 O  OH  . TYR A 1 209 ? 15.302 14.351  -16.156 1.00 23.23 ? 209 TYR A OH  1 
ATOM   1643 N  N   . ALA A 1 210 ? 7.792  11.085  -13.084 1.00 17.07 ? 210 ALA A N   1 
ATOM   1644 C  CA  . ALA A 1 210 ? 6.504  10.389  -13.082 1.00 17.45 ? 210 ALA A CA  1 
ATOM   1645 C  C   . ALA A 1 210 ? 5.354  11.343  -13.392 1.00 20.38 ? 210 ALA A C   1 
ATOM   1646 O  O   . ALA A 1 210 ? 4.424  10.989  -14.139 1.00 21.08 ? 210 ALA A O   1 
ATOM   1647 C  CB  . ALA A 1 210 ? 6.269  9.693   -11.739 1.00 18.38 ? 210 ALA A CB  1 
ATOM   1648 N  N   . ALA A 1 211 ? 5.379  12.549  -12.811 1.00 18.09 ? 211 ALA A N   1 
ATOM   1649 C  CA  . ALA A 1 211 ? 4.328  13.524  -13.091 1.00 19.66 ? 211 ALA A CA  1 
ATOM   1650 C  C   . ALA A 1 211 ? 4.265  13.847  -14.576 1.00 24.53 ? 211 ALA A C   1 
ATOM   1651 O  O   . ALA A 1 211 ? 3.185  13.857  -15.177 1.00 24.37 ? 211 ALA A O   1 
ATOM   1652 C  CB  . ALA A 1 211 ? 4.556  14.794  -12.279 1.00 24.00 ? 211 ALA A CB  1 
ATOM   1653 N  N   . VAL A 1 212 ? 5.418  14.113  -15.190 1.00 18.57 ? 212 VAL A N   1 
ATOM   1654 C  CA  . VAL A 1 212 ? 5.437  14.443  -16.613 1.00 21.98 ? 212 VAL A CA  1 
ATOM   1655 C  C   . VAL A 1 212 ? 4.838  13.301  -17.424 1.00 24.02 ? 212 VAL A C   1 
ATOM   1656 O  O   . VAL A 1 212 ? 3.974  13.507  -18.287 1.00 27.90 ? 212 VAL A O   1 
ATOM   1657 C  CB  . VAL A 1 212 ? 6.871  14.761  -17.076 1.00 20.73 ? 212 VAL A CB  1 
ATOM   1658 C  CG1 . VAL A 1 212 ? 6.901  14.867  -18.602 1.00 18.46 ? 212 VAL A CG1 1 
ATOM   1659 C  CG2 . VAL A 1 212 ? 7.383  16.046  -16.446 1.00 20.78 ? 212 VAL A CG2 1 
ATOM   1660 N  N   . ILE A 1 213 ? 5.306  12.076  -17.170 1.00 19.94 ? 213 ILE A N   1 
ATOM   1661 C  CA  . ILE A 1 213 ? 4.784  10.907  -17.874 1.00 22.15 ? 213 ILE A CA  1 
ATOM   1662 C  C   . ILE A 1 213 ? 3.270  10.833  -17.745 1.00 31.44 ? 213 ILE A C   1 
ATOM   1663 O  O   . ILE A 1 213 ? 2.585  10.358  -18.659 1.00 31.99 ? 213 ILE A O   1 
ATOM   1664 C  CB  . ILE A 1 213 ? 5.470  9.627   -17.341 1.00 28.65 ? 213 ILE A CB  1 
ATOM   1665 C  CG1 . ILE A 1 213 ? 6.953  9.634   -17.720 1.00 21.75 ? 213 ILE A CG1 1 
ATOM   1666 C  CG2 . ILE A 1 213 ? 4.793  8.378   -17.879 1.00 31.50 ? 213 ILE A CG2 1 
ATOM   1667 C  CD1 . ILE A 1 213 ? 7.791  8.635   -16.966 1.00 23.20 ? 213 ILE A CD1 1 
ATOM   1668 N  N   . ASN A 1 214 ? 2.717  11.316  -16.632 1.00 28.21 ? 214 ASN A N   1 
ATOM   1669 C  CA  . ASN A 1 214 ? 1.281  11.219  -16.401 1.00 34.49 ? 214 ASN A CA  1 
ATOM   1670 C  C   . ASN A 1 214 ? 0.500  12.450  -16.849 1.00 33.60 ? 214 ASN A C   1 
ATOM   1671 O  O   . ASN A 1 214 ? -0.731 12.438  -16.775 1.00 35.63 ? 214 ASN A O   1 
ATOM   1672 C  CB  . ASN A 1 214 ? 1.007  10.925  -14.931 1.00 30.90 ? 214 ASN A CB  1 
ATOM   1673 C  CG  . ASN A 1 214 ? 1.119  9.453   -14.630 1.00 38.14 ? 214 ASN A CG  1 
ATOM   1674 O  OD1 . ASN A 1 214 ? 2.209  8.934   -14.372 1.00 36.44 ? 214 ASN A OD1 1 
ATOM   1675 N  ND2 . ASN A 1 214 ? 0.002  8.752   -14.737 1.00 40.80 ? 214 ASN A ND2 1 
ATOM   1676 N  N   . GLY A 1 215 ? 1.165  13.501  -17.326 1.00 32.38 ? 215 GLY A N   1 
ATOM   1677 C  CA  . GLY A 1 215 ? 0.466  14.643  -17.884 1.00 31.02 ? 215 GLY A CA  1 
ATOM   1678 C  C   . GLY A 1 215 ? 0.425  15.873  -17.011 1.00 29.05 ? 215 GLY A C   1 
ATOM   1679 O  O   . GLY A 1 215 ? -0.153 16.885  -17.430 1.00 32.74 ? 215 GLY A O   1 
ATOM   1680 N  N   . ASP A 1 216 ? 1.011  15.822  -15.816 1.00 25.43 ? 216 ASP A N   1 
ATOM   1681 C  CA  . ASP A 1 216 ? 1.145  16.981  -14.940 1.00 26.82 ? 216 ASP A CA  1 
ATOM   1682 C  C   . ASP A 1 216 ? 2.411  17.707  -15.360 1.00 37.37 ? 216 ASP A C   1 
ATOM   1683 O  O   . ASP A 1 216 ? 3.513  17.341  -14.943 1.00 40.07 ? 216 ASP A O   1 
ATOM   1684 C  CB  . ASP A 1 216 ? 1.216  16.550  -13.477 1.00 25.61 ? 216 ASP A CB  1 
ATOM   1685 C  CG  . ASP A 1 216 ? -0.123 16.155  -12.923 1.00 50.08 ? 216 ASP A CG  1 
ATOM   1686 O  OD1 . ASP A 1 216 ? -0.856 15.417  -13.622 1.00 56.57 ? 216 ASP A OD1 1 
ATOM   1687 O  OD2 . ASP A 1 216 ? -0.441 16.575  -11.789 1.00 51.91 ? 216 ASP A OD2 1 
ATOM   1688 N  N   . ARG A 1 217 ? 2.259  18.733  -16.193 1.00 26.60 ? 217 ARG A N   1 
ATOM   1689 C  CA  . ARG A 1 217 ? 3.391  19.396  -16.826 1.00 28.58 ? 217 ARG A CA  1 
ATOM   1690 C  C   . ARG A 1 217 ? 3.579  20.846  -16.401 1.00 27.39 ? 217 ARG A C   1 
ATOM   1691 O  O   . ARG A 1 217 ? 4.542  21.481  -16.848 1.00 29.77 ? 217 ARG A O   1 
ATOM   1692 C  CB  . ARG A 1 217 ? 3.233  19.351  -18.356 1.00 29.49 ? 217 ARG A CB  1 
ATOM   1693 C  CG  . ARG A 1 217 ? 3.618  18.034  -19.028 1.00 31.24 ? 217 ARG A CG  1 
ATOM   1694 C  CD  . ARG A 1 217 ? 3.663  18.168  -20.569 1.00 37.47 ? 217 ARG A CD  1 
ATOM   1695 N  N   . TRP A 1 218 ? 2.697  21.395  -15.560 1.00 29.08 ? 218 TRP A N   1 
ATOM   1696 C  CA  . TRP A 1 218 ? 2.667  22.842  -15.349 1.00 27.16 ? 218 TRP A CA  1 
ATOM   1697 C  C   . TRP A 1 218 ? 3.956  23.387  -14.744 1.00 23.38 ? 218 TRP A C   1 
ATOM   1698 O  O   . TRP A 1 218 ? 4.263  24.566  -14.942 1.00 25.97 ? 218 TRP A O   1 
ATOM   1699 C  CB  . TRP A 1 218 ? 1.468  23.223  -14.471 1.00 28.73 ? 218 TRP A CB  1 
ATOM   1700 C  CG  . TRP A 1 218 ? 1.543  22.729  -13.043 1.00 27.57 ? 218 TRP A CG  1 
ATOM   1701 C  CD1 . TRP A 1 218 ? 0.897  21.639  -12.516 1.00 29.75 ? 218 TRP A CD1 1 
ATOM   1702 C  CD2 . TRP A 1 218 ? 2.283  23.313  -11.964 1.00 24.57 ? 218 TRP A CD2 1 
ATOM   1703 N  NE1 . TRP A 1 218 ? 1.195  21.509  -11.184 1.00 24.70 ? 218 TRP A NE1 1 
ATOM   1704 C  CE2 . TRP A 1 218 ? 2.046  22.522  -10.819 1.00 30.56 ? 218 TRP A CE2 1 
ATOM   1705 C  CE3 . TRP A 1 218 ? 3.126  24.427  -11.852 1.00 27.22 ? 218 TRP A CE3 1 
ATOM   1706 C  CZ2 . TRP A 1 218 ? 2.622  22.808  -9.578  1.00 25.88 ? 218 TRP A CZ2 1 
ATOM   1707 C  CZ3 . TRP A 1 218 ? 3.698  24.707  -10.610 1.00 32.97 ? 218 TRP A CZ3 1 
ATOM   1708 C  CH2 . TRP A 1 218 ? 3.442  23.903  -9.498  1.00 25.88 ? 218 TRP A CH2 1 
ATOM   1709 N  N   . PHE A 1 219 ? 4.717  22.563  -14.030 1.00 23.09 ? 219 PHE A N   1 
ATOM   1710 C  CA  . PHE A 1 219 ? 5.920  23.013  -13.331 1.00 24.52 ? 219 PHE A CA  1 
ATOM   1711 C  C   . PHE A 1 219 ? 7.158  23.029  -14.224 1.00 26.30 ? 219 PHE A C   1 
ATOM   1712 O  O   . PHE A 1 219 ? 8.211  23.531  -13.808 1.00 24.05 ? 219 PHE A O   1 
ATOM   1713 C  CB  . PHE A 1 219 ? 6.179  22.100  -12.130 1.00 24.84 ? 219 PHE A CB  1 
ATOM   1714 C  CG  . PHE A 1 219 ? 6.305  20.661  -12.517 1.00 21.57 ? 219 PHE A CG  1 
ATOM   1715 C  CD1 . PHE A 1 219 ? 7.538  20.134  -12.882 1.00 22.40 ? 219 PHE A CD1 1 
ATOM   1716 C  CD2 . PHE A 1 219 ? 5.183  19.845  -12.561 1.00 23.15 ? 219 PHE A CD2 1 
ATOM   1717 C  CE1 . PHE A 1 219 ? 7.655  18.808  -13.277 1.00 24.16 ? 219 PHE A CE1 1 
ATOM   1718 C  CE2 . PHE A 1 219 ? 5.290  18.525  -12.941 1.00 22.90 ? 219 PHE A CE2 1 
ATOM   1719 C  CZ  . PHE A 1 219 ? 6.526  18.005  -13.313 1.00 21.50 ? 219 PHE A CZ  1 
ATOM   1720 N  N   . LEU A 1 220 ? 7.078  22.447  -15.405 1.00 27.96 ? 220 LEU A N   1 
ATOM   1721 C  CA  . LEU A 1 220 ? 8.185  22.513  -16.345 1.00 22.62 ? 220 LEU A CA  1 
ATOM   1722 C  C   . LEU A 1 220 ? 8.418  23.962  -16.751 1.00 35.87 ? 220 LEU A C   1 
ATOM   1723 O  O   . LEU A 1 220 ? 7.504  24.627  -17.248 1.00 35.22 ? 220 LEU A O   1 
ATOM   1724 C  CB  . LEU A 1 220 ? 7.845  21.664  -17.565 1.00 27.32 ? 220 LEU A CB  1 
ATOM   1725 C  CG  . LEU A 1 220 ? 7.747  20.154  -17.331 1.00 23.43 ? 220 LEU A CG  1 
ATOM   1726 C  CD1 . LEU A 1 220 ? 7.353  19.444  -18.628 1.00 24.29 ? 220 LEU A CD1 1 
ATOM   1727 C  CD2 . LEU A 1 220 ? 9.055  19.609  -16.782 1.00 27.08 ? 220 LEU A CD2 1 
ATOM   1728 N  N   . ASN A 1 221 ? 9.626  24.463  -16.532 1.00 32.12 ? 221 ASN A N   1 
ATOM   1729 C  CA  . ASN A 1 221 ? 9.943  25.813  -16.961 1.00 36.02 ? 221 ASN A CA  1 
ATOM   1730 C  C   . ASN A 1 221 ? 10.963 25.741  -18.102 1.00 33.70 ? 221 ASN A C   1 
ATOM   1731 O  O   . ASN A 1 221 ? 11.279 24.671  -18.624 1.00 31.44 ? 221 ASN A O   1 
ATOM   1732 C  CB  . ASN A 1 221 ? 10.439 26.630  -15.770 1.00 30.13 ? 221 ASN A CB  1 
ATOM   1733 C  CG  . ASN A 1 221 ? 11.649 26.019  -15.117 1.00 38.66 ? 221 ASN A CG  1 
ATOM   1734 O  OD1 . ASN A 1 221 ? 12.497 25.413  -15.789 1.00 38.20 ? 221 ASN A OD1 1 
ATOM   1735 N  ND2 . ASN A 1 221 ? 11.725 26.129  -13.799 1.00 46.27 ? 221 ASN A ND2 1 
ATOM   1736 N  N   . ARG A 1 222 ? 11.478 26.886  -18.517 1.00 48.08 ? 222 ARG A N   1 
ATOM   1737 C  CA  . ARG A 1 222 ? 12.413 26.891  -19.633 1.00 43.96 ? 222 ARG A CA  1 
ATOM   1738 C  C   . ARG A 1 222 ? 13.809 27.313  -19.193 1.00 43.51 ? 222 ARG A C   1 
ATOM   1739 O  O   . ARG A 1 222 ? 14.573 27.891  -19.973 1.00 35.58 ? 222 ARG A O   1 
ATOM   1740 C  CB  . ARG A 1 222 ? 11.886 27.781  -20.752 1.00 65.03 ? 222 ARG A CB  1 
ATOM   1741 C  CG  . ARG A 1 222 ? 11.611 29.183  -20.318 1.00 59.71 ? 222 ARG A CG  1 
ATOM   1742 C  CD  . ARG A 1 222 ? 10.393 29.732  -21.020 1.00 76.41 ? 222 ARG A CD  1 
ATOM   1743 N  NE  . ARG A 1 222 ? 10.214 31.136  -20.686 1.00 82.52 ? 222 ARG A NE  1 
ATOM   1744 C  CZ  . ARG A 1 222 ? 9.839  31.579  -19.495 1.00 92.02 ? 222 ARG A CZ  1 
ATOM   1745 N  NH1 . ARG A 1 222 ? 9.596  30.748  -18.494 1.00 95.78 ? 222 ARG A NH1 1 
ATOM   1746 N  NH2 . ARG A 1 222 ? 9.713  32.889  -19.302 1.00 84.47 ? 222 ARG A NH2 1 
ATOM   1747 N  N   . PHE A 1 223 ? 14.156 27.007  -17.950 1.00 34.05 ? 223 PHE A N   1 
ATOM   1748 C  CA  . PHE A 1 223 ? 15.491 27.231  -17.423 1.00 29.20 ? 223 PHE A CA  1 
ATOM   1749 C  C   . PHE A 1 223 ? 16.247 25.911  -17.356 1.00 26.97 ? 223 PHE A C   1 
ATOM   1750 O  O   . PHE A 1 223 ? 15.674 24.822  -17.449 1.00 26.51 ? 223 PHE A O   1 
ATOM   1751 C  CB  . PHE A 1 223 ? 15.431 27.881  -16.034 1.00 34.92 ? 223 PHE A CB  1 
ATOM   1752 C  CG  . PHE A 1 223 ? 14.387 28.959  -15.918 1.00 39.12 ? 223 PHE A CG  1 
ATOM   1753 C  CD1 . PHE A 1 223 ? 13.502 28.984  -14.860 1.00 34.40 ? 223 PHE A CD1 1 
ATOM   1754 C  CD2 . PHE A 1 223 ? 14.260 29.922  -16.905 1.00 45.35 ? 223 PHE A CD2 1 
ATOM   1755 C  CE1 . PHE A 1 223 ? 12.539 29.974  -14.765 1.00 43.95 ? 223 PHE A CE1 1 
ATOM   1756 C  CE2 . PHE A 1 223 ? 13.294 30.905  -16.817 1.00 40.82 ? 223 PHE A CE2 1 
ATOM   1757 C  CZ  . PHE A 1 223 ? 12.434 30.931  -15.741 1.00 50.99 ? 223 PHE A CZ  1 
ATOM   1758 N  N   . THR A 1 224 ? 17.557 26.020  -17.213 1.00 23.54 ? 224 THR A N   1 
ATOM   1759 C  CA  . THR A 1 224 ? 18.381 24.886  -16.848 1.00 24.97 ? 224 THR A CA  1 
ATOM   1760 C  C   . THR A 1 224 ? 19.277 25.334  -15.700 1.00 27.70 ? 224 THR A C   1 
ATOM   1761 O  O   . THR A 1 224 ? 19.159 26.458  -15.199 1.00 25.40 ? 224 THR A O   1 
ATOM   1762 C  CB  . THR A 1 224 ? 19.169 24.361  -18.060 1.00 26.79 ? 224 THR A CB  1 
ATOM   1763 O  OG1 . THR A 1 224 ? 19.673 23.048  -17.787 1.00 27.68 ? 224 THR A OG1 1 
ATOM   1764 C  CG2 . THR A 1 224 ? 20.325 25.293  -18.424 1.00 27.44 ? 224 THR A CG2 1 
ATOM   1765 N  N   . THR A 1 225 ? 20.151 24.445  -15.249 1.00 24.75 ? 225 THR A N   1 
ATOM   1766 C  CA  . THR A 1 225 ? 21.099 24.791  -14.197 1.00 23.31 ? 225 THR A CA  1 
ATOM   1767 C  C   . THR A 1 225 ? 22.299 23.865  -14.313 1.00 26.57 ? 225 THR A C   1 
ATOM   1768 O  O   . THR A 1 225 ? 22.383 23.036  -15.229 1.00 26.56 ? 225 THR A O   1 
ATOM   1769 C  CB  . THR A 1 225 ? 20.463 24.706  -12.801 1.00 27.68 ? 225 THR A CB  1 
ATOM   1770 O  OG1 . THR A 1 225 ? 21.405 25.173  -11.832 1.00 30.66 ? 225 THR A OG1 1 
ATOM   1771 C  CG2 . THR A 1 225 ? 20.089 23.266  -12.460 1.00 25.17 ? 225 THR A CG2 1 
ATOM   1772 N  N   . THR A 1 226 ? 23.236 24.025  -13.381 1.00 26.20 ? 226 THR A N   1 
ATOM   1773 C  CA  . THR A 1 226 ? 24.369 23.132  -13.217 1.00 24.53 ? 226 THR A CA  1 
ATOM   1774 C  C   . THR A 1 226 ? 24.239 22.365  -11.911 1.00 27.24 ? 226 THR A C   1 
ATOM   1775 O  O   . THR A 1 226 ? 23.507 22.758  -11.003 1.00 26.45 ? 226 THR A O   1 
ATOM   1776 C  CB  . THR A 1 226 ? 25.693 23.890  -13.177 1.00 26.69 ? 226 THR A CB  1 
ATOM   1777 O  OG1 . THR A 1 226 ? 25.685 24.763  -12.039 1.00 29.01 ? 226 THR A OG1 1 
ATOM   1778 C  CG2 . THR A 1 226 ? 25.897 24.705  -14.433 1.00 28.20 ? 226 THR A CG2 1 
ATOM   1779 N  N   . LEU A 1 227 ? 25.006 21.280  -11.816 1.00 29.21 ? 227 LEU A N   1 
ATOM   1780 C  CA  . LEU A 1 227 ? 25.025 20.494  -10.589 1.00 25.79 ? 227 LEU A CA  1 
ATOM   1781 C  C   . LEU A 1 227 ? 25.418 21.353  -9.394  1.00 31.03 ? 227 LEU A C   1 
ATOM   1782 O  O   . LEU A 1 227 ? 24.738 21.343  -8.361  1.00 28.38 ? 227 LEU A O   1 
ATOM   1783 C  CB  . LEU A 1 227 ? 25.975 19.308  -10.754 1.00 30.18 ? 227 LEU A CB  1 
ATOM   1784 C  CG  . LEU A 1 227 ? 25.621 18.022  -10.007 1.00 37.75 ? 227 LEU A CG  1 
ATOM   1785 C  CD1 . LEU A 1 227 ? 24.140 17.682  -10.094 1.00 26.84 ? 227 LEU A CD1 1 
ATOM   1786 C  CD2 . LEU A 1 227 ? 26.467 16.884  -10.558 1.00 43.72 ? 227 LEU A CD2 1 
ATOM   1787 N  N   . ASN A 1 228 ? 26.508 22.122  -9.516  1.00 28.43 ? 228 ASN A N   1 
ATOM   1788 C  CA  . ASN A 1 228 ? 26.960 22.897  -8.364  1.00 27.46 ? 228 ASN A CA  1 
ATOM   1789 C  C   . ASN A 1 228 ? 25.946 23.964  -7.977  1.00 28.95 ? 228 ASN A C   1 
ATOM   1790 O  O   . ASN A 1 228 ? 25.707 24.196  -6.786  1.00 30.36 ? 228 ASN A O   1 
ATOM   1791 C  CB  . ASN A 1 228 ? 28.333 23.531  -8.617  1.00 27.77 ? 228 ASN A CB  1 
ATOM   1792 C  CG  . ASN A 1 228 ? 29.464 22.507  -8.582  1.00 40.32 ? 228 ASN A CG  1 
ATOM   1793 O  OD1 . ASN A 1 228 ? 29.406 21.536  -7.820  1.00 37.20 ? 228 ASN A OD1 1 
ATOM   1794 N  ND2 . ASN A 1 228 ? 30.547 22.782  -9.320  1.00 35.86 ? 228 ASN A ND2 1 
ATOM   1795 N  N   . ASP A 1 229 ? 25.335 24.627  -8.963  1.00 29.01 ? 229 ASP A N   1 
ATOM   1796 C  CA  . ASP A 1 229 ? 24.358 25.658  -8.633  1.00 30.19 ? 229 ASP A CA  1 
ATOM   1797 C  C   . ASP A 1 229 ? 23.113 25.049  -7.995  1.00 32.36 ? 229 ASP A C   1 
ATOM   1798 O  O   . ASP A 1 229 ? 22.591 25.576  -7.003  1.00 29.35 ? 229 ASP A O   1 
ATOM   1799 C  CB  . ASP A 1 229 ? 23.974 26.452  -9.880  1.00 32.56 ? 229 ASP A CB  1 
ATOM   1800 C  CG  . ASP A 1 229 ? 22.761 27.330  -9.653  1.00 41.46 ? 229 ASP A CG  1 
ATOM   1801 O  OD1 . ASP A 1 229 ? 22.813 28.173  -8.729  1.00 50.93 ? 229 ASP A OD1 1 
ATOM   1802 O  OD2 . ASP A 1 229 ? 21.756 27.172  -10.377 1.00 46.06 ? 229 ASP A OD2 1 
ATOM   1803 N  N   . PHE A 1 230 ? 22.617 23.943  -8.551  1.00 23.31 ? 230 PHE A N   1 
ATOM   1804 C  CA  . PHE A 1 230 ? 21.448 23.309  -7.958  1.00 24.97 ? 230 PHE A CA  1 
ATOM   1805 C  C   . PHE A 1 230 ? 21.729 22.934  -6.512  1.00 23.28 ? 230 PHE A C   1 
ATOM   1806 O  O   . PHE A 1 230 ? 20.903 23.166  -5.624  1.00 25.32 ? 230 PHE A O   1 
ATOM   1807 C  CB  . PHE A 1 230 ? 21.051 22.060  -8.739  1.00 25.51 ? 230 PHE A CB  1 
ATOM   1808 C  CG  . PHE A 1 230 ? 19.907 21.320  -8.114  1.00 25.64 ? 230 PHE A CG  1 
ATOM   1809 C  CD1 . PHE A 1 230 ? 18.612 21.810  -8.205  1.00 23.47 ? 230 PHE A CD1 1 
ATOM   1810 C  CD2 . PHE A 1 230 ? 20.144 20.213  -7.324  1.00 28.17 ? 230 PHE A CD2 1 
ATOM   1811 C  CE1 . PHE A 1 230 ? 17.563 21.151  -7.589  1.00 23.91 ? 230 PHE A CE1 1 
ATOM   1812 C  CE2 . PHE A 1 230 ? 19.107 19.556  -6.706  1.00 31.73 ? 230 PHE A CE2 1 
ATOM   1813 C  CZ  . PHE A 1 230 ? 17.811 20.024  -6.839  1.00 28.11 ? 230 PHE A CZ  1 
ATOM   1814 N  N   . ASN A 1 231 ? 22.903 22.347  -6.257  1.00 23.46 ? 231 ASN A N   1 
ATOM   1815 C  CA  . ASN A 1 231 ? 23.225 21.887  -4.909  1.00 28.84 ? 231 ASN A CA  1 
ATOM   1816 C  C   . ASN A 1 231 ? 23.299 23.036  -3.916  1.00 26.54 ? 231 ASN A C   1 
ATOM   1817 O  O   . ASN A 1 231 ? 22.947 22.859  -2.746  1.00 26.72 ? 231 ASN A O   1 
ATOM   1818 C  CB  . ASN A 1 231 ? 24.517 21.063  -4.941  1.00 28.51 ? 231 ASN A CB  1 
ATOM   1819 C  CG  . ASN A 1 231 ? 24.262 19.634  -5.418  1.00 33.42 ? 231 ASN A CG  1 
ATOM   1820 O  OD1 . ASN A 1 231 ? 23.159 19.118  -5.247  1.00 30.97 ? 231 ASN A OD1 1 
ATOM   1821 N  ND2 . ASN A 1 231 ? 25.249 19.014  -6.053  1.00 32.63 ? 231 ASN A ND2 1 
ATOM   1822 N  N   . LEU A 1 232 ? 23.713 24.224  -4.360  1.00 31.06 ? 232 LEU A N   1 
ATOM   1823 C  CA  . LEU A 1 232 ? 23.615 25.391  -3.489  1.00 28.63 ? 232 LEU A CA  1 
ATOM   1824 C  C   . LEU A 1 232 ? 22.176 25.590  -3.031  1.00 35.91 ? 232 LEU A C   1 
ATOM   1825 O  O   . LEU A 1 232 ? 21.923 25.908  -1.863  1.00 35.86 ? 232 LEU A O   1 
ATOM   1826 C  CB  . LEU A 1 232 ? 24.114 26.631  -4.224  1.00 34.06 ? 232 LEU A CB  1 
ATOM   1827 C  CG  . LEU A 1 232 ? 25.599 26.973  -4.209  1.00 42.10 ? 232 LEU A CG  1 
ATOM   1828 C  CD1 . LEU A 1 232 ? 25.786 28.335  -4.861  1.00 50.71 ? 232 LEU A CD1 1 
ATOM   1829 C  CD2 . LEU A 1 232 ? 26.182 26.956  -2.804  1.00 42.23 ? 232 LEU A CD2 1 
ATOM   1830 N  N   . VAL A 1 233 ? 21.221 25.403  -3.947  1.00 27.84 ? 233 VAL A N   1 
ATOM   1831 C  CA  . VAL A 1 233 ? 19.806 25.533  -3.613  1.00 23.38 ? 233 VAL A CA  1 
ATOM   1832 C  C   . VAL A 1 233 ? 19.336 24.351  -2.776  1.00 28.02 ? 233 VAL A C   1 
ATOM   1833 O  O   . VAL A 1 233 ? 18.602 24.524  -1.795  1.00 29.35 ? 233 VAL A O   1 
ATOM   1834 C  CB  . VAL A 1 233 ? 18.970 25.688  -4.896  1.00 30.53 ? 233 VAL A CB  1 
ATOM   1835 C  CG1 . VAL A 1 233 ? 17.490 25.787  -4.547  1.00 31.92 ? 233 VAL A CG1 1 
ATOM   1836 C  CG2 . VAL A 1 233 ? 19.421 26.919  -5.665  1.00 32.69 ? 233 VAL A CG2 1 
ATOM   1837 N  N   . ALA A 1 234 ? 19.746 23.132  -3.142  1.00 25.98 ? 234 ALA A N   1 
ATOM   1838 C  CA  . ALA A 1 234 ? 19.402 21.976  -2.317  1.00 29.85 ? 234 ALA A CA  1 
ATOM   1839 C  C   . ALA A 1 234 ? 19.789 22.196  -0.859  1.00 29.37 ? 234 ALA A C   1 
ATOM   1840 O  O   . ALA A 1 234 ? 19.007 21.903  0.052   1.00 31.05 ? 234 ALA A O   1 
ATOM   1841 C  CB  . ALA A 1 234 ? 20.074 20.713  -2.866  1.00 26.35 ? 234 ALA A CB  1 
ATOM   1842 N  N   . MET A 1 235 ? 20.993 22.716  -0.615  1.00 24.47 ? 235 MET A N   1 
ATOM   1843 C  CA  . MET A 1 235 ? 21.452 22.894  0.756   1.00 34.78 ? 235 MET A CA  1 
ATOM   1844 C  C   . MET A 1 235 ? 20.553 23.856  1.519   1.00 32.08 ? 235 MET A C   1 
ATOM   1845 O  O   . MET A 1 235 ? 20.201 23.605  2.675   1.00 30.31 ? 235 MET A O   1 
ATOM   1846 C  CB  . MET A 1 235 ? 22.891 23.397  0.766   1.00 39.00 ? 235 MET A CB  1 
ATOM   1847 C  CG  . MET A 1 235 ? 23.922 22.366  0.359   1.00 44.41 ? 235 MET A CG  1 
ATOM   1848 S  SD  . MET A 1 235 ? 25.335 22.454  1.484   1.00 78.25 ? 235 MET A SD  1 
ATOM   1849 C  CE  . MET A 1 235 ? 25.294 24.185  1.925   1.00 46.52 ? 235 MET A CE  1 
ATOM   1850 N  N   . LYS A 1 236 ? 20.164 24.957  0.881   1.00 30.13 ? 236 LYS A N   1 
ATOM   1851 C  CA  . LYS A 1 236 ? 19.343 25.957  1.550   1.00 27.20 ? 236 LYS A CA  1 
ATOM   1852 C  C   . LYS A 1 236 ? 17.999 25.389  1.997   1.00 28.05 ? 236 LYS A C   1 
ATOM   1853 O  O   . LYS A 1 236 ? 17.456 25.830  3.017   1.00 32.60 ? 236 LYS A O   1 
ATOM   1854 C  CB  . LYS A 1 236 ? 19.155 27.163  0.619   1.00 31.34 ? 236 LYS A CB  1 
ATOM   1855 C  CG  . LYS A 1 236 ? 18.105 28.179  1.050   1.00 34.49 ? 236 LYS A CG  1 
ATOM   1856 C  CD  . LYS A 1 236 ? 18.387 29.523  0.356   1.00 40.99 ? 236 LYS A CD  1 
ATOM   1857 C  CE  . LYS A 1 236 ? 17.201 30.486  0.365   1.00 53.42 ? 236 LYS A CE  1 
ATOM   1858 N  NZ  . LYS A 1 236 ? 16.006 29.979  1.097   1.00 54.73 ? 236 LYS A NZ  1 
ATOM   1859 N  N   . TYR A 1 237 ? 17.458 24.398  1.276   1.00 28.16 ? 237 TYR A N   1 
ATOM   1860 C  CA  . TYR A 1 237 ? 16.135 23.845  1.566   1.00 23.38 ? 237 TYR A CA  1 
ATOM   1861 C  C   . TYR A 1 237 ? 16.202 22.465  2.220   1.00 24.32 ? 237 TYR A C   1 
ATOM   1862 O  O   . TYR A 1 237 ? 15.202 21.741  2.258   1.00 22.87 ? 237 TYR A O   1 
ATOM   1863 C  CB  . TYR A 1 237 ? 15.303 23.807  0.283   1.00 21.61 ? 237 TYR A CB  1 
ATOM   1864 C  CG  . TYR A 1 237 ? 14.914 25.208  -0.158  1.00 28.63 ? 237 TYR A CG  1 
ATOM   1865 C  CD1 . TYR A 1 237 ? 13.797 25.842  0.378   1.00 30.70 ? 237 TYR A CD1 1 
ATOM   1866 C  CD2 . TYR A 1 237 ? 15.690 25.908  -1.074  1.00 25.49 ? 237 TYR A CD2 1 
ATOM   1867 C  CE1 . TYR A 1 237 ? 13.443 27.128  -0.010  1.00 25.29 ? 237 TYR A CE1 1 
ATOM   1868 C  CE2 . TYR A 1 237 ? 15.353 27.201  -1.460  1.00 30.34 ? 237 TYR A CE2 1 
ATOM   1869 C  CZ  . TYR A 1 237 ? 14.223 27.799  -0.925  1.00 37.81 ? 237 TYR A CZ  1 
ATOM   1870 O  OH  . TYR A 1 237 ? 13.871 29.073  -1.301  1.00 34.36 ? 237 TYR A OH  1 
ATOM   1871 N  N   . ASN A 1 238 ? 17.358 22.109  2.773   1.00 20.15 ? 238 ASN A N   1 
ATOM   1872 C  CA  . ASN A 1 238 ? 17.558 20.852  3.494   1.00 23.13 ? 238 ASN A CA  1 
ATOM   1873 C  C   . ASN A 1 238 ? 17.231 19.667  2.593   1.00 23.96 ? 238 ASN A C   1 
ATOM   1874 O  O   . ASN A 1 238 ? 16.600 18.696  3.016   1.00 23.39 ? 238 ASN A O   1 
ATOM   1875 C  CB  . ASN A 1 238 ? 16.739 20.802  4.787   1.00 25.05 ? 238 ASN A CB  1 
ATOM   1876 C  CG  . ASN A 1 238 ? 17.285 21.738  5.856   1.00 38.14 ? 238 ASN A CG  1 
ATOM   1877 O  OD1 . ASN A 1 238 ? 18.494 21.815  6.082   1.00 34.79 ? 238 ASN A OD1 1 
ATOM   1878 N  ND2 . ASN A 1 238 ? 16.388 22.448  6.523   1.00 44.68 ? 238 ASN A ND2 1 
ATOM   1879 N  N   . TYR A 1 239 ? 17.631 19.783  1.324   1.00 19.74 ? 239 TYR A N   1 
ATOM   1880 C  CA  . TYR A 1 239 ? 17.634 18.679  0.375   1.00 20.77 ? 239 TYR A CA  1 
ATOM   1881 C  C   . TYR A 1 239 ? 19.013 18.029  0.365   1.00 21.75 ? 239 TYR A C   1 
ATOM   1882 O  O   . TYR A 1 239 ? 20.027 18.698  0.572   1.00 21.85 ? 239 TYR A O   1 
ATOM   1883 C  CB  . TYR A 1 239 ? 17.289 19.182  -1.029  1.00 19.01 ? 239 TYR A CB  1 
ATOM   1884 C  CG  . TYR A 1 239 ? 15.817 19.163  -1.339  1.00 17.03 ? 239 TYR A CG  1 
ATOM   1885 C  CD1 . TYR A 1 239 ? 14.905 19.814  -0.517  1.00 20.69 ? 239 TYR A CD1 1 
ATOM   1886 C  CD2 . TYR A 1 239 ? 15.330 18.486  -2.446  1.00 22.49 ? 239 TYR A CD2 1 
ATOM   1887 C  CE1 . TYR A 1 239 ? 13.542 19.791  -0.805  1.00 22.61 ? 239 TYR A CE1 1 
ATOM   1888 C  CE2 . TYR A 1 239 ? 13.977 18.462  -2.733  1.00 18.25 ? 239 TYR A CE2 1 
ATOM   1889 C  CZ  . TYR A 1 239 ? 13.096 19.115  -1.920  1.00 22.29 ? 239 TYR A CZ  1 
ATOM   1890 O  OH  . TYR A 1 239 ? 11.746 19.093  -2.198  1.00 23.85 ? 239 TYR A OH  1 
ATOM   1891 N  N   . GLU A 1 240 ? 19.045 16.717  0.130   1.00 23.00 ? 240 GLU A N   1 
ATOM   1892 C  CA  . GLU A 1 240 ? 20.321 16.023  -0.012  1.00 29.74 ? 240 GLU A CA  1 
ATOM   1893 C  C   . GLU A 1 240 ? 21.036 16.497  -1.281  1.00 23.03 ? 240 GLU A C   1 
ATOM   1894 O  O   . GLU A 1 240 ? 20.387 16.816  -2.281  1.00 24.21 ? 240 GLU A O   1 
ATOM   1895 C  CB  . GLU A 1 240 ? 20.098 14.509  -0.066  1.00 31.71 ? 240 GLU A CB  1 
ATOM   1896 C  CG  . GLU A 1 240 ? 19.625 13.884  1.245   1.00 33.21 ? 240 GLU A CG  1 
ATOM   1897 C  CD  . GLU A 1 240 ? 20.737 13.736  2.280   1.00 41.46 ? 240 GLU A CD  1 
ATOM   1898 O  OE1 . GLU A 1 240 ? 21.601 12.846  2.113   1.00 43.68 ? 240 GLU A OE1 1 
ATOM   1899 O  OE2 . GLU A 1 240 ? 20.759 14.517  3.259   1.00 44.83 ? 240 GLU A OE2 1 
ATOM   1900 N  N   . PRO A 1 241 ? 22.368 16.571  -1.271  1.00 27.12 ? 241 PRO A N   1 
ATOM   1901 C  CA  . PRO A 1 241 ? 23.078 16.942  -2.498  1.00 24.57 ? 241 PRO A CA  1 
ATOM   1902 C  C   . PRO A 1 241 ? 22.858 15.898  -3.579  1.00 28.23 ? 241 PRO A C   1 
ATOM   1903 O  O   . PRO A 1 241 ? 22.714 14.706  -3.301  1.00 31.30 ? 241 PRO A O   1 
ATOM   1904 C  CB  . PRO A 1 241 ? 24.547 17.016  -2.059  1.00 36.04 ? 241 PRO A CB  1 
ATOM   1905 C  CG  . PRO A 1 241 ? 24.621 16.175  -0.823  1.00 42.81 ? 241 PRO A CG  1 
ATOM   1906 C  CD  . PRO A 1 241 ? 23.288 16.309  -0.147  1.00 32.41 ? 241 PRO A CD  1 
ATOM   1907 N  N   . LEU A 1 242 ? 22.776 16.376  -4.817  1.00 26.33 ? 242 LEU A N   1 
ATOM   1908 C  CA  . LEU A 1 242 ? 22.664 15.526  -5.992  1.00 25.58 ? 242 LEU A CA  1 
ATOM   1909 C  C   . LEU A 1 242 ? 24.058 15.247  -6.544  1.00 29.49 ? 242 LEU A C   1 
ATOM   1910 O  O   . LEU A 1 242 ? 24.898 16.149  -6.629  1.00 26.76 ? 242 LEU A O   1 
ATOM   1911 C  CB  . LEU A 1 242 ? 21.802 16.209  -7.055  1.00 28.41 ? 242 LEU A CB  1 
ATOM   1912 C  CG  . LEU A 1 242 ? 21.251 15.339  -8.182  1.00 29.09 ? 242 LEU A CG  1 
ATOM   1913 C  CD1 . LEU A 1 242 ? 20.203 14.393  -7.636  1.00 33.30 ? 242 LEU A CD1 1 
ATOM   1914 C  CD2 . LEU A 1 242 ? 20.657 16.235  -9.254  1.00 25.03 ? 242 LEU A CD2 1 
ATOM   1915 N  N   . THR A 1 243 ? 24.306 13.991  -6.899  1.00 28.49 ? 243 THR A N   1 
ATOM   1916 C  CA  . THR A 1 243 ? 25.596 13.578  -7.432  1.00 30.03 ? 243 THR A CA  1 
ATOM   1917 C  C   . THR A 1 243 ? 25.456 13.156  -8.888  1.00 26.79 ? 243 THR A C   1 
ATOM   1918 O  O   . THR A 1 243 ? 24.348 12.979  -9.412  1.00 27.67 ? 243 THR A O   1 
ATOM   1919 C  CB  . THR A 1 243 ? 26.185 12.421  -6.629  1.00 26.89 ? 243 THR A CB  1 
ATOM   1920 O  OG1 . THR A 1 243 ? 25.372 11.257  -6.828  1.00 29.54 ? 243 THR A OG1 1 
ATOM   1921 C  CG2 . THR A 1 243 ? 26.218 12.773  -5.148  1.00 28.92 ? 243 THR A CG2 1 
ATOM   1922 N  N   . GLN A 1 244 ? 26.612 12.996  -9.539  1.00 29.48 ? 244 GLN A N   1 
ATOM   1923 C  CA  . GLN A 1 244 ? 26.635 12.422  -10.882 1.00 30.19 ? 244 GLN A CA  1 
ATOM   1924 C  C   . GLN A 1 244 ? 26.036 11.023  -10.896 1.00 26.47 ? 244 GLN A C   1 
ATOM   1925 O  O   . GLN A 1 244 ? 25.360 10.640  -11.855 1.00 24.20 ? 244 GLN A O   1 
ATOM   1926 C  CB  . GLN A 1 244 ? 28.066 12.381  -11.420 1.00 29.23 ? 244 GLN A CB  1 
ATOM   1927 C  CG  . GLN A 1 244 ? 28.161 12.105  -12.926 1.00 28.49 ? 244 GLN A CG  1 
ATOM   1928 C  CD  . GLN A 1 244 ? 27.244 12.974  -13.747 1.00 26.61 ? 244 GLN A CD  1 
ATOM   1929 O  OE1 . GLN A 1 244 ? 27.311 14.202  -13.672 1.00 36.60 ? 244 GLN A OE1 1 
ATOM   1930 N  NE2 . GLN A 1 244 ? 26.396 12.348  -14.557 1.00 29.53 ? 244 GLN A NE2 1 
ATOM   1931 N  N   . ASP A 1 245 ? 26.295 10.231  -9.854  1.00 26.52 ? 245 ASP A N   1 
ATOM   1932 C  CA  . ASP A 1 245 ? 25.663 8.922   -9.783  1.00 26.38 ? 245 ASP A CA  1 
ATOM   1933 C  C   . ASP A 1 245 ? 24.148 9.051   -9.824  1.00 20.69 ? 245 ASP A C   1 
ATOM   1934 O  O   . ASP A 1 245 ? 23.478 8.303   -10.540 1.00 22.69 ? 245 ASP A O   1 
ATOM   1935 C  CB  . ASP A 1 245 ? 26.123 8.175   -8.530  1.00 33.87 ? 245 ASP A CB  1 
ATOM   1936 C  CG  . ASP A 1 245 ? 27.548 7.651   -8.647  1.00 39.74 ? 245 ASP A CG  1 
ATOM   1937 O  OD1 . ASP A 1 245 ? 28.191 7.859   -9.700  1.00 42.32 ? 245 ASP A OD1 1 
ATOM   1938 O  OD2 . ASP A 1 245 ? 28.031 7.046   -7.668  1.00 45.43 ? 245 ASP A OD2 1 
ATOM   1939 N  N   . HIS A 1 246 ? 23.588 9.998   -9.059  1.00 22.83 ? 246 HIS A N   1 
ATOM   1940 C  CA  . HIS A 1 246 ? 22.144 10.231  -9.113  1.00 23.95 ? 246 HIS A CA  1 
ATOM   1941 C  C   . HIS A 1 246 ? 21.697 10.640  -10.513 1.00 27.05 ? 246 HIS A C   1 
ATOM   1942 O  O   . HIS A 1 246 ? 20.641 10.202  -10.992 1.00 22.82 ? 246 HIS A O   1 
ATOM   1943 C  CB  . HIS A 1 246 ? 21.744 11.307  -8.105  1.00 22.59 ? 246 HIS A CB  1 
ATOM   1944 C  CG  . HIS A 1 246 ? 21.921 10.896  -6.677  1.00 23.96 ? 246 HIS A CG  1 
ATOM   1945 N  ND1 . HIS A 1 246 ? 22.375 11.763  -5.704  1.00 25.34 ? 246 HIS A ND1 1 
ATOM   1946 C  CD2 . HIS A 1 246 ? 21.671 9.722   -6.048  1.00 25.79 ? 246 HIS A CD2 1 
ATOM   1947 C  CE1 . HIS A 1 246 ? 22.414 11.134  -4.543  1.00 32.01 ? 246 HIS A CE1 1 
ATOM   1948 N  NE2 . HIS A 1 246 ? 21.989 9.896   -4.724  1.00 31.96 ? 246 HIS A NE2 1 
ATOM   1949 N  N   . VAL A 1 247 ? 22.462 11.515  -11.165 1.00 22.44 ? 247 VAL A N   1 
ATOM   1950 C  CA  . VAL A 1 247 ? 22.118 11.924  -12.526 1.00 25.23 ? 247 VAL A CA  1 
ATOM   1951 C  C   . VAL A 1 247 ? 22.043 10.706  -13.431 1.00 20.10 ? 247 VAL A C   1 
ATOM   1952 O  O   . VAL A 1 247 ? 21.124 10.581  -14.249 1.00 22.29 ? 247 VAL A O   1 
ATOM   1953 C  CB  . VAL A 1 247 ? 23.128 12.960  -13.053 1.00 23.41 ? 247 VAL A CB  1 
ATOM   1954 C  CG1 . VAL A 1 247 ? 22.862 13.279  -14.529 1.00 24.89 ? 247 VAL A CG1 1 
ATOM   1955 C  CG2 . VAL A 1 247 ? 23.071 14.221  -12.222 1.00 27.63 ? 247 VAL A CG2 1 
ATOM   1956 N  N   . ASP A 1 248 ? 22.993 9.774   -13.280 1.00 19.86 ? 248 ASP A N   1 
ATOM   1957 C  CA  . ASP A 1 248 ? 23.007 8.588   -14.132 1.00 22.32 ? 248 ASP A CA  1 
ATOM   1958 C  C   . ASP A 1 248 ? 21.831 7.670   -13.844 1.00 21.84 ? 248 ASP A C   1 
ATOM   1959 O  O   . ASP A 1 248 ? 21.263 7.072   -14.769 1.00 23.84 ? 248 ASP A O   1 
ATOM   1960 C  CB  . ASP A 1 248 ? 24.324 7.821   -13.986 1.00 24.88 ? 248 ASP A CB  1 
ATOM   1961 C  CG  . ASP A 1 248 ? 25.535 8.658   -14.368 1.00 28.89 ? 248 ASP A CG  1 
ATOM   1962 O  OD1 . ASP A 1 248 ? 25.386 9.525   -15.254 1.00 32.40 ? 248 ASP A OD1 1 
ATOM   1963 O  OD2 . ASP A 1 248 ? 26.639 8.399   -13.851 1.00 29.73 ? 248 ASP A OD2 1 
ATOM   1964 N  N   . ILE A 1 249 ? 21.457 7.527   -12.568 1.00 22.26 ? 249 ILE A N   1 
ATOM   1965 C  CA  . ILE A 1 249 ? 20.320 6.669   -12.259 1.00 18.98 ? 249 ILE A CA  1 
ATOM   1966 C  C   . ILE A 1 249 ? 19.040 7.231   -12.843 1.00 21.29 ? 249 ILE A C   1 
ATOM   1967 O  O   . ILE A 1 249 ? 18.106 6.476   -13.148 1.00 22.38 ? 249 ILE A O   1 
ATOM   1968 C  CB  . ILE A 1 249 ? 20.196 6.459   -10.737 1.00 23.34 ? 249 ILE A CB  1 
ATOM   1969 C  CG1 . ILE A 1 249 ? 21.512 5.914   -10.178 1.00 27.91 ? 249 ILE A CG1 1 
ATOM   1970 C  CG2 . ILE A 1 249 ? 19.016 5.538   -10.425 1.00 33.43 ? 249 ILE A CG2 1 
ATOM   1971 C  CD1 . ILE A 1 249 ? 21.437 5.460   -8.742  1.00 34.43 ? 249 ILE A CD1 1 
ATOM   1972 N  N   . LEU A 1 250 ? 18.965 8.548   -13.020 1.00 19.79 ? 250 LEU A N   1 
ATOM   1973 C  CA  . LEU A 1 250 ? 17.777 9.139   -13.623 1.00 21.98 ? 250 LEU A CA  1 
ATOM   1974 C  C   . LEU A 1 250 ? 17.796 9.088   -15.149 1.00 22.83 ? 250 LEU A C   1 
ATOM   1975 O  O   . LEU A 1 250 ? 16.830 9.540   -15.783 1.00 23.59 ? 250 LEU A O   1 
ATOM   1976 C  CB  . LEU A 1 250 ? 17.628 10.591  -13.160 1.00 21.57 ? 250 LEU A CB  1 
ATOM   1977 C  CG  . LEU A 1 250 ? 17.208 10.796  -11.710 1.00 23.15 ? 250 LEU A CG  1 
ATOM   1978 C  CD1 . LEU A 1 250 ? 17.618 12.175  -11.263 1.00 19.88 ? 250 LEU A CD1 1 
ATOM   1979 C  CD2 . LEU A 1 250 ? 15.697 10.611  -11.602 1.00 24.20 ? 250 LEU A CD2 1 
ATOM   1980 N  N   . GLY A 1 251 ? 18.855 8.550   -15.751 1.00 22.43 ? 251 GLY A N   1 
ATOM   1981 C  CA  . GLY A 1 251 ? 19.005 8.552   -17.194 1.00 24.45 ? 251 GLY A CA  1 
ATOM   1982 C  C   . GLY A 1 251 ? 17.826 7.968   -17.950 1.00 26.29 ? 251 GLY A C   1 
ATOM   1983 O  O   . GLY A 1 251 ? 17.346 8.544   -18.937 1.00 26.60 ? 251 GLY A O   1 
ATOM   1984 N  N   . PRO A 1 252 ? 17.354 6.790   -17.529 1.00 21.55 ? 252 PRO A N   1 
ATOM   1985 C  CA  . PRO A 1 252 ? 16.193 6.189   -18.212 1.00 25.29 ? 252 PRO A CA  1 
ATOM   1986 C  C   . PRO A 1 252 ? 14.947 7.056   -18.201 1.00 24.84 ? 252 PRO A C   1 
ATOM   1987 O  O   . PRO A 1 252 ? 14.205 7.068   -19.196 1.00 22.27 ? 252 PRO A O   1 
ATOM   1988 C  CB  . PRO A 1 252 ? 15.990 4.880   -17.440 1.00 25.43 ? 252 PRO A CB  1 
ATOM   1989 C  CG  . PRO A 1 252 ? 17.372 4.531   -16.977 1.00 30.93 ? 252 PRO A CG  1 
ATOM   1990 C  CD  . PRO A 1 252 ? 17.949 5.857   -16.554 1.00 30.67 ? 252 PRO A CD  1 
ATOM   1991 N  N   . LEU A 1 253 ? 14.675 7.767   -17.099 1.00 21.49 ? 253 LEU A N   1 
ATOM   1992 C  CA  . LEU A 1 253 ? 13.519 8.660   -17.075 1.00 19.40 ? 253 LEU A CA  1 
ATOM   1993 C  C   . LEU A 1 253 ? 13.748 9.863   -17.980 1.00 20.53 ? 253 LEU A C   1 
ATOM   1994 O  O   . LEU A 1 253 ? 12.833 10.311  -18.685 1.00 21.18 ? 253 LEU A O   1 
ATOM   1995 C  CB  . LEU A 1 253 ? 13.231 9.095   -15.637 1.00 19.09 ? 253 LEU A CB  1 
ATOM   1996 C  CG  . LEU A 1 253 ? 12.672 7.908   -14.847 1.00 24.27 ? 253 LEU A CG  1 
ATOM   1997 C  CD1 . LEU A 1 253 ? 12.564 8.188   -13.340 1.00 24.23 ? 253 LEU A CD1 1 
ATOM   1998 C  CD2 . LEU A 1 253 ? 11.315 7.524   -15.429 1.00 27.90 ? 253 LEU A CD2 1 
ATOM   1999 N  N   . SER A 1 254 ? 14.969 10.398  -17.963 1.00 20.77 ? 254 SER A N   1 
ATOM   2000 C  CA  . SER A 1 254 ? 15.350 11.442  -18.907 1.00 24.13 ? 254 SER A CA  1 
ATOM   2001 C  C   . SER A 1 254 ? 15.159 10.988  -20.354 1.00 25.96 ? 254 SER A C   1 
ATOM   2002 O  O   . SER A 1 254 ? 14.643 11.743  -21.188 1.00 23.85 ? 254 SER A O   1 
ATOM   2003 C  CB  . SER A 1 254 ? 16.807 11.842  -18.648 1.00 23.12 ? 254 SER A CB  1 
ATOM   2004 O  OG  . SER A 1 254 ? 17.202 12.896  -19.503 1.00 34.50 ? 254 SER A OG  1 
ATOM   2005 N  N   . ALA A 1 255 ? 15.574 9.759   -20.675 1.00 21.71 ? 255 ALA A N   1 
ATOM   2006 C  CA  . ALA A 1 255 ? 15.446 9.261   -22.040 1.00 25.10 ? 255 ALA A CA  1 
ATOM   2007 C  C   . ALA A 1 255 ? 13.984 9.118   -22.448 1.00 27.22 ? 255 ALA A C   1 
ATOM   2008 O  O   . ALA A 1 255 ? 13.619 9.417   -23.593 1.00 28.28 ? 255 ALA A O   1 
ATOM   2009 C  CB  . ALA A 1 255 ? 16.169 7.925   -22.179 1.00 27.68 ? 255 ALA A CB  1 
ATOM   2010 N  N   . GLN A 1 256 ? 13.134 8.671   -21.523 1.00 27.44 ? 256 GLN A N   1 
ATOM   2011 C  CA  . GLN A 1 256 ? 11.729 8.439   -21.849 1.00 27.63 ? 256 GLN A CA  1 
ATOM   2012 C  C   . GLN A 1 256 ? 10.980 9.747   -22.077 1.00 30.82 ? 256 GLN A C   1 
ATOM   2013 O  O   . GLN A 1 256 ? 10.105 9.824   -22.947 1.00 29.15 ? 256 GLN A O   1 
ATOM   2014 C  CB  . GLN A 1 256 ? 11.053 7.644   -20.732 1.00 29.88 ? 256 GLN A CB  1 
ATOM   2015 C  CG  . GLN A 1 256 ? 9.532  7.652   -20.799 1.00 38.32 ? 256 GLN A CG  1 
ATOM   2016 C  CD  . GLN A 1 256 ? 8.926  6.494   -20.036 1.00 50.16 ? 256 GLN A CD  1 
ATOM   2017 O  OE1 . GLN A 1 256 ? 7.705  6.397   -19.890 1.00 51.30 ? 256 GLN A OE1 1 
ATOM   2018 N  NE2 . GLN A 1 256 ? 9.784  5.622   -19.511 1.00 49.84 ? 256 GLN A NE2 1 
ATOM   2019 N  N   . THR A 1 257 ? 11.299 10.783  -21.307 1.00 21.56 ? 257 THR A N   1 
ATOM   2020 C  CA  . THR A 1 257 ? 10.563 12.039  -21.366 1.00 23.91 ? 257 THR A CA  1 
ATOM   2021 C  C   . THR A 1 257 ? 11.242 13.084  -22.230 1.00 28.87 ? 257 THR A C   1 
ATOM   2022 O  O   . THR A 1 257 ? 10.626 14.113  -22.521 1.00 28.97 ? 257 THR A O   1 
ATOM   2023 C  CB  . THR A 1 257 ? 10.372 12.628  -19.963 1.00 22.09 ? 257 THR A CB  1 
ATOM   2024 O  OG1 . THR A 1 257 ? 11.657 12.922  -19.397 1.00 21.50 ? 257 THR A OG1 1 
ATOM   2025 C  CG2 . THR A 1 257 ? 9.622  11.677  -19.030 1.00 23.74 ? 257 THR A CG2 1 
ATOM   2026 N  N   . GLY A 1 258 ? 12.499 12.870  -22.602 1.00 25.68 ? 258 GLY A N   1 
ATOM   2027 C  CA  . GLY A 1 258 ? 13.234 13.858  -23.362 1.00 27.91 ? 258 GLY A CA  1 
ATOM   2028 C  C   . GLY A 1 258 ? 13.688 15.051  -22.550 1.00 27.66 ? 258 GLY A C   1 
ATOM   2029 O  O   . GLY A 1 258 ? 14.174 16.031  -23.123 1.00 33.13 ? 258 GLY A O   1 
ATOM   2030 N  N   . ILE A 1 259 ? 13.555 15.002  -21.231 1.00 24.25 ? 259 ILE A N   1 
ATOM   2031 C  CA  . ILE A 1 259 ? 13.883 16.128  -20.373 1.00 25.09 ? 259 ILE A CA  1 
ATOM   2032 C  C   . ILE A 1 259 ? 15.216 15.823  -19.712 1.00 23.92 ? 259 ILE A C   1 
ATOM   2033 O  O   . ILE A 1 259 ? 15.313 14.912  -18.883 1.00 22.27 ? 259 ILE A O   1 
ATOM   2034 C  CB  . ILE A 1 259 ? 12.795 16.378  -19.324 1.00 21.77 ? 259 ILE A CB  1 
ATOM   2035 C  CG1 . ILE A 1 259 ? 11.442 16.607  -19.984 1.00 23.28 ? 259 ILE A CG1 1 
ATOM   2036 C  CG2 . ILE A 1 259 ? 13.152 17.575  -18.455 1.00 27.05 ? 259 ILE A CG2 1 
ATOM   2037 C  CD1 . ILE A 1 259 ? 10.325 16.766  -18.970 1.00 29.86 ? 259 ILE A CD1 1 
ATOM   2038 N  N   . ALA A 1 260 ? 16.234 16.604  -20.062 1.00 24.09 ? 260 ALA A N   1 
ATOM   2039 C  CA  . ALA A 1 260 ? 17.550 16.435  -19.467 1.00 24.50 ? 260 ALA A CA  1 
ATOM   2040 C  C   . ALA A 1 260 ? 17.463 16.576  -17.951 1.00 21.17 ? 260 ALA A C   1 
ATOM   2041 O  O   . ALA A 1 260 ? 16.684 17.375  -17.425 1.00 21.47 ? 260 ALA A O   1 
ATOM   2042 C  CB  . ALA A 1 260 ? 18.524 17.459  -20.052 1.00 24.45 ? 260 ALA A CB  1 
ATOM   2043 N  N   . VAL A 1 261 ? 18.277 15.792  -17.240 1.00 20.20 ? 261 VAL A N   1 
ATOM   2044 C  CA  . VAL A 1 261 ? 18.190 15.801  -15.779 1.00 22.23 ? 261 VAL A CA  1 
ATOM   2045 C  C   . VAL A 1 261 ? 18.410 17.207  -15.233 1.00 22.83 ? 261 VAL A C   1 
ATOM   2046 O  O   . VAL A 1 261 ? 17.711 17.643  -14.311 1.00 20.63 ? 261 VAL A O   1 
ATOM   2047 C  CB  . VAL A 1 261 ? 19.186 14.797  -15.165 1.00 26.39 ? 261 VAL A CB  1 
ATOM   2048 C  CG1 . VAL A 1 261 ? 19.294 15.007  -13.664 1.00 23.21 ? 261 VAL A CG1 1 
ATOM   2049 C  CG2 . VAL A 1 261 ? 18.759 13.364  -15.475 1.00 25.69 ? 261 VAL A CG2 1 
ATOM   2050 N  N   . LEU A 1 262 ? 19.391 17.930  -15.776 1.00 24.14 ? 262 LEU A N   1 
ATOM   2051 C  CA  . LEU A 1 262 ? 19.683 19.270  -15.278 1.00 24.00 ? 262 LEU A CA  1 
ATOM   2052 C  C   . LEU A 1 262 ? 18.545 20.242  -15.578 1.00 25.99 ? 262 LEU A C   1 
ATOM   2053 O  O   . LEU A 1 262 ? 18.347 21.209  -14.833 1.00 22.60 ? 262 LEU A O   1 
ATOM   2054 C  CB  . LEU A 1 262 ? 20.991 19.768  -15.881 1.00 26.94 ? 262 LEU A CB  1 
ATOM   2055 C  CG  . LEU A 1 262 ? 22.224 19.136  -15.231 1.00 27.97 ? 262 LEU A CG  1 
ATOM   2056 C  CD1 . LEU A 1 262 ? 23.503 19.652  -15.901 1.00 31.46 ? 262 LEU A CD1 1 
ATOM   2057 C  CD2 . LEU A 1 262 ? 22.244 19.393  -13.725 1.00 26.76 ? 262 LEU A CD2 1 
ATOM   2058 N  N   . ASP A 1 263 ? 17.788 20.005  -16.651 1.00 20.15 ? 263 ASP A N   1 
ATOM   2059 C  CA  . ASP A 1 263 ? 16.581 20.788  -16.901 1.00 20.53 ? 263 ASP A CA  1 
ATOM   2060 C  C   . ASP A 1 263 ? 15.550 20.546  -15.808 1.00 26.04 ? 263 ASP A C   1 
ATOM   2061 O  O   . ASP A 1 263 ? 14.919 21.483  -15.308 1.00 22.80 ? 263 ASP A O   1 
ATOM   2062 C  CB  . ASP A 1 263 ? 15.999 20.417  -18.266 1.00 28.09 ? 263 ASP A CB  1 
ATOM   2063 C  CG  . ASP A 1 263 ? 16.749 21.039  -19.410 1.00 30.38 ? 263 ASP A CG  1 
ATOM   2064 O  OD1 . ASP A 1 263 ? 17.864 21.567  -19.191 1.00 26.48 ? 263 ASP A OD1 1 
ATOM   2065 O  OD2 . ASP A 1 263 ? 16.252 20.936  -20.558 1.00 29.71 ? 263 ASP A OD2 1 
ATOM   2066 N  N   . MET A 1 264 ? 15.349 19.279  -15.441 1.00 23.73 ? 264 MET A N   1 
ATOM   2067 C  CA  . MET A 1 264 ? 14.433 18.978  -14.349 1.00 19.20 ? 264 MET A CA  1 
ATOM   2068 C  C   . MET A 1 264 ? 14.918 19.560  -13.032 1.00 20.72 ? 264 MET A C   1 
ATOM   2069 O  O   . MET A 1 264 ? 14.114 20.039  -12.226 1.00 23.15 ? 264 MET A O   1 
ATOM   2070 C  CB  . MET A 1 264 ? 14.206 17.470  -14.232 1.00 21.03 ? 264 MET A CB  1 
ATOM   2071 C  CG  . MET A 1 264 ? 13.005 17.205  -13.329 1.00 16.80 ? 264 MET A CG  1 
ATOM   2072 S  SD  . MET A 1 264 ? 11.415 17.628  -14.077 1.00 21.94 ? 264 MET A SD  1 
ATOM   2073 C  CE  . MET A 1 264 ? 11.117 16.180  -15.086 1.00 20.68 ? 264 MET A CE  1 
ATOM   2074 N  N   . CYS A 1 265 ? 16.228 19.527  -12.781 1.00 19.25 ? 265 CYS A N   1 
ATOM   2075 C  CA  . CYS A 1 265 ? 16.727 20.215  -11.596 1.00 23.60 ? 265 CYS A CA  1 
ATOM   2076 C  C   . CYS A 1 265 ? 16.344 21.689  -11.613 1.00 21.97 ? 265 CYS A C   1 
ATOM   2077 O  O   . CYS A 1 265 ? 16.024 22.265  -10.568 1.00 21.85 ? 265 CYS A O   1 
ATOM   2078 C  CB  . CYS A 1 265 ? 18.247 20.076  -11.482 1.00 22.84 ? 265 CYS A CB  1 
ATOM   2079 S  SG  . CYS A 1 265 ? 18.831 18.403  -11.203 1.00 24.20 ? 265 CYS A SG  1 
ATOM   2080 N  N   . ALA A 1 266 ? 16.361 22.317  -12.793 1.00 20.99 ? 266 ALA A N   1 
ATOM   2081 C  CA  . ALA A 1 266 ? 16.015 23.733  -12.858 1.00 22.84 ? 266 ALA A CA  1 
ATOM   2082 C  C   . ALA A 1 266 ? 14.553 23.957  -12.505 1.00 26.01 ? 266 ALA A C   1 
ATOM   2083 O  O   . ALA A 1 266 ? 14.208 24.962  -11.872 1.00 26.83 ? 266 ALA A O   1 
ATOM   2084 C  CB  . ALA A 1 266 ? 16.329 24.297  -14.243 1.00 25.08 ? 266 ALA A CB  1 
ATOM   2085 N  N   . SER A 1 267 ? 13.681 23.027  -12.906 1.00 20.07 ? 267 SER A N   1 
ATOM   2086 C  CA  . SER A 1 267 ? 12.276 23.109  -12.544 1.00 20.43 ? 267 SER A CA  1 
ATOM   2087 C  C   . SER A 1 267 ? 12.087 22.895  -11.049 1.00 20.61 ? 267 SER A C   1 
ATOM   2088 O  O   . SER A 1 267 ? 11.279 23.585  -10.410 1.00 23.29 ? 267 SER A O   1 
ATOM   2089 C  CB  . SER A 1 267 ? 11.476 22.074  -13.336 1.00 27.42 ? 267 SER A CB  1 
ATOM   2090 O  OG  . SER A 1 267 ? 11.382 22.444  -14.707 1.00 34.21 ? 267 SER A OG  1 
ATOM   2091 N  N   . LEU A 1 268 ? 12.829 21.944  -10.471 1.00 19.47 ? 268 LEU A N   1 
ATOM   2092 C  CA  . LEU A 1 268 ? 12.771 21.727  -9.024  1.00 15.53 ? 268 LEU A CA  1 
ATOM   2093 C  C   . LEU A 1 268 ? 13.264 22.949  -8.247  1.00 21.87 ? 268 LEU A C   1 
ATOM   2094 O  O   . LEU A 1 268 ? 12.665 23.335  -7.237  1.00 21.36 ? 268 LEU A O   1 
ATOM   2095 C  CB  . LEU A 1 268 ? 13.587 20.488  -8.642  1.00 16.45 ? 268 LEU A CB  1 
ATOM   2096 C  CG  . LEU A 1 268 ? 13.625 20.184  -7.126  1.00 17.74 ? 268 LEU A CG  1 
ATOM   2097 C  CD1 . LEU A 1 268 ? 12.240 20.205  -6.476  1.00 19.91 ? 268 LEU A CD1 1 
ATOM   2098 C  CD2 . LEU A 1 268 ? 14.294 18.844  -6.856  1.00 19.33 ? 268 LEU A CD2 1 
ATOM   2099 N  N   . LYS A 1 269 ? 14.351 23.570  -8.705  1.00 20.38 ? 269 LYS A N   1 
ATOM   2100 C  CA  . LYS A 1 269 ? 14.858 24.794  -8.079  1.00 18.55 ? 269 LYS A CA  1 
ATOM   2101 C  C   . LYS A 1 269 ? 13.790 25.884  -8.038  1.00 26.89 ? 269 LYS A C   1 
ATOM   2102 O  O   . LYS A 1 269 ? 13.609 26.558  -7.017  1.00 26.42 ? 269 LYS A O   1 
ATOM   2103 C  CB  . LYS A 1 269 ? 16.091 25.273  -8.847  1.00 23.84 ? 269 LYS A CB  1 
ATOM   2104 C  CG  . LYS A 1 269 ? 16.474 26.730  -8.653  1.00 28.80 ? 269 LYS A CG  1 
ATOM   2105 C  CD  . LYS A 1 269 ? 17.941 26.945  -9.018  1.00 35.76 ? 269 LYS A CD  1 
ATOM   2106 C  CE  . LYS A 1 269 ? 18.223 28.403  -9.384  1.00 48.33 ? 269 LYS A CE  1 
ATOM   2107 N  NZ  . LYS A 1 269 ? 19.216 28.545  -10.499 1.00 39.08 ? 269 LYS A NZ  1 
ATOM   2108 N  N   . GLU A 1 270 ? 13.071 26.084  -9.146  1.00 27.41 ? 270 GLU A N   1 
ATOM   2109 C  CA  . GLU A 1 270 ? 12.021 27.100  -9.136  1.00 26.53 ? 270 GLU A CA  1 
ATOM   2110 C  C   . GLU A 1 270 ? 10.888 26.711  -8.183  1.00 25.83 ? 270 GLU A C   1 
ATOM   2111 O  O   . GLU A 1 270 ? 10.303 27.576  -7.516  1.00 29.11 ? 270 GLU A O   1 
ATOM   2112 C  CB  . GLU A 1 270 ? 11.490 27.324  -10.558 1.00 26.28 ? 270 GLU A CB  1 
ATOM   2113 C  CG  . GLU A 1 270 ? 12.499 27.891  -11.578 1.00 37.07 ? 270 GLU A CG  1 
ATOM   2114 C  CD  . GLU A 1 270 ? 13.138 29.217  -11.183 1.00 42.32 ? 270 GLU A CD  1 
ATOM   2115 O  OE1 . GLU A 1 270 ? 12.398 30.194  -10.924 1.00 47.96 ? 270 GLU A OE1 1 
ATOM   2116 O  OE2 . GLU A 1 270 ? 14.386 29.288  -11.142 1.00 38.78 ? 270 GLU A OE2 1 
ATOM   2117 N  N   . LEU A 1 271 ? 10.572 25.415  -8.085  1.00 22.04 ? 271 LEU A N   1 
ATOM   2118 C  CA  . LEU A 1 271 ? 9.538  24.977  -7.154  1.00 27.30 ? 271 LEU A CA  1 
ATOM   2119 C  C   . LEU A 1 271 ? 9.967  25.211  -5.714  1.00 26.76 ? 271 LEU A C   1 
ATOM   2120 O  O   . LEU A 1 271 ? 9.156  25.598  -4.869  1.00 28.56 ? 271 LEU A O   1 
ATOM   2121 C  CB  . LEU A 1 271 ? 9.224  23.498  -7.369  1.00 24.45 ? 271 LEU A CB  1 
ATOM   2122 C  CG  . LEU A 1 271 ? 8.266  23.115  -8.498  1.00 22.46 ? 271 LEU A CG  1 
ATOM   2123 C  CD1 . LEU A 1 271 ? 8.215  21.594  -8.661  1.00 21.53 ? 271 LEU A CD1 1 
ATOM   2124 C  CD2 . LEU A 1 271 ? 6.878  23.677  -8.234  1.00 29.02 ? 271 LEU A CD2 1 
ATOM   2125 N  N   . LEU A 1 272 ? 11.238 24.970  -5.413  1.00 23.32 ? 272 LEU A N   1 
ATOM   2126 C  CA  . LEU A 1 272 ? 11.727 25.184  -4.055  1.00 25.92 ? 272 LEU A CA  1 
ATOM   2127 C  C   . LEU A 1 272 ? 11.736 26.661  -3.698  1.00 29.85 ? 272 LEU A C   1 
ATOM   2128 O  O   . LEU A 1 272 ? 11.500 27.026  -2.540  1.00 32.94 ? 272 LEU A O   1 
ATOM   2129 C  CB  . LEU A 1 272 ? 13.128 24.597  -3.911  1.00 21.96 ? 272 LEU A CB  1 
ATOM   2130 C  CG  . LEU A 1 272 ? 13.188 23.080  -3.833  1.00 23.08 ? 272 LEU A CG  1 
ATOM   2131 C  CD1 . LEU A 1 272 ? 14.645 22.610  -3.749  1.00 23.83 ? 272 LEU A CD1 1 
ATOM   2132 C  CD2 . LEU A 1 272 ? 12.424 22.629  -2.609  1.00 33.74 ? 272 LEU A CD2 1 
ATOM   2133 N  N   . GLN A 1 273 ? 11.993 27.517  -4.679  1.00 26.39 ? 273 GLN A N   1 
ATOM   2134 C  CA  . GLN A 1 273 ? 12.145 28.943  -4.443  1.00 31.31 ? 273 GLN A CA  1 
ATOM   2135 C  C   . GLN A 1 273 ? 10.820 29.686  -4.413  1.00 36.41 ? 273 GLN A C   1 
ATOM   2136 O  O   . GLN A 1 273 ? 10.726 30.737  -3.773  1.00 35.58 ? 273 GLN A O   1 
ATOM   2137 C  CB  . GLN A 1 273 ? 13.065 29.521  -5.514  1.00 36.42 ? 273 GLN A CB  1 
ATOM   2138 C  CG  . GLN A 1 273 ? 14.538 29.250  -5.231  1.00 33.52 ? 273 GLN A CG  1 
ATOM   2139 C  CD  . GLN A 1 273 ? 15.439 29.752  -6.324  1.00 35.60 ? 273 GLN A CD  1 
ATOM   2140 O  OE1 . GLN A 1 273 ? 14.974 30.358  -7.289  1.00 34.69 ? 273 GLN A OE1 1 
ATOM   2141 N  NE2 . GLN A 1 273 ? 16.750 29.567  -6.149  1.00 35.15 ? 273 GLN A NE2 1 
ATOM   2142 N  N   . ASN A 1 274 ? 9.793  29.163  -5.071  1.00 30.24 ? 274 ASN A N   1 
ATOM   2143 C  CA  . ASN A 1 274 ? 8.519  29.856  -5.192  1.00 33.43 ? 274 ASN A CA  1 
ATOM   2144 C  C   . ASN A 1 274 ? 7.337  29.045  -4.687  1.00 33.45 ? 274 ASN A C   1 
ATOM   2145 O  O   . ASN A 1 274 ? 6.207  29.528  -4.750  1.00 33.60 ? 274 ASN A O   1 
ATOM   2146 C  CB  . ASN A 1 274 ? 8.288  30.261  -6.660  1.00 42.96 ? 274 ASN A CB  1 
ATOM   2147 C  CG  . ASN A 1 274 ? 9.444  31.074  -7.229  1.00 38.31 ? 274 ASN A CG  1 
ATOM   2148 O  OD1 . ASN A 1 274 ? 9.858  30.875  -8.368  1.00 42.02 ? 274 ASN A OD1 1 
ATOM   2149 N  ND2 . ASN A 1 274 ? 9.953  32.013  -6.440  1.00 46.11 ? 274 ASN A ND2 1 
ATOM   2150 N  N   . GLY A 1 275 ? 7.554  27.841  -4.192  1.00 28.28 ? 275 GLY A N   1 
ATOM   2151 C  CA  . GLY A 1 275 ? 6.453  27.012  -3.755  1.00 37.55 ? 275 GLY A CA  1 
ATOM   2152 C  C   . GLY A 1 275 ? 5.555  26.650  -4.929  1.00 31.53 ? 275 GLY A C   1 
ATOM   2153 O  O   . GLY A 1 275 ? 5.863  26.886  -6.093  1.00 31.66 ? 275 GLY A O   1 
ATOM   2154 N  N   . MET A 1 276 ? 4.422  26.042  -4.602  1.00 36.57 ? 276 MET A N   1 
ATOM   2155 C  CA  . MET A 1 276 ? 3.532  25.472  -5.605  1.00 35.96 ? 276 MET A CA  1 
ATOM   2156 C  C   . MET A 1 276 ? 2.288  26.313  -5.874  1.00 31.62 ? 276 MET A C   1 
ATOM   2157 O  O   . MET A 1 276 ? 1.458  25.906  -6.692  1.00 35.97 ? 276 MET A O   1 
ATOM   2158 C  CB  . MET A 1 276 ? 3.152  24.048  -5.188  1.00 32.00 ? 276 MET A CB  1 
ATOM   2159 C  CG  . MET A 1 276 ? 4.361  23.103  -5.306  1.00 35.17 ? 276 MET A CG  1 
ATOM   2160 S  SD  . MET A 1 276 ? 4.059  21.417  -4.762  1.00 54.16 ? 276 MET A SD  1 
ATOM   2161 C  CE  . MET A 1 276 ? 2.682  20.980  -5.793  1.00 28.67 ? 276 MET A CE  1 
ATOM   2162 N  N   . ASN A 1 277 ? 2.162  27.484  -5.246  1.00 35.59 ? 277 ASN A N   1 
ATOM   2163 C  CA  . ASN A 1 277 ? 1.044  28.404  -5.486  1.00 40.13 ? 277 ASN A CA  1 
ATOM   2164 C  C   . ASN A 1 277 ? -0.300 27.684  -5.511  1.00 38.70 ? 277 ASN A C   1 
ATOM   2165 O  O   . ASN A 1 277 ? -1.073 27.786  -6.468  1.00 45.63 ? 277 ASN A O   1 
ATOM   2166 C  CB  . ASN A 1 277 ? 1.234  29.193  -6.777  1.00 38.62 ? 277 ASN A CB  1 
ATOM   2167 C  CG  . ASN A 1 277 ? 2.314  30.240  -6.669  1.00 48.89 ? 277 ASN A CG  1 
ATOM   2168 O  OD1 . ASN A 1 277 ? 3.352  30.152  -7.325  1.00 65.47 ? 277 ASN A OD1 1 
ATOM   2169 N  ND2 . ASN A 1 277 ? 2.065  31.258  -5.854  1.00 47.95 ? 277 ASN A ND2 1 
ATOM   2170 N  N   . GLY A 1 278 ? -0.584 26.951  -4.436  1.00 31.65 ? 278 GLY A N   1 
ATOM   2171 C  CA  . GLY A 1 278 ? -1.860 26.279  -4.311  1.00 34.14 ? 278 GLY A CA  1 
ATOM   2172 C  C   . GLY A 1 278 ? -2.142 25.231  -5.360  1.00 31.32 ? 278 GLY A C   1 
ATOM   2173 O  O   . GLY A 1 278 ? -3.274 24.746  -5.426  1.00 35.01 ? 278 GLY A O   1 
ATOM   2174 N  N   . ARG A 1 279 ? -1.169 24.892  -6.201  1.00 31.07 ? 279 ARG A N   1 
ATOM   2175 C  CA  . ARG A 1 279 ? -1.329 23.862  -7.216  1.00 25.35 ? 279 ARG A CA  1 
ATOM   2176 C  C   . ARG A 1 279 ? -0.937 22.498  -6.641  1.00 28.21 ? 279 ARG A C   1 
ATOM   2177 O  O   . ARG A 1 279 ? -0.444 22.392  -5.517  1.00 29.97 ? 279 ARG A O   1 
ATOM   2178 C  CB  . ARG A 1 279 ? -0.484 24.196  -8.445  1.00 24.98 ? 279 ARG A CB  1 
ATOM   2179 C  CG  . ARG A 1 279 ? -0.973 25.415  -9.250  1.00 31.26 ? 279 ARG A CG  1 
ATOM   2180 C  CD  . ARG A 1 279 ? 0.080  25.813  -10.266 1.00 41.46 ? 279 ARG A CD  1 
ATOM   2181 N  NE  . ARG A 1 279 ? 1.031  26.756  -9.684  1.00 59.61 ? 279 ARG A NE  1 
ATOM   2182 C  CZ  . ARG A 1 279 ? 1.681  27.704  -10.348 1.00 56.27 ? 279 ARG A CZ  1 
ATOM   2183 N  NH1 . ARG A 1 279 ? 1.610  27.805  -11.666 1.00 59.24 ? 279 ARG A NH1 1 
ATOM   2184 N  NH2 . ARG A 1 279 ? 2.445  28.559  -9.674  1.00 50.45 ? 279 ARG A NH2 1 
ATOM   2185 N  N   . THR A 1 280 ? -1.183 21.441  -7.419  1.00 26.47 ? 280 THR A N   1 
ATOM   2186 C  CA  . THR A 1 280 ? -0.835 20.081  -7.021  1.00 25.65 ? 280 THR A CA  1 
ATOM   2187 C  C   . THR A 1 280 ? -0.093 19.360  -8.143  1.00 29.40 ? 280 THR A C   1 
ATOM   2188 O  O   . THR A 1 280 ? -0.222 19.694  -9.324  1.00 27.05 ? 280 THR A O   1 
ATOM   2189 C  CB  . THR A 1 280 ? -2.069 19.257  -6.641  1.00 25.42 ? 280 THR A CB  1 
ATOM   2190 O  OG1 . THR A 1 280 ? -2.991 19.259  -7.730  1.00 29.45 ? 280 THR A OG1 1 
ATOM   2191 C  CG2 . THR A 1 280 ? -2.753 19.838  -5.419  1.00 29.11 ? 280 THR A CG2 1 
ATOM   2192 N  N   . ILE A 1 281 ? 0.682  18.349  -7.752  1.00 24.48 ? 281 ILE A N   1 
ATOM   2193 C  CA  . ILE A 1 281 ? 1.420  17.479  -8.669  1.00 19.07 ? 281 ILE A CA  1 
ATOM   2194 C  C   . ILE A 1 281 ? 1.115  16.040  -8.275  1.00 23.26 ? 281 ILE A C   1 
ATOM   2195 O  O   . ILE A 1 281 ? 1.351  15.646  -7.121  1.00 22.76 ? 281 ILE A O   1 
ATOM   2196 C  CB  . ILE A 1 281 ? 2.938  17.743  -8.633  1.00 23.13 ? 281 ILE A CB  1 
ATOM   2197 C  CG1 . ILE A 1 281 ? 3.254  19.189  -9.030  1.00 21.49 ? 281 ILE A CG1 1 
ATOM   2198 C  CG2 . ILE A 1 281 ? 3.688  16.733  -9.505  1.00 22.88 ? 281 ILE A CG2 1 
ATOM   2199 C  CD1 . ILE A 1 281 ? 4.692  19.602  -8.743  1.00 21.25 ? 281 ILE A CD1 1 
ATOM   2200 N  N   . LEU A 1 282 ? 0.555  15.269  -9.213  1.00 27.51 ? 282 LEU A N   1 
ATOM   2201 C  CA  . LEU A 1 282 ? 0.140  13.888  -8.946  1.00 25.73 ? 282 LEU A CA  1 
ATOM   2202 C  C   . LEU A 1 282 ? -0.709 13.803  -7.674  1.00 28.19 ? 282 LEU A C   1 
ATOM   2203 O  O   . LEU A 1 282 ? -0.556 12.899  -6.852  1.00 28.08 ? 282 LEU A O   1 
ATOM   2204 C  CB  . LEU A 1 282 ? 1.358  12.964  -8.860  1.00 24.13 ? 282 LEU A CB  1 
ATOM   2205 C  CG  . LEU A 1 282 ? 2.050  12.670  -10.200 1.00 25.71 ? 282 LEU A CG  1 
ATOM   2206 C  CD1 . LEU A 1 282 ? 3.270  11.775  -9.997  1.00 23.27 ? 282 LEU A CD1 1 
ATOM   2207 C  CD2 . LEU A 1 282 ? 1.067  12.052  -11.186 1.00 25.65 ? 282 LEU A CD2 1 
ATOM   2208 N  N   . GLY A 1 283 ? -1.624 14.760  -7.519  1.00 25.96 ? 283 GLY A N   1 
ATOM   2209 C  CA  . GLY A 1 283 ? -2.509 14.797  -6.373  1.00 28.91 ? 283 GLY A CA  1 
ATOM   2210 C  C   . GLY A 1 283 ? -1.889 15.213  -5.053  1.00 31.41 ? 283 GLY A C   1 
ATOM   2211 O  O   . GLY A 1 283 ? -2.556 15.110  -4.016  1.00 30.92 ? 283 GLY A O   1 
ATOM   2212 N  N   A SER A 1 284 ? -0.642 15.679  -5.048  0.54 25.48 ? 284 SER A N   1 
ATOM   2213 N  N   B SER A 1 284 ? -0.645 15.687  -5.050  0.46 25.49 ? 284 SER A N   1 
ATOM   2214 C  CA  A SER A 1 284 ? 0.032  16.090  -3.824  0.54 24.02 ? 284 SER A CA  1 
ATOM   2215 C  CA  B SER A 1 284 ? 0.042  16.083  -3.829  0.46 24.04 ? 284 SER A CA  1 
ATOM   2216 C  C   A SER A 1 284 ? 0.260  17.594  -3.834  0.54 22.85 ? 284 SER A C   1 
ATOM   2217 C  C   B SER A 1 284 ? 0.290  17.587  -3.830  0.46 22.88 ? 284 SER A C   1 
ATOM   2218 O  O   A SER A 1 284 ? 0.555  18.183  -4.877  0.54 24.38 ? 284 SER A O   1 
ATOM   2219 O  O   B SER A 1 284 ? 0.626  18.170  -4.863  0.46 24.40 ? 284 SER A O   1 
ATOM   2220 C  CB  A SER A 1 284 ? 1.377  15.372  -3.656  0.54 24.31 ? 284 SER A CB  1 
ATOM   2221 C  CB  B SER A 1 284 ? 1.375  15.338  -3.680  0.46 24.34 ? 284 SER A CB  1 
ATOM   2222 O  OG  A SER A 1 284 ? 2.000  15.734  -2.431  0.54 25.71 ? 284 SER A OG  1 
ATOM   2223 O  OG  B SER A 1 284 ? 1.174  13.935  -3.595  0.46 30.20 ? 284 SER A OG  1 
ATOM   2224 N  N   . ALA A 1 285 ? 0.134  18.214  -2.663  1.00 22.72 ? 285 ALA A N   1 
ATOM   2225 C  CA  . ALA A 1 285 ? 0.432  19.630  -2.514  1.00 24.52 ? 285 ALA A CA  1 
ATOM   2226 C  C   . ALA A 1 285 ? 1.837  19.873  -1.980  1.00 26.50 ? 285 ALA A C   1 
ATOM   2227 O  O   . ALA A 1 285 ? 2.194  21.021  -1.704  1.00 31.20 ? 285 ALA A O   1 
ATOM   2228 C  CB  . ALA A 1 285 ? -0.606 20.300  -1.617  1.00 29.07 ? 285 ALA A CB  1 
ATOM   2229 N  N   . LEU A 1 286 ? 2.644  18.825  -1.836  1.00 21.67 ? 286 LEU A N   1 
ATOM   2230 C  CA  . LEU A 1 286 ? 4.049  18.957  -1.492  1.00 22.98 ? 286 LEU A CA  1 
ATOM   2231 C  C   . LEU A 1 286 ? 4.863  18.066  -2.419  1.00 25.10 ? 286 LEU A C   1 
ATOM   2232 O  O   . LEU A 1 286 ? 4.326  17.241  -3.160  1.00 25.23 ? 286 LEU A O   1 
ATOM   2233 C  CB  . LEU A 1 286 ? 4.326  18.584  -0.028  1.00 28.93 ? 286 LEU A CB  1 
ATOM   2234 C  CG  . LEU A 1 286 ? 3.747  17.282  0.519   1.00 37.67 ? 286 LEU A CG  1 
ATOM   2235 C  CD1 . LEU A 1 286 ? 4.602  16.108  0.056   1.00 33.89 ? 286 LEU A CD1 1 
ATOM   2236 C  CD2 . LEU A 1 286 ? 3.692  17.325  2.039   1.00 30.64 ? 286 LEU A CD2 1 
ATOM   2237 N  N   . LEU A 1 287 ? 6.178  18.227  -2.360  1.00 21.72 ? 287 LEU A N   1 
ATOM   2238 C  CA  . LEU A 1 287 ? 7.071  17.455  -3.215  1.00 21.70 ? 287 LEU A CA  1 
ATOM   2239 C  C   . LEU A 1 287 ? 7.339  16.109  -2.542  1.00 23.80 ? 287 LEU A C   1 
ATOM   2240 O  O   . LEU A 1 287 ? 7.782  16.068  -1.392  1.00 27.54 ? 287 LEU A O   1 
ATOM   2241 C  CB  . LEU A 1 287 ? 8.366  18.232  -3.444  1.00 19.45 ? 287 LEU A CB  1 
ATOM   2242 C  CG  . LEU A 1 287 ? 8.135  19.593  -4.134  1.00 26.08 ? 287 LEU A CG  1 
ATOM   2243 C  CD1 . LEU A 1 287 ? 9.372  20.490  -4.084  1.00 30.00 ? 287 LEU A CD1 1 
ATOM   2244 C  CD2 . LEU A 1 287 ? 7.611  19.440  -5.559  1.00 27.00 ? 287 LEU A CD2 1 
ATOM   2245 N  N   . GLU A 1 288 ? 7.059  15.011  -3.241  1.00 18.83 ? 288 GLU A N   1 
ATOM   2246 C  CA  . GLU A 1 288 ? 7.146  13.675  -2.658  1.00 22.68 ? 288 GLU A CA  1 
ATOM   2247 C  C   . GLU A 1 288 ? 8.517  13.061  -2.915  1.00 16.76 ? 288 GLU A C   1 
ATOM   2248 O  O   . GLU A 1 288 ? 8.995  13.064  -4.062  1.00 18.76 ? 288 GLU A O   1 
ATOM   2249 C  CB  . GLU A 1 288 ? 6.054  12.773  -3.231  1.00 20.08 ? 288 GLU A CB  1 
ATOM   2250 C  CG  . GLU A 1 288 ? 4.644  13.344  -3.139  1.00 26.24 ? 288 GLU A CG  1 
ATOM   2251 C  CD  . GLU A 1 288 ? 3.979  12.986  -1.827  1.00 38.35 ? 288 GLU A CD  1 
ATOM   2252 O  OE1 . GLU A 1 288 ? 4.617  12.272  -1.022  1.00 34.10 ? 288 GLU A OE1 1 
ATOM   2253 O  OE2 . GLU A 1 288 ? 2.834  13.429  -1.592  1.00 40.12 ? 288 GLU A OE2 1 
ATOM   2254 N  N   . ASP A 1 289 ? 9.129  12.482  -1.860  1.00 19.81 ? 289 ASP A N   1 
ATOM   2255 C  CA  . ASP A 1 289 ? 10.469 11.912  -2.006  1.00 20.87 ? 289 ASP A CA  1 
ATOM   2256 C  C   . ASP A 1 289 ? 10.549 10.438  -1.608  1.00 20.94 ? 289 ASP A C   1 
ATOM   2257 O  O   . ASP A 1 289 ? 11.644 9.942   -1.325  1.00 22.61 ? 289 ASP A O   1 
ATOM   2258 C  CB  . ASP A 1 289 ? 11.529 12.693  -1.213  1.00 19.16 ? 289 ASP A CB  1 
ATOM   2259 C  CG  . ASP A 1 289 ? 11.379 12.576  0.297   1.00 25.41 ? 289 ASP A CG  1 
ATOM   2260 O  OD1 . ASP A 1 289 ? 10.386 11.995  0.795   1.00 20.98 ? 289 ASP A OD1 1 
ATOM   2261 O  OD2 . ASP A 1 289 ? 12.322 13.041  1.002   1.00 20.66 ? 289 ASP A OD2 1 
ATOM   2262 N  N   . GLU A 1 290 ? 9.442  9.702   -1.586  1.00 20.11 ? 290 GLU A N   1 
ATOM   2263 C  CA  . GLU A 1 290 ? 9.539  8.280   -1.266  1.00 20.26 ? 290 GLU A CA  1 
ATOM   2264 C  C   . GLU A 1 290 ? 9.169  7.395   -2.457  1.00 21.21 ? 290 GLU A C   1 
ATOM   2265 O  O   . GLU A 1 290 ? 8.673  6.282   -2.285  1.00 23.50 ? 290 GLU A O   1 
ATOM   2266 C  CB  . GLU A 1 290 ? 8.727  7.957   -0.001  1.00 20.51 ? 290 GLU A CB  1 
ATOM   2267 C  CG  . GLU A 1 290 ? 9.197  8.807   1.210   1.00 22.55 ? 290 GLU A CG  1 
ATOM   2268 C  CD  . GLU A 1 290 ? 8.953  8.152   2.574   1.00 28.00 ? 290 GLU A CD  1 
ATOM   2269 O  OE1 . GLU A 1 290 ? 8.065  7.292   2.670   1.00 24.37 ? 290 GLU A OE1 1 
ATOM   2270 O  OE2 . GLU A 1 290 ? 9.645  8.502   3.559   1.00 27.79 ? 290 GLU A OE2 1 
ATOM   2271 N  N   . PHE A 1 291 ? 9.466  7.875   -3.672  1.00 21.78 ? 291 PHE A N   1 
ATOM   2272 C  CA  . PHE A 1 291 ? 9.522  7.065   -4.886  1.00 21.42 ? 291 PHE A CA  1 
ATOM   2273 C  C   . PHE A 1 291 ? 10.944 7.115   -5.419  1.00 17.88 ? 291 PHE A C   1 
ATOM   2274 O  O   . PHE A 1 291 ? 11.442 8.198   -5.741  1.00 19.78 ? 291 PHE A O   1 
ATOM   2275 C  CB  . PHE A 1 291 ? 8.577  7.601   -5.961  1.00 20.32 ? 291 PHE A CB  1 
ATOM   2276 C  CG  . PHE A 1 291 ? 7.129  7.513   -5.593  1.00 23.32 ? 291 PHE A CG  1 
ATOM   2277 C  CD1 . PHE A 1 291 ? 6.444  6.309   -5.686  1.00 26.00 ? 291 PHE A CD1 1 
ATOM   2278 C  CD2 . PHE A 1 291 ? 6.461  8.631   -5.121  1.00 24.85 ? 291 PHE A CD2 1 
ATOM   2279 C  CE1 . PHE A 1 291 ? 5.100  6.225   -5.352  1.00 27.70 ? 291 PHE A CE1 1 
ATOM   2280 C  CE2 . PHE A 1 291 ? 5.117  8.557   -4.766  1.00 32.59 ? 291 PHE A CE2 1 
ATOM   2281 C  CZ  . PHE A 1 291 ? 4.433  7.350   -4.885  1.00 31.77 ? 291 PHE A CZ  1 
ATOM   2282 N  N   . THR A 1 292 ? 11.582 5.955   -5.559  1.00 20.81 ? 292 THR A N   1 
ATOM   2283 C  CA  . THR A 1 292 ? 12.895 5.937   -6.188  1.00 23.23 ? 292 THR A CA  1 
ATOM   2284 C  C   . THR A 1 292 ? 12.744 5.981   -7.705  1.00 23.40 ? 292 THR A C   1 
ATOM   2285 O  O   . THR A 1 292 ? 11.654 5.741   -8.245  1.00 18.39 ? 292 THR A O   1 
ATOM   2286 C  CB  . THR A 1 292 ? 13.677 4.677   -5.834  1.00 21.15 ? 292 THR A CB  1 
ATOM   2287 O  OG1 . THR A 1 292 ? 13.002 3.545   -6.387  1.00 25.31 ? 292 THR A OG1 1 
ATOM   2288 C  CG2 . THR A 1 292 ? 13.848 4.498   -4.309  1.00 19.26 ? 292 THR A CG2 1 
ATOM   2289 N  N   . PRO A 1 293 ? 13.827 6.292   -8.417  1.00 23.62 ? 293 PRO A N   1 
ATOM   2290 C  CA  . PRO A 1 293 ? 13.819 6.116   -9.880  1.00 18.18 ? 293 PRO A CA  1 
ATOM   2291 C  C   . PRO A 1 293 ? 13.324 4.745   -10.306 1.00 24.32 ? 293 PRO A C   1 
ATOM   2292 O  O   . PRO A 1 293 ? 12.530 4.642   -11.249 1.00 25.09 ? 293 PRO A O   1 
ATOM   2293 C  CB  . PRO A 1 293 ? 15.289 6.333   -10.249 1.00 23.99 ? 293 PRO A CB  1 
ATOM   2294 C  CG  . PRO A 1 293 ? 15.768 7.293   -9.240  1.00 22.56 ? 293 PRO A CG  1 
ATOM   2295 C  CD  . PRO A 1 293 ? 15.093 6.880   -7.944  1.00 18.77 ? 293 PRO A CD  1 
ATOM   2296 N  N   . PHE A 1 294 ? 13.736 3.681   -9.604  1.00 24.26 ? 294 PHE A N   1 
ATOM   2297 C  CA  . PHE A 1 294 ? 13.273 2.354   -9.994  1.00 27.83 ? 294 PHE A CA  1 
ATOM   2298 C  C   . PHE A 1 294 ? 11.792 2.167   -9.702  1.00 27.72 ? 294 PHE A C   1 
ATOM   2299 O  O   . PHE A 1 294 ? 11.078 1.564   -10.510 1.00 27.82 ? 294 PHE A O   1 
ATOM   2300 C  CB  . PHE A 1 294 ? 14.107 1.244   -9.348  1.00 32.70 ? 294 PHE A CB  1 
ATOM   2301 C  CG  . PHE A 1 294 ? 15.586 1.515   -9.327  1.00 50.30 ? 294 PHE A CG  1 
ATOM   2302 C  CD1 . PHE A 1 294 ? 16.136 2.520   -8.536  1.00 51.18 ? 294 PHE A CD1 1 
ATOM   2303 C  CD2 . PHE A 1 294 ? 16.427 0.797   -10.173 1.00 65.66 ? 294 PHE A CD2 1 
ATOM   2304 C  CE1 . PHE A 1 294 ? 17.504 2.762   -8.551  1.00 55.65 ? 294 PHE A CE1 1 
ATOM   2305 C  CE2 . PHE A 1 294 ? 17.790 1.035   -10.202 1.00 59.33 ? 294 PHE A CE2 1 
ATOM   2306 C  CZ  . PHE A 1 294 ? 18.331 2.018   -9.392  1.00 65.02 ? 294 PHE A CZ  1 
ATOM   2307 N  N   . ASP A 1 295 ? 11.302 2.681   -8.570  1.00 22.64 ? 295 ASP A N   1 
ATOM   2308 C  CA  . ASP A 1 295 ? 9.856  2.674   -8.338  1.00 25.42 ? 295 ASP A CA  1 
ATOM   2309 C  C   . ASP A 1 295 ? 9.094  3.311   -9.491  1.00 26.27 ? 295 ASP A C   1 
ATOM   2310 O  O   . ASP A 1 295 ? 8.051  2.798   -9.913  1.00 24.64 ? 295 ASP A O   1 
ATOM   2311 C  CB  . ASP A 1 295 ? 9.500  3.399   -7.037  1.00 23.83 ? 295 ASP A CB  1 
ATOM   2312 C  CG  . ASP A 1 295 ? 10.077 2.731   -5.800  1.00 26.65 ? 295 ASP A CG  1 
ATOM   2313 O  OD1 . ASP A 1 295 ? 10.388 1.512   -5.841  1.00 33.41 ? 295 ASP A OD1 1 
ATOM   2314 O  OD2 . ASP A 1 295 ? 10.247 3.448   -4.792  1.00 24.62 ? 295 ASP A OD2 1 
ATOM   2315 N  N   . VAL A 1 296 ? 9.575  4.450   -9.995  1.00 21.04 ? 296 VAL A N   1 
ATOM   2316 C  CA  . VAL A 1 296 ? 8.811  5.173   -11.004 1.00 22.35 ? 296 VAL A CA  1 
ATOM   2317 C  C   . VAL A 1 296 ? 8.777  4.380   -12.303 1.00 26.87 ? 296 VAL A C   1 
ATOM   2318 O  O   . VAL A 1 296 ? 7.724  4.249   -12.940 1.00 27.57 ? 296 VAL A O   1 
ATOM   2319 C  CB  . VAL A 1 296 ? 9.391  6.588   -11.212 1.00 19.96 ? 296 VAL A CB  1 
ATOM   2320 C  CG1 . VAL A 1 296 ? 8.779  7.246   -12.460 1.00 20.82 ? 296 VAL A CG1 1 
ATOM   2321 C  CG2 . VAL A 1 296 ? 9.148  7.439   -9.963  1.00 20.91 ? 296 VAL A CG2 1 
ATOM   2322 N  N   . VAL A 1 297 ? 9.918  3.812   -12.700 1.00 24.90 ? 297 VAL A N   1 
ATOM   2323 C  CA  . VAL A 1 297 ? 9.953  3.028   -13.937 1.00 26.21 ? 297 VAL A CA  1 
ATOM   2324 C  C   . VAL A 1 297 ? 9.099  1.775   -13.801 1.00 31.49 ? 297 VAL A C   1 
ATOM   2325 O  O   . VAL A 1 297 ? 8.338  1.424   -14.710 1.00 32.81 ? 297 VAL A O   1 
ATOM   2326 C  CB  . VAL A 1 297 ? 11.405 2.670   -14.309 1.00 26.39 ? 297 VAL A CB  1 
ATOM   2327 C  CG1 . VAL A 1 297 ? 11.432 1.792   -15.561 1.00 30.18 ? 297 VAL A CG1 1 
ATOM   2328 C  CG2 . VAL A 1 297 ? 12.232 3.941   -14.508 1.00 30.03 ? 297 VAL A CG2 1 
ATOM   2329 N  N   . ARG A 1 298 ? 9.220  1.067   -12.677 1.00 28.04 ? 298 ARG A N   1 
ATOM   2330 C  CA  . ARG A 1 298 ? 8.418  -0.134  -12.481 1.00 28.97 ? 298 ARG A CA  1 
ATOM   2331 C  C   . ARG A 1 298 ? 6.930  0.190   -12.549 1.00 31.19 ? 298 ARG A C   1 
ATOM   2332 O  O   . ARG A 1 298 ? 6.165  -0.489  -13.245 1.00 35.09 ? 298 ARG A O   1 
ATOM   2333 C  CB  . ARG A 1 298 ? 8.776  -0.793  -11.146 1.00 27.66 ? 298 ARG A CB  1 
ATOM   2334 C  CG  . ARG A 1 298 ? 7.662  -1.632  -10.543 1.00 45.72 ? 298 ARG A CG  1 
ATOM   2335 N  N   . GLN A 1 299 ? 6.498  1.237   -11.842 1.00 33.54 ? 299 GLN A N   1 
ATOM   2336 C  CA  . GLN A 1 299 ? 5.073  1.550   -11.826 1.00 34.60 ? 299 GLN A CA  1 
ATOM   2337 C  C   . GLN A 1 299 ? 4.601  2.045   -13.186 1.00 39.78 ? 299 GLN A C   1 
ATOM   2338 O  O   . GLN A 1 299 ? 3.488  1.720   -13.621 1.00 41.02 ? 299 GLN A O   1 
ATOM   2339 C  CB  . GLN A 1 299 ? 4.747  2.578   -10.735 1.00 31.36 ? 299 GLN A CB  1 
ATOM   2340 C  CG  . GLN A 1 299 ? 3.243  2.874   -10.654 1.00 32.35 ? 299 GLN A CG  1 
ATOM   2341 C  CD  . GLN A 1 299 ? 2.796  3.643   -9.411  1.00 31.85 ? 299 GLN A CD  1 
ATOM   2342 O  OE1 . GLN A 1 299 ? 1.646  4.073   -9.333  1.00 31.14 ? 299 GLN A OE1 1 
ATOM   2343 N  NE2 . GLN A 1 299 ? 3.683  3.799   -8.435  1.00 25.07 ? 299 GLN A NE2 1 
ATOM   2344 N  N   . CYS A 1 300 ? 5.426  2.825   -13.873 1.00 29.62 ? 300 CYS A N   1 
ATOM   2345 C  CA  . CYS A 1 300 ? 5.064  3.390   -15.163 1.00 33.46 ? 300 CYS A CA  1 
ATOM   2346 C  C   . CYS A 1 300 ? 5.315  2.432   -16.334 1.00 40.88 ? 300 CYS A C   1 
ATOM   2347 O  O   . CYS A 1 300 ? 5.027  2.794   -17.481 1.00 52.46 ? 300 CYS A O   1 
ATOM   2348 C  CB  . CYS A 1 300 ? 5.817  4.711   -15.375 1.00 40.14 ? 300 CYS A CB  1 
ATOM   2349 S  SG  . CYS A 1 300 ? 5.257  6.085   -14.298 1.00 41.38 ? 300 CYS A SG  1 
ATOM   2350 N  N   . SER A 1 301 ? 5.811  1.210   -16.078 1.00 42.49 ? 301 SER A N   1 
ATOM   2351 C  CA  . SER A 1 301 ? 6.036  0.218   -17.126 1.00 39.97 ? 301 SER A CA  1 
ATOM   2352 C  C   . SER A 1 301 ? 5.281  -1.089  -16.924 1.00 50.40 ? 301 SER A C   1 
ATOM   2353 O  O   . SER A 1 301 ? 5.103  -1.831  -17.896 1.00 59.21 ? 301 SER A O   1 
ATOM   2354 C  CB  . SER A 1 301 ? 7.537  -0.105  -17.254 1.00 51.10 ? 301 SER A CB  1 
ATOM   2355 O  OG  . SER A 1 301 ? 7.945  -1.107  -16.330 1.00 44.29 ? 301 SER A OG  1 
ATOM   2356 N  N   . GLY A 1 302 ? 4.856  -1.410  -15.705 1.00 57.22 ? 302 GLY A N   1 
ATOM   2357 C  CA  . GLY A 1 302 ? 4.074  -2.613  -15.487 1.00 64.17 ? 302 GLY A CA  1 
ATOM   2358 C  C   . GLY A 1 302 ? 4.834  -3.851  -15.056 1.00 68.88 ? 302 GLY A C   1 
ATOM   2359 O  O   . GLY A 1 302 ? 4.390  -4.966  -15.352 1.00 55.93 ? 302 GLY A O   1 
ATOM   2360 N  N   . VAL A 1 303 ? 5.967  -3.701  -14.363 1.00 62.00 ? 303 VAL A N   1 
ATOM   2361 C  CA  . VAL A 1 303 ? 6.776  -4.856  -13.974 1.00 72.20 ? 303 VAL A CA  1 
ATOM   2362 C  C   . VAL A 1 303 ? 6.039  -5.691  -12.934 1.00 70.94 ? 303 VAL A C   1 
ATOM   2363 O  O   . VAL A 1 303 ? 5.514  -5.160  -11.946 1.00 66.78 ? 303 VAL A O   1 
ATOM   2364 C  CB  . VAL A 1 303 ? 8.140  -4.405  -13.430 1.00 71.02 ? 303 VAL A CB  1 
ATOM   2365 C  CG1 . VAL A 1 303 ? 8.917  -5.605  -12.908 1.00 70.58 ? 303 VAL A CG1 1 
ATOM   2366 C  CG2 . VAL A 1 303 ? 8.934  -3.656  -14.494 1.00 68.86 ? 303 VAL A CG2 1 
ATOM   2367 N  N   . THR A 1 304 ? 6.040  -7.010  -13.122 1.00 61.11 ? 304 THR A N   1 
ATOM   2368 C  CA  . THR A 1 304 ? 5.353  -7.932  -12.225 1.00 52.14 ? 304 THR A CA  1 
ATOM   2369 C  C   . THR A 1 304 ? 6.343  -8.825  -11.483 1.00 63.60 ? 304 THR A C   1 
ATOM   2370 O  O   . THR A 1 304 ? 7.552  -8.820  -11.741 1.00 59.81 ? 304 THR A O   1 
ATOM   2371 C  CB  . THR A 1 304 ? 4.339  -8.796  -12.987 1.00 54.75 ? 304 THR A CB  1 
ATOM   2372 O  OG1 . THR A 1 304 ? 4.944  -9.330  -14.177 1.00 56.55 ? 304 THR A OG1 1 
ATOM   2373 C  CG2 . THR A 1 304 ? 3.128  -7.968  -13.360 1.00 43.01 ? 304 THR A CG2 1 
ATOM   2374 N  N   . PHE A 1 305 ? 5.800  -9.605  -10.547 1.00 57.93 ? 305 PHE A N   1 
ATOM   2375 C  CA  . PHE A 1 305 ? 6.609  -10.433 -9.653  1.00 57.91 ? 305 PHE A CA  1 
ATOM   2376 C  C   . PHE A 1 305 ? 5.969  -11.803 -9.447  1.00 60.55 ? 305 PHE A C   1 
ATOM   2377 O  O   . PHE A 1 305 ? 5.248  -12.300 -10.312 1.00 60.66 ? 305 PHE A O   1 
ATOM   2378 C  CB  . PHE A 1 305 ? 6.797  -9.735  -8.299  1.00 43.60 ? 305 PHE A CB  1 
ATOM   2379 C  CG  . PHE A 1 305 ? 7.279  -8.317  -8.414  1.00 45.30 ? 305 PHE A CG  1 
ATOM   2380 C  CD1 . PHE A 1 305 ? 8.614  -8.039  -8.668  1.00 49.08 ? 305 PHE A CD1 1 
ATOM   2381 C  CD2 . PHE A 1 305 ? 6.394  -7.256  -8.272  1.00 55.85 ? 305 PHE A CD2 1 
ATOM   2382 C  CE1 . PHE A 1 305 ? 9.058  -6.732  -8.778  1.00 49.98 ? 305 PHE A CE1 1 
ATOM   2383 C  CE2 . PHE A 1 305 ? 6.834  -5.938  -8.381  1.00 53.46 ? 305 PHE A CE2 1 
ATOM   2384 C  CZ  . PHE A 1 305 ? 8.168  -5.679  -8.635  1.00 55.77 ? 305 PHE A CZ  1 
HETATM 2385 C  C1  A XEK B 2 .   ? 8.865  -0.359  21.184  0.39 22.98 ? 401 XEK A C1  1 
HETATM 2386 C  C1  B XEK B 2 .   ? 8.866  -0.383  21.170  0.48 22.96 ? 401 XEK A C1  1 
HETATM 2387 C  C2  A XEK B 2 .   ? 9.569  -1.171  22.078  0.39 23.97 ? 401 XEK A C2  1 
HETATM 2388 C  C2  B XEK B 2 .   ? 9.575  -1.198  22.057  0.48 23.95 ? 401 XEK A C2  1 
HETATM 2389 C  C3  A XEK B 2 .   ? 10.885 -0.738  22.613  0.39 24.38 ? 401 XEK A C3  1 
HETATM 2390 C  C3  B XEK B 2 .   ? 10.896 -0.768  22.586  0.48 24.36 ? 401 XEK A C3  1 
HETATM 2391 C  C4  A XEK B 2 .   ? 11.943 -1.644  22.719  0.39 23.77 ? 401 XEK A C4  1 
HETATM 2392 C  C4  B XEK B 2 .   ? 11.947 -1.674  22.753  0.48 23.77 ? 401 XEK A C4  1 
HETATM 2393 C  C5  A XEK B 2 .   ? 13.164 -1.240  23.229  0.39 25.30 ? 401 XEK A C5  1 
HETATM 2394 C  C5  B XEK B 2 .   ? 13.163 -1.255  23.262  0.48 25.31 ? 401 XEK A C5  1 
HETATM 2395 C  C6  A XEK B 2 .   ? 13.341 0.066   23.645  0.39 26.41 ? 401 XEK A C6  1 
HETATM 2396 C  C6  B XEK B 2 .   ? 13.343 0.069   23.618  0.48 26.40 ? 401 XEK A C6  1 
HETATM 2397 C  C7  A XEK B 2 .   ? 12.314 0.985   23.547  0.39 26.04 ? 401 XEK A C7  1 
HETATM 2398 C  C7  B XEK B 2 .   ? 12.324 0.986   23.462  0.48 25.98 ? 401 XEK A C7  1 
HETATM 2399 C  C8  A XEK B 2 .   ? 11.926 3.363   23.276  0.39 33.52 ? 401 XEK A C8  1 
HETATM 2400 C  C8  B XEK B 2 .   ? 12.093 3.307   22.919  0.48 33.38 ? 401 XEK A C8  1 
HETATM 2401 C  C9  A XEK B 2 .   ? 12.429 4.641   23.886  0.39 35.24 ? 401 XEK A C9  1 
HETATM 2402 C  C9  B XEK B 2 .   ? 12.749 4.598   23.317  0.48 32.97 ? 401 XEK A C9  1 
HETATM 2403 C  C10 A XEK B 2 .   ? 11.813 5.209   24.994  0.39 37.03 ? 401 XEK A C10 1 
HETATM 2404 C  C10 B XEK B 2 .   ? 13.979 4.977   22.793  0.48 35.18 ? 401 XEK A C10 1 
HETATM 2405 C  C11 A XEK B 2 .   ? 12.289 6.381   25.554  0.39 32.70 ? 401 XEK A C11 1 
HETATM 2406 C  C11 B XEK B 2 .   ? 14.580 6.164   23.170  0.48 34.00 ? 401 XEK A C11 1 
HETATM 2407 C  C12 A XEK B 2 .   ? 13.389 7.008   25.018  0.39 33.19 ? 401 XEK A C12 1 
HETATM 2408 C  C12 B XEK B 2 .   ? 13.967 6.989   24.084  0.48 38.04 ? 401 XEK A C12 1 
HETATM 2409 C  C13 A XEK B 2 .   ? 14.024 6.471   23.924  0.39 37.03 ? 401 XEK A C13 1 
HETATM 2410 C  C13 B XEK B 2 .   ? 12.755 6.639   24.628  0.48 36.13 ? 401 XEK A C13 1 
HETATM 2411 C  C14 A XEK B 2 .   ? 13.545 5.296   23.369  0.39 35.11 ? 401 XEK A C14 1 
HETATM 2412 C  C14 B XEK B 2 .   ? 12.156 5.451   24.246  0.48 37.85 ? 401 XEK A C14 1 
HETATM 2413 C  C15 A XEK B 2 .   ? 11.087 0.579   23.039  0.39 24.31 ? 401 XEK A C15 1 
HETATM 2414 C  C15 B XEK B 2 .   ? 11.102 0.566   22.953  0.48 24.30 ? 401 XEK A C15 1 
HETATM 2415 C  C17 A XEK B 2 .   ? 7.793  -2.846  22.023  0.39 30.75 ? 401 XEK A C17 1 
HETATM 2416 C  C17 B XEK B 2 .   ? 7.785  -2.860  22.018  0.48 30.80 ? 401 XEK A C17 1 
HETATM 2417 C  C21 A XEK B 2 .   ? 7.286  -6.237  25.541  0.39 43.27 ? 401 XEK A C21 1 
HETATM 2418 C  C21 B XEK B 2 .   ? 7.247  -6.247  25.537  0.48 43.29 ? 401 XEK A C21 1 
HETATM 2419 C  C22 A XEK B 2 .   ? 6.212  -6.583  23.378  0.39 42.21 ? 401 XEK A C22 1 
HETATM 2420 C  C22 B XEK B 2 .   ? 6.182  -6.590  23.369  0.48 42.26 ? 401 XEK A C22 1 
HETATM 2421 C  C24 A XEK B 2 .   ? 6.833  -0.052  19.782  0.39 18.91 ? 401 XEK A C24 1 
HETATM 2422 C  C24 B XEK B 2 .   ? 6.825  -0.067  19.784  0.48 18.85 ? 401 XEK A C24 1 
HETATM 2423 C  C25 A XEK B 2 .   ? 5.711  0.638   20.181  0.39 24.90 ? 401 XEK A C25 1 
HETATM 2424 C  C25 B XEK B 2 .   ? 5.698  0.610   20.190  0.48 24.93 ? 401 XEK A C25 1 
HETATM 2425 C  C27 A XEK B 2 .   ? 5.470  1.412   17.952  0.39 24.22 ? 401 XEK A C27 1 
HETATM 2426 C  C27 B XEK B 2 .   ? 5.446  1.400   17.968  0.48 24.26 ? 401 XEK A C27 1 
HETATM 2427 C  C16 A XEK B 2 .   ? 9.026  -2.386  22.489  0.39 26.56 ? 401 XEK A C16 1 
HETATM 2428 C  C16 B XEK B 2 .   ? 9.025  -2.408  22.476  0.48 26.56 ? 401 XEK A C16 1 
HETATM 2429 C  C18 A XEK B 2 .   ? 7.244  -4.145  22.478  0.39 32.65 ? 401 XEK A C18 1 
HETATM 2430 C  C18 B XEK B 2 .   ? 7.228  -4.156  22.473  0.48 32.67 ? 401 XEK A C18 1 
HETATM 2431 C  C19 A XEK B 2 .   ? 6.421  -4.943  21.579  0.39 32.00 ? 401 XEK A C19 1 
HETATM 2432 C  C19 B XEK B 2 .   ? 6.406  -4.951  21.571  0.48 31.99 ? 401 XEK A C19 1 
HETATM 2433 C  C20 A XEK B 2 .   ? 7.492  -4.597  23.737  0.39 39.07 ? 401 XEK A C20 1 
HETATM 2434 C  C20 B XEK B 2 .   ? 7.468  -4.608  23.734  0.48 39.12 ? 401 XEK A C20 1 
HETATM 2435 C  C23 A XEK B 2 .   ? 7.066  -2.063  21.134  0.39 25.50 ? 401 XEK A C23 1 
HETATM 2436 C  C23 B XEK B 2 .   ? 7.058  -2.074  21.133  0.48 25.49 ? 401 XEK A C23 1 
HETATM 2437 C  C26 A XEK B 2 .   ? 5.017  1.389   19.249  0.39 20.86 ? 401 XEK A C26 1 
HETATM 2438 C  C26 B XEK B 2 .   ? 4.997  1.364   19.266  0.48 20.82 ? 401 XEK A C26 1 
HETATM 2439 C  C28 A XEK B 2 .   ? 7.222  0.017   18.450  0.39 20.22 ? 401 XEK A C28 1 
HETATM 2440 C  C28 B XEK B 2 .   ? 7.209  0.014   18.451  0.48 20.21 ? 401 XEK A C28 1 
HETATM 2441 F  F1  A XEK B 2 .   ? 14.536 0.448   24.146  0.39 26.24 ? 401 XEK A F1  1 
HETATM 2442 F  F1  B XEK B 2 .   ? 14.533 0.468   24.120  0.48 26.25 ? 401 XEK A F1  1 
HETATM 2443 N  N1  A XEK B 2 .   ? 5.959  -6.132  22.107  0.39 32.30 ? 401 XEK A N1  1 
HETATM 2444 N  N1  B XEK B 2 .   ? 5.937  -6.138  22.097  0.48 32.26 ? 401 XEK A N1  1 
HETATM 2445 N  N2  A XEK B 2 .   ? 6.989  -5.773  24.181  0.39 41.56 ? 401 XEK A N2  1 
HETATM 2446 N  N2  B XEK B 2 .   ? 6.958  -5.782  24.176  0.48 41.60 ? 401 XEK A N2  1 
HETATM 2447 N  N3  A XEK B 2 .   ? 7.584  -0.854  20.720  0.39 20.27 ? 401 XEK A N3  1 
HETATM 2448 N  N3  B XEK B 2 .   ? 7.581  -0.872  20.715  0.48 20.20 ? 401 XEK A N3  1 
HETATM 2449 N  N4  A XEK B 2 .   ? 6.554  0.742   17.549  0.39 20.54 ? 401 XEK A N4  1 
HETATM 2450 N  N4  B XEK B 2 .   ? 6.534  0.741   17.557  0.48 20.52 ? 401 XEK A N4  1 
HETATM 2451 O  O1  A XEK B 2 .   ? 9.223  0.731   20.760  0.39 21.69 ? 401 XEK A O1  1 
HETATM 2452 O  O1  B XEK B 2 .   ? 9.220  0.706   20.740  0.48 21.71 ? 401 XEK A O1  1 
HETATM 2453 O  O2  A XEK B 2 .   ? 12.542 2.268   23.973  0.39 32.57 ? 401 XEK A O2  1 
HETATM 2454 O  O2  B XEK B 2 .   ? 12.553 2.288   23.819  0.48 32.58 ? 401 XEK A O2  1 
HETATM 2455 O  O3  A XEK B 2 .   ? 6.125  -4.661  20.421  0.39 32.41 ? 401 XEK A O3  1 
HETATM 2456 O  O3  B XEK B 2 .   ? 6.116  -4.671  20.411  0.48 32.41 ? 401 XEK A O3  1 
HETATM 2457 O  O4  A XEK B 2 .   ? 5.764  -7.648  23.772  0.39 42.37 ? 401 XEK A O4  1 
HETATM 2458 O  O4  B XEK B 2 .   ? 5.727  -7.653  23.762  0.48 42.41 ? 401 XEK A O4  1 
HETATM 2459 CL CL1 A XEK B 2 .   ? 14.463 -2.374  23.358  0.39 27.72 ? 401 XEK A CL1 1 
HETATM 2460 CL CL1 B XEK B 2 .   ? 14.454 -2.387  23.472  0.48 27.56 ? 401 XEK A CL1 1 
HETATM 2461 CL CL2 A XEK B 2 .   ? 14.380 4.646   21.981  0.39 37.54 ? 401 XEK A CL2 1 
HETATM 2462 CL CL2 B XEK B 2 .   ? 10.607 5.044   24.948  0.48 39.48 ? 401 XEK A CL2 1 
HETATM 2463 H  H1  A XEK B 2 .   ? 11.821 -2.537  22.440  0.39 28.53 ? 401 XEK A H1  1 
HETATM 2464 H  H1  B XEK B 2 .   ? 11.822 -2.579  22.515  0.48 28.53 ? 401 XEK A H1  1 
HETATM 2465 H  H2  A XEK B 2 .   ? 10.951 3.310   23.360  0.39 40.23 ? 401 XEK A H2  1 
HETATM 2466 H  H2  B XEK B 2 .   ? 11.119 3.392   22.975  0.48 40.06 ? 401 XEK A H2  1 
HETATM 2467 H  H3  A XEK B 2 .   ? 12.158 3.330   22.324  0.39 40.23 ? 401 XEK A H3  1 
HETATM 2468 H  H3  B XEK B 2 .   ? 12.332 3.076   21.997  0.48 40.06 ? 401 XEK A H3  1 
HETATM 2469 H  H4  A XEK B 2 .   ? 11.057 4.786   25.368  0.39 44.44 ? 401 XEK A H4  1 
HETATM 2470 H  H4  B XEK B 2 .   ? 14.409 4.412   22.170  0.48 42.22 ? 401 XEK A H4  1 
HETATM 2471 H  H5  A XEK B 2 .   ? 11.856 6.752   26.307  0.39 39.24 ? 401 XEK A H5  1 
HETATM 2472 H  H5  B XEK B 2 .   ? 15.413 6.408   22.799  0.48 40.81 ? 401 XEK A H5  1 
HETATM 2473 H  H6  A XEK B 2 .   ? 13.710 7.805   25.399  0.39 39.83 ? 401 XEK A H6  1 
HETATM 2474 H  H6  B XEK B 2 .   ? 14.377 7.796   24.338  0.48 45.65 ? 401 XEK A H6  1 
HETATM 2475 H  H7  A XEK B 2 .   ? 14.775 6.895   23.554  0.39 44.44 ? 401 XEK A H7  1 
HETATM 2476 H  H7  B XEK B 2 .   ? 12.335 7.199   25.254  0.48 43.36 ? 401 XEK A H7  1 
HETATM 2477 H  H8  A XEK B 2 .   ? 10.378 1.201   22.981  0.39 29.18 ? 401 XEK A H8  1 
HETATM 2478 H  H8  B XEK B 2 .   ? 10.400 1.191   22.852  0.48 29.16 ? 401 XEK A H8  1 
HETATM 2479 H  H13 A XEK B 2 .   ? 7.918  -6.973  25.499  0.39 51.92 ? 401 XEK A H13 1 
HETATM 2480 H  H13 B XEK B 2 .   ? 7.893  -6.971  25.500  0.48 51.96 ? 401 XEK A H13 1 
HETATM 2481 H  H14 A XEK B 2 .   ? 6.466  -6.537  25.965  0.39 51.92 ? 401 XEK A H14 1 
HETATM 2482 H  H14 B XEK B 2 .   ? 6.427  -6.563  25.950  0.48 51.96 ? 401 XEK A H14 1 
HETATM 2483 H  H12 A XEK B 2 .   ? 7.670  -5.507  26.054  0.39 51.92 ? 401 XEK A H12 1 
HETATM 2484 H  H12 B XEK B 2 .   ? 7.611  -5.513  26.058  0.48 51.96 ? 401 XEK A H12 1 
HETATM 2485 H  H16 A XEK B 2 .   ? 5.418  0.601   21.071  0.39 29.89 ? 401 XEK A H16 1 
HETATM 2486 H  H16 B XEK B 2 .   ? 5.408  0.563   21.081  0.48 29.92 ? 401 XEK A H16 1 
HETATM 2487 H  H18 A XEK B 2 .   ? 4.997  1.921   17.316  0.39 29.07 ? 401 XEK A H18 1 
HETATM 2488 H  H18 B XEK B 2 .   ? 4.968  1.910   17.337  0.48 29.12 ? 401 XEK A H18 1 
HETATM 2489 H  H9  A XEK B 2 .   ? 9.510  -2.920  23.106  0.39 31.88 ? 401 XEK A H9  1 
HETATM 2490 H  H9  B XEK B 2 .   ? 9.507  -2.944  23.092  0.48 31.88 ? 401 XEK A H9  1 
HETATM 2491 H  H11 A XEK B 2 .   ? 8.025  -4.090  24.327  0.39 46.88 ? 401 XEK A H11 1 
HETATM 2492 H  H11 B XEK B 2 .   ? 8.001  -4.103  24.326  0.48 46.94 ? 401 XEK A H11 1 
HETATM 2493 H  H15 A XEK B 2 .   ? 6.224  -2.346  20.810  0.39 30.60 ? 401 XEK A H15 1 
HETATM 2494 H  H15 B XEK B 2 .   ? 6.212  -2.352  20.815  0.48 30.59 ? 401 XEK A H15 1 
HETATM 2495 H  H17 A XEK B 2 .   ? 4.251  1.873   19.505  0.39 25.04 ? 401 XEK A H17 1 
HETATM 2496 H  H17 B XEK B 2 .   ? 4.228  1.840   19.528  0.48 24.99 ? 401 XEK A H17 1 
HETATM 2497 H  H19 A XEK B 2 .   ? 7.985  -0.466  18.173  0.39 24.27 ? 401 XEK A H19 1 
HETATM 2498 H  H19 B XEK B 2 .   ? 7.974  -0.463  18.168  0.48 24.26 ? 401 XEK A H19 1 
HETATM 2499 H  H10 A XEK B 2 .   ? 5.465  -6.635  21.581  0.39 38.76 ? 401 XEK A H10 1 
HETATM 2500 H  H10 B XEK B 2 .   ? 5.443  -6.640  21.569  0.48 38.72 ? 401 XEK A H10 1 
HETATM 2501 S  S   . DMS C 3 .   ? 7.152  -28.549 21.198  1.00 33.13 ? 402 DMS A S   1 
HETATM 2502 O  O   . DMS C 3 .   ? 7.951  -27.646 22.071  1.00 29.07 ? 402 DMS A O   1 
HETATM 2503 C  C1  . DMS C 3 .   ? 6.044  -27.567 20.153  1.00 31.42 ? 402 DMS A C1  1 
HETATM 2504 C  C2  . DMS C 3 .   ? 5.965  -29.468 22.223  1.00 36.38 ? 402 DMS A C2  1 
HETATM 2505 H  H11 . DMS C 3 .   ? 5.387  -28.213 19.630  1.00 37.71 ? 402 DMS A H11 1 
HETATM 2506 H  H12 . DMS C 3 .   ? 6.615  -27.008 19.458  1.00 37.71 ? 402 DMS A H12 1 
HETATM 2507 H  H13 . DMS C 3 .   ? 5.480  -26.906 20.758  1.00 37.71 ? 402 DMS A H13 1 
HETATM 2508 H  H21 . DMS C 3 .   ? 4.984  -29.304 21.860  1.00 43.66 ? 402 DMS A H21 1 
HETATM 2509 H  H22 . DMS C 3 .   ? 6.030  -29.133 23.226  1.00 43.66 ? 402 DMS A H22 1 
HETATM 2510 H  H23 . DMS C 3 .   ? 6.188  -30.502 22.181  1.00 43.66 ? 402 DMS A H23 1 
HETATM 2511 S  S   . DMS D 3 .   ? 27.640 -10.883 16.736  1.00 48.89 ? 403 DMS A S   1 
HETATM 2512 O  O   . DMS D 3 .   ? 26.427 -11.072 17.593  1.00 32.48 ? 403 DMS A O   1 
HETATM 2513 C  C1  . DMS D 3 .   ? 28.673 -12.376 16.833  1.00 44.61 ? 403 DMS A C1  1 
HETATM 2514 C  C2  . DMS D 3 .   ? 28.766 -9.711  17.545  1.00 48.45 ? 403 DMS A C2  1 
HETATM 2515 H  H11 . DMS D 3 .   ? 28.345 -13.080 16.114  1.00 53.54 ? 403 DMS A H11 1 
HETATM 2516 H  H12 . DMS D 3 .   ? 28.594 -12.798 17.801  1.00 53.54 ? 403 DMS A H12 1 
HETATM 2517 H  H13 . DMS D 3 .   ? 29.682 -12.120 16.641  1.00 53.54 ? 403 DMS A H13 1 
HETATM 2518 H  H21 . DMS D 3 .   ? 29.299 -10.207 18.315  1.00 58.15 ? 403 DMS A H21 1 
HETATM 2519 H  H22 . DMS D 3 .   ? 28.207 -8.914  17.961  1.00 58.15 ? 403 DMS A H22 1 
HETATM 2520 H  H23 . DMS D 3 .   ? 29.450 -9.329  16.833  1.00 58.15 ? 403 DMS A H23 1 
HETATM 2521 S  S   . DMS E 3 .   ? 20.866 -16.400 4.843   1.00 66.98 ? 404 DMS A S   1 
HETATM 2522 O  O   . DMS E 3 .   ? 19.928 -16.725 5.964   1.00 47.99 ? 404 DMS A O   1 
HETATM 2523 C  C1  . DMS E 3 .   ? 21.732 -14.853 5.235   1.00 59.19 ? 404 DMS A C1  1 
HETATM 2524 C  C2  . DMS E 3 .   ? 19.936 -15.888 3.371   1.00 52.88 ? 404 DMS A C2  1 
HETATM 2525 H  H11 . DMS E 3 .   ? 22.660 -14.829 4.725   1.00 71.03 ? 404 DMS A H11 1 
HETATM 2526 H  H12 . DMS E 3 .   ? 21.902 -14.797 6.279   1.00 71.03 ? 404 DMS A H12 1 
HETATM 2527 H  H13 . DMS E 3 .   ? 21.141 -14.029 4.929   1.00 71.03 ? 404 DMS A H13 1 
HETATM 2528 H  H21 . DMS E 3 .   ? 19.278 -16.666 3.080   1.00 63.46 ? 404 DMS A H21 1 
HETATM 2529 H  H22 . DMS E 3 .   ? 20.610 -15.684 2.580   1.00 63.46 ? 404 DMS A H22 1 
HETATM 2530 H  H23 . DMS E 3 .   ? 19.377 -15.017 3.591   1.00 63.46 ? 404 DMS A H23 1 
HETATM 2531 S  S   A DMS F 3 .   ? 6.405  -0.715  -6.564  0.71 35.75 ? 405 DMS A S   1 
HETATM 2532 S  S   B DMS F 3 .   ? 6.264  -0.470  -5.905  0.29 40.13 ? 405 DMS A S   1 
HETATM 2533 O  O   A DMS F 3 .   ? 7.425  -0.964  -7.632  0.71 44.81 ? 405 DMS A O   1 
HETATM 2534 O  O   B DMS F 3 .   ? 7.220  -0.374  -4.757  0.29 35.65 ? 405 DMS A O   1 
HETATM 2535 C  C1  A DMS F 3 .   ? 7.300  -0.358  -5.024  0.71 36.66 ? 405 DMS A C1  1 
HETATM 2536 C  C1  B DMS F 3 .   ? 5.609  -2.160  -5.991  0.29 36.80 ? 405 DMS A C1  1 
HETATM 2537 C  C2  A DMS F 3 .   ? 5.564  -2.263  -6.129  0.71 37.09 ? 405 DMS A C2  1 
HETATM 2538 C  C2  B DMS F 3 .   ? 7.224  -0.454  -7.444  0.29 39.95 ? 405 DMS A C2  1 
HETATM 2539 H  H11 A DMS F 3 .   ? 8.194  -0.924  -4.995  0.71 44.00 ? 405 DMS A H11 1 
HETATM 2540 H  H11 B DMS F 3 .   ? 5.869  -2.684  -5.108  0.29 44.17 ? 405 DMS A H11 1 
HETATM 2541 H  H12 A DMS F 3 .   ? 6.693  -0.615  -4.195  0.71 44.00 ? 405 DMS A H12 1 
HETATM 2542 H  H12 B DMS F 3 .   ? 6.021  -2.656  -6.830  0.29 44.17 ? 405 DMS A H12 1 
HETATM 2543 H  H13 A DMS F 3 .   ? 7.534  0.674   -4.982  0.71 44.00 ? 405 DMS A H13 1 
HETATM 2544 H  H13 B DMS F 3 .   ? 4.555  -2.125  -6.083  0.29 44.17 ? 405 DMS A H13 1 
HETATM 2545 H  H21 A DMS F 3 .   ? 5.718  -2.976  -6.896  0.71 44.51 ? 405 DMS A H21 1 
HETATM 2546 H  H21 B DMS F 3 .   ? 7.930  0.334   -7.412  0.29 47.95 ? 405 DMS A H21 1 
HETATM 2547 H  H22 A DMS F 3 .   ? 4.527  -2.082  -6.017  0.71 44.51 ? 405 DMS A H22 1 
HETATM 2548 H  H22 B DMS F 3 .   ? 6.572  -0.311  -8.266  0.29 47.95 ? 405 DMS A H22 1 
HETATM 2549 H  H23 A DMS F 3 .   ? 5.957  -2.634  -5.218  0.71 44.51 ? 405 DMS A H23 1 
HETATM 2550 H  H23 B DMS F 3 .   ? 7.732  -1.377  -7.553  0.29 47.95 ? 405 DMS A H23 1 
HETATM 2551 CL CL  . CL  G 4 .   ? -1.585 6.471   -2.524  1.00 46.04 ? 406 CL  A CL  1 
HETATM 2552 O  O   . HOH H 5 .   ? 22.489 -1.122  28.708  1.00 37.31 ? 501 HOH A O   1 
HETATM 2553 O  O   . HOH H 5 .   ? 22.031 -20.794 30.645  1.00 38.66 ? 502 HOH A O   1 
HETATM 2554 O  O   . HOH H 5 .   ? 26.856 6.336   -12.812 1.00 46.94 ? 503 HOH A O   1 
HETATM 2555 O  O   . HOH H 5 .   ? 2.457  -8.924  30.154  1.00 40.46 ? 504 HOH A O   1 
HETATM 2556 O  O   . HOH H 5 .   ? 14.535 -11.583 30.839  1.00 32.90 ? 505 HOH A O   1 
HETATM 2557 O  O   . HOH H 5 .   ? 24.417 -5.792  8.462   1.00 32.74 ? 506 HOH A O   1 
HETATM 2558 O  O   . HOH H 5 .   ? 23.408 26.983  -0.330  1.00 42.81 ? 507 HOH A O   1 
HETATM 2559 O  O   . HOH H 5 .   ? 14.351 -9.391  -4.395  1.00 35.19 ? 508 HOH A O   1 
HETATM 2560 O  O   . HOH H 5 .   ? 3.101  4.979   20.142  1.00 37.92 ? 509 HOH A O   1 
HETATM 2561 O  O   . HOH H 5 .   ? 26.112 -15.218 18.116  1.00 42.45 ? 510 HOH A O   1 
HETATM 2562 O  O   . HOH H 5 .   ? 3.613  -9.963  -16.092 1.00 47.11 ? 511 HOH A O   1 
HETATM 2563 O  O   . HOH H 5 .   ? 3.890  -8.896  24.736  1.00 40.31 ? 512 HOH A O   1 
HETATM 2564 O  O   . HOH H 5 .   ? 27.997 -10.637 24.000  1.00 42.99 ? 513 HOH A O   1 
HETATM 2565 O  O   . HOH H 5 .   ? 12.706 -7.333  35.482  1.00 47.35 ? 514 HOH A O   1 
HETATM 2566 O  O   . HOH H 5 .   ? 6.130  -8.128  8.635   1.00 27.16 ? 515 HOH A O   1 
HETATM 2567 O  O   . HOH H 5 .   ? 13.338 23.293  -18.705 1.00 46.42 ? 516 HOH A O   1 
HETATM 2568 O  O   . HOH H 5 .   ? 24.213 10.379  -17.304 1.00 35.04 ? 517 HOH A O   1 
HETATM 2569 O  O   . HOH H 5 .   ? 6.200  6.176   1.382   1.00 32.74 ? 518 HOH A O   1 
HETATM 2570 O  O   . HOH H 5 .   ? 7.049  -23.328 20.584  1.00 25.35 ? 519 HOH A O   1 
HETATM 2571 O  O   . HOH H 5 .   ? 27.414 -7.892  8.706   1.00 49.78 ? 520 HOH A O   1 
HETATM 2572 O  O   . HOH H 5 .   ? 3.160  13.689  -20.697 1.00 53.07 ? 521 HOH A O   1 
HETATM 2573 O  O   . HOH H 5 .   ? 6.439  10.491  -0.870  1.00 28.25 ? 522 HOH A O   1 
HETATM 2574 O  O   . HOH H 5 .   ? 23.454 1.616   15.756  1.00 24.61 ? 523 HOH A O   1 
HETATM 2575 O  O   . HOH H 5 .   ? 25.735 16.126  -14.250 1.00 33.18 ? 524 HOH A O   1 
HETATM 2576 O  O   . HOH H 5 .   ? 1.861  -11.098 26.663  1.00 45.75 ? 525 HOH A O   1 
HETATM 2577 O  O   . HOH H 5 .   ? 17.028 28.469  -20.414 1.00 28.31 ? 526 HOH A O   1 
HETATM 2578 O  O   . HOH H 5 .   ? 15.823 18.767  -21.851 1.00 30.36 ? 527 HOH A O   1 
HETATM 2579 O  O   . HOH H 5 .   ? 15.710 27.311  -12.144 1.00 30.34 ? 528 HOH A O   1 
HETATM 2580 O  O   . HOH H 5 .   ? 0.467  -0.796  12.139  1.00 29.04 ? 529 HOH A O   1 
HETATM 2581 O  O   . HOH H 5 .   ? 13.454 -24.467 3.572   1.00 36.48 ? 530 HOH A O   1 
HETATM 2582 O  O   . HOH H 5 .   ? 8.240  14.901  -21.898 1.00 29.94 ? 531 HOH A O   1 
HETATM 2583 O  O   . HOH H 5 .   ? 20.860 -18.759 26.263  1.00 29.46 ? 532 HOH A O   1 
HETATM 2584 O  O   . HOH H 5 .   ? 25.997 -11.759 20.057  1.00 34.96 ? 533 HOH A O   1 
HETATM 2585 O  O   . HOH H 5 .   ? 0.322  4.870   -14.514 1.00 33.59 ? 534 HOH A O   1 
HETATM 2586 O  O   . HOH H 5 .   ? 19.257 10.202  13.316  1.00 24.74 ? 535 HOH A O   1 
HETATM 2587 O  O   . HOH H 5 .   ? 22.403 9.824   5.509   1.00 36.81 ? 536 HOH A O   1 
HETATM 2588 O  O   . HOH H 5 .   ? 24.457 -15.613 27.031  1.00 25.74 ? 537 HOH A O   1 
HETATM 2589 O  O   . HOH H 5 .   ? 20.844 7.667   26.054  1.00 41.28 ? 538 HOH A O   1 
HETATM 2590 O  O   . HOH H 5 .   ? 15.668 6.479   -14.154 1.00 32.16 ? 539 HOH A O   1 
HETATM 2591 O  O   . HOH H 5 .   ? 29.667 14.933  -12.737 1.00 43.03 ? 540 HOH A O   1 
HETATM 2592 O  O   . HOH H 5 .   ? 14.498 17.384  10.385  1.00 38.03 ? 541 HOH A O   1 
HETATM 2593 O  O   . HOH H 5 .   ? 7.690  -28.410 15.613  1.00 34.48 ? 542 HOH A O   1 
HETATM 2594 O  O   . HOH H 5 .   ? 24.630 -0.552  12.947  1.00 32.52 ? 543 HOH A O   1 
HETATM 2595 O  O   . HOH H 5 .   ? 19.120 6.337   -2.067  1.00 42.97 ? 544 HOH A O   1 
HETATM 2596 O  O   . HOH H 5 .   ? 11.935 9.996   -25.570 1.00 39.82 ? 545 HOH A O   1 
HETATM 2597 O  O   . HOH H 5 .   ? 5.198  27.210  -8.655  1.00 39.91 ? 546 HOH A O   1 
HETATM 2598 O  O   . HOH H 5 .   ? 0.270  23.575  -3.229  1.00 35.48 ? 547 HOH A O   1 
HETATM 2599 O  O   . HOH H 5 .   ? 12.515 -27.403 22.764  1.00 28.48 ? 548 HOH A O   1 
HETATM 2600 O  O   . HOH H 5 .   ? 6.374  8.235   12.120  1.00 38.64 ? 549 HOH A O   1 
HETATM 2601 O  O   . HOH H 5 .   ? 17.840 -6.000  33.739  1.00 44.59 ? 550 HOH A O   1 
HETATM 2602 O  O   . HOH H 5 .   ? 7.409  -26.109 0.200   1.00 44.06 ? 551 HOH A O   1 
HETATM 2603 O  O   . HOH H 5 .   ? 22.871 -0.663  18.054  1.00 22.94 ? 552 HOH A O   1 
HETATM 2604 O  O   . HOH H 5 .   ? 1.640  23.623  -1.303  1.00 41.61 ? 553 HOH A O   1 
HETATM 2605 O  O   . HOH H 5 .   ? 5.578  -31.939 18.765  1.00 49.13 ? 554 HOH A O   1 
HETATM 2606 O  O   . HOH H 5 .   ? 16.867 -18.810 7.336   1.00 25.50 ? 555 HOH A O   1 
HETATM 2607 O  O   . HOH H 5 .   ? 15.653 -22.347 31.538  1.00 38.21 ? 556 HOH A O   1 
HETATM 2608 O  O   . HOH H 5 .   ? 5.227  -17.334 1.781   1.00 31.58 ? 557 HOH A O   1 
HETATM 2609 O  O   . HOH H 5 .   ? 20.877 18.802  3.136   1.00 36.89 ? 558 HOH A O   1 
HETATM 2610 O  O   . HOH H 5 .   ? 22.447 -18.043 10.723  1.00 43.22 ? 559 HOH A O   1 
HETATM 2611 O  O   . HOH H 5 .   ? 18.309 27.963  -13.120 1.00 36.88 ? 560 HOH A O   1 
HETATM 2612 O  O   . HOH H 5 .   ? 0.909  9.246   -5.792  1.00 42.34 ? 561 HOH A O   1 
HETATM 2613 O  O   . HOH H 5 .   ? 9.632  10.540  -4.820  1.00 15.65 ? 562 HOH A O   1 
HETATM 2614 O  O   . HOH H 5 .   ? 20.747 -13.073 10.251  1.00 31.66 ? 563 HOH A O   1 
HETATM 2615 O  O   . HOH H 5 .   ? 3.658  29.092  -3.651  1.00 37.20 ? 564 HOH A O   1 
HETATM 2616 O  O   . HOH H 5 .   ? 16.782 2.625   12.233  1.00 23.11 ? 565 HOH A O   1 
HETATM 2617 O  O   . HOH H 5 .   ? 2.662  -8.999  18.608  1.00 30.22 ? 566 HOH A O   1 
HETATM 2618 O  O   . HOH H 5 .   ? 20.542 10.122  15.793  1.00 24.91 ? 567 HOH A O   1 
HETATM 2619 O  O   . HOH H 5 .   ? -1.753 -15.061 2.964   1.00 38.94 ? 568 HOH A O   1 
HETATM 2620 O  O   . HOH H 5 .   ? 8.205  -31.708 16.756  1.00 34.97 ? 569 HOH A O   1 
HETATM 2621 O  O   . HOH H 5 .   ? 25.478 9.292   -4.945  1.00 38.08 ? 570 HOH A O   1 
HETATM 2622 O  O   . HOH H 5 .   ? 10.049 20.240  -0.399  1.00 29.27 ? 571 HOH A O   1 
HETATM 2623 O  O   . HOH H 5 .   ? 21.775 8.932   22.608  1.00 42.11 ? 572 HOH A O   1 
HETATM 2624 O  O   . HOH H 5 .   ? 21.278 21.672  4.280   1.00 38.71 ? 573 HOH A O   1 
HETATM 2625 O  O   . HOH H 5 .   ? 9.038  25.151  -11.767 1.00 29.07 ? 574 HOH A O   1 
HETATM 2626 O  O   . HOH H 5 .   ? 4.948  24.894  -18.186 1.00 43.00 ? 575 HOH A O   1 
HETATM 2627 O  O   . HOH H 5 .   ? 16.940 6.777   -4.041  1.00 26.80 ? 576 HOH A O   1 
HETATM 2628 O  O   . HOH H 5 .   ? 15.140 -26.263 26.532  1.00 28.27 ? 577 HOH A O   1 
HETATM 2629 O  O   . HOH H 5 .   ? 21.234 10.963  -16.964 1.00 25.58 ? 578 HOH A O   1 
HETATM 2630 O  O   . HOH H 5 .   ? 9.835  6.676   5.670   1.00 20.64 ? 579 HOH A O   1 
HETATM 2631 O  O   . HOH H 5 .   ? 18.411 -24.483 25.702  1.00 31.02 ? 580 HOH A O   1 
HETATM 2632 O  O   . HOH H 5 .   ? 20.458 -21.812 27.109  1.00 35.01 ? 581 HOH A O   1 
HETATM 2633 O  O   . HOH H 5 .   ? 10.287 -26.201 21.896  1.00 24.94 ? 582 HOH A O   1 
HETATM 2634 O  O   . HOH H 5 .   ? 3.126  10.355  -21.358 1.00 38.30 ? 583 HOH A O   1 
HETATM 2635 O  O   . HOH H 5 .   ? 8.391  -24.904 25.526  1.00 29.10 ? 584 HOH A O   1 
HETATM 2636 O  O   . HOH H 5 .   ? -0.211 7.840   -3.899  1.00 41.49 ? 585 HOH A O   1 
HETATM 2637 O  O   . HOH H 5 .   ? 27.421 23.286  -4.827  1.00 33.05 ? 586 HOH A O   1 
HETATM 2638 O  O   . HOH H 5 .   ? 24.686 -9.161  20.292  1.00 23.10 ? 587 HOH A O   1 
HETATM 2639 O  O   . HOH H 5 .   ? -1.185 16.940  -19.993 1.00 33.00 ? 588 HOH A O   1 
HETATM 2640 O  O   . HOH H 5 .   ? 18.050 13.976  -21.902 1.00 36.72 ? 589 HOH A O   1 
HETATM 2641 O  O   . HOH H 5 .   ? -1.561 3.141   -1.298  1.00 40.71 ? 590 HOH A O   1 
HETATM 2642 O  O   . HOH H 5 .   ? 5.703  -17.831 28.096  1.00 39.86 ? 591 HOH A O   1 
HETATM 2643 O  O   . HOH H 5 .   ? 5.103  11.274  18.226  1.00 33.82 ? 592 HOH A O   1 
HETATM 2644 O  O   . HOH H 5 .   ? 23.972 23.030  -17.495 1.00 24.03 ? 593 HOH A O   1 
HETATM 2645 O  O   . HOH H 5 .   ? 27.861 26.459  -11.798 1.00 40.45 ? 594 HOH A O   1 
HETATM 2646 O  O   . HOH H 5 .   ? -0.522 1.840   13.355  1.00 34.92 ? 595 HOH A O   1 
HETATM 2647 O  O   . HOH H 5 .   ? 11.869 -31.543 24.449  1.00 26.56 ? 596 HOH A O   1 
HETATM 2648 O  O   . HOH H 5 .   ? 15.128 -4.903  0.154   1.00 29.39 ? 597 HOH A O   1 
HETATM 2649 O  O   . HOH H 5 .   ? 18.739 -7.443  5.873   1.00 24.96 ? 598 HOH A O   1 
HETATM 2650 O  O   . HOH H 5 .   ? 23.658 -7.916  34.146  1.00 43.21 ? 599 HOH A O   1 
HETATM 2651 O  O   . HOH H 5 .   ? 20.164 -20.306 16.246  1.00 35.76 ? 600 HOH A O   1 
HETATM 2652 O  O   . HOH H 5 .   ? 4.005  -17.568 20.776  1.00 29.44 ? 601 HOH A O   1 
HETATM 2653 O  O   . HOH H 5 .   ? 4.726  22.716  -19.335 1.00 41.66 ? 602 HOH A O   1 
HETATM 2654 O  O   . HOH H 5 .   ? 16.553 -13.146 31.540  1.00 36.38 ? 603 HOH A O   1 
HETATM 2655 O  O   . HOH H 5 .   ? 13.863 12.055  17.613  1.00 35.24 ? 604 HOH A O   1 
HETATM 2656 O  O   . HOH H 5 .   ? -3.956 -11.755 2.563   1.00 26.93 ? 605 HOH A O   1 
HETATM 2657 O  O   . HOH H 5 .   ? 12.667 31.571  -8.507  1.00 31.15 ? 606 HOH A O   1 
HETATM 2658 O  O   . HOH H 5 .   ? -3.149 28.943  -7.940  1.00 31.61 ? 607 HOH A O   1 
HETATM 2659 O  O   . HOH H 5 .   ? 10.983 -24.819 2.707   1.00 32.58 ? 608 HOH A O   1 
HETATM 2660 O  O   . HOH H 5 .   ? 15.862 -27.908 11.658  1.00 31.17 ? 609 HOH A O   1 
HETATM 2661 O  O   . HOH H 5 .   ? 15.968 -5.583  20.164  1.00 22.14 ? 610 HOH A O   1 
HETATM 2662 O  O   . HOH H 5 .   ? 24.259 -16.233 21.200  1.00 29.66 ? 611 HOH A O   1 
HETATM 2663 O  O   . HOH H 5 .   ? 23.847 12.757  -1.636  1.00 40.91 ? 612 HOH A O   1 
HETATM 2664 O  O   . HOH H 5 .   ? 22.205 6.958   0.061   1.00 46.23 ? 613 HOH A O   1 
HETATM 2665 O  O   . HOH H 5 .   ? 10.472 -0.205  -3.244  1.00 31.43 ? 614 HOH A O   1 
HETATM 2666 O  O   . HOH H 5 .   ? 23.192 -2.498  15.860  1.00 22.74 ? 615 HOH A O   1 
HETATM 2667 O  O   . HOH H 5 .   ? 13.417 0.982   -5.326  1.00 31.11 ? 616 HOH A O   1 
HETATM 2668 O  O   . HOH H 5 .   ? 9.912  8.057   -25.120 1.00 35.33 ? 617 HOH A O   1 
HETATM 2669 O  O   . HOH H 5 .   ? 7.841  3.842   -3.398  1.00 24.27 ? 618 HOH A O   1 
HETATM 2670 O  O   . HOH H 5 .   ? 5.542  2.820   -4.737  1.00 25.03 ? 619 HOH A O   1 
HETATM 2671 O  O   . HOH H 5 .   ? 8.059  -28.400 6.093   1.00 33.89 ? 620 HOH A O   1 
HETATM 2672 O  O   . HOH H 5 .   ? 22.688 19.613  0.688   1.00 32.58 ? 621 HOH A O   1 
HETATM 2673 O  O   . HOH H 5 .   ? 20.663 13.830  8.884   1.00 40.31 ? 622 HOH A O   1 
HETATM 2674 O  O   . HOH H 5 .   ? 6.161  2.692   -7.656  1.00 31.73 ? 623 HOH A O   1 
HETATM 2675 O  O   . HOH H 5 .   ? 25.108 -8.275  25.914  1.00 37.45 ? 624 HOH A O   1 
HETATM 2676 O  O   . HOH H 5 .   ? 23.684 2.789   9.541   1.00 34.70 ? 625 HOH A O   1 
HETATM 2677 O  O   . HOH H 5 .   ? 13.611 11.123  19.933  1.00 32.98 ? 626 HOH A O   1 
HETATM 2678 O  O   . HOH H 5 .   ? 26.643 20.744  -14.080 1.00 33.69 ? 627 HOH A O   1 
HETATM 2679 O  O   . HOH H 5 .   ? 25.787 -14.194 21.957  1.00 46.15 ? 628 HOH A O   1 
HETATM 2680 O  O   . HOH H 5 .   ? 1.863  11.950  -5.675  1.00 27.99 ? 629 HOH A O   1 
HETATM 2681 O  O   . HOH H 5 .   ? 3.886  -22.041 6.968   1.00 30.72 ? 630 HOH A O   1 
HETATM 2682 O  O   . HOH H 5 .   ? 8.408  -18.521 28.334  1.00 41.50 ? 631 HOH A O   1 
HETATM 2683 O  O   . HOH H 5 .   ? 14.620 0.579   -2.926  1.00 29.99 ? 632 HOH A O   1 
HETATM 2684 O  O   . HOH H 5 .   ? 22.957 1.843   5.229   1.00 40.65 ? 633 HOH A O   1 
HETATM 2685 O  O   . HOH H 5 .   ? -5.375 25.038  -7.355  1.00 30.17 ? 634 HOH A O   1 
HETATM 2686 O  O   . HOH H 5 .   ? 31.017 25.233  -10.732 1.00 39.62 ? 635 HOH A O   1 
HETATM 2687 O  O   . HOH H 5 .   ? 7.967  3.613   29.733  1.00 35.81 ? 636 HOH A O   1 
HETATM 2688 O  O   . HOH H 5 .   ? 11.758 -29.600 7.790   1.00 39.57 ? 637 HOH A O   1 
HETATM 2689 O  O   . HOH H 5 .   ? 4.268  25.160  -1.861  1.00 38.36 ? 638 HOH A O   1 
HETATM 2690 O  O   . HOH H 5 .   ? 21.954 -1.902  20.416  1.00 26.97 ? 639 HOH A O   1 
HETATM 2691 O  O   . HOH H 5 .   ? 27.922 20.803  -5.456  1.00 38.15 ? 640 HOH A O   1 
HETATM 2692 O  O   . HOH H 5 .   ? 9.311  -24.249 22.587  1.00 47.82 ? 641 HOH A O   1 
HETATM 2693 O  O   . HOH H 5 .   ? 2.772  -19.887 21.544  1.00 35.16 ? 642 HOH A O   1 
HETATM 2694 O  O   . HOH H 5 .   ? 1.461  -16.612 12.458  1.00 34.35 ? 643 HOH A O   1 
HETATM 2695 O  O   . HOH H 5 .   ? 9.513  -17.338 -3.969  1.00 33.93 ? 644 HOH A O   1 
HETATM 2696 O  O   . HOH H 5 .   ? 14.869 26.640  4.058   1.00 35.63 ? 645 HOH A O   1 
HETATM 2697 O  O   . HOH H 5 .   ? 23.390 -5.790  1.596   1.00 34.06 ? 646 HOH A O   1 
HETATM 2698 O  O   . HOH H 5 .   ? 21.318 -1.932  23.995  1.00 32.12 ? 647 HOH A O   1 
HETATM 2699 O  O   . HOH H 5 .   ? 12.368 22.371  2.509   1.00 35.72 ? 648 HOH A O   1 
HETATM 2700 O  O   . HOH H 5 .   ? 10.408 25.205  -0.537  1.00 37.69 ? 649 HOH A O   1 
HETATM 2701 O  O   . HOH H 5 .   ? 26.596 -16.342 23.468  1.00 38.56 ? 650 HOH A O   1 
HETATM 2702 O  O   . HOH H 5 .   ? 20.493 -8.804  33.835  1.00 47.82 ? 651 HOH A O   1 
HETATM 2703 O  O   . HOH H 5 .   ? 18.675 3.768   32.372  1.00 44.76 ? 652 HOH A O   1 
HETATM 2704 O  O   . HOH H 5 .   ? 11.790 15.933  5.223   1.00 42.35 ? 653 HOH A O   1 
HETATM 2705 O  O   . HOH H 5 .   ? -2.985 22.122  -9.637  1.00 32.48 ? 654 HOH A O   1 
HETATM 2706 O  O   . HOH H 5 .   ? -2.214 19.897  -11.477 1.00 37.38 ? 655 HOH A O   1 
HETATM 2707 O  O   . HOH H 5 .   ? 22.245 16.860  4.238   1.00 37.63 ? 656 HOH A O   1 
HETATM 2708 O  O   . HOH H 5 .   ? 0.869  1.961   20.406  1.00 39.26 ? 657 HOH A O   1 
HETATM 2709 O  O   . HOH H 5 .   ? 21.364 9.995   2.827   1.00 44.06 ? 658 HOH A O   1 
HETATM 2710 O  O   . HOH H 5 .   ? -0.002 -15.027 7.976   1.00 46.17 ? 659 HOH A O   1 
HETATM 2711 O  O   . HOH H 5 .   ? 21.212 -13.331 2.057   1.00 38.30 ? 660 HOH A O   1 
HETATM 2712 O  O   . HOH H 5 .   ? 12.210 -22.752 32.609  1.00 48.37 ? 661 HOH A O   1 
HETATM 2713 O  O   . HOH H 5 .   ? 21.579 6.287   20.122  1.00 38.45 ? 662 HOH A O   1 
HETATM 2714 O  O   . HOH H 5 .   ? -2.648 9.812   -10.657 1.00 41.56 ? 663 HOH A O   1 
HETATM 2715 O  O   . HOH H 5 .   ? -2.338 16.926  -9.523  1.00 35.81 ? 664 HOH A O   1 
HETATM 2716 O  O   . HOH H 5 .   ? 17.853 29.210  -3.406  1.00 43.44 ? 665 HOH A O   1 
HETATM 2717 O  O   . HOH H 5 .   ? 24.843 5.671   -10.820 1.00 36.78 ? 666 HOH A O   1 
HETATM 2718 O  O   . HOH H 5 .   ? 3.926  -18.813 8.981   1.00 38.46 ? 667 HOH A O   1 
HETATM 2719 O  O   . HOH H 5 .   ? 6.019  4.334   21.681  1.00 34.43 ? 668 HOH A O   1 
HETATM 2720 O  O   . HOH H 5 .   ? 19.615 12.727  -3.648  1.00 26.49 ? 669 HOH A O   1 
HETATM 2721 O  O   . HOH H 5 .   ? 12.518 -32.682 16.736  1.00 40.75 ? 670 HOH A O   1 
HETATM 2722 O  O   . HOH H 5 .   ? 21.374 -23.049 21.360  1.00 34.91 ? 671 HOH A O   1 
HETATM 2723 O  O   . HOH H 5 .   ? 7.400  20.272  -0.526  1.00 30.32 ? 672 HOH A O   1 
HETATM 2724 O  O   . HOH H 5 .   ? 20.058 -6.786  32.321  1.00 28.31 ? 673 HOH A O   1 
HETATM 2725 O  O   . HOH H 5 .   ? 23.859 -5.759  26.166  1.00 27.86 ? 674 HOH A O   1 
HETATM 2726 O  O   . HOH H 5 .   ? 16.551 -28.418 23.332  1.00 31.90 ? 675 HOH A O   1 
HETATM 2727 O  O   . HOH H 5 .   ? -0.434 -15.994 14.431  1.00 48.03 ? 676 HOH A O   1 
HETATM 2728 O  O   . HOH H 5 .   ? 15.713 24.955  8.091   1.00 43.84 ? 677 HOH A O   1 
HETATM 2729 O  O   . HOH H 5 .   ? 20.571 -25.809 21.886  1.00 34.33 ? 678 HOH A O   1 
HETATM 2730 O  O   . HOH H 5 .   ? 0.000  16.764  0.000   0.50 21.37 ? 679 HOH A O   1 
HETATM 2731 O  O   . HOH H 5 .   ? 1.524  14.417  0.970   1.00 40.07 ? 680 HOH A O   1 
HETATM 2732 O  O   . HOH H 5 .   ? 14.434 -20.236 -0.030  1.00 41.04 ? 681 HOH A O   1 
HETATM 2733 O  O   . HOH H 5 .   ? 20.604 -26.735 17.338  1.00 48.06 ? 682 HOH A O   1 
HETATM 2734 O  O   . HOH H 5 .   ? 13.252 18.958  -23.260 1.00 37.85 ? 683 HOH A O   1 
HETATM 2735 O  O   . HOH H 5 .   ? 27.870 0.808   1.635   1.00 43.71 ? 684 HOH A O   1 
HETATM 2736 O  O   . HOH H 5 .   ? 28.489 21.843  -11.848 1.00 29.70 ? 685 HOH A O   1 
HETATM 2737 O  O   . HOH H 5 .   ? 8.233  17.282  1.397   1.00 42.37 ? 686 HOH A O   1 
HETATM 2738 O  O   . HOH H 5 .   ? 6.402  26.763  -14.621 1.00 39.46 ? 687 HOH A O   1 
HETATM 2739 O  O   . HOH H 5 .   ? 7.644  -8.405  -15.360 1.00 48.79 ? 688 HOH A O   1 
HETATM 2740 O  O   . HOH H 5 .   ? 18.555 -29.750 19.846  1.00 39.24 ? 689 HOH A O   1 
HETATM 2741 O  O   . HOH H 5 .   ? 23.789 19.982  -1.876  1.00 35.41 ? 690 HOH A O   1 
HETATM 2742 O  O   . HOH H 5 .   ? 8.000  2.962   22.570  1.00 34.08 ? 691 HOH A O   1 
HETATM 2743 O  O   . HOH H 5 .   ? 8.987  -12.734 31.276  1.00 46.17 ? 692 HOH A O   1 
HETATM 2744 O  O   . HOH H 5 .   ? -0.381 20.382  -15.875 1.00 38.45 ? 693 HOH A O   1 
HETATM 2745 O  O   . HOH H 5 .   ? 21.621 16.722  -17.611 1.00 31.41 ? 694 HOH A O   1 
HETATM 2746 O  O   . HOH H 5 .   ? 9.087  28.691  -1.394  1.00 39.39 ? 695 HOH A O   1 
HETATM 2747 O  O   . HOH H 5 .   ? 13.300 -2.512  -5.544  1.00 42.36 ? 696 HOH A O   1 
HETATM 2748 O  O   . HOH H 5 .   ? 16.407 -18.588 -0.989  1.00 36.29 ? 697 HOH A O   1 
HETATM 2749 O  O   . HOH H 5 .   ? 7.280  12.558  0.876   1.00 34.22 ? 698 HOH A O   1 
HETATM 2750 O  O   . HOH H 5 .   ? 25.516 3.481   28.579  1.00 38.46 ? 699 HOH A O   1 
HETATM 2751 O  O   . HOH H 5 .   ? 25.253 13.533  -17.271 1.00 31.53 ? 700 HOH A O   1 
HETATM 2752 O  O   . HOH H 5 .   ? 14.870 10.894  23.552  1.00 35.61 ? 701 HOH A O   1 
HETATM 2753 O  O   . HOH H 5 .   ? 18.637 -26.052 29.631  1.00 40.15 ? 702 HOH A O   1 
HETATM 2754 O  O   . HOH H 5 .   ? 27.352 27.124  -8.748  1.00 41.39 ? 703 HOH A O   1 
HETATM 2755 O  O   . HOH H 5 .   ? 12.464 -20.598 33.237  1.00 52.09 ? 704 HOH A O   1 
HETATM 2756 O  O   . HOH H 5 .   ? 13.804 -19.802 -7.496  1.00 53.82 ? 705 HOH A O   1 
HETATM 2757 O  O   . HOH H 5 .   ? 10.887 -23.695 0.127   1.00 38.22 ? 706 HOH A O   1 
HETATM 2758 O  O   . HOH H 5 .   ? 19.493 9.737   0.945   1.00 33.58 ? 707 HOH A O   1 
HETATM 2759 O  O   . HOH H 5 .   ? -0.315 4.761   -19.280 1.00 45.97 ? 708 HOH A O   1 
HETATM 2760 O  O   . HOH H 5 .   ? 24.542 -20.031 21.229  1.00 37.49 ? 709 HOH A O   1 
HETATM 2761 O  O   . HOH H 5 .   ? 2.087  -18.915 8.001   1.00 29.13 ? 710 HOH A O   1 
HETATM 2762 O  O   . HOH H 5 .   ? 1.782  5.935   -15.932 1.00 39.83 ? 711 HOH A O   1 
HETATM 2763 O  O   . HOH H 5 .   ? 18.602 4.473   -2.891  1.00 44.15 ? 712 HOH A O   1 
HETATM 2764 O  O   . HOH H 5 .   ? 4.151  10.329  14.847  1.00 44.40 ? 713 HOH A O   1 
HETATM 2765 O  O   . HOH H 5 .   ? 4.728  27.740  -13.165 1.00 48.21 ? 714 HOH A O   1 
HETATM 2766 O  O   . HOH H 5 .   ? 29.481 24.214  -12.306 1.00 38.32 ? 715 HOH A O   1 
HETATM 2767 O  O   . HOH H 5 .   ? 21.025 -22.219 17.004  1.00 35.46 ? 716 HOH A O   1 
HETATM 2768 O  O   . HOH H 5 .   ? 5.830  -18.691 -1.175  1.00 39.28 ? 717 HOH A O   1 
HETATM 2769 O  O   . HOH H 5 .   ? 16.464 -4.021  -2.181  1.00 36.86 ? 718 HOH A O   1 
HETATM 2770 O  O   . HOH H 5 .   ? 24.379 6.881   0.537   1.00 47.02 ? 719 HOH A O   1 
HETATM 2771 O  O   . HOH H 5 .   ? 13.826 19.671  7.275   1.00 49.41 ? 720 HOH A O   1 
HETATM 2772 O  O   . HOH H 5 .   ? 19.299 12.266  23.199  1.00 39.48 ? 721 HOH A O   1 
HETATM 2773 O  O   . HOH H 5 .   ? 4.111  -7.538  27.120  1.00 41.82 ? 722 HOH A O   1 
HETATM 2774 O  O   . HOH H 5 .   ? 15.761 -26.106 6.625   1.00 34.96 ? 723 HOH A O   1 
HETATM 2775 O  O   . HOH H 5 .   ? 14.617 -6.686  -4.615  1.00 39.71 ? 724 HOH A O   1 
HETATM 2776 O  O   . HOH H 5 .   ? 18.156 -24.380 5.928   1.00 45.12 ? 725 HOH A O   1 
HETATM 2777 O  O   . HOH H 5 .   ? 21.094 8.469   18.332  1.00 33.52 ? 726 HOH A O   1 
HETATM 2778 O  O   . HOH H 5 .   ? 3.516  -17.861 0.189   1.00 35.89 ? 727 HOH A O   1 
HETATM 2779 O  O   . HOH H 5 .   ? -2.360 10.987  -12.976 1.00 44.05 ? 728 HOH A O   1 
HETATM 2780 O  O   . HOH H 5 .   ? 17.829 15.606  -23.555 1.00 40.53 ? 729 HOH A O   1 
HETATM 2781 O  O   . HOH H 5 .   ? 26.589 23.125  -1.822  1.00 41.93 ? 730 HOH A O   1 
HETATM 2782 O  O   . HOH H 5 .   ? 18.578 -8.143  36.136  1.00 47.96 ? 731 HOH A O   1 
HETATM 2783 O  O   . HOH H 5 .   ? 16.062 -2.020  -3.451  1.00 44.00 ? 732 HOH A O   1 
HETATM 2784 O  O   . HOH H 5 .   ? 25.016 -12.017 35.230  1.00 39.19 ? 733 HOH A O   1 
HETATM 2785 O  O   . HOH H 5 .   ? 24.902 9.988   -2.298  1.00 33.45 ? 734 HOH A O   1 
HETATM 2786 O  O   . HOH H 5 .   ? 23.253 -17.393 25.467  1.00 31.31 ? 735 HOH A O   1 
HETATM 2787 O  O   . HOH H 5 .   ? 23.609 -1.682  22.453  1.00 40.27 ? 736 HOH A O   1 
HETATM 2788 O  O   . HOH H 5 .   ? -4.853 -11.764 5.098   1.00 42.03 ? 737 HOH A O   1 
HETATM 2789 O  O   . HOH H 5 .   ? 5.448  1.244   24.523  1.00 46.17 ? 738 HOH A O   1 
HETATM 2790 O  O   . HOH H 5 .   ? 6.575  22.046  -1.579  1.00 41.20 ? 739 HOH A O   1 
HETATM 2791 O  O   . HOH H 5 .   ? 19.892 11.028  -1.607  1.00 35.20 ? 740 HOH A O   1 
HETATM 2792 O  O   . HOH H 5 .   ? 14.162 -28.101 24.972  1.00 28.10 ? 741 HOH A O   1 
HETATM 2793 O  O   . HOH H 5 .   ? 19.063 -20.773 7.288   1.00 38.74 ? 742 HOH A O   1 
HETATM 2794 O  O   . HOH H 5 .   ? 27.079 18.190  -14.641 1.00 44.22 ? 743 HOH A O   1 
HETATM 2795 O  O   . HOH H 5 .   ? 28.716 -10.444 21.335  1.00 37.56 ? 744 HOH A O   1 
HETATM 2796 O  O   . HOH H 5 .   ? 13.401 12.555  22.115  1.00 37.50 ? 745 HOH A O   1 
HETATM 2797 O  O   . HOH H 5 .   ? 14.477 15.025  18.069  1.00 42.88 ? 746 HOH A O   1 
HETATM 2798 O  O   . HOH H 5 .   ? 16.580 13.197  23.660  1.00 34.09 ? 747 HOH A O   1 
HETATM 2799 O  O   . HOH H 5 .   ? 12.866 24.912  3.702   1.00 31.64 ? 748 HOH A O   1 
HETATM 2800 O  O   . HOH H 5 .   ? 11.674 -34.087 23.891  1.00 35.25 ? 749 HOH A O   1 
HETATM 2801 O  O   . HOH H 5 .   ? 10.791 14.132  22.100  1.00 42.34 ? 750 HOH A O   1 
HETATM 2802 O  O   . HOH H 5 .   ? 12.558 20.356  5.346   1.00 40.59 ? 751 HOH A O   1 
HETATM 2803 O  O   . HOH H 5 .   ? 17.730 -26.669 27.021  1.00 32.25 ? 752 HOH A O   1 
HETATM 2804 O  O   . HOH H 5 .   ? 18.305 6.504   -6.332  1.00 39.50 ? 753 HOH A O   1 
HETATM 2805 O  O   . HOH H 5 .   ? -5.347 22.765  -9.075  1.00 44.90 ? 754 HOH A O   1 
HETATM 2806 O  O   . HOH H 5 .   ? 28.633 -4.206  16.673  1.00 45.79 ? 755 HOH A O   1 
HETATM 2807 O  O   . HOH H 5 .   ? -4.675 26.780  -9.144  1.00 36.43 ? 756 HOH A O   1 
HETATM 2808 O  O   . HOH H 5 .   ? 25.674 0.856   16.347  1.00 42.11 ? 757 HOH A O   1 
HETATM 2809 O  O   . HOH H 5 .   ? 26.319 21.533  -16.749 1.00 35.47 ? 758 HOH A O   1 
HETATM 2810 O  O   . HOH H 5 .   ? 26.480 20.269  -1.556  1.00 38.01 ? 759 HOH A O   1 
HETATM 2811 O  O   . HOH H 5 .   ? 15.836 2.671   -14.255 1.00 40.60 ? 760 HOH A O   1 
HETATM 2812 O  O   . HOH H 5 .   ? 10.649 -27.430 2.502   1.00 34.90 ? 761 HOH A O   1 
HETATM 2813 O  O   . HOH H 5 .   ? 22.146 4.124   -2.934  1.00 45.47 ? 762 HOH A O   1 
HETATM 2814 O  O   . HOH H 5 .   ? 10.883 22.681  0.654   1.00 32.26 ? 763 HOH A O   1 
HETATM 2815 O  O   . HOH H 5 .   ? 24.260 15.999  -16.730 1.00 34.94 ? 764 HOH A O   1 
HETATM 2816 O  O   . HOH H 5 .   ? 21.558 -17.691 36.293  1.00 46.76 ? 765 HOH A O   1 
HETATM 2817 O  O   . HOH H 5 .   ? 0.480  19.359  -21.386 1.00 45.65 ? 766 HOH A O   1 
HETATM 2818 O  O   . HOH H 5 .   ? 0.000  25.336  0.000   0.50 51.89 ? 767 HOH A O   1 
HETATM 2819 O  O   . HOH H 5 .   ? 24.427 18.846  2.375   1.00 37.72 ? 768 HOH A O   1 
HETATM 2820 O  O   . HOH H 5 .   ? 23.732 5.676   -2.696  1.00 45.63 ? 769 HOH A O   1 
HETATM 2821 O  O   . HOH H 5 .   ? 5.068  21.007  -21.691 0.50 37.99 ? 770 HOH A O   1 
HETATM 2822 O  O   . HOH H 5 .   ? 4.714  1.393   26.374  1.00 49.49 ? 771 HOH A O   1 
HETATM 2823 O  O   . HOH H 5 .   ? 24.475 8.383   4.707   1.00 40.19 ? 772 HOH A O   1 
HETATM 2824 O  O   . HOH H 5 .   ? 16.517 15.439  22.458  1.00 41.25 ? 773 HOH A O   1 
HETATM 2825 O  O   . HOH H 5 .   ? 1.926  20.775  -21.476 1.00 42.62 ? 774 HOH A O   1 
HETATM 2826 O  O   . HOH H 5 .   ? 14.241 14.786  21.055  1.00 41.87 ? 775 HOH A O   1 
HETATM 2827 O  O   . HOH H 5 .   ? 27.772 18.846  0.506   1.00 40.87 ? 776 HOH A O   1 
HETATM 2828 O  O   . HOH H 5 .   ? 25.324 17.563  -18.736 1.00 37.15 ? 777 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 1   ? 0.3229 0.4854 0.3208 -0.0876 -0.1139 0.1681  1   SER A N   
2    C CA  . SER A 1   ? 0.2997 0.4593 0.3247 -0.0798 -0.1099 0.1751  1   SER A CA  
3    C C   . SER A 1   ? 0.3341 0.4833 0.3800 -0.0733 -0.1068 0.1667  1   SER A C   
4    O O   . SER A 1   ? 0.3626 0.5069 0.4020 -0.0746 -0.1066 0.1553  1   SER A O   
5    C CB  . SER A 1   ? 0.4068 0.5802 0.4498 -0.0808 -0.1176 0.1956  1   SER A CB  
6    O OG  . SER A 1   ? 0.5577 0.7420 0.6044 -0.0855 -0.1275 0.2016  1   SER A OG  
7    N N   . GLY A 2   ? 0.3543 0.5000 0.4250 -0.0666 -0.1043 0.1726  2   GLY A N   
8    C CA  . GLY A 2   ? 0.2504 0.3844 0.3381 -0.0593 -0.0992 0.1631  2   GLY A CA  
9    C C   . GLY A 2   ? 0.3456 0.4665 0.4245 -0.0559 -0.0898 0.1506  2   GLY A C   
10   O O   . GLY A 2   ? 0.3316 0.4513 0.3877 -0.0591 -0.0863 0.1448  2   GLY A O   
11   N N   . PHE A 3   ? 0.3427 0.4538 0.4400 -0.0490 -0.0855 0.1462  3   PHE A N   
12   C CA  . PHE A 3   ? 0.3259 0.4254 0.4175 -0.0457 -0.0773 0.1350  3   PHE A CA  
13   C C   . PHE A 3   ? 0.2809 0.3704 0.3855 -0.0396 -0.0740 0.1248  3   PHE A C   
14   O O   . PHE A 3   ? 0.3590 0.4467 0.4852 -0.0350 -0.0755 0.1293  3   PHE A O   
15   C CB  . PHE A 3   ? 0.2813 0.3797 0.3804 -0.0446 -0.0754 0.1430  3   PHE A CB  
16   C CG  . PHE A 3   ? 0.3459 0.4381 0.4320 -0.0440 -0.0680 0.1342  3   PHE A CG  
17   C CD1 . PHE A 3   ? 0.3251 0.4223 0.3873 -0.0481 -0.0654 0.1321  3   PHE A CD1 
18   C CD2 . PHE A 3   ? 0.3754 0.4570 0.4731 -0.0393 -0.0635 0.1275  3   PHE A CD2 
19   C CE1 . PHE A 3   ? 0.3686 0.4612 0.4206 -0.0466 -0.0580 0.1247  3   PHE A CE1 
20   C CE2 . PHE A 3   ? 0.2608 0.3383 0.3482 -0.0388 -0.0571 0.1204  3   PHE A CE2 
21   C CZ  . PHE A 3   ? 0.3388 0.4224 0.4045 -0.0420 -0.0540 0.1194  3   PHE A CZ  
22   N N   . ARG A 4   ? 0.2690 0.3520 0.3600 -0.0393 -0.0691 0.1114  4   ARG A N   
23   C CA  . ARG A 4   ? 0.2533 0.3290 0.3519 -0.0346 -0.0661 0.1014  4   ARG A CA  
24   C C   . ARG A 4   ? 0.2371 0.3026 0.3282 -0.0319 -0.0590 0.0903  4   ARG A C   
25   O O   . ARG A 4   ? 0.2733 0.3384 0.3481 -0.0345 -0.0562 0.0880  4   ARG A O   
26   C CB  . ARG A 4   ? 0.2455 0.3251 0.3349 -0.0381 -0.0685 0.0972  4   ARG A CB  
27   C CG  . ARG A 4   ? 0.2497 0.3398 0.3535 -0.0391 -0.0753 0.1069  4   ARG A CG  
28   C CD  . ARG A 4   ? 0.3437 0.4306 0.4689 -0.0317 -0.0730 0.1050  4   ARG A CD  
29   N NE  . ARG A 4   ? 0.4321 0.5300 0.5733 -0.0316 -0.0787 0.1147  4   ARG A NE  
30   C CZ  . ARG A 4   ? 0.3809 0.4789 0.5436 -0.0245 -0.0771 0.1163  4   ARG A CZ  
31   N NH1 . ARG A 4   ? 0.4259 0.5125 0.5948 -0.0174 -0.0705 0.1078  4   ARG A NH1 
32   N NH2 . ARG A 4   ? 0.3036 0.4137 0.4816 -0.0243 -0.0823 0.1268  4   ARG A NH2 
33   N N   . LYS A 5   ? 0.2155 0.2733 0.3182 -0.0263 -0.0558 0.0837  5   LYS A N   
34   C CA  . LYS A 5   ? 0.2404 0.2899 0.3348 -0.0241 -0.0498 0.0725  5   LYS A CA  
35   C C   . LYS A 5   ? 0.2862 0.3358 0.3649 -0.0265 -0.0483 0.0649  5   LYS A C   
36   O O   . LYS A 5   ? 0.4646 0.5154 0.5475 -0.0258 -0.0495 0.0626  5   LYS A O   
37   C CB  . LYS A 5   ? 0.3445 0.3863 0.4534 -0.0181 -0.0475 0.0671  5   LYS A CB  
38   C CG  . LYS A 5   ? 0.3728 0.4073 0.4788 -0.0166 -0.0434 0.0614  5   LYS A CG  
39   C CD  . LYS A 5   ? 0.6265 0.6529 0.7457 -0.0113 -0.0422 0.0561  5   LYS A CD  
40   C CE  . LYS A 5   ? 0.5833 0.6063 0.7167 -0.0109 -0.0450 0.0631  5   LYS A CE  
41   N NZ  . LYS A 5   ? 0.4388 0.4602 0.5675 -0.0136 -0.0436 0.0634  5   LYS A NZ  
42   N N   . MET A 6   ? 0.2693 0.3178 0.3303 -0.0292 -0.0456 0.0616  6   MET A N   
43   C CA  . MET A 6   ? 0.2756 0.3230 0.3198 -0.0326 -0.0451 0.0555  6   MET A CA  
44   C C   . MET A 6   ? 0.2639 0.3031 0.2988 -0.0298 -0.0385 0.0456  6   MET A C   
45   O O   . MET A 6   ? 0.2968 0.3346 0.3286 -0.0282 -0.0347 0.0455  6   MET A O   
46   C CB  . MET A 6   ? 0.2815 0.3344 0.3101 -0.0383 -0.0479 0.0602  6   MET A CB  
47   C CG  . MET A 6   ? 0.4980 0.5524 0.5153 -0.0437 -0.0520 0.0579  6   MET A CG  
48   S SD  . MET A 6   ? 0.5759 0.6394 0.5789 -0.0506 -0.0575 0.0664  6   MET A SD  
49   C CE  . MET A 6   ? 0.2881 0.3459 0.2748 -0.0480 -0.0490 0.0609  6   MET A CE  
50   N N   . ALA A 7   ? 0.2592 0.2940 0.2911 -0.0294 -0.0372 0.0385  7   ALA A N   
51   C CA  . ALA A 7   ? 0.2551 0.2821 0.2782 -0.0269 -0.0313 0.0298  7   ALA A CA  
52   C C   . ALA A 7   ? 0.3671 0.3906 0.3705 -0.0307 -0.0304 0.0257  7   ALA A C   
53   O O   . ALA A 7   ? 0.3045 0.3308 0.3013 -0.0360 -0.0352 0.0279  7   ALA A O   
54   C CB  . ALA A 7   ? 0.2234 0.2474 0.2547 -0.0241 -0.0302 0.0249  7   ALA A CB  
55   N N   . PHE A 8   ? 0.2896 0.3067 0.2836 -0.0280 -0.0245 0.0197  8   PHE A N   
56   C CA  . PHE A 8   ? 0.3162 0.3266 0.2915 -0.0305 -0.0227 0.0140  8   PHE A CA  
57   C C   . PHE A 8   ? 0.3366 0.3423 0.3114 -0.0334 -0.0254 0.0099  8   PHE A C   
58   O O   . PHE A 8   ? 0.3183 0.3248 0.3062 -0.0312 -0.0255 0.0098  8   PHE A O   
59   C CB  . PHE A 8   ? 0.3175 0.3217 0.2855 -0.0257 -0.0150 0.0088  8   PHE A CB  
60   C CG  . PHE A 8   ? 0.3898 0.3996 0.3564 -0.0235 -0.0118 0.0130  8   PHE A CG  
61   C CD1 . PHE A 8   ? 0.4249 0.4362 0.3760 -0.0259 -0.0108 0.0140  8   PHE A CD1 
62   C CD2 . PHE A 8   ? 0.4105 0.4246 0.3914 -0.0195 -0.0099 0.0165  8   PHE A CD2 
63   C CE1 . PHE A 8   ? 0.3684 0.3867 0.3190 -0.0238 -0.0072 0.0192  8   PHE A CE1 
64   C CE2 . PHE A 8   ? 0.3603 0.3806 0.3417 -0.0183 -0.0072 0.0217  8   PHE A CE2 
65   C CZ  . PHE A 8   ? 0.4234 0.4465 0.3902 -0.0202 -0.0054 0.0236  8   PHE A CZ  
66   N N   . PRO A 9   ? 0.3457 0.3464 0.3053 -0.0387 -0.0276 0.0065  9   PRO A N   
67   C CA  . PRO A 9   ? 0.3643 0.3593 0.3234 -0.0422 -0.0300 0.0026  9   PRO A CA  
68   C C   . PRO A 9   ? 0.3100 0.2967 0.2711 -0.0368 -0.0237 -0.0029 9   PRO A C   
69   O O   . PRO A 9   ? 0.4090 0.3893 0.3615 -0.0328 -0.0177 -0.0069 9   PRO A O   
70   C CB  . PRO A 9   ? 0.2966 0.2851 0.2356 -0.0488 -0.0329 -0.0014 9   PRO A CB  
71   C CG  . PRO A 9   ? 0.3988 0.3942 0.3300 -0.0497 -0.0340 0.0028  9   PRO A CG  
72   C CD  . PRO A 9   ? 0.3802 0.3800 0.3215 -0.0420 -0.0280 0.0058  9   PRO A CD  
73   N N   . SER A 10  ? 0.3401 0.3280 0.3131 -0.0366 -0.0247 -0.0023 10  SER A N   
74   C CA  . SER A 10  ? 0.3268 0.3103 0.3048 -0.0310 -0.0191 -0.0054 10  SER A CA  
75   C C   . SER A 10  ? 0.3270 0.2989 0.2963 -0.0328 -0.0174 -0.0106 10  SER A C   
76   O O   . SER A 10  ? 0.3207 0.2883 0.2925 -0.0280 -0.0126 -0.0127 10  SER A O   
77   C CB  . SER A 10  ? 0.3299 0.3217 0.3254 -0.0285 -0.0200 -0.0017 10  SER A CB  
78   O OG  . SER A 10  ? 0.3507 0.3471 0.3522 -0.0335 -0.0249 0.0012  10  SER A OG  
79   N N   . GLY A 11  ? 0.3984 0.3647 0.3575 -0.0398 -0.0216 -0.0126 11  GLY A N   
80   C CA  . GLY A 11  ? 0.4510 0.4053 0.4041 -0.0427 -0.0212 -0.0169 11  GLY A CA  
81   C C   . GLY A 11  ? 0.3467 0.2892 0.2923 -0.0366 -0.0138 -0.0222 11  GLY A C   
82   O O   . GLY A 11  ? 0.3789 0.3146 0.3276 -0.0355 -0.0116 -0.0233 11  GLY A O   
83   N N   . LYS A 12  ? 0.3513 0.2918 0.2875 -0.0326 -0.0098 -0.0246 12  LYS A N   
84   C CA  . LYS A 12  ? 0.3531 0.2830 0.2827 -0.0262 -0.0024 -0.0291 12  LYS A CA  
85   C C   . LYS A 12  ? 0.3576 0.2929 0.3014 -0.0196 0.0016  -0.0259 12  LYS A C   
86   O O   . LYS A 12  ? 0.3216 0.2484 0.2643 -0.0153 0.0064  -0.0280 12  LYS A O   
87   C CB  . LYS A 12  ? 0.3669 0.2969 0.2851 -0.0230 0.0016  -0.0311 12  LYS A CB  
88   C CG  . LYS A 12  ? 0.4419 0.3587 0.3399 -0.0269 0.0013  -0.0380 12  LYS A CG  
89   C CD  . LYS A 12  ? 0.5288 0.4502 0.4153 -0.0253 0.0038  -0.0384 12  LYS A CD  
90   C CE  . LYS A 12  ? 0.6575 0.5631 0.5211 -0.0264 0.0065  -0.0474 12  LYS A CE  
91   N NZ  . LYS A 12  ? 0.6765 0.5861 0.5288 -0.0216 0.0126  -0.0481 12  LYS A NZ  
92   N N   . VAL A 13  ? 0.3410 0.2897 0.2978 -0.0188 -0.0006 -0.0207 13  VAL A N   
93   C CA  . VAL A 13  ? 0.2916 0.2456 0.2602 -0.0134 0.0021  -0.0183 13  VAL A CA  
94   C C   . VAL A 13  ? 0.3576 0.3124 0.3340 -0.0158 -0.0001 -0.0166 13  VAL A C   
95   O O   . VAL A 13  ? 0.3099 0.2641 0.2910 -0.0120 0.0030  -0.0159 13  VAL A O   
96   C CB  . VAL A 13  ? 0.3064 0.2727 0.2842 -0.0109 0.0013  -0.0146 13  VAL A CB  
97   C CG1 . VAL A 13  ? 0.3695 0.3410 0.3578 -0.0060 0.0034  -0.0130 13  VAL A CG1 
98   C CG2 . VAL A 13  ? 0.3284 0.2949 0.2991 -0.0089 0.0039  -0.0149 13  VAL A CG2 
99   N N   . GLU A 14  ? 0.3288 0.2862 0.3070 -0.0221 -0.0053 -0.0152 14  GLU A N   
100  C CA  . GLU A 14  ? 0.2890 0.2484 0.2751 -0.0248 -0.0070 -0.0127 14  GLU A CA  
101  C C   . GLU A 14  ? 0.2536 0.2009 0.2347 -0.0247 -0.0041 -0.0147 14  GLU A C   
102  O O   . GLU A 14  ? 0.3154 0.2651 0.3038 -0.0230 -0.0024 -0.0120 14  GLU A O   
103  C CB  . GLU A 14  ? 0.2974 0.2607 0.2852 -0.0325 -0.0134 -0.0105 14  GLU A CB  
104  C CG  . GLU A 14  ? 0.2823 0.2590 0.2789 -0.0321 -0.0164 -0.0067 14  GLU A CG  
105  C CD  . GLU A 14  ? 0.3327 0.3132 0.3295 -0.0401 -0.0233 -0.0040 14  GLU A CD  
106  O OE1 . GLU A 14  ? 0.4182 0.3980 0.4176 -0.0455 -0.0261 -0.0024 14  GLU A OE1 
107  O OE2 . GLU A 14  ? 0.3439 0.3288 0.3385 -0.0414 -0.0263 -0.0026 14  GLU A OE2 
108  N N   . GLY A 15  ? 0.3280 0.2617 0.2963 -0.0263 -0.0034 -0.0194 15  GLY A N   
109  C CA  . GLY A 15  ? 0.3083 0.2276 0.2718 -0.0262 -0.0008 -0.0216 15  GLY A CA  
110  C C   . GLY A 15  ? 0.3435 0.2614 0.3099 -0.0177 0.0056  -0.0208 15  GLY A C   
111  O O   . GLY A 15  ? 0.3606 0.2672 0.3252 -0.0166 0.0081  -0.0213 15  GLY A O   
112  N N   . CYS A 16  ? 0.3023 0.2315 0.2738 -0.0121 0.0077  -0.0191 16  CYS A N   
113  C CA  . CYS A 16  ? 0.2514 0.1819 0.2265 -0.0045 0.0128  -0.0175 16  CYS A CA  
114  C C   . CYS A 16  ? 0.2919 0.2349 0.2783 -0.0027 0.0122  -0.0128 16  CYS A C   
115  O O   . CYS A 16  ? 0.2954 0.2411 0.2851 0.0028  0.0154  -0.0107 16  CYS A O   
116  C CB  . CYS A 16  ? 0.3196 0.2540 0.2921 0.0003  0.0155  -0.0189 16  CYS A CB  
117  S SG  . CYS A 16  ? 0.3517 0.2730 0.3087 -0.0002 0.0179  -0.0248 16  CYS A SG  
118  N N   . MET A 17  ? 0.2582 0.2094 0.2502 -0.0067 0.0085  -0.0109 17  MET A N   
119  C CA  . MET A 17  ? 0.2545 0.2178 0.2553 -0.0040 0.0087  -0.0077 17  MET A CA  
120  C C   . MET A 17  ? 0.3005 0.2627 0.3043 -0.0046 0.0100  -0.0042 17  MET A C   
121  O O   . MET A 17  ? 0.2955 0.2516 0.2985 -0.0097 0.0085  -0.0032 17  MET A O   
122  C CB  . MET A 17  ? 0.2829 0.2562 0.2895 -0.0065 0.0053  -0.0072 17  MET A CB  
123  C CG  . MET A 17  ? 0.2774 0.2513 0.2814 -0.0062 0.0039  -0.0095 17  MET A CG  
124  S SD  . MET A 17  ? 0.2822 0.2598 0.2873 0.0001  0.0065  -0.0101 17  MET A SD  
125  C CE  . MET A 17  ? 0.2965 0.2830 0.3091 0.0034  0.0072  -0.0084 17  MET A CE  
126  N N   . VAL A 18  ? 0.2704 0.2385 0.2772 0.0003  0.0125  -0.0017 18  VAL A N   
127  C CA  . VAL A 18  ? 0.2362 0.2057 0.2459 0.0004  0.0140  0.0030  18  VAL A CA  
128  C C   . VAL A 18  ? 0.2693 0.2529 0.2833 0.0036  0.0146  0.0048  18  VAL A C   
129  O O   . VAL A 18  ? 0.2631 0.2527 0.2776 0.0061  0.0137  0.0018  18  VAL A O   
130  C CB  . VAL A 18  ? 0.2305 0.1905 0.2374 0.0036  0.0169  0.0049  18  VAL A CB  
131  C CG1 . VAL A 18  ? 0.2902 0.2338 0.2910 0.0011  0.0170  0.0014  18  VAL A CG1 
132  C CG2 . VAL A 18  ? 0.2607 0.2261 0.2677 0.0099  0.0186  0.0048  18  VAL A CG2 
133  N N   . GLN A 19  ? 0.2436 0.2319 0.2602 0.0033  0.0160  0.0097  19  GLN A N   
134  C CA  . GLN A 19  ? 0.2624 0.2635 0.2805 0.0065  0.0172  0.0115  19  GLN A CA  
135  C C   . GLN A 19  ? 0.2534 0.2546 0.2689 0.0105  0.0188  0.0147  19  GLN A C   
136  O O   . GLN A 19  ? 0.3126 0.3067 0.3281 0.0100  0.0201  0.0192  19  GLN A O   
137  C CB  . GLN A 19  ? 0.3407 0.3494 0.3631 0.0038  0.0183  0.0159  19  GLN A CB  
138  C CG  . GLN A 19  ? 0.3420 0.3646 0.3645 0.0074  0.0204  0.0167  19  GLN A CG  
139  C CD  . GLN A 19  ? 0.4720 0.5034 0.4996 0.0051  0.0225  0.0221  19  GLN A CD  
140  O OE1 . GLN A 19  ? 0.5974 0.6399 0.6268 0.0073  0.0244  0.0210  19  GLN A OE1 
141  N NE2 . GLN A 19  ? 0.5991 0.6254 0.6296 0.0006  0.0226  0.0282  19  GLN A NE2 
142  N N   . VAL A 20  ? 0.2270 0.2359 0.2408 0.0143  0.0184  0.0128  20  VAL A N   
143  C CA  . VAL A 20  ? 0.2627 0.2748 0.2746 0.0178  0.0190  0.0169  20  VAL A CA  
144  C C   . VAL A 20  ? 0.2572 0.2823 0.2668 0.0192  0.0193  0.0181  20  VAL A C   
145  O O   . VAL A 20  ? 0.2535 0.2844 0.2618 0.0197  0.0183  0.0127  20  VAL A O   
146  C CB  . VAL A 20  ? 0.2242 0.2347 0.2357 0.0207  0.0176  0.0144  20  VAL A CB  
147  C CG1 . VAL A 20  ? 0.2025 0.2177 0.2136 0.0241  0.0179  0.0203  20  VAL A CG1 
148  C CG2 . VAL A 20  ? 0.2838 0.2821 0.2960 0.0201  0.0184  0.0125  20  VAL A CG2 
149  N N   . THR A 21  ? 0.2884 0.3175 0.2971 0.0199  0.0210  0.0253  21  THR A N   
150  C CA  . THR A 21  ? 0.2672 0.3093 0.2715 0.0213  0.0218  0.0275  21  THR A CA  
151  C C   . THR A 21  ? 0.3219 0.3687 0.3231 0.0240  0.0206  0.0327  21  THR A C   
152  O O   . THR A 21  ? 0.3260 0.3674 0.3304 0.0245  0.0213  0.0396  21  THR A O   
153  C CB  . THR A 21  ? 0.3521 0.3980 0.3586 0.0189  0.0251  0.0335  21  THR A CB  
154  O OG1 . THR A 21  ? 0.3679 0.4122 0.3784 0.0164  0.0256  0.0293  21  THR A OG1 
155  C CG2 . THR A 21  ? 0.3968 0.4572 0.3975 0.0209  0.0269  0.0367  21  THR A CG2 
156  N N   . CYS A 22  ? 0.3150 0.3715 0.3101 0.0257  0.0186  0.0294  22  CYS A N   
157  C CA  . CYS A 22  ? 0.3856 0.4504 0.3765 0.0276  0.0166  0.0348  22  CYS A CA  
158  C C   . CYS A 22  ? 0.3935 0.4711 0.3751 0.0280  0.0172  0.0340  22  CYS A C   
159  O O   . CYS A 22  ? 0.3928 0.4732 0.3690 0.0282  0.0158  0.0251  22  CYS A O   
160  C CB  . CYS A 22  ? 0.3354 0.3996 0.3271 0.0287  0.0122  0.0313  22  CYS A CB  
161  S SG  . CYS A 22  ? 0.4443 0.5174 0.4354 0.0308  0.0094  0.0413  22  CYS A SG  
162  N N   . GLY A 23  ? 0.4470 0.5318 0.4263 0.0282  0.0195  0.0433  23  GLY A N   
163  C CA  . GLY A 23  ? 0.3906 0.4885 0.3596 0.0289  0.0211  0.0430  23  GLY A CA  
164  C C   . GLY A 23  ? 0.3282 0.4259 0.2973 0.0287  0.0251  0.0361  23  GLY A C   
165  O O   . GLY A 23  ? 0.4655 0.5588 0.4427 0.0270  0.0284  0.0395  23  GLY A O   
166  N N   . THR A 24  ? 0.4546 0.5564 0.4154 0.0302  0.0245  0.0262  24  THR A N   
167  C CA  . THR A 24  ? 0.5366 0.6389 0.4982 0.0312  0.0285  0.0194  24  THR A CA  
168  C C   . THR A 24  ? 0.5620 0.6524 0.5316 0.0305  0.0264  0.0113  24  THR A C   
169  O O   . THR A 24  ? 0.4719 0.5620 0.4450 0.0313  0.0296  0.0070  24  THR A O   
170  C CB  . THR A 24  ? 0.5928 0.7044 0.5405 0.0342  0.0299  0.0123  24  THR A CB  
171  O OG1 . THR A 24  ? 0.7242 0.8369 0.6741 0.0364  0.0351  0.0066  24  THR A OG1 
172  C CG2 . THR A 24  ? 0.5780 0.6851 0.5192 0.0341  0.0235  0.0030  24  THR A CG2 
173  N N   . THR A 25  ? 0.4907 0.5726 0.4639 0.0291  0.0216  0.0102  25  THR A N   
174  C CA  . THR A 25  ? 0.4767 0.5487 0.4562 0.0283  0.0193  0.0029  25  THR A CA  
175  C C   . THR A 25  ? 0.3311 0.3949 0.3209 0.0260  0.0205  0.0072  25  THR A C   
176  O O   . THR A 25  ? 0.4086 0.4702 0.4010 0.0249  0.0209  0.0148  25  THR A O   
177  C CB  . THR A 25  ? 0.4721 0.5408 0.4500 0.0278  0.0136  -0.0008 25  THR A CB  
178  O OG1 . THR A 25  ? 0.5266 0.6019 0.4938 0.0289  0.0114  -0.0058 25  THR A OG1 
179  C CG2 . THR A 25  ? 0.4747 0.5339 0.4595 0.0268  0.0114  -0.0070 25  THR A CG2 
180  N N   . THR A 26  ? 0.3910 0.4501 0.3863 0.0253  0.0209  0.0023  26  THR A N   
181  C CA  . THR A 26  ? 0.3310 0.3818 0.3344 0.0224  0.0210  0.0050  26  THR A CA  
182  C C   . THR A 26  ? 0.3543 0.3983 0.3613 0.0219  0.0182  -0.0016 26  THR A C   
183  O O   . THR A 26  ? 0.4320 0.4783 0.4398 0.0233  0.0183  -0.0070 26  THR A O   
184  C CB  . THR A 26  ? 0.4813 0.5361 0.4894 0.0209  0.0246  0.0094  26  THR A CB  
185  O OG1 . THR A 26  ? 0.4276 0.4876 0.4335 0.0205  0.0270  0.0174  26  THR A OG1 
186  C CG2 . THR A 26  ? 0.4055 0.4515 0.4210 0.0169  0.0234  0.0106  26  THR A CG2 
187  N N   . LEU A 27  ? 0.2566 0.2923 0.2660 0.0202  0.0160  -0.0008 27  LEU A N   
188  C CA  . LEU A 27  ? 0.3061 0.3361 0.3192 0.0192  0.0135  -0.0055 27  LEU A CA  
189  C C   . LEU A 27  ? 0.2418 0.2632 0.2572 0.0166  0.0134  -0.0027 27  LEU A C   
190  O O   . LEU A 27  ? 0.2488 0.2678 0.2641 0.0152  0.0152  0.0019  27  LEU A O   
191  C CB  . LEU A 27  ? 0.2993 0.3298 0.3103 0.0207  0.0104  -0.0097 27  LEU A CB  
192  C CG  . LEU A 27  ? 0.3005 0.3330 0.3081 0.0217  0.0092  -0.0066 27  LEU A CG  
193  C CD1 . LEU A 27  ? 0.2912 0.3175 0.3015 0.0212  0.0102  -0.0020 27  LEU A CD1 
194  C CD2 . LEU A 27  ? 0.2938 0.3280 0.3009 0.0220  0.0052  -0.0108 27  LEU A CD2 
195  N N   . ASN A 28  ? 0.2032 0.2196 0.2205 0.0157  0.0113  -0.0056 28  ASN A N   
196  C CA  . ASN A 28  ? 0.2351 0.2432 0.2527 0.0131  0.0113  -0.0045 28  ASN A CA  
197  C C   . ASN A 28  ? 0.2359 0.2392 0.2512 0.0148  0.0118  -0.0034 28  ASN A C   
198  O O   . ASN A 28  ? 0.2609 0.2680 0.2766 0.0170  0.0107  -0.0041 28  ASN A O   
199  C CB  . ASN A 28  ? 0.2532 0.2596 0.2737 0.0111  0.0090  -0.0074 28  ASN A CB  
200  C CG  . ASN A 28  ? 0.3132 0.3251 0.3382 0.0103  0.0087  -0.0080 28  ASN A CG  
201  O OD1 . ASN A 28  ? 0.2637 0.2760 0.2904 0.0077  0.0093  -0.0054 28  ASN A OD1 
202  N ND2 . ASN A 28  ? 0.2466 0.2626 0.2741 0.0126  0.0077  -0.0112 28  ASN A ND2 
203  N N   . GLY A 29  ? 0.2115 0.2064 0.2247 0.0136  0.0134  -0.0016 29  GLY A N   
204  C CA  . GLY A 29  ? 0.2194 0.2088 0.2308 0.0161  0.0150  -0.0008 29  GLY A CA  
205  C C   . GLY A 29  ? 0.2751 0.2550 0.2831 0.0139  0.0155  -0.0033 29  GLY A C   
206  O O   . GLY A 29  ? 0.2574 0.2342 0.2643 0.0097  0.0141  -0.0046 29  GLY A O   
207  N N   . LEU A 30  ? 0.2519 0.2283 0.2583 0.0168  0.0176  -0.0035 30  LEU A N   
208  C CA  . LEU A 30  ? 0.2825 0.2502 0.2834 0.0158  0.0189  -0.0063 30  LEU A CA  
209  C C   . LEU A 30  ? 0.2327 0.1899 0.2301 0.0191  0.0232  -0.0055 30  LEU A C   
210  O O   . LEU A 30  ? 0.2515 0.2113 0.2519 0.0244  0.0259  -0.0028 30  LEU A O   
211  C CB  . LEU A 30  ? 0.2336 0.2070 0.2358 0.0173  0.0188  -0.0070 30  LEU A CB  
212  C CG  . LEU A 30  ? 0.2636 0.2305 0.2589 0.0158  0.0200  -0.0099 30  LEU A CG  
213  C CD1 . LEU A 30  ? 0.3072 0.2729 0.2999 0.0097  0.0160  -0.0120 30  LEU A CD1 
214  C CD2 . LEU A 30  ? 0.2704 0.2441 0.2680 0.0184  0.0214  -0.0086 30  LEU A CD2 
215  N N   . TRP A 31  ? 0.2526 0.1978 0.2444 0.0159  0.0234  -0.0076 31  TRP A N   
216  C CA  . TRP A 31  ? 0.2329 0.1647 0.2212 0.0184  0.0271  -0.0076 31  TRP A CA  
217  C C   . TRP A 31  ? 0.3123 0.2332 0.2913 0.0193  0.0299  -0.0129 31  TRP A C   
218  O O   . TRP A 31  ? 0.3100 0.2238 0.2816 0.0137  0.0276  -0.0173 31  TRP A O   
219  C CB  . TRP A 31  ? 0.2511 0.1755 0.2392 0.0133  0.0250  -0.0065 31  TRP A CB  
220  C CG  . TRP A 31  ? 0.2941 0.2027 0.2796 0.0147  0.0280  -0.0061 31  TRP A CG  
221  C CD1 . TRP A 31  ? 0.2628 0.1652 0.2489 0.0219  0.0329  -0.0046 31  TRP A CD1 
222  C CD2 . TRP A 31  ? 0.2796 0.1758 0.2627 0.0087  0.0260  -0.0065 31  TRP A CD2 
223  N NE1 . TRP A 31  ? 0.2961 0.1814 0.2799 0.0212  0.0344  -0.0046 31  TRP A NE1 
224  C CE2 . TRP A 31  ? 0.3299 0.2108 0.3117 0.0126  0.0299  -0.0059 31  TRP A CE2 
225  C CE3 . TRP A 31  ? 0.2965 0.1934 0.2796 0.0002  0.0211  -0.0069 31  TRP A CE3 
226  C CZ2 . TRP A 31  ? 0.3269 0.1915 0.3067 0.0077  0.0287  -0.0061 31  TRP A CZ2 
227  C CZ3 . TRP A 31  ? 0.3244 0.2072 0.3061 -0.0052 0.0196  -0.0066 31  TRP A CZ3 
228  C CH2 . TRP A 31  ? 0.3483 0.2141 0.3280 -0.0017 0.0233  -0.0064 31  TRP A CH2 
229  N N   . LEU A 32  ? 0.2810 0.2014 0.2604 0.0264  0.0350  -0.0122 32  LEU A N   
230  C CA  . LEU A 32  ? 0.3066 0.2182 0.2769 0.0291  0.0394  -0.0171 32  LEU A CA  
231  C C   . LEU A 32  ? 0.3218 0.2221 0.2920 0.0364  0.0458  -0.0165 32  LEU A C   
232  O O   . LEU A 32  ? 0.3357 0.2440 0.3155 0.0424  0.0481  -0.0105 32  LEU A O   
233  C CB  . LEU A 32  ? 0.3134 0.2387 0.2860 0.0316  0.0405  -0.0159 32  LEU A CB  
234  C CG  . LEU A 32  ? 0.3262 0.2622 0.3002 0.0253  0.0347  -0.0159 32  LEU A CG  
235  C CD1 . LEU A 32  ? 0.3043 0.2542 0.2843 0.0285  0.0359  -0.0127 32  LEU A CD1 
236  C CD2 . LEU A 32  ? 0.3024 0.2303 0.2648 0.0194  0.0325  -0.0213 32  LEU A CD2 
237  N N   . ASP A 33  ? 0.2931 0.1745 0.2523 0.0360  0.0483  -0.0226 33  ASP A N   
238  C CA  . ASP A 33  ? 0.3346 0.2012 0.2937 0.0428  0.0542  -0.0226 33  ASP A CA  
239  C C   . ASP A 33  ? 0.3416 0.2107 0.3120 0.0425  0.0516  -0.0151 33  ASP A C   
240  O O   . ASP A 33  ? 0.3472 0.2174 0.3186 0.0347  0.0458  -0.0142 33  ASP A O   
241  C CB  . ASP A 33  ? 0.3591 0.2309 0.3204 0.0529  0.0618  -0.0213 33  ASP A CB  
242  C CG  . ASP A 33  ? 0.5010 0.3716 0.4500 0.0530  0.0647  -0.0281 33  ASP A CG  
243  O OD1 . ASP A 33  ? 0.5399 0.3957 0.4749 0.0477  0.0633  -0.0360 33  ASP A OD1 
244  O OD2 . ASP A 33  ? 0.5317 0.4171 0.4853 0.0578  0.0681  -0.0249 33  ASP A OD2 
245  N N   . ASP A 34  ? 0.3110 0.1830 0.2907 0.0507  0.0558  -0.0088 34  ASP A N   
246  C CA  . ASP A 34  ? 0.2913 0.1662 0.2809 0.0506  0.0536  -0.0007 34  ASP A CA  
247  C C   . ASP A 34  ? 0.2765 0.1748 0.2765 0.0518  0.0508  0.0068  34  ASP A C   
248  O O   . ASP A 34  ? 0.3256 0.2293 0.3342 0.0550  0.0507  0.0148  34  ASP A O   
249  C CB  . ASP A 34  ? 0.3343 0.1947 0.3274 0.0586  0.0595  0.0022  34  ASP A CB  
250  C CG  . ASP A 34  ? 0.3795 0.2471 0.3779 0.0693  0.0660  0.0048  34  ASP A CG  
251  O OD1 . ASP A 34  ? 0.4296 0.3119 0.4279 0.0699  0.0661  0.0037  34  ASP A OD1 
252  O OD2 . ASP A 34  ? 0.4216 0.2799 0.4253 0.0773  0.0713  0.0085  34  ASP A OD2 
253  N N   . VAL A 35  ? 0.2952 0.2072 0.2941 0.0488  0.0480  0.0045  35  VAL A N   
254  C CA  . VAL A 35  ? 0.3171 0.2495 0.3244 0.0487  0.0445  0.0100  35  VAL A CA  
255  C C   . VAL A 35  ? 0.2761 0.2154 0.2807 0.0407  0.0386  0.0070  35  VAL A C   
256  O O   . VAL A 35  ? 0.2946 0.2288 0.2923 0.0364  0.0376  0.0009  35  VAL A O   
257  C CB  . VAL A 35  ? 0.3066 0.2504 0.3184 0.0541  0.0471  0.0115  35  VAL A CB  
258  C CG1 . VAL A 35  ? 0.3075 0.2709 0.3274 0.0526  0.0421  0.0166  35  VAL A CG1 
259  C CG2 . VAL A 35  ? 0.2914 0.2297 0.3076 0.0633  0.0538  0.0153  35  VAL A CG2 
260  N N   . VAL A 36  ? 0.2435 0.1948 0.2535 0.0389  0.0347  0.0114  36  VAL A N   
261  C CA  . VAL A 36  ? 0.2156 0.1756 0.2247 0.0330  0.0298  0.0091  36  VAL A CA  
262  C C   . VAL A 36  ? 0.2508 0.2265 0.2651 0.0345  0.0275  0.0108  36  VAL A C   
263  O O   . VAL A 36  ? 0.2693 0.2530 0.2886 0.0379  0.0273  0.0162  36  VAL A O   
264  C CB  . VAL A 36  ? 0.2460 0.2066 0.2558 0.0295  0.0277  0.0120  36  VAL A CB  
265  C CG1 . VAL A 36  ? 0.2459 0.2166 0.2557 0.0250  0.0237  0.0095  36  VAL A CG1 
266  C CG2 . VAL A 36  ? 0.3167 0.2612 0.3224 0.0265  0.0291  0.0105  36  VAL A CG2 
267  N N   . TYR A 37  ? 0.2402 0.2200 0.2533 0.0315  0.0252  0.0066  37  TYR A N   
268  C CA  . TYR A 37  ? 0.2650 0.2575 0.2830 0.0316  0.0222  0.0073  37  TYR A CA  
269  C C   . TYR A 37  ? 0.2244 0.2226 0.2422 0.0273  0.0177  0.0050  37  TYR A C   
270  O O   . TYR A 37  ? 0.2549 0.2486 0.2696 0.0238  0.0169  0.0016  37  TYR A O   
271  C CB  . TYR A 37  ? 0.2305 0.2233 0.2486 0.0315  0.0231  0.0051  37  TYR A CB  
272  C CG  . TYR A 37  ? 0.2429 0.2301 0.2600 0.0363  0.0287  0.0063  37  TYR A CG  
273  C CD1 . TYR A 37  ? 0.2468 0.2202 0.2561 0.0363  0.0322  0.0028  37  TYR A CD1 
274  C CD2 . TYR A 37  ? 0.2577 0.2536 0.2818 0.0409  0.0306  0.0110  37  TYR A CD2 
275  C CE1 . TYR A 37  ? 0.2999 0.2667 0.3070 0.0416  0.0382  0.0028  37  TYR A CE1 
276  C CE2 . TYR A 37  ? 0.2925 0.2838 0.3163 0.0467  0.0370  0.0123  37  TYR A CE2 
277  C CZ  . TYR A 37  ? 0.3007 0.2768 0.3153 0.0474  0.0412  0.0077  37  TYR A CZ  
278  O OH  . TYR A 37  ? 0.3191 0.2892 0.3320 0.0538  0.0483  0.0078  37  TYR A OH  
279  N N   . CYS A 38  ? 0.2418 0.2501 0.2627 0.0278  0.0147  0.0067  38  CYS A N   
280  C CA  . CYS A 38  ? 0.2210 0.2340 0.2407 0.0248  0.0111  0.0035  38  CYS A CA  
281  C C   . CYS A 38  ? 0.2354 0.2582 0.2579 0.0249  0.0072  0.0038  38  CYS A C   
282  O O   . CYS A 38  ? 0.2070 0.2346 0.2330 0.0271  0.0070  0.0081  38  CYS A O   
283  C CB  . CYS A 38  ? 0.1961 0.2085 0.2125 0.0244  0.0122  0.0050  38  CYS A CB  
284  S SG  . CYS A 38  ? 0.2632 0.2836 0.2793 0.0273  0.0119  0.0113  38  CYS A SG  
285  N N   . PRO A 39  ? 0.1970 0.2227 0.2185 0.0225  0.0038  -0.0007 39  PRO A N   
286  C CA  . PRO A 39  ? 0.1607 0.1939 0.1836 0.0217  -0.0009 -0.0015 39  PRO A CA  
287  C C   . PRO A 39  ? 0.1975 0.2377 0.2174 0.0232  -0.0018 0.0022  39  PRO A C   
288  O O   . PRO A 39  ? 0.1987 0.2387 0.2139 0.0243  0.0005  0.0033  39  PRO A O   
289  C CB  . PRO A 39  ? 0.1852 0.2167 0.2062 0.0194  -0.0033 -0.0083 39  PRO A CB  
290  C CG  . PRO A 39  ? 0.2153 0.2400 0.2364 0.0191  0.0000  -0.0097 39  PRO A CG  
291  C CD  . PRO A 39  ? 0.1849 0.2068 0.2043 0.0206  0.0041  -0.0052 39  PRO A CD  
292  N N   . ARG A 40  ? 0.2134 0.2611 0.2368 0.0231  -0.0054 0.0052  40  ARG A N   
293  C CA  . ARG A 40  ? 0.2082 0.2641 0.2292 0.0244  -0.0071 0.0101  40  ARG A CA  
294  C C   . ARG A 40  ? 0.2174 0.2768 0.2294 0.0227  -0.0099 0.0055  40  ARG A C   
295  O O   . ARG A 40  ? 0.2385 0.3039 0.2459 0.0239  -0.0099 0.0097  40  ARG A O   
296  C CB  . ARG A 40  ? 0.2606 0.3253 0.2889 0.0242  -0.0110 0.0151  40  ARG A CB  
297  C CG  . ARG A 40  ? 0.2337 0.3025 0.2629 0.0196  -0.0179 0.0106  40  ARG A CG  
298  C CD  . ARG A 40  ? 0.2019 0.2822 0.2388 0.0188  -0.0225 0.0175  40  ARG A CD  
299  N NE  . ARG A 40  ? 0.1967 0.2794 0.2359 0.0133  -0.0296 0.0133  40  ARG A NE  
300  C CZ  . ARG A 40  ? 0.2203 0.3138 0.2667 0.0105  -0.0357 0.0183  40  ARG A CZ  
301  N NH1 . ARG A 40  ? 0.1953 0.2992 0.2483 0.0135  -0.0351 0.0282  40  ARG A NH1 
302  N NH2 . ARG A 40  ? 0.2031 0.2967 0.2510 0.0045  -0.0428 0.0136  40  ARG A NH2 
303  N N   . HIS A 41  ? 0.2158 0.2711 0.2249 0.0204  -0.0114 -0.0027 41  HIS A N   
304  C CA  . HIS A 41  ? 0.3079 0.3658 0.3072 0.0198  -0.0129 -0.0081 41  HIS A CA  
305  C C   . HIS A 41  ? 0.2593 0.3164 0.2536 0.0222  -0.0072 -0.0070 41  HIS A C   
306  O O   . HIS A 41  ? 0.2579 0.3184 0.2435 0.0226  -0.0070 -0.0107 41  HIS A O   
307  C CB  . HIS A 41  ? 0.2889 0.3415 0.2878 0.0175  -0.0162 -0.0172 41  HIS A CB  
308  C CG  . HIS A 41  ? 0.3147 0.3589 0.3170 0.0183  -0.0122 -0.0209 41  HIS A CG  
309  N ND1 . HIS A 41  ? 0.2775 0.3157 0.2872 0.0165  -0.0139 -0.0230 41  HIS A ND1 
310  C CD2 . HIS A 41  ? 0.3525 0.3945 0.3522 0.0203  -0.0073 -0.0223 41  HIS A CD2 
311  C CE1 . HIS A 41  ? 0.2381 0.2707 0.2494 0.0175  -0.0103 -0.0253 41  HIS A CE1 
312  N NE2 . HIS A 41  ? 0.3643 0.3992 0.3701 0.0198  -0.0064 -0.0250 41  HIS A NE2 
313  N N   . VAL A 42  ? 0.2472 0.3005 0.2461 0.0237  -0.0027 -0.0014 42  VAL A N   
314  C CA  . VAL A 42  ? 0.2456 0.2995 0.2411 0.0250  0.0019  0.0019  42  VAL A CA  
315  C C   . VAL A 42  ? 0.2774 0.3409 0.2667 0.0260  0.0012  0.0075  42  VAL A C   
316  O O   . VAL A 42  ? 0.2937 0.3604 0.2784 0.0268  0.0046  0.0097  42  VAL A O   
317  C CB  . VAL A 42  ? 0.2423 0.2885 0.2441 0.0255  0.0057  0.0068  42  VAL A CB  
318  C CG1 . VAL A 42  ? 0.2071 0.2546 0.2121 0.0274  0.0056  0.0145  42  VAL A CG1 
319  C CG2 . VAL A 42  ? 0.3062 0.3508 0.3065 0.0252  0.0099  0.0087  42  VAL A CG2 
320  N N   . ILE A 43  ? 0.2776 0.3471 0.2672 0.0260  -0.0031 0.0108  43  ILE A N   
321  C CA  . ILE A 43  ? 0.2905 0.3705 0.2742 0.0267  -0.0047 0.0172  43  ILE A CA  
322  C C   . ILE A 43  ? 0.2779 0.3652 0.2499 0.0250  -0.0087 0.0109  43  ILE A C   
323  O O   . ILE A 43  ? 0.3116 0.4089 0.2761 0.0252  -0.0104 0.0157  43  ILE A O   
324  C CB  . ILE A 43  ? 0.2539 0.3385 0.2444 0.0277  -0.0077 0.0257  43  ILE A CB  
325  C CG1 . ILE A 43  ? 0.2492 0.3367 0.2423 0.0253  -0.0140 0.0214  43  ILE A CG1 
326  C CG2 . ILE A 43  ? 0.2476 0.3237 0.2482 0.0303  -0.0029 0.0313  43  ILE A CG2 
327  C CD1 . ILE A 43  ? 0.2783 0.3753 0.2778 0.0259  -0.0181 0.0305  43  ILE A CD1 
328  N N   . CYS A 44  ? 0.3382 0.3529 0.2974 0.0216  0.0319  -0.0242 44  CYS A N   
329  C CA  . CYS A 44  ? 0.3618 0.3665 0.3125 0.0204  0.0348  -0.0386 44  CYS A CA  
330  C C   . CYS A 44  ? 0.4241 0.4432 0.3739 0.0233  0.0467  -0.0535 44  CYS A C   
331  O O   . CYS A 44  ? 0.4824 0.5155 0.4489 0.0326  0.0518  -0.0538 44  CYS A O   
332  C CB  . CYS A 44  ? 0.3684 0.3543 0.3322 0.0295  0.0312  -0.0408 44  CYS A CB  
333  S SG  . CYS A 44  ? 0.4237 0.3923 0.3869 0.0236  0.0191  -0.0267 44  CYS A SG  
334  N N   . THR A 45  ? 0.4591 0.4753 0.3899 0.0148  0.0513  -0.0662 45  THR A N   
335  C CA  . THR A 45  ? 0.5643 0.5902 0.4961 0.0190  0.0648  -0.0849 45  THR A CA  
336  C C   . THR A 45  ? 0.6551 0.6623 0.5999 0.0307  0.0666  -0.0976 45  THR A C   
337  O O   . THR A 45  ? 0.5319 0.5183 0.4809 0.0330  0.0565  -0.0911 45  THR A O   
338  C CB  . THR A 45  ? 0.5772 0.6084 0.4789 0.0025  0.0704  -0.0941 45  THR A CB  
339  O OG1 . THR A 45  ? 0.5839 0.5922 0.4675 -0.0058 0.0640  -0.0986 45  THR A OG1 
340  C CG2 . THR A 45  ? 0.5503 0.5954 0.4391 -0.0104 0.0651  -0.0787 45  THR A CG2 
341  N N   . SER A 46  ? 0.7622 0.7769 0.7145 0.0379  0.0799  -0.1162 46  SER A N   
342  C CA  . SER A 46  ? 0.6718 0.6670 0.6388 0.0500  0.0821  -0.1299 46  SER A CA  
343  C C   . SER A 46  ? 0.7110 0.6786 0.6549 0.0400  0.0757  -0.1352 46  SER A C   
344  O O   . SER A 46  ? 0.6852 0.6294 0.6399 0.0469  0.0681  -0.1347 46  SER A O   
345  C CB  . SER A 46  ? 0.8046 0.8136 0.7831 0.0584  0.0996  -0.1518 46  SER A CB  
346  O OG  . SER A 46  ? 0.8844 0.9070 0.8996 0.0753  0.1009  -0.1473 46  SER A OG  
347  N N   . GLU A 47  ? 0.7422 0.7119 0.6536 0.0221  0.0772  -0.1389 47  GLU A N   
348  C CA  . GLU A 47  ? 0.7274 0.6718 0.6152 0.0102  0.0698  -0.1433 47  GLU A CA  
349  C C   . GLU A 47  ? 0.6925 0.6250 0.5821 0.0056  0.0518  -0.1213 47  GLU A C   
350  O O   . GLU A 47  ? 0.6834 0.5919 0.5689 0.0028  0.0433  -0.1220 47  GLU A O   
351  C CB  . GLU A 47  ? 0.8813 0.8321 0.7324 -0.0096 0.0751  -0.1522 47  GLU A CB  
352  C CG  . GLU A 47  ? 0.9548 0.8791 0.7798 -0.0219 0.0705  -0.1632 47  GLU A CG  
353  C CD  . GLU A 47  ? 1.1375 1.0625 0.9385 -0.0293 0.0869  -0.1896 47  GLU A CD  
354  O OE1 . GLU A 47  ? 1.2301 1.1803 1.0242 -0.0332 0.0993  -0.1942 47  GLU A OE1 
355  O OE2 . GLU A 47  ? 1.2379 1.1382 1.0263 -0.0321 0.0880  -0.2062 47  GLU A OE2 
356  N N   . ASP A 48  ? 0.6722 0.6213 0.5682 0.0042  0.0465  -0.1022 48  ASP A N   
357  C CA  . ASP A 48  ? 0.6796 0.6202 0.5806 0.0008  0.0319  -0.0824 48  ASP A CA  
358  C C   . ASP A 48  ? 0.5616 0.4862 0.4856 0.0136  0.0270  -0.0788 48  ASP A C   
359  O O   . ASP A 48  ? 0.5174 0.4273 0.4420 0.0089  0.0160  -0.0690 48  ASP A O   
360  C CB  . ASP A 48  ? 0.4427 0.4031 0.3498 -0.0005 0.0294  -0.0652 48  ASP A CB  
361  C CG  . ASP A 48  ? 0.6618 0.6374 0.5472 -0.0143 0.0320  -0.0653 48  ASP A CG  
362  O OD1 . ASP A 48  ? 0.6013 0.5695 0.4626 -0.0280 0.0302  -0.0720 48  ASP A OD1 
363  O OD2 . ASP A 48  ? 0.5131 0.5072 0.4045 -0.0127 0.0349  -0.0577 48  ASP A OD2 
364  N N   . MET A 49  ? 0.5934 0.5218 0.5380 0.0290  0.0340  -0.0852 49  MET A N   
365  C CA  . MET A 49  ? 0.5308 0.4459 0.4983 0.0404  0.0276  -0.0781 49  MET A CA  
366  C C   . MET A 49  ? 0.5417 0.4279 0.5060 0.0391  0.0220  -0.0858 49  MET A C   
367  O O   . MET A 49  ? 0.4873 0.3591 0.4661 0.0440  0.0135  -0.0765 49  MET A O   
368  C CB  . MET A 49  ? 0.5773 0.5030 0.5688 0.0564  0.0348  -0.0829 49  MET A CB  
369  C CG  . MET A 49  ? 0.6681 0.6214 0.6647 0.0575  0.0389  -0.0739 49  MET A CG  
370  S SD  . MET A 49  ? 0.7429 0.6987 0.7581 0.0632  0.0291  -0.0517 49  MET A SD  
371  C CE  . MET A 49  ? 0.4799 0.4649 0.5090 0.0704  0.0369  -0.0512 49  MET A CE  
372  N N   . LEU A 50  ? 0.5478 0.4244 0.4916 0.0311  0.0262  -0.1025 50  LEU A N   
373  C CA  . LEU A 50  ? 0.5594 0.4063 0.4979 0.0286  0.0206  -0.1114 50  LEU A CA  
374  C C   . LEU A 50  ? 0.5269 0.3625 0.4556 0.0150  0.0062  -0.0958 50  LEU A C   
375  O O   . LEU A 50  ? 0.5454 0.3579 0.4800 0.0152  -0.0023 -0.0939 50  LEU A O   
376  C CB  . LEU A 50  ? 0.6016 0.4412 0.5180 0.0226  0.0306  -0.1358 50  LEU A CB  
377  C CG  . LEU A 50  ? 0.6685 0.5123 0.6002 0.0381  0.0459  -0.1563 50  LEU A CG  
378  C CD1 . LEU A 50  ? 0.7230 0.5687 0.6274 0.0287  0.0594  -0.1799 50  LEU A CD1 
379  C CD2 . LEU A 50  ? 0.7307 0.5488 0.6866 0.0525  0.0421  -0.1620 50  LEU A CD2 
380  N N   . ASN A 51  ? 0.5594 0.4111 0.4755 0.0031  0.0028  -0.0840 51  ASN A N   
381  C CA  . ASN A 51  ? 0.5066 0.3518 0.4188 -0.0091 -0.0106 -0.0683 51  ASN A CA  
382  C C   . ASN A 51  ? 0.5421 0.4107 0.4535 -0.0152 -0.0125 -0.0526 51  ASN A C   
383  O O   . ASN A 51  ? 0.6351 0.5063 0.5298 -0.0297 -0.0183 -0.0490 51  ASN A O   
384  C CB  . ASN A 51  ? 0.6509 0.4770 0.5389 -0.0240 -0.0162 -0.0783 51  ASN A CB  
385  C CG  . ASN A 51  ? 0.6369 0.4545 0.5262 -0.0359 -0.0314 -0.0623 51  ASN A CG  
386  O OD1 . ASN A 51  ? 0.6671 0.4922 0.5766 -0.0320 -0.0361 -0.0450 51  ASN A OD1 
387  N ND2 . ASN A 51  ? 0.7934 0.5966 0.6608 -0.0516 -0.0387 -0.0681 51  ASN A ND2 
388  N N   . PRO A 52  ? 0.4648 0.3493 0.3940 -0.0051 -0.0088 -0.0426 52  PRO A N   
389  C CA  . PRO A 52  ? 0.4689 0.3743 0.3971 -0.0097 -0.0089 -0.0308 52  PRO A CA  
390  C C   . PRO A 52  ? 0.4148 0.3198 0.3493 -0.0180 -0.0196 -0.0139 52  PRO A C   
391  O O   . PRO A 52  ? 0.5555 0.4513 0.5036 -0.0156 -0.0244 -0.0066 52  PRO A O   
392  C CB  . PRO A 52  ? 0.4244 0.3428 0.3699 0.0039  -0.0018 -0.0271 52  PRO A CB  
393  C CG  . PRO A 52  ? 0.4073 0.3100 0.3683 0.0125  -0.0048 -0.0257 52  PRO A CG  
394  C CD  . PRO A 52  ? 0.4383 0.3201 0.3892 0.0095  -0.0065 -0.0398 52  PRO A CD  
395  N N   . ASN A 53  ? 0.4104 0.3263 0.3366 -0.0282 -0.0235 -0.0071 53  ASN A N   
396  C CA  . ASN A 53  ? 0.3952 0.3167 0.3342 -0.0336 -0.0320 0.0099  53  ASN A CA  
397  C C   . ASN A 53  ? 0.3707 0.3099 0.3192 -0.0277 -0.0265 0.0172  53  ASN A C   
398  O O   . ASN A 53  ? 0.3704 0.3194 0.3089 -0.0331 -0.0265 0.0180  53  ASN A O   
399  C CB  . ASN A 53  ? 0.4217 0.3405 0.3481 -0.0498 -0.0433 0.0140  53  ASN A CB  
400  C CG  . ASN A 53  ? 0.4122 0.3371 0.3586 -0.0541 -0.0526 0.0315  53  ASN A CG  
401  O OD1 . ASN A 53  ? 0.3981 0.3363 0.3598 -0.0488 -0.0498 0.0406  53  ASN A OD1 
402  N ND2 . ASN A 53  ? 0.4155 0.3308 0.3631 -0.0640 -0.0635 0.0359  53  ASN A ND2 
403  N N   . TYR A 54  ? 0.3529 0.2951 0.3189 -0.0178 -0.0222 0.0228  54  TYR A N   
404  C CA  . TYR A 54  ? 0.3341 0.2903 0.3055 -0.0114 -0.0155 0.0262  54  TYR A CA  
405  C C   . TYR A 54  ? 0.3386 0.3043 0.3148 -0.0177 -0.0198 0.0368  54  TYR A C   
406  O O   . TYR A 54  ? 0.3322 0.3077 0.3037 -0.0177 -0.0168 0.0372  54  TYR A O   
407  C CB  . TYR A 54  ? 0.3219 0.2775 0.3077 -0.0019 -0.0109 0.0300  54  TYR A CB  
408  C CG  . TYR A 54  ? 0.3301 0.2794 0.3133 0.0063  -0.0066 0.0204  54  TYR A CG  
409  C CD1 . TYR A 54  ? 0.3255 0.2845 0.3061 0.0127  0.0002  0.0146  54  TYR A CD1 
410  C CD2 . TYR A 54  ? 0.3438 0.2772 0.3298 0.0075  -0.0102 0.0176  54  TYR A CD2 
411  C CE1 . TYR A 54  ? 0.3337 0.2881 0.3175 0.0214  0.0036  0.0063  54  TYR A CE1 
412  C CE2 . TYR A 54  ? 0.3534 0.2795 0.3411 0.0161  -0.0073 0.0091  54  TYR A CE2 
413  C CZ  . TYR A 54  ? 0.3478 0.2852 0.3360 0.0236  -0.0003 0.0035  54  TYR A CZ  
414  O OH  . TYR A 54  ? 0.3580 0.2893 0.3531 0.0332  0.0019  -0.0044 54  TYR A OH  
415  N N   . GLU A 55  ? 0.3272 0.2904 0.3152 -0.0231 -0.0274 0.0460  55  GLU A N   
416  C CA  . GLU A 55  ? 0.3167 0.2884 0.3143 -0.0280 -0.0325 0.0564  55  GLU A CA  
417  C C   . GLU A 55  ? 0.3297 0.3031 0.3090 -0.0378 -0.0387 0.0551  55  GLU A C   
418  O O   . GLU A 55  ? 0.3372 0.3184 0.3172 -0.0393 -0.0394 0.0601  55  GLU A O   
419  C CB  . GLU A 55  ? 0.4005 0.3710 0.4178 -0.0322 -0.0400 0.0664  55  GLU A CB  
420  C CG  . GLU A 55  ? 0.3805 0.3611 0.4198 -0.0317 -0.0419 0.0774  55  GLU A CG  
421  C CD  . GLU A 55  ? 0.4258 0.4121 0.4777 -0.0212 -0.0296 0.0771  55  GLU A CD  
422  O OE1 . GLU A 55  ? 0.4941 0.4802 0.5588 -0.0178 -0.0248 0.0787  55  GLU A OE1 
423  O OE2 . GLU A 55  ? 0.4685 0.4590 0.5159 -0.0178 -0.0252 0.0757  55  GLU A OE2 
424  N N   . ASP A 56  ? 0.3503 0.3154 0.3113 -0.0459 -0.0433 0.0483  56  ASP A N   
425  C CA  . ASP A 56  ? 0.3674 0.3341 0.3061 -0.0580 -0.0487 0.0466  56  ASP A CA  
426  C C   . ASP A 56  ? 0.3651 0.3399 0.2901 -0.0542 -0.0382 0.0382  56  ASP A C   
427  O O   . ASP A 56  ? 0.4105 0.3926 0.3264 -0.0617 -0.0412 0.0429  56  ASP A O   
428  C CB  . ASP A 56  ? 0.3943 0.3488 0.3130 -0.0685 -0.0543 0.0387  56  ASP A CB  
429  C CG  . ASP A 56  ? 0.4844 0.4327 0.4146 -0.0768 -0.0682 0.0495  56  ASP A CG  
430  O OD1 . ASP A 56  ? 0.4719 0.4280 0.4255 -0.0760 -0.0742 0.0638  56  ASP A OD1 
431  O OD2 . ASP A 56  ? 0.4452 0.3810 0.3628 -0.0842 -0.0729 0.0433  56  ASP A OD2 
432  N N   . LEU A 57  ? 0.3611 0.3351 0.2859 -0.0433 -0.0268 0.0269  57  LEU A N   
433  C CA  . LEU A 57  ? 0.4004 0.3849 0.3169 -0.0390 -0.0166 0.0195  57  LEU A CA  
434  C C   . LEU A 57  ? 0.3642 0.3592 0.2923 -0.0358 -0.0159 0.0298  57  LEU A C   
435  O O   . LEU A 57  ? 0.3843 0.3892 0.3025 -0.0395 -0.0129 0.0291  57  LEU A O   
436  C CB  . LEU A 57  ? 0.3560 0.3380 0.2776 -0.0263 -0.0065 0.0079  57  LEU A CB  
437  C CG  . LEU A 57  ? 0.3803 0.3519 0.2880 -0.0284 -0.0040 -0.0070 57  LEU A CG  
438  C CD1 . LEU A 57  ? 0.4986 0.4699 0.4160 -0.0143 0.0060  -0.0177 57  LEU A CD1 
439  C CD2 . LEU A 57  ? 0.5246 0.5010 0.4068 -0.0414 -0.0028 -0.0142 57  LEU A CD2 
440  N N   . LEU A 58  ? 0.3225 0.3154 0.2713 -0.0298 -0.0181 0.0388  58  LEU A N   
441  C CA  . LEU A 58  ? 0.3612 0.3612 0.3213 -0.0261 -0.0162 0.0466  58  LEU A CA  
442  C C   . LEU A 58  ? 0.4632 0.4656 0.4217 -0.0362 -0.0255 0.0563  58  LEU A C   
443  O O   . LEU A 58  ? 0.4445 0.4521 0.4056 -0.0357 -0.0242 0.0606  58  LEU A O   
444  C CB  . LEU A 58  ? 0.4280 0.4246 0.4092 -0.0179 -0.0143 0.0516  58  LEU A CB  
445  C CG  . LEU A 58  ? 0.4066 0.4077 0.3971 -0.0099 -0.0067 0.0532  58  LEU A CG  
446  C CD1 . LEU A 58  ? 0.2879 0.2955 0.2667 -0.0064 0.0002  0.0461  58  LEU A CD1 
447  C CD2 . LEU A 58  ? 0.3835 0.3801 0.3874 -0.0037 -0.0031 0.0545  58  LEU A CD2 
448  N N   . ILE A 59  ? 0.3721 0.3695 0.3263 -0.0464 -0.0362 0.0608  59  ILE A N   
449  C CA  . ILE A 59  ? 0.4042 0.4029 0.3578 -0.0573 -0.0480 0.0723  59  ILE A CA  
450  C C   . ILE A 59  ? 0.4934 0.4987 0.4263 -0.0643 -0.0459 0.0703  59  ILE A C   
451  O O   . ILE A 59  ? 0.5254 0.5326 0.4613 -0.0698 -0.0529 0.0804  59  ILE A O   
452  C CB  . ILE A 59  ? 0.4461 0.4387 0.3938 -0.0696 -0.0612 0.0770  59  ILE A CB  
453  C CG1 . ILE A 59  ? 0.4088 0.3977 0.3840 -0.0647 -0.0662 0.0842  59  ILE A CG1 
454  C CG2 . ILE A 59  ? 0.4177 0.4117 0.3567 -0.0841 -0.0747 0.0885  59  ILE A CG2 
455  C CD1 . ILE A 59  ? 0.4598 0.4426 0.4301 -0.0767 -0.0793 0.0883  59  ILE A CD1 
456  N N   . ARG A 60  ? 0.4450 0.4543 0.3586 -0.0641 -0.0363 0.0574  60  ARG A N   
457  C CA  . ARG A 60  ? 0.4998 0.5180 0.3920 -0.0729 -0.0331 0.0542  60  ARG A CA  
458  C C   . ARG A 60  ? 0.4113 0.4388 0.3101 -0.0638 -0.0228 0.0515  60  ARG A C   
459  O O   . ARG A 60  ? 0.4715 0.5093 0.3549 -0.0696 -0.0174 0.0473  60  ARG A O   
460  C CB  . ARG A 60  ? 0.5071 0.5260 0.3758 -0.0788 -0.0272 0.0402  60  ARG A CB  
461  C CG  . ARG A 60  ? 0.6826 0.6912 0.5393 -0.0916 -0.0391 0.0432  60  ARG A CG  
462  C CD  . ARG A 60  ? 0.7918 0.7990 0.6209 -0.0997 -0.0327 0.0276  60  ARG A CD  
463  N NE  . ARG A 60  ? 1.0170 1.0107 0.8491 -0.0971 -0.0355 0.0220  60  ARG A NE  
464  C CZ  . ARG A 60  ? 0.9344 0.9233 0.7624 -0.0896 -0.0246 0.0052  60  ARG A CZ  
465  N NH1 . ARG A 60  ? 0.8932 0.8915 0.7159 -0.0831 -0.0096 -0.0084 60  ARG A NH1 
466  N NH2 . ARG A 60  ? 0.7533 0.7276 0.5850 -0.0883 -0.0294 0.0023  60  ARG A NH2 
467  N N   . LYS A 61  ? 0.4196 0.4445 0.3400 -0.0513 -0.0200 0.0542  61  LYS A N   
468  C CA  . LYS A 61  ? 0.3899 0.4222 0.3155 -0.0434 -0.0112 0.0516  61  LYS A CA  
469  C C   . LYS A 61  ? 0.5144 0.5427 0.4538 -0.0426 -0.0162 0.0625  61  LYS A C   
470  O O   . LYS A 61  ? 0.4754 0.4952 0.4304 -0.0401 -0.0218 0.0688  61  LYS A O   
471  C CB  . LYS A 61  ? 0.3915 0.4229 0.3272 -0.0299 -0.0024 0.0435  61  LYS A CB  
472  C CG  . LYS A 61  ? 0.4054 0.4386 0.3319 -0.0281 0.0033  0.0313  61  LYS A CG  
473  C CD  . LYS A 61  ? 0.3702 0.4178 0.2881 -0.0280 0.0122  0.0230  61  LYS A CD  
474  C CE  . LYS A 61  ? 0.4945 0.5431 0.4020 -0.0287 0.0179  0.0096  61  LYS A CE  
475  N NZ  . LYS A 61  ? 0.7214 0.7748 0.6064 -0.0440 0.0166  0.0075  61  LYS A NZ  
476  N N   . SER A 62  ? 0.3775 0.4120 0.3123 -0.0449 -0.0140 0.0641  62  SER A N   
477  C CA  . SER A 62  ? 0.4011 0.4300 0.3476 -0.0437 -0.0172 0.0720  62  SER A CA  
478  C C   . SER A 62  ? 0.3212 0.3544 0.2704 -0.0356 -0.0076 0.0666  62  SER A C   
479  O O   . SER A 62  ? 0.3409 0.3836 0.2834 -0.0325 -0.0003 0.0589  62  SER A O   
480  C CB  . SER A 62  ? 0.3783 0.4074 0.3152 -0.0569 -0.0264 0.0809  62  SER A CB  
481  O OG  . SER A 62  ? 0.4821 0.5084 0.4123 -0.0671 -0.0367 0.0867  62  SER A OG  
482  N N   . ASN A 63  ? 0.3388 0.3645 0.2987 -0.0325 -0.0080 0.0706  63  ASN A N   
483  C CA  . ASN A 63  ? 0.2781 0.3064 0.2373 -0.0276 -0.0004 0.0664  63  ASN A CA  
484  C C   . ASN A 63  ? 0.2748 0.3170 0.2201 -0.0328 0.0022  0.0637  63  ASN A C   
485  O O   . ASN A 63  ? 0.2761 0.3263 0.2208 -0.0276 0.0087  0.0583  63  ASN A O   
486  C CB  . ASN A 63  ? 0.3743 0.3914 0.3415 -0.0276 -0.0020 0.0704  63  ASN A CB  
487  C CG  . ASN A 63  ? 0.3234 0.3297 0.3084 -0.0204 -0.0007 0.0708  63  ASN A CG  
488  O OD1 . ASN A 63  ? 0.3324 0.3402 0.3222 -0.0143 0.0039  0.0672  63  ASN A OD1 
489  N ND2 . ASN A 63  ? 0.3158 0.3113 0.3125 -0.0212 -0.0046 0.0752  63  ASN A ND2 
490  N N   . HIS A 64  ? 0.3263 0.3727 0.2616 -0.0439 -0.0033 0.0684  64  HIS A N   
491  C CA  . HIS A 64  ? 0.3221 0.3841 0.2458 -0.0504 0.0000  0.0665  64  HIS A CA  
492  C C   . HIS A 64  ? 0.3789 0.4558 0.2975 -0.0483 0.0070  0.0578  64  HIS A C   
493  O O   . HIS A 64  ? 0.3605 0.4538 0.2747 -0.0512 0.0123  0.0544  64  HIS A O   
494  C CB  . HIS A 64  ? 0.3752 0.4375 0.2883 -0.0651 -0.0079 0.0749  64  HIS A CB  
495  C CG  . HIS A 64  ? 0.3612 0.4243 0.2644 -0.0737 -0.0132 0.0774  64  HIS A CG  
496  N ND1 . HIS A 64  ? 0.4239 0.4725 0.3316 -0.0773 -0.0241 0.0859  64  HIS A ND1 
497  C CD2 . HIS A 64  ? 0.3960 0.4729 0.2845 -0.0808 -0.0093 0.0724  64  HIS A CD2 
498  C CE1 . HIS A 64  ? 0.3856 0.4382 0.2795 -0.0873 -0.0282 0.0872  64  HIS A CE1 
499  N NE2 . HIS A 64  ? 0.4999 0.5691 0.3804 -0.0899 -0.0184 0.0781  64  HIS A NE2 
500  N N   . ASN A 65  ? 0.3297 0.4015 0.2507 -0.0433 0.0076  0.0536  65  ASN A N   
501  C CA  . ASN A 65  ? 0.3577 0.4402 0.2762 -0.0392 0.0152  0.0432  65  ASN A CA  
502  C C   . ASN A 65  ? 0.3626 0.4481 0.2940 -0.0263 0.0213  0.0380  65  ASN A C   
503  O O   . ASN A 65  ? 0.3913 0.4876 0.3250 -0.0217 0.0279  0.0295  65  ASN A O   
504  C CB  . ASN A 65  ? 0.4023 0.4760 0.3168 -0.0401 0.0124  0.0404  65  ASN A CB  
505  C CG  . ASN A 65  ? 0.3147 0.3870 0.2136 -0.0552 0.0051  0.0460  65  ASN A CG  
506  O OD1 . ASN A 65  ? 0.3791 0.4387 0.2799 -0.0585 -0.0042 0.0532  65  ASN A OD1 
507  N ND2 . ASN A 65  ? 0.4250 0.5117 0.3090 -0.0654 0.0088  0.0435  65  ASN A ND2 
508  N N   . PHE A 66  ? 0.2913 0.3673 0.2314 -0.0208 0.0194  0.0426  66  PHE A N   
509  C CA  . PHE A 66  ? 0.2610 0.3387 0.2108 -0.0110 0.0232  0.0399  66  PHE A CA  
510  C C   . PHE A 66  ? 0.3550 0.4436 0.3044 -0.0136 0.0242  0.0424  66  PHE A C   
511  O O   . PHE A 66  ? 0.4736 0.5564 0.4188 -0.0193 0.0209  0.0481  66  PHE A O   
512  C CB  . PHE A 66  ? 0.3324 0.3942 0.2888 -0.0056 0.0214  0.0431  66  PHE A CB  
513  C CG  . PHE A 66  ? 0.3189 0.3713 0.2780 -0.0033 0.0198  0.0414  66  PHE A CG  
514  C CD1 . PHE A 66  ? 0.3147 0.3665 0.2781 0.0035  0.0220  0.0359  66  PHE A CD1 
515  C CD2 . PHE A 66  ? 0.3067 0.3501 0.2656 -0.0083 0.0148  0.0461  66  PHE A CD2 
516  C CE1 . PHE A 66  ? 0.3368 0.3786 0.3017 0.0041  0.0196  0.0346  66  PHE A CE1 
517  C CE2 . PHE A 66  ? 0.3614 0.3970 0.3236 -0.0075 0.0120  0.0458  66  PHE A CE2 
518  C CZ  . PHE A 66  ? 0.3818 0.4164 0.3456 -0.0019 0.0145  0.0397  66  PHE A CZ  
519  N N   A LEU A 67  ? 0.2857 0.3897 0.2412 -0.0096 0.0282  0.0382  67  LEU A N   
520  N N   B LEU A 67  ? 0.2858 0.3899 0.2412 -0.0097 0.0282  0.0381  67  LEU A N   
521  C CA  A LEU A 67  ? 0.3359 0.4533 0.2937 -0.0125 0.0283  0.0410  67  LEU A CA  
522  C CA  B LEU A 67  ? 0.3359 0.4532 0.2936 -0.0126 0.0283  0.0411  67  LEU A CA  
523  C C   A LEU A 67  ? 0.2955 0.4101 0.2625 -0.0047 0.0270  0.0427  67  LEU A C   
524  C C   B LEU A 67  ? 0.2954 0.4101 0.2624 -0.0047 0.0270  0.0427  67  LEU A C   
525  O O   A LEU A 67  ? 0.3466 0.4624 0.3240 0.0043  0.0285  0.0389  67  LEU A O   
526  O O   B LEU A 67  ? 0.3465 0.4626 0.3239 0.0043  0.0285  0.0389  67  LEU A O   
527  C CB  A LEU A 67  ? 0.3374 0.4780 0.2990 -0.0145 0.0335  0.0361  67  LEU A CB  
528  C CB  B LEU A 67  ? 0.3376 0.4784 0.2990 -0.0148 0.0334  0.0362  67  LEU A CB  
529  C CG  A LEU A 67  ? 0.3050 0.4536 0.2539 -0.0270 0.0344  0.0368  67  LEU A CG  
530  C CG  B LEU A 67  ? 0.3182 0.4640 0.2664 -0.0258 0.0349  0.0353  67  LEU A CG  
531  C CD1 A LEU A 67  ? 0.3152 0.4515 0.2536 -0.0297 0.0337  0.0344  67  LEU A CD1 
532  C CD1 B LEU A 67  ? 0.4015 0.5732 0.3540 -0.0283 0.0426  0.0292  67  LEU A CD1 
533  C CD2 A LEU A 67  ? 0.4076 0.5830 0.3633 -0.0283 0.0419  0.0312  67  LEU A CD2 
534  C CD2 B LEU A 67  ? 0.3117 0.4495 0.2489 -0.0370 0.0283  0.0446  67  LEU A CD2 
535  N N   . VAL A 68  ? 0.2908 0.4000 0.2528 -0.0091 0.0235  0.0485  68  VAL A N   
536  C CA  . VAL A 68  ? 0.2657 0.3711 0.2313 -0.0053 0.0210  0.0516  68  VAL A CA  
537  C C   . VAL A 68  ? 0.3006 0.4196 0.2663 -0.0115 0.0178  0.0558  68  VAL A C   
538  O O   . VAL A 68  ? 0.3188 0.4353 0.2740 -0.0208 0.0162  0.0584  68  VAL A O   
539  C CB  . VAL A 68  ? 0.3261 0.4101 0.2828 -0.0064 0.0203  0.0536  68  VAL A CB  
540  C CG1 . VAL A 68  ? 0.3110 0.3910 0.2683 -0.0041 0.0180  0.0568  68  VAL A CG1 
541  C CG2 . VAL A 68  ? 0.3389 0.4117 0.2975 -0.0021 0.0226  0.0505  68  VAL A CG2 
542  N N   . GLN A 69  ? 0.2753 0.4080 0.2543 -0.0065 0.0159  0.0572  69  GLN A N   
543  C CA  . GLN A 69  ? 0.3282 0.4777 0.3118 -0.0122 0.0116  0.0623  69  GLN A CA  
544  C C   . GLN A 69  ? 0.2873 0.4330 0.2740 -0.0105 0.0047  0.0685  69  GLN A C   
545  O O   . GLN A 69  ? 0.2915 0.4336 0.2886 -0.0012 0.0038  0.0682  69  GLN A O   
546  C CB  . GLN A 69  ? 0.3853 0.5612 0.3873 -0.0087 0.0154  0.0589  69  GLN A CB  
547  C CG  . GLN A 69  ? 0.4806 0.6782 0.4876 -0.0174 0.0128  0.0636  69  GLN A CG  
548  C CD  . GLN A 69  ? 0.4512 0.6775 0.4802 -0.0126 0.0191  0.0586  69  GLN A CD  
549  O OE1 . GLN A 69  ? 0.4558 0.6848 0.4838 -0.0103 0.0275  0.0505  69  GLN A OE1 
550  N NE2 . GLN A 69  ? 0.5315 0.7799 0.5810 -0.0117 0.0153  0.0632  69  GLN A NE2 
551  N N   . ALA A 70  ? 0.3483 0.4931 0.3241 -0.0207 -0.0011 0.0746  70  ALA A N   
552  C CA  . ALA A 70  ? 0.4682 0.6079 0.4405 -0.0235 -0.0092 0.0819  70  ALA A CA  
553  C C   . ALA A 70  ? 0.5089 0.6676 0.4864 -0.0320 -0.0166 0.0886  70  ALA A C   
554  O O   . ALA A 70  ? 0.5163 0.6713 0.4777 -0.0438 -0.0179 0.0895  70  ALA A O   
555  C CB  . ALA A 70  ? 0.4673 0.5813 0.4143 -0.0304 -0.0082 0.0814  70  ALA A CB  
556  N N   . GLY A 71  ? 0.5419 0.5645 0.5900 -0.0099 -0.0285 0.0435  71  GLY A N   
557  C CA  . GLY A 71  ? 0.5363 0.5657 0.6032 -0.0150 -0.0350 0.0531  71  GLY A CA  
558  C C   . GLY A 71  ? 0.5900 0.6353 0.6704 -0.0127 -0.0273 0.0591  71  GLY A C   
559  O O   . GLY A 71  ? 0.6395 0.6965 0.7202 -0.0065 -0.0171 0.0574  71  GLY A O   
560  N N   . ASN A 72  ? 0.6526 0.6969 0.7429 -0.0178 -0.0327 0.0664  72  ASN A N   
561  C CA  . ASN A 72  ? 0.7120 0.7667 0.8098 -0.0161 -0.0257 0.0714  72  ASN A CA  
562  C C   . ASN A 72  ? 0.7749 0.8161 0.8572 -0.0159 -0.0257 0.0662  72  ASN A C   
563  O O   . ASN A 72  ? 0.8269 0.8752 0.9115 -0.0136 -0.0193 0.0687  72  ASN A O   
564  C CB  . ASN A 72  ? 0.8515 0.9156 0.9722 -0.0217 -0.0303 0.0840  72  ASN A CB  
565  C CG  . ASN A 72  ? 0.8698 0.9515 1.0109 -0.0204 -0.0272 0.0909  72  ASN A CG  
566  O OD1 . ASN A 72  ? 1.0188 1.0980 1.1596 -0.0205 -0.0314 0.0880  72  ASN A OD1 
567  N ND2 . ASN A 72  ? 0.7821 0.8815 0.9412 -0.0189 -0.0193 0.1006  72  ASN A ND2 
568  N N   . VAL A 73  ? 0.6283 0.6492 0.6943 -0.0178 -0.0323 0.0595  73  VAL A N   
569  C CA  . VAL A 73  ? 0.6390 0.6465 0.6900 -0.0159 -0.0306 0.0536  73  VAL A CA  
570  C C   . VAL A 73  ? 0.4977 0.5153 0.5459 -0.0090 -0.0193 0.0500  73  VAL A C   
571  O O   . VAL A 73  ? 0.3784 0.3996 0.4212 -0.0048 -0.0144 0.0449  73  VAL A O   
572  C CB  . VAL A 73  ? 0.7387 0.7232 0.7695 -0.0164 -0.0356 0.0453  73  VAL A CB  
573  C CG1 . VAL A 73  ? 0.6136 0.5910 0.6308 -0.0106 -0.0278 0.0378  73  VAL A CG1 
574  C CG2 . VAL A 73  ? 0.9348 0.9015 0.9621 -0.0230 -0.0475 0.0481  73  VAL A CG2 
575  N N   . GLN A 74  ? 0.5827 0.6036 0.6343 -0.0083 -0.0164 0.0531  74  GLN A N   
576  C CA  . GLN A 74  ? 0.3762 0.4043 0.4247 -0.0027 -0.0079 0.0507  74  GLN A CA  
577  C C   . GLN A 74  ? 0.4753 0.4883 0.5121 -0.0006 -0.0080 0.0442  74  GLN A C   
578  O O   . GLN A 74  ? 0.4216 0.4230 0.4568 -0.0034 -0.0128 0.0452  74  GLN A O   
579  C CB  . GLN A 74  ? 0.4341 0.4740 0.4928 -0.0033 -0.0050 0.0589  74  GLN A CB  
580  C CG  . GLN A 74  ? 0.3578 0.4059 0.4128 0.0020  0.0028  0.0580  74  GLN A CG  
581  C CD  . GLN A 74  ? 0.4898 0.5489 0.5453 0.0058  0.0082  0.0571  74  GLN A CD  
582  O OE1 . GLN A 74  ? 0.4289 0.4874 0.4761 0.0103  0.0115  0.0514  74  GLN A OE1 
583  N NE2 . GLN A 74  ? 0.4848 0.5527 0.5511 0.0038  0.0082  0.0627  74  GLN A NE2 
584  N N   . LEU A 75  ? 0.3129 0.3253 0.3424 0.0043  -0.0028 0.0380  75  LEU A N   
585  C CA  . LEU A 75  ? 0.3595 0.3591 0.3805 0.0071  -0.0011 0.0325  75  LEU A CA  
586  C C   . LEU A 75  ? 0.3784 0.3835 0.4041 0.0101  0.0025  0.0344  75  LEU A C   
587  O O   . LEU A 75  ? 0.3874 0.4049 0.4173 0.0115  0.0053  0.0370  75  LEU A O   
588  C CB  . LEU A 75  ? 0.2856 0.2812 0.2981 0.0105  0.0025  0.0260  75  LEU A CB  
589  C CG  . LEU A 75  ? 0.4333 0.4212 0.4382 0.0078  -0.0014 0.0235  75  LEU A CG  
590  C CD1 . LEU A 75  ? 0.3509 0.3365 0.3479 0.0117  0.0036  0.0179  75  LEU A CD1 
591  C CD2 . LEU A 75  ? 0.4823 0.4510 0.4781 0.0047  -0.0070 0.0224  75  LEU A CD2 
592  N N   A ARG A 76  ? 0.3008 0.2948 0.3246 0.0111  0.0021  0.0330  76  ARG A N   
593  N N   B ARG A 76  ? 0.2993 0.2932 0.3230 0.0112  0.0022  0.0329  76  ARG A N   
594  C CA  A ARG A 76  ? 0.3297 0.3271 0.3592 0.0134  0.0039  0.0353  76  ARG A CA  
595  C CA  B ARG A 76  ? 0.3298 0.3268 0.3591 0.0134  0.0039  0.0352  76  ARG A CA  
596  C C   A ARG A 76  ? 0.3255 0.3220 0.3540 0.0187  0.0090  0.0309  76  ARG A C   
597  C C   B ARG A 76  ? 0.3257 0.3221 0.3543 0.0187  0.0090  0.0309  76  ARG A C   
598  O O   A ARG A 76  ? 0.3003 0.2860 0.3238 0.0211  0.0115  0.0262  76  ARG A O   
599  O O   B ARG A 76  ? 0.3003 0.2858 0.3240 0.0212  0.0115  0.0262  76  ARG A O   
600  C CB  A ARG A 76  ? 0.3309 0.3176 0.3620 0.0118  0.0002  0.0374  76  ARG A CB  
601  C CB  B ARG A 76  ? 0.3306 0.3165 0.3612 0.0116  0.0001  0.0372  76  ARG A CB  
602  C CG  A ARG A 76  ? 0.3384 0.3284 0.3764 0.0135  0.0007  0.0408  76  ARG A CG  
603  C CG  B ARG A 76  ? 0.3397 0.3283 0.3772 0.0132  0.0003  0.0407  76  ARG A CG  
604  C CD  A ARG A 76  ? 0.3925 0.3727 0.4332 0.0111  -0.0040 0.0439  76  ARG A CD  
605  C CD  B ARG A 76  ? 0.3825 0.3582 0.4212 0.0118  -0.0038 0.0419  76  ARG A CD  
606  N NE  A ARG A 76  ? 0.3639 0.3397 0.4097 0.0148  -0.0030 0.0438  76  ARG A NE  
607  N NE  B ARG A 76  ? 0.3008 0.2758 0.3402 0.0057  -0.0099 0.0468  76  ARG A NE  
608  C CZ  A ARG A 76  ? 0.3216 0.3060 0.3736 0.0159  -0.0027 0.0475  76  ARG A CZ  
609  C CZ  B ARG A 76  ? 0.2960 0.2809 0.3424 0.0021  -0.0121 0.0545  76  ARG A CZ  
610  N NH1 A ARG A 76  ? 0.2264 0.2229 0.2774 0.0141  -0.0025 0.0510  76  ARG A NH1 
611  N NH1 B ARG A 76  ? 0.3019 0.2957 0.3518 0.0038  -0.0096 0.0576  76  ARG A NH1 
612  N NH2 A ARG A 76  ? 0.3521 0.3314 0.4109 0.0191  -0.0028 0.0478  76  ARG A NH2 
613  N NH2 B ARG A 76  ? 0.3163 0.3016 0.3659 -0.0036 -0.0173 0.0598  76  ARG A NH2 
614  N N   . VAL A 77  ? 0.2971 0.3040 0.3300 0.0204  0.0104  0.0329  77  VAL A N   
615  C CA  . VAL A 77  ? 0.2254 0.2335 0.2606 0.0246  0.0137  0.0305  77  VAL A CA  
616  C C   . VAL A 77  ? 0.3193 0.3232 0.3624 0.0266  0.0134  0.0326  77  VAL A C   
617  O O   . VAL A 77  ? 0.3066 0.3135 0.3535 0.0251  0.0098  0.0373  77  VAL A O   
618  C CB  . VAL A 77  ? 0.2791 0.2980 0.3139 0.0251  0.0134  0.0318  77  VAL A CB  
619  C CG1 . VAL A 77  ? 0.2704 0.2904 0.3099 0.0286  0.0146  0.0308  77  VAL A CG1 
620  C CG2 . VAL A 77  ? 0.2498 0.2727 0.2787 0.0239  0.0141  0.0296  77  VAL A CG2 
621  N N   . ILE A 78  ? 0.2937 0.2902 0.3394 0.0303  0.0175  0.0296  78  ILE A N   
622  C CA  . ILE A 78  ? 0.2621 0.2540 0.3178 0.0329  0.0178  0.0318  78  ILE A CA  
623  C C   . ILE A 78  ? 0.2866 0.2836 0.3534 0.0367  0.0205  0.0330  78  ILE A C   
624  O O   . ILE A 78  ? 0.3081 0.3025 0.3869 0.0396  0.0213  0.0354  78  ILE A O   
625  C CB  . ILE A 78  ? 0.3418 0.3191 0.3937 0.0349  0.0208  0.0286  78  ILE A CB  
626  C CG1 . ILE A 78  ? 0.2666 0.2372 0.3104 0.0382  0.0280  0.0229  78  ILE A CG1 
627  C CG2 . ILE A 78  ? 0.3376 0.3095 0.3811 0.0300  0.0153  0.0291  78  ILE A CG2 
628  C CD1 . ILE A 78  ? 0.3237 0.2761 0.3606 0.0418  0.0324  0.0192  78  ILE A CD1 
629  N N   . GLY A 79  ? 0.2726 0.2769 0.3374 0.0367  0.0211  0.0320  79  GLY A N   
630  C CA  . GLY A 79  ? 0.2193 0.2289 0.2960 0.0393  0.0218  0.0344  79  GLY A CA  
631  C C   . GLY A 79  ? 0.2750 0.2910 0.3460 0.0383  0.0213  0.0327  79  GLY A C   
632  O O   . GLY A 79  ? 0.2657 0.2815 0.3245 0.0367  0.0224  0.0290  79  GLY A O   
633  N N   . HIS A 80  ? 0.2515 0.2726 0.3322 0.0391  0.0183  0.0360  80  HIS A N   
634  C CA  . HIS A 80  ? 0.2614 0.2874 0.3373 0.0384  0.0168  0.0347  80  HIS A CA  
635  C C   . HIS A 80  ? 0.3067 0.3361 0.3981 0.0399  0.0151  0.0388  80  HIS A C   
636  O O   . HIS A 80  ? 0.2959 0.3253 0.4008 0.0404  0.0112  0.0439  80  HIS A O   
637  C CB  . HIS A 80  ? 0.2987 0.3269 0.3624 0.0356  0.0104  0.0347  80  HIS A CB  
638  C CG  . HIS A 80  ? 0.2879 0.3156 0.3549 0.0345  0.0026  0.0396  80  HIS A CG  
639  N ND1 . HIS A 80  ? 0.2834 0.3082 0.3503 0.0333  0.0002  0.0425  80  HIS A ND1 
640  C CD2 . HIS A 80  ? 0.2908 0.3186 0.3598 0.0341  -0.0044 0.0425  80  HIS A CD2 
641  C CE1 . HIS A 80  ? 0.3634 0.3864 0.4310 0.0322  -0.0077 0.0469  80  HIS A CE1 
642  N NE2 . HIS A 80  ? 0.3271 0.3512 0.3955 0.0326  -0.0111 0.0469  80  HIS A NE2 
643  N N   . SER A 81  ? 0.2858 0.3179 0.3765 0.0404  0.0174  0.0372  81  SER A N   
644  C CA  . SER A 81  ? 0.2252 0.2613 0.3316 0.0411  0.0150  0.0420  81  SER A CA  
645  C C   . SER A 81  ? 0.2682 0.3067 0.3664 0.0398  0.0130  0.0397  81  SER A C   
646  O O   . SER A 81  ? 0.2782 0.3154 0.3615 0.0394  0.0164  0.0343  81  SER A O   
647  C CB  . SER A 81  ? 0.3190 0.3557 0.4421 0.0448  0.0244  0.0445  81  SER A CB  
648  O OG  . SER A 81  ? 0.2990 0.3328 0.4111 0.0464  0.0340  0.0393  81  SER A OG  
649  N N   . MET A 82  ? 0.2463 0.2874 0.3552 0.0390  0.0063  0.0444  82  MET A N   
650  C CA  . MET A 82  ? 0.2792 0.3217 0.3832 0.0378  0.0033  0.0432  82  MET A CA  
651  C C   . MET A 82  ? 0.2013 0.2481 0.3222 0.0391  0.0092  0.0470  82  MET A C   
652  O O   . MET A 82  ? 0.2574 0.3073 0.3997 0.0400  0.0092  0.0538  82  MET A O   
653  C CB  . MET A 82  ? 0.2809 0.3207 0.3815 0.0355  -0.0102 0.0457  82  MET A CB  
654  C CG  . MET A 82  ? 0.2551 0.2941 0.3479 0.0344  -0.0149 0.0439  82  MET A CG  
655  S SD  . MET A 82  ? 0.2751 0.3055 0.3561 0.0324  -0.0307 0.0452  82  MET A SD  
656  C CE  . MET A 82  ? 0.2329 0.2631 0.3390 0.0305  -0.0401 0.0553  82  MET A CE  
657  N N   . GLN A 83  ? 0.2170 0.2640 0.3289 0.0392  0.0150  0.0432  83  GLN A N   
658  C CA  . GLN A 83  ? 0.2070 0.2576 0.3313 0.0402  0.0214  0.0468  83  GLN A CA  
659  C C   . GLN A 83  ? 0.1775 0.2288 0.2955 0.0375  0.0141  0.0461  83  GLN A C   
660  O O   . GLN A 83  ? 0.2022 0.2506 0.3018 0.0368  0.0148  0.0398  83  GLN A O   
661  C CB  . GLN A 83  ? 0.2510 0.2983 0.3671 0.0428  0.0352  0.0429  83  GLN A CB  
662  C CG  . GLN A 83  ? 0.3789 0.4275 0.4970 0.0432  0.0421  0.0445  83  GLN A CG  
663  C CD  . GLN A 83  ? 0.3228 0.3664 0.4375 0.0470  0.0573  0.0433  83  GLN A CD  
664  O OE1 . GLN A 83  ? 0.3499 0.3853 0.4465 0.0478  0.0611  0.0369  83  GLN A OE1 
665  N NE2 . GLN A 83  ? 0.3718 0.4191 0.5025 0.0494  0.0662  0.0497  83  GLN A NE2 
666  N N   . ASN A 84  ? 0.1672 0.2215 0.3010 0.0358  0.0059  0.0528  84  ASN A N   
667  C CA  . ASN A 84  ? 0.1670 0.2201 0.2943 0.0332  -0.0031 0.0522  84  ASN A CA  
668  C C   . ASN A 84  ? 0.1795 0.2264 0.2827 0.0327  -0.0096 0.0447  84  ASN A C   
669  O O   . ASN A 84  ? 0.2342 0.2778 0.3330 0.0327  -0.0157 0.0444  84  ASN A O   
670  C CB  . ASN A 84  ? 0.2248 0.2803 0.3524 0.0333  0.0054  0.0521  84  ASN A CB  
671  C CG  . ASN A 84  ? 0.2727 0.3345 0.4246 0.0346  0.0140  0.0606  84  ASN A CG  
672  O OD1 . ASN A 84  ? 0.2511 0.3171 0.4249 0.0334  0.0073  0.0689  84  ASN A OD1 
673  N ND2 . ASN A 84  ? 0.2317 0.2933 0.3799 0.0373  0.0288  0.0590  84  ASN A ND2 
674  N N   . CYS A 85  ? 0.1974 0.2426 0.2853 0.0324  -0.0081 0.0390  85  CYS A N   
675  C CA  . CYS A 85  ? 0.1925 0.2328 0.2606 0.0327  -0.0135 0.0330  85  CYS A CA  
676  C C   . CYS A 85  ? 0.2124 0.2529 0.2682 0.0341  -0.0054 0.0273  85  CYS A C   
677  O O   . CYS A 85  ? 0.2355 0.2739 0.2770 0.0346  -0.0073 0.0226  85  CYS A O   
678  C CB  . CYS A 85  ? 0.1875 0.2252 0.2476 0.0319  -0.0194 0.0308  85  CYS A CB  
679  S SG  . CYS A 85  ? 0.2255 0.2605 0.2981 0.0295  -0.0323 0.0376  85  CYS A SG  
680  N N   A VAL A 86  ? 0.2106 0.2528 0.2725 0.0348  0.0032  0.0282  86  VAL A N   
681  N N   B VAL A 86  ? 0.2106 0.2528 0.2723 0.0348  0.0033  0.0281  86  VAL A N   
682  C CA  A VAL A 86  ? 0.2080 0.2488 0.2592 0.0354  0.0095  0.0236  86  VAL A CA  
683  C CA  B VAL A 86  ? 0.2079 0.2486 0.2584 0.0354  0.0089  0.0234  86  VAL A CA  
684  C C   A VAL A 86  ? 0.2357 0.2761 0.2917 0.0362  0.0109  0.0254  86  VAL A C   
685  C C   B VAL A 86  ? 0.2365 0.2769 0.2922 0.0362  0.0103  0.0254  86  VAL A C   
686  O O   A VAL A 86  ? 0.2348 0.2765 0.3052 0.0369  0.0114  0.0302  86  VAL A O   
687  O O   B VAL A 86  ? 0.2309 0.2726 0.3010 0.0367  0.0100  0.0303  86  VAL A O   
688  C CB  A VAL A 86  ? 0.2052 0.2443 0.2541 0.0355  0.0183  0.0219  86  VAL A CB  
689  C CB  B VAL A 86  ? 0.2009 0.2398 0.2471 0.0353  0.0174  0.0210  86  VAL A CB  
690  C CG1 A VAL A 86  ? 0.2696 0.3051 0.3148 0.0364  0.0250  0.0201  86  VAL A CG1 
691  C CG1 B VAL A 86  ? 0.2576 0.2959 0.2955 0.0340  0.0149  0.0184  86  VAL A CG1 
692  C CG2 A VAL A 86  ? 0.2660 0.3037 0.3026 0.0341  0.0165  0.0179  86  VAL A CG2 
693  C CG2 B VAL A 86  ? 0.2344 0.2736 0.2931 0.0366  0.0247  0.0250  86  VAL A CG2 
694  N N   . LEU A 87  ? 0.2346 0.2736 0.2801 0.0361  0.0112  0.0224  87  LEU A N   
695  C CA  . LEU A 87  ? 0.2360 0.2739 0.2843 0.0364  0.0129  0.0237  87  LEU A CA  
696  C C   . LEU A 87  ? 0.2871 0.3216 0.3329 0.0368  0.0209  0.0213  87  LEU A C   
697  O O   . LEU A 87  ? 0.2900 0.3226 0.3258 0.0358  0.0229  0.0176  87  LEU A O   
698  C CB  . LEU A 87  ? 0.2203 0.2580 0.2586 0.0358  0.0088  0.0229  87  LEU A CB  
699  C CG  . LEU A 87  ? 0.3493 0.3858 0.3856 0.0359  0.0008  0.0253  87  LEU A CG  
700  C CD1 . LEU A 87  ? 0.3945 0.4298 0.4194 0.0359  -0.0003 0.0249  87  LEU A CD1 
701  C CD2 . LEU A 87  ? 0.3658 0.4014 0.4160 0.0357  -0.0028 0.0305  87  LEU A CD2 
702  N N   . LYS A 88  ? 0.2309 0.2633 0.2853 0.0382  0.0248  0.0235  88  LYS A N   
703  C CA  . LYS A 88  ? 0.2128 0.2386 0.2625 0.0391  0.0318  0.0210  88  LYS A CA  
704  C C   . LYS A 88  ? 0.2710 0.2945 0.3202 0.0385  0.0298  0.0217  88  LYS A C   
705  O O   . LYS A 88  ? 0.3242 0.3486 0.3845 0.0397  0.0287  0.0254  88  LYS A O   
706  C CB  . LYS A 88  ? 0.2613 0.2847 0.3209 0.0423  0.0397  0.0230  88  LYS A CB  
707  C CG  . LYS A 88  ? 0.2413 0.2671 0.3017 0.0425  0.0421  0.0234  88  LYS A CG  
708  C CD  . LYS A 88  ? 0.3755 0.3977 0.4426 0.0461  0.0529  0.0252  88  LYS A CD  
709  C CE  . LYS A 88  ? 0.3823 0.4098 0.4719 0.0487  0.0539  0.0315  88  LYS A CE  
710  N NZ  . LYS A 88  ? 0.4435 0.4701 0.5436 0.0530  0.0657  0.0348  88  LYS A NZ  
711  N N   . LEU A 89  ? 0.2462 0.2667 0.2839 0.0363  0.0287  0.0188  89  LEU A N   
712  C CA  . LEU A 89  ? 0.1948 0.2131 0.2318 0.0351  0.0264  0.0201  89  LEU A CA  
713  C C   . LEU A 89  ? 0.2804 0.2878 0.3129 0.0358  0.0309  0.0178  89  LEU A C   
714  O O   . LEU A 89  ? 0.3187 0.3197 0.3401 0.0345  0.0320  0.0143  89  LEU A O   
715  C CB  . LEU A 89  ? 0.2092 0.2316 0.2387 0.0321  0.0221  0.0199  89  LEU A CB  
716  C CG  . LEU A 89  ? 0.2517 0.2818 0.2810 0.0323  0.0187  0.0209  89  LEU A CG  
717  C CD1 . LEU A 89  ? 0.3245 0.3584 0.3470 0.0305  0.0169  0.0208  89  LEU A CD1 
718  C CD2 . LEU A 89  ? 0.2852 0.3171 0.3209 0.0333  0.0153  0.0248  89  LEU A CD2 
719  N N   . LYS A 90  ? 0.2406 0.2442 0.2810 0.0380  0.0328  0.0197  90  LYS A N   
720  C CA  . LYS A 90  ? 0.2607 0.2515 0.2956 0.0394  0.0365  0.0174  90  LYS A CA  
721  C C   . LYS A 90  ? 0.2909 0.2785 0.3195 0.0353  0.0305  0.0177  90  LYS A C   
722  O O   . LYS A 90  ? 0.2517 0.2460 0.2869 0.0335  0.0258  0.0216  90  LYS A O   
723  C CB  . LYS A 90  ? 0.2649 0.2535 0.3131 0.0437  0.0406  0.0200  90  LYS A CB  
724  C CG  . LYS A 90  ? 0.3392 0.3122 0.3811 0.0471  0.0466  0.0170  90  LYS A CG  
725  C CD  . LYS A 90  ? 0.4085 0.3720 0.4376 0.0497  0.0546  0.0126  90  LYS A CD  
726  C CE  . LYS A 90  ? 0.5180 0.4716 0.5510 0.0568  0.0653  0.0122  90  LYS A CE  
727  N NZ  . LYS A 90  ? 0.4976 0.4468 0.5235 0.0604  0.0754  0.0102  90  LYS A NZ  
728  N N   . VAL A 91  ? 0.3030 0.2798 0.3185 0.0335  0.0300  0.0143  91  VAL A N   
729  C CA  . VAL A 91  ? 0.2502 0.2237 0.2615 0.0289  0.0234  0.0156  91  VAL A CA  
730  C C   . VAL A 91  ? 0.3466 0.3024 0.3509 0.0301  0.0241  0.0134  91  VAL A C   
731  O O   . VAL A 91  ? 0.3352 0.2805 0.3347 0.0348  0.0308  0.0100  91  VAL A O   
732  C CB  . VAL A 91  ? 0.2917 0.2670 0.2950 0.0247  0.0194  0.0146  91  VAL A CB  
733  C CG1 . VAL A 91  ? 0.2816 0.2738 0.2921 0.0240  0.0183  0.0172  91  VAL A CG1 
734  C CG2 . VAL A 91  ? 0.2736 0.2375 0.2637 0.0259  0.0225  0.0096  91  VAL A CG2 
735  N N   . ASP A 92  ? 0.2953 0.2469 0.2991 0.0262  0.0174  0.0157  92  ASP A N   
736  C CA  . ASP A 92  ? 0.3939 0.3269 0.3909 0.0276  0.0170  0.0137  92  ASP A CA  
737  C C   . ASP A 92  ? 0.4112 0.3251 0.3890 0.0256  0.0142  0.0093  92  ASP A C   
738  O O   . ASP A 92  ? 0.4294 0.3240 0.3976 0.0263  0.0124  0.0071  92  ASP A O   
739  C CB  . ASP A 92  ? 0.3416 0.2764 0.3472 0.0243  0.0104  0.0188  92  ASP A CB  
740  C CG  . ASP A 92  ? 0.3904 0.3278 0.3944 0.0171  0.0018  0.0223  92  ASP A CG  
741  O OD1 . ASP A 92  ? 0.4676 0.4108 0.4682 0.0146  0.0007  0.0218  92  ASP A OD1 
742  O OD2 . ASP A 92  ? 0.5021 0.4364 0.5104 0.0138  -0.0041 0.0264  92  ASP A OD2 
743  N N   . THR A 93  ? 0.3332 0.2500 0.3042 0.0230  0.0129  0.0079  93  THR A N   
744  C CA  . THR A 93  ? 0.4045 0.3024 0.3563 0.0201  0.0081  0.0044  93  THR A CA  
745  C C   . THR A 93  ? 0.3753 0.2716 0.3170 0.0226  0.0142  0.0003  93  THR A C   
746  O O   . THR A 93  ? 0.3488 0.2634 0.3004 0.0223  0.0161  0.0021  93  THR A O   
747  C CB  . THR A 93  ? 0.3367 0.2397 0.2923 0.0122  -0.0033 0.0089  93  THR A CB  
748  O OG1 . THR A 93  ? 0.4323 0.3367 0.3978 0.0096  -0.0087 0.0136  93  THR A OG1 
749  C CG2 . THR A 93  ? 0.4434 0.3253 0.3797 0.0084  -0.0105 0.0059  93  THR A CG2 
750  N N   . ALA A 94  ? 0.3688 0.2418 0.2893 0.0253  0.0174  -0.0050 94  ALA A N   
751  C CA  . ALA A 94  ? 0.3864 0.2540 0.2931 0.0266  0.0221  -0.0085 94  ALA A CA  
752  C C   . ALA A 94  ? 0.3849 0.2512 0.2849 0.0193  0.0111  -0.0076 94  ALA A C   
753  O O   . ALA A 94  ? 0.4153 0.2699 0.3090 0.0140  0.0003  -0.0065 94  ALA A O   
754  C CB  . ALA A 94  ? 0.4130 0.2528 0.2955 0.0318  0.0292  -0.0142 94  ALA A CB  
755  N N   . ASN A 95  ? 0.3336 0.2122 0.2367 0.0187  0.0130  -0.0072 95  ASN A N   
756  C CA  . ASN A 95  ? 0.3511 0.2288 0.2494 0.0122  0.0027  -0.0060 95  ASN A CA  
757  C C   . ASN A 95  ? 0.3940 0.2408 0.2637 0.0100  -0.0025 -0.0100 95  ASN A C   
758  O O   . ASN A 95  ? 0.3851 0.2175 0.2361 0.0139  0.0052  -0.0144 95  ASN A O   
759  C CB  . ASN A 95  ? 0.3100 0.2040 0.2152 0.0128  0.0061  -0.0054 95  ASN A CB  
760  C CG  . ASN A 95  ? 0.3423 0.2372 0.2463 0.0063  -0.0048 -0.0035 95  ASN A CG  
761  O OD1 . ASN A 95  ? 0.3500 0.2335 0.2489 0.0011  -0.0153 -0.0019 95  ASN A OD1 
762  N ND2 . ASN A 95  ? 0.3272 0.2359 0.2379 0.0067  -0.0031 -0.0029 95  ASN A ND2 
763  N N   . PRO A 96  ? 0.4018 0.2365 0.2666 0.0037  -0.0156 -0.0082 96  PRO A N   
764  C CA  . PRO A 96  ? 0.4519 0.2534 0.2861 0.0011  -0.0227 -0.0121 96  PRO A CA  
765  C C   . PRO A 96  ? 0.4570 0.2529 0.2777 -0.0014 -0.0252 -0.0134 96  PRO A C   
766  O O   . PRO A 96  ? 0.5552 0.3215 0.3452 -0.0019 -0.0276 -0.0177 96  PRO A O   
767  C CB  . PRO A 96  ? 0.5061 0.3012 0.3454 -0.0065 -0.0388 -0.0076 96  PRO A CB  
768  C CG  . PRO A 96  ? 0.4222 0.2507 0.2951 -0.0090 -0.0403 -0.0005 96  PRO A CG  
769  C CD  . PRO A 96  ? 0.4001 0.2499 0.2867 -0.0015 -0.0250 -0.0017 96  PRO A CD  
770  N N   . LYS A 97  ? 0.4212 0.2429 0.2620 -0.0026 -0.0245 -0.0099 97  LYS A N   
771  C CA  . LYS A 97  ? 0.4743 0.2933 0.3060 -0.0053 -0.0279 -0.0103 97  LYS A CA  
772  C C   . LYS A 97  ? 0.4469 0.2718 0.2742 0.0010  -0.0134 -0.0135 97  LYS A C   
773  O O   . LYS A 97  ? 0.4886 0.3187 0.3151 -0.0007 -0.0147 -0.0130 97  LYS A O   
774  C CB  . LYS A 97  ? 0.4842 0.3269 0.3416 -0.0105 -0.0369 -0.0042 97  LYS A CB  
775  C CG  . LYS A 97  ? 0.5449 0.3807 0.4074 -0.0182 -0.0530 0.0007  97  LYS A CG  
776  C CD  . LYS A 97  ? 0.5781 0.4381 0.4679 -0.0223 -0.0600 0.0076  97  LYS A CD  
777  C CE  . LYS A 97  ? 0.7707 0.6340 0.6772 -0.0282 -0.0713 0.0146  97  LYS A CE  
778  N NZ  . LYS A 97  ? 0.7135 0.6088 0.6534 -0.0280 -0.0694 0.0215  97  LYS A NZ  
779  N N   . THR A 98  ? 0.4090 0.2340 0.2358 0.0081  -0.0002 -0.0160 98  THR A N   
780  C CA  . THR A 98  ? 0.4640 0.2965 0.2909 0.0139  0.0136  -0.0174 98  THR A CA  
781  C C   . THR A 98  ? 0.4272 0.2348 0.2229 0.0138  0.0156  -0.0209 98  THR A C   
782  O O   . THR A 98  ? 0.4804 0.2587 0.2487 0.0147  0.0157  -0.0247 98  THR A O   
783  C CB  . THR A 98  ? 0.4242 0.2601 0.2582 0.0215  0.0269  -0.0184 98  THR A CB  
784  O OG1 . THR A 98  ? 0.3908 0.2479 0.2515 0.0211  0.0242  -0.0149 98  THR A OG1 
785  C CG2 . THR A 98  ? 0.4631 0.3095 0.3024 0.0268  0.0402  -0.0180 98  THR A CG2 
786  N N   . PRO A 99  ? 0.4622 0.2783 0.2591 0.0128  0.0170  -0.0198 99  PRO A N   
787  C CA  . PRO A 99  ? 0.5301 0.3232 0.2969 0.0130  0.0207  -0.0224 99  PRO A CA  
788  C C   . PRO A 99  ? 0.5117 0.3032 0.2740 0.0215  0.0398  -0.0237 99  PRO A C   
789  O O   . PRO A 99  ? 0.4792 0.2916 0.2663 0.0262  0.0485  -0.0217 99  PRO A O   
790  C CB  . PRO A 99  ? 0.4250 0.2329 0.2015 0.0085  0.0144  -0.0195 99  PRO A CB  
791  C CG  . PRO A 99  ? 0.4403 0.2821 0.2528 0.0108  0.0177  -0.0162 99  PRO A CG  
792  C CD  . PRO A 99  ? 0.4144 0.2606 0.2392 0.0115  0.0152  -0.0159 99  PRO A CD  
793  N N   . LYS A 100 ? 0.5138 0.2799 0.2446 0.0232  0.0462  -0.0263 100 LYS A N   
794  C CA  . LYS A 100 ? 0.5636 0.3331 0.2942 0.0305  0.0650  -0.0255 100 LYS A CA  
795  C C   . LYS A 100 ? 0.5125 0.3137 0.2731 0.0292  0.0656  -0.0206 100 LYS A C   
796  O O   . LYS A 100 ? 0.4530 0.2609 0.2167 0.0228  0.0537  -0.0192 100 LYS A O   
797  C CB  . LYS A 100 ? 0.5424 0.2798 0.2323 0.0316  0.0713  -0.0282 100 LYS A CB  
798  C CG  . LYS A 100 ? 0.7826 0.4836 0.4374 0.0317  0.0668  -0.0337 100 LYS A CG  
799  N N   . TYR A 101 ? 0.4206 0.2413 0.2050 0.0352  0.0780  -0.0176 101 TYR A N   
800  C CA  . TYR A 101 ? 0.4170 0.2662 0.2299 0.0336  0.0764  -0.0129 101 TYR A CA  
801  C C   . TYR A 101 ? 0.4466 0.3079 0.2759 0.0403  0.0925  -0.0089 101 TYR A C   
802  O O   . TYR A 101 ? 0.4825 0.3349 0.3079 0.0468  0.1052  -0.0093 101 TYR A O   
803  C CB  . TYR A 101 ? 0.4040 0.2746 0.2432 0.0307  0.0650  -0.0119 101 TYR A CB  
804  C CG  . TYR A 101 ? 0.4169 0.2983 0.2759 0.0357  0.0713  -0.0108 101 TYR A CG  
805  C CD1 . TYR A 101 ? 0.4111 0.2796 0.2621 0.0368  0.0698  -0.0137 101 TYR A CD1 
806  C CD2 . TYR A 101 ? 0.4240 0.3275 0.3100 0.0388  0.0770  -0.0063 101 TYR A CD2 
807  C CE1 . TYR A 101 ? 0.4080 0.2859 0.2774 0.0412  0.0748  -0.0123 101 TYR A CE1 
808  C CE2 . TYR A 101 ? 0.5017 0.4145 0.4065 0.0429  0.0812  -0.0047 101 TYR A CE2 
809  C CZ  . TYR A 101 ? 0.4573 0.3575 0.3537 0.0442  0.0804  -0.0078 101 TYR A CZ  
810  O OH  . TYR A 101 ? 0.4514 0.3602 0.3665 0.0481  0.0839  -0.0059 101 TYR A OH  
811  N N   . LYS A 102 ? 0.4516 0.3329 0.3004 0.0386  0.0912  -0.0044 102 LYS A N   
812  C CA  . LYS A 102 ? 0.4017 0.3002 0.2748 0.0433  0.1025  0.0013  102 LYS A CA  
813  C C   . LYS A 102 ? 0.4268 0.3491 0.3249 0.0393  0.0924  0.0049  102 LYS A C   
814  O O   . LYS A 102 ? 0.4010 0.3247 0.2944 0.0338  0.0797  0.0030  102 LYS A O   
815  C CB  . LYS A 102 ? 0.5162 0.4028 0.3747 0.0469  0.1177  0.0038  102 LYS A CB  
816  C CG  . LYS A 102 ? 0.4813 0.3705 0.3352 0.0426  0.1152  0.0069  102 LYS A CG  
817  C CD  . LYS A 102 ? 0.5461 0.4140 0.3730 0.0461  0.1306  0.0077  102 LYS A CD  
818  C CE  . LYS A 102 ? 0.6757 0.5334 0.4813 0.0404  0.1254  0.0082  102 LYS A CE  
819  N NZ  . LYS A 102 ? 0.7591 0.6394 0.5893 0.0361  0.1181  0.0136  102 LYS A NZ  
820  N N   . PHE A 103 ? 0.3658 0.3059 0.2911 0.0424  0.0976  0.0103  103 PHE A N   
821  C CA  . PHE A 103 ? 0.3417 0.3017 0.2893 0.0393  0.0886  0.0141  103 PHE A CA  
822  C C   . PHE A 103 ? 0.3793 0.3433 0.3323 0.0394  0.0953  0.0200  103 PHE A C   
823  O O   . PHE A 103 ? 0.3629 0.3254 0.3209 0.0441  0.1095  0.0244  103 PHE A O   
824  C CB  . PHE A 103 ? 0.2600 0.2361 0.2346 0.0414  0.0864  0.0169  103 PHE A CB  
825  C CG  . PHE A 103 ? 0.3398 0.3143 0.3118 0.0409  0.0793  0.0124  103 PHE A CG  
826  C CD1 . PHE A 103 ? 0.3251 0.2889 0.2772 0.0374  0.0719  0.0069  103 PHE A CD1 
827  C CD2 . PHE A 103 ? 0.3540 0.3389 0.3460 0.0432  0.0786  0.0147  103 PHE A CD2 
828  C CE1 . PHE A 103 ? 0.3388 0.3030 0.2918 0.0365  0.0654  0.0041  103 PHE A CE1 
829  C CE2 . PHE A 103 ? 0.3848 0.3689 0.3752 0.0424  0.0722  0.0115  103 PHE A CE2 
830  C CZ  . PHE A 103 ? 0.3464 0.3208 0.3179 0.0391  0.0659  0.0064  103 PHE A CZ  
831  N N   . VAL A 104 ? 0.2990 0.2676 0.2515 0.0346  0.0858  0.0207  104 VAL A N   
832  C CA  . VAL A 104 ? 0.2839 0.2571 0.2430 0.0336  0.0900  0.0270  104 VAL A CA  
833  C C   . VAL A 104 ? 0.3273 0.3165 0.3063 0.0301  0.0770  0.0297  104 VAL A C   
834  O O   . VAL A 104 ? 0.3913 0.3829 0.3683 0.0276  0.0645  0.0251  104 VAL A O   
835  C CB  . VAL A 104 ? 0.4697 0.4259 0.4005 0.0310  0.0924  0.0253  104 VAL A CB  
836  C CG1 . VAL A 104 ? 0.4481 0.3834 0.3526 0.0343  0.1025  0.0209  104 VAL A CG1 
837  C CG2 . VAL A 104 ? 0.4593 0.4143 0.3813 0.0252  0.0762  0.0212  104 VAL A CG2 
838  N N   . ARG A 105 ? 0.3429 0.3426 0.3418 0.0304  0.0802  0.0376  105 ARG A N   
839  C CA  . ARG A 105 ? 0.2936 0.3048 0.3084 0.0269  0.0679  0.0409  105 ARG A CA  
840  C C   . ARG A 105 ? 0.2595 0.2654 0.2636 0.0233  0.0674  0.0432  105 ARG A C   
841  O O   . ARG A 105 ? 0.3812 0.3851 0.3860 0.0242  0.0792  0.0493  105 ARG A O   
842  C CB  . ARG A 105 ? 0.3066 0.3318 0.3518 0.0285  0.0691  0.0492  105 ARG A CB  
843  C CG  . ARG A 105 ? 0.2897 0.3239 0.3492 0.0249  0.0532  0.0513  105 ARG A CG  
844  C CD  . ARG A 105 ? 0.3221 0.3681 0.4115 0.0258  0.0520  0.0600  105 ARG A CD  
845  N NE  . ARG A 105 ? 0.3767 0.4275 0.4765 0.0221  0.0361  0.0624  105 ARG A NE  
846  C CZ  . ARG A 105 ? 0.2943 0.3446 0.3907 0.0215  0.0231  0.0572  105 ARG A CZ  
847  N NH1 . ARG A 105 ? 0.2596 0.3070 0.3454 0.0239  0.0239  0.0501  105 ARG A NH1 
848  N NH2 . ARG A 105 ? 0.2720 0.3236 0.3748 0.0185  0.0091  0.0592  105 ARG A NH2 
849  N N   . ILE A 106 ? 0.3019 0.3055 0.2965 0.0194  0.0544  0.0389  106 ILE A N   
850  C CA  . ILE A 106 ? 0.3274 0.3242 0.3093 0.0155  0.0522  0.0404  106 ILE A CA  
851  C C   . ILE A 106 ? 0.3863 0.3935 0.3880 0.0129  0.0451  0.0473  106 ILE A C   
852  O O   . ILE A 106 ? 0.3095 0.3276 0.3315 0.0136  0.0382  0.0493  106 ILE A O   
853  C CB  . ILE A 106 ? 0.3033 0.2910 0.2655 0.0125  0.0414  0.0327  106 ILE A CB  
854  C CG1 . ILE A 106 ? 0.2999 0.2970 0.2742 0.0123  0.0277  0.0293  106 ILE A CG1 
855  C CG2 . ILE A 106 ? 0.3466 0.3205 0.2869 0.0138  0.0473  0.0270  106 ILE A CG2 
856  C CD1 . ILE A 106 ? 0.2781 0.2691 0.2392 0.0095  0.0166  0.0240  106 ILE A CD1 
857  N N   . GLN A 107 ? 0.3497 0.3521 0.3441 0.0097  0.0462  0.0513  107 GLN A N   
858  C CA  . GLN A 107 ? 0.3408 0.3505 0.3512 0.0063  0.0388  0.0585  107 GLN A CA  
859  C C   . GLN A 107 ? 0.3298 0.3364 0.3326 0.0028  0.0223  0.0534  107 GLN A C   
860  O O   . GLN A 107 ? 0.3254 0.3224 0.3080 0.0021  0.0193  0.0464  107 GLN A O   
861  C CB  . GLN A 107 ? 0.4241 0.4299 0.4306 0.0046  0.0500  0.0667  107 GLN A CB  
862  C CG  . GLN A 107 ? 0.6044 0.6131 0.6194 0.0090  0.0689  0.0728  107 GLN A CG  
863  C CD  . GLN A 107 ? 0.6149 0.6402 0.6650 0.0101  0.0681  0.0815  107 GLN A CD  
864  O OE1 . GLN A 107 ? 0.6389 0.6718 0.7059 0.0062  0.0559  0.0866  107 GLN A OE1 
865  N NE2 . GLN A 107 ? 0.7094 0.7395 0.7712 0.0152  0.0801  0.0836  107 GLN A NE2 
866  N N   . PRO A 108 ? 0.3211 0.3344 0.3399 0.0006  0.0108  0.0572  108 PRO A N   
867  C CA  . PRO A 108 ? 0.3453 0.3542 0.3565 -0.0020 -0.0039 0.0528  108 PRO A CA  
868  C C   . PRO A 108 ? 0.3488 0.3471 0.3412 -0.0057 -0.0019 0.0534  108 PRO A C   
869  O O   . PRO A 108 ? 0.3622 0.3582 0.3524 -0.0073 0.0082  0.0603  108 PRO A O   
870  C CB  . PRO A 108 ? 0.4209 0.4365 0.4522 -0.0039 -0.0145 0.0589  108 PRO A CB  
871  C CG  . PRO A 108 ? 0.4694 0.4944 0.5206 -0.0016 -0.0082 0.0645  108 PRO A CG  
872  C CD  . PRO A 108 ? 0.3549 0.3789 0.3998 0.0004  0.0101  0.0662  108 PRO A CD  
873  N N   . GLY A 109 ? 0.3076 0.2989 0.2864 -0.0069 -0.0114 0.0467  109 GLY A N   
874  C CA  . GLY A 109 ? 0.3528 0.3320 0.3116 -0.0106 -0.0116 0.0466  109 GLY A CA  
875  C C   . GLY A 109 ? 0.4234 0.3922 0.3612 -0.0097 -0.0048 0.0411  109 GLY A C   
876  O O   . GLY A 109 ? 0.4211 0.3784 0.3414 -0.0129 -0.0103 0.0387  109 GLY A O   
877  N N   . GLN A 110 ? 0.3439 0.3153 0.2830 -0.0058 0.0057  0.0395  110 GLN A N   
878  C CA  . GLN A 110 ? 0.3339 0.2935 0.2523 -0.0051 0.0107  0.0342  110 GLN A CA  
879  C C   . GLN A 110 ? 0.2718 0.2326 0.1903 -0.0044 0.0000  0.0270  110 GLN A C   
880  O O   . GLN A 110 ? 0.3069 0.2795 0.2426 -0.0022 -0.0063 0.0252  110 GLN A O   
881  C CB  . GLN A 110 ? 0.4494 0.4089 0.3671 -0.0009 0.0264  0.0352  110 GLN A CB  
882  C CG  . GLN A 110 ? 0.5500 0.5159 0.4802 0.0003  0.0381  0.0439  110 GLN A CG  
883  C CD  . GLN A 110 ? 0.6066 0.5678 0.5307 0.0049  0.0556  0.0449  110 GLN A CD  
884  O OE1 . GLN A 110 ? 0.4301 0.4029 0.3744 0.0088  0.0622  0.0477  110 GLN A OE1 
885  N NE2 . GLN A 110 ? 0.7848 0.7273 0.6799 0.0045  0.0628  0.0426  110 GLN A NE2 
886  N N   . THR A 111 ? 0.3377 0.2849 0.2361 -0.0067 -0.0023 0.0234  111 THR A N   
887  C CA  . THR A 111 ? 0.3443 0.2911 0.2423 -0.0070 -0.0124 0.0180  111 THR A CA  
888  C C   . THR A 111 ? 0.3559 0.2994 0.2480 -0.0045 -0.0060 0.0144  111 THR A C   
889  O O   . THR A 111 ? 0.3788 0.3151 0.2604 -0.0031 0.0056  0.0153  111 THR A O   
890  C CB  . THR A 111 ? 0.3442 0.2769 0.2256 -0.0123 -0.0222 0.0177  111 THR A CB  
891  O OG1 . THR A 111 ? 0.3853 0.2999 0.2414 -0.0146 -0.0151 0.0186  111 THR A OG1 
892  C CG2 . THR A 111 ? 0.3365 0.2719 0.2241 -0.0148 -0.0293 0.0213  111 THR A CG2 
893  N N   . PHE A 112 ? 0.3204 0.2686 0.2193 -0.0038 -0.0134 0.0107  112 PHE A N   
894  C CA  . PHE A 112 ? 0.3521 0.2976 0.2472 -0.0021 -0.0098 0.0076  112 PHE A CA  
895  C C   . PHE A 112 ? 0.3373 0.2867 0.2397 -0.0031 -0.0207 0.0052  112 PHE A C   
896  O O   . PHE A 112 ? 0.3348 0.2921 0.2487 -0.0032 -0.0287 0.0056  112 PHE A O   
897  C CB  . PHE A 112 ? 0.3324 0.2896 0.2412 0.0029  -0.0003 0.0078  112 PHE A CB  
898  C CG  . PHE A 112 ? 0.3369 0.3112 0.2676 0.0057  -0.0044 0.0082  112 PHE A CG  
899  C CD1 . PHE A 112 ? 0.3395 0.3220 0.2801 0.0078  -0.0088 0.0056  112 PHE A CD1 
900  C CD2 . PHE A 112 ? 0.3142 0.2947 0.2542 0.0061  -0.0040 0.0117  112 PHE A CD2 
901  C CE1 . PHE A 112 ? 0.3096 0.3043 0.2656 0.0108  -0.0121 0.0056  112 PHE A CE1 
902  C CE2 . PHE A 112 ? 0.3179 0.3102 0.2744 0.0084  -0.0092 0.0118  112 PHE A CE2 
903  C CZ  . PHE A 112 ? 0.3579 0.3564 0.3207 0.0111  -0.0130 0.0084  112 PHE A CZ  
904  N N   . SER A 113 ? 0.3381 0.2813 0.2341 -0.0036 -0.0209 0.0033  113 SER A N   
905  C CA  . SER A 113 ? 0.3056 0.2538 0.2115 -0.0044 -0.0298 0.0024  113 SER A CA  
906  C C   . SER A 113 ? 0.3369 0.3008 0.2602 0.0004  -0.0253 0.0015  113 SER A C   
907  O O   . SER A 113 ? 0.3162 0.2809 0.2382 0.0030  -0.0163 0.0008  113 SER A O   
908  C CB  . SER A 113 ? 0.2803 0.2118 0.1701 -0.0088 -0.0347 0.0019  113 SER A CB  
909  O OG  . SER A 113 ? 0.3507 0.2632 0.2183 -0.0133 -0.0380 0.0026  113 SER A OG  
910  N N   . VAL A 114 ? 0.2863 0.2619 0.2255 0.0019  -0.0311 0.0017  114 VAL A N   
911  C CA  . VAL A 114 ? 0.2474 0.2366 0.2014 0.0063  -0.0277 0.0012  114 VAL A CA  
912  C C   . VAL A 114 ? 0.2613 0.2511 0.2205 0.0047  -0.0324 0.0022  114 VAL A C   
913  O O   . VAL A 114 ? 0.2864 0.2750 0.2497 0.0021  -0.0408 0.0038  114 VAL A O   
914  C CB  . VAL A 114 ? 0.2710 0.2723 0.2382 0.0105  -0.0292 0.0010  114 VAL A CB  
915  C CG1 . VAL A 114 ? 0.2436 0.2563 0.2227 0.0148  -0.0263 0.0007  114 VAL A CG1 
916  C CG2 . VAL A 114 ? 0.2986 0.2999 0.2633 0.0118  -0.0251 0.0010  114 VAL A CG2 
917  N N   . LEU A 115 ? 0.2187 0.2113 0.1803 0.0060  -0.0276 0.0020  115 LEU A N   
918  C CA  . LEU A 115 ? 0.2312 0.2274 0.2018 0.0048  -0.0312 0.0042  115 LEU A CA  
919  C C   . LEU A 115 ? 0.2450 0.2579 0.2317 0.0103  -0.0268 0.0047  115 LEU A C   
920  O O   . LEU A 115 ? 0.2496 0.2666 0.2368 0.0132  -0.0200 0.0039  115 LEU A O   
921  C CB  . LEU A 115 ? 0.2370 0.2229 0.1977 0.0023  -0.0295 0.0039  115 LEU A CB  
922  C CG  . LEU A 115 ? 0.3241 0.3118 0.2942 -0.0004 -0.0350 0.0073  115 LEU A CG  
923  C CD1 . LEU A 115 ? 0.3273 0.3094 0.2997 -0.0055 -0.0467 0.0102  115 LEU A CD1 
924  C CD2 . LEU A 115 ? 0.3044 0.2812 0.2642 -0.0023 -0.0331 0.0066  115 LEU A CD2 
925  N N   . ALA A 116 ? 0.2471 0.2683 0.2459 0.0122  -0.0304 0.0062  116 ALA A N   
926  C CA  . ALA A 116 ? 0.2127 0.2472 0.2234 0.0181  -0.0255 0.0067  116 ALA A CA  
927  C C   . ALA A 116 ? 0.2471 0.2874 0.2670 0.0177  -0.0235 0.0101  116 ALA A C   
928  O O   . ALA A 116 ? 0.2873 0.3267 0.3142 0.0139  -0.0292 0.0137  116 ALA A O   
929  C CB  . ALA A 116 ? 0.2733 0.3136 0.2935 0.0213  -0.0288 0.0072  116 ALA A CB  
930  N N   . CYS A 117 ? 0.2487 0.2946 0.2691 0.0213  -0.0164 0.0097  117 CYS A N   
931  C CA  . CYS A 117 ? 0.2199 0.2715 0.2485 0.0209  -0.0138 0.0134  117 CYS A CA  
932  C C   . CYS A 117 ? 0.2318 0.2943 0.2669 0.0272  -0.0069 0.0144  117 CYS A C   
933  O O   . CYS A 117 ? 0.2675 0.3302 0.2963 0.0316  -0.0038 0.0111  117 CYS A O   
934  C CB  . CYS A 117 ? 0.3012 0.3454 0.3207 0.0180  -0.0119 0.0125  117 CYS A CB  
935  S SG  . CYS A 117 ? 0.3376 0.3648 0.3436 0.0116  -0.0183 0.0109  117 CYS A SG  
936  N N   . TYR A 118 ? 0.2555 0.3258 0.3023 0.0273  -0.0046 0.0194  118 TYR A N   
937  C CA  . TYR A 118 ? 0.2558 0.3357 0.3079 0.0332  0.0032  0.0216  118 TYR A CA  
938  C C   . TYR A 118 ? 0.2804 0.3639 0.3386 0.0304  0.0054  0.0266  118 TYR A C   
939  O O   . TYR A 118 ? 0.2920 0.3768 0.3611 0.0255  0.0008  0.0313  118 TYR A O   
940  C CB  . TYR A 118 ? 0.3159 0.4043 0.3805 0.0378  0.0050  0.0242  118 TYR A CB  
941  C CG  . TYR A 118 ? 0.2864 0.3701 0.3447 0.0405  0.0018  0.0193  118 TYR A CG  
942  C CD1 . TYR A 118 ? 0.2826 0.3620 0.3441 0.0362  -0.0065 0.0190  118 TYR A CD1 
943  C CD2 . TYR A 118 ? 0.3113 0.3926 0.3586 0.0467  0.0058  0.0148  118 TYR A CD2 
944  C CE1 . TYR A 118 ? 0.2729 0.3475 0.3284 0.0382  -0.0099 0.0148  118 TYR A CE1 
945  C CE2 . TYR A 118 ? 0.2378 0.3137 0.2794 0.0487  0.0018  0.0105  118 TYR A CE2 
946  C CZ  . TYR A 118 ? 0.3118 0.3851 0.3581 0.0445  -0.0056 0.0107  118 TYR A CZ  
947  O OH  . TYR A 118 ? 0.3012 0.3690 0.3419 0.0462  -0.0099 0.0069  118 TYR A OH  
948  N N   . ASN A 119 ? 0.3229 0.4068 0.3742 0.0328  0.0110  0.0260  119 ASN A N   
949  C CA  . ASN A 119 ? 0.3875 0.4739 0.4435 0.0300  0.0128  0.0308  119 ASN A CA  
950  C C   . ASN A 119 ? 0.3057 0.3830 0.3596 0.0229  0.0058  0.0305  119 ASN A C   
951  O O   . ASN A 119 ? 0.3560 0.4347 0.4192 0.0186  0.0030  0.0359  119 ASN A O   
952  C CB  . ASN A 119 ? 0.4096 0.5078 0.4828 0.0311  0.0165  0.0386  119 ASN A CB  
953  C CG  . ASN A 119 ? 0.4574 0.5626 0.5302 0.0392  0.0253  0.0390  119 ASN A CG  
954  O OD1 . ASN A 119 ? 0.5517 0.6624 0.6336 0.0426  0.0266  0.0402  119 ASN A OD1 
955  N ND2 . ASN A 119 ? 0.4886 0.5923 0.5499 0.0427  0.0312  0.0379  119 ASN A ND2 
956  N N   . GLY A 120 ? 0.2834 0.3504 0.3246 0.0218  0.0030  0.0246  120 GLY A N   
957  C CA  . GLY A 120 ? 0.3513 0.4066 0.3864 0.0162  -0.0025 0.0235  120 GLY A CA  
958  C C   . GLY A 120 ? 0.3352 0.3861 0.3748 0.0112  -0.0105 0.0258  120 GLY A C   
959  O O   . GLY A 120 ? 0.3460 0.3847 0.3786 0.0062  -0.0159 0.0254  120 GLY A O   
960  N N   . SER A 121 ? 0.3048 0.3296 0.3530 -0.0590 -0.0309 0.0591  121 SER A N   
961  C CA  . SER A 121 ? 0.3599 0.3862 0.4111 -0.0673 -0.0386 0.0652  121 SER A CA  
962  C C   . SER A 121 ? 0.3330 0.3610 0.3822 -0.0640 -0.0369 0.0605  121 SER A C   
963  O O   . SER A 121 ? 0.3154 0.3566 0.3713 -0.0556 -0.0300 0.0600  121 SER A O   
964  C CB  . SER A 121 ? 0.4003 0.4476 0.4692 -0.0699 -0.0403 0.0791  121 SER A CB  
965  O OG  . SER A 121 ? 0.4216 0.4636 0.4914 -0.0785 -0.0469 0.0856  121 SER A OG  
966  N N   . PRO A 122 ? 0.3244 0.3380 0.3630 -0.0701 -0.0431 0.0572  122 PRO A N   
967  C CA  . PRO A 122 ? 0.3269 0.3419 0.3634 -0.0669 -0.0414 0.0526  122 PRO A CA  
968  C C   . PRO A 122 ? 0.3215 0.3574 0.3738 -0.0670 -0.0420 0.0623  122 PRO A C   
969  O O   . PRO A 122 ? 0.3694 0.4134 0.4307 -0.0747 -0.0484 0.0733  122 PRO A O   
970  C CB  . PRO A 122 ? 0.4196 0.4131 0.4399 -0.0746 -0.0487 0.0483  122 PRO A CB  
971  C CG  . PRO A 122 ? 0.5141 0.4900 0.5233 -0.0780 -0.0508 0.0462  122 PRO A CG  
972  C CD  . PRO A 122 ? 0.3948 0.3865 0.4193 -0.0793 -0.0509 0.0557  122 PRO A CD  
973  N N   . SER A 123 ? 0.3212 0.3656 0.3769 -0.0585 -0.0352 0.0589  123 SER A N   
974  C CA  . SER A 123 ? 0.3559 0.4195 0.4258 -0.0556 -0.0332 0.0674  123 SER A CA  
975  C C   . SER A 123 ? 0.3660 0.4281 0.4339 -0.0575 -0.0361 0.0660  123 SER A C   
976  O O   . SER A 123 ? 0.2847 0.3601 0.3641 -0.0607 -0.0391 0.0763  123 SER A O   
977  C CB  . SER A 123 ? 0.3191 0.3924 0.3930 -0.0435 -0.0227 0.0654  123 SER A CB  
978  O OG  . SER A 123 ? 0.6099 0.7023 0.6983 -0.0399 -0.0196 0.0765  123 SER A OG  
979  N N   . GLY A 124 ? 0.2684 0.3161 0.3232 -0.0554 -0.0350 0.0547  124 GLY A N   
980  C CA  . GLY A 124 ? 0.2658 0.3112 0.3177 -0.0570 -0.0376 0.0528  124 GLY A CA  
981  C C   . GLY A 124 ? 0.3227 0.3510 0.3592 -0.0541 -0.0357 0.0404  124 GLY A C   
982  O O   . GLY A 124 ? 0.2889 0.3095 0.3190 -0.0499 -0.0315 0.0340  124 GLY A O   
983  N N   . VAL A 125 ? 0.2464 0.2698 0.2779 -0.0565 -0.0387 0.0381  125 VAL A N   
984  C CA  . VAL A 125 ? 0.2324 0.2407 0.2499 -0.0538 -0.0370 0.0280  125 VAL A CA  
985  C C   . VAL A 125 ? 0.2717 0.2865 0.2928 -0.0496 -0.0347 0.0265  125 VAL A C   
986  O O   . VAL A 125 ? 0.2833 0.3081 0.3126 -0.0526 -0.0378 0.0331  125 VAL A O   
987  C CB  . VAL A 125 ? 0.3534 0.3425 0.3551 -0.0621 -0.0441 0.0259  125 VAL A CB  
988  C CG1 . VAL A 125 ? 0.4336 0.4252 0.4366 -0.0705 -0.0521 0.0321  125 VAL A CG1 
989  C CG2 . VAL A 125 ? 0.3120 0.2855 0.2990 -0.0575 -0.0404 0.0163  125 VAL A CG2 
990  N N   . TYR A 126 ? 0.2795 0.2896 0.2956 -0.0426 -0.0293 0.0189  126 TYR A N   
991  C CA  . TYR A 126 ? 0.2601 0.2748 0.2788 -0.0387 -0.0272 0.0171  126 TYR A CA  
992  C C   . TYR A 126 ? 0.3104 0.3142 0.3190 -0.0347 -0.0243 0.0091  126 TYR A C   
993  O O   . TYR A 126 ? 0.3135 0.3088 0.3153 -0.0332 -0.0223 0.0054  126 TYR A O   
994  C CB  . TYR A 126 ? 0.2739 0.3026 0.3043 -0.0321 -0.0221 0.0201  126 TYR A CB  
995  C CG  . TYR A 126 ? 0.2840 0.3121 0.3135 -0.0262 -0.0167 0.0167  126 TYR A CG  
996  C CD1 . TYR A 126 ? 0.3015 0.3235 0.3251 -0.0214 -0.0135 0.0100  126 TYR A CD1 
997  C CD2 . TYR A 126 ? 0.2970 0.3310 0.3315 -0.0259 -0.0153 0.0211  126 TYR A CD2 
998  C CE1 . TYR A 126 ? 0.2816 0.3029 0.3038 -0.0171 -0.0097 0.0077  126 TYR A CE1 
999  C CE2 . TYR A 126 ? 0.3348 0.3679 0.3674 -0.0209 -0.0108 0.0182  126 TYR A CE2 
1000 C CZ  . TYR A 126 ? 0.2755 0.3019 0.3015 -0.0168 -0.0083 0.0114  126 TYR A CZ  
1001 O OH  . TYR A 126 ? 0.3532 0.3786 0.3768 -0.0129 -0.0049 0.0093  126 TYR A OH  
1002 N N   . GLN A 127 ? 0.2633 0.2685 0.2721 -0.0328 -0.0240 0.0075  127 GLN A N   
1003 C CA  . GLN A 127 ? 0.2432 0.2403 0.2444 -0.0292 -0.0215 0.0017  127 GLN A CA  
1004 C C   . GLN A 127 ? 0.3142 0.3176 0.3213 -0.0226 -0.0169 -0.0001 127 GLN A C   
1005 O O   . GLN A 127 ? 0.3517 0.3640 0.3667 -0.0206 -0.0160 0.0024  127 GLN A O   
1006 C CB  . GLN A 127 ? 0.3291 0.3231 0.3260 -0.0319 -0.0246 0.0017  127 GLN A CB  
1007 C CG  . GLN A 127 ? 0.4499 0.4342 0.4371 -0.0289 -0.0224 -0.0029 127 GLN A CG  
1008 C CD  . GLN A 127 ? 0.3510 0.3199 0.3240 -0.0311 -0.0231 -0.0049 127 GLN A CD  
1009 O OE1 . GLN A 127 ? 0.3394 0.3045 0.3101 -0.0349 -0.0253 -0.0036 127 GLN A OE1 
1010 N NE2 . GLN A 127 ? 0.3614 0.3209 0.3242 -0.0282 -0.0208 -0.0077 127 GLN A NE2 
1011 N N   . CYS A 128 ? 0.2992 0.2970 0.3016 -0.0193 -0.0142 -0.0037 128 CYS A N   
1012 C CA  . CYS A 128 ? 0.3244 0.3259 0.3303 -0.0147 -0.0118 -0.0051 128 CYS A CA  
1013 C C   . CYS A 128 ? 0.2864 0.2823 0.2875 -0.0127 -0.0104 -0.0071 128 CYS A C   
1014 O O   . CYS A 128 ? 0.3305 0.3193 0.3248 -0.0137 -0.0104 -0.0077 128 CYS A O   
1015 C CB  . CYS A 128 ? 0.4671 0.4727 0.4766 -0.0122 -0.0096 -0.0047 128 CYS A CB  
1016 S SG  . CYS A 128 ? 0.5151 0.5177 0.5220 -0.0133 -0.0086 -0.0043 128 CYS A SG  
1017 N N   . ALA A 129 ? 0.3217 0.3203 0.3257 -0.0098 -0.0093 -0.0075 129 ALA A N   
1018 C CA  . ALA A 129 ? 0.2667 0.2633 0.2694 -0.0079 -0.0084 -0.0072 129 ALA A CA  
1019 C C   . ALA A 129 ? 0.2345 0.2329 0.2393 -0.0064 -0.0078 -0.0064 129 ALA A C   
1020 O O   . ALA A 129 ? 0.2994 0.2997 0.3057 -0.0064 -0.0086 -0.0070 129 ALA A O   
1021 C CB  . ALA A 129 ? 0.2737 0.2727 0.2788 -0.0075 -0.0098 -0.0069 129 ALA A CB  
1022 N N   . MET A 130 ? 0.2471 0.2442 0.2512 -0.0049 -0.0061 -0.0043 130 MET A N   
1023 C CA  . MET A 130 ? 0.2279 0.2280 0.2352 -0.0043 -0.0068 -0.0016 130 MET A CA  
1024 C C   . MET A 130 ? 0.2543 0.2567 0.2644 -0.0051 -0.0100 -0.0009 130 MET A C   
1025 O O   . MET A 130 ? 0.2532 0.2568 0.2651 -0.0045 -0.0101 0.0010  130 MET A O   
1026 C CB  . MET A 130 ? 0.3127 0.3130 0.3207 -0.0020 -0.0039 0.0026  130 MET A CB  
1027 C CG  . MET A 130 ? 0.2935 0.2978 0.3055 -0.0022 -0.0046 0.0068  130 MET A CG  
1028 S SD  . MET A 130 ? 0.2970 0.3013 0.3078 -0.0045 -0.0066 0.0050  130 MET A SD  
1029 C CE  . MET A 130 ? 0.2784 0.2789 0.2858 -0.0032 -0.0025 0.0030  130 MET A CE  
1030 N N   . ARG A 131 ? 0.2342 0.2357 0.2434 -0.0064 -0.0126 -0.0022 131 ARG A N   
1031 C CA  . ARG A 131 ? 0.2793 0.2797 0.2888 -0.0076 -0.0162 -0.0018 131 ARG A CA  
1032 C C   . ARG A 131 ? 0.2543 0.2572 0.2671 -0.0091 -0.0189 0.0036  131 ARG A C   
1033 O O   . ARG A 131 ? 0.2636 0.2691 0.2782 -0.0091 -0.0179 0.0068  131 ARG A O   
1034 C CB  . ARG A 131 ? 0.2528 0.2481 0.2568 -0.0079 -0.0178 -0.0047 131 ARG A CB  
1035 C CG  . ARG A 131 ? 0.2810 0.2759 0.2835 -0.0057 -0.0148 -0.0079 131 ARG A CG  
1036 C CD  . ARG A 131 ? 0.2950 0.2925 0.3011 -0.0051 -0.0140 -0.0082 131 ARG A CD  
1037 N NE  . ARG A 131 ? 0.2645 0.2599 0.2710 -0.0054 -0.0167 -0.0077 131 ARG A NE  
1038 C CZ  . ARG A 131 ? 0.2877 0.2855 0.2976 -0.0051 -0.0166 -0.0074 131 ARG A CZ  
1039 N NH1 . ARG A 131 ? 0.2679 0.2697 0.2803 -0.0049 -0.0147 -0.0074 131 ARG A NH1 
1040 N NH2 . ARG A 131 ? 0.2858 0.2814 0.2963 -0.0056 -0.0193 -0.0065 131 ARG A NH2 
1041 N N   . PRO A 132 ? 0.2671 0.2697 0.2817 -0.0108 -0.0227 0.0055  132 PRO A N   
1042 C CA  . PRO A 132 ? 0.2543 0.2607 0.2737 -0.0133 -0.0264 0.0125  132 PRO A CA  
1043 C C   . PRO A 132 ? 0.3007 0.3043 0.3167 -0.0167 -0.0304 0.0143  132 PRO A C   
1044 O O   . PRO A 132 ? 0.2917 0.3008 0.3132 -0.0190 -0.0330 0.0217  132 PRO A O   
1045 C CB  . PRO A 132 ? 0.2434 0.2481 0.2639 -0.0151 -0.0305 0.0134  132 PRO A CB  
1046 C CG  . PRO A 132 ? 0.2966 0.3011 0.3166 -0.0119 -0.0264 0.0088  132 PRO A CG  
1047 C CD  . PRO A 132 ? 0.2726 0.2734 0.2870 -0.0102 -0.0232 0.0031  132 PRO A CD  
1048 N N   . ASN A 133 ? 0.2452 0.2410 0.2523 -0.0170 -0.0310 0.0086  133 ASN A N   
1049 C CA  . ASN A 133 ? 0.2298 0.2215 0.2311 -0.0201 -0.0346 0.0097  133 ASN A CA  
1050 C C   . ASN A 133 ? 0.2736 0.2694 0.2760 -0.0179 -0.0300 0.0093  133 ASN A C   
1051 O O   . ASN A 133 ? 0.3010 0.2932 0.2974 -0.0198 -0.0320 0.0091  133 ASN A O   
1052 C CB  . ASN A 133 ? 0.2950 0.2737 0.2834 -0.0211 -0.0376 0.0042  133 ASN A CB  
1053 C CG  . ASN A 133 ? 0.3277 0.3037 0.3119 -0.0160 -0.0314 -0.0023 133 ASN A CG  
1054 O OD1 . ASN A 133 ? 0.2964 0.2800 0.2873 -0.0130 -0.0262 -0.0028 133 ASN A OD1 
1055 N ND2 . ASN A 133 ? 0.3004 0.2650 0.2731 -0.0148 -0.0320 -0.0064 133 ASN A ND2 
1056 N N   . PHE A 134 ? 0.2286 0.2302 0.2369 -0.0142 -0.0241 0.0091  134 PHE A N   
1057 C CA  . PHE A 134 ? 0.2615 0.2663 0.2713 -0.0122 -0.0197 0.0096  134 PHE A CA  
1058 C C   . PHE A 134 ? 0.2774 0.2777 0.2806 -0.0113 -0.0180 0.0041  134 PHE A C   
1059 O O   . PHE A 134 ? 0.2863 0.2881 0.2893 -0.0110 -0.0163 0.0049  134 PHE A O   
1060 C CB  . PHE A 134 ? 0.2393 0.2491 0.2535 -0.0141 -0.0216 0.0169  134 PHE A CB  
1061 C CG  . PHE A 134 ? 0.2616 0.2784 0.2845 -0.0136 -0.0214 0.0244  134 PHE A CG  
1062 C CD1 . PHE A 134 ? 0.2896 0.3101 0.3170 -0.0087 -0.0149 0.0266  134 PHE A CD1 
1063 C CD2 . PHE A 134 ? 0.2849 0.3039 0.3109 -0.0178 -0.0278 0.0300  134 PHE A CD2 
1064 C CE1 . PHE A 134 ? 0.3979 0.4250 0.4329 -0.0067 -0.0134 0.0345  134 PHE A CE1 
1065 C CE2 . PHE A 134 ? 0.3528 0.3803 0.3886 -0.0169 -0.0273 0.0387  134 PHE A CE2 
1066 C CZ  . PHE A 134 ? 0.2574 0.2896 0.2980 -0.0107 -0.0194 0.0412  134 PHE A CZ  
1067 N N   . THR A 135 ? 0.2780 0.2738 0.2767 -0.0104 -0.0181 -0.0006 135 THR A N   
1068 C CA  . THR A 135 ? 0.2724 0.2663 0.2672 -0.0082 -0.0149 -0.0044 135 THR A CA  
1069 C C   . THR A 135 ? 0.3235 0.3204 0.3227 -0.0065 -0.0118 -0.0059 135 THR A C   
1070 O O   . THR A 135 ? 0.2627 0.2610 0.2654 -0.0067 -0.0121 -0.0051 135 THR A O   
1071 C CB  . THR A 135 ? 0.3388 0.3249 0.3246 -0.0076 -0.0164 -0.0073 135 THR A CB  
1072 O OG1 . THR A 135 ? 0.3025 0.2867 0.2890 -0.0067 -0.0170 -0.0087 135 THR A OG1 
1073 C CG2 . THR A 135 ? 0.3108 0.2907 0.2892 -0.0108 -0.0215 -0.0059 135 THR A CG2 
1074 N N   . ILE A 136 ? 0.2901 0.2880 0.2888 -0.0051 -0.0090 -0.0073 136 ILE A N   
1075 C CA  . ILE A 136 ? 0.2770 0.2773 0.2789 -0.0046 -0.0075 -0.0079 136 ILE A CA  
1076 C C   . ILE A 136 ? 0.2737 0.2742 0.2740 -0.0023 -0.0059 -0.0085 136 ILE A C   
1077 O O   . ILE A 136 ? 0.2601 0.2586 0.2559 -0.0006 -0.0047 -0.0087 136 ILE A O   
1078 C CB  . ILE A 136 ? 0.3663 0.3684 0.3706 -0.0058 -0.0060 -0.0069 136 ILE A CB  
1079 C CG1 . ILE A 136 ? 0.3145 0.3184 0.3187 -0.0055 -0.0044 -0.0060 136 ILE A CG1 
1080 C CG2 . ILE A 136 ? 0.3032 0.3035 0.3075 -0.0062 -0.0059 -0.0056 136 ILE A CG2 
1081 C CD1 . ILE A 136 ? 0.3294 0.3334 0.3350 -0.0075 -0.0038 -0.0048 136 ILE A CD1 
1082 N N   . LYS A 137 ? 0.2992 0.3018 0.3026 -0.0016 -0.0055 -0.0082 137 LYS A N   
1083 C CA  . LYS A 137 ? 0.2807 0.2853 0.2845 0.0016  -0.0029 -0.0070 137 LYS A CA  
1084 C C   . LYS A 137 ? 0.3399 0.3519 0.3502 0.0002  -0.0019 -0.0036 137 LYS A C   
1085 O O   . LYS A 137 ? 0.3431 0.3590 0.3584 -0.0016 -0.0029 -0.0016 137 LYS A O   
1086 C CB  . LYS A 137 ? 0.2894 0.2926 0.2937 0.0032  -0.0032 -0.0072 137 LYS A CB  
1087 C CG  . LYS A 137 ? 0.3350 0.3304 0.3337 0.0030  -0.0059 -0.0098 137 LYS A CG  
1088 C CD  . LYS A 137 ? 0.5269 0.5208 0.5265 0.0048  -0.0060 -0.0097 137 LYS A CD  
1089 C CE  . LYS A 137 ? 0.6587 0.6441 0.6526 0.0037  -0.0096 -0.0116 137 LYS A CE  
1090 N NZ  . LYS A 137 ? 0.5814 0.5684 0.5801 0.0027  -0.0115 -0.0109 137 LYS A NZ  
1091 N N   . GLY A 138 ? 0.2558 0.2693 0.2657 0.0002  -0.0005 -0.0024 138 GLY A N   
1092 C CA  . GLY A 138 ? 0.3188 0.3385 0.3345 -0.0022 -0.0004 0.0015  138 GLY A CA  
1093 C C   . GLY A 138 ? 0.3052 0.3322 0.3253 0.0012  0.0029  0.0065  138 GLY A C   
1094 O O   . GLY A 138 ? 0.3478 0.3742 0.3660 0.0063  0.0060  0.0068  138 GLY A O   
1095 N N   . SER A 139 ? 0.2575 0.2908 0.2833 -0.0013 0.0026  0.0112  139 SER A N   
1096 C CA  . SER A 139 ? 0.2568 0.2991 0.2882 0.0022  0.0064  0.0179  139 SER A CA  
1097 C C   . SER A 139 ? 0.2659 0.3099 0.2979 0.0003  0.0064  0.0196  139 SER A C   
1098 O O   . SER A 139 ? 0.2825 0.3280 0.3186 -0.0058 0.0024  0.0220  139 SER A O   
1099 C CB  . SER A 139 ? 0.2860 0.3382 0.3279 0.0000  0.0050  0.0253  139 SER A CB  
1100 O OG  . SER A 139 ? 0.3024 0.3656 0.3521 0.0029  0.0085  0.0339  139 SER A OG  
1101 N N   . PHE A 140 ? 0.2413 0.2832 0.2676 0.0052  0.0104  0.0184  140 PHE A N   
1102 C CA  . PHE A 140 ? 0.2538 0.2959 0.2791 0.0038  0.0105  0.0189  140 PHE A CA  
1103 C C   . PHE A 140 ? 0.2573 0.3032 0.2804 0.0105  0.0163  0.0224  140 PHE A C   
1104 O O   . PHE A 140 ? 0.3015 0.3413 0.3156 0.0163  0.0197  0.0195  140 PHE A O   
1105 C CB  . PHE A 140 ? 0.2436 0.2759 0.2607 0.0020  0.0083  0.0121  140 PHE A CB  
1106 C CG  . PHE A 140 ? 0.2696 0.2974 0.2875 -0.0035 0.0039  0.0093  140 PHE A CG  
1107 C CD1 . PHE A 140 ? 0.2809 0.3096 0.3028 -0.0084 0.0013  0.0119  140 PHE A CD1 
1108 C CD2 . PHE A 140 ? 0.2475 0.2688 0.2608 -0.0035 0.0023  0.0045  140 PHE A CD2 
1109 C CE1 . PHE A 140 ? 0.2864 0.3077 0.3055 -0.0123 -0.0018 0.0090  140 PHE A CE1 
1110 C CE2 . PHE A 140 ? 0.2699 0.2866 0.2827 -0.0071 -0.0004 0.0025  140 PHE A CE2 
1111 C CZ  . PHE A 140 ? 0.2742 0.2900 0.2888 -0.0111 -0.0021 0.0044  140 PHE A CZ  
1112 N N   . LEU A 141 ? 0.2302 0.2844 0.2599 0.0097  0.0174  0.0287  141 LEU A N   
1113 C CA  . LEU A 141 ? 0.2383 0.2967 0.2656 0.0163  0.0235  0.0329  141 LEU A CA  
1114 C C   . LEU A 141 ? 0.2491 0.3051 0.2729 0.0140  0.0224  0.0313  141 LEU A C   
1115 O O   . LEU A 141 ? 0.2747 0.3275 0.3001 0.0076  0.0174  0.0285  141 LEU A O   
1116 C CB  . LEU A 141 ? 0.2154 0.2887 0.2558 0.0179  0.0262  0.0442  141 LEU A CB  
1117 C CG  . LEU A 141 ? 0.3707 0.4491 0.4174 0.0201  0.0274  0.0482  141 LEU A CG  
1118 C CD1 . LEU A 141 ? 0.4217 0.5173 0.4849 0.0186  0.0277  0.0614  141 LEU A CD1 
1119 C CD2 . LEU A 141 ? 0.4362 0.5082 0.4723 0.0304  0.0346  0.0457  141 LEU A CD2 
1120 N N   . ASN A 142 ? 0.3144 0.3715 0.3325 0.0200  0.0276  0.0335  142 ASN A N   
1121 C CA  . ASN A 142 ? 0.2710 0.3277 0.2872 0.0177  0.0266  0.0333  142 ASN A CA  
1122 C C   . ASN A 142 ? 0.2610 0.3262 0.2908 0.0109  0.0228  0.0388  142 ASN A C   
1123 O O   . ASN A 142 ? 0.2916 0.3663 0.3323 0.0097  0.0226  0.0459  142 ASN A O   
1124 C CB  . ASN A 142 ? 0.3706 0.4291 0.3798 0.0251  0.0332  0.0368  142 ASN A CB  
1125 C CG  . ASN A 142 ? 0.4155 0.4726 0.4211 0.0226  0.0318  0.0360  142 ASN A CG  
1126 O OD1 . ASN A 142 ? 0.6357 0.7024 0.6490 0.0225  0.0334  0.0429  142 ASN A OD1 
1127 N ND2 . ASN A 142 ? 0.4632 0.5093 0.4584 0.0202  0.0284  0.0287  142 ASN A ND2 
1128 N N   . GLY A 143 ? 0.2322 0.2931 0.2607 0.0062  0.0194  0.0361  143 GLY A N   
1129 C CA  . GLY A 143 ? 0.2592 0.3232 0.2969 -0.0006 0.0152  0.0399  143 GLY A CA  
1130 C C   . GLY A 143 ? 0.2860 0.3421 0.3237 -0.0065 0.0099  0.0354  143 GLY A C   
1131 O O   . GLY A 143 ? 0.2598 0.3138 0.3012 -0.0123 0.0060  0.0374  143 GLY A O   
1132 N N   . SER A 144 ? 0.2833 0.3336 0.3157 -0.0049 0.0097  0.0297  144 SER A N   
1133 C CA  . SER A 144 ? 0.2264 0.2693 0.2577 -0.0095 0.0054  0.0258  144 SER A CA  
1134 C C   . SER A 144 ? 0.2105 0.2434 0.2351 -0.0106 0.0042  0.0200  144 SER A C   
1135 O O   . SER A 144 ? 0.2198 0.2455 0.2425 -0.0138 0.0014  0.0174  144 SER A O   
1136 C CB  . SER A 144 ? 0.2451 0.2881 0.2752 -0.0070 0.0059  0.0236  144 SER A CB  
1137 O OG  . SER A 144 ? 0.2304 0.2684 0.2524 -0.0025 0.0082  0.0183  144 SER A OG  
1138 N N   . CYS A 145 ? 0.2518 0.2844 0.2728 -0.0079 0.0063  0.0190  145 CYS A N   
1139 C CA  . CYS A 145 ? 0.2579 0.2836 0.2748 -0.0086 0.0055  0.0157  145 CYS A CA  
1140 C C   . CYS A 145 ? 0.1931 0.2136 0.2117 -0.0124 0.0038  0.0168  145 CYS A C   
1141 O O   . CYS A 145 ? 0.2336 0.2564 0.2562 -0.0149 0.0031  0.0209  145 CYS A O   
1142 C CB  . CYS A 145 ? 0.3243 0.3522 0.3382 -0.0063 0.0073  0.0165  145 CYS A CB  
1143 S SG  . CYS A 145 ? 0.3559 0.3828 0.3617 -0.0022 0.0084  0.0134  145 CYS A SG  
1144 N N   . GLY A 146 ? 0.2091 0.2215 0.2239 -0.0127 0.0032  0.0137  146 GLY A N   
1145 C CA  . GLY A 146 ? 0.2200 0.2232 0.2326 -0.0152 0.0023  0.0140  146 GLY A CA  
1146 C C   . GLY A 146 ? 0.2848 0.2817 0.2946 -0.0184 -0.0005 0.0126  146 GLY A C   
1147 O O   . GLY A 146 ? 0.2897 0.2751 0.2937 -0.0203 -0.0014 0.0119  146 GLY A O   
1148 N N   . SER A 147 ? 0.2496 0.2527 0.2622 -0.0189 -0.0019 0.0125  147 SER A N   
1149 C CA  . SER A 147 ? 0.2863 0.2838 0.2959 -0.0221 -0.0050 0.0112  147 SER A CA  
1150 C C   . SER A 147 ? 0.2465 0.2351 0.2491 -0.0198 -0.0037 0.0066  147 SER A C   
1151 O O   . SER A 147 ? 0.2494 0.2409 0.2526 -0.0157 -0.0011 0.0051  147 SER A O   
1152 C CB  . SER A 147 ? 0.2506 0.2582 0.2659 -0.0218 -0.0057 0.0127  147 SER A CB  
1153 O OG  . SER A 147 ? 0.2465 0.2640 0.2693 -0.0228 -0.0058 0.0185  147 SER A OG  
1154 N N   . VAL A 148 ? 0.2535 0.2308 0.2488 -0.0226 -0.0059 0.0052  148 VAL A N   
1155 C CA  . VAL A 148 ? 0.2588 0.2269 0.2465 -0.0194 -0.0036 0.0019  148 VAL A CA  
1156 C C   . VAL A 148 ? 0.3294 0.2955 0.3140 -0.0207 -0.0058 -0.0003 148 VAL A C   
1157 O O   . VAL A 148 ? 0.2636 0.2315 0.2493 -0.0253 -0.0100 0.0009  148 VAL A O   
1158 C CB  . VAL A 148 ? 0.3055 0.2577 0.2831 -0.0195 -0.0023 0.0017  148 VAL A CB  
1159 C CG1 . VAL A 148 ? 0.2437 0.1991 0.2257 -0.0172 0.0006  0.0043  148 VAL A CG1 
1160 C CG2 . VAL A 148 ? 0.3233 0.2641 0.2929 -0.0261 -0.0075 0.0020  148 VAL A CG2 
1161 N N   . GLY A 149 ? 0.2634 0.2271 0.2450 -0.0165 -0.0030 -0.0023 149 GLY A N   
1162 C CA  . GLY A 149 ? 0.2688 0.2289 0.2459 -0.0169 -0.0042 -0.0044 149 GLY A CA  
1163 C C   . GLY A 149 ? 0.3000 0.2438 0.2638 -0.0151 -0.0021 -0.0058 149 GLY A C   
1164 O O   . GLY A 149 ? 0.2792 0.2175 0.2398 -0.0111 0.0022  -0.0050 149 GLY A O   
1165 N N   . PHE A 150 ? 0.2945 0.2301 0.2496 -0.0175 -0.0046 -0.0075 150 PHE A N   
1166 C CA  . PHE A 150 ? 0.2695 0.1856 0.2077 -0.0158 -0.0025 -0.0092 150 PHE A CA  
1167 C C   . PHE A 150 ? 0.3581 0.2687 0.2881 -0.0172 -0.0046 -0.0111 150 PHE A C   
1168 O O   . PHE A 150 ? 0.3124 0.2326 0.2494 -0.0215 -0.0092 -0.0107 150 PHE A O   
1169 C CB  . PHE A 150 ? 0.3223 0.2238 0.2501 -0.0208 -0.0056 -0.0092 150 PHE A CB  
1170 C CG  . PHE A 150 ? 0.3471 0.2508 0.2765 -0.0300 -0.0139 -0.0081 150 PHE A CG  
1171 C CD1 . PHE A 150 ? 0.3488 0.2697 0.2942 -0.0330 -0.0165 -0.0049 150 PHE A CD1 
1172 C CD2 . PHE A 150 ? 0.4248 0.3139 0.3397 -0.0353 -0.0189 -0.0094 150 PHE A CD2 
1173 C CE1 . PHE A 150 ? 0.3488 0.2745 0.2982 -0.0410 -0.0237 -0.0017 150 PHE A CE1 
1174 C CE2 . PHE A 150 ? 0.4210 0.3143 0.3393 -0.0445 -0.0273 -0.0065 150 PHE A CE2 
1175 C CZ  . PHE A 150 ? 0.3829 0.2955 0.3196 -0.0471 -0.0294 -0.0021 150 PHE A CZ  
1176 N N   . ASN A 151 ? 0.3294 0.2235 0.2437 -0.0130 -0.0006 -0.0125 151 ASN A N   
1177 C CA  . ASN A 151 ? 0.3975 0.2798 0.2976 -0.0144 -0.0025 -0.0146 151 ASN A CA  
1178 C C   . ASN A 151 ? 0.4011 0.2567 0.2777 -0.0162 -0.0032 -0.0166 151 ASN A C   
1179 O O   . ASN A 151 ? 0.4435 0.2897 0.3151 -0.0133 0.0004  -0.0163 151 ASN A O   
1180 C CB  . ASN A 151 ? 0.3661 0.2518 0.2665 -0.0063 0.0040  -0.0139 151 ASN A CB  
1181 C CG  . ASN A 151 ? 0.3975 0.3051 0.3166 -0.0067 0.0022  -0.0125 151 ASN A CG  
1182 O OD1 . ASN A 151 ? 0.5462 0.4567 0.4655 -0.0108 -0.0023 -0.0133 151 ASN A OD1 
1183 N ND2 . ASN A 151 ? 0.4125 0.3346 0.3466 -0.0030 0.0052  -0.0101 151 ASN A ND2 
1184 N N   . ILE A 152 ? 0.4647 0.3065 0.3257 -0.0214 -0.0083 -0.0186 152 ILE A N   
1185 C CA  . ILE A 152 ? 0.4941 0.3061 0.3282 -0.0241 -0.0102 -0.0210 152 ILE A CA  
1186 C C   . ILE A 152 ? 0.5686 0.3645 0.3824 -0.0201 -0.0073 -0.0235 152 ILE A C   
1187 O O   . ILE A 152 ? 0.5415 0.3464 0.3594 -0.0233 -0.0112 -0.0233 152 ILE A O   
1188 C CB  . ILE A 152 ? 0.5726 0.3797 0.4037 -0.0372 -0.0218 -0.0202 152 ILE A CB  
1189 C CG1 . ILE A 152 ? 0.5861 0.4056 0.4340 -0.0398 -0.0232 -0.0173 152 ILE A CG1 
1190 C CG2 . ILE A 152 ? 0.6909 0.4634 0.4898 -0.0415 -0.0255 -0.0231 152 ILE A CG2 
1191 C CD1 . ILE A 152 ? 0.5208 0.3407 0.3707 -0.0526 -0.0346 -0.0142 152 ILE A CD1 
1192 N N   . ASP A 153 ? 0.6192 0.3913 0.4112 -0.0123 0.0002  -0.0252 153 ASP A N   
1193 C CA  . ASP A 153 ? 0.7971 0.5498 0.5654 -0.0070 0.0043  -0.0274 153 ASP A CA  
1194 C C   . ASP A 153 ? 0.6718 0.3866 0.4055 -0.0100 0.0020  -0.0310 153 ASP A C   
1195 O O   . ASP A 153 ? 0.7245 0.4230 0.4471 -0.0036 0.0086  -0.0314 153 ASP A O   
1196 C CB  . ASP A 153 ? 0.7971 0.5560 0.5698 0.0077  0.0176  -0.0248 153 ASP A CB  
1197 C CG  . ASP A 153 ? 1.0310 0.7657 0.7753 0.0152  0.0240  -0.0263 153 ASP A CG  
1198 O OD1 . ASP A 153 ? 0.9152 0.6390 0.6444 0.0085  0.0172  -0.0292 153 ASP A OD1 
1199 O OD2 . ASP A 153 ? 1.1417 0.8681 0.8784 0.0280  0.0360  -0.0240 153 ASP A OD2 
1200 N N   . TYR A 154 ? 0.7360 0.4358 0.4517 -0.0198 -0.0076 -0.0334 154 TYR A N   
1201 C CA  . TYR A 154 ? 0.7386 0.4010 0.4205 -0.0261 -0.0133 -0.0368 154 TYR A CA  
1202 C C   . TYR A 154 ? 0.8139 0.4765 0.5040 -0.0335 -0.0191 -0.0355 154 TYR A C   
1203 O O   . TYR A 154 ? 0.8647 0.5458 0.5739 -0.0451 -0.0296 -0.0326 154 TYR A O   
1204 C CB  . TYR A 154 ? 0.8594 0.4899 0.5095 -0.0132 -0.0015 -0.0398 154 TYR A CB  
1205 N N   . ASP A 155 ? 0.7971 0.4399 0.4736 -0.0262 -0.0117 -0.0367 155 ASP A N   
1206 C CA  . ASP A 155 ? 0.8014 0.4416 0.4835 -0.0325 -0.0165 -0.0353 155 ASP A CA  
1207 C C   . ASP A 155 ? 0.7052 0.3677 0.4128 -0.0223 -0.0063 -0.0322 155 ASP A C   
1208 O O   . ASP A 155 ? 0.7324 0.3901 0.4423 -0.0244 -0.0074 -0.0310 155 ASP A O   
1209 C CB  . ASP A 155 ? 0.9074 0.5018 0.5497 -0.0349 -0.0189 -0.0390 155 ASP A CB  
1210 C CG  . ASP A 155 ? 0.9295 0.5031 0.5542 -0.0185 -0.0034 -0.0407 155 ASP A CG  
1211 O OD1 . ASP A 155 ? 1.1594 0.7200 0.7794 -0.0168 -0.0012 -0.0403 155 ASP A OD1 
1212 O OD2 . ASP A 155 ? 1.0917 0.6638 0.7091 -0.0067 0.0068  -0.0415 155 ASP A OD2 
1213 N N   . CYS A 156 ? 0.6244 0.3116 0.3516 -0.0123 0.0026  -0.0303 156 CYS A N   
1214 C CA  . CYS A 156 ? 0.6116 0.3184 0.3607 -0.0025 0.0123  -0.0266 156 CYS A CA  
1215 C C   . CYS A 156 ? 0.4897 0.2353 0.2743 -0.0066 0.0084  -0.0234 156 CYS A C   
1216 O O   . CYS A 156 ? 0.5046 0.2665 0.2992 -0.0071 0.0071  -0.0232 156 CYS A O   
1217 C CB  . CYS A 156 ? 0.6826 0.3857 0.4253 0.0130  0.0262  -0.0253 156 CYS A CB  
1218 S SG  . CYS A 156 ? 0.6815 0.4096 0.4516 0.0242  0.0372  -0.0187 156 CYS A SG  
1219 N N   . VAL A 157 ? 0.4787 0.2379 0.2808 -0.0090 0.0071  -0.0209 157 VAL A N   
1220 C CA  . VAL A 157 ? 0.4524 0.2455 0.2855 -0.0115 0.0046  -0.0179 157 VAL A CA  
1221 C C   . VAL A 157 ? 0.3965 0.2059 0.2444 -0.0003 0.0148  -0.0148 157 VAL A C   
1222 O O   . VAL A 157 ? 0.4303 0.2335 0.2761 0.0063  0.0216  -0.0128 157 VAL A O   
1223 C CB  . VAL A 157 ? 0.4153 0.2153 0.2593 -0.0196 -0.0019 -0.0160 157 VAL A CB  
1224 C CG1 . VAL A 157 ? 0.3874 0.2204 0.2603 -0.0214 -0.0038 -0.0131 157 VAL A CG1 
1225 C CG2 . VAL A 157 ? 0.4627 0.2458 0.2919 -0.0316 -0.0128 -0.0171 157 VAL A CG2 
1226 N N   . SER A 158 ? 0.3871 0.2180 0.2509 0.0013  0.0152  -0.0136 158 SER A N   
1227 C CA  . SER A 158 ? 0.4117 0.2610 0.2921 0.0096  0.0225  -0.0095 158 SER A CA  
1228 C C   . SER A 158 ? 0.3087 0.1829 0.2127 0.0048  0.0179  -0.0078 158 SER A C   
1229 O O   . SER A 158 ? 0.3436 0.2321 0.2580 0.0009  0.0134  -0.0085 158 SER A O   
1230 C CB  . SER A 158 ? 0.4186 0.2720 0.2982 0.0151  0.0264  -0.0087 158 SER A CB  
1231 O OG  . SER A 158 ? 0.4849 0.3169 0.3440 0.0233  0.0341  -0.0084 158 SER A OG  
1232 N N   . PHE A 159 ? 0.3386 0.2166 0.2497 0.0056  0.0195  -0.0055 159 PHE A N   
1233 C CA  . PHE A 159 ? 0.2867 0.1860 0.2173 0.0021  0.0161  -0.0037 159 PHE A CA  
1234 C C   . PHE A 159 ? 0.2861 0.2028 0.2305 0.0071  0.0196  -0.0003 159 PHE A C   
1235 O O   . PHE A 159 ? 0.3280 0.2441 0.2729 0.0141  0.0261  0.0037  159 PHE A O   
1236 C CB  . PHE A 159 ? 0.3586 0.2558 0.2912 0.0013  0.0167  -0.0018 159 PHE A CB  
1237 C CG  . PHE A 159 ? 0.3258 0.2081 0.2475 -0.0056 0.0114  -0.0040 159 PHE A CG  
1238 C CD1 . PHE A 159 ? 0.3191 0.2109 0.2485 -0.0138 0.0039  -0.0043 159 PHE A CD1 
1239 C CD2 . PHE A 159 ? 0.3216 0.1801 0.2252 -0.0037 0.0140  -0.0048 159 PHE A CD2 
1240 C CE1 . PHE A 159 ? 0.3025 0.1821 0.2235 -0.0212 -0.0020 -0.0045 159 PHE A CE1 
1241 C CE2 . PHE A 159 ? 0.3820 0.2251 0.2744 -0.0114 0.0077  -0.0063 159 PHE A CE2 
1242 C CZ  . PHE A 159 ? 0.3578 0.2125 0.2600 -0.0206 -0.0008 -0.0057 159 PHE A CZ  
1243 N N   . CYS A 160 ? 0.2873 0.2191 0.2428 0.0036  0.0152  -0.0011 160 CYS A N   
1244 C CA  . CYS A 160 ? 0.2817 0.2283 0.2490 0.0067  0.0167  0.0021  160 CYS A CA  
1245 C C   . CYS A 160 ? 0.2715 0.2330 0.2515 0.0035  0.0131  0.0030  160 CYS A C   
1246 O O   . CYS A 160 ? 0.2784 0.2502 0.2668 0.0053  0.0135  0.0062  160 CYS A O   
1247 C CB  . CYS A 160 ? 0.2914 0.2402 0.2581 0.0067  0.0153  0.0007  160 CYS A CB  
1248 S SG  . CYS A 160 ? 0.3266 0.2776 0.2936 -0.0007 0.0080  -0.0040 160 CYS A SG  
1249 N N   . TYR A 161 ? 0.2284 0.1909 0.2095 -0.0011 0.0096  0.0009  161 TYR A N   
1250 C CA  . TYR A 161 ? 0.2832 0.2583 0.2738 -0.0032 0.0068  0.0014  161 TYR A CA  
1251 C C   . TYR A 161 ? 0.2553 0.2308 0.2470 -0.0057 0.0059  0.0019  161 TYR A C   
1252 O O   . TYR A 161 ? 0.2371 0.2053 0.2239 -0.0086 0.0045  0.0008  161 TYR A O   
1253 C CB  . TYR A 161 ? 0.2303 0.2105 0.2231 -0.0057 0.0032  -0.0012 161 TYR A CB  
1254 C CG  . TYR A 161 ? 0.2157 0.2057 0.2149 -0.0067 0.0013  -0.0011 161 TYR A CG  
1255 C CD1 . TYR A 161 ? 0.1894 0.1846 0.1918 -0.0053 0.0008  0.0001  161 TYR A CD1 
1256 C CD2 . TYR A 161 ? 0.2435 0.2364 0.2443 -0.0090 -0.0002 -0.0014 161 TYR A CD2 
1257 C CE1 . TYR A 161 ? 0.2435 0.2437 0.2476 -0.0061 -0.0010 -0.0003 161 TYR A CE1 
1258 C CE2 . TYR A 161 ? 0.2058 0.2057 0.2098 -0.0085 -0.0007 -0.0012 161 TYR A CE2 
1259 C CZ  . TYR A 161 ? 0.2504 0.2523 0.2545 -0.0069 -0.0011 -0.0013 161 TYR A CZ  
1260 O OH  . TYR A 161 ? 0.2226 0.2274 0.2258 -0.0062 -0.0017 -0.0016 161 TYR A OH  
1261 N N   . MET A 162 ? 0.2348 0.2185 0.2326 -0.0051 0.0062  0.0041  162 MET A N   
1262 C CA  . MET A 162 ? 0.2517 0.2390 0.2521 -0.0071 0.0053  0.0051  162 MET A CA  
1263 C C   . MET A 162 ? 0.1978 0.1947 0.2023 -0.0075 0.0035  0.0048  162 MET A C   
1264 O O   . MET A 162 ? 0.1909 0.1913 0.1967 -0.0062 0.0033  0.0056  162 MET A O   
1265 C CB  . MET A 162 ? 0.2377 0.2245 0.2394 -0.0052 0.0081  0.0087  162 MET A CB  
1266 C CG  . MET A 162 ? 0.2855 0.2771 0.2905 -0.0071 0.0073  0.0104  162 MET A CG  
1267 S SD  . MET A 162 ? 0.3025 0.2877 0.3064 -0.0072 0.0095  0.0136  162 MET A SD  
1268 C CE  . MET A 162 ? 0.3285 0.2986 0.3238 -0.0099 0.0082  0.0114  162 MET A CE  
1269 N N   . HIS A 163 ? 0.2111 0.2114 0.2170 -0.0093 0.0022  0.0043  163 HIS A N   
1270 C CA  . HIS A 163 ? 0.1891 0.1959 0.1961 -0.0083 0.0017  0.0039  163 HIS A CA  
1271 C C   . HIS A 163 ? 0.1958 0.2062 0.2029 -0.0074 0.0026  0.0060  163 HIS A C   
1272 O O   . HIS A 163 ? 0.2191 0.2310 0.2282 -0.0081 0.0036  0.0084  163 HIS A O   
1273 C CB  . HIS A 163 ? 0.2530 0.2632 0.2621 -0.0091 0.0012  0.0042  163 HIS A CB  
1274 C CG  . HIS A 163 ? 0.2342 0.2485 0.2423 -0.0065 0.0020  0.0037  163 HIS A CG  
1275 N ND1 . HIS A 163 ? 0.2267 0.2384 0.2312 -0.0050 0.0013  0.0010  163 HIS A ND1 
1276 C CD2 . HIS A 163 ? 0.2196 0.2390 0.2286 -0.0045 0.0040  0.0059  163 HIS A CD2 
1277 C CE1 . HIS A 163 ? 0.2336 0.2464 0.2349 -0.0023 0.0026  0.0008  163 HIS A CE1 
1278 N NE2 . HIS A 163 ? 0.2336 0.2513 0.2374 -0.0013 0.0048  0.0039  163 HIS A NE2 
1279 N N   . HIS A 164 ? 0.2214 0.2327 0.2255 -0.0063 0.0017  0.0054  164 HIS A N   
1280 C CA  . HIS A 164 ? 0.2105 0.2239 0.2123 -0.0061 0.0017  0.0073  164 HIS A CA  
1281 C C   . HIS A 164 ? 0.2568 0.2698 0.2520 -0.0045 0.0016  0.0058  164 HIS A C   
1282 O O   . HIS A 164 ? 0.2724 0.2876 0.2654 -0.0034 0.0031  0.0075  164 HIS A O   
1283 C CB  . HIS A 164 ? 0.2225 0.2354 0.2243 -0.0072 -0.0002 0.0095  164 HIS A CB  
1284 C CG  . HIS A 164 ? 0.2328 0.2464 0.2402 -0.0071 0.0016  0.0128  164 HIS A CG  
1285 N ND1 . HIS A 164 ? 0.2055 0.2220 0.2150 -0.0074 0.0021  0.0172  164 HIS A ND1 
1286 C CD2 . HIS A 164 ? 0.2327 0.2427 0.2422 -0.0062 0.0034  0.0126  164 HIS A CD2 
1287 C CE1 . HIS A 164 ? 0.2080 0.2230 0.2215 -0.0061 0.0047  0.0197  164 HIS A CE1 
1288 N NE2 . HIS A 164 ? 0.2168 0.2268 0.2292 -0.0052 0.0057  0.0167  164 HIS A NE2 
1289 N N   . MET A 165 ? 0.2441 0.2530 0.2345 -0.0038 0.0002  0.0030  165 MET A N   
1290 C CA  . MET A 165 ? 0.2401 0.2450 0.2207 -0.0014 0.0007  0.0014  165 MET A CA  
1291 C C   . MET A 165 ? 0.2690 0.2700 0.2467 0.0008  0.0011  -0.0015 165 MET A C   
1292 O O   . MET A 165 ? 0.2193 0.2201 0.2013 -0.0007 -0.0006 -0.0026 165 MET A O   
1293 C CB  . MET A 165 ? 0.2736 0.2727 0.2447 -0.0033 -0.0030 0.0015  165 MET A CB  
1294 C CG  . MET A 165 ? 0.3662 0.3694 0.3427 -0.0069 -0.0054 0.0052  165 MET A CG  
1295 S SD  . MET A 165 ? 0.4049 0.4017 0.3703 -0.0108 -0.0116 0.0067  165 MET A SD  
1296 C CE  . MET A 165 ? 0.3626 0.3521 0.3241 -0.0124 -0.0158 0.0040  165 MET A CE  
1297 N N   . GLU A 166 ? 0.2491 0.2465 0.2185 0.0049  0.0039  -0.0022 166 GLU A N   
1298 C CA  . GLU A 166 ? 0.2493 0.2403 0.2123 0.0081  0.0049  -0.0047 166 GLU A CA  
1299 C C   . GLU A 166 ? 0.2757 0.2534 0.2220 0.0083  0.0023  -0.0074 166 GLU A C   
1300 O O   . GLU A 166 ? 0.3034 0.2772 0.2400 0.0096  0.0034  -0.0069 166 GLU A O   
1301 C CB  . GLU A 166 ? 0.3349 0.3305 0.3000 0.0139  0.0110  -0.0023 166 GLU A CB  
1302 C CG  . GLU A 166 ? 0.3141 0.3038 0.2739 0.0184  0.0133  -0.0038 166 GLU A CG  
1303 C CD  . GLU A 166 ? 0.4326 0.4306 0.3987 0.0242  0.0197  0.0010  166 GLU A CD  
1304 O OE1 . GLU A 166 ? 0.3619 0.3704 0.3420 0.0222  0.0194  0.0042  166 GLU A OE1 
1305 O OE2 . GLU A 166 ? 0.4451 0.4393 0.4018 0.0307  0.0251  0.0025  166 GLU A OE2 
1306 N N   . LEU A 167 ? 0.2849 0.2550 0.2270 0.0065  -0.0015 -0.0099 167 LEU A N   
1307 C CA  . LEU A 167 ? 0.3562 0.3109 0.2807 0.0053  -0.0055 -0.0124 167 LEU A CA  
1308 C C   . LEU A 167 ? 0.3802 0.3237 0.2900 0.0126  -0.0003 -0.0147 167 LEU A C   
1309 O O   . LEU A 167 ? 0.3761 0.3256 0.2927 0.0181  0.0058  -0.0136 167 LEU A O   
1310 C CB  . LEU A 167 ? 0.3667 0.3175 0.2928 0.0005  -0.0118 -0.0133 167 LEU A CB  
1311 C CG  . LEU A 167 ? 0.3918 0.3533 0.3321 -0.0053 -0.0159 -0.0100 167 LEU A CG  
1312 C CD1 . LEU A 167 ? 0.4015 0.3596 0.3434 -0.0091 -0.0214 -0.0097 167 LEU A CD1 
1313 C CD2 . LEU A 167 ? 0.3393 0.3018 0.2768 -0.0090 -0.0189 -0.0071 167 LEU A CD2 
1314 N N   . PRO A 168 ? 0.4008 0.3272 0.2894 0.0128  -0.0025 -0.0171 168 PRO A N   
1315 C CA  . PRO A 168 ? 0.4514 0.3638 0.3227 0.0212  0.0036  -0.0193 168 PRO A CA  
1316 C C   . PRO A 168 ? 0.4426 0.3529 0.3173 0.0252  0.0063  -0.0204 168 PRO A C   
1317 O O   . PRO A 168 ? 0.4716 0.3775 0.3400 0.0342  0.0143  -0.0199 168 PRO A O   
1318 C CB  . PRO A 168 ? 0.4028 0.2930 0.2484 0.0180  -0.0023 -0.0225 168 PRO A CB  
1319 C CG  . PRO A 168 ? 0.3958 0.2940 0.2469 0.0101  -0.0085 -0.0200 168 PRO A CG  
1320 C CD  . PRO A 168 ? 0.4027 0.3238 0.2822 0.0069  -0.0086 -0.0165 168 PRO A CD  
1321 N N   . THR A 169 ? 0.3863 0.3003 0.2716 0.0193  0.0004  -0.0209 169 THR A N   
1322 C CA  . THR A 169 ? 0.3849 0.2980 0.2746 0.0227  0.0027  -0.0215 169 THR A CA  
1323 C C   . THR A 169 ? 0.4453 0.3781 0.3560 0.0258  0.0084  -0.0177 169 THR A C   
1324 O O   . THR A 169 ? 0.5497 0.4835 0.4648 0.0295  0.0113  -0.0170 169 THR A O   
1325 C CB  . THR A 169 ? 0.5217 0.4314 0.4144 0.0153  -0.0058 -0.0228 169 THR A CB  
1326 O OG1 . THR A 169 ? 0.4405 0.3642 0.3482 0.0081  -0.0106 -0.0204 169 THR A OG1 
1327 C CG2 . THR A 169 ? 0.4618 0.3480 0.3311 0.0125  -0.0119 -0.0260 169 THR A CG2 
1328 N N   . GLY A 170 ? 0.3406 0.2883 0.2638 0.0239  0.0094  -0.0147 170 GLY A N   
1329 C CA  . GLY A 170 ? 0.3412 0.3057 0.2824 0.0256  0.0134  -0.0106 170 GLY A CA  
1330 C C   . GLY A 170 ? 0.3483 0.3231 0.3050 0.0190  0.0087  -0.0101 170 GLY A C   
1331 O O   . GLY A 170 ? 0.4027 0.3890 0.3723 0.0193  0.0107  -0.0069 170 GLY A O   
1332 N N   . VAL A 171 ? 0.3727 0.3434 0.3278 0.0132  0.0025  -0.0125 171 VAL A N   
1333 C CA  . VAL A 171 ? 0.3603 0.3397 0.3281 0.0081  -0.0009 -0.0116 171 VAL A CA  
1334 C C   . VAL A 171 ? 0.2857 0.2708 0.2577 0.0049  -0.0018 -0.0100 171 VAL A C   
1335 O O   . VAL A 171 ? 0.3125 0.2949 0.2777 0.0057  -0.0010 -0.0098 171 VAL A O   
1336 C CB  . VAL A 171 ? 0.3658 0.3393 0.3317 0.0045  -0.0063 -0.0133 171 VAL A CB  
1337 C CG1 . VAL A 171 ? 0.4377 0.4056 0.4004 0.0077  -0.0052 -0.0146 171 VAL A CG1 
1338 C CG2 . VAL A 171 ? 0.3924 0.3569 0.3479 0.0013  -0.0109 -0.0140 171 VAL A CG2 
1339 N N   . HIS A 172 ? 0.2132 0.2053 0.1953 0.0016  -0.0032 -0.0088 172 HIS A N   
1340 C CA  . HIS A 172 ? 0.2673 0.2651 0.2545 -0.0001 -0.0025 -0.0067 172 HIS A CA  
1341 C C   . HIS A 172 ? 0.2433 0.2410 0.2329 -0.0036 -0.0057 -0.0059 172 HIS A C   
1342 O O   . HIS A 172 ? 0.2422 0.2392 0.2341 -0.0047 -0.0076 -0.0061 172 HIS A O   
1343 C CB  . HIS A 172 ? 0.2323 0.2366 0.2277 -0.0001 -0.0004 -0.0051 172 HIS A CB  
1344 C CG  . HIS A 172 ? 0.2458 0.2531 0.2414 0.0035  0.0030  -0.0035 172 HIS A CG  
1345 N ND1 . HIS A 172 ? 0.2757 0.2864 0.2761 0.0045  0.0038  -0.0022 172 HIS A ND1 
1346 C CD2 . HIS A 172 ? 0.2521 0.2601 0.2439 0.0070  0.0063  -0.0019 172 HIS A CD2 
1347 C CE1 . HIS A 172 ? 0.2917 0.3059 0.2925 0.0087  0.0078  0.0008  172 HIS A CE1 
1348 N NE2 . HIS A 172 ? 0.3153 0.3276 0.3104 0.0106  0.0097  0.0009  172 HIS A NE2 
1349 N N   . VAL A 173 ? 0.2374 0.2367 0.2271 -0.0047 -0.0057 -0.0039 173 VAL A N   
1350 C CA  . VAL A 173 ? 0.2229 0.2235 0.2158 -0.0071 -0.0079 -0.0012 173 VAL A CA  
1351 C C   . VAL A 173 ? 0.2849 0.2893 0.2825 -0.0070 -0.0053 0.0013  173 VAL A C   
1352 O O   . VAL A 173 ? 0.2323 0.2381 0.2292 -0.0062 -0.0033 0.0012  173 VAL A O   
1353 C CB  . VAL A 173 ? 0.2219 0.2190 0.2087 -0.0094 -0.0121 0.0003  173 VAL A CB  
1354 C CG1 . VAL A 173 ? 0.2501 0.2404 0.2306 -0.0100 -0.0154 -0.0021 173 VAL A CG1 
1355 C CG2 . VAL A 173 ? 0.2451 0.2404 0.2250 -0.0089 -0.0115 0.0002  173 VAL A CG2 
1356 N N   . GLY A 174 ? 0.1888 0.1947 0.1911 -0.0073 -0.0049 0.0040  174 GLY A N   
1357 C CA  . GLY A 174 ? 0.2658 0.2727 0.2712 -0.0066 -0.0019 0.0062  174 GLY A CA  
1358 C C   . GLY A 174 ? 0.2207 0.2285 0.2300 -0.0056 -0.0008 0.0105  174 GLY A C   
1359 O O   . GLY A 174 ? 0.2086 0.2185 0.2197 -0.0061 -0.0030 0.0130  174 GLY A O   
1360 N N   . THR A 175 ? 0.2182 0.2239 0.2285 -0.0038 0.0029  0.0120  175 THR A N   
1361 C CA  . THR A 175 ? 0.2210 0.2269 0.2344 -0.0011 0.0059  0.0173  175 THR A CA  
1362 C C   . THR A 175 ? 0.1982 0.1960 0.2076 0.0018  0.0097  0.0156  175 THR A C   
1363 O O   . THR A 175 ? 0.2241 0.2160 0.2286 0.0004  0.0091  0.0106  175 THR A O   
1364 C CB  . THR A 175 ? 0.2420 0.2501 0.2581 -0.0004 0.0078  0.0217  175 THR A CB  
1365 O OG1 . THR A 175 ? 0.2487 0.2505 0.2611 -0.0002 0.0100  0.0188  175 THR A OG1 
1366 C CG2 . THR A 175 ? 0.1898 0.2046 0.2075 -0.0037 0.0036  0.0235  175 THR A CG2 
1367 N N   . ASP A 176 ? 0.2601 0.2572 0.2710 0.0058  0.0136  0.0206  176 ASP A N   
1368 C CA  . ASP A 176 ? 0.2521 0.2380 0.2557 0.0097  0.0185  0.0196  176 ASP A CA  
1369 C C   . ASP A 176 ? 0.2503 0.2304 0.2514 0.0104  0.0211  0.0203  176 ASP A C   
1370 O O   . ASP A 176 ? 0.2700 0.2566 0.2760 0.0078  0.0189  0.0216  176 ASP A O   
1371 C CB  . ASP A 176 ? 0.3155 0.3019 0.3205 0.0153  0.0232  0.0252  176 ASP A CB  
1372 C CG  . ASP A 176 ? 0.2910 0.2865 0.3052 0.0182  0.0258  0.0346  176 ASP A CG  
1373 O OD1 . ASP A 176 ? 0.2362 0.2334 0.2528 0.0171  0.0257  0.0362  176 ASP A OD1 
1374 O OD2 . ASP A 176 ? 0.2928 0.2947 0.3128 0.0216  0.0279  0.0415  176 ASP A OD2 
1375 N N   . LEU A 177 ? 0.2926 0.2590 0.2843 0.0138  0.0255  0.0195  177 LEU A N   
1376 C CA  . LEU A 177 ? 0.2754 0.2342 0.2635 0.0139  0.0273  0.0199  177 LEU A CA  
1377 C C   . LEU A 177 ? 0.2815 0.2440 0.2753 0.0193  0.0327  0.0277  177 LEU A C   
1378 O O   . LEU A 177 ? 0.3553 0.3120 0.3470 0.0201  0.0348  0.0291  177 LEU A O   
1379 C CB  . LEU A 177 ? 0.2773 0.2164 0.2504 0.0143  0.0288  0.0155  177 LEU A CB  
1380 C CG  . LEU A 177 ? 0.2875 0.2231 0.2567 0.0068  0.0222  0.0099  177 LEU A CG  
1381 C CD1 . LEU A 177 ? 0.2901 0.2315 0.2658 0.0032  0.0198  0.0113  177 LEU A CD1 
1382 C CD2 . LEU A 177 ? 0.3149 0.2612 0.2896 0.0034  0.0177  0.0072  177 LEU A CD2 
1383 N N   . GLU A 178 ? 0.2752 0.2476 0.2766 0.0229  0.0349  0.0339  178 GLU A N   
1384 C CA  . GLU A 178 ? 0.2570 0.2390 0.2682 0.0263  0.0383  0.0434  178 GLU A CA  
1385 C C   . GLU A 178 ? 0.2866 0.2838 0.3083 0.0201  0.0317  0.0453  178 GLU A C   
1386 O O   . GLU A 178 ? 0.2648 0.2720 0.2957 0.0212  0.0326  0.0538  178 GLU A O   
1387 C CB  . GLU A 178 ? 0.3517 0.3388 0.3677 0.0327  0.0433  0.0514  178 GLU A CB  
1388 C CG  . GLU A 178 ? 0.4852 0.4555 0.4880 0.0401  0.0508  0.0497  178 GLU A CG  
1389 C CD  . GLU A 178 ? 0.5962 0.5718 0.6045 0.0491  0.0587  0.0606  178 GLU A CD  
1390 O OE1 . GLU A 178 ? 0.5662 0.5588 0.5875 0.0476  0.0559  0.0672  178 GLU A OE1 
1391 O OE2 . GLU A 178 ? 0.6316 0.5933 0.6302 0.0579  0.0679  0.0631  178 GLU A OE2 
1392 N N   . GLY A 179 ? 0.2770 0.2758 0.2968 0.0140  0.0253  0.0382  179 GLY A N   
1393 C CA  . GLY A 179 ? 0.2140 0.2234 0.2395 0.0088  0.0197  0.0391  179 GLY A CA  
1394 C C   . GLY A 179 ? 0.2257 0.2454 0.2570 0.0062  0.0151  0.0429  179 GLY A C   
1395 O O   . GLY A 179 ? 0.2605 0.2869 0.2941 0.0018  0.0101  0.0442  179 GLY A O   
1396 N N   . ASN A 180 ? 0.2147 0.2349 0.2474 0.0085  0.0163  0.0449  180 ASN A N   
1397 C CA  . ASN A 180 ? 0.2566 0.2857 0.2948 0.0052  0.0109  0.0489  180 ASN A CA  
1398 C C   . ASN A 180 ? 0.2292 0.2543 0.2612 0.0013  0.0060  0.0401  180 ASN A C   
1399 O O   . ASN A 180 ? 0.2755 0.2939 0.3027 0.0033  0.0083  0.0346  180 ASN A O   
1400 C CB  . ASN A 180 ? 0.2409 0.2747 0.2856 0.0097  0.0147  0.0573  180 ASN A CB  
1401 C CG  . ASN A 180 ? 0.2798 0.3207 0.3331 0.0138  0.0193  0.0688  180 ASN A CG  
1402 O OD1 . ASN A 180 ? 0.3396 0.3895 0.3994 0.0097  0.0150  0.0750  180 ASN A OD1 
1403 N ND2 . ASN A 180 ? 0.2495 0.2856 0.3019 0.0219  0.0281  0.0721  180 ASN A ND2 
1404 N N   . PHE A 181 ? 0.2085 0.2367 0.2396 -0.0041 -0.0006 0.0392  181 PHE A N   
1405 C CA  . PHE A 181 ? 0.2047 0.2284 0.2294 -0.0069 -0.0046 0.0318  181 PHE A CA  
1406 C C   . PHE A 181 ? 0.2166 0.2408 0.2437 -0.0058 -0.0048 0.0328  181 PHE A C   
1407 O O   . PHE A 181 ? 0.2447 0.2753 0.2789 -0.0054 -0.0051 0.0410  181 PHE A O   
1408 C CB  . PHE A 181 ? 0.2452 0.2694 0.2659 -0.0122 -0.0115 0.0316  181 PHE A CB  
1409 C CG  . PHE A 181 ? 0.2327 0.2528 0.2463 -0.0127 -0.0112 0.0260  181 PHE A CG  
1410 C CD1 . PHE A 181 ? 0.2691 0.2833 0.2758 -0.0121 -0.0109 0.0183  181 PHE A CD1 
1411 C CD2 . PHE A 181 ? 0.2236 0.2469 0.2386 -0.0130 -0.0103 0.0295  181 PHE A CD2 
1412 C CE1 . PHE A 181 ? 0.2187 0.2307 0.2200 -0.0116 -0.0096 0.0147  181 PHE A CE1 
1413 C CE2 . PHE A 181 ? 0.2366 0.2572 0.2456 -0.0131 -0.0095 0.0253  181 PHE A CE2 
1414 C CZ  . PHE A 181 ? 0.2277 0.2428 0.2301 -0.0121 -0.0089 0.0181  181 PHE A CZ  
1415 N N   . TYR A 182 ? 0.2138 0.2322 0.2356 -0.0054 -0.0046 0.0253  182 TYR A N   
1416 C CA  . TYR A 182 ? 0.2471 0.2657 0.2698 -0.0061 -0.0070 0.0251  182 TYR A CA  
1417 C C   . TYR A 182 ? 0.2826 0.3016 0.3033 -0.0113 -0.0143 0.0256  182 TYR A C   
1418 O O   . TYR A 182 ? 0.2880 0.3022 0.3016 -0.0134 -0.0167 0.0207  182 TYR A O   
1419 C CB  . TYR A 182 ? 0.2596 0.2721 0.2772 -0.0046 -0.0050 0.0175  182 TYR A CB  
1420 C CG  . TYR A 182 ? 0.2095 0.2184 0.2259 -0.0004 0.0009  0.0173  182 TYR A CG  
1421 C CD1 . TYR A 182 ? 0.2283 0.2380 0.2469 0.0029  0.0038  0.0211  182 TYR A CD1 
1422 C CD2 . TYR A 182 ? 0.2190 0.2225 0.2309 0.0003  0.0036  0.0136  182 TYR A CD2 
1423 C CE1 . TYR A 182 ? 0.2303 0.2332 0.2439 0.0073  0.0095  0.0204  182 TYR A CE1 
1424 C CE2 . TYR A 182 ? 0.2760 0.2725 0.2835 0.0035  0.0082  0.0131  182 TYR A CE2 
1425 C CZ  . TYR A 182 ? 0.2260 0.2210 0.2330 0.0073  0.0114  0.0160  182 TYR A CZ  
1426 O OH  . TYR A 182 ? 0.2705 0.2551 0.2693 0.0110  0.0162  0.0150  182 TYR A OH  
1427 N N   . GLY A 183 ? 0.2557 0.2793 0.2819 -0.0133 -0.0179 0.0322  183 GLY A N   
1428 C CA  . GLY A 183 ? 0.2755 0.2973 0.2985 -0.0193 -0.0261 0.0337  183 GLY A CA  
1429 C C   . GLY A 183 ? 0.3042 0.3278 0.3261 -0.0233 -0.0302 0.0384  183 GLY A C   
1430 O O   . GLY A 183 ? 0.2573 0.2865 0.2842 -0.0212 -0.0264 0.0425  183 GLY A O   
1431 N N   . PRO A 184 ? 0.2662 0.2835 0.2798 -0.0293 -0.0382 0.0378  184 PRO A N   
1432 C CA  . PRO A 184 ? 0.3310 0.3492 0.3423 -0.0349 -0.0442 0.0436  184 PRO A CA  
1433 C C   . PRO A 184 ? 0.2855 0.2974 0.2862 -0.0342 -0.0427 0.0376  184 PRO A C   
1434 O O   . PRO A 184 ? 0.3304 0.3405 0.3257 -0.0394 -0.0485 0.0412  184 PRO A O   
1435 C CB  . PRO A 184 ? 0.3585 0.3691 0.3623 -0.0422 -0.0545 0.0451  184 PRO A CB  
1436 C CG  . PRO A 184 ? 0.3547 0.3549 0.3500 -0.0391 -0.0522 0.0349  184 PRO A CG  
1437 C CD  . PRO A 184 ? 0.2659 0.2738 0.2714 -0.0316 -0.0427 0.0327  184 PRO A CD  
1438 N N   . PHE A 185 ? 0.3009 0.3100 0.2990 -0.0284 -0.0354 0.0296  185 PHE A N   
1439 C CA  . PHE A 185 ? 0.2541 0.2571 0.2418 -0.0274 -0.0338 0.0241  185 PHE A CA  
1440 C C   . PHE A 185 ? 0.2880 0.2987 0.2816 -0.0270 -0.0315 0.0291  185 PHE A C   
1441 O O   . PHE A 185 ? 0.2839 0.3039 0.2899 -0.0251 -0.0281 0.0350  185 PHE A O   
1442 C CB  . PHE A 185 ? 0.2805 0.2799 0.2657 -0.0218 -0.0274 0.0158  185 PHE A CB  
1443 C CG  . PHE A 185 ? 0.2768 0.2696 0.2576 -0.0217 -0.0292 0.0116  185 PHE A CG  
1444 C CD1 . PHE A 185 ? 0.2861 0.2669 0.2527 -0.0239 -0.0338 0.0082  185 PHE A CD1 
1445 C CD2 . PHE A 185 ? 0.2595 0.2565 0.2490 -0.0194 -0.0265 0.0115  185 PHE A CD2 
1446 C CE1 . PHE A 185 ? 0.3587 0.3325 0.3210 -0.0235 -0.0353 0.0048  185 PHE A CE1 
1447 C CE2 . PHE A 185 ? 0.3146 0.3062 0.3008 -0.0195 -0.0283 0.0083  185 PHE A CE2 
1448 C CZ  . PHE A 185 ? 0.2848 0.2652 0.2582 -0.0215 -0.0326 0.0051  185 PHE A CZ  
1449 N N   . VAL A 186 ? 0.2350 0.2410 0.2185 -0.0285 -0.0331 0.0273  186 VAL A N   
1450 C CA  . VAL A 186 ? 0.2991 0.3116 0.2867 -0.0284 -0.0312 0.0317  186 VAL A CA  
1451 C C   . VAL A 186 ? 0.3083 0.3162 0.2876 -0.0249 -0.0267 0.0252  186 VAL A C   
1452 O O   . VAL A 186 ? 0.3220 0.3203 0.2889 -0.0239 -0.0271 0.0189  186 VAL A O   
1453 C CB  . VAL A 186 ? 0.3806 0.3941 0.3651 -0.0354 -0.0394 0.0392  186 VAL A CB  
1454 C CG1 . VAL A 186 ? 0.3342 0.3562 0.3312 -0.0386 -0.0432 0.0486  186 VAL A CG1 
1455 C CG2 . VAL A 186 ? 0.3245 0.3232 0.2889 -0.0394 -0.0459 0.0342  186 VAL A CG2 
1456 N N   . ASP A 187 ? 0.2399 0.2546 0.2262 -0.0225 -0.0221 0.0276  187 ASP A N   
1457 C CA  . ASP A 187 ? 0.2559 0.2685 0.2372 -0.0190 -0.0174 0.0230  187 ASP A CA  
1458 C C   . ASP A 187 ? 0.3194 0.3286 0.2892 -0.0214 -0.0205 0.0240  187 ASP A C   
1459 O O   . ASP A 187 ? 0.2847 0.2994 0.2576 -0.0215 -0.0191 0.0279  187 ASP A O   
1460 C CB  . ASP A 187 ? 0.2092 0.2287 0.2019 -0.0157 -0.0113 0.0246  187 ASP A CB  
1461 C CG  . ASP A 187 ? 0.2892 0.3161 0.2917 -0.0169 -0.0114 0.0324  187 ASP A CG  
1462 O OD1 . ASP A 187 ? 0.2531 0.2823 0.2557 -0.0207 -0.0165 0.0378  187 ASP A OD1 
1463 O OD2 . ASP A 187 ? 0.2542 0.2841 0.2641 -0.0140 -0.0065 0.0339  187 ASP A OD2 
1464 N N   A ARG A 188 ? 0.2880 0.2863 0.2427 -0.0233 -0.0249 0.0206  188 ARG A N   
1465 N N   B ARG A 188 ? 0.2878 0.2861 0.2424 -0.0231 -0.0247 0.0204  188 ARG A N   
1466 C CA  A ARG A 188 ? 0.3356 0.3253 0.2732 -0.0251 -0.0280 0.0199  188 ARG A CA  
1467 C CA  B ARG A 188 ? 0.3348 0.3248 0.2726 -0.0250 -0.0278 0.0199  188 ARG A CA  
1468 C C   A ARG A 188 ? 0.3759 0.3518 0.2968 -0.0216 -0.0265 0.0125  188 ARG A C   
1469 C C   B ARG A 188 ? 0.3765 0.3522 0.2971 -0.0218 -0.0268 0.0126  188 ARG A C   
1470 O O   A ARG A 188 ? 0.3485 0.3198 0.2693 -0.0213 -0.0275 0.0095  188 ARG A O   
1471 O O   B ARG A 188 ? 0.3478 0.3185 0.2677 -0.0220 -0.0284 0.0098  188 ARG A O   
1472 C CB  A ARG A 188 ? 0.3534 0.3405 0.2858 -0.0332 -0.0376 0.0255  188 ARG A CB  
1473 C CB  B ARG A 188 ? 0.3521 0.3403 0.2858 -0.0330 -0.0372 0.0259  188 ARG A CB  
1474 C CG  A ARG A 188 ? 0.3942 0.3932 0.3373 -0.0364 -0.0392 0.0342  188 ARG A CG  
1475 C CG  B ARG A 188 ? 0.4139 0.3928 0.3289 -0.0362 -0.0416 0.0263  188 ARG A CG  
1476 C CD  A ARG A 188 ? 0.2928 0.2945 0.2397 -0.0444 -0.0485 0.0424  188 ARG A CD  
1477 C CD  B ARG A 188 ? 0.4555 0.4299 0.3643 -0.0457 -0.0531 0.0320  188 ARG A CD  
1478 N NE  A ARG A 188 ? 0.4241 0.4106 0.3533 -0.0495 -0.0566 0.0393  188 ARG A NE  
1479 N NE  B ARG A 188 ? 0.3800 0.3358 0.2617 -0.0492 -0.0589 0.0289  188 ARG A NE  
1480 C CZ  A ARG A 188 ? 0.4408 0.4271 0.3712 -0.0574 -0.0661 0.0459  188 ARG A CZ  
1481 C CZ  B ARG A 188 ? 0.5463 0.4965 0.4179 -0.0586 -0.0697 0.0346  188 ARG A CZ  
1482 N NH1 A ARG A 188 ? 0.5285 0.5304 0.4774 -0.0609 -0.0685 0.0571  188 ARG A NH1 
1483 N NH1 B ARG A 188 ? 0.4996 0.4631 0.3881 -0.0655 -0.0760 0.0448  188 ARG A NH1 
1484 N NH2 A ARG A 188 ? 0.5641 0.5337 0.4767 -0.0619 -0.0733 0.0420  188 ARG A NH2 
1485 N NH2 B ARG A 188 ? 0.5582 0.4884 0.4014 -0.0610 -0.0742 0.0306  188 ARG A NH2 
1486 N N   . GLN A 189 ? 0.3641 0.3335 0.2711 -0.0182 -0.0234 0.0102  189 GLN A N   
1487 C CA  . GLN A 189 ? 0.4148 0.3692 0.3032 -0.0135 -0.0210 0.0041  189 GLN A CA  
1488 C C   . GLN A 189 ? 0.3810 0.3176 0.2479 -0.0192 -0.0297 0.0029  189 GLN A C   
1489 O O   . GLN A 189 ? 0.4999 0.4249 0.3470 -0.0198 -0.0316 0.0023  189 GLN A O   
1490 C CB  . GLN A 189 ? 0.3921 0.3462 0.2730 -0.0065 -0.0133 0.0032  189 GLN A CB  
1491 C CG  . GLN A 189 ? 0.4619 0.4041 0.3290 0.0010  -0.0077 -0.0018 189 GLN A CG  
1492 C CD  . GLN A 189 ? 0.5031 0.4490 0.3676 0.0095  0.0017  -0.0008 189 GLN A CD  
1493 O OE1 . GLN A 189 ? 0.5432 0.5042 0.4226 0.0099  0.0048  0.0035  189 GLN A OE1 
1494 N NE2 . GLN A 189 ? 0.5231 0.4546 0.3683 0.0166  0.0065  -0.0039 189 GLN A NE2 
1495 N N   . THR A 190 ? 0.4177 0.3515 0.2881 -0.0239 -0.0357 0.0029  190 THR A N   
1496 C CA  . THR A 190 ? 0.4254 0.3426 0.2777 -0.0312 -0.0459 0.0029  190 THR A CA  
1497 C C   . THR A 190 ? 0.4727 0.3837 0.3261 -0.0311 -0.0475 -0.0003 190 THR A C   
1498 O O   . THR A 190 ? 0.4520 0.3758 0.3246 -0.0277 -0.0425 -0.0004 190 THR A O   
1499 C CB  . THR A 190 ? 0.4175 0.3434 0.2782 -0.0409 -0.0551 0.0112  190 THR A CB  
1500 O OG1 . THR A 190 ? 0.5731 0.4808 0.4126 -0.0492 -0.0662 0.0119  190 THR A OG1 
1501 C CG2 . THR A 190 ? 0.4653 0.4085 0.3522 -0.0429 -0.0556 0.0164  190 THR A CG2 
1502 N N   . ALA A 191 ? 0.4811 0.3711 0.3124 -0.0353 -0.0548 -0.0028 191 ALA A N   
1503 C CA  . ALA A 191 ? 0.4947 0.3750 0.3230 -0.0345 -0.0560 -0.0065 191 ALA A CA  
1504 C C   . ALA A 191 ? 0.5353 0.4335 0.3897 -0.0381 -0.0583 -0.0017 191 ALA A C   
1505 O O   . ALA A 191 ? 0.4500 0.3567 0.3141 -0.0462 -0.0660 0.0056  191 ALA A O   
1506 C CB  . ALA A 191 ? 0.5328 0.3865 0.3329 -0.0411 -0.0662 -0.0084 191 ALA A CB  
1507 N N   . GLN A 192 ? 0.4572 0.3609 0.3223 -0.0318 -0.0514 -0.0050 192 GLN A N   
1508 C CA  . GLN A 192 ? 0.4447 0.3646 0.3332 -0.0331 -0.0515 -0.0013 192 GLN A CA  
1509 C C   . GLN A 192 ? 0.4892 0.4036 0.3769 -0.0280 -0.0475 -0.0065 192 GLN A C   
1510 O O   . GLN A 192 ? 0.5419 0.4579 0.4303 -0.0200 -0.0386 -0.0106 192 GLN A O   
1511 C CB  . GLN A 192 ? 0.4091 0.3496 0.3184 -0.0296 -0.0445 0.0017  192 GLN A CB  
1512 C CG  . GLN A 192 ? 0.5003 0.4482 0.4129 -0.0338 -0.0474 0.0075  192 GLN A CG  
1513 C CD  . GLN A 192 ? 0.4586 0.4246 0.3914 -0.0304 -0.0408 0.0107  192 GLN A CD  
1514 O OE1 . GLN A 192 ? 0.3306 0.3068 0.2791 -0.0305 -0.0400 0.0139  192 GLN A OE1 
1515 N NE2 . GLN A 192 ? 0.3932 0.3622 0.3246 -0.0271 -0.0359 0.0100  192 GLN A NE2 
1516 N N   . ALA A 193 ? 0.4776 0.3865 0.3650 -0.0328 -0.0541 -0.0052 193 ALA A N   
1517 C CA  . ALA A 193 ? 0.4651 0.3685 0.3520 -0.0285 -0.0511 -0.0095 193 ALA A CA  
1518 C C   . ALA A 193 ? 0.4733 0.3933 0.3826 -0.0301 -0.0514 -0.0053 193 ALA A C   
1519 O O   . ALA A 193 ? 0.4212 0.3497 0.3403 -0.0365 -0.0575 0.0015  193 ALA A O   
1520 C CB  . ALA A 193 ? 0.4263 0.3057 0.2908 -0.0318 -0.0581 -0.0123 193 ALA A CB  
1521 N N   . ALA A 194 ? 0.4074 0.3321 0.3245 -0.0240 -0.0447 -0.0085 194 ALA A N   
1522 C CA  . ALA A 194 ? 0.3717 0.3102 0.3073 -0.0245 -0.0442 -0.0052 194 ALA A CA  
1523 C C   . ALA A 194 ? 0.3871 0.3177 0.3198 -0.0290 -0.0513 -0.0038 194 ALA A C   
1524 O O   . ALA A 194 ? 0.4406 0.3533 0.3564 -0.0296 -0.0545 -0.0074 194 ALA A O   
1525 C CB  . ALA A 194 ? 0.4114 0.3573 0.3553 -0.0174 -0.0354 -0.0087 194 ALA A CB  
1526 N N   . GLY A 195 ? 0.3913 0.3346 0.3399 -0.0318 -0.0534 0.0020  195 GLY A N   
1527 C CA  . GLY A 195 ? 0.3758 0.3150 0.3254 -0.0358 -0.0596 0.0046  195 GLY A CA  
1528 C C   . GLY A 195 ? 0.4126 0.3494 0.3632 -0.0304 -0.0547 -0.0003 195 GLY A C   
1529 O O   . GLY A 195 ? 0.3317 0.2688 0.2808 -0.0238 -0.0471 -0.0056 195 GLY A O   
1530 N N   . THR A 196 ? 0.3519 0.2880 0.3066 -0.0336 -0.0596 0.0027  196 THR A N   
1531 C CA  . THR A 196 ? 0.3856 0.3191 0.3414 -0.0294 -0.0561 -0.0009 196 THR A CA  
1532 C C   . THR A 196 ? 0.3191 0.2684 0.2890 -0.0236 -0.0476 -0.0017 196 THR A C   
1533 O O   . THR A 196 ? 0.3602 0.3234 0.3428 -0.0244 -0.0465 0.0030  196 THR A O   
1534 C CB  . THR A 196 ? 0.3579 0.2908 0.3184 -0.0347 -0.0634 0.0043  196 THR A CB  
1535 O OG1 . THR A 196 ? 0.3807 0.2953 0.3254 -0.0411 -0.0726 0.0047  196 THR A OG1 
1536 C CG2 . THR A 196 ? 0.4024 0.3345 0.3659 -0.0301 -0.0595 0.0012  196 THR A CG2 
1537 N N   . ASP A 197 ? 0.3421 0.2886 0.3091 -0.0177 -0.0414 -0.0069 197 ASP A N   
1538 C CA  . ASP A 197 ? 0.4223 0.3822 0.4013 -0.0136 -0.0349 -0.0071 197 ASP A CA  
1539 C C   . ASP A 197 ? 0.4052 0.3688 0.3916 -0.0135 -0.0357 -0.0056 197 ASP A C   
1540 O O   . ASP A 197 ? 0.4853 0.4446 0.4694 -0.0104 -0.0335 -0.0081 197 ASP A O   
1541 C CB  . ASP A 197 ? 0.4359 0.3944 0.4109 -0.0081 -0.0284 -0.0113 197 ASP A CB  
1542 C CG  . ASP A 197 ? 0.5236 0.4953 0.5097 -0.0059 -0.0233 -0.0107 197 ASP A CG  
1543 O OD1 . ASP A 197 ? 0.3470 0.3272 0.3414 -0.0080 -0.0241 -0.0079 197 ASP A OD1 
1544 O OD2 . ASP A 197 ? 0.4762 0.4493 0.4619 -0.0021 -0.0186 -0.0124 197 ASP A OD2 
1545 N N   . THR A 198 ? 0.3097 0.2822 0.3056 -0.0165 -0.0382 -0.0005 198 THR A N   
1546 C CA  . THR A 198 ? 0.2857 0.2621 0.2885 -0.0166 -0.0391 0.0018  198 THR A CA  
1547 C C   . THR A 198 ? 0.3118 0.2971 0.3210 -0.0125 -0.0329 0.0003  198 THR A C   
1548 O O   . THR A 198 ? 0.2539 0.2427 0.2631 -0.0105 -0.0287 -0.0017 198 THR A O   
1549 C CB  . THR A 198 ? 0.3049 0.2882 0.3156 -0.0206 -0.0436 0.0092  198 THR A CB  
1550 O OG1 . THR A 198 ? 0.4547 0.4470 0.4706 -0.0199 -0.0407 0.0121  198 THR A OG1 
1551 C CG2 . THR A 198 ? 0.3673 0.3404 0.3711 -0.0265 -0.0520 0.0117  198 THR A CG2 
1552 N N   . THR A 199 ? 0.2479 0.2362 0.2620 -0.0120 -0.0330 0.0015  199 THR A N   
1553 C CA  . THR A 199 ? 0.2335 0.2290 0.2523 -0.0093 -0.0285 0.0006  199 THR A CA  
1554 C C   . THR A 199 ? 0.2436 0.2475 0.2684 -0.0095 -0.0274 0.0047  199 THR A C   
1555 O O   . THR A 199 ? 0.2460 0.2526 0.2750 -0.0112 -0.0303 0.0097  199 THR A O   
1556 C CB  . THR A 199 ? 0.2479 0.2420 0.2680 -0.0081 -0.0287 0.0000  199 THR A CB  
1557 O OG1 . THR A 199 ? 0.2726 0.2574 0.2857 -0.0063 -0.0283 -0.0032 199 THR A OG1 
1558 C CG2 . THR A 199 ? 0.2462 0.2477 0.2705 -0.0064 -0.0252 -0.0002 199 THR A CG2 
1559 N N   . ILE A 200 ? 0.2275 0.2347 0.2518 -0.0077 -0.0232 0.0033  200 ILE A N   
1560 C CA  . ILE A 200 ? 0.2462 0.2581 0.2723 -0.0065 -0.0206 0.0065  200 ILE A CA  
1561 C C   . ILE A 200 ? 0.2112 0.2261 0.2395 -0.0058 -0.0204 0.0080  200 ILE A C   
1562 O O   . ILE A 200 ? 0.1979 0.2123 0.2235 -0.0054 -0.0188 0.0055  200 ILE A O   
1563 C CB  . ILE A 200 ? 0.2120 0.2223 0.2334 -0.0052 -0.0168 0.0039  200 ILE A CB  
1564 C CG1 . ILE A 200 ? 0.2230 0.2307 0.2425 -0.0060 -0.0172 0.0020  200 ILE A CG1 
1565 C CG2 . ILE A 200 ? 0.2091 0.2209 0.2294 -0.0027 -0.0132 0.0074  200 ILE A CG2 
1566 C CD1 . ILE A 200 ? 0.2327 0.2382 0.2479 -0.0055 -0.0144 -0.0014 200 ILE A CD1 
1567 N N   . THR A 201 ? 0.1952 0.2139 0.2287 -0.0061 -0.0223 0.0132  201 THR A N   
1568 C CA  . THR A 201 ? 0.2536 0.2756 0.2900 -0.0057 -0.0228 0.0153  201 THR A CA  
1569 C C   . THR A 201 ? 0.2002 0.2231 0.2321 -0.0032 -0.0184 0.0151  201 THR A C   
1570 O O   . THR A 201 ? 0.2057 0.2284 0.2359 -0.0036 -0.0186 0.0133  201 THR A O   
1571 C CB  . THR A 201 ? 0.2273 0.2541 0.2709 -0.0067 -0.0257 0.0224  201 THR A CB  
1572 O OG1 . THR A 201 ? 0.2479 0.2704 0.2923 -0.0101 -0.0307 0.0222  201 THR A OG1 
1573 C CG2 . THR A 201 ? 0.1893 0.2192 0.2367 -0.0068 -0.0270 0.0245  201 THR A CG2 
1574 N N   . VAL A 202 ? 0.2080 0.2308 0.2368 -0.0004 -0.0144 0.0172  202 VAL A N   
1575 C CA  . VAL A 202 ? 0.2168 0.2366 0.2374 0.0024  -0.0100 0.0168  202 VAL A CA  
1576 C C   . VAL A 202 ? 0.2628 0.2762 0.2756 0.0001  -0.0107 0.0104  202 VAL A C   
1577 O O   . VAL A 202 ? 0.2189 0.2293 0.2250 -0.0001 -0.0103 0.0094  202 VAL A O   
1578 C CB  . VAL A 202 ? 0.2237 0.2420 0.2404 0.0069  -0.0045 0.0203  202 VAL A CB  
1579 C CG1 . VAL A 202 ? 0.2684 0.2826 0.2828 0.0062  -0.0040 0.0171  202 VAL A CG1 
1580 C CG2 . VAL A 202 ? 0.2442 0.2558 0.2487 0.0108  0.0005  0.0199  202 VAL A CG2 
1581 N N   . ASN A 203 ? 0.2173 0.2289 0.2309 -0.0020 -0.0122 0.0069  203 ASN A N   
1582 C CA  . ASN A 203 ? 0.1838 0.1914 0.1921 -0.0046 -0.0133 0.0027  203 ASN A CA  
1583 C C   . ASN A 203 ? 0.1806 0.1920 0.1935 -0.0069 -0.0166 0.0026  203 ASN A C   
1584 O O   . ASN A 203 ? 0.2035 0.2134 0.2121 -0.0092 -0.0177 0.0018  203 ASN A O   
1585 C CB  . ASN A 203 ? 0.2073 0.2132 0.2161 -0.0055 -0.0134 0.0001  203 ASN A CB  
1586 C CG  . ASN A 203 ? 0.2393 0.2405 0.2424 -0.0036 -0.0100 0.0001  203 ASN A CG  
1587 O OD1 . ASN A 203 ? 0.2443 0.2424 0.2421 -0.0007 -0.0069 0.0021  203 ASN A OD1 
1588 N ND2 . ASN A 203 ? 0.2460 0.2463 0.2497 -0.0044 -0.0101 -0.0017 203 ASN A ND2 
1589 N N   . VAL A 204 ? 0.2054 0.2210 0.2263 -0.0067 -0.0184 0.0039  204 VAL A N   
1590 C CA  . VAL A 204 ? 0.1798 0.1988 0.2054 -0.0079 -0.0207 0.0046  204 VAL A CA  
1591 C C   . VAL A 204 ? 0.1847 0.2055 0.2083 -0.0082 -0.0209 0.0069  204 VAL A C   
1592 O O   . VAL A 204 ? 0.2075 0.2297 0.2302 -0.0103 -0.0224 0.0071  204 VAL A O   
1593 C CB  . VAL A 204 ? 0.1739 0.1937 0.2059 -0.0071 -0.0225 0.0056  204 VAL A CB  
1594 C CG1 . VAL A 204 ? 0.1987 0.2214 0.2354 -0.0074 -0.0240 0.0072  204 VAL A CG1 
1595 C CG2 . VAL A 204 ? 0.1712 0.1872 0.2020 -0.0067 -0.0222 0.0030  204 VAL A CG2 
1596 N N   . LEU A 205 ? 0.1885 0.2097 0.2110 -0.0061 -0.0193 0.0094  205 LEU A N   
1597 C CA  . LEU A 205 ? 0.1862 0.2085 0.2051 -0.0055 -0.0187 0.0119  205 LEU A CA  
1598 C C   . LEU A 205 ? 0.1900 0.2054 0.1964 -0.0069 -0.0179 0.0094  205 LEU A C   
1599 O O   . LEU A 205 ? 0.2114 0.2268 0.2144 -0.0092 -0.0199 0.0100  205 LEU A O   
1600 C CB  . LEU A 205 ? 0.2078 0.2321 0.2276 -0.0018 -0.0158 0.0163  205 LEU A CB  
1601 C CG  . LEU A 205 ? 0.2271 0.2582 0.2591 -0.0019 -0.0183 0.0205  205 LEU A CG  
1602 C CD1 . LEU A 205 ? 0.2077 0.2427 0.2427 0.0013  -0.0157 0.0267  205 LEU A CD1 
1603 C CD2 . LEU A 205 ? 0.2212 0.2565 0.2585 -0.0035 -0.0213 0.0222  205 LEU A CD2 
1604 N N   . ALA A 206 ? 0.1949 0.2035 0.1938 -0.0063 -0.0157 0.0068  206 ALA A N   
1605 C CA  . ALA A 206 ? 0.2139 0.2129 0.1989 -0.0086 -0.0161 0.0043  206 ALA A CA  
1606 C C   . ALA A 206 ? 0.2710 0.2727 0.2589 -0.0143 -0.0211 0.0037  206 ALA A C   
1607 O O   . ALA A 206 ? 0.2320 0.2295 0.2113 -0.0179 -0.0239 0.0041  206 ALA A O   
1608 C CB  . ALA A 206 ? 0.2119 0.2029 0.1897 -0.0072 -0.0133 0.0018  206 ALA A CB  
1609 N N   . TRP A 207 ? 0.1950 0.2035 0.1944 -0.0150 -0.0224 0.0037  207 TRP A N   
1610 C CA  . TRP A 207 ? 0.2403 0.2534 0.2446 -0.0193 -0.0261 0.0051  207 TRP A CA  
1611 C C   . TRP A 207 ? 0.2692 0.2889 0.2791 -0.0205 -0.0285 0.0086  207 TRP A C   
1612 O O   . TRP A 207 ? 0.2184 0.2405 0.2282 -0.0250 -0.0322 0.0112  207 TRP A O   
1613 C CB  . TRP A 207 ? 0.2558 0.2735 0.2697 -0.0179 -0.0252 0.0047  207 TRP A CB  
1614 C CG  . TRP A 207 ? 0.3007 0.3257 0.3230 -0.0199 -0.0272 0.0078  207 TRP A CG  
1615 C CD1 . TRP A 207 ? 0.2621 0.2883 0.2840 -0.0240 -0.0294 0.0098  207 TRP A CD1 
1616 C CD2 . TRP A 207 ? 0.2129 0.2448 0.2457 -0.0174 -0.0266 0.0104  207 TRP A CD2 
1617 N NE1 . TRP A 207 ? 0.2430 0.2786 0.2760 -0.0237 -0.0298 0.0144  207 TRP A NE1 
1618 C CE2 . TRP A 207 ? 0.1992 0.2375 0.2382 -0.0191 -0.0276 0.0144  207 TRP A CE2 
1619 C CE3 . TRP A 207 ? 0.2585 0.2913 0.2959 -0.0138 -0.0254 0.0103  207 TRP A CE3 
1620 C CZ2 . TRP A 207 ? 0.2682 0.3134 0.3173 -0.0160 -0.0261 0.0183  207 TRP A CZ2 
1621 C CZ3 . TRP A 207 ? 0.2795 0.3170 0.3253 -0.0115 -0.0247 0.0131  207 TRP A CZ3 
1622 C CH2 . TRP A 207 ? 0.2461 0.2895 0.2974 -0.0120 -0.0244 0.0170  207 TRP A CH2 
1623 N N   . LEU A 208 ? 0.1862 0.2094 0.2013 -0.0170 -0.0269 0.0097  208 LEU A N   
1624 C CA  . LEU A 208 ? 0.1874 0.2163 0.2070 -0.0180 -0.0290 0.0132  208 LEU A CA  
1625 C C   . LEU A 208 ? 0.2140 0.2379 0.2212 -0.0208 -0.0306 0.0138  208 LEU A C   
1626 O O   . LEU A 208 ? 0.2173 0.2448 0.2252 -0.0245 -0.0342 0.0169  208 LEU A O   
1627 C CB  . LEU A 208 ? 0.2242 0.2567 0.2513 -0.0141 -0.0275 0.0146  208 LEU A CB  
1628 C CG  . LEU A 208 ? 0.2512 0.2864 0.2884 -0.0123 -0.0273 0.0144  208 LEU A CG  
1629 C CD1 . LEU A 208 ? 0.2866 0.3231 0.3294 -0.0100 -0.0273 0.0162  208 LEU A CD1 
1630 C CD2 . LEU A 208 ? 0.2398 0.2800 0.2838 -0.0135 -0.0287 0.0166  208 LEU A CD2 
1631 N N   . TYR A 209 ? 0.2338 0.2484 0.2282 -0.0187 -0.0278 0.0114  209 TYR A N   
1632 C CA  . TYR A 209 ? 0.2393 0.2446 0.2169 -0.0209 -0.0289 0.0112  209 TYR A CA  
1633 C C   . TYR A 209 ? 0.2510 0.2511 0.2213 -0.0280 -0.0341 0.0106  209 TYR A C   
1634 O O   . TYR A 209 ? 0.2602 0.2579 0.2230 -0.0329 -0.0385 0.0126  209 TYR A O   
1635 C CB  . TYR A 209 ? 0.2379 0.2322 0.2019 -0.0159 -0.0235 0.0090  209 TYR A CB  
1636 C CG  . TYR A 209 ? 0.2591 0.2582 0.2266 -0.0098 -0.0190 0.0121  209 TYR A CG  
1637 C CD1 . TYR A 209 ? 0.2853 0.2848 0.2475 -0.0096 -0.0195 0.0149  209 TYR A CD1 
1638 C CD2 . TYR A 209 ? 0.2504 0.2540 0.2267 -0.0047 -0.0149 0.0133  209 TYR A CD2 
1639 C CE1 . TYR A 209 ? 0.2527 0.2578 0.2193 -0.0039 -0.0153 0.0191  209 TYR A CE1 
1640 C CE2 . TYR A 209 ? 0.2451 0.2546 0.2265 0.0002  -0.0115 0.0180  209 TYR A CE2 
1641 C CZ  . TYR A 209 ? 0.2837 0.2942 0.2605 0.0009  -0.0114 0.0210  209 TYR A CZ  
1642 O OH  . TYR A 209 ? 0.2939 0.3117 0.2770 0.0059  -0.0079 0.0269  209 TYR A OH  
1643 N N   . ALA A 210 ? 0.2256 0.2245 0.1986 -0.0292 -0.0342 0.0087  210 ALA A N   
1644 C CA  . ALA A 210 ? 0.2324 0.2290 0.2018 -0.0367 -0.0400 0.0100  210 ALA A CA  
1645 C C   . ALA A 210 ? 0.2608 0.2704 0.2432 -0.0409 -0.0447 0.0158  210 ALA A C   
1646 O O   . ALA A 210 ? 0.2723 0.2801 0.2487 -0.0483 -0.0510 0.0191  210 ALA A O   
1647 C CB  . ALA A 210 ? 0.2427 0.2392 0.2166 -0.0366 -0.0389 0.0083  210 ALA A CB  
1648 N N   . ALA A 211 ? 0.2218 0.2439 0.2215 -0.0366 -0.0420 0.0178  211 ALA A N   
1649 C CA  . ALA A 211 ? 0.2332 0.2678 0.2460 -0.0390 -0.0452 0.0241  211 ALA A CA  
1650 C C   . ALA A 211 ? 0.2972 0.3312 0.3034 -0.0425 -0.0488 0.0268  211 ALA A C   
1651 O O   . ALA A 211 ? 0.2931 0.3319 0.3009 -0.0489 -0.0545 0.0324  211 ALA A O   
1652 C CB  . ALA A 211 ? 0.2799 0.3237 0.3084 -0.0325 -0.0408 0.0248  211 ALA A CB  
1653 N N   . VAL A 212 ? 0.2258 0.2547 0.2249 -0.0383 -0.0457 0.0239  212 VAL A N   
1654 C CA  . VAL A 212 ? 0.2719 0.2998 0.2635 -0.0408 -0.0484 0.0265  212 VAL A CA  
1655 C C   . VAL A 212 ? 0.3079 0.3241 0.2806 -0.0485 -0.0542 0.0265  212 VAL A C   
1656 O O   . VAL A 212 ? 0.3564 0.3758 0.3278 -0.0551 -0.0604 0.0314  212 VAL A O   
1657 C CB  . VAL A 212 ? 0.2593 0.2831 0.2453 -0.0342 -0.0432 0.0240  212 VAL A CB  
1658 C CG1 . VAL A 212 ? 0.2359 0.2559 0.2097 -0.0366 -0.0456 0.0263  212 VAL A CG1 
1659 C CG2 . VAL A 212 ? 0.2501 0.2851 0.2545 -0.0287 -0.0397 0.0255  212 VAL A CG2 
1660 N N   . ILE A 213 ? 0.2665 0.2678 0.2232 -0.0482 -0.0527 0.0212  213 ILE A N   
1661 C CA  . ILE A 213 ? 0.3069 0.2926 0.2420 -0.0559 -0.0586 0.0204  213 ILE A CA  
1662 C C   . ILE A 213 ? 0.4190 0.4128 0.3627 -0.0655 -0.0671 0.0266  213 ILE A C   
1663 O O   . ILE A 213 ? 0.4332 0.4192 0.3632 -0.0744 -0.0750 0.0294  213 ILE A O   
1664 C CB  . ILE A 213 ? 0.4001 0.3689 0.3196 -0.0532 -0.0549 0.0140  213 ILE A CB  
1665 C CG1 . ILE A 213 ? 0.3190 0.2795 0.2280 -0.0438 -0.0466 0.0101  213 ILE A CG1 
1666 C CG2 . ILE A 213 ? 0.4498 0.4004 0.3468 -0.0621 -0.0621 0.0132  213 ILE A CG2 
1667 C CD1 . ILE A 213 ? 0.3438 0.2930 0.2446 -0.0384 -0.0407 0.0052  213 ILE A CD1 
1668 N N   . ASN A 214 ? 0.3503 0.4223 0.2993 -0.0562 -0.0142 -0.0195 214 ASN A N   
1669 C CA  . ASN A 214 ? 0.4233 0.5125 0.3748 -0.0586 -0.0210 -0.0167 214 ASN A CA  
1670 C C   . ASN A 214 ? 0.4098 0.5144 0.3525 -0.0535 -0.0281 -0.0098 214 ASN A C   
1671 O O   . ASN A 214 ? 0.4285 0.5508 0.3746 -0.0549 -0.0342 -0.0073 214 ASN A O   
1672 C CB  . ASN A 214 ? 0.3726 0.4626 0.3389 -0.0551 -0.0211 -0.0114 214 ASN A CB  
1673 C CG  . ASN A 214 ? 0.4639 0.5452 0.4401 -0.0632 -0.0168 -0.0166 214 ASN A CG  
1674 O OD1 . ASN A 214 ? 0.4460 0.5109 0.4279 -0.0622 -0.0110 -0.0184 214 ASN A OD1 
1675 N ND2 . ASN A 214 ? 0.4929 0.5851 0.4723 -0.0716 -0.0195 -0.0190 214 ASN A ND2 
1676 N N   . GLY A 215 ? 0.3994 0.4982 0.3325 -0.0476 -0.0275 -0.0062 215 GLY A N   
1677 C CA  . GLY A 215 ? 0.3809 0.4919 0.3057 -0.0426 -0.0342 0.0016  215 GLY A CA  
1678 C C   . GLY A 215 ? 0.3543 0.4639 0.2854 -0.0302 -0.0355 0.0106  215 GLY A C   
1679 O O   . GLY A 215 ? 0.3998 0.5177 0.3266 -0.0243 -0.0407 0.0182  215 GLY A O   
1680 N N   . ASP A 216 ? 0.3086 0.4081 0.2496 -0.0263 -0.0311 0.0101  216 ASP A N   
1681 C CA  . ASP A 216 ? 0.3260 0.4214 0.2715 -0.0159 -0.0308 0.0159  216 ASP A CA  
1682 C C   . ASP A 216 ? 0.4678 0.5465 0.4055 -0.0141 -0.0267 0.0165  216 ASP A C   
1683 O O   . ASP A 216 ? 0.5049 0.5719 0.4457 -0.0161 -0.0215 0.0126  216 ASP A O   
1684 C CB  . ASP A 216 ? 0.3072 0.4016 0.2644 -0.0146 -0.0283 0.0145  216 ASP A CB  
1685 C CG  . ASP A 216 ? 0.6083 0.7205 0.5740 -0.0149 -0.0317 0.0157  216 ASP A CG  
1686 O OD1 . ASP A 216 ? 0.6870 0.8102 0.6522 -0.0217 -0.0347 0.0139  216 ASP A OD1 
1687 O OD2 . ASP A 216 ? 0.6278 0.7440 0.6006 -0.0093 -0.0308 0.0178  216 ASP A OD2 
1688 N N   . ARG A 217 ? 0.3345 0.4130 0.2632 -0.0104 -0.0291 0.0224  217 ARG A N   
1689 C CA  . ARG A 217 ? 0.3675 0.4313 0.2870 -0.0107 -0.0249 0.0238  217 ARG A CA  
1690 C C   . ARG A 217 ? 0.3551 0.4094 0.2762 -0.0018 -0.0245 0.0305  217 ARG A C   
1691 O O   . ARG A 217 ? 0.3918 0.4330 0.3065 -0.0026 -0.0205 0.0323  217 ARG A O   
1692 C CB  . ARG A 217 ? 0.3826 0.4513 0.2865 -0.0163 -0.0269 0.0257  217 ARG A CB  
1693 C CG  . ARG A 217 ? 0.4061 0.4763 0.3045 -0.0274 -0.0234 0.0159  217 ARG A CG  
1694 C CD  . ARG A 217 ? 0.4903 0.5641 0.3692 -0.0338 -0.0240 0.0171  217 ARG A CD  
1695 N N   . TRP A 218 ? 0.3716 0.4316 0.3018 0.0062  -0.0275 0.0336  218 TRP A N   
1696 C CA  . TRP A 218 ? 0.3500 0.4005 0.2816 0.0152  -0.0271 0.0399  218 TRP A CA  
1697 C C   . TRP A 218 ? 0.3079 0.3399 0.2406 0.0146  -0.0209 0.0364  218 TRP A C   
1698 O O   . TRP A 218 ? 0.3458 0.3648 0.2761 0.0187  -0.0192 0.0412  218 TRP A O   
1699 C CB  . TRP A 218 ? 0.3623 0.4234 0.3058 0.0240  -0.0299 0.0414  218 TRP A CB  
1700 C CG  . TRP A 218 ? 0.3438 0.4071 0.2965 0.0235  -0.0268 0.0337  218 TRP A CG  
1701 C CD1 . TRP A 218 ? 0.3643 0.4431 0.3229 0.0199  -0.0283 0.0300  218 TRP A CD1 
1702 C CD2 . TRP A 218 ? 0.3089 0.3596 0.2650 0.0256  -0.0220 0.0292  218 TRP A CD2 
1703 N NE1 . TRP A 218 ? 0.2992 0.3757 0.2635 0.0200  -0.0247 0.0250  218 TRP A NE1 
1704 C CE2 . TRP A 218 ? 0.3794 0.4398 0.3418 0.0233  -0.0211 0.0238  218 TRP A CE2 
1705 C CE3 . TRP A 218 ? 0.3494 0.3817 0.3033 0.0280  -0.0182 0.0293  218 TRP A CE3 
1706 C CZ2 . TRP A 218 ? 0.3214 0.3756 0.2863 0.0235  -0.0175 0.0185  218 TRP A CZ2 
1707 C CZ3 . TRP A 218 ? 0.4231 0.4488 0.3808 0.0277  -0.0144 0.0225  218 TRP A CZ3 
1708 C CH2 . TRP A 218 ? 0.3278 0.3653 0.2902 0.0255  -0.0144 0.0173  218 TRP A CH2 
1709 N N   . PHE A 219 ? 0.3032 0.3340 0.2401 0.0092  -0.0177 0.0288  219 PHE A N   
1710 C CA  . PHE A 219 ? 0.3247 0.3423 0.2647 0.0080  -0.0130 0.0251  219 PHE A CA  
1711 C C   . PHE A 219 ? 0.3526 0.3603 0.2864 0.0017  -0.0088 0.0250  219 PHE A C   
1712 O O   . PHE A 219 ? 0.3265 0.3239 0.2633 -0.0001 -0.0049 0.0228  219 PHE A O   
1713 C CB  . PHE A 219 ? 0.3240 0.3476 0.2724 0.0054  -0.0127 0.0189  219 PHE A CB  
1714 C CG  . PHE A 219 ? 0.2798 0.3107 0.2290 -0.0008 -0.0129 0.0165  219 PHE A CG  
1715 C CD1 . PHE A 219 ? 0.2922 0.3168 0.2420 -0.0064 -0.0090 0.0134  219 PHE A CD1 
1716 C CD2 . PHE A 219 ? 0.2952 0.3389 0.2457 -0.0013 -0.0163 0.0167  219 PHE A CD2 
1717 C CE1 . PHE A 219 ? 0.3124 0.3413 0.2644 -0.0116 -0.0080 0.0101  219 PHE A CE1 
1718 C CE2 . PHE A 219 ? 0.2902 0.3378 0.2419 -0.0078 -0.0158 0.0135  219 PHE A CE2 
1719 C CZ  . PHE A 219 ? 0.2752 0.3143 0.2275 -0.0125 -0.0113 0.0099  219 PHE A CZ  
1720 N N   . LEU A 220 ? 0.3750 0.3870 0.3004 -0.0027 -0.0089 0.0264  220 LEU A N   
1721 C CA  . LEU A 220 ? 0.3123 0.3164 0.2306 -0.0088 -0.0036 0.0262  220 LEU A CA  
1722 C C   . LEU A 220 ? 0.4864 0.4780 0.3986 -0.0062 -0.0021 0.0337  220 LEU A C   
1723 O O   . LEU A 220 ? 0.4799 0.4723 0.3859 -0.0014 -0.0061 0.0418  220 LEU A O   
1724 C CB  . LEU A 220 ? 0.3725 0.3852 0.2802 -0.0142 -0.0040 0.0255  220 LEU A CB  
1725 C CG  . LEU A 220 ? 0.3184 0.3398 0.2322 -0.0185 -0.0038 0.0171  220 LEU A CG  
1726 C CD1 . LEU A 220 ? 0.3309 0.3598 0.2322 -0.0251 -0.0039 0.0148  220 LEU A CD1 
1727 C CD2 . LEU A 220 ? 0.3631 0.3783 0.2877 -0.0213 0.0024  0.0106  220 LEU A CD2 
1728 N N   . ASN A 221 ? 0.4415 0.4219 0.3571 -0.0094 0.0035  0.0318  221 ASN A N   
1729 C CA  . ASN A 221 ? 0.4974 0.4634 0.4077 -0.0087 0.0061  0.0390  221 ASN A CA  
1730 C C   . ASN A 221 ? 0.4722 0.4348 0.3735 -0.0172 0.0126  0.0403  221 ASN A C   
1731 O O   . ASN A 221 ? 0.4414 0.4133 0.3400 -0.0225 0.0149  0.0352  221 ASN A O   
1732 C CB  . ASN A 221 ? 0.4229 0.3781 0.3439 -0.0068 0.0078  0.0355  221 ASN A CB  
1733 C CG  . ASN A 221 ? 0.5267 0.4849 0.4573 -0.0131 0.0113  0.0267  221 ASN A CG  
1734 O OD1 . ASN A 221 ? 0.5202 0.4817 0.4497 -0.0195 0.0156  0.0249  221 ASN A OD1 
1735 N ND2 . ASN A 221 ? 0.6196 0.5784 0.5599 -0.0112 0.0095  0.0211  221 ASN A ND2 
1736 N N   . ARG A 222 ? 0.6605 0.6092 0.5572 -0.0189 0.0164  0.0471  222 ARG A N   
1737 C CA  . ARG A 222 ? 0.6123 0.5588 0.4993 -0.0276 0.0236  0.0492  222 ARG A CA  
1738 C C   . ARG A 222 ? 0.6059 0.5439 0.5034 -0.0336 0.0310  0.0447  222 ARG A C   
1739 O O   . ARG A 222 ? 0.5101 0.4408 0.4011 -0.0402 0.0377  0.0494  222 ARG A O   
1740 C CB  . ARG A 222 ? 0.8868 0.8266 0.7573 -0.0269 0.0225  0.0632  222 ARG A CB  
1741 C CG  . ARG A 222 ? 0.8240 0.7464 0.6985 -0.0209 0.0210  0.0718  222 ARG A CG  
1742 C CD  . ARG A 222 ? 1.0391 0.9612 0.9029 -0.0137 0.0142  0.0858  222 ARG A CD  
1743 N NE  . ARG A 222 ? 1.1214 1.0234 0.9907 -0.0075 0.0144  0.0947  222 ARG A NE  
1744 C CZ  . ARG A 222 ? 1.2391 1.1338 1.1234 0.0002  0.0127  0.0895  222 ARG A CZ  
1745 N NH1 . ARG A 222 ? 1.2793 1.1864 1.1736 0.0024  0.0102  0.0769  222 ARG A NH1 
1746 N NH2 . ARG A 222 ? 1.1489 1.0226 1.0378 0.0054  0.0143  0.0970  222 ARG A NH2 
1747 N N   . PHE A 223 ? 0.4799 0.4207 0.3933 -0.0322 0.0296  0.0359  223 PHE A N   
1748 C CA  . PHE A 223 ? 0.4152 0.3533 0.3411 -0.0384 0.0350  0.0303  223 PHE A CA  
1749 C C   . PHE A 223 ? 0.3786 0.3317 0.3143 -0.0419 0.0378  0.0217  223 PHE A C   
1750 O O   . PHE A 223 ? 0.3700 0.3331 0.3043 -0.0389 0.0350  0.0188  223 PHE A O   
1751 C CB  . PHE A 223 ? 0.4861 0.4179 0.4229 -0.0352 0.0311  0.0265  223 PHE A CB  
1752 C CG  . PHE A 223 ? 0.5460 0.4640 0.4762 -0.0285 0.0277  0.0330  223 PHE A CG  
1753 C CD1 . PHE A 223 ? 0.4841 0.4039 0.4191 -0.0210 0.0219  0.0295  223 PHE A CD1 
1754 C CD2 . PHE A 223 ? 0.6331 0.5371 0.5528 -0.0292 0.0308  0.0435  223 PHE A CD2 
1755 C CE1 . PHE A 223 ? 0.6103 0.5178 0.5420 -0.0135 0.0199  0.0348  223 PHE A CE1 
1756 C CE2 . PHE A 223 ? 0.5813 0.4720 0.4978 -0.0214 0.0277  0.0506  223 PHE A CE2 
1757 C CZ  . PHE A 223 ? 0.7070 0.5996 0.6307 -0.0131 0.0226  0.0456  223 PHE A CZ  
1758 N N   . THR A 224 ? 0.3309 0.2854 0.2781 -0.0484 0.0437  0.0178  224 THR A N   
1759 C CA  . THR A 224 ? 0.3391 0.3077 0.3020 -0.0499 0.0457  0.0100  224 THR A CA  
1760 C C   . THR A 224 ? 0.3673 0.3378 0.3475 -0.0525 0.0441  0.0064  224 THR A C   
1761 O O   . THR A 224 ? 0.3425 0.3022 0.3204 -0.0535 0.0419  0.0083  224 THR A O   
1762 C CB  . THR A 224 ? 0.3608 0.3350 0.3222 -0.0558 0.0557  0.0081  224 THR A CB  
1763 O OG1 . THR A 224 ? 0.3625 0.3498 0.3395 -0.0543 0.0572  0.0005  224 THR A OG1 
1764 C CG2 . THR A 224 ? 0.3691 0.3391 0.3343 -0.0642 0.0638  0.0099  224 THR A CG2 
1765 N N   . THR A 225 ? 0.3193 0.3037 0.3173 -0.0535 0.0449  0.0010  225 THR A N   
1766 C CA  . THR A 225 ? 0.2932 0.2839 0.3084 -0.0571 0.0425  -0.0022 225 THR A CA  
1767 C C   . THR A 225 ? 0.3224 0.3294 0.3578 -0.0593 0.0472  -0.0059 225 THR A C   
1768 O O   . THR A 225 ? 0.3211 0.3317 0.3562 -0.0581 0.0536  -0.0071 225 THR A O   
1769 C CB  . THR A 225 ? 0.3471 0.3403 0.3644 -0.0522 0.0321  -0.0036 225 THR A CB  
1770 O OG1 . THR A 225 ? 0.3779 0.3779 0.4091 -0.0575 0.0294  -0.0069 225 THR A OG1 
1771 C CG2 . THR A 225 ? 0.3094 0.3142 0.3328 -0.0458 0.0280  -0.0043 225 THR A CG2 
1772 N N   . THR A 226 ? 0.3081 0.3257 0.3619 -0.0626 0.0440  -0.0083 226 THR A N   
1773 C CA  . THR A 226 ? 0.2724 0.3088 0.3507 -0.0629 0.0461  -0.0109 226 THR A CA  
1774 C C   . THR A 226 ? 0.2990 0.3471 0.3889 -0.0571 0.0352  -0.0104 226 THR A C   
1775 O O   . THR A 226 ? 0.2939 0.3374 0.3739 -0.0558 0.0266  -0.0095 226 THR A O   
1776 C CB  . THR A 226 ? 0.2919 0.3364 0.3857 -0.0722 0.0503  -0.0127 226 THR A CB  
1777 O OG1 . THR A 226 ? 0.3218 0.3651 0.4154 -0.0762 0.0416  -0.0134 226 THR A OG1 
1778 C CG2 . THR A 226 ? 0.3188 0.3517 0.4011 -0.0793 0.0617  -0.0116 226 THR A CG2 
1779 N N   . LEU A 227 ? 0.3113 0.3752 0.4234 -0.0538 0.0361  -0.0108 227 LEU A N   
1780 C CA  . LEU A 227 ? 0.2593 0.3359 0.3845 -0.0486 0.0257  -0.0080 227 LEU A CA  
1781 C C   . LEU A 227 ? 0.3219 0.4069 0.4504 -0.0543 0.0165  -0.0078 227 LEU A C   
1782 O O   . LEU A 227 ? 0.2911 0.3763 0.4110 -0.0522 0.0069  -0.0060 227 LEU A O   
1783 C CB  . LEU A 227 ? 0.3006 0.3928 0.4534 -0.0440 0.0292  -0.0074 227 LEU A CB  
1784 C CG  . LEU A 227 ? 0.3912 0.4892 0.5539 -0.0351 0.0219  -0.0026 227 LEU A CG  
1785 C CD1 . LEU A 227 ? 0.2663 0.3480 0.4056 -0.0312 0.0200  -0.0018 227 LEU A CD1 
1786 C CD2 . LEU A 227 ? 0.4551 0.5620 0.6441 -0.0296 0.0295  -0.0033 227 LEU A CD2 
1787 N N   . ASN A 228 ? 0.2825 0.3750 0.4226 -0.0626 0.0198  -0.0105 228 ASN A N   
1788 C CA  . ASN A 228 ? 0.2656 0.3679 0.4099 -0.0697 0.0108  -0.0119 228 ASN A CA  
1789 C C   . ASN A 228 ? 0.2994 0.3828 0.4178 -0.0728 0.0078  -0.0147 228 ASN A C   
1790 O O   . ASN A 228 ? 0.3170 0.4056 0.4310 -0.0745 -0.0018 -0.0159 228 ASN A O   
1791 C CB  . ASN A 228 ? 0.2591 0.3737 0.4224 -0.0796 0.0154  -0.0149 228 ASN A CB  
1792 C CG  . ASN A 228 ? 0.3987 0.5391 0.5941 -0.0762 0.0153  -0.0122 228 ASN A CG  
1793 O OD1 . ASN A 228 ? 0.3515 0.5047 0.5571 -0.0686 0.0066  -0.0074 228 ASN A OD1 
1794 N ND2 . ASN A 228 ? 0.3334 0.4829 0.5464 -0.0822 0.0246  -0.0146 228 ASN A ND2 
1795 N N   . ASP A 229 ? 0.3131 0.3750 0.4143 -0.0735 0.0161  -0.0156 229 ASP A N   
1796 C CA  . ASP A 229 ? 0.3415 0.3845 0.4211 -0.0748 0.0141  -0.0177 229 ASP A CA  
1797 C C   . ASP A 229 ? 0.3737 0.4146 0.4410 -0.0659 0.0072  -0.0158 229 ASP A C   
1798 O O   . ASP A 229 ? 0.3396 0.3779 0.3978 -0.0668 0.0012  -0.0189 229 ASP A O   
1799 C CB  . ASP A 229 ? 0.3835 0.4048 0.4489 -0.0764 0.0239  -0.0164 229 ASP A CB  
1800 C CG  . ASP A 229 ? 0.5099 0.5107 0.5548 -0.0738 0.0220  -0.0168 229 ASP A CG  
1801 O OD1 . ASP A 229 ? 0.6314 0.6286 0.6750 -0.0788 0.0182  -0.0219 229 ASP A OD1 
1802 O OD2 . ASP A 229 ? 0.5766 0.5660 0.6076 -0.0669 0.0244  -0.0126 229 ASP A OD2 
1803 N N   . PHE A 230 ? 0.2589 0.3011 0.3258 -0.0578 0.0088  -0.0116 230 PHE A N   
1804 C CA  . PHE A 230 ? 0.2835 0.3250 0.3403 -0.0504 0.0028  -0.0094 230 PHE A CA  
1805 C C   . PHE A 230 ? 0.2538 0.3120 0.3186 -0.0511 -0.0071 -0.0091 230 PHE A C   
1806 O O   . PHE A 230 ? 0.2842 0.3408 0.3368 -0.0499 -0.0125 -0.0101 230 PHE A O   
1807 C CB  . PHE A 230 ? 0.2895 0.3315 0.3482 -0.0435 0.0060  -0.0058 230 PHE A CB  
1808 C CG  . PHE A 230 ? 0.2935 0.3364 0.3445 -0.0372 0.0000  -0.0030 230 PHE A CG  
1809 C CD1 . PHE A 230 ? 0.2761 0.3071 0.3085 -0.0345 -0.0003 -0.0033 230 PHE A CD1 
1810 C CD2 . PHE A 230 ? 0.3168 0.3734 0.3803 -0.0342 -0.0057 0.0007  230 PHE A CD2 
1811 C CE1 . PHE A 230 ? 0.2827 0.3165 0.3092 -0.0297 -0.0051 -0.0010 230 PHE A CE1 
1812 C CE2 . PHE A 230 ? 0.3640 0.4213 0.4201 -0.0298 -0.0106 0.0040  230 PHE A CE2 
1813 C CZ  . PHE A 230 ? 0.3279 0.3745 0.3655 -0.0280 -0.0100 0.0026  230 PHE A CZ  
1814 N N   . ASN A 231 ? 0.2432 0.3193 0.3288 -0.0530 -0.0095 -0.0072 231 ASN A N   
1815 C CA  . ASN A 231 ? 0.3023 0.3973 0.3960 -0.0535 -0.0202 -0.0044 231 ASN A CA  
1816 C C   . ASN A 231 ? 0.2756 0.3726 0.3600 -0.0619 -0.0256 -0.0105 231 ASN A C   
1817 O O   . ASN A 231 ? 0.2769 0.3834 0.3549 -0.0622 -0.0340 -0.0096 231 ASN A O   
1818 C CB  . ASN A 231 ? 0.2824 0.3973 0.4035 -0.0529 -0.0217 0.0000  231 ASN A CB  
1819 C CG  . ASN A 231 ? 0.3415 0.4564 0.4719 -0.0431 -0.0192 0.0063  231 ASN A CG  
1820 O OD1 . ASN A 231 ? 0.3177 0.4242 0.4350 -0.0380 -0.0209 0.0090  231 ASN A OD1 
1821 N ND2 . ASN A 231 ? 0.3209 0.4444 0.4745 -0.0409 -0.0142 0.0078  231 ASN A ND2 
1822 N N   . LEU A 232 ? 0.3370 0.4240 0.4191 -0.0695 -0.0202 -0.0171 232 LEU A N   
1823 C CA  . LEU A 232 ? 0.3113 0.3945 0.3821 -0.0777 -0.0235 -0.0252 232 LEU A CA  
1824 C C   . LEU A 232 ? 0.4151 0.4852 0.4642 -0.0725 -0.0243 -0.0271 232 LEU A C   
1825 O O   . LEU A 232 ? 0.4153 0.4916 0.4556 -0.0762 -0.0303 -0.0319 232 LEU A O   
1826 C CB  . LEU A 232 ? 0.3850 0.4532 0.4560 -0.0859 -0.0154 -0.0312 232 LEU A CB  
1827 C CG  . LEU A 232 ? 0.4753 0.5584 0.5659 -0.0968 -0.0158 -0.0338 232 LEU A CG  
1828 C CD1 . LEU A 232 ? 0.5931 0.6551 0.6785 -0.1054 -0.0070 -0.0398 232 LEU A CD1 
1829 C CD2 . LEU A 232 ? 0.4672 0.5735 0.5637 -0.1039 -0.0274 -0.0373 232 LEU A CD2 
1830 N N   . VAL A 233 ? 0.3211 0.3750 0.3616 -0.0644 -0.0180 -0.0238 233 VAL A N   
1831 C CA  . VAL A 233 ? 0.2738 0.3174 0.2969 -0.0583 -0.0182 -0.0249 233 VAL A CA  
1832 C C   . VAL A 233 ? 0.3276 0.3871 0.3501 -0.0535 -0.0252 -0.0196 233 VAL A C   
1833 O O   . VAL A 233 ? 0.3474 0.4094 0.3582 -0.0534 -0.0286 -0.0226 233 VAL A O   
1834 C CB  . VAL A 233 ? 0.3733 0.3978 0.3889 -0.0517 -0.0105 -0.0219 233 VAL A CB  
1835 C CG1 . VAL A 233 ? 0.3980 0.4155 0.3991 -0.0449 -0.0110 -0.0225 233 VAL A CG1 
1836 C CG2 . VAL A 233 ? 0.4066 0.4143 0.4213 -0.0570 -0.0036 -0.0252 233 VAL A CG2 
1837 N N   . ALA A 234 ? 0.2939 0.3637 0.3294 -0.0497 -0.0267 -0.0116 234 ALA A N   
1838 C CA  . ALA A 234 ? 0.3378 0.4218 0.3748 -0.0458 -0.0335 -0.0048 234 ALA A CA  
1839 C C   . ALA A 234 ? 0.3268 0.4276 0.3613 -0.0520 -0.0423 -0.0064 234 ALA A C   
1840 O O   . ALA A 234 ? 0.3501 0.4565 0.3732 -0.0509 -0.0464 -0.0047 234 ALA A O   
1841 C CB  . ALA A 234 ? 0.2844 0.3765 0.3403 -0.0416 -0.0335 0.0033  234 ALA A CB  
1842 N N   . MET A 235 ? 0.2582 0.3687 0.3027 -0.0597 -0.0452 -0.0098 235 MET A N   
1843 C CA  . MET A 235 ? 0.3833 0.5129 0.4252 -0.0672 -0.0548 -0.0115 235 MET A CA  
1844 C C   . MET A 235 ? 0.3594 0.4810 0.3786 -0.0712 -0.0538 -0.0216 235 MET A C   
1845 O O   . MET A 235 ? 0.3361 0.4709 0.3446 -0.0733 -0.0603 -0.0209 235 MET A O   
1846 C CB  . MET A 235 ? 0.4274 0.5691 0.4852 -0.0760 -0.0576 -0.0148 235 MET A CB  
1847 C CG  . MET A 235 ? 0.4821 0.6398 0.5657 -0.0723 -0.0604 -0.0046 235 MET A CG  
1848 S SD  . MET A 235 ? 0.8946 1.0853 0.9934 -0.0825 -0.0734 -0.0033 235 MET A SD  
1849 C CE  . MET A 235 ? 0.5020 0.6833 0.5823 -0.0967 -0.0716 -0.0208 235 MET A CE  
1850 N N   . LYS A 236 ? 0.3445 0.4441 0.3563 -0.0720 -0.0453 -0.0310 236 LYS A N   
1851 C CA  . LYS A 236 ? 0.3169 0.4065 0.3101 -0.0749 -0.0427 -0.0421 236 LYS A CA  
1852 C C   . LYS A 236 ? 0.3318 0.4220 0.3118 -0.0673 -0.0423 -0.0389 236 LYS A C   
1853 O O   . LYS A 236 ? 0.3932 0.4869 0.3587 -0.0706 -0.0431 -0.0466 236 LYS A O   
1854 C CB  . LYS A 236 ? 0.3788 0.4420 0.3701 -0.0750 -0.0329 -0.0499 236 LYS A CB  
1855 C CG  . LYS A 236 ? 0.4295 0.4765 0.4045 -0.0741 -0.0274 -0.0607 236 LYS A CG  
1856 C CD  . LYS A 236 ? 0.5193 0.5421 0.4961 -0.0780 -0.0197 -0.0686 236 LYS A CD  
1857 C CE  . LYS A 236 ? 0.6880 0.6884 0.6533 -0.0725 -0.0119 -0.0763 236 LYS A CE  
1858 N NZ  . LYS A 236 ? 0.7054 0.7143 0.6599 -0.0652 -0.0128 -0.0765 236 LYS A NZ  
1859 N N   . TYR A 237 ? 0.3600 0.3764 0.3334 -0.0625 0.0135  -0.0492 237 TYR A N   
1860 C CA  . TYR A 237 ? 0.3007 0.3179 0.2698 -0.0529 0.0150  -0.0451 237 TYR A CA  
1861 C C   . TYR A 237 ? 0.3068 0.3427 0.2746 -0.0507 0.0100  -0.0405 237 TYR A C   
1862 O O   . TYR A 237 ? 0.2880 0.3267 0.2542 -0.0447 0.0111  -0.0347 237 TYR A O   
1863 C CB  . TYR A 237 ? 0.2799 0.2878 0.2535 -0.0465 0.0184  -0.0371 237 TYR A CB  
1864 C CG  . TYR A 237 ? 0.3770 0.3630 0.3480 -0.0456 0.0235  -0.0404 237 TYR A CG  
1865 C CD1 . TYR A 237 ? 0.4079 0.3852 0.3733 -0.0384 0.0271  -0.0447 237 TYR A CD1 
1866 C CD2 . TYR A 237 ? 0.3404 0.3141 0.3139 -0.0516 0.0249  -0.0392 237 TYR A CD2 
1867 C CE1 . TYR A 237 ? 0.3483 0.3022 0.3105 -0.0354 0.0313  -0.0475 237 TYR A CE1 
1868 C CE2 . TYR A 237 ? 0.4116 0.3606 0.3806 -0.0507 0.0295  -0.0408 237 TYR A CE2 
1869 C CZ  . TYR A 237 ? 0.5118 0.4496 0.4750 -0.0417 0.0323  -0.0450 237 TYR A CZ  
1870 O OH  . TYR A 237 ? 0.4790 0.3893 0.4371 -0.0385 0.0365  -0.0464 237 TYR A OH  
1871 N N   . ASN A 238 ? 0.2494 0.2984 0.2178 -0.0555 0.0045  -0.0429 238 ASN A N   
1872 C CA  . ASN A 238 ? 0.2832 0.3475 0.2483 -0.0526 -0.0011 -0.0379 238 ASN A CA  
1873 C C   . ASN A 238 ? 0.2918 0.3560 0.2624 -0.0469 -0.0017 -0.0273 238 ASN A C   
1874 O O   . ASN A 238 ? 0.2855 0.3523 0.2509 -0.0430 -0.0028 -0.0210 238 ASN A O   
1875 C CB  . ASN A 238 ? 0.3107 0.3780 0.2631 -0.0508 -0.0002 -0.0400 238 ASN A CB  
1876 C CG  . ASN A 238 ? 0.4777 0.5489 0.4225 -0.0566 -0.0016 -0.0518 238 ASN A CG  
1877 O OD1 . ASN A 238 ? 0.4310 0.5124 0.3784 -0.0618 -0.0071 -0.0559 238 ASN A OD1 
1878 N ND2 . ASN A 238 ? 0.5657 0.6305 0.5014 -0.0557 0.0034  -0.0585 238 ASN A ND2 
1879 N N   . TYR A 239 ? 0.2365 0.2967 0.2167 -0.0473 -0.0004 -0.0255 239 TYR A N   
1880 C CA  . TYR A 239 ? 0.2473 0.3087 0.2332 -0.0428 -0.0018 -0.0179 239 TYR A CA  
1881 C C   . TYR A 239 ? 0.2533 0.3281 0.2450 -0.0424 -0.0075 -0.0178 239 TYR A C   
1882 O O   . TYR A 239 ? 0.2503 0.3339 0.2460 -0.0476 -0.0089 -0.0239 239 TYR A O   
1883 C CB  . TYR A 239 ? 0.2263 0.2781 0.2178 -0.0426 0.0030  -0.0165 239 TYR A CB  
1884 C CG  . TYR A 239 ? 0.2051 0.2484 0.1937 -0.0386 0.0066  -0.0130 239 TYR A CG  
1885 C CD1 . TYR A 239 ? 0.2547 0.2941 0.2372 -0.0380 0.0095  -0.0160 239 TYR A CD1 
1886 C CD2 . TYR A 239 ? 0.2736 0.3151 0.2658 -0.0353 0.0071  -0.0077 239 TYR A CD2 
1887 C CE1 . TYR A 239 ? 0.2802 0.3167 0.2623 -0.0337 0.0128  -0.0132 239 TYR A CE1 
1888 C CE2 . TYR A 239 ? 0.2214 0.2594 0.2125 -0.0322 0.0096  -0.0050 239 TYR A CE2 
1889 C CZ  . TYR A 239 ? 0.2744 0.3111 0.2614 -0.0312 0.0124  -0.0075 239 TYR A CZ  
1890 O OH  . TYR A 239 ? 0.2934 0.3314 0.2813 -0.0274 0.0149  -0.0054 239 TYR A OH  
1891 N N   . GLU A 240 ? 0.2682 0.3449 0.2608 -0.0363 -0.0108 -0.0116 240 GLU A N   
1892 C CA  . GLU A 240 ? 0.3469 0.4365 0.3464 -0.0328 -0.0162 -0.0114 240 GLU A CA  
1893 C C   . GLU A 240 ? 0.2568 0.3509 0.2674 -0.0352 -0.0129 -0.0146 240 GLU A C   
1894 O O   . GLU A 240 ? 0.2750 0.3585 0.2864 -0.0363 -0.0076 -0.0133 240 GLU A O   
1895 C CB  . GLU A 240 ? 0.3746 0.4593 0.3712 -0.0245 -0.0198 -0.0040 240 GLU A CB  
1896 C CG  . GLU A 240 ? 0.3985 0.4803 0.3829 -0.0226 -0.0235 0.0011  240 GLU A CG  
1897 C CD  . GLU A 240 ? 0.4985 0.5958 0.4810 -0.0199 -0.0310 0.0002  240 GLU A CD  
1898 O OE1 . GLU A 240 ? 0.5231 0.6264 0.5101 -0.0120 -0.0365 0.0028  240 GLU A OE1 
1899 O OE2 . GLU A 240 ? 0.5407 0.6455 0.5172 -0.0250 -0.0316 -0.0039 240 GLU A OE2 
1900 N N   . PRO A 241 ? 0.2996 0.4117 0.3190 -0.0362 -0.0159 -0.0187 241 PRO A N   
1901 C CA  . PRO A 241 ? 0.2615 0.3807 0.2915 -0.0392 -0.0118 -0.0212 241 PRO A CA  
1902 C C   . PRO A 241 ? 0.3087 0.4233 0.3407 -0.0309 -0.0108 -0.0170 241 PRO A C   
1903 O O   . PRO A 241 ? 0.3493 0.4612 0.3786 -0.0219 -0.0153 -0.0135 241 PRO A O   
1904 C CB  . PRO A 241 ? 0.3949 0.5397 0.4348 -0.0411 -0.0163 -0.0266 241 PRO A CB  
1905 C CG  . PRO A 241 ? 0.4806 0.6310 0.5151 -0.0336 -0.0246 -0.0245 241 PRO A CG  
1906 C CD  . PRO A 241 ? 0.3605 0.4903 0.3806 -0.0347 -0.0233 -0.0210 241 PRO A CD  
1907 N N   . LEU A 242 ? 0.2848 0.3961 0.3198 -0.0343 -0.0046 -0.0173 242 LEU A N   
1908 C CA  . LEU A 242 ? 0.2753 0.3846 0.3120 -0.0277 -0.0029 -0.0154 242 LEU A CA  
1909 C C   . LEU A 242 ? 0.3136 0.4450 0.3619 -0.0254 -0.0028 -0.0196 242 LEU A C   
1910 O O   . LEU A 242 ? 0.2718 0.4177 0.3271 -0.0336 0.0001  -0.0231 242 LEU A O   
1911 C CB  . LEU A 242 ? 0.3170 0.4134 0.3489 -0.0321 0.0034  -0.0131 242 LEU A CB  
1912 C CG  . LEU A 242 ? 0.3286 0.4188 0.3579 -0.0259 0.0046  -0.0113 242 LEU A CG  
1913 C CD1 . LEU A 242 ? 0.3885 0.4655 0.4114 -0.0209 0.0005  -0.0084 242 LEU A CD1 
1914 C CD2 . LEU A 242 ? 0.2809 0.3641 0.3059 -0.0308 0.0104  -0.0090 242 LEU A CD2 
1915 N N   . THR A 243 ? 0.2992 0.4334 0.3498 -0.0144 -0.0056 -0.0198 243 THR A N   
1916 C CA  . THR A 243 ? 0.3071 0.4643 0.3695 -0.0090 -0.0054 -0.0246 243 THR A CA  
1917 C C   . THR A 243 ? 0.2671 0.4217 0.3289 -0.0054 0.0000  -0.0259 243 THR A C   
1918 O O   . THR A 243 ? 0.2882 0.4228 0.3402 -0.0057 0.0017  -0.0230 243 THR A O   
1919 C CB  . THR A 243 ? 0.2639 0.4282 0.3297 0.0038  -0.0135 -0.0249 243 THR A CB  
1920 O OG1 . THR A 243 ? 0.3080 0.4497 0.3649 0.0130  -0.0157 -0.0217 243 THR A OG1 
1921 C CG2 . THR A 243 ? 0.2897 0.4563 0.3528 0.0007  -0.0196 -0.0229 243 THR A CG2 
1922 N N   . GLN A 244 ? 0.2896 0.4681 0.3624 -0.0021 0.0026  -0.0312 244 GLN A N   
1923 C CA  . GLN A 244 ? 0.2985 0.4780 0.3704 0.0035  0.0074  -0.0343 244 GLN A CA  
1924 C C   . GLN A 244 ? 0.2601 0.4203 0.3253 0.0164  0.0025  -0.0345 244 GLN A C   
1925 O O   . GLN A 244 ? 0.2383 0.3856 0.2956 0.0177  0.0053  -0.0355 244 GLN A O   
1926 C CB  . GLN A 244 ? 0.2706 0.4832 0.3569 0.0065  0.0110  -0.0409 244 GLN A CB  
1927 C CG  . GLN A 244 ? 0.2600 0.4782 0.3444 0.0092  0.0184  -0.0448 244 GLN A CG  
1928 C CD  . GLN A 244 ? 0.2453 0.4485 0.3174 -0.0026 0.0246  -0.0399 244 GLN A CD  
1929 O OE1 . GLN A 244 ? 0.3708 0.5770 0.4429 -0.0160 0.0285  -0.0359 244 GLN A OE1 
1930 N NE2 . GLN A 244 ? 0.2916 0.4780 0.3526 0.0025  0.0251  -0.0403 244 GLN A NE2 
1931 N N   . ASP A 245 ? 0.2610 0.4184 0.3281 0.0257  -0.0052 -0.0336 245 ASP A N   
1932 C CA  . ASP A 245 ? 0.2702 0.4032 0.3288 0.0361  -0.0097 -0.0326 245 ASP A CA  
1933 C C   . ASP A 245 ? 0.2114 0.3180 0.2569 0.0276  -0.0089 -0.0275 245 ASP A C   
1934 O O   . ASP A 245 ? 0.2445 0.3345 0.2831 0.0303  -0.0082 -0.0293 245 ASP A O   
1935 C CB  . ASP A 245 ? 0.3651 0.4966 0.4253 0.0464  -0.0183 -0.0297 245 ASP A CB  
1936 C CG  . ASP A 245 ? 0.4267 0.5830 0.5002 0.0602  -0.0204 -0.0357 245 ASP A CG  
1937 O OD1 . ASP A 245 ? 0.4499 0.6260 0.5320 0.0611  -0.0143 -0.0429 245 ASP A OD1 
1938 O OD2 . ASP A 245 ? 0.4978 0.6555 0.5730 0.0707  -0.0282 -0.0330 245 ASP A OD2 
1939 N N   . HIS A 246 ? 0.2403 0.3442 0.2827 0.0173  -0.0090 -0.0222 246 HIS A N   
1940 C CA  . HIS A 246 ? 0.2646 0.3486 0.2968 0.0098  -0.0076 -0.0178 246 HIS A CA  
1941 C C   . HIS A 246 ? 0.3045 0.3888 0.3343 0.0055  -0.0017 -0.0202 246 HIS A C   
1942 O O   . HIS A 246 ? 0.2584 0.3279 0.2807 0.0044  -0.0018 -0.0195 246 HIS A O   
1943 C CB  . HIS A 246 ? 0.2480 0.3323 0.2782 0.0009  -0.0078 -0.0134 246 HIS A CB  
1944 C CG  . HIS A 246 ? 0.2666 0.3489 0.2951 0.0041  -0.0139 -0.0102 246 HIS A CG  
1945 N ND1 . HIS A 246 ? 0.2793 0.3732 0.3101 -0.0006 -0.0152 -0.0100 246 HIS A ND1 
1946 C CD2 . HIS A 246 ? 0.2961 0.3649 0.3188 0.0109  -0.0191 -0.0066 246 HIS A CD2 
1947 C CE1 . HIS A 246 ? 0.3665 0.4568 0.3928 0.0040  -0.0213 -0.0064 246 HIS A CE1 
1948 N NE2 . HIS A 246 ? 0.3730 0.4472 0.3941 0.0110  -0.0236 -0.0034 246 HIS A NE2 
1949 N N   . VAL A 247 ? 0.2384 0.3404 0.2738 0.0018  0.0034  -0.0225 247 VAL A N   
1950 C CA  . VAL A 247 ? 0.2747 0.3781 0.3057 -0.0019 0.0091  -0.0235 247 VAL A CA  
1951 C C   . VAL A 247 ? 0.2122 0.3115 0.2400 0.0063  0.0086  -0.0292 247 VAL A C   
1952 O O   . VAL A 247 ? 0.2459 0.3360 0.2652 0.0043  0.0096  -0.0294 247 VAL A O   
1953 C CB  . VAL A 247 ? 0.2429 0.3665 0.2799 -0.0077 0.0153  -0.0245 247 VAL A CB  
1954 C CG1 . VAL A 247 ? 0.2633 0.3891 0.2934 -0.0104 0.0214  -0.0246 247 VAL A CG1 
1955 C CG2 . VAL A 247 ? 0.2964 0.4188 0.3345 -0.0174 0.0160  -0.0198 247 VAL A CG2 
1956 N N   . ASP A 248 ? 0.2048 0.3107 0.2390 0.0164  0.0064  -0.0346 248 ASP A N   
1957 C CA  . ASP A 248 ? 0.2392 0.3388 0.2699 0.0253  0.0062  -0.0418 248 ASP A CA  
1958 C C   . ASP A 248 ? 0.2454 0.3175 0.2669 0.0259  0.0011  -0.0405 248 ASP A C   
1959 O O   . ASP A 248 ? 0.2763 0.3391 0.2906 0.0265  0.0018  -0.0456 248 ASP A O   
1960 C CB  . ASP A 248 ? 0.2641 0.3767 0.3044 0.0383  0.0049  -0.0481 248 ASP A CB  
1961 C CG  . ASP A 248 ? 0.3004 0.4454 0.3519 0.0366  0.0108  -0.0508 248 ASP A CG  
1962 O OD1 . ASP A 248 ? 0.3430 0.4968 0.3911 0.0273  0.0174  -0.0501 248 ASP A OD1 
1963 O OD2 . ASP A 248 ? 0.3014 0.4636 0.3645 0.0447  0.0089  -0.0536 248 ASP A OD2 
1964 N N   . ILE A 249 ? 0.2551 0.3149 0.2760 0.0247  -0.0039 -0.0340 249 ILE A N   
1965 C CA  . ILE A 249 ? 0.2248 0.2593 0.2370 0.0228  -0.0077 -0.0319 249 ILE A CA  
1966 C C   . ILE A 249 ? 0.2571 0.2885 0.2633 0.0122  -0.0055 -0.0302 249 ILE A C   
1967 O O   . ILE A 249 ? 0.2782 0.2940 0.2780 0.0096  -0.0074 -0.0321 249 ILE A O   
1968 C CB  . ILE A 249 ? 0.2837 0.3080 0.2953 0.0229  -0.0126 -0.0242 249 ILE A CB  
1969 C CG1 . ILE A 249 ? 0.3376 0.3679 0.3552 0.0353  -0.0160 -0.0254 249 ILE A CG1 
1970 C CG2 . ILE A 249 ? 0.4232 0.4216 0.4255 0.0189  -0.0156 -0.0213 249 ILE A CG2 
1971 C CD1 . ILE A 249 ? 0.4254 0.4435 0.4392 0.0376  -0.0219 -0.0174 249 ILE A CD1 
1972 N N   . LEU A 250 ? 0.2326 0.2784 0.2408 0.0061  -0.0018 -0.0268 250 LEU A N   
1973 C CA  . LEU A 250 ? 0.2626 0.3073 0.2654 -0.0015 -0.0003 -0.0246 250 LEU A CA  
1974 C C   . LEU A 250 ? 0.2724 0.3243 0.2708 -0.0006 0.0026  -0.0305 250 LEU A C   
1975 O O   . LEU A 250 ? 0.2834 0.3366 0.2764 -0.0056 0.0030  -0.0288 250 LEU A O   
1976 C CB  . LEU A 250 ? 0.2541 0.3067 0.2589 -0.0071 0.0022  -0.0180 250 LEU A CB  
1977 C CG  . LEU A 250 ? 0.2758 0.3217 0.2820 -0.0098 -0.0003 -0.0126 250 LEU A CG  
1978 C CD1 . LEU A 250 ? 0.2305 0.2850 0.2398 -0.0133 0.0026  -0.0093 250 LEU A CD1 
1979 C CD2 . LEU A 250 ? 0.2936 0.3307 0.2952 -0.0144 -0.0019 -0.0100 250 LEU A CD2 
1980 N N   . GLY A 251 ? 0.2644 0.3230 0.2646 0.0063  0.0044  -0.0375 251 GLY A N   
1981 C CA  . GLY A 251 ? 0.2885 0.3571 0.2833 0.0073  0.0082  -0.0437 251 GLY A CA  
1982 C C   . GLY A 251 ? 0.3182 0.3772 0.3035 0.0043  0.0055  -0.0476 251 GLY A C   
1983 O O   . GLY A 251 ? 0.3213 0.3895 0.2998 0.0006  0.0074  -0.0472 251 GLY A O   
1984 N N   . PRO A 252 ? 0.2648 0.3052 0.2488 0.0054  0.0008  -0.0516 252 PRO A N   
1985 C CA  . PRO A 252 ? 0.3176 0.3497 0.2935 0.0002  -0.0023 -0.0566 252 PRO A CA  
1986 C C   . PRO A 252 ? 0.3103 0.3486 0.2847 -0.0086 -0.0036 -0.0492 252 PRO A C   
1987 O O   . PRO A 252 ? 0.2779 0.3227 0.2456 -0.0121 -0.0047 -0.0529 252 PRO A O   
1988 C CB  . PRO A 252 ? 0.3274 0.3352 0.3035 0.0011  -0.0066 -0.0596 252 PRO A CB  
1989 C CG  . PRO A 252 ? 0.3959 0.4019 0.3774 0.0122  -0.0054 -0.0612 252 PRO A CG  
1990 C CD  . PRO A 252 ? 0.3836 0.4097 0.3722 0.0119  -0.0020 -0.0527 252 PRO A CD  
1991 N N   . LEU A 253 ? 0.2663 0.3040 0.2464 -0.0114 -0.0038 -0.0395 253 LEU A N   
1992 C CA  . LEU A 253 ? 0.2374 0.2826 0.2171 -0.0173 -0.0046 -0.0329 253 LEU A CA  
1993 C C   . LEU A 253 ? 0.2478 0.3082 0.2239 -0.0158 -0.0011 -0.0294 253 LEU A C   
1994 O O   . LEU A 253 ? 0.2550 0.3234 0.2263 -0.0180 -0.0026 -0.0277 253 LEU A O   
1995 C CB  . LEU A 253 ? 0.2330 0.2732 0.2189 -0.0196 -0.0050 -0.0249 253 LEU A CB  
1996 C CG  . LEU A 253 ? 0.3035 0.3286 0.2901 -0.0234 -0.0085 -0.0264 253 LEU A CG  
1997 C CD1 . LEU A 253 ? 0.3031 0.3236 0.2940 -0.0251 -0.0083 -0.0188 253 LEU A CD1 
1998 C CD2 . LEU A 253 ? 0.3494 0.3771 0.3336 -0.0306 -0.0113 -0.0295 253 LEU A CD2 
1999 N N   . SER A 254 ? 0.2486 0.3137 0.2267 -0.0123 0.0034  -0.0279 254 SER A N   
2000 C CA  . SER A 254 ? 0.2888 0.3662 0.2616 -0.0121 0.0078  -0.0244 254 SER A CA  
2001 C C   . SER A 254 ? 0.3127 0.3981 0.2755 -0.0110 0.0077  -0.0308 254 SER A C   
2002 O O   . SER A 254 ? 0.2860 0.3795 0.2406 -0.0122 0.0081  -0.0261 254 SER A O   
2003 C CB  . SER A 254 ? 0.2724 0.3555 0.2506 -0.0103 0.0131  -0.0238 254 SER A CB  
2004 O OG  . SER A 254 ? 0.4149 0.5083 0.3875 -0.0123 0.0184  -0.0191 254 SER A OG  
2005 N N   . ALA A 255 ? 0.2602 0.3426 0.2221 -0.0080 0.0069  -0.0416 255 ALA A N   
2006 C CA  . ALA A 255 ? 0.3042 0.3941 0.2553 -0.0070 0.0069  -0.0501 255 ALA A CA  
2007 C C   . ALA A 255 ? 0.3331 0.4231 0.2782 -0.0117 0.0008  -0.0506 255 ALA A C   
2008 O O   . ALA A 255 ? 0.3459 0.4483 0.2802 -0.0122 0.0005  -0.0515 255 ALA A O   
2009 C CB  . ALA A 255 ? 0.3389 0.4220 0.2907 -0.0017 0.0071  -0.0632 255 ALA A CB  
2010 N N   . GLN A 256 ? 0.3373 0.4161 0.2891 -0.0156 -0.0040 -0.0498 256 GLN A N   
2011 C CA  . GLN A 256 ? 0.3395 0.4220 0.2884 -0.0212 -0.0099 -0.0515 256 GLN A CA  
2012 C C   . GLN A 256 ? 0.3757 0.4723 0.3230 -0.0213 -0.0106 -0.0407 256 GLN A C   
2013 O O   . GLN A 256 ? 0.3526 0.4618 0.2933 -0.0228 -0.0148 -0.0422 256 GLN A O   
2014 C CB  . GLN A 256 ? 0.3700 0.4382 0.3273 -0.0267 -0.0135 -0.0526 256 GLN A CB  
2015 C CG  . GLN A 256 ? 0.4735 0.5504 0.4322 -0.0340 -0.0189 -0.0518 256 GLN A CG  
2016 C CD  . GLN A 256 ? 0.6266 0.6890 0.5904 -0.0421 -0.0219 -0.0567 256 GLN A CD  
2017 O OE1 . GLN A 256 ? 0.6370 0.7073 0.6047 -0.0499 -0.0257 -0.0563 256 GLN A OE1 
2018 N NE2 . GLN A 256 ? 0.6295 0.6708 0.5934 -0.0403 -0.0201 -0.0605 256 GLN A NE2 
2019 N N   . THR A 257 ? 0.2573 0.3517 0.2100 -0.0191 -0.0072 -0.0301 257 THR A N   
2020 C CA  . THR A 257 ? 0.2848 0.3873 0.2364 -0.0176 -0.0080 -0.0195 257 THR A CA  
2021 C C   . THR A 257 ? 0.3490 0.4572 0.2908 -0.0138 -0.0035 -0.0127 257 THR A C   
2022 O O   . THR A 257 ? 0.3500 0.4632 0.2875 -0.0113 -0.0045 -0.0035 257 THR A O   
2023 C CB  . THR A 257 ? 0.2610 0.3553 0.2231 -0.0178 -0.0068 -0.0123 257 THR A CB  
2024 O OG1 . THR A 257 ? 0.2556 0.3411 0.2204 -0.0167 -0.0014 -0.0105 257 THR A OG1 
2025 C CG2 . THR A 257 ? 0.2806 0.3700 0.2513 -0.0226 -0.0104 -0.0168 257 THR A CG2 
2026 N N   . GLY A 258 ? 0.3100 0.4174 0.2485 -0.0133 0.0018  -0.0164 258 GLY A N   
2027 C CA  . GLY A 258 ? 0.3393 0.4523 0.2687 -0.0120 0.0076  -0.0092 258 GLY A CA  
2028 C C   . GLY A 258 ? 0.3374 0.4417 0.2719 -0.0127 0.0120  0.0013  258 GLY A C   
2029 O O   . GLY A 258 ? 0.4089 0.5147 0.3352 -0.0133 0.0169  0.0094  258 GLY A O   
2030 N N   . ILE A 259 ? 0.2934 0.3880 0.2401 -0.0136 0.0107  0.0013  259 ILE A N   
2031 C CA  . ILE A 259 ? 0.3055 0.3909 0.2568 -0.0149 0.0141  0.0095  259 ILE A CA  
2032 C C   . ILE A 259 ? 0.2883 0.3725 0.2480 -0.0174 0.0183  0.0050  259 ILE A C   
2033 O O   . ILE A 259 ? 0.2655 0.3470 0.2337 -0.0169 0.0156  -0.0014 259 ILE A O   
2034 C CB  . ILE A 259 ? 0.2636 0.3418 0.2218 -0.0136 0.0099  0.0122  259 ILE A CB  
2035 C CG1 . ILE A 259 ? 0.2825 0.3671 0.2349 -0.0098 0.0050  0.0157  259 ILE A CG1 
2036 C CG2 . ILE A 259 ? 0.3331 0.4002 0.2944 -0.0147 0.0136  0.0188  259 ILE A CG2 
2037 C CD1 . ILE A 259 ? 0.3636 0.4462 0.3247 -0.0081 0.0014  0.0170  259 ILE A CD1 
2038 N N   . ALA A 260 ? 0.2905 0.3772 0.2475 -0.0205 0.0247  0.0089  260 ALA A N   
2039 C CA  . ALA A 260 ? 0.2912 0.3820 0.2578 -0.0232 0.0286  0.0046  260 ALA A CA  
2040 C C   . ALA A 260 ? 0.2488 0.3300 0.2257 -0.0242 0.0259  0.0048  260 ALA A C   
2041 O O   . ALA A 260 ? 0.2565 0.3270 0.2321 -0.0249 0.0245  0.0106  260 ALA A O   
2042 C CB  . ALA A 260 ? 0.2901 0.3862 0.2525 -0.0290 0.0364  0.0102  260 ALA A CB  
2043 N N   . VAL A 261 ? 0.2318 0.3175 0.2183 -0.0232 0.0251  -0.0019 261 VAL A N   
2044 C CA  . VAL A 261 ? 0.2574 0.3356 0.2518 -0.0237 0.0218  -0.0019 261 VAL A CA  
2045 C C   . VAL A 261 ? 0.2666 0.3394 0.2616 -0.0297 0.0250  0.0036  261 VAL A C   
2046 O O   . VAL A 261 ? 0.2420 0.3044 0.2375 -0.0300 0.0227  0.0059  261 VAL A O   
2047 C CB  . VAL A 261 ? 0.3046 0.3899 0.3081 -0.0206 0.0201  -0.0088 261 VAL A CB  
2048 C CG1 . VAL A 261 ? 0.2639 0.3443 0.2736 -0.0221 0.0173  -0.0077 261 VAL A CG1 
2049 C CG2 . VAL A 261 ? 0.2973 0.3797 0.2990 -0.0143 0.0160  -0.0144 261 VAL A CG2 
2050 N N   . LEU A 262 ? 0.2810 0.3605 0.2757 -0.0351 0.0309  0.0053  262 LEU A N   
2051 C CA  . LEU A 262 ? 0.2819 0.3534 0.2766 -0.0427 0.0343  0.0097  262 LEU A CA  
2052 C C   . LEU A 262 ? 0.3165 0.3703 0.3006 -0.0420 0.0346  0.0176  262 LEU A C   
2053 O O   . LEU A 262 ? 0.2782 0.3184 0.2619 -0.0452 0.0352  0.0200  262 LEU A O   
2054 C CB  . LEU A 262 ? 0.3143 0.3980 0.3111 -0.0507 0.0412  0.0099  262 LEU A CB  
2055 C CG  . LEU A 262 ? 0.3165 0.4190 0.3271 -0.0517 0.0406  0.0019  262 LEU A CG  
2056 C CD1 . LEU A 262 ? 0.3537 0.4734 0.3681 -0.0607 0.0484  0.0017  262 LEU A CD1 
2057 C CD2 . LEU A 262 ? 0.3010 0.3974 0.3183 -0.0538 0.0363  -0.0005 262 LEU A CD2 
2058 N N   . ASP A 263 ? 0.2452 0.2997 0.2206 -0.0370 0.0338  0.0212  263 ASP A N   
2059 C CA  . ASP A 263 ? 0.2576 0.2983 0.2240 -0.0332 0.0323  0.0286  263 ASP A CA  
2060 C C   . ASP A 263 ? 0.3275 0.3624 0.2993 -0.0282 0.0269  0.0260  263 ASP A C   
2061 O O   . ASP A 263 ? 0.2917 0.3133 0.2614 -0.0265 0.0269  0.0298  263 ASP A O   
2062 C CB  . ASP A 263 ? 0.3543 0.4022 0.3108 -0.0284 0.0310  0.0317  263 ASP A CB  
2063 C CG  . ASP A 263 ? 0.3860 0.4361 0.3324 -0.0331 0.0373  0.0379  263 ASP A CG  
2064 O OD1 . ASP A 263 ? 0.3358 0.3852 0.2853 -0.0414 0.0432  0.0383  263 ASP A OD1 
2065 O OD2 . ASP A 263 ? 0.3796 0.4347 0.3147 -0.0293 0.0365  0.0419  263 ASP A OD2 
2066 N N   . MET A 264 ? 0.2930 0.3373 0.2712 -0.0256 0.0227  0.0194  264 MET A N   
2067 C CA  . MET A 264 ? 0.2352 0.2762 0.2183 -0.0227 0.0186  0.0173  264 MET A CA  
2068 C C   . MET A 264 ? 0.2552 0.2890 0.2430 -0.0262 0.0200  0.0156  264 MET A C   
2069 O O   . MET A 264 ? 0.2882 0.3150 0.2764 -0.0240 0.0191  0.0162  264 MET A O   
2070 C CB  . MET A 264 ? 0.2542 0.3034 0.2415 -0.0212 0.0145  0.0115  264 MET A CB  
2071 C CG  . MET A 264 ? 0.2001 0.2475 0.1906 -0.0193 0.0110  0.0112  264 MET A CG  
2072 S SD  . MET A 264 ? 0.2653 0.3164 0.2519 -0.0144 0.0087  0.0153  264 MET A SD  
2073 C CE  . MET A 264 ? 0.2463 0.3079 0.2316 -0.0153 0.0047  0.0105  264 MET A CE  
2074 N N   . CYS A 265 ? 0.2339 0.2718 0.2258 -0.0315 0.0222  0.0126  265 CYS A N   
2075 C CA  . CYS A 265 ? 0.2896 0.3220 0.2849 -0.0360 0.0232  0.0103  265 CYS A CA  
2076 C C   . CYS A 265 ? 0.2766 0.2926 0.2657 -0.0377 0.0265  0.0145  265 CYS A C   
2077 O O   . CYS A 265 ? 0.2780 0.2850 0.2674 -0.0380 0.0262  0.0123  265 CYS A O   
2078 C CB  . CYS A 265 ? 0.2744 0.3175 0.2759 -0.0421 0.0249  0.0064  265 CYS A CB  
2079 S SG  . CYS A 265 ? 0.2837 0.3430 0.2928 -0.0375 0.0203  0.0009  265 CYS A SG  
2080 N N   . ALA A 266 ? 0.2682 0.2788 0.2505 -0.0384 0.0299  0.0207  266 ALA A N   
2081 C CA  . ALA A 266 ? 0.3010 0.2912 0.2757 -0.0391 0.0331  0.0260  266 ALA A CA  
2082 C C   . ALA A 266 ? 0.3446 0.3268 0.3169 -0.0290 0.0300  0.0275  266 ALA A C   
2083 O O   . ALA A 266 ? 0.3615 0.3269 0.3311 -0.0276 0.0314  0.0274  266 ALA A O   
2084 C CB  . ALA A 266 ? 0.3340 0.3195 0.2996 -0.0416 0.0372  0.0343  266 ALA A CB  
2085 N N   . SER A 267 ? 0.2646 0.2596 0.2384 -0.0220 0.0259  0.0279  267 SER A N   
2086 C CA  . SER A 267 ? 0.2691 0.2636 0.2435 -0.0129 0.0230  0.0284  267 SER A CA  
2087 C C   . SER A 267 ? 0.2688 0.2646 0.2497 -0.0136 0.0222  0.0214  267 SER A C   
2088 O O   . SER A 267 ? 0.3053 0.2938 0.2857 -0.0081 0.0228  0.0206  267 SER A O   
2089 C CB  . SER A 267 ? 0.3516 0.3628 0.3272 -0.0082 0.0187  0.0294  267 SER A CB  
2090 O OG  . SER A 267 ? 0.4409 0.4512 0.4079 -0.0054 0.0188  0.0364  267 SER A OG  
2091 N N   . LEU A 268 ? 0.2492 0.2549 0.2355 -0.0195 0.0211  0.0164  268 LEU A N   
2092 C CA  . LEU A 268 ? 0.1975 0.2049 0.1875 -0.0209 0.0203  0.0107  268 LEU A CA  
2093 C C   . LEU A 268 ? 0.2836 0.2767 0.2708 -0.0242 0.0234  0.0077  268 LEU A C   
2094 O O   . LEU A 268 ? 0.2785 0.2679 0.2651 -0.0215 0.0239  0.0039  268 LEU A O   
2095 C CB  . LEU A 268 ? 0.2039 0.2227 0.1984 -0.0255 0.0177  0.0074  268 LEU A CB  
2096 C CG  . LEU A 268 ? 0.2188 0.2403 0.2148 -0.0272 0.0163  0.0029  268 LEU A CG  
2097 C CD1 . LEU A 268 ? 0.2461 0.2689 0.2413 -0.0225 0.0164  0.0028  268 LEU A CD1 
2098 C CD2 . LEU A 268 ? 0.2347 0.2658 0.2338 -0.0290 0.0128  0.0018  268 LEU A CD2 
2099 N N   . LYS A 269 ? 0.2678 0.2534 0.2531 -0.0310 0.0260  0.0085  269 LYS A N   
2100 C CA  . LYS A 269 ? 0.2511 0.2204 0.2331 -0.0364 0.0291  0.0050  269 LYS A CA  
2101 C C   . LYS A 269 ? 0.3653 0.3155 0.3410 -0.0286 0.0311  0.0068  269 LYS A C   
2102 O O   . LYS A 269 ? 0.3635 0.3033 0.3372 -0.0284 0.0323  0.0006  269 LYS A O   
2103 C CB  . LYS A 269 ? 0.3198 0.2851 0.3009 -0.0462 0.0324  0.0074  269 LYS A CB  
2104 C CG  . LYS A 269 ? 0.3924 0.3343 0.3677 -0.0531 0.0366  0.0064  269 LYS A CG  
2105 C CD  . LYS A 269 ? 0.4781 0.4245 0.4562 -0.0672 0.0397  0.0058  269 LYS A CD  
2106 C CE  . LYS A 269 ? 0.6493 0.5681 0.6190 -0.0752 0.0452  0.0090  269 LYS A CE  
2107 N NZ  . LYS A 269 ? 0.5308 0.4539 0.5000 -0.0857 0.0498  0.0152  269 LYS A NZ  
2108 N N   . GLU A 270 ? 0.3745 0.3203 0.3465 -0.0212 0.0313  0.0148  270 GLU A N   
2109 C CA  . GLU A 270 ? 0.3710 0.2996 0.3376 -0.0108 0.0325  0.0170  270 GLU A CA  
2110 C C   . GLU A 270 ? 0.3565 0.2968 0.3281 -0.0020 0.0305  0.0115  270 GLU A C   
2111 O O   . GLU A 270 ? 0.4032 0.3306 0.3723 0.0045  0.0325  0.0076  270 GLU A O   
2112 C CB  . GLU A 270 ? 0.3708 0.2957 0.3319 -0.0035 0.0318  0.0278  270 GLU A CB  
2113 C CG  . GLU A 270 ? 0.5148 0.4259 0.4679 -0.0118 0.0351  0.0350  270 GLU A CG  
2114 C CD  . GLU A 270 ? 0.5935 0.4747 0.5398 -0.0186 0.0399  0.0341  270 GLU A CD  
2115 O OE1 . GLU A 270 ? 0.6743 0.5333 0.6148 -0.0096 0.0407  0.0349  270 GLU A OE1 
2116 O OE2 . GLU A 270 ? 0.5487 0.4290 0.4959 -0.0330 0.0429  0.0320  270 GLU A OE2 
2117 N N   . LEU A 271 ? 0.2982 0.2624 0.2766 -0.0022 0.0273  0.0107  271 LEU A N   
2118 C CA  . LEU A 271 ? 0.3588 0.3365 0.3420 0.0035  0.0265  0.0061  271 LEU A CA  
2119 C C   . LEU A 271 ? 0.3536 0.3276 0.3357 -0.0013 0.0284  -0.0025 271 LEU A C   
2120 O O   . LEU A 271 ? 0.3762 0.3509 0.3580 0.0049  0.0302  -0.0075 271 LEU A O   
2121 C CB  . LEU A 271 ? 0.3129 0.3136 0.3023 0.0013  0.0230  0.0076  271 LEU A CB  
2122 C CG  . LEU A 271 ? 0.2831 0.2952 0.2751 0.0078  0.0202  0.0132  271 LEU A CG  
2123 C CD1 . LEU A 271 ? 0.2638 0.2938 0.2606 0.0021  0.0170  0.0129  271 LEU A CD1 
2124 C CD2 . LEU A 271 ? 0.3634 0.3811 0.3583 0.0191  0.0208  0.0127  271 LEU A CD2 
2125 N N   . LEU A 272 ? 0.3107 0.2834 0.2920 -0.0120 0.0279  -0.0051 272 LEU A N   
2126 C CA  . LEU A 272 ? 0.3447 0.3161 0.3239 -0.0172 0.0287  -0.0136 272 LEU A CA  
2127 C C   . LEU A 272 ? 0.4043 0.3527 0.3772 -0.0159 0.0324  -0.0190 272 LEU A C   
2128 O O   . LEU A 272 ? 0.4451 0.3918 0.4148 -0.0149 0.0338  -0.0275 272 LEU A O   
2129 C CB  . LEU A 272 ? 0.2917 0.2701 0.2727 -0.0281 0.0263  -0.0149 272 LEU A CB  
2130 C CG  . LEU A 272 ? 0.2977 0.2960 0.2833 -0.0288 0.0225  -0.0121 272 LEU A CG  
2131 C CD1 . LEU A 272 ? 0.3040 0.3092 0.2922 -0.0370 0.0199  -0.0135 272 LEU A CD1 
2132 C CD2 . LEU A 272 ? 0.4302 0.4376 0.4140 -0.0262 0.0220  -0.0154 272 LEU A CD2 
2133 N N   . GLN A 273 ? 0.3680 0.2971 0.3377 -0.0159 0.0342  -0.0142 273 GLN A N   
2134 C CA  . GLN A 273 ? 0.4422 0.3430 0.4044 -0.0163 0.0378  -0.0187 273 GLN A CA  
2135 C C   . GLN A 273 ? 0.5119 0.4004 0.4709 -0.0008 0.0398  -0.0188 273 GLN A C   
2136 O O   . GLN A 273 ? 0.5106 0.3776 0.4635 0.0015  0.0428  -0.0264 273 GLN A O   
2137 C CB  . GLN A 273 ? 0.5138 0.3975 0.4727 -0.0246 0.0394  -0.0120 273 GLN A CB  
2138 C CG  . GLN A 273 ? 0.4734 0.3650 0.4353 -0.0412 0.0389  -0.0163 273 GLN A CG  
2139 C CD  . GLN A 273 ? 0.5045 0.3839 0.4641 -0.0507 0.0416  -0.0094 273 GLN A CD  
2140 O OE1 . GLN A 273 ? 0.5011 0.3625 0.4544 -0.0451 0.0439  -0.0006 273 GLN A OE1 
2141 N NE2 . GLN A 273 ? 0.4938 0.3837 0.4579 -0.0654 0.0416  -0.0133 273 GLN A NE2 
2142 N N   . ASN A 274 ? 0.4275 0.3304 0.3910 0.0103  0.0380  -0.0117 274 ASN A N   
2143 C CA  . ASN A 274 ? 0.4707 0.3664 0.4332 0.0270  0.0392  -0.0108 274 ASN A CA  
2144 C C   . ASN A 274 ? 0.4581 0.3836 0.4291 0.0357  0.0381  -0.0133 274 ASN A C   
2145 O O   . ASN A 274 ? 0.4591 0.3857 0.4319 0.0507  0.0390  -0.0133 274 ASN A O   
2146 C CB  . ASN A 274 ? 0.5963 0.4803 0.5556 0.0338  0.0379  0.0016  274 ASN A CB  
2147 C CG  . ASN A 274 ? 0.5505 0.4048 0.5004 0.0235  0.0401  0.0058  274 ASN A CG  
2148 O OD1 . ASN A 274 ? 0.5981 0.4526 0.5458 0.0195  0.0390  0.0158  274 ASN A OD1 
2149 N ND2 . ASN A 274 ? 0.6596 0.4888 0.6035 0.0185  0.0436  -0.0025 274 ASN A ND2 
2150 N N   . GLY A 275 ? 0.3829 0.3325 0.3590 0.0269  0.0365  -0.0151 275 GLY A N   
2151 C CA  . GLY A 275 ? 0.4884 0.4661 0.4722 0.0323  0.0361  -0.0163 275 GLY A CA  
2152 C C   . GLY A 275 ? 0.4055 0.3968 0.3957 0.0404  0.0331  -0.0077 275 GLY A C   
2153 O O   . GLY A 275 ? 0.4116 0.3923 0.3992 0.0413  0.0308  -0.0002 275 GLY A O   
2154 N N   . MET A 276 ? 0.4578 0.4755 0.4562 0.0454  0.0331  -0.0092 276 MET A N   
2155 C CA  . MET A 276 ? 0.4406 0.4787 0.4470 0.0505  0.0294  -0.0026 276 MET A CA  
2156 C C   . MET A 276 ? 0.3820 0.4264 0.3931 0.0684  0.0298  -0.0025 276 MET A C   
2157 O O   . MET A 276 ? 0.4276 0.4929 0.4462 0.0736  0.0260  0.0023  276 MET A O   
2158 C CB  . MET A 276 ? 0.3787 0.4447 0.3925 0.0410  0.0285  -0.0036 276 MET A CB  
2159 C CG  . MET A 276 ? 0.4225 0.4818 0.4321 0.0262  0.0262  -0.0013 276 MET A CG  
2160 S SD  . MET A 276 ? 0.6534 0.7360 0.6684 0.0144  0.0253  -0.0013 276 MET A SD  
2161 C CE  . MET A 276 ? 0.3188 0.4261 0.3444 0.0193  0.0222  0.0020  276 MET A CE  
2162 N N   . ASN A 277 ? 0.4396 0.4663 0.4462 0.0786  0.0338  -0.0080 277 ASN A N   
2163 C CA  . ASN A 277 ? 0.4952 0.5241 0.5056 0.0989  0.0342  -0.0082 277 ASN A CA  
2164 C C   . ASN A 277 ? 0.4580 0.5292 0.4834 0.1049  0.0328  -0.0087 277 ASN A C   
2165 O O   . ASN A 277 ? 0.5392 0.6238 0.5706 0.1160  0.0284  -0.0027 277 ASN A O   
2166 C CB  . ASN A 277 ? 0.4861 0.4916 0.4896 0.1076  0.0304  0.0017  277 ASN A CB  
2167 C CG  . ASN A 277 ? 0.6356 0.5973 0.6249 0.1047  0.0332  0.0013  277 ASN A CG  
2168 O OD1 . ASN A 277 ? 0.8536 0.7985 0.8353 0.0931  0.0318  0.0076  277 ASN A OD1 
2169 N ND2 . ASN A 277 ? 0.6310 0.5742 0.6166 0.1150  0.0376  -0.0069 277 ASN A ND2 
2170 N N   . GLY A 278 ? 0.3592 0.4530 0.3903 0.0968  0.0367  -0.0156 278 GLY A N   
2171 C CA  . GLY A 278 ? 0.3719 0.5075 0.4179 0.0998  0.0370  -0.0171 278 GLY A CA  
2172 C C   . GLY A 278 ? 0.3265 0.4838 0.3800 0.0920  0.0306  -0.0097 278 GLY A C   
2173 O O   . GLY A 278 ? 0.3564 0.5500 0.4236 0.0945  0.0300  -0.0107 278 GLY A O   
2174 N N   . ARG A 279 ? 0.3325 0.4703 0.3778 0.0826  0.0261  -0.0031 279 ARG A N   
2175 C CA  . ARG A 279 ? 0.2527 0.4079 0.3028 0.0743  0.0201  0.0024  279 ARG A CA  
2176 C C   . ARG A 279 ? 0.2858 0.4494 0.3368 0.0546  0.0214  0.0005  279 ARG A C   
2177 O O   . ARG A 279 ? 0.3124 0.4672 0.3589 0.0479  0.0263  -0.0035 279 ARG A O   
2178 C CB  . ARG A 279 ? 0.2596 0.3903 0.2992 0.0753  0.0153  0.0100  279 ARG A CB  
2179 C CG  . ARG A 279 ? 0.3425 0.4654 0.3798 0.0948  0.0126  0.0150  279 ARG A CG  
2180 C CD  . ARG A 279 ? 0.4865 0.5793 0.5096 0.0928  0.0100  0.0231  279 ARG A CD  
2181 N NE  . ARG A 279 ? 0.7322 0.7884 0.7444 0.0926  0.0151  0.0218  279 ARG A NE  
2182 C CZ  . ARG A 279 ? 0.7044 0.7294 0.7041 0.0969  0.0150  0.0285  279 ARG A CZ  
2183 N NH1 . ARG A 279 ? 0.7440 0.7686 0.7382 0.1015  0.0101  0.0383  279 ARG A NH1 
2184 N NH2 . ARG A 279 ? 0.6441 0.6374 0.6355 0.0951  0.0201  0.0253  279 ARG A NH2 
2185 N N   . THR A 280 ? 0.2565 0.4367 0.3125 0.0456  0.0166  0.0033  280 THR A N   
2186 C CA  . THR A 280 ? 0.2450 0.4290 0.3008 0.0274  0.0171  0.0025  280 THR A CA  
2187 C C   . THR A 280 ? 0.2980 0.4709 0.3483 0.0195  0.0114  0.0063  280 THR A C   
2188 O O   . THR A 280 ? 0.2679 0.4423 0.3176 0.0263  0.0066  0.0094  280 THR A O   
2189 C CB  . THR A 280 ? 0.2260 0.4450 0.2949 0.0210  0.0183  -0.0002 280 THR A CB  
2190 O OG1 . THR A 280 ? 0.2659 0.5086 0.3445 0.0267  0.0128  0.0008  280 THR A OG1 
2191 C CG2 . THR A 280 ? 0.2664 0.4994 0.3403 0.0274  0.0254  -0.0048 280 THR A CG2 
2192 N N   . ILE A 281 ? 0.2408 0.4031 0.2864 0.0058  0.0120  0.0059  281 ILE A N   
2193 C CA  . ILE A 281 ? 0.1773 0.3295 0.2179 -0.0024 0.0075  0.0077  281 ILE A CA  
2194 C C   . ILE A 281 ? 0.2260 0.3874 0.2701 -0.0169 0.0074  0.0060  281 ILE A C   
2195 O O   . ILE A 281 ? 0.2223 0.3783 0.2641 -0.0233 0.0113  0.0057  281 ILE A O   
2196 C CB  . ILE A 281 ? 0.2417 0.3657 0.2714 -0.0031 0.0084  0.0091  281 ILE A CB  
2197 C CG1 . ILE A 281 ? 0.2267 0.3381 0.2518 0.0088  0.0092  0.0114  281 ILE A CG1 
2198 C CG2 . ILE A 281 ? 0.2425 0.3589 0.2679 -0.0108 0.0046  0.0096  281 ILE A CG2 
2199 C CD1 . ILE A 281 ? 0.2349 0.3215 0.2510 0.0065  0.0114  0.0117  281 ILE A CD1 
2200 N N   . LEU A 282 ? 0.2740 0.4487 0.3225 -0.0223 0.0028  0.0049  282 LEU A N   
2201 C CA  . LEU A 282 ? 0.2480 0.4297 0.2999 -0.0376 0.0025  0.0030  282 LEU A CA  
2202 C C   . LEU A 282 ? 0.2715 0.4695 0.3302 -0.0423 0.0081  0.0028  282 LEU A C   
2203 O O   . LEU A 282 ? 0.2736 0.4642 0.3290 -0.0541 0.0109  0.0039  282 LEU A O   
2204 C CB  . LEU A 282 ? 0.2403 0.3946 0.2819 -0.0454 0.0019  0.0037  282 LEU A CB  
2205 C CG  . LEU A 282 ? 0.2658 0.4093 0.3019 -0.0442 -0.0032 0.0021  282 LEU A CG  
2206 C CD1 . LEU A 282 ? 0.2463 0.3643 0.2737 -0.0496 -0.0033 0.0020  282 LEU A CD1 
2207 C CD2 . LEU A 282 ? 0.2567 0.4194 0.2987 -0.0501 -0.0080 -0.0018 282 LEU A CD2 
2208 N N   . GLY A 283 ? 0.2327 0.4533 0.3003 -0.0322 0.0100  0.0017  283 GLY A N   
2209 C CA  . GLY A 283 ? 0.2606 0.5021 0.3356 -0.0350 0.0163  0.0005  283 GLY A CA  
2210 C C   . GLY A 283 ? 0.3004 0.5263 0.3667 -0.0329 0.0226  0.0014  283 GLY A C   
2211 O O   . GLY A 283 ? 0.2874 0.5301 0.3575 -0.0370 0.0286  0.0004  283 GLY A O   
2212 N N   A SER A 284 ? 0.2388 0.4357 0.2937 -0.0273 0.0215  0.0027  284 SER A N   
2213 N N   B SER A 284 ? 0.2389 0.4359 0.2939 -0.0272 0.0215  0.0027  284 SER A N   
2214 C CA  A SER A 284 ? 0.2280 0.4107 0.2739 -0.0258 0.0263  0.0025  284 SER A CA  
2215 C CA  B SER A 284 ? 0.2284 0.4109 0.2742 -0.0259 0.0263  0.0025  284 SER A CA  
2216 C C   A SER A 284 ? 0.2162 0.3914 0.2604 -0.0101 0.0275  -0.0002 284 SER A C   
2217 C C   B SER A 284 ? 0.2170 0.3916 0.2608 -0.0103 0.0275  -0.0001 284 SER A C   
2218 O O   A SER A 284 ? 0.2388 0.4047 0.2827 -0.0022 0.0235  0.0008  284 SER A O   
2219 O O   B SER A 284 ? 0.2396 0.4043 0.2830 -0.0025 0.0235  0.0009  284 SER A O   
2220 C CB  A SER A 284 ? 0.2446 0.4002 0.2787 -0.0334 0.0241  0.0055  284 SER A CB  
2221 C CB  B SER A 284 ? 0.2451 0.4007 0.2792 -0.0337 0.0239  0.0056  284 SER A CB  
2222 O OG  A SER A 284 ? 0.2687 0.4143 0.2939 -0.0326 0.0278  0.0050  284 SER A OG  
2223 O OG  B SER A 284 ? 0.3188 0.4759 0.3527 -0.0476 0.0231  0.0084  284 SER A OG  
2224 N N   . ALA A 285 ? 0.2148 0.3923 0.2561 -0.0062 0.0333  -0.0036 285 ALA A N   
2225 C CA  . ALA A 285 ? 0.2432 0.4079 0.2808 0.0075  0.0351  -0.0074 285 ALA A CA  
2226 C C   . ALA A 285 ? 0.2818 0.4189 0.3063 0.0043  0.0350  -0.0081 285 ALA A C   
2227 O O   . ALA A 285 ? 0.3475 0.4707 0.3672 0.0128  0.0369  -0.0122 285 ALA A O   
2228 C CB  . ALA A 285 ? 0.2923 0.4771 0.3350 0.0158  0.0416  -0.0133 285 ALA A CB  
2229 N N   . LEU A 286 ? 0.2252 0.3541 0.2442 -0.0074 0.0325  -0.0044 286 LEU A N   
2230 C CA  . LEU A 286 ? 0.2525 0.3593 0.2613 -0.0104 0.0309  -0.0047 286 LEU A CA  
2231 C C   . LEU A 286 ? 0.2829 0.3797 0.2912 -0.0165 0.0254  0.0002  286 LEU A C   
2232 O O   . LEU A 286 ? 0.2798 0.3851 0.2937 -0.0200 0.0231  0.0032  286 LEU A O   
2233 C CB  . LEU A 286 ? 0.3301 0.4388 0.3305 -0.0166 0.0338  -0.0061 286 LEU A CB  
2234 C CG  . LEU A 286 ? 0.4362 0.5588 0.4364 -0.0265 0.0351  -0.0015 286 LEU A CG  
2235 C CD1 . LEU A 286 ? 0.3937 0.5033 0.3907 -0.0344 0.0296  0.0046  286 LEU A CD1 
2236 C CD2 . LEU A 286 ? 0.3483 0.4771 0.3390 -0.0293 0.0398  -0.0036 286 LEU A CD2 
2237 N N   . LEU A 287 ? 0.2478 0.3277 0.2496 -0.0180 0.0234  0.0000  287 LEU A N   
2238 C CA  . LEU A 287 ? 0.2506 0.3219 0.2521 -0.0220 0.0188  0.0033  287 LEU A CA  
2239 C C   . LEU A 287 ? 0.2783 0.3500 0.2760 -0.0299 0.0172  0.0063  287 LEU A C   
2240 O O   . LEU A 287 ? 0.3285 0.3984 0.3197 -0.0320 0.0180  0.0059  287 LEU A O   
2241 C CB  . LEU A 287 ? 0.2281 0.2848 0.2260 -0.0203 0.0178  0.0016  287 LEU A CB  
2242 C CG  . LEU A 287 ? 0.3138 0.3644 0.3129 -0.0131 0.0197  0.0002  287 LEU A CG  
2243 C CD1 . LEU A 287 ? 0.3699 0.4053 0.3646 -0.0142 0.0202  -0.0022 287 LEU A CD1 
2244 C CD2 . LEU A 287 ? 0.3227 0.3770 0.3261 -0.0098 0.0177  0.0041  287 LEU A CD2 
2245 N N   . GLU A 288 ? 0.2140 0.2870 0.2146 -0.0342 0.0146  0.0093  288 GLU A N   
2246 C CA  . GLU A 288 ? 0.2652 0.3349 0.2615 -0.0417 0.0133  0.0131  288 GLU A CA  
2247 C C   . GLU A 288 ? 0.1966 0.2515 0.1888 -0.0412 0.0089  0.0143  288 GLU A C   
2248 O O   . GLU A 288 ? 0.2223 0.2729 0.2178 -0.0385 0.0066  0.0126  288 GLU A O   
2249 C CB  . GLU A 288 ? 0.2281 0.3052 0.2295 -0.0478 0.0131  0.0147  288 GLU A CB  
2250 C CG  . GLU A 288 ? 0.2969 0.3945 0.3056 -0.0475 0.0170  0.0129  288 GLU A CG  
2251 C CD  . GLU A 288 ? 0.4481 0.5551 0.4538 -0.0540 0.0217  0.0152  288 GLU A CD  
2252 O OE1 . GLU A 288 ? 0.4014 0.4965 0.3975 -0.0589 0.0212  0.0193  288 GLU A OE1 
2253 O OE2 . GLU A 288 ? 0.4616 0.5890 0.4739 -0.0535 0.0259  0.0132  288 GLU A OE2 
2254 N N   . ASP A 289 ? 0.2397 0.2886 0.2243 -0.0433 0.0076  0.0174  289 ASP A N   
2255 C CA  . ASP A 289 ? 0.2579 0.2956 0.2396 -0.0407 0.0030  0.0183  289 ASP A CA  
2256 C C   . ASP A 289 ? 0.2646 0.2912 0.2399 -0.0441 0.0002  0.0242  289 ASP A C   
2257 O O   . ASP A 289 ? 0.2898 0.3082 0.2610 -0.0402 -0.0038 0.0260  289 ASP A O   
2258 C CB  . ASP A 289 ? 0.2366 0.2763 0.2150 -0.0371 0.0020  0.0163  289 ASP A CB  
2259 C CG  . ASP A 289 ? 0.3179 0.3606 0.2869 -0.0395 0.0026  0.0193  289 ASP A CG  
2260 O OD1 . ASP A 289 ? 0.2627 0.3067 0.2276 -0.0444 0.0051  0.0236  289 ASP A OD1 
2261 O OD2 . ASP A 289 ? 0.2582 0.3033 0.2233 -0.0373 0.0004  0.0173  289 ASP A OD2 
2262 N N   . GLU A 290 ? 0.2548 0.2802 0.2292 -0.0513 0.0021  0.0273  290 GLU A N   
2263 C CA  . GLU A 290 ? 0.2646 0.2738 0.2314 -0.0555 -0.0003 0.0335  290 GLU A CA  
2264 C C   . GLU A 290 ? 0.2785 0.2779 0.2494 -0.0591 -0.0018 0.0313  290 GLU A C   
2265 O O   . GLU A 290 ? 0.3134 0.3001 0.2793 -0.0669 -0.0020 0.0356  290 GLU A O   
2266 C CB  . GLU A 290 ? 0.2697 0.2815 0.2281 -0.0635 0.0032  0.0403  290 GLU A CB  
2267 C CG  . GLU A 290 ? 0.2945 0.3159 0.2463 -0.0594 0.0042  0.0411  290 GLU A CG  
2268 C CD  . GLU A 290 ? 0.3694 0.3873 0.3070 -0.0650 0.0055  0.0502  290 GLU A CD  
2269 O OE1 . GLU A 290 ? 0.3263 0.3390 0.2608 -0.0747 0.0084  0.0558  290 GLU A OE1 
2270 O OE2 . GLU A 290 ? 0.3687 0.3898 0.2975 -0.0608 0.0039  0.0519  290 GLU A OE2 
2271 N N   . PHE A 291 ? 0.2817 0.2856 0.2604 -0.0540 -0.0030 0.0245  291 PHE A N   
2272 C CA  . PHE A 291 ? 0.2797 0.2735 0.2605 -0.0546 -0.0056 0.0204  291 PHE A CA  
2273 C C   . PHE A 291 ? 0.2367 0.2246 0.2179 -0.0442 -0.0086 0.0170  291 PHE A C   
2274 O O   . PHE A 291 ? 0.2551 0.2554 0.2410 -0.0388 -0.0076 0.0140  291 PHE A O   
2275 C CB  . PHE A 291 ? 0.2582 0.2669 0.2470 -0.0576 -0.0041 0.0150  291 PHE A CB  
2276 C CG  . PHE A 291 ? 0.2916 0.3114 0.2831 -0.0677 -0.0013 0.0169  291 PHE A CG  
2277 C CD1 . PHE A 291 ? 0.3293 0.3398 0.3188 -0.0786 -0.0018 0.0176  291 PHE A CD1 
2278 C CD2 . PHE A 291 ? 0.3028 0.3425 0.2990 -0.0665 0.0024  0.0175  291 PHE A CD2 
2279 C CE1 . PHE A 291 ? 0.3445 0.3696 0.3383 -0.0896 0.0013  0.0190  291 PHE A CE1 
2280 C CE2 . PHE A 291 ? 0.3943 0.4490 0.3948 -0.0751 0.0056  0.0185  291 PHE A CE2 
2281 C CZ  . PHE A 291 ? 0.3859 0.4353 0.3859 -0.0874 0.0052  0.0194  291 PHE A CZ  
2282 N N   . THR A 292 ? 0.2816 0.2509 0.2582 -0.0414 -0.0120 0.0172  292 THR A N   
2283 C CA  . THR A 292 ? 0.3119 0.2797 0.2909 -0.0307 -0.0143 0.0126  292 THR A CA  
2284 C C   . THR A 292 ? 0.3113 0.2832 0.2948 -0.0305 -0.0136 0.0044  292 THR A C   
2285 O O   . THR A 292 ? 0.2478 0.2196 0.2314 -0.0384 -0.0129 0.0023  292 THR A O   
2286 C CB  . THR A 292 ? 0.2948 0.2413 0.2674 -0.0248 -0.0184 0.0150  292 THR A CB  
2287 O OG1 . THR A 292 ? 0.3554 0.2825 0.3238 -0.0305 -0.0190 0.0131  292 THR A OG1 
2288 C CG2 . THR A 292 ? 0.2752 0.2163 0.2403 -0.0245 -0.0200 0.0247  292 THR A CG2 
2289 N N   . PRO A 293 ? 0.3108 0.2889 0.2978 -0.0219 -0.0139 -0.0005 293 PRO A N   
2290 C CA  . PRO A 293 ? 0.2407 0.2209 0.2290 -0.0208 -0.0133 -0.0085 293 PRO A CA  
2291 C C   . PRO A 293 ? 0.3268 0.2875 0.3098 -0.0241 -0.0156 -0.0124 293 PRO A C   
2292 O O   . PRO A 293 ? 0.3357 0.2993 0.3183 -0.0298 -0.0153 -0.0177 293 PRO A O   
2293 C CB  . PRO A 293 ? 0.3109 0.2981 0.3027 -0.0104 -0.0131 -0.0122 293 PRO A CB  
2294 C CG  . PRO A 293 ? 0.2880 0.2861 0.2831 -0.0095 -0.0123 -0.0066 293 PRO A CG  
2295 C CD  . PRO A 293 ? 0.2453 0.2324 0.2355 -0.0141 -0.0142 0.0004  293 PRO A CD  
2296 N N   . PHE A 294 ? 0.3346 0.2742 0.3128 -0.0210 -0.0182 -0.0098 294 PHE A N   
2297 C CA  . PHE A 294 ? 0.3899 0.3056 0.3619 -0.0251 -0.0202 -0.0138 294 PHE A CA  
2298 C C   . PHE A 294 ? 0.3901 0.3028 0.3601 -0.0406 -0.0194 -0.0105 294 PHE A C   
2299 O O   . PHE A 294 ? 0.3942 0.3002 0.3625 -0.0483 -0.0200 -0.0173 294 PHE A O   
2300 C CB  . PHE A 294 ? 0.4623 0.3520 0.4281 -0.0165 -0.0234 -0.0110 294 PHE A CB  
2301 C CG  . PHE A 294 ? 0.6807 0.5797 0.6509 -0.0006 -0.0244 -0.0125 294 PHE A CG  
2302 C CD1 . PHE A 294 ? 0.6834 0.6026 0.6587 0.0028  -0.0240 -0.0064 294 PHE A CD1 
2303 C CD2 . PHE A 294 ? 0.8781 0.7683 0.8483 0.0106  -0.0255 -0.0217 294 PHE A CD2 
2304 C CE1 . PHE A 294 ? 0.7339 0.6655 0.7150 0.0158  -0.0251 -0.0088 294 PHE A CE1 
2305 C CE2 . PHE A 294 ? 0.7914 0.6950 0.7678 0.0253  -0.0260 -0.0240 294 PHE A CE2 
2306 C CZ  . PHE A 294 ? 0.8541 0.7796 0.8366 0.0272  -0.0259 -0.0173 294 PHE A CZ  
2307 N N   . ASP A 295 ? 0.3231 0.2433 0.2936 -0.0459 -0.0178 -0.0011 295 ASP A N   
2308 C CA  . ASP A 295 ? 0.3562 0.2820 0.3276 -0.0606 -0.0160 0.0014  295 ASP A CA  
2309 C C   . ASP A 295 ? 0.3575 0.3048 0.3358 -0.0646 -0.0152 -0.0061 295 ASP A C   
2310 O O   . ASP A 295 ? 0.3367 0.2840 0.3156 -0.0761 -0.0157 -0.0096 295 ASP A O   
2311 C CB  . ASP A 295 ? 0.3319 0.2698 0.3038 -0.0634 -0.0133 0.0110  295 ASP A CB  
2312 C CG  . ASP A 295 ? 0.3772 0.2954 0.3399 -0.0611 -0.0144 0.0200  295 ASP A CG  
2313 O OD1 . ASP A 295 ? 0.4746 0.3653 0.4298 -0.0608 -0.0170 0.0208  295 ASP A OD1 
2314 O OD2 . ASP A 295 ? 0.3480 0.2777 0.3099 -0.0587 -0.0130 0.0262  295 ASP A OD2 
2315 N N   . VAL A 296 ? 0.2833 0.2498 0.2665 -0.0560 -0.0143 -0.0081 296 VAL A N   
2316 C CA  . VAL A 296 ? 0.2911 0.2787 0.2793 -0.0585 -0.0140 -0.0128 296 VAL A CA  
2317 C C   . VAL A 296 ? 0.3515 0.3328 0.3366 -0.0602 -0.0166 -0.0227 296 VAL A C   
2318 O O   . VAL A 296 ? 0.3565 0.3478 0.3434 -0.0687 -0.0180 -0.0271 296 VAL A O   
2319 C CB  . VAL A 296 ? 0.2540 0.2588 0.2457 -0.0492 -0.0120 -0.0111 296 VAL A CB  
2320 C CG1 . VAL A 296 ? 0.2580 0.2809 0.2520 -0.0492 -0.0125 -0.0154 296 VAL A CG1 
2321 C CG2 . VAL A 296 ? 0.2625 0.2750 0.2570 -0.0494 -0.0094 -0.0034 296 VAL A CG2 
2322 N N   . VAL A 297 ? 0.3331 0.2993 0.3136 -0.0519 -0.0175 -0.0274 297 VAL A N   
2323 C CA  . VAL A 297 ? 0.3536 0.3127 0.3297 -0.0525 -0.0196 -0.0387 297 VAL A CA  
2324 C C   . VAL A 297 ? 0.4283 0.3676 0.4005 -0.0650 -0.0218 -0.0421 297 VAL A C   
2325 O O   . VAL A 297 ? 0.4438 0.3877 0.4149 -0.0731 -0.0238 -0.0506 297 VAL A O   
2326 C CB  . VAL A 297 ? 0.3607 0.3088 0.3333 -0.0394 -0.0192 -0.0437 297 VAL A CB  
2327 C CG1 . VAL A 297 ? 0.4137 0.3530 0.3802 -0.0395 -0.0209 -0.0571 297 VAL A CG1 
2328 C CG2 . VAL A 297 ? 0.3980 0.3679 0.3750 -0.0301 -0.0163 -0.0406 297 VAL A CG2 
2329 N N   . ARG A 298 ? 0.3931 0.3098 0.3624 -0.0674 -0.0216 -0.0354 298 ARG A N   
2330 C CA  . ARG A 298 ? 0.4140 0.3082 0.3785 -0.0812 -0.0230 -0.0371 298 ARG A CA  
2331 C C   . ARG A 298 ? 0.4327 0.3488 0.4036 -0.0971 -0.0226 -0.0368 298 ARG A C   
2332 O O   . ARG A 298 ? 0.4835 0.3964 0.4533 -0.1090 -0.0247 -0.0454 298 ARG A O   
2333 C CB  . ARG A 298 ? 0.4082 0.2757 0.3670 -0.0810 -0.0224 -0.0265 298 ARG A CB  
2334 C CG  . ARG A 298 ? 0.6433 0.4952 0.5987 -0.0996 -0.0218 -0.0223 298 ARG A CG  
2335 N N   . GLN A 299 ? 0.4521 0.3922 0.4300 -0.0972 -0.0201 -0.0279 299 GLN A N   
2336 C CA  . GLN A 299 ? 0.4549 0.4191 0.4406 -0.1106 -0.0194 -0.0275 299 GLN A CA  
2337 C C   . GLN A 299 ? 0.5108 0.4997 0.5010 -0.1100 -0.0224 -0.0370 299 GLN A C   
2338 O O   . GLN A 299 ? 0.5208 0.5226 0.5152 -0.1230 -0.0243 -0.0423 299 GLN A O   
2339 C CB  . GLN A 299 ? 0.4052 0.3892 0.3970 -0.1086 -0.0156 -0.0169 299 GLN A CB  
2340 C CG  . GLN A 299 ? 0.4052 0.4173 0.4067 -0.1212 -0.0144 -0.0168 299 GLN A CG  
2341 C CD  . GLN A 299 ? 0.3917 0.4202 0.3981 -0.1212 -0.0096 -0.0072 299 GLN A CD  
2342 O OE1 . GLN A 299 ? 0.3702 0.4268 0.3863 -0.1278 -0.0080 -0.0074 299 GLN A OE1 
2343 N NE2 . GLN A 299 ? 0.3132 0.3264 0.3130 -0.1135 -0.0073 0.0002  299 GLN A NE2 
2344 N N   . CYS A 300 ? 0.3798 0.3769 0.3687 -0.0956 -0.0228 -0.0389 300 CYS A N   
2345 C CA  . CYS A 300 ? 0.4201 0.4407 0.4106 -0.0932 -0.0256 -0.0459 300 CYS A CA  
2346 C C   . CYS A 300 ? 0.5209 0.5290 0.5035 -0.0956 -0.0290 -0.0589 300 CYS A C   
2347 O O   . CYS A 300 ? 0.6614 0.6890 0.6428 -0.0941 -0.0319 -0.0655 300 CYS A O   
2348 C CB  . CYS A 300 ? 0.5000 0.5341 0.4910 -0.0781 -0.0237 -0.0409 300 CYS A CB  
2349 S SG  . CYS A 300 ? 0.5059 0.5602 0.5060 -0.0750 -0.0203 -0.0289 300 CYS A SG  
2350 N N   . SER A 301 ? 0.5544 0.5299 0.5303 -0.0988 -0.0291 -0.0630 301 SER A N   
2351 C CA  . SER A 301 ? 0.5305 0.4901 0.4980 -0.1010 -0.0320 -0.0772 301 SER A CA  
2352 C C   . SER A 301 ? 0.6710 0.6080 0.6359 -0.1184 -0.0339 -0.0830 301 SER A C   
2353 O O   . SER A 301 ? 0.7871 0.7165 0.7459 -0.1242 -0.0371 -0.0970 301 SER A O   
2354 C CB  . SER A 301 ? 0.6814 0.6186 0.6416 -0.0857 -0.0302 -0.0800 301 SER A CB  
2355 O OG  . SER A 301 ? 0.6082 0.5102 0.5645 -0.0866 -0.0295 -0.0768 301 SER A OG  
2356 N N   . GLY A 302 ? 0.7605 0.6853 0.7284 -0.1276 -0.0318 -0.0732 302 GLY A N   
2357 C CA  . GLY A 302 ? 0.8567 0.7596 0.8218 -0.1469 -0.0328 -0.0773 302 GLY A CA  
2358 C C   . GLY A 302 ? 0.9367 0.7902 0.8903 -0.1458 -0.0323 -0.0778 302 GLY A C   
2359 O O   . GLY A 302 ? 0.7828 0.6116 0.7305 -0.1600 -0.0341 -0.0867 302 GLY A O   
2360 N N   . VAL A 303 ? 0.8561 0.6938 0.8060 -0.1293 -0.0302 -0.0689 303 VAL A N   
2361 C CA  . VAL A 303 ? 1.0047 0.7954 0.9433 -0.1242 -0.0305 -0.0688 303 VAL A CA  
2362 C C   . VAL A 303 ? 0.9988 0.7634 0.9331 -0.1420 -0.0291 -0.0595 303 VAL A C   
2363 O O   . VAL A 303 ? 0.9388 0.7200 0.8785 -0.1485 -0.0262 -0.0462 303 VAL A O   
2364 C CB  . VAL A 303 ? 0.9911 0.7784 0.9288 -0.1017 -0.0293 -0.0606 303 VAL A CB  
2365 C CG1 . VAL A 303 ? 1.0053 0.7448 0.9316 -0.0948 -0.0303 -0.0584 303 VAL A CG1 
2366 C CG2 . VAL A 303 ? 0.9547 0.7659 0.8957 -0.0858 -0.0297 -0.0698 303 VAL A CG2 
2367 N N   . THR A 304 ? 0.8922 0.6140 0.8158 -0.1496 -0.0306 -0.0662 304 THR A N   
2368 C CA  . THR A 304 ? 0.7911 0.4818 0.7081 -0.1687 -0.0289 -0.0575 304 THR A CA  
2369 C C   . THR A 304 ? 0.9579 0.5980 0.8608 -0.1568 -0.0292 -0.0491 304 THR A C   
2370 O O   . THR A 304 ? 0.9145 0.5441 0.8141 -0.1336 -0.0311 -0.0523 304 THR A O   
2371 C CB  . THR A 304 ? 0.8277 0.5085 0.7440 -0.1911 -0.0304 -0.0710 304 THR A CB  
2372 O OG1 . THR A 304 ? 0.8586 0.5213 0.7687 -0.1816 -0.0340 -0.0893 304 THR A OG1 
2373 C CG2 . THR A 304 ? 0.6560 0.3903 0.5878 -0.2053 -0.0301 -0.0741 304 THR A CG2 
2374 N N   . PHE A 305 ? 0.8981 0.5094 0.7935 -0.1723 -0.0270 -0.0375 305 PHE A N   
2375 C CA  . PHE A 305 ? 0.9165 0.4844 0.7994 -0.1603 -0.0271 -0.0251 305 PHE A CA  
2376 C C   . PHE A 305 ? 0.9610 0.4988 0.8409 -0.1737 -0.0249 -0.0234 305 PHE A C   
2377 O O   . PHE A 305 ? 0.9595 0.4999 0.8453 -0.1868 -0.0252 -0.0373 305 PHE A O   
2378 C CB  . PHE A 305 ? 0.7327 0.3111 0.6127 -0.1569 -0.0251 -0.0045 305 PHE A CB  
2379 C CG  . PHE A 305 ? 0.7328 0.3620 0.6265 -0.1402 -0.0251 -0.0052 305 PHE A CG  
2380 C CD1 . PHE A 305 ? 0.7805 0.4099 0.6745 -0.1137 -0.0281 -0.0083 305 PHE A CD1 
2381 C CD2 . PHE A 305 ? 0.8463 0.5231 0.7528 -0.1511 -0.0219 -0.0030 305 PHE A CD2 
2382 C CE1 . PHE A 305 ? 0.7730 0.4469 0.6790 -0.1008 -0.0277 -0.0088 305 PHE A CE1 
2383 C CE2 . PHE A 305 ? 0.7984 0.5169 0.7160 -0.1361 -0.0218 -0.0035 305 PHE A CE2 
2384 C CZ  . PHE A 305 ? 0.8287 0.5447 0.7457 -0.1122 -0.0246 -0.0062 305 PHE A CZ  
# 
